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TGF-β signaling in health, disease and therapeutics

Ziqin Deng, Tao Fan, Chu Xiao and 4 more

Signal Transduction and Targeted Therapy · 2024 · Review · CC BY

Abstract

Transforming growth factor (TGF)-β is a multifunctional cytokine expressed by almost every tissue and cell type. The signal transduction of TGF-β can stimulate diverse cellular responses and is particularly critical to embryonic development, wound healing, tissue homeostasis, and immune homeostasis in health. The dysfunction of TGF-β can play key roles in many diseases, and numerous targeted therapies have been developed to rectify its pathogenic activity. In the past decades, a large number of studies on TGF-β signaling have been carried out, covering a broad spectrum of topics in health, disease, and therapeutics. Thus, a comprehensive overview of TGF-β signaling is required for a general picture of the studies in this field. In this review, we retrace the research history of TGF-β and introduce the molecular mechanisms regarding its biosynthesis, activation, and signal transduction. We also provide deep insights into the functions of TGF-β signaling in physiological conditions as well as in pathological processes. TGF-β-targeting therapies which have brought fresh hope to the treatment of relevant diseases are highlighted. Through the summary of previous knowledge and recent updates, this review aims to provide a systematic understanding of TGF-β signaling and to attract more attention and interest to this research area.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 21, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

1The studies on TGF-β started as early as the 1980s and have developed rapidly ever since. Although TGF-β was first found to be secreted by transformed cells, it is widely produced by non-neoplastic tissues such as salivary glands, muscles, kidneys, liver, heart, brain, and embryos as well.– In fact, platelets have been identified as one of the most abundant sources of TGF-β among all normal tissues. The ubiquitous expression of TGF-β in health strongly indicates its critical and multiple roles in physiological conditions.

2Accumulating evidence has suggested that TGF-β functions diversely among different cell types in a context-dependent manner. Generally, cell survival, metabolism, growth, proliferation, differentiation, adhesion, migration, and death are all under the regulation of TGF-β. Proper TGF-β signaling is critical to the normal functioning and homeostasis of healthy bodies while aberrant TGF-β signaling can lead to diseases of various categories. For this reason, numerous targeted therapies that can remedy dysregulated TGF-β activity have been developed with some demonstrating encouraging safety and efficacy in clinical trials.

3In this review, we focus on the mechanism, physiology, pathology, as well as therapeutics of TGF-β signaling, aiming to provide historical, current, and future perspectives on relevant topics.

History of research on TGF-β signaling

4TGF-β was first reported in 1978 when De Larco and Todaro discovered the ‘sarcoma growth factors’ which were produced by transformed murine fibroblasts and were able to transform normal fibroblasts to anchorage-independent growth. In 1981, Roberts et al. successfully isolated and purified TGF-β from non-neoplastic murine tissues, while at about the same time, Moses et al. independently accomplished the purification and characterization of the cytokine as well. Both groups also noticed that this relatively acid- and heat-stable polypeptide required disulfide bonds for activity and was sensitive to disulfide-reducing agent dithiothreitol. In 1983, studies by electrophoresis on sodium dodecyl sulfate-polyacrylamide gels indicated that the 25,000-dalton TGF-β molecule in humans was actually composed of two 12,500-dalton subunits cross-linked by disulfide bonds., Two years later, the amino-acid sequence of human TGF-β1, the first known TGF-β isoform, was revealed by Derynck et al. through direct protein sequencing and complementary deoxyribonucleic acid (DNA) cloning. The sequencing established that the 112-amino-acid-long TGF-β1 monomer is initially synthesized as the C-terminal segment of a 390-amino-acid-long precursor polypeptide. By the time of 1988, researchers had realized that TGF-β generally remained non-covalently associated with the N-terminal segment of its precursor when it was secreted., TGF-β cannot bind to its receptors with its receptor-binding site being masked in this inactive form, however, certain treatments such as acidification could convert latent TGF-β complex into active TGF-β ligand. In addition, the other two TGF-β isoforms in mammals, TGF-β2 and TGF-β3, were respectively identified in 1987 and 1988., Although the three TGF-β isoforms are encoded by three different genes, their mature ligands show strong conservation of amino acid sequences.

5The effects of TGF-β signaling in cell proliferation,, cell differentiation,, embryonic development, wound healing, immune regulation,, tissue fibrosis,, and tumor development, have been studied shortly after the discovery of the cytokine. Meanwhile, the receptors in TGF-β signaling known as TGF-β receptor I (TβRI) and TβRII were also identified and characterized in the 1980s.– But it was not until the discovery of signaling mediators small (Sma) in Caenorhabditis elegans and mothers against decapentaplegic (Mad) in Drosophila melanogaster that the homologous small mothers against decapentaplegic (SMAD) proteins were identified as the canonical signal transducers of TGF-β signaling in humans in 1996.– Since then, the development of TGF-β research has been largely accelerated. In recent times, as studies on TGF-β signaling in both health and disease going deeper and further, a lot of TGF-β-targeting therapies have been developed and assessed for the treatment of various diseases,– revealing a promising future for the studies in this area (Fig. 1).

Biosynthesis and activation of TGF-β

6During the biosynthesis of TGF-β, the precursor undergoes post-translational processing to become a latent complex which is the secretory form of TGF-β. The latent TGF-β complex still requires further activation to eventually become a mature cytokine before it can trigger signal transduction in cells (Fig. 2).

TGF-β biosynthesis and latency

7Each TGF-β monomer is initially synthesized as a precursor polypeptide composed of a mature cytokine as its C-terminal segment, a signal peptide at the N-terminus, and a latency-associated peptide (LAP) in between. The signal peptide leads the precursor into the endoplasmic reticulum lumen and promptly gets removed. The remainder of the precursor then dimerizes through three disulfide bonds and transits into the Golgi where it gets cleaved between the mature cytokine and LAP by protease furin. However, the cytokine segment is still unable to bind its receptors after the cleavage, for it remains associated with LAP in a non-covalent way that masks its receptor-binding site and forms a small latent complex (SLC). In most cases, LAP is linked to latent TGF-β-binding protein (LTBP) through a disulfide bond, making the SLC into a large latent complex (LLC) when secreted. LTBP can further bind to fibrillin to target the LLC into the extracellular matrix (ECM) for storage. Alternatively, LAP can also form disulfide linkage with leucine-rich repeat-containing protein 32 (LRRC32) or LRRC33 to tether SLC to the cell surface. Unlike LTBP which is widely expressed by many cell types, LRRC32, also known as glycoprotein-A repetitions predominant protein (GARP), is specifically detected in regulatory T cells (Tregs), platelets, and endothelium, whereas high expression of LRRC33 is found in macrophages, dendritic cells (DCs), and B cells.

TGF-β activation

8The bioactivity of TGF-β is based on ligand-receptor interaction which requires the exposure of its receptor-binding site. Thus, the activation of TGF-β represents the release of mature cytokine from the latent complex. Numerous factors have been identified as TGF-β activators as introduced below. Notably, integrin-dependent activation is so far the best described and likely the most important mechanism, while TGF-β activation mediated by acids, bases, reactive oxygen species (ROS), thrombospondin-1 (TSP-1), proteases, and other TGF-β activators is collectively known as integrin-independent activation.

TGF-β activation by integrins

9Integrins are heterodimeric transmembrane receptors each consisting of an α-subunit and a β-subunit. TGF-β activation by integrins requires the binding of the integrins to an RGD sequence in the LAP of TGF-β1 and TGF-β3. Therefore, latent TGF-β2 without the RGD motif is excluded from integrin-dependent activation.

10Among all integrins, αVβ6 and αVβ8 integrins are the best studied TGF-β activators. The expression of αVβ6 integrin is nearly restricted to epithelial cells and is upregulated in response to morphogenesis, wounding, inflammation, and tumorigenesis. In contrast, αVβ8 integrin is widely expressed by epithelial cells, fibroblasts, macrophages, DCs, Tregs, and different kinds of tumor cells. The lack of αVβ6 and αVβ8 integrin activity reproduces the phenotypes of TGF-β1- and TGF-β3-null mice, indicating the central importance of integrin-dependent activation.,

11Upon binding to the RGD motif in LAP, the mechanisms by which αVβ6 and αVβ8 integrins activate TGF-β are quite different. With latent TGF-β being tethered to ECM or cell membrane (through the binding of LAP to LTBP, GARP, or LRRC33 as mentioned before) and the cytoplasmic domain of integrin β6 subunit linking to the actin cytoskeleton, αVβ6 integrin can transmit contractile force which changes the conformation of LAP to release TGF-β ligand., However, the cytoplasmic domain of integrin β8 subunit does not link to the actin cytoskeleton. One effective mechanism for αVβ8 integrin-mediated TGF-β activation requires the proteolytic activity of membrane type 1-matrix metalloproteinase (MT1-MMP, also known as MMP14). Alternatively, membrane molecules such as GARP and LRRC33 which bind and present latent TGF-β on the surface of one cell can cooperate with the αVβ8 integrin expressed on a different cell to activate TGF-β in trans.,, A recent study reveals that upon binding to αVβ8 integrin, the flexible membrane-presented latent complex can expose the active domain of the TGF-β ligand to its receptors for binding and signaling without the need to release diffusible cytokine.

TGF-β activation by acids and bases

12It has long been noticed that acidification can unmask the activity of freshly secreted TGF-β. Sharply defined parameters for human TGF-β activation by acids and bases show that the transition from latency of all three isoforms occurred between pH 2.5 and 4, and between pH 10 and 12. Thus, extremely acidic environments such as the microenvironments in tumor tissues and the resorption lacunae of osteoclasts are possibly conducive to local TGF-β activation., A study on lung fibrosis even suggests that physiologic concentrations of lactic acid are sufficient enough to activate TGF-β in a pH-dependent manner.

TGF-β activation by ROS

13TGF-β1 is the only isoform that can be directly activated by ROS, for a unique methionine residue at the amino acid position 253 of its LAP is required for oxidation-triggered conformational change. However, ROS can induce other TGF-β activators such as TSP-1 and MMPs to activate all three isoforms in an indirect manner. ROS-mediated TGF-β activation prevails in tissues exposed to asbestos,, ultraviolet, and ionizing radiation. High glucose intake can also induce ROS production and consequentially increase TGF-β activation to play roles in the development of fibrotic diseases and inflammatory diseases., Moreover, in T cells, ROS can be elevated during apoptosis or upon stimulation by T cell receptor (TCR) and cluster of differentiation 28 (CD28) to contribute to the immunosuppression mediated by activated TGF-β.,

TGF-β activation by TSP-1

14TSP-1 is a multi-functional ECM protein not only abundant in platelet α-granules but also secreted by fibroblasts, endothelial cells, macrophages, T cells, and many other cell types. The KRFK sequence in TSP-1 can recognize the LSKL sequence in LAP to competitively disrupt its interaction with the receptor-binding site of the TGF-β ligand. Since the LSKL sequence in LAP is conserved among TGF-β isoforms, it is suggested that the direct binding of TSP-1 to latent complex is capable of activating all three TGF-β isoforms through this protease- and cell-independent mechanism. Interestingly, TSP-1 can also bind to the mature TGF-β ligand to form a complex that retains the biological activity of the cytokine. ROS, glucose, angiotensin II, hypoxia, wounding, inflammation, pathogens,– and many other factors can all induce TSP-1 to function as a TGF-β activator in wound healing,, cardiovascular diseases,, renal diseases, fibrotic diseases,, inflammatory diseases, infectious diseases, and tumors.

TGF-β activation by proteases

15Many proteases have been proved capable of directly activating TGF-β in vitro. However, the function of an individual protease seems redundant in vivo, as deficiency of a single species generally leads to no significant signs of impaired TGF-β activation. Among these proteases, MMPs such as MMP-2, MMP-9, and MMP-13 are conducive to the TGF-β activation in wound healing, cardiovascular diseases, renal diseases, fibrotic diseases, and tumors. Interestingly, although the activation by MMPs works for all three TGF-β isoforms, latent TGF-β2 and TGF-β3 appear much more sensitive to MMP-9 treatment than latent TGF-β1. Moreover, a serine protease known as plasmin plays an important role in the TGF-β activation mediated by macrophages, and endothelial cells.,

Signal transduction of TGF-β

16TGF-β signal is transmitted into the cells by TβRI (also known as activin receptor-like kinase 5, ALK5) and TβRII both of which are enzyme-linked receptors with dual specificity of serine/threonine kinase and tyrosine kinase. Studies have revealed that TGF-β1 and TGF-β3 bind TβRII prior to TβRI due to higher affinity, while TGF-β2 binds poorly to both receptors.,, TβRIII, also known as β-glycan, lacks the motifs to directly mediate TGF-β signal transduction. However, TβRIII is able to bind TGF-β especially TGF-β2 with high affinity and thus acts as a co-receptor that presents the ligand to the receptors and further enhances their binding.,– The ligand-receptor interaction subsequently activates the intracellular signaling of TGF-β through a canonical pathway and several non-canonical pathways.

Canonical TGF-β signaling

17The canonical TGF-β signaling is mediated by transcription factors SMADs and thus is also known as the SMAD signaling. Notably, the canonical pathway is under the regulation of various factors that can control the intensity and manner of cellular responses at different levels (Fig. 3).

TGF-β-activated SMAD signaling

18TGF-β ligand initially binds to TβRII monomer to promote its homodimerization or directly binds to pre-existing TβRII homodimer to recruit TβRI for assembly.– This forms a heteromeric TGF-β-TβRI-TβRII complex in which low-affinity TβRI requires high-affinity TβRII to bind TGF-β ligand and constitutively active TβRII requires phosphorylating TβRI to transduce intracellular signal. The phosphorylation of TβRI occurs in its juxtamembrane GS domain at several serine and threonine residues, triggering conformational changes that transform the GS domain from a site that binds the signaling inhibitor known as immunophilin FK506-binding protein 1A (FKBP12) into a binding site for the signaling effectors known as receptor-activated SMADs (R-SMADs).

19R-SMADs, including SMAD2 and SMAD3, consist of a globular Mad homology 1 (MH1) domain at the N-terminus, a globular MH2 domain at the C-terminus, and a highly flexible long linker region in between. R-SMADs are retained in cytoplasm and presented to TβRI by the adaptor protein known as SMAD anchor for receptor activation (SARA). The R-SMAD MH2 domain then gets phosphorylated at two serine residues in the extreme C-terminal SXS motif by the TβRI kinase domain which is located immediately downstream of the TβRI GS domain. Activated R-SMADs undergo homo-oligomerization or hetero-oligomerization through their MH2 domains upon phosphorylation, and they can also oligomerize with SMAD4, the common-partner SMAD (co-SMAD) which lacks the SXS motif for phosphorylation by TβRI kinase. Notably, studies have suggested that SMAD heterotrimers containing two R-SMADs and one SMAD4 are likely more common and stable than other SMAD oligomers.– Although different SMAD oligomers can vary in function, they all act to regulate the transcription of target genes by binding to DNA after translocating into the nucleus. The MH1 domains of SMAD4, SMAD3, and a specific SMAD2 splicing variant recognize the nucleic acid sequence GTCT or its reverse complement AGAC in double-stranded DNA which are known as the canonical SMAD-binding elements (SBEs). Other SBEs such as the 5GC SBEs including GGCGC and GGCCG have also been discovered, indicating a relatively loose DNA-binding specificity of the SMAD oligomers. However, the binding to a single SBE is so weak that SMAD oligomers generally require interacting with replications of SBE copies as well as other DNA-binding sequence-specific transcription factors to function.,, In fact, many SBE repeats are enriched at the binding sites for SMAD-interacting transcription factors, exactly increasing the binding accessibility, specificity, and affinity of SMAD oligomers associated with specific transcription factors.– Despite a large number of SMAD-interacting transcription factors indicating a huge amount of potential gene targets for canonical TGF-β signaling, the dominant effects are generally determined by the master transcription factors in specific cell types and contexts which contribute to the complexity and variability of cellular responses to TGF-β.

Regulation of SMAD signaling by inhibitory SMADs (I-SMADs)

20TGF-β and many other factors can induce the expression of SMAD6 and SMAD7 which function to inhibit TGF-β signaling and thus are known as I-SMADs., Unlike R-SMADs, I-SMADs lack the N-terminal MH1 domain and the C-terminal SXS motif, however, they retain the C-terminal MH2 domain which can competitively bind to activated receptor TβRI to inhibit the phosphorylation of R-SMADs., Through some extra mechanisms, SMAD7 confers greater abilities in suppressing TGF-β signaling than SMAD6 does. For example, SMAD7 recruits E3 ubiquitin ligases such as SMAD ubiquitination regulatory factors (SMURFs) and neural precursor cell expressed, developmentally downregulated 4-like (NEDD4L) to TβRI, R-SMADs, and co-SMAD to mediate the proteasomal and lysosomal degradation of these TGF-β signaling components.– SMAD7 can also trigger the dephosphorylation of TβRI by recruiting protein phosphatase 1 (PP1) to the receptor. Moreover, with its MH2 domain, SMAD7 can oligomerize with R-SMADs to compete with co-SMAD and can bind to specific DNA sequences to disrupt the formation of the transcriptional SMAD-DNA complex. Taken together, TGF-β signaling induces I-SMADs to form a negative feedback loop of itself.

Regulation of SMAD signaling by transcriptional cofactors

21Transcriptional cofactors are actively recruited to the transcriptional SMAD complex to regulate its activity. Notably, many of these transcriptional cofactors have histone modification activity and thus enable TGF-β signaling to trigger epigenetic changes. Histone acetyltransferases (HATs) such as p300, cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB)-binding protein (CBP), p300/CBP-associated factor (PCAF), and general control non‐repressed protein 5 (GCN5) act as the transcriptional coactivators of SMADs by increasing the accessibility to DNA.– The interaction between p300/CBP and doubly phosphorylated R-SMADs requires SMAD4 for stabilization and is critical for SMAD-mediated transcriptional activation. Other SMAD coactivators include melanocyte-specific gene 1 (MSG1), zinc finger E-box-binding homeobox 1 (ZEB1),, and the histone methyltransferase (HMT) known as SET domain-containing protein 7 (SETD7). Contrary to HATs, histone deacetylases (HDACs) generally act as the transcriptional corepressors of SMADs by decreasing the accessibility to DNA. SMAD3 can directly recruit HDAC4 and HDAC5 to gene promoters to inhibit the function of transcription factors via histone deacetylation. SMADs can also associate with HDACs through interaction with other corepressors such as TGF-β-induced factor (TGIF), ecotropic viral integration site 1 (EVI1),, Sloan-Kettering Institute proto-oncogene (SKI),– as well as SKI-related novel gene N (SNO). Other transcriptional corepressors of SMADs include cellular-myelocytomatosis viral oncogene (MYC), SMAD nuclear-interacting protein 1 (SNIP1), ZEB2,, and HMTs such as suppressor of variegation 3-9 homolog 1 (SUV39H1) and SET domain bifurcated 1 (SETDB1) which can both trigger the methylation of histone 3 lysine 9 (H3K9) at gene promoters.,

Regulation of SMAD signaling by SMAD modifications

22Post-translational modifications can also regulate the functions of SMADs. Apart from TβRI kinase which phosphorylates R-SMADs in their C-terminal SXS motif to mediate their activation, many other protein kinases such as mitogen-activated protein kinase kinase kinase 1 (MAPKKK1), p38 MAPK, c-Jun N-terminal kinase (JNK), extracellular signal-regulated kinase (ERK),– rat sarcoma (RAS) homolog (Rho)-associated coiled-coil-containing protein kinase (ROCK), glycogen synthase kinase (GSK)-3β,– calcium/calmodulin-dependent protein kinase II (CAMK2), protein kinase C (PKC), PKG, and several cyclin-dependent kinases (CDKs),, can phosphorylate R-SMADs as well as co-SMAD at many different sites to enhance or attenuate SMAD activity. Meanwhile, the various phosphorylation of SMADs can be reversed by phosphatases. Several nuclear phosphatases known as the small C-terminal domain phosphatases (SCPs) can specifically dephosphorylate the linker region and MH1 domain of R-SMADs,, whereas protein phosphatase, magnesium/manganese-dependent 1A (PPM1A), myotubularin-related protein 4 (MTMR4), and protein phosphatase 2A (PP2A) catalyze the dephosphorylation of the C-terminal SXS motif to terminate the signaling and promote the dissociation and cytoplasmic localization of SMADs.

23Furthermore, SMADs can be ubiquitinated and deubiquitinated respectively by E3 ubiquitin ligases and deubiquitylating enzymes (DUBs). The E3 ubiquitin ligases that can mediate SMAD ubiquitination include SMURFs,,– NEDD4L,, WW domain-containing proteins (WWPs),– really interesting new gene (RING) finger protein 111 (RNF111), C-terminus of heat shock protein (HSP) 70-interacting protein (CHIP), itchy (ITCH) E3 ubiquitin ligase, and S-phase kinase-associated protein (SKP)-cullin-F-box (SCF) E3 ubiquitin ligase complex., The ubiquitination generally leads to the proteasomal degradation of SMADs, but in some cases, it also exerts non-degradative effects on SMAD activity. Notably, the degradative ubiquitination of R-SMADs by NEDD4L requires the phosphorylation of the R-SMAD linker by CDK8/9 and GSK-3 in sequence to create binding sites for the E3 ubiquitin ligase.,,

Non-canonical TGF-β signaling

24Apart from the SMAD-dependent pathway, TGF-β can also signal through SMAD-independent pathways to activate ERK signaling, Rho guanosine triphosphatase (GTPase) signaling, p38 MAPK signaling, JNK signaling, nuclear factor-κB (NF-κB) signaling, phosphatidylinositol 3-kinase (PI3K)/AKR mouse thymoma proto-oncogene (AKT) signaling, as well as Janus kinase (JAK)/signal transducer and activator of transcription (STAT) signaling. These non-canonical TGF-β signaling pathways are involved in an extensive range of cellular events, greatly expanding the participation of TGF-β signaling in health and disease (Fig. 4).

TGF-β-activated ERK signaling

25As a dual-specificity kinase, TβRI can phosphorylate at its tyrosine residues to activate ERK signaling upon TGF-β stimulation. In this case, TβRI with tyrosine kinase activity initially phosphorylates the adapter protein known as sarcoma (SRC) homology and collagen A (SHCA) which subsequently forms a complex with growth factor receptor-bound protein 2 (GRB2) and son of sevenless homolog (SOS). The SHCA-GRB2-SOS complex then initiates a canonical MAPK signaling cascade which involves the sequential activation of RAS, the MAPKKK known as RAS-associated factor (RAF), the MAPKK known as MAPK/ERK kinase (MEK), and eventually, the ERK MAPK. Activated ERK is known to regulate various biological events including cell survival, proliferation, differentiation, adhesion, migration, as well as metabolism, and is implicated in a spectrum of diseases such as developmental disorders, chronic inflammation, neurodegeneration, obesity, and cancers.,

TGF-β-activated Rho GTPase signaling

26Rho GTPases such as RHO, RAS-related C3 botulinum toxin substrate 1 (RAC1), and cell division cycle 42 (CDC42) play a central role in the organization and dynamics of the actin cytoskeleton. They are activated by guanine nucleotide exchange factors (GEFs) through the exchange of a bound GDP for GTP. TGF-β can trigger RHO activation in a rapid SMAD-independent manner or by inducing a GEF known as neuroepithelial cell transforming 1 (NET1) through SMAD and MEK/ERK pathways.– RHO then activates its key effector ROCK1 which further mediates the phosphorylation of LIM domain kinase 2 (LIMK2). Activated LIMK2 subsequently phosphorylates cofilin to inhibit its function as a constitutive actin-depolymerizing factor, leading to the reorganization of the actin cytoskeleton in the end.– Additionally, TGF-β-triggered RHO/ROCK1 signaling can contribute to ERK phosphorylation,, and besides RHO, TGF-β can also activate the signaling of other Rho GTPases such as RAC1 and CDC42. Besides the regulation of cell morphogenesis, adhesion, and movement, Rho GTPase signaling is also known to participate in transcriptional regulation, cell cycle progression, vesicular trafficking, and pathological processes such as fibrosis, inflammation, wound repair, and tumor development.,

TGF-β-activated p38, JNK, and NF-κB signaling

27TGF-β can activate the signaling of another two MAPKs known as p38 and JNK through a receptor kinase-independent mechanism which is different from that of ERK signaling. TGF-β-activated TβR complex can recruit tumor necrosis factor (TNF) receptor-associated factor 4 (TRAF4) and TRAF6 to trigger their lysine 63 (K63)-linked polyubiquitination. With E3 ubiquitin ligase activity, polyubiquitinated TRAF then attaches the polyubiquitin chain on the MAPKKK known as TGF-β-activated kinase 1 (TAK1) which subsequently gets activated and phosphorylates several MAPKKs (MKKs).– As a result, MKK3 and MKK6 specifically trigger the activation of p38 while MKK4 mediates the phosphorylation of both p38 and JNK. TGF-β-activated Rho GTPases such as RHOA, RAC1, and CDC42 can also contribute to p38 and JNK activation.,– Both the two MAPKs regulate a series of biological events to respond to all kinds of environmental and intracellular stresses, meanwhile, they engage actively in embryonic development, metabolic regulation, neuronal functions, immunological actions, as well as tumor development.–

28Additionally, TGF-β-activated TRAF/TAK1 signaling, RHO/ROCK1 signaling, and PI3K/AKT signaling can also lead to the phosphorylation of NF-κB inhibitor (IκB) kinase (IKK).– Activated IKK then triggers the phosphorylation of IκB which subsequently gets polyubiquitinated and degraded while releasing active NF-κB for nuclear translocation. NF-κB as a transcription factor can regulate hundreds of genes involved in cell survival, proliferation, metabolism, and immunity in particular.–

TGF-β-activated PI3K/AKT signaling

29The TβR complex can activate the lipid kinase PI3K upon TGF-β stimulation, either via the kinase activity of TβRI or through the recruitment of TRAF6, which polyubiquitylates PI3K regulatory subunit p85α independent of the receptor kinase., Activated PI3K then phosphorylates phosphoinositide phosphatidylinositol-4,5-bisphosphate (PIP2) into phosphatidylinositol-3,4,5-trisphosphate (PIP3) which further triggers the phosphorylation of AKT., Activated AKT targets plenty of substrates, including mechanistic target of rapamycin (MTOR),, GSK-3β, and several forkhead box O (FOXO) transcription factors.Among them, MTOR is the most common downstream effector of AKT, and ribosomal protein S6 kinase (S6K) and eukaryotic initiation factor 4E-binding protein 1 (4EBP1) are the best-characterized downstream effectors of MTOR. In general, the consequences of PI3K/AKT signaling include diverse cellular responses such as survival, metabolism, growth, proliferation, and differentiation.

TGF-β-activated JAK/STAT signaling

30TGF-β is found to induce JAK1 and JAK2 activation respectively in hepatic stellate cells (HSCs) and fibroblasts. In these cases, activated JAK triggers the phosphorylation of STAT3 which functions to mediate the fibrogenic effects of TGF-β, including increased cell proliferation, myofibroblast (MF) differentiation, ECM production, α-smooth muscle actin (α-SMA) expression, and stress fiber formation.– Like other signaling pathways, JAK/STAT signaling can also drive many physiological and pathological events, including development, metabolism, immunity, wounding, and cancers.

TGF-β signaling in health

31In physiological conditions, TGF-β signaling is greatly required by multiple biological processes and is particularly critical to embryonic development, wound healing, tissue homeostasis, and immune homeostasis (Fig. 5).

Embryonic development

32In situ hybridization and immunohistochemical staining reveal overlapping but distinct expression patterns of the three TGF-β isoforms at different developmental stages of murine embryos. TGF-β is expressed in nearly all kinds of embryonic tissues such as heart, vessels, lungs, kidneys, liver, gut, bones, teeth, cartilages, muscles, skin, thymus, thyroid, suprarenal glands, salivary glands, nervous system, and craniofacial tissues.,– In particular, mesenchymal and epithelial components undergoing organogenesis and morphogenesis which involve active cell differentiation and epithelial-mesenchymal interactions generally express high levels of TGF-β.,–

33TGF-β has a significant impact on cell differentiation. Studies on Xenopus embryos reveal that TGF-β can induce mesoderm formation which is a primary patterning event in early vertebrate development., TGF-β can further regulate the development of hemangioblasts from mesoderm as well as subsequent differentiation of hematopoietic stem and progenitor cells (HSPCs) to participate in hematopoiesis and vasculogenesis.,– Mesenchymal stem cells (MSCs) which are derived from the mesoderm as well also respond actively to TGF-β signaling during their differentiation into several connective tissue cell lineages such as osteocytes, chondrocytes, myocytes, and adipocytes., TGF-β inhibits osteogenic differentiation by inducing the nuclear translocation of β-catenin and repressing the transcriptional activity of core-binding factor subunit α-1 (CBFA1) in a SMAD3-dependent manner., TGF-β-induced SMAD signaling also inhibits myogenesis and adipogenesis by respectively repressing the transcriptional activity of myogenic differentiation (MYOD) family members– and CCAAT/enhancer-binding proteins (C/EBPs).,, However, the differentiation of MSCs into smooth muscle cells (SMCs) is promoted by TGF-β through mechanisms involving the activation of SMAD signaling, RHO signaling, and NOTCH signaling. Moreover, TGF-β stimulates chondrogenesis by inducing mesenchymal cells to differentiate into chondrocytes and produce cartilage-specific proteoglycan and type II collagen.,, As for other cell types, TGF-β signaling also regulates the differentiation and development in epidermis, lungs,, kidneys, pancreas,, teeth, and nervous system.–

34Especially for epithelial cells, TGF-β can induce a reversible de-differentiation process known as epithelial-mesenchymal transition (EMT) which is critical to embryonic development. During EMT, epithelial cells lose their cellular polarity, intercellular junctions, and epithelial markers such as E-cadherin, but turn to acquire mesenchymal or fibroblastic phenotype with increased cell migratory motility, ECM proteolytic activity, and expression of mesenchymal markers such as fibronectin. This process is generally mediated by transcription factors such as SNAIL, SLUG, ZEB, and TWIST, involving both SMAD-dependent and SMAD-independent pathways in the case of TGF-β signaling.,,,–,, The developmental functions of TGF-β-induced EMT have been well studied in embryonic palate formation during which the expression of TGF-β is significantly elevated., Among the three TGF-β isoforms expressed in developing murine palate,, only TGF-β3 is indispensable to the fusion of palatal shelves which is a crucial step during palatogenesis. Mechanically, TGF-β3 induces the EMT of palatal midline epithelial seam (MES) cells, leading to the disintegration of the epithelium and subsequent confluence of the mesenchyme., Interestingly, endothelial cells can undergo a similar process known as endothelial-mesenchymal transition (EndMT) which is crucial for cardiovascular development. In humans, TGF-β2 is the most potent inducer of EndMT, while TGF-β1 and TGF-β3 at least partially rely on the induction of TGF-β2 to trigger this process. Consistently, although all three TGF-β isoforms are differentially expressed during murine cardiogenesis,,,,,– only TGF-β2 is obligatory to the EndMT during the endocardial cushion development in the atrioventricular canal which is necessary to valvular formation.– Moreover, TGF-β1 and TGF-β2 can trigger EndMT in the epicardium to contribute to coronary vessel formation., In fact, TGF-β signaling is essential to vasculogenesis in many developing tissues by promoting the proliferation and migration of endothelial cells.,

35Furthermore, TGF-β can induce apoptosis of unnecessary cells during embryonic development to ensure proper histogenesis and organogenesis. During murine palatogenesis, the disintegration of MES not only relies on TGF-β3-induced EMT as introduced above but also requires TGF-β3-induced apoptosis of MES cells to complete palatal confluency. In murine limb buds, highly expressed TGF-β triggers massive cell death in the mesenchyme of interdigital spaces to induce the regression of interdigital webs and the formation of free digits.,, Endogenous TGF-β also mediates the apoptotic death of certain neuron types in chick embryos to contribute to nervous system development. Notably, TGF-β2 and TGF-β3 presenting in the central part of the developing chick retina are essentially required to trigger retinal cell apoptosis, which can create space for incoming axons of retinal ganglion cells to form optic nerve., In mice, however, TGF-β signaling also protects retinal neurons from excessive apoptosis to ensure proper development of eyes.

Wound healing

36Wound healing which happens after tissue injuries generally involves four orderly and overlapping stages known as hemostasis, inflammation, proliferation, and remodeling. Throughout the healing of cutaneous wounds, all TGF-β isoforms and TβR types are induced in a distinct spatial and temporal pattern., During hemostasis, platelets provide an immediate and abundant supply of TGF-β after wounding, contributing largely to subsequent healing stages by promoting the influx of inflammatory cells and fibroblasts into the wounds due to its chemotactic activity.,– Interestingly, many of the cell types recruited by TGF-β are also active in secreting TGF-β, leading to even higher TGF-β concentrations in the wounds. In ovine skin, all three TGF-β isoforms increase dramatically only one day after wounding, attributed to the expression by epithelial cells, endothelial cells, fibroblasts, and inflammatory cells such as neutrophils, macrophages, and lymphocytes. During the stage of proliferation and remodeling, TGF-β is implicated in wound re-epithelialization, tissue angiogenesis, and fibroblast activation., Upon cutaneous injury, TGF-β1 is initially expressed by all epidermal keratinocytes adjacent to the wounds but gradually gets excluded from the basal keratinocytes, corresponding to the transient block and subsequent burst of basal keratinocyte proliferation after wounding. TGF-β1 also contributes to the migration of epithelial sheets at the leading edges of cutaneous wounds through the regulation of integrins and the activation of PI3K.– Other TGF-β isoforms such as TGF-β3 can have similar impacts on cell migration during cutaneous wound healing. As for angiogenesis, TGF-β regulates the proliferation and migration of endothelial cells in vitro and shows potent angiogenic activity when overexpressed or directly applied in vivo.,– A possible mechanism of TGF-β-induced angiogenesis involves the induction of vascular endothelial growth factor (VEGF) in epithelial cells and fibroblasts., Moreover, TGF-β can stimulate fibroblasts to proliferate and produce bioactive factors such as collagen, fibronectin, MMPs, tissue inhibitor of MMPs (TIMPs), and plasminogen activator inhibitor 1 (PAI-1) which contribute to the deposition and remodeling of wound ECM.,,,,,,– It can also promote fibroblast-mediated wound contraction through MF differentiation and RHO activation.–

37Apart from the skin, TGF-β also functions in the repair and regeneration of many other tissues. During rat liver regeneration, all TGF-β isoforms are induced in non-parenchymal cells rather than hepatocytes, which however, exhibit upregulation of all TβR types to enhance the responsiveness to TGF-β, which may help to prevent uncontrolled cell proliferation.– Similarly, the marked increase in TGF-β and TβR expression following acute pancreatitis suggests the role of TGF-β signaling in pancreatic repair.– Upon vascular injury, TGF-β mobilizes MSCs to peripheral blood and further recruits them to the injured sites for vascular repair. As for cardiac repair after myocardial injury, TGF-β triggers the EndMT of epicardial cells, which then migrate into the injured myocardium to generate various cardiac cell types. TGF-β also plays a role in cartilage repair by stimulating proteoglycan synthesis in chondrocytes., Moreover, after injury in the nervous system, neurons, astrocytes, microglia, as well as recruited macrophages all upregulate the expression of TGF-β which may contribute to the healing process of the nervous tissues.,

Tissue homeostasis

38Tissue homeostasis is maintained by the balance between cell proliferation and cell death in which TGF-β acts as a key regulator.

39Cell proliferation is generally driven by CDKs through a series of events collectively known as the cell cycle. For most cells, TGF-β inhibits their proliferation, or in other words, triggers their cytostasis by inducing cell cycle arrest in the gap 1 (G1) phase. In epithelial cells and glial cells, TGF-β suppresses the activity of CDKs by activating the transcription of CDK inhibitors (CKIs) such as p15 and p21 to induce cytostasis.– The transcriptional activation of CKIs in response to TGF-β is likely mediated by SMADs in cooperation with transcription factor FOXO, or specificity protein 1 (SP1)., Notably, the SMAD-FOXO complex additionally requires transcription factor C/EBPβ for the induction of p15 but not of p21. In epithelial cells, TGF-β-mediated upregulation of p15 also prevents the non-inhibitory binding of CKI p27 to CDK4. As a result, p15 and p27 turn to bind their own targets which are respectively CDK4 and CDK2 to exert their inhibitory effects., Interestingly, in murine B cells, TGF-β increases the expression of p27 instead of p21 to trigger cytostasis, while in human hematopoietic cells, p57 is likely the only TGF-β-induced CKI for cell cycle arrest. Besides CKIs, TGF-β can also target other proliferative factors such as MYC, inhibitors of DNA binding (IDs), and CDC25A to inhibit cell proliferation as mostly shown in epithelial cells. TGF-β induces the transcriptional repression of MYC through a complex containing SMADs, transcription factors E2F4/5 and C/EBPβ, as well as transcriptional corepressor p107.,, It also inhibits ID1 expression through SMADs which mediate the induction and recruitment of transcriptional repressor activating transcription factor 3 (ATF3) to target ID1 promoter. As for ID2 which can be induced by MYC at the transcriptional level, its suppression by TGF-β is attributed to the downregulation of MYC or the upregulation of antagonistic MYC repressors known as MYC-associated factor X (MAX) dimerization proteins (MADs)., By these means, TGF-β is able to relieve the transcriptional repression on CKIs exerted by MYC and IDs to facilitate the induction of cytostasis.– Furthermore, TGF-β can downregulate the activity of the CDK-activating phosphatase CDC25A through several mechanisms such as the transcriptional repression by E2F4-p130-HDAC1 complex, the inhibitory phosphorylation by RHOA/ROCK1 signaling, as well as the SMAD3-dependent degradative ubiquitination by E3 ubiquitin ligase complex SCF. Notably, TGF-β can also stimulate the proliferation of certain cell types, including SMCs, fibroblasts, and chondrocytes, likely due to the induction of autocrine growth factors such as fibroblast growth factor (FGF) and platelet-derived growth factor (PDGF).,,

40As for cell death, TGF-β can trigger apoptosis which is one of the most common forms of cell death in a wide range of cell types including lymphocytes, hepatocytes, podocytes, glial cells, hematopoietic cells, and epithelial cells. Such effect is generally attributed to SMAD-dependent regulation of B-cell lymphoma-2 (BCL-2) family members. More specifically, TGF-β can upregulate pro-apoptotic BCL-2 family members such as BCL-2-associated X protein (BAX) and BCL-2-interacting mediator of cell death (BIM),– meanwhile, it can also downregulate anti-apoptotic BCL-2 family members such as BCL-2 and BCL-extra-large (BCL-XL).,, Apart from BCL-2 family members, many other effectors and pathways are also involved in TGF-β-induced cell apoptosis. A septin-like protein known as apoptosis-related protein in the TGF-β signaling pathway (ARTS) undergoes mitochondrial-to-nuclear translocation to promote cell apoptosis in response to TGF-β. Death domain-associated protein (DAXX) interacts with TβRII as an intermediary to convey pro-apoptotic TGF-β signal to downstream machinery. In B cells and hepatocytes, TGF-β triggers the transient activation of TAK1/IKK/NF-κB pathway, sequentially leading to the transcriptional activation of IκB-α, the post-repression of NF-κB, the upregulation of JNK signaling, the increase of activator protein 1 (AP-1) complex activity, and finally, the apoptotic death of cells.– In hepatocytes, TGF-β also promotes the expression of growth arrest and DNA damage-inducible β (GADD45β), which functions as a positive mediator of cell apoptosis by acting upstream of p38 MAPK. As for podocytes, TGF-β can activate both pro-apoptotic p38 signaling and anti-apoptotic PI3K/AKT signaling to regulate their survival and death., In fact, AKT, especially when phosphorylated, can bind to unphosphorylated SMAD3 to inhibit its activity and thus protect several cell types from SMAD-dependent apoptosis. In contrast, TGF-β can prevent the AKT-SMAD3 interaction by triggering SMAD3 phosphorylation to facilitate the cell death program., Moreover, in hematopoietic cells, SMAD-dependent TGF-β signaling induces the expression of a central regulator of phospholipid metabolism known as SRC homology 2 (SH2) domain-containing inositol 5’-phosphatase (SHIP) to inhibit AKT phosphorylation as well as cell survival. Furthermore, TGF-β triggers the apoptosis of oligodendrocytes and epithelial cells by inducing transcription factors TGF-β-inducible early genes (TIEGs) to downregulate BCL-XL expression.– Notably, TGF-β is also found to promote cell survival in certain cases.,– Related mechanisms involve the AKT-dependent inhibition of FOXO3 as in epithelial cells, the suppression of AKT and the induction of BCL-2 as in pre-B lymphocytes, the early induction and phosphorylation of c-Jun and consequential attenuation of JNK as in lung carcinoma cells, the downregulation of CD95L and p53 as well as the upregulation of NF-κB, BCL-XL, and p21 as in HSCs.

Immune homeostasis

41Generally, TGF-β functions to suppress the activity of multiple immunocompetent cells while inducing the phenotypes of several immune immunosuppressive cells. For this reason, it is regarded as one of the most potent immunosuppressive cytokines which are of vital importance to the maintenance of immune homeostasis and self-immune tolerance.

Cytotoxic T lymphocytes (CTLs), T helper type 1 (Th1), and Th2 cells

42TGF-β prevents naïve T cells from differentiating into classical effecter T cells through numerous mechanisms. For CD8+ T cells which can develop into CTLs upon activation, TGF-β inhibits their functions by suppressing the expression of cytolytic factors such as perforin, granzyme A, granzyme B, Fas ligand, and interferon (IFN)-γ. Mechanically, the encoding genes of granzyme B and IFN-γ are directly recognized by SMADs and transcription factor ATF1 which both bind to the gene promoter regions to mediate transcriptional repression in response to TGF-β signaling. The suppression of IFN-γ release is also correlated to the reduction of transcription factor T-box expressed in T cells (T-BET) while the decrease in Fas ligand expression is partially attributed to the downregulation of MYC. In CD4+ T cells, TGF-β inhibits the phosphorylation of T-cell kinase (ITK) to decrease the influx of calcium ion and subsequent activation of nuclear factor of activated T cells (NFATC) which are both critical events for Th1 and Th2 cell differentiation. TGF-β also suppresses the expression of transcription factors T-BET and GATA-3 in CD4+ T cells which act as master transcriptional activators during Th1 and Th2 cell development respectively.–

Tregs, Th9, and Th17 cells

43TGF-β induces the expression of transcription factor forkhead box P3 (FOXP3) in an interleukin (IL)-2-dependent manner in CD4+ CD25− naïve T cells to convert them into CD4+ CD25+ Tregs which can express TGF-β and inhibit other T cell proliferation with potent immunosuppressive activity.– Similarly, TGF-β can induce the generation of Tregs from CD8+ T cells through the expression of FOXP3., Interestingly, IL-4 inhibits the induction of FOXP3 by TGF-β in naïve CD4+ T cells, instead, both cytokines cooperate to drive the differentiation of another Th cell subset known as Th9 cells by inducing the expression of transcription factor purine-rich box-1 (PU.1).– Unlike the immunosuppressive Tregs, these IL-9- and IL-10-secreting cells can potently promote tissue inflammation.– In addition, inflammatory cytokines such as IL-1β, IL-6, IL-21, and IL-23 also suppress TGF-β-induced FOXP3 in naïve CD4+ T cells, meanwhile, they elevate the activity of a TGF-β-induced transcription factor known as retinoic acid receptor-related orphan receptor γt (RORγt) to contribute to the generation of Th17 cells. This pro-inflammatory Th cell subset characterized by IL-17 expression plays important roles in anti-microbial defense and autoimmunity.,

B cells

44As critical effectors of humoral immune responses, B cells mainly function by secreting antibodies which are also known as immunoglobulins (Igs). TGF-β decreases B cell Ig secretion by inhibiting the synthesis and the switch from the membrane form to the secreted form of Ig messenger ribonucleic acids (mRNAs). More specifically, TGF-β selectively inhibits the expression of Ig λ light chains while inducing less pronounced reductions in Ig κ light chains,, moreover, it suppresses the production of isotypes IgM and IgG but enhances the class switching to isotype IgA.,, Notably, TGF-β-induced IgA with poor specificity is considered insufficient to mediate immune responses such as antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cellular phagocytosis (ADCP)., Furthermore, TGF-β can convert B cells into regulatory B cells (Bregs) which produce numerous factors such as TGF-β, IL-10, IL-35, Fas-L, and programmed death-ligand 1 (PD-L1) to mediate immunosuppression.–

Natural killer (NK) cells

45NK cells are cytotoxic lymphocytes of the innate immunity. TGF-β suppresses NK cell development by downregulating transcription factor E4 promoter-binding protein 4 (E4BP4) in a SMAD3-dependent manner. The SMAD3 also decreases NK cell IFN-γ secretion through the inhibition of E4BP4 and T-BET., Moreover, TGF-β downregulates the surface expression of NK triggering receptors such as NKP30 and NK group 2 member D (NKG2D) which are responsible for the recognition and killing of target cells., It also negatively regulates the expression of cytolytic factors such as granzyme A, granzyme B, and perforin through SMAD signaling to further impair NK cytotoxicity.,

DCs, macrophages, and neutrophils

46DCs, macrophages, and neutrophils can function as antigen-presenting cells (APCs), which are the keys to the activation of adaptive immune responses. TGF-β can impair antigen presentation through the downregulation of major histocompatibility complex (MHC) molecules.– It also reduces the expression of IL-12 and co-stimulatory molecules such as CD40 in macrophages and CD80, CD83, and CD86 in DCs to interfere in APC-mediated immune cell activation., Apart from antigen presentation, TGF-β also inhibits the cytotoxicity of macrophages, on one hand, through the downregulation of cytotoxic factors, such as TNF-α and nitric oxide (NO),– on the other hand, by suppressing the activity of Fcγ receptors (FcγRs) which function to mediate the ADCC and ADCP of macrophages. Moreover, TGF-β can trigger the polarization of macrophages and neutrophils from classical M1 macrophages and N1 neutrophils to alternative M2 macrophages and N2 neutrophils which are characterized by multiple immunosuppressive properties.,–

TGF-β signaling in disease

47Dysfunctional TGF-β signaling can play key roles in numerous pathological processes, contributing to the disorders of developmental defects, aberrant healing, fibrotic diseases, inflammatory diseases, infectious diseases, as well as tumors (Fig. 6).

Developmental defects

48Loss of TβRI or TβRII functions due to homozygous mutations generally results in embryonic lethality in mice due to defects in the hematopoiesis and vasculogenesis of yolk sac., However, the lack of different TGF-β isoforms can lead to distinct phenotypes in mice, consistent with the isoform-specific roles of TGF-β in embryonic development. TGF-β1-knockout mice show no gross developmental abnormalities in spite of the defective hematopoiesis and vasculogenesis in yolk sac during embryonic development.– In contrast, TGF-β2-knockout mice exhibit perinatal mortality and a wide range of developmental defects in heart, lungs, bones, eyes, inner ears, craniofacial structures, urogenital organs, and hair follicles.,– TGF-β3-knockout mice also die shortly after birth but show no detectable abnormalities except for cleft palate and abnormal lung development., Notably, palatal shelves that fail to elevate in TGF-β2-knockout mice undergo elevation in TGF-β3-knockout mice but still fail in fusion.,, Also, branching morphogenesis and respiratory epithelial cell differentiation which appear normal in the lungs of TGF-β2-knockout mice are defective in TGF-β3-knockout mice., In humans, loss-of-function mutations of a single TGF-β signaling component such as TGF-β2,– TGF-β3,– TβRI,– TβRII,– SMAD2,– or SMAD3– can cause Loeys-Dietz syndrome (LDS), an autosomal dominant connective tissue disorder with a range of cardiovascular, skeletal, craniofacial, and cutaneous manifestations. LDS patients typically present with features including congenital heart defects, aneurysms, arterial tortuosity and dissections, skeletal overgrowth, cervical spine instability, clubfoot deformity, craniosynostosis, hypertelorism, bifid uvula, cleft palate, thin skin, and mental retardation. Dermal fibroblasts derived from LDS patients demonstrate impaired deposition of extracellular collagen and elastin, suggesting a possible mechanism of the connective tissue defects of the patients., However, the aortic tissues of LDS patients show increased accumulation of collagen, elevated expression of connective tissue growth factor (CTGF), and enhanced activity of non-mutant TGF-β signaling components.–,,,,,,, Therefore, primary downregulation and compensatory upregulation of TGF-β signaling are both responsible for the abnormalities of LDS.

49Excessive TGF-β signaling can also act as a primary pathogenic factor in developmental defects. In mice, overexpression of TGF-β or SMAD can lead to developmental abnormalities in several tissues, such as skin,, bones, eyes, lungs,, mammary glands,– salivary glands, and central nervous system. In humans, Camurati-Engelmann disease (CED), a progressive bone dysplasia inherited in an autosomal dominant manner, is ascribed to mutations of TGF-β1, which lead to increased TGF-β1 activation and signaling., This disease is characterized by hyperostosis and sclerosis of the long bones and the skull., Studies on CED have suggested that hyperactive TGF-β1 in the bone microenvironment can induce osteoclasts and osteoblasts to increase but cluster in separated areas, uncoupling bone resorption and formation to cause bone remodeling defects.,,

Aberrant healing and fibrotic diseases

50Dysregulated TGF-β signaling can contribute to the tissue damage in aberrant healing and fibrotic diseases which are caused by all kinds of injuries such as wounding, burns, radiation, infection, and inflammation.

Aberrant healing

51The lack of TGF-β and TβR expression is commonly found in the chronic wounds in patients, indicating that deficient TGF-β signaling may lead to wound chronicity and even unhealing.– However, in vivo studies in mice have reported quite complicated findings. An activating mutation of TβRI can lead to a regenerative healing phenotype which enables rapid regeneration of normal tissues with differentiated structures instead of scar formation in ear punch wounds. Paradoxically, overexpression of TGF-β1 in keratinocytes accelerates the re-epithelialization in partial-thickness cutaneous wounds but slows that of full-thickness cutaneous wounds., In TGF-β1-deficient mice, the healing of full-thickness cutaneous wounds is initially normal but ultimately damaged by severe inflammatory diseases. In immunodeficient mice without inflammatory diseases, the lack of TGF-β1 still leads to significant delays in each healing stage of full-thickness cutaneous wounds. However, loss of TGF-β signaling in keratinocytes due to expression of dominant negative TβRII leads to increased proliferation and reduced apoptosis, thus facilitating the re-epithelialization in full-thickness cutaneous wounds. Furthermore, cutaneous wound healing is accelerated in mice lacking SMAD3 but is aberrant in mice lacking SMAD4 exclusively in keratinocytes.,

52In contrast to chronic wounds, hypertrophic scars and keloids both characterized by overabundant ECM deposition are the results of hyperactive cutaneous wound healing. In fact, the expression of TGF-β and TβR which decreases eventually in normal cutaneous wounds remains elevated in hypertrophic scars and keloids.– In contrast to normal cutaneous fibroblasts, both keloid fibroblasts and hypertrophic scar fibroblasts are significantly higher in collagen production, however, only keloid fibroblasts exhibit increased sensitivity to TGF-β stimulation. For keloid fibroblasts, overexpressed TGF-β can promote the resistance to apoptosis, the ability of proliferation, the conversion to MFs, and the expression of CTGF and VEGF, thus contributing to the ECM deposition, focal adhesion, fibrous growth, and angiogenesis in keloid tissues.,–

Fibrotic diseases

53Besides wounding, other forms of injurious stimulation can also cause excessive ECM deposition in different kinds of tissues, leading to fibrotic diseases, which are closely associated with the hyperactivity of TGF-β signaling.

54TGF-β expression is significantly elevated in fibrotic lungs in various cases such as idiopathic pulmonary fibrosis (IPF) and cystic fibrosis (CF).– In situ hybridization and immunohistochemical staining suggest that alveolar macrophages and epithelial cells are likely the major sources of TGF-β which contribute to the fibrosis of lungs.– In vitro studies show that TGF-β1 can trigger the EMT of alveolar epithelial cells and enhance the activity of lung fibroblasts to mediate fibrogenic effects.– Transgenic expression of TGF-β1 in murine and rat lungs induces pulmonary fibrosis which is accompanied by alveolar EMT, MF differentiation, and mononuclear-rich inflammation.– Interestingly, the suppression of TGF-β1, the deletion of TβRII, the ablation of SMAD3, the upregulation of SMAD7, but the administration of TGF-β3 can all significantly protect mice from experimentally induced pulmonary fibrosis.–

55Similarly, the fibrotic kidneys of human glomerulonephritis, IgA nephropathy, diabetic nephropathy, lupus nephritis, as well as renal allografts in chronic rejection all show significant increases in three TGF-β isoforms in the glomeruli and tubulointerstitium where ECM deposition and PAI-1 production is closely related to the expression of TGF-β1 isoform in particular.– In vitro, TGF-β1 stimulates kidney fibroblasts, mesangial cells, glomerular epithelial cells, and tubular epithelial cells to produce several ECM components and remodelers such as collagen, fibronectin, laminin, proteoglycan, MMP, and TIMP.– TGF-β1 also contributes to the EMT induction and MF differentiation in renal fibrosis. Transgenic mice that have increased levels of TGF-β1 in plasma develop progressive renal disease characterized by glomerulosclerosis and tubulointerstitial fibrosis with TIMP overexpression and ECM deposition in sub-endothelial and mesangial locations.,

56In fibrotic livers, TGF-β1 expression increases markedly with fibrogenic activity.– Induction of TGF-β1 expression in murine livers leads to hepatic fibrosis characterized by prominent ECM deposition in peri-sinusoidal areas with activation of HSCs and apoptosis of hepatocytes., Notably, activated HSCs which play a major role in hepatic fibrosis can provide an important source of TGF-β, while overproduced TGF-β can in turn activate several signaling pathways such as those of SMAD, MEK, JNK, PI3K, and JAK/STAT in HSCs to contribute to their functions.,

57As for the cardiovascular system, TGF-β is also elevated during myocardial fibrosis, valve fibrosis, and arteriosclerosis, generally attributed to the expression by SMCs, fibroblasts, endothelial cells, and inflammatory cells such as macrophages.– On one hand, TGF-β can stimulate cardiovascular fibroblasts to differentiate into MFs and produce ECM components and remodelers,,,– on the other hand, it can also stimulate endothelial cells to undergo EndMT to induce their fibrogenic phenotype.,,

58Furthermore, TGF-β is widely involved in the fibrosis of many other tissues and diseases as in the cases of cutaneous fibrosis,, muscular fibrosis, pancreatic fibrosis,– myelofibrosis,, adenomyosis, autoimmune diseases,,,,– and infectious diseases.–

Inflammatory diseases and infectious diseases

59Inflammatory diseases and infectious diseases can demonstrate aberrant immune responses and various tissue injuries which usually implicate the dysfunction of TGF-β signaling.

Inflammatory diseases

60Since TGF-β acts as a negative regulator to maintain immune homeostasis, deficient TGF-β signaling can lead to hyperactive immune responses, contributing to the pathology of numerous inflammatory diseases. TGF-β1-null mice initially appear normal after birth but soon develop a rapid wasting syndrome accompanied by a multifocal inflammatory disease which leads to organ failure and early death by 3-4 weeks of age.,– Many organs in these mice, including heart, lungs, stomach, liver, pancreas, and muscles, all exhibit massive infiltration of inflammatory cells such as lymphocytes, macrophages, and granulocytes. Moreover, their total numbers of blood leukocytes increase mainly due to the elevated absolute numbers of neutrophils and monocytes, while their levels of autoantibodies, MHC molecules, and inflammatory cytokines such as IFN-γ, TNF-α, and CCL3 also rise correspondingly in serum or tissues.

61In the absence of any pathogens, the inflammatory diseases in TGF-β1-knockout mice actually resemble a special group of inflammatory diseases known as autoimmune diseases, which are characterized by dysregulated immune responses attacking self-tissues. In fact, even cell type-specific loss of TGF-β signaling can lead to the development of various autoimmune diseases in mice.– In patients with autoimmune diseases such as systemic lupus erythematosus (SLE),– systemic sclerosis (SSc),– rheumatoid arthritis (RA),– Sjögren’s syndrome,,– Crohn’s disease,,– ulcerative colitis (UC),– autoimmune hepatitis (AIH),, and Hashimoto’s thyroiditis (HT),,, the levels of TGF-β or TβR in tissues or circulation are associated with the presence, activity, and severity of the diseases. Notably, although all these diseases show correlations with dysregulated TGF-β signaling, their correlations with TGF-β levels can be either positive or negative. Some cases of the diseases are likely caused by insufficient TGF-β expression and thus exhibit decreased TGF-β production.,,– In other cases, however, the autoimmune inflammation is likely attributed to impaired cell responsiveness to TGF-β especially due to deficient TβR functions, therefore, TGF-β production is elevated as a compensatory response.,,–

62Allergic diseases, including asthma, allergic rhinitis, food allergy, and atopic dermatitis, are another group of inflammatory diseases that are caused by aberrant immune responses to harmless environmental antigens. TGF-β production is increased in the airways and serum of asthmatic patients and is further increased after allergen exposure, disease progression, or certain treatments.– Bronchial epithelial cells, fibroblasts, SMCs, eosinophils, neutrophils, and macrophages can all contribute to the excessive TGF-β production in asthmatic patients.– However, the functions of TGF-β are seemingly contradictory in the context of allergic airway inflammation, for TGF-β can either enhance or suppress the activity of eosinophils, lymphocytes, macrophages, and mast cells in asthma.,– Nevertheless, it is clear that TGF-β can promote asthmatic airway remodeling by inducing airway EMT,, ECM production,, MF differentiation,, and smooth muscle hyperplasia. In patients with allergic rhinitis, TGF-β levels in serum are found dependent on allergen exposure, while TGF-β and TβR expression in nasal mucosa is noticed correlated with intra-epithelial mast cell abundance.– In fact, allergen challenge can activate TGF-β signaling in the mast cells and epithelial cells in nasal mucosa which may contribute to the mast cell accumulation and goblet cell hyperplasia in allergic rhinitis., Allergen challenge can also induce the loss of TGF-β1-expressing Bregs and Tregs which function to suppress the inflammatory Th2 responses of allergic rhinitis. However, with prolonged challenging time, the proportion of TGF-β1-expressing Bregs and Tregs can gradually recover to reconstitute the immune homeostasis in nasal mucosa. Similarly, TGF-β can inhibit the Th2 responses of food allergy by promoting Treg activity in the intestines.,, Therefore, reduced TGF-β1 expression in the intestinal epithelial cells and mononuclear cells of patients with food allergy can partially account for the development of the disease., Moreover, TGF-β can inhibit the pathology of atopic dermatitis by suppressing B cell maturation, mast cell activation, eosinophil infiltration, as well as the secretion of IgE, TNF-α, and histamine by those cells.– Aberrant TGF-β expression or attenuated cell responsiveness discovered in patients with atopic dermatitis may play a key role in the disorder.–

63Furthermore, TGF-β signaling is implicated in the pathology of other inflammatory diseases and inflammation-related diseases such as bronchitis, pancreatitis,– glomerulonephritis,, osteomyelitis, arthritis, diabetes, and Alzheimer’s disease (AD).,

Infectious diseases

64Infectious diseases caused by different kinds of pathogenic organisms can result in tissue damage due to diverse pathogen virulence and dysregulated host responses.

65TGF-β can function to reduce pathogen burdens as well as tissue injuries in some cases of infection. In patients with H1N1 influenza A virus sepsis, blood TGF-β levels are negatively correlated with clinical severity scores on admission. Consistently, increased TGF-β activity in mice confers resistance against lethal influenza infection due to reductions in both viral titers and pulmonary inflammation., TGF-β expression also prevents mice from coxsackievirus-induced myocarditis and type 1 diabetes in a Treg-dependent manner., Moreover, TGF-β acts as a pro-survival factor to protect murine neurons and intestinal epithelial cells against cell death during reovirus infection., As for bacterial infection, TGF-β can attenuate sepsis-induced tissue injuries through mechanisms involving the induction of Tregs. It also enhances the pathogen clearance and host resistance of mice during the infection of Streptococcus pneumoniae, Streptococcus pyogenes, Listeria monocytogenes, and Yersinia enterocolitica, likely, by suppressing IFN-γ, TNF-α, and IL-6 production while promoting Th17 and Treg responses. In rats with pulmonary cryptococcosis, TGF-β reduces fungal burdens by promoting the lysozyme secretion of macrophages, meanwhile, it also limits inflammation by inhibiting macrophage phagocytosis, chemokine production, and oxidative burst. Moreover, TGF-β can be protective during parasitic infection. The lack of TGF-β exacerbates the severity of murine malaria infection, whereas TGF-β treatment, in contrast, suppresses plasmodium proliferation and prolongs mice survival with decreased TNF-α and increased IL-10 in serum. During Trypanosoma congolense infection, exogenous TGF-β1 confers early protection against parasitemia, anemia, splenomegaly, and mortality due to enhanced macrophage activity and Th1 responses which are characterized by increased NO, IFN-γ, TNF-α, IL-12, and IgG2a production. During Toxoplasma infection, TGF-β can prevent tissue damage by reducing inflammatory cell infiltration and cytokine production, while it can also improve the outcomes of infection-related abnormal pregnancy by promoting Treg functions and suppressing NK cytotoxicity.– Furthermore, TGF-β can prevent the lung injuries during hookworm infection by inducing the immunosuppressive activity of myeloid cells to reduce Th2 responses.

66In other cases of infection, however, TGF-β can turn to facilitate pathogen infection and tissue injuries. In clinical patients, circulating TGF-β1 levels are positively correlated with the severity and mortality of severe community-acquired pneumonia (CAP) and sepsis-induced acute respiratory distress syndrome (ARDS). Increased TGF-β production can impair the anti-bacterial functions of neutrophils, uncouple the cytokine production and glycolysis of macrophages, and suppress the IL-2 expression and proliferation of T cells to participate in the pathology of sepsis.– As for bacterial infection in local tissues, on one hand, TGF-β can upregulate fibronectin and integrins in hosts to promote bacterial adhesion and invasion,, on the other hand, it can attenuate anti-infectious innate responses and Th1 responses while inducing immunotolerant Treg responses to facilitate the immune escape of the pathogens.– TGF-β-mediated immunosuppression can also contribute to viral infection, as elevated TGF-β expression during viral infection not only impairs early innate immunity such as IFN responses, NK functions, and macrophage activity but also suppresses the adaptive immune responses of T cells and B cells.,– Notably, TGF-β can also enhance viral infection through certain pathogen-specific mechanisms as in the cases of human immunodeficiency virus type 1 (HIV-1) infection,– human T-cell leukemia virus type I (HTLV-I) infection, hepatitis C virus (HCV) infection, Zika virus (ZIKV) infection, as well as rubella virus (RuV) infection. Furthermore, TGF-β can promote the survival and growth of parasites in hosts through downregulation of NO, IFN-γ, TNF-α, IL-6, IL-17, and Th17 cells as well as upregulation of IL-4, IL-10, and Treg cells, contributing to the infection of Fasciola hepatica, Echinococcus multilocularis, Toxoplasma gondii, Leishmania, and Plasmodium.,

Tumors

67It is generally accepted that TGF-β acts as a tumor suppressor during the early stages of tumorigenesis but turns into a tumor promotor at later stages of tumor development.

Tumorigenesis

68Evidence from animal models firmly establishes the suppressor role of TGF-β signaling in early tumorigenesis. TGF-β and its receptors can be strongly induced in the murine epidermis upon exposure to carcinogens that tend to disrupt tissue homeostasis and cause oncogenic transformation., Increased TGF-β expression in murine epidermis can potently attenuate cell proliferation and confer resistance to hyperproliferation induced by carcinogens.,, Similarly, in murine mammary epithelia, the overexpression of TGF-β or TβR can result in remarkable protection from carcinogen-induced tumorigenesis with reduced premalignant lesions, prolonged tumor latency, and decreased cancer incidence.,,– Such tumor-inhibitory effects by TGF-β signaling are attributed to the early apoptosis of differentiating cells and, more importantly, the premature senescence of stem cells which reduces the reproductive capacity of the mammary epithelia and thus decreases the frequency with which transforming mutations may occur and be fixed in the cell population.,

69In contrast, loss of TGF-β signaling can be an early event that contributes to tumorigenesis. In clinical patients, heterogeneous patterns of TβRII expression in normal breast lobular units as well as loss of TβRII expression in breast epithelial hyperplastic lesions are both associated with increased risks of invasive breast cancer. More convincing evidence is provided by germline mutations of TGF-β signaling components which show strong correlations with increased risks of tumorigenesis. Loss-of-function TβRI mutations can result in an autosomal dominant skin cancer condition known as multiple self-healing squamous epithelioma (MSSE) or Ferguson-Smith disease (FSD) which is characterized by multiple squamous-carcinoma-like skin tumors that invade locally and then regress spontaneously after several months., Inactivating TβRII mutations are considered causative of some cases of hereditary nonpolyposis colorectal cancer (HNPCC) or Lynch syndrome, an autosomal dominant cancer predisposition syndrome, by impairing cell growth inhibition in response to TGF-β. Moreover, germline mutations of SMAD4 are responsible for juvenile polyposis, an autosomal dominant syndrome predisposing to gastrointestinal hamartomatous polyps and cancers., Mechanically, impaired TGF-β signaling can cause serious disturbance to tissue homeostasis, thus largely facilitating the development of pre-neoplastic lesions, as well as subsequent tumors, as shown in different murine tissues with deficiencies in the activity of TGF-β,, TβR,,– or SMAD.,– Among them, TβR-deleted murine epithelia exhibit significant reductions in p15 and p21 and remarkable increases in MYC expression and RAS/ERK signaling, accompanied by elevated cell proliferation, reduced cell apoptosis, and enhanced cell malignant transformation to become tumorigenic.–

70Furthermore, TGF-β can provide additional protection against tumorigenesis by controlling pathogen infection, inhibiting excessive inflammation,– reducing genomic instability, inducing replicative senescence, and regulating epithelial-mesenchymal interaction.

Tumor growth

71TGF-β can inhibit tumor growth by triggering cytostasis and apoptosis through similar mechanisms as it does in cells from normal tissues. In tumor cells, TGF-β signaling induces cell cycle arrest by targeting effectors, such as p15,, p21,,, p27, MYC, ID, and CDC25A,, while it also induces apoptotic cell death through effectors including CTGF, programmed cell death 4 (PDCD4), Fas receptor, death-associated protein kinase (DAPK), DAXX, IκB-α,, sex-determining region Y (SRY)-box 4 (SOX4), ARTS, TIEGs, as well as several BCL-2 family members.– Consistently, primary tumors induced from murine tissues with intact TGF-β signaling pathways are initially responsive to TGF-β-mediated inhibitory effects.,,,,,

72On the contrary, deficient TGF-β signaling can potently promote the growth of tumors. The downregulation of tumor TGF-β signaling in many cases is attributed to reduced expression or inactivating mutations of TβR or SMAD, as shown in various tumor types such as leukemia, lymphoma,, esophageal cancer,– gastric cancer, colorectal cancer,,,– pancreatic cancer,,, biliary cancer, ampullary cancer, thyroid cancer, prostate cancer,, breast cancer, ovarian cancer, endometrial cancer, genital squamous cell carcinomas (SCC), head and neck SCC,– etc. These changes are able to confer resistance to the tumor-inhibitory effects of TGF-β. In mouse models, tumors developed from tissues with deletion or inactivation of TβR exhibit increased cell proliferation and decreased cell apoptosis, accompanied by reduction in p15, p21, and p27, the elevation of MYC, cyclin D1, and epidermal growth factor receptor (EGFR), as well as activation of STAT3 and PI3K/AKT pathways.– Interestingly, reconstituted expression of TβRII in tumor cells with corresponding deficiency not only restores the inhibitory responses to TGF-β but also significantly attenuates the tumorigenicity of these cells.

73Notably, TGF-β can fail to suppress the growth of tumors where there is likely no loss of functional TGF-β signaling components, and even formerly inhibited tumor cells can subsequently resume proliferating in vitro and develop larger tumor masses in vivo.,, On one hand, such resistance may result from the dysfunction of the downstream targets of TGF-β signaling such as CKIs. On the other hand, the tumor-suppressive signaling of TGF-β can be offset or interfered by enhanced I-SMAD activity or potent oncogenic factors such as E1A,, EVI1,, SKI,, SNO, MYC, ID2, mutant p53, as well as RAS/RAF/ERK signaling., Moreover, TGF-β-mediated tumor-promoting effects can also account for the enhanced tumor growth in vivo, as discussed in a later section.

Tumor invasion and metastasis

74Contrary to its role as a suppressor of tumor growth, TGF-β generally acts as a promoter of tumor invasion and metastasis especially in advanced tumors. Upregulation of TGF-β as well as its receptors is associated with disease progression and poor prognosis in some patients with tumors such as breast cancer,, pancreatic cancer,, and gastric cancer. Consistently, TGF-β overexpression or pre-treatment enables tumor cells to form increased metastases in vivo,, while loss of TGF-β responsiveness due to the introduction of dominant negative TβRII decreases the metastatic efficiency of high-grade tumor cells., Moreover, tumors derived from transgenic murine epithelia that overexpress TGF-β or TβR are significantly more malignant and more invasive.,,,, Notably, these TGF-β-overexpressing tumor cells are more likely to undergo the transition from epithelial cell phenotype into spindle cell phenotype which is the most malignant and invasive cell type., This indicates that TGF-β can facilitate the progression of epithelial-derived tumors through the induction of EMT which is inoperative in tumors with deficiencies in TβR or SMAD.,,,, Similar to the EMT of normal cells, TGF-β-induced EMT of tumor cells is characterized by changes in keratin, integrin, cadherin, catenin, claudin, vimentin, occludin, fibronectin, and MMP expression which can contribute to the invasive and metastatic capacity of tumors.,,,,,,,,,–

75However, loss of functional TGF-β signaling components can occur in tumor cells during disease progression., In fact, reduced TGF-β signaling can also contribute to tumor invasion and metastasis. For some patients, decreased expression of TβR is correlated with higher tumor grades, later clinical stages, and worse clinical prognosis.,, A large number of cell models and mouse models also demonstrate that tumors lacking TGF-β signaling tend to be more malignant and more aggressive.,–,,,,,– Relevant mechanisms in these cases involve the loss of E-cadherin, the reduction in PAI, the increase in RHO/RAC signaling, the activation of integrin/focal adhesion kinase (FAK)/SRC/MAPK pathway, and more importantly, the overexpression of various pro-invasive and pro-metastatic factors. In mouse models, deficient TGF-β signaling can stimulate tumor cells and stromal cells to produce high levels of TGF-β and other tumor-promoting factors such as CTGF, VEGF, IL-1β, C-X-C motif chemokine ligand (CXCL8), CXCL12, cyclooxygenase(COX)-2, MMPs, collagen, and tenascin C (TNC) which can strongly promote tumor angiogenesis, fibroblasts activation, immune infiltration, and ECM remodeling.–,,,

Tumor microenvironment (TME) remodeling

76TGF-β can stimulate tumor progression even when its signaling pathways are unavailable in the tumor cells, indicating its additional tumor-promoting effects exerted on tumor stroma.–, Fibroblasts, endothelial cells, and immune cells are the major stromal cell types in TME and can all be manipulated by TGF-β in favor of tumor progression.

77Actively produced TGF-β in the TME can stimulate the chemotactic migration of fibroblasts and convert them into MFs which are also known as cancer-associated fibroblasts (CAFs) in terms of tumors., Activated CAFs can in turn repay TME with more TGF-β as well as other tumor-promoting factors such as TGF-α, FGF, HGF, PDGF, and CTGF to exert a strong stimulation on tumor growth.,– Moreover, TGF-β regulates the production of various ECM components and remodelers by CAFs to facilitate the migration of tumor cells during invasion and metastasis., Interestingly, fibroblasts with the loss of TβRII can also contribute to tumor development through the production of TGF-α, HGF, and macrophage-stimulating protein (MSP).

78Endothelial cells can also be converted into CAFs through TGF-β-mediated EndMT. More importantly, TGF-β promotes the angiogenesis of endothelial cells by inducing VEGF production in tumor cells and fibroblasts.,,,, TGF-β also disrupts inter-endothelial junctions to increase the vascular permeability in TME through the process of EndMT and the induction of angiopoietin-like 4 (ANGPTL4). Therefore, TGF-β-mediated angiogenesis not only increases the blood supply to tumors to favor their growth but also provides tumors with more accessible entrances into the circulation to form metastasis.

79Furthermore, TGF-β can modulate immune cell activity to facilitate tumor survival and development. TGF-β inhibits the tumoricidal activity of macrophages and neutrophils and polarizes them into tumor-promoting M2 macrophages and N2 neutrophils, which are also known as tumor-associated macrophages (TAMs) and tumor-associated neutrophils (TANs) in terms of tumors.,,,,, It also promotes the functions of Tregs while suppressing the cytotoxicity of CTLs and NK cells to facilitate tumor evasion from immune surveillance.– Moreover, TGF-β can inhibit the expression of MHC antigens in tumor cells to further attenuate their recognition by adaptive anti-tumor immunity., However, TGF-β-mediated downregulation of MHC antigens and NKG2D ligands can increase tumor susceptibility to NK cytotoxicity to some extent.,

TGF-β-targeting therapies

80To rectify the dysfunction of TGF-β in different kinds of diseases, several targeted therapies have been developed to regulate TGF-β activity at the levels of biosynthesis, activation, and signaling. Many completed clinical trials have preliminarily confirmed the safety and efficacy of some therapeutic strategies, while there are still numerous clinical trials ongoing at present (Table 1).

Targeting TGF-β mRNAs

81Trabedersen (AP 12009 or OT-101) is an antisense oligonucleotide complementary to human TGF-β2 mRNA and can specifically inhibit TGF-β2 biosynthesis. It is hypothesized that trabedersen mainly acts by reversing TGF-β2-mediated immunosuppression to facilitate immune responses against tumors. A phase 2b clinical trial showed no advantage in early tumor control rate but in long-term survival rate for glioma patients treated with trabedersen in comparison with standard chemotherapy. Tumor responses which continued to increase long after discontinuation in the study suggested that the clinically relevant beneficial effects of trabedersen might increase over time. Moreover, compared with the standard chemotherapy group, drug-related or possibly drug-related adverse events in the trabedersen group were less common and mostly nervous system disorders. The study also indicated that the optimal dose of trabedersen is 10 µM, as both its efficacy and safety tended to be superior to the 80 µM dose, although the mechanism for this counterintuitive result has not been fully understood. TGF-β1 antisense oligonucleotides or small interfering RNAs (siRNAs) were also developed and evaluated in different pre-clinical models, suggested as potential therapeutic strategies for tuberculosis,, wound scarring,, and several renal diseases.–

82TGF-β antisense gene-modified tumor cell vaccines are designed to exhibit increased immunogenicity due to reduced TGF-β expression in the tumor cells that comprise the vaccines. Vaccine Lucanix (belagenpumatucel-L) made from allogeneic non-small cell lung cancer (NSCLC) cell lines was well tolerated and brought survival advantages to NSCLC patients who were randomized within 12 weeks of completion of platinum-based chemotherapy and in those who had received prior radiation, as shown in a phase 3 trial which, however, failed to demonstrate a significant increase in survival in the overall patient population. TGF-β antisense-modified autologous tumor cell vaccines have also been tested in advanced glioma and other solid tumors, respectively, in two phase 1 studies in which enhanced anti-tumor activity and improved survival were observed., Notably, in the study among glioma patients, the most common treatment-related adverse events were delayed-type hypersensitivity-like reactions observed at the sites of the second and subsequent vaccinations in all patients. Some of these patients also experienced transient, flu-like symptoms consisting of musculoskeletal aches and pains and fatigue during the course of treatment.

Targeting furin

83Convertase furin is a therapeutic target participating in the post-translational processing of TGF-β. Vigil (FANG or Gemogenovatucel-T) is an autologous tumor cell vaccine incorporating a plasmid encoding granulocyte-macrophage colony-stimulating factor (GMCSF) and a bifunctional short-hairpin RNA (shRNA) targeting the expression of furin. A phase 1 study confirmed its safety and efficacy in various advanced solid tumors, with significant survival differences noted between patients who received less than four vaccinations and those who received no less than four vaccinations. A later phase 2b trial also demonstrated significant clinical benefit in homologous recombination proficient ovarian cancer (NCT02346747). Both studies reported no treatment-related serious adverse events, while the most common grade one and two adverse events related to study medication were local reactions at the injection site.

Targeting latent TGF-β complex

84SRK-181 is an antibody that selectively binds to latent TGF-β1 to inhibit its activation. Co-administration of SRK-181 and anti-PD-1 antibody induced profound anti-tumor responses and survival benefit in mice, with increased infiltrating CD8+ T cells and decreased immunosuppressive myeloid cells observed in tumors refractory to anti-PD-1 treatment. The selective blockade of TGF-β1 by SRK-181 neither caused cardiac valvulopathy in rats as pan-TGFβ inhibitors might do nor did it induce cytokine release in human peripheral blood. Moreover, SRK-181 showed no effect on human platelet aggregation, activation, and binding., The favorable safety profile displayed in these preclinical assessments supports the ongoing phase 1 trial of SRK-181 in patients with advanced cancers (NCT04291079).

Targeting GARP

85GARP expressed by Tregs, platelets, and endothelium functions to tether latent TGF-β complex to the cell surface for activation. Anti-GARP monoclonal antibody PIIO-1 proved to be an effective and safe strategy to block TGF-β activation in preclinical models, for it specifically bound to ligand-free GARP on Tregs but lacked recognition of GARP-latent TGF-β complex on platelets, actually avoiding the risk of platelet-related toxicities such as thrombocytopenia. More importantly, PIIO-1 showed therapeutic efficacy against both GARP+ and GARP- cancers alone or in combination with anti-PD-1 antibody, by preventing T cell exhaustion and enhancing CD8+ T cell migration into the TME in a C-X-C motif chemokine receptor 3 (CXCR3)-dependent manner.

Targeting αV integrins

86Integrins are regarded as the most important activators of TGF-β. Abituzumab (EMD 525797 or DI17E6) is an antibody against pan-αV integrins. In a phase 1/2 trial on KRAS wild-type metastatic colorectal cancer (NCT01008475), the progression-free survival (PFS) and response rates were similar among all groups in the intent-to-treat population comprising all patients randomized, although a trend toward improved overall survival (OS) was observed in the groups that received abituzumab treatment. However, exploratory analysis suggested that in patients with high αVβ6 expression, PFS and response rates might be increased with abituzumab therapy. This pan-αV integrin inhibitor was also found to inhibit prostate cancer-associated bone lesion formation in a randomized phase 2 trial (NCT01360840), although PFS was not significantly extended. Recently, abituzumab has been investigated in SSc-associated interstitial lung disease in a phase 2 trial (NCT02745145). However, the study was terminated prematurely due to slow enrollment and no meaningful conclusions could be drawn due to a small sample size. The most commonly reported treatment-related adverse events of abituzumab included fatigue, headache, gastrointestinal disorders, as well as abnormal biochemistry and hematology values.,,

87Cilengitide (EMD 121974, NSC 707544) is a selective αvβ3 and αvβ5 integrin inhibitor which has been evaluated for therapeutic efficacy in NSCLC (NCT00842712),, head and neck SCC (NCT00705016), glioblastoma (NCT00689221, NCT00813943, and NCT01124240),– melanoma, pancreatic cancer, and prostate cancer, in a series of phase 2 studies and one phase 3 study. Although cilengitide failed to demonstrate significant clinical benefits in these studies on tumors, it might be a novel treatment for fibrotic diseases as relevant preclinical studies suggested., Notably, the adverse events possibly related to cilengitide treatment included fatigue, arthralgia, lymphopenia, and gastrointestinal disorders.,,,,,, Furthermore, an inhibitor of pan-integrins and TGF-β known as GLPG-0187 was proved to enhance T cell killing of colorectal cancer cells in vitro, possibly by suppressing TGF-β-mediated PD-L1 upregulation.,

Targeting TSP-1

88TSP-1 can directly activate all three TGF-β isoforms independent of other activators or cellular activity. The conserved LSKL sequence in LAP which is recognized by TSP-1 can be synthesized as peptides to block TSP-1-mediated TGF-β activation. Pre-clinical studies suggested that treatment of LSKL or relevant tripeptide SRI31277 could be novel therapeutic strategies for various cardiovascular diseases, pulmonary diseases, renal diseases,– nervous diseases,, fibrotic diseases,– wound healing,, and tumors.– Moreover, TSP-1 antisense oligonucleotides were successfully developed and applied to inhibit TGF-β activation in a rat model of mesangial proliferative glomerulonephritis, demonstrating a remarkable prevention against renal fibrosis.

Targeting TGF-β ligands

89A TGF-β2-enriched polymeric dietary supplement known as Modulen (CT3211) was effective in inducing earlier remission of inflammatory bowel diseases (IBDs) including both Crohn’s disease and UC with significant improvements in endoscopic and histologic appearances, mucosal cytokine parameters, C-reactive protein (CRP) values, erythrocyte sedimentation rates (ESRs), serum albumin levels, as well as weight and height scores in the patients.– Notably, an exclusive Modulen diet was more efficient than steroids to induce mucosal healing in children with Crohn’s disease, possibly due to its additional advantage in regulating intestinal microbiota (NCT00265772)., Moreover, a pre-operative polymeric diet enriched with TGF-β2 was able to decrease post-operative complications after surgery for complicated ileocolonic Crohn’s disease. The side effects of Modulen were mild, including abdominal pain, flatulence, nausea, and vomiting.,, In mouse models, oral TGF-β supplementation also showed beneficial effects on food allergy prevention.– In fact, it is believed that the presence of TGF-β in breast milk can protect the progeny from several allergic diseases such as asthma, eczema, and food allergy.

90Recombinant human TGF-β3 known as avotermin (Juvista) is a potential therapy for the improvement of cutaneous scarring. In a series of phase 1/2 studies (NCT00847925, NCT00847795, NCT00629811, NCT00432211, NCT00594581, and NCT00430326), visual assessment of scar formation revealed that, in contrast to placebo, intradermal avotermin could significantly improve total scar scores which were derived from a visual analog scale to assess how closely scars resembled normal skin. The results were further confirmed by histological assessments that scars treated with avotermin showed better organized ECM of the papillary and reticular dermis. The incidence of adverse events at wound sites, including infection, exudate, erythema, pain, burning, itching, and thickening was low and similar for avotermin and controls.– Although the other two TGF-β isoforms, TGF-β1 and TGF-β2, showed no therapeutic activity of scarring, they were found to improve and accelerate the healing of cutaneous wounds in animal models as well as clinical patients.,,,,,, Moreover, TGF-β also showed therapeutic potential for tissue regeneration,,, inflammatory diseases,,, and influenza as shown in relevant preclinical models.

91TGF-β neutralizing antibodies and ligand traps can block the binding of TGF-β to its receptors. Fresolimumab (GC1008), a monoclonal antibody that neutralizes all three TGF-β isoforms demonstrated acceptable safety and preliminary evidence of anti-tumor activity in a phase 1 study on advanced malignant melanoma and renal cell carcinoma (NCT00356460). In a phase 2 trial (NCT01401062), a higher dose of fresolimumab is associated with longer median OS as well as improved peripheral blood mononuclear cell counts and boosted central memory CD8+ T cell levels in metastatic breast cancer patients receiving radiotherapy. Fresolimumab also showed therapeutic effects on SSc with decreased biomarkers of skin fibrosis and improved clinical symptoms in the patients in a phase 1 study (NCT01284322). Moreover, a phase 1 study evaluated the safety of fresolimumab in patients with treatment-resistant primary focal segmental glomerulosclerosis and the good tolerability supported additional evaluation in larger randomized dose-ranging clinical trials. Notably, the major drug-related adverse events of fresolimumab were skin disorders, bleeding episodes, and anemia. Skin toxicity was particularly significant and tumor patients assigned to high doses of treatment even developed skin tumors, including keratoacanthoma, basal cell carcinoma, and SCC.– Another anti-TGF-β monoclonal antibody known as NIS793 was well tolerated alone or in combination with anti-PD-1 antibody in patients with advanced solid tumors in a phase 1 study (NCT02947165). Treatment-related adverse events of all patients in the study were mostly skin toxicity and gastrointestinal events, and no dose-limiting toxicities were observed during dose escalation. Notably, biomarker analyses in the study showed evidence of systemic target engagement, local signaling inhibition, and tumor immune activation. Apart from tumors, a recombinant human anti-TGF-β1 antibody known as CAT-192 was evaluated in the treatment of early-stage diffuse cutaneous SSc but showed no evidence of efficacy in the pilot phase 1/2 study. The most commonly reported adverse events in the study affected the gastrointestinal, musculoskeletal, respiratory, and skin systems, but none of them were considered to be related to the treatment. Moreover, a phase 2 study assessing the safety and efficacy of TGF-β1 monoclonal antibody in patients with diabetic nephropathy was terminated early for futility (NCT01113801). The frequencies of the various categories of adverse effects in this study were generally similar between the treatment and placebo groups. Furthermore, monotherapy of a selective TGF-β1/3 trap known as AVID200 in a population of patients with an advanced stage of myelofibrosis in a phase 1b trial resulted in limited toxicity as well as improvements in spleen size, symptom benefit, and platelet counts (NCT03895112). Remarkably, platelet count increase was a therapeutic effect not observed with other myelofibrosis therapies, suggesting a potential advantage of AVID200 treatment. Adverse events that occurred during the study regardless of attribution mainly included pruritus, fatigue, abdominal pain, anemia, and thrombocytopenia. Additionally, other potential applications of neutralizing TGF-β antibodies suggested by pre-clinical studies include wound healing,,, prostatic hyperplasia, pulmonary diseases,, cardiovascular diseases,, musculoskeletal diseases,– inflammatory diseases,, and Chagas disease (Trypanosoma cruzi infection).

92Bifunctional antibody-ligand traps containing the extracellular domain of TβRII can target both TGF-β and immune checkpoints. In preclinical studies, both the anti-CTL associated protein (CTLA)-4-TβRII chimera and the anti-PD-L1-TβRII chimera exhibited superior anti-tumor efficacy compared with their parent immune checkpoint inhibitors. Bintrafusp alfa (M7824), a bifunctional fusion protein targeting both TGF-β and PD-L1 was assessed in several phase 1 trials (NCT02699515, NCT02517398, NCT02699515, and NCT04247282). The results showed that bintrafusp alfa had encouraging efficacy in NSCLC, gastric cancer, biliary tract cancer, as well as human papillomavirus (HPV)-unrelated head and neck cancer in which enhanced tumor antigen-specific immunity has been observed. Similar to fresolimumab, the treatment-related adverse events of bintrafusp alfa included fatigue, colitis, bleeding, anemia, hypokalemia, lipase increase, hepatic function abnormalities, as well as several skin disorders from rash, hyperkeratosis, to keratoacanthoma and SCC.– BR102 is another bifunctional fusion protein simultaneously targeting PD-L1 and TGF-β. The efficacy and safety of BR102 demonstrated in preclinical characterization supported its further clinical development for anti-cancer therapy. Notably, the bifunctional antibody-ligand traps have inspired the development of chimeric antigen receptor (CAR)-T cells secreting bispecific trap protein, which co-targets PD-1 and TGF-β to enhance anti-tumor efficacy as shown in mouse models.

93Furthermore, LAP, TβRIII (β-glycan), and decorin can bind to TGF-β as natural inhibitors. They have shown treatment effects in preclinical models of wound healing,– cardiovascular diseases,– nervous diseases,– renal diseases,– fibrotic diseases,– tuberculosis, and tumors– and thus warrant further development.

Targeting TβRs

94TGF-β-insensitive CAR-T cells armored with dominant-negative TβRII showed preliminary evidence for early anti-tumor function in prostate cancer, including a biomarker decline among approximately 30% of the patients in a phase 1 trial (NCT03089203). This strategy which is considered generally feasible, despite no partial response being observed in the study, and safe, with study-related serious adverse events mostly being cytokine release syndrome, warrants further validation and investigation. Dominant-negative TβRII can also enhance the anti-tumor efficacy of DC vaccines, manifested by powerful tumor-specific CTL responses, inhibited tumor development, and prolonged survival times in mouse models., Moreover, dominant-negative TβRII showed great potential for reducing hypertrophic scars as in rabbit ear models.

95Many small-molecule inhibitors have been developed to suppress the kinase activity of TβRI. In a series of phase 2 studies, a TβRI kinase inhibitor known as galunisertib (LY2157299) showed preliminary efficacy in patients with myelodysplastic syndromes (MDS) (NCT02008318), NSCLC (NCT02423343), hepatocellular carcinoma (NCT01246986),, rectal cancer (NCT02688712), and pancreatic cancer, but failed to demonstrate clinical benefit in patients with glioma (NCT01582269 and NCT01220271)., The most common adverse events related to galunisertib treatment included fatigue, pyrexia, anemia, nausea, vomiting, diarrhea, and abdominal pain.,, Despite comprehensive cardiovascular monitoring for galunisertib did not detect medically relevant cardiac toxicity in cancer patients, galunisertib-related uncontrolled cytokine release was reported in patients with advanced solid tumors in a phase 1 trial (NCT01646203). Other TβRI kinase inhibitors such as SM16, SD-208, NP-40208, SB-431542, LY3200882, LY364947, and vactosertib (EW-7197) also showed therapeutic potential in pre-clinical studies on tumors– as well as many other diseases such as cardiovascular diseases,,– renal diseases, ophthalmic diseases, skeletal diseases, fibrotic diseases,– inflammatory diseases,– Chagas disease,, coronavirus disease 2019 (COVID-19), and wound healing.–

Targeting SMADs

96An oral SMAD7 antisense oligonucleotide known as mongersen (GED-0301) showed promising results in patients with active Crohn’s disease in phase 1 and 2 phase trials, but further phase 3 study failed due to lack of clinical benefit (EudraCT 2009-012465-66, EudraCT 2011-002640-27, and NCT02596893).– Meanwhile, SMAD3 antisense oligonucleotide treatment was found to improve flexor tendon repair in mice and might have possible therapeutic applications in clinical practice.

97Moreover, a small-molecule SMAD3 inhibitor known as specific inhibitor of SMAD3 (SIS3) has shown pre-clinical therapeutic efficacy in wound healing, cardiovascular diseases,,, nervous diseases, renal diseases,, skeletal diseases, fibrotic diseases,, inflammatory diseases,, type 2 diabetes,, and tumors,, suggesting a novel approach that could be further tested to treat clinical patients.

98Furthermore, several SMAD-binding peptide aptamers have been developed to selectively inhibit the binding between SMADs and their interacting factors. An aptamer containing the SMAD-binding domain of transcription factor lymphoid enhancer-binding factor 1 (LEF1) can suppress tumor cell proliferation by inhibiting the interaction between SMAD4 and LEF/T cell-specific factor (TCF) to suppress MYC expression. Other aptamers that bind specifically to R-SMADs through the SMAD-binding domain from SARA can impair the formation of functional SMAD oligomers to inhibit TGF-β-induced EMT., Moreover, aptamers that disrupt the interaction between SMAD and transcription coactivator yes-associated protein (YAP) have been designed for bone tumor therapy.

Conclusions and future perspectives

99TGF-β signaling is so extensively and indispensably involved in a large number of biological processes that it has attracted great interest and attention over the past decades during which relevant knowledge has exploded in the fields of health, disease, and therapeutics. However, there are still some specific issues that have not been fully elucidated, while some previous knowledge is facing updates and challenges.

100Studies on embryonic development and wound healing have revealed the isoform-specific roles of TGF-β which remain poorly aware in other fields of research, as studies on immune homeostasis, fibrotic diseases, and tumor development so far have focused on the most abundant TGF-β1 isoform in particular. Since all TGF-β isoforms are believed to signal through the same receptors and downstream pathways, the causes of the differences in biological effects between isotypes have not been fully understood. Moreover, since a natural TGF-β heterodimer containing one TGF-β1 monomer and one TGF-β2 monomer has long been discovered,, it would be very interesting to identify and characterize novel TGF-β heterodimers in the future. Furthermore, with the discovery and study of TGF-β superfamily which also includes polypeptides structurally similar to TGF-β such as nodal, myostatin, inhibins, activins, Müllerian-inhibiting substance (MIS), bone morphogenetic proteins (BMPs), and growth and differentiation factors (GDFs), researchers have realized that TGF-β can also signal through pathways ‘specific’ to other TGF-β superfamily members, for example, via receptors ALK1/2/3 and transcription factors SMAD1/5/8.– The significance of the signaling crosstalk within the TGF-β superfamily also warrants future exploration. Notably, Reblozyl (luspatercept or ACE-536), a ligand trap that contains the extracellular domain of human activin receptor type IIB (ActRIIB) to inhibit GDF11-mediated SMAD2/3 signaling has been approved by the US Federal Drug Agency (FDA) for the treatment of anemia in adult patients with β-thalassemia or with MDS.

101As for TGF-β-targeting therapy, the efficacy and safety of treatment are always issues of concern. The current lack of systematic studies on the dural roles of TGF-β in wound healing, infectious diseases, and tumor development may hinder the development of related therapeutics. Given the extensive impacts of TGF-β on a lot of biological processes, the development of TGF-β isoform-specific therapies and SMAD-binding peptide aptamers is expected to cause less adverse effects through more precise targeting. Moreover, the identification of the applicable population for each therapeutic approach is also important for better efficacy and less toxicity. Serum and tissue levels of TGF-β have shown potential as predictors or indicators of the development,– complication,– response,– recurrence,– and outcomes– of various kinds of diseases, meanwhile, bioinformatic tools of TGF-β signaling-related gene expression signatures have also been developed for patient stratification., But so far, TGF-β or related factors as clinical biomarkers still need further development and assessment.

102To summarize, this review focuses on the multiple roles of TGF-β in health and disease while emphasizing the mechanisms of TGF-β production, activation, signaling, as well as corresponding therapeutic strategies. These understandings might be instructive for the basic and applied research of relevant topics in the future.

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31.
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32.
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33.
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35.
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36.
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37.
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38.
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39.
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40.
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44.
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46.
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48.
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49.
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51.
Intestinal Dendritic Cells Specialize to Activate Transforming Growth Factor-β and Induce Foxp3+ Regulatory T Cells via Integrin αvβ8 · 2011
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52.
Regulatory T cells promote cancer immune-escape through integrin αvβ8-mediated TGF-β activation · 2021
No notice
53.
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54.
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55.
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56.
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57.
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58.
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59.
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60.
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66.
Jobling MF, et al. Isoform-specific activation of latent transforming growth factor beta (LTGF-beta) by reactive oxygen species. Radiat. Res. 2006;166:839-848.
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67.
Hayashi H, Sakai K, Baba H, Sakai T. Thrombospondin-1 is a novel negative regulator of liver regeneration after partial hepatectomy through transforming growth factor-beta1 activation in mice. Hepatology. 2012;55:1562-1573.
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68.
Wang H, Kochevar IE. Involvement of UVB-induced reactive oxygen species in TGF-beta biosynthesis and activation in keratinocytes. Free Radic. Biol. Med. 2005;38:890-897.
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69.
Pociask DA, Sime PJ, Brody AR. Asbestos-derived reactive oxygen species activate TGF-beta1. Lab Invest. 2004;84:1013-1023.
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Sullivan DE, Ferris M, Pociask D, Brody AR. The latent form of TGFbeta(1) is induced by TNFalpha through an ERK specific pathway and is activated by asbestos-derived reactive oxygen species in vitro and in vivo. J. Immunotoxicol. 2008;5:145-149.
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71.
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72.
Effect of high glucose supplementation on pulmonary fibrosis involving reactive oxygen species and TGF-β · 2022
Not checked
73.
Zhang D, et al. High Glucose Intake Exacerbates Autoimmunity through Reactive-Oxygen-Species-Mediated TGF-beta Cytokine Activation. Immunity. 2019;51:671-681.e675.
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74.
Chen W, Frank ME, Jin W, Wahl SM. TGF-beta released by apoptotic T cells contributes to an immunosuppressive milieu. Immunity. 2001;14:715-725.
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75.
Endogenous TGF-β activation by reactive oxygen species is key to Foxp3 induction in TCR-stimulated and HIV-1-infected human CD4<sup>+</sup>CD25<sup>- </sup>T cells · 2007
Not checked
76.
Sweetwyne MT, Murphy-Ullrich JE. Thrombospondin1 in tissue repair and fibrosis: TGF-beta-dependent and independent mechanisms. Matrix Biol. 2012;31:178-186.
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77.
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78.
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80.
Naito T, et al. Angiotensin II induces thrombospondin-1 production in human mesangial cells via p38 MAPK and JNK: a mechanism for activation of latent TGF-beta1. Am. J. Physiol. Ren. Physiol. 2004;286:F278-F287.
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81.
Kumar R, et al. Interstitial macrophage-derived thrombospondin-1 contributes to hypoxia-induced pulmonary hypertension. Cardiovasc Res. 2020;116:2021-2030.
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82.
Matsuba M, Hutcheon AE, Zieske JD. Localization of thrombospondin-1 and myofibroblasts during corneal wound repair. Exp. Eye Res. 2011;93:534-540.
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83.
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Thrombospondin-1 contributes to mortality in murine sepsis through effects on innate immunity. · 2011
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85.
Presser LD, Haskett A, Waris G. Hepatitis C virus-induced furin and thrombospondin-1 activate TGF-beta1: role of TGF-beta1 in HCV replication. Virology. 2011;412:284-296.
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86.
TGF-β activation by bone marrow-derived thrombospondin-1 causes Schistosoma- and hypoxia-induced pulmonary hypertension · 2017
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87.
Zhou Y, Poczatek MH, Berecek KH, Murphy-Ullrich JE. Thrombospondin 1 mediates angiotensin II induction of TGF-beta activation by cardiac and renal cells under both high and low glucose conditions. Biochem Biophys. Res Commun. 2006;339:633-641.
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88.
Atanasova VS, et al. Thrombospondin-1 Is a Major Activator of TGF-beta Signaling in Recessive Dystrophic Epidermolysis Bullosa Fibroblasts. J. Invest Dermatol. 2019;139:1497-1505.e1495.
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89.
Presser LD, Haskett A, Waris G. Hepatitis C virus-induced furin and thrombospondin-1 activate TGF-β1: role of TGF-β1 in HCV replication. Virology. 2011;412:284-296.
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90.
Matsumura K, et al. Thrombospondin-1 overexpression stimulates loss of Smad4 and accelerates malignant behavior via TGF-beta signal activation in pancreatic ductal adenocarcinoma. Transl. Oncol. 2022;26:101533.
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91.
Jenkins G. The role of proteases in transforming growth factor-beta activation. Int J. Biochem. Cell Biol. 2008;40:1068-1078.
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93.
Bai P, et al. Macrophage-Derived Legumain Promotes Pulmonary Hypertension by Activating the MMP (Matrix Metalloproteinase)-2/TGF (Transforming Growth Factor)-β1 Signaling. Arterioscler Thromb. Vasc. Biol. 2019;39:e130-e145.
Not in our library10.1161/atvbaha.118.312254
94.
Feng W, et al. Matrix metalloproteinase-9 regulates afferent arteriolar remodeling and function in hypertension-induced kidney disease. Kidney Int. 2023;104:740-753.
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95.
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96.
Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000;14:163-176.
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97.
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98.
Nunes I, Shapiro RL, Rifkin DB. Characterization of latent TGF-beta activation by murine peritoneal macrophages. J. Immunol. 1995;155:1450-1459.
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101.
Sankar S, Mahooti-Brooks N, Centrella M, McCarthy TL, Madri JA. Expression of transforming growth factor type III receptor in vascular endothelial cells increases their responsiveness to transforming growth factor beta 2. J. Biol. Chem. 1995;270:13567-13572.
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103.
Wang XF, et al. Expression cloning and characterization of the TGF-beta type III receptor. Cell. 1991;67:797-805.
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104.
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Lopez-Casillas F, Wrana JL, Massague J. Betaglycan presents ligand to the TGF beta signaling receptor. Cell. 1993;73:1435-1444.
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Esparza-Lopez J, et al. Ligand binding and functional properties of betaglycan, a co-receptor of the transforming growth factor-beta superfamily. Specialized binding regions for transforming growth factor-beta and inhibin A. J. Biol. Chem. 2001;276:14588-14596.
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107.
Madamanchi A, Ingle M, Hinck AP, Umulis DM. Computational modeling of TGF-β2:TβRI:TβRII receptor complex assembly as mediated by the TGF-β coreceptor betaglycan. Biophys. J. 2023;122:1342-1354.
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108.
Zhang W, et al. Single-molecule imaging reveals transforming growth factor-beta-induced type II receptor dimerization. Proc. Natl Acad. Sci. USA. 2009;106:15679-15683.
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109.
Gilboa L, Wells RG, Lodish HF, Henis YI. Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane. J. Cell Biol. 1998;140:767-777.
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110.
Chen RH, Derynck R. Homomeric interactions between type II transforming growth factor-beta receptors. J. Biol. Chem. 1994;269:22868-22874.
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Groppe J, et al. Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding. Mol. Cell. 2008;29:157-168.
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112.
Wrana JL, et al. TGF beta signals through a heteromeric protein kinase receptor complex. Cell. 1992;71:1003-1014.
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113.
Huse M, et al. The TGF beta receptor activation process: an inhibitor- to substrate-binding switch. Mol. Cell. 2001;8:671-682.
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114.
Tsukazaki T, Chiang TA, Davison AF, Attisano L, Wrana JL. SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor. Cell. 1998;95:779-791.
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115.
Wu JW, et al. Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. Mol. Cell. 2001;8:1277-1289.
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116.
Kawabata M, Inoue H, Hanyu A, Imamura T, Miyazono K. Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors. Embo j. 1998;17:4056-4065.
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117.
Chacko BM, et al. The L3 loop and C-terminal phosphorylation jointly define Smad protein trimerization. Nat. Struct. Biol. 2001;8:248-253.
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Lucarelli P, et al. Resolving the Combinatorial Complexity of Smad Protein Complex Formation and Its Link to Gene Expression. Cell Syst. 2018;6:75-89.e11.
Not in our library10.1016/j.cels.2017.11.010
119.
Inman GJ, Hill CS. Stoichiometry of active smad-transcription factor complexes on DNA. J. Biol. Chem. 2002;277:51008-51016.
Not in our library10.1074/jbc.m208532200
120.
Shi Y, et al. Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling. Cell. 1998;94:585-594.
Not in our library10.1016/s0092-8674(00)81600-1
121.
Structural basis for genome wide recognition of 5-bp GC motifs by SMAD transcription factors · 2017
Not checked
122.
Zawel L, et al. Human Smad3 and Smad4 are sequence-specific transcription activators. Mol. Cell. 1998;1:611-617.
Not in our library10.1016/s1097-2765(00)80061-1
123.
Liu Z, et al. Global identification of SMAD2 target genes reveals a role for multiple co-regulatory factors in zebrafish early gastrulas. J. Biol. Chem. 2011;286:28520-28532.
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124.
Koinuma D, et al. Promoter-wide analysis of Smad4 binding sites in human epithelial cells. Cancer Sci. 2009;100:2133-2142.
Not in our library10.1111/j.1349-7006.2009.01299.x
125.
Mullen AC, et al. Master transcription factors determine cell-type-specific responses to TGF-β signaling. Cell. 2011;147:565-576.
Not in our library10.1016/j.cell.2011.08.050
126.
Afrakhte M, et al. Induction of inhibitory Smad6 and Smad7 mRNA by TGF-beta family members. Biochem Biophys. Res Commun. 1998;249:505-511.
Not in our library10.1006/bbrc.1998.9170
127.
Transforming growth factor β-inducible independent binding of SMAD to the Smad7 promoter · 2000
Not checked
128.
Imamura T, et al. Smad6 inhibits signalling by the TGF-beta superfamily. Nature. 1997;389:622-626.
Not in our library10.1038/39355
129.
Kamiya Y, Miyazono K, Miyazawa K. Smad7 inhibits transforming growth factor-beta family type i receptors through two distinct modes of interaction. J. Biol. Chem. 2010;285:30804-30813.
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130.
Hanyu A, et al. The N domain of Smad7 is essential for specific inhibition of transforming growth factor-beta signaling. J. Cell Biol. 2001;155:1017-1027.
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131.
Suzuki C, et al. Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane. J. Biol. Chem. 2002;277:39919-39925.
Not in our library10.1074/jbc.m201901200
132.
Kavsak P, et al. Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. Mol. Cell. 2000;6:1365-1375.
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133.
Yan X, et al. Smad7 Protein Interacts with Receptor-regulated Smads (R-Smads) to Inhibit Transforming Growth Factor-β (TGF-β)/Smad Signaling. J. Biol. Chem. 2016;291:382-392.
Not in our library10.1074/jbc.m115.694281
134.
Kuratomi G, et al. NEDD4-2 (neural precursor cell expressed, developmentally down-regulated 4-2) negatively regulates TGF-beta (transforming growth factor-beta) signalling by inducing ubiquitin-mediated degradation of Smad2 and TGF-beta type I receptor. Biochem J. 2005;386:461-470.
Not in our library10.1042/bj20040738
135.
Morén A, Imamura T, Miyazono K, Heldin CH, Moustakas A. Degradation of the tumor suppressor Smad4 by WW and HECT domain ubiquitin ligases. J. Biol. Chem. 2005;280:22115-22123.
Not in our library10.1074/jbc.m414027200
136.
Shi W, et al. GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I receptor. J. Cell Biol. 2004;164:291-300.
Not in our library10.1083/jcb.200307151
137.
Zhang S, et al. Smad7 antagonizes transforming growth factor beta signaling in the nucleus by interfering with functional Smad-DNA complex formation. Mol. Cell Biol. 2007;27:4488-4499.
Not in our library10.1128/mcb.01636-06
138.
Ross S, et al. Smads orchestrate specific histone modifications and chromatin remodeling to activate transcription. Embo j. 2006;25:4490-4502.
Not in our library10.1038/sj.emboj.7601332
139.
Feng XH, Zhang Y, Wu RY, Derynck R. The tumor suppressor Smad4/DPC4 and transcriptional adaptor CBP/p300 are coactivators for smad3 in TGF-beta-induced transcriptional activation. Genes Dev. 1998;12:2153-2163.
Not in our library10.1101/gad.12.14.2153
140.
Itoh S, Ericsson J, Nishikawa J, Heldin CH, ten Dijke P. The transcriptional co-activator P/CAF potentiates TGF-beta/Smad signaling. Nucleic Acids Res. 2000;28:4291-4298.
Not in our library10.1093/nar/28.21.4291
141.
Kahata K, et al. Regulation of transforming growth factor-beta and bone morphogenetic protein signalling by transcriptional coactivator GCN5. Genes Cells. 2004;9:143-151.
Not in our library10.1111/j.1365-2443.2004.00706.x
142.
Yahata T, et al. The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors. J. Biol. Chem. 2000;275:8825-8834.
Not in our library10.1074/jbc.275.12.8825
143.
Postigo AA. Opposing functions of ZEB proteins in the regulation of the TGFbeta/BMP signaling pathway. Embo j. 2003;22:2443-2452.
Not in our library10.1093/emboj/cdg225
144.
Postigo AA, Depp JL, Taylor JJ, Kroll KL. Regulation of Smad signaling through a differential recruitment of coactivators and corepressors by ZEB proteins. Embo j. 2003;22:2453-2462.
Not in our library10.1093/emboj/cdg226
145.
Shuttleworth VG, et al. The methyltransferase SET9 regulates TGFB1 activation of renal fibroblasts via interaction with SMAD3. J. Cell Sci. 2018;131:jcs207761.
Not in our library10.1242/jcs.207761
146.
Kang JS, Alliston T, Delston R, Derynck R. Repression of Runx2 function by TGF-beta through recruitment of class II histone deacetylases by Smad3. Embo j. 2005;24:2543-2555.
Not in our library10.1038/sj.emboj.7600729
147.
Wotton D, Lo RS, Lee S, Massagué J. A Smad transcriptional corepressor. Cell. 1999;97:29-39.
Not in our library10.1016/s0092-8674(00)80712-6
148.
Alliston T, et al. Repression of bone morphogenetic protein and activin-inducible transcription by Evi-1. J. Biol. Chem. 2005;280:24227-24237.
Not in our library10.1074/jbc.m414305200
149.
Izutsu K, et al. The corepressor CtBP interacts with Evi-1 to repress transforming growth factor beta signaling. Blood. 2001;97:2815-2822.
Not in our library10.1182/blood.v97.9.2815
150.
Luo K, et al. The Ski oncoprotein interacts with the Smad proteins to repress TGFbeta signaling. Genes Dev. 1999;13:2196-2206.
Not in our library10.1101/gad.13.17.2196
151.
Akiyoshi S, et al. c-Ski acts as a transcriptional co-repressor in transforming growth factor-beta signaling through interaction with smads. J. Biol. Chem. 1999;274:35269-35277.
Not in our library10.1074/jbc.274.49.35269
152.
Sun Y, et al. Interaction of the Ski oncoprotein with Smad3 regulates TGF-beta signaling. Mol. Cell. 1999;4:499-509.
Not in our library10.1016/s1097-2765(00)80201-4
153.
Stroschein SL, Wang W, Zhou S, Zhou Q, Luo K. Negative feedback regulation of TGF-beta signaling by the SnoN oncoprotein. Science. 1999;286:771-774.
Not in our library10.1126/science.286.5440.771
154.
Feng XH, Liang YY, Liang M, Zhai W, Lin X. Direct Interaction of c-Myc with Smad2 and Smad3 to Inhibit TGF-β-Mediated Induction of the CDK Inhibitor p15(Ink4B). Mol. Cell. 2016;63:1089.
Not in our library10.1016/j.molcel.2016.08.027
155.
Kim RH, et al. A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction. Genes Dev. 2000;14:1605-1616.
Not in our library10.1101/gad.14.13.1605
156.
Verschueren K, et al. SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad proteins and binds to 5’-CACCT sequences in candidate target genes. J. Biol. Chem. 1999;274:20489-20498.
Not in our library10.1074/jbc.274.29.20489
157.
Wakabayashi Y, et al. Histone 3 lysine 9 (H3K9) methyltransferase recruitment to the interleukin-2 (IL-2) promoter is a mechanism of suppression of IL-2 transcription by the transforming growth factor-β-Smad pathway. J. Biol. Chem. 2011;286:35456-35465.
Not in our library10.1074/jbc.m111.236794
158.
Du D, et al. Smad3-mediated recruitment of the methyltransferase SETDB1/ESET controls Snail1 expression and epithelial-mesenchymal transition. EMBO Rep. 2018;19:135-155.
Not in our library10.15252/embr.201744250
159.
Brown JD, DiChiara MR, Anderson KR, Gimbrone MA, Topper JN. MEKK-1, a component of the stress (stress-activated protein kinase/c-Jun N-terminal kinase) pathway, can selectively activate Smad2-mediated transcriptional activation in endothelial cells. J. Biol. Chem. 1999;274:8797-8805.
Not in our library10.1074/jbc.274.13.8797
160.
Kamaraju AK, Roberts AB. Role of Rho/ROCK and p38 MAP kinase pathways in transforming growth factor-beta-mediated Smad-dependent growth inhibition of human breast carcinoma cells in vivo. J. Biol. Chem. 2005;280:1024-1036.
Not in our library10.1074/jbc.m403960200
161.
Mori S, et al. TGF-beta and HGF transmit the signals through JNK-dependent Smad2/3 phosphorylation at the linker regions. Oncogene. 2004;23:7416-7429.
Not in our library10.1038/sj.onc.1207981
162.
Lehmann K, et al. Raf induces TGFbeta production while blocking its apoptotic but not invasive responses: a mechanism leading to increased malignancy in epithelial cells. Genes Dev. 2000;14:2610-2622.
Not in our library10.1101/gad.181700
163.
Funaba M, Zimmerman CM, Mathews LS. Modulation of Smad2-mediated signaling by extracellular signal-regulated kinase. J. Biol. Chem. 2002;277:41361-41368.
Not in our library10.1074/jbc.m204597200
164.
Roelen BA, et al. Phosphorylation of threonine 276 in Smad4 is involved in transforming growth factor-beta-induced nuclear accumulation. Am. J. Physiol. Cell Physiol. 2003;285:C823-C830.
Not in our library10.1152/ajpcell.00053.2003
165.
Guo X, et al. Axin and GSK3- control Smad3 protein stability and modulate TGF- signaling. Genes Dev. 2008;22:106-120.
Not in our library10.1101/gad.1590908
166.
Millet C, et al. A negative feedback control of transforming growth factor-beta signaling by glycogen synthase kinase 3-mediated Smad3 linker phosphorylation at Ser-204. J. Biol. Chem. 2009;284:19808-19816.
Not in our library10.1074/jbc.m109.016667
167.
Wang G, Matsuura I, He D, Liu F. Transforming growth factor-{beta}-inducible phosphorylation of Smad3. J. Biol. Chem. 2009;284:9663-9673.
Not in our library10.1074/jbc.m809281200
168.
Wicks SJ, Lui S, Abdel-Wahab N, Mason RM, Chantry A. Inactivation of smad-transforming growth factor beta signaling by Ca(2+)-calmodulin-dependent protein kinase II. Mol. Cell Biol. 2000;20:8103-8111.
Not in our library10.1128/.20.21.8103-8111.2000
169.
Yakymovych I, Ten Dijke P, Heldin CH, Souchelnytskyi S. Regulation of Smad signaling by protein kinase C. Faseb j. 2001;15:553-555.
Not in our library10.1096/fj.00-0474fje
170.
Saura M, et al. Nitric oxide regulates transforming growth factor-beta signaling in endothelial cells. Circ. Res. 2005;97:1115-1123.
Not in our library10.1161/01.res.0000191538.76771.66
171.
Alarcón C, et al. Nuclear CDKs drive Smad transcriptional activation and turnover in BMP and TGF-beta pathways. Cell. 2009;139:757-769.
Not in our library10.1016/j.cell.2009.09.035
172.
Matsuura I, et al. Cyclin-dependent kinases regulate the antiproliferative function of Smads. Nature. 2004;430:226-231.
Not in our library10.1038/nature02650
173.
Sapkota G, et al. Dephosphorylation of the linker regions of Smad1 and Smad2/3 by small C-terminal domain phosphatases has distinct outcomes for bone morphogenetic protein and transforming growth factor-beta pathways. J. Biol. Chem. 2006;281:40412-40419.
Not in our library10.1074/jbc.m610172200
174.
Wrighton KH, et al. Small C-terminal domain phosphatases dephosphorylate the regulatory linker regions of Smad2 and Smad3 to enhance transforming growth factor-beta signaling. J. Biol. Chem. 2006;281:38365-38375.
Not in our library10.1074/jbc.m607246200
175.
Lin X, et al. PPM1A functions as a Smad phosphatase to terminate TGFbeta signaling. Cell. 2006;125:915-928.
Not in our library10.1016/j.cell.2006.03.044
176.
Yu J, et al. MTMR4 attenuates transforming growth factor beta (TGFbeta) signaling by dephosphorylating R-Smads in endosomes. J. Biol. Chem. 2010;285:8454-8462.
Not in our library10.1074/jbc.m109.075036
177.
Heikkinen PT, et al. Hypoxia-activated Smad3-specific dephosphorylation by PP2A. J. Biol. Chem. 2010;285:3740-3749.
Not in our library10.1074/jbc.m109.042978
178.
Lin X, Liang M, Feng XH. Smurf2 is a ubiquitin E3 ligase mediating proteasome-dependent degradation of Smad2 in transforming growth factor-beta signaling. J. Biol. Chem. 2000;275:36818-36822.
Not in our library10.1074/jbc.c000580200
179.
Regulation of Smad degradation and activity by Smurf2, an E3 ubiquitin ligase · 2001
Not checked
180.
Tang LY, et al. Ablation of Smurf2 reveals an inhibition in TGF-β signalling through multiple mono-ubiquitination of Smad3. Embo j. 2011;30:4777-4789.
Not in our library10.1038/emboj.2011.393
181.
Gao S, et al. Ubiquitin ligase Nedd4L targets activated Smad2/3 to limit TGF-beta signaling. Mol. Cell. 2009;36:457-468.
Not in our library10.1016/j.molcel.2009.09.043
182.
Komuro A, et al. Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1). Oncogene. 2004;23:6914-6923.
Not in our library10.1038/sj.onc.1207885
183.
Seo SR, et al. The novel E3 ubiquitin ligase Tiul1 associates with TGIF to target Smad2 for degradation. Embo j. 2004;23:3780-3792.
Not in our library10.1038/sj.emboj.7600398
184.
Soond SM, Chantry A. Selective targeting of activating and inhibitory Smads by distinct WWP2 ubiquitin ligase isoforms differentially modulates TGFβ signalling and EMT. Oncogene. 2011;30:2451-2462.
Not in our library10.1038/onc.2010.617
185.
Mavrakis KJ, et al. Arkadia enhances Nodal/TGF-beta signaling by coupling phospho-Smad2/3 activity and turnover. PLoS Biol. 2007;5:e67.
Not in our library10.1371/journal.pbio.0050067
186.
Xin H, et al. CHIP controls the sensitivity of transforming growth factor-beta signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation. J. Biol. Chem. 2005;280:20842-20850.
Not in our library10.1074/jbc.m412275200
187.
Bai Y, Yang C, Hu K, Elly C, Liu YC. Itch E3 ligase-mediated regulation of TGF-beta signaling by modulating smad2 phosphorylation. Mol. Cell. 2004;15:825-831.
Not in our library10.1016/j.molcel.2004.07.021
188.
Fukuchi M, et al. Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins. Mol. Biol. Cell. 2001;12:1431-1443.
Not in our library10.1091/mbc.12.5.1431
189.
Wan M, et al. Smad4 protein stability is regulated by ubiquitin ligase SCF beta-TrCP1. J. Biol. Chem. 2004;279:14484-14487.
Not in our library10.1074/jbc.c400005200
190.
Tang LY, Zhang YE. Non-degradative ubiquitination in Smad-dependent TGF-β signaling. Cell Biosci. 2011;1:43.
Not in our library10.1186/2045-3701-1-43
191.
Aragón E, et al. A Smad action turnover switch operated by WW domain readers of a phosphoserine code. Genes Dev. 2011;25:1275-1288.
Not in our library10.1101/gad.2060811
192.
Lee MK, et al. TGF-beta activates Erk MAP kinase signalling through direct phosphorylation of ShcA. Embo j. 2007;26:3957-3967.
Not in our library10.1038/sj.emboj.7601818
193.
Lavoie H, Gagnon J, Therrien M. ERK signalling: a master regulator of cell behaviour, life and fate. Nat. Rev. Mol. Cell Biol. 2020;21:607-632.
Not in our library10.1038/s41580-020-0255-7
194.
Extracellular Signal-Regulated Kinase: A Regulator of Cell Growth, Inflammation, Chondrocyte and Bone Cell Receptor-Mediated Gene Expression · 2019
No notice
195.
Schmidt A, Hall A. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 2002;16:1587-1609.
Not in our library10.1101/gad.1003302
196.
Papadimitriou E, Kardassis D, Moustakas A, Stournaras C. TGFβ-induced early activation of the small GTPase RhoA is Smad2/3-independent and involves Src and the guanine nucleotide exchange factor Vav2. Cell Physiol. Biochem. 2011;28:229-238.
Not in our library10.1159/000331734
197.
Lu X, et al. Effect of RhoC on the epithelial-mesenchymal transition process induced by TGF-β1 in lung adenocarcinoma cells. Oncol. Rep. 2016;36:3105-3112.
Not in our library10.3892/or.2016.5146
198.
Bhowmick NA, et al. Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a RhoA-dependent mechanism. Mol. Biol. Cell. 2001;12:27-36.
Not in our library10.1091/mbc.12.1.27
199.
Shen X, et al. The activity of guanine exchange factor NET1 is essential for transforming growth factor-beta-mediated stress fiber formation. J. Biol. Chem. 2001;276:15362-15368.
Not in our library10.1074/jbc.m009534200
200.
Papadimitriou E, et al. Differential regulation of the two RhoA-specific GEF isoforms Net1/Net1A by TGF-β and miR-24: role in epithelial-to-mesenchymal transition. Oncogene. 2012;31:2862-2875.
Not in our library10.1038/onc.2011.457
201.
Vardouli L, Moustakas A, Stournaras C. LIM-kinase 2 and cofilin phosphorylation mediate actin cytoskeleton reorganization induced by transforming growth factor-beta. J. Biol. Chem. 2005;280:11448-11457.
Not in our library10.1074/jbc.m402651200
202.
Lee J, Ko M, Joo CK. Rho plays a key role in TGF-beta1-induced cytoskeletal rearrangement in human retinal pigment epithelium. J. Cell Physiol. 2008;216:520-526.
Not in our library10.1002/jcp.21424
203.
Sousa-Squiavinato ACM, Rocha MR, Barcellos-de-Souza P, de Souza WF, Morgado-Diaz JA. Cofilin-1 signaling mediates epithelial-mesenchymal transition by promoting actin cytoskeleton reorganization and cell-cell adhesion regulation in colorectal cancer cells. Biochim Biophys. Acta Mol. Cell Res. 2019;1866:418-429.
Not in our library10.1016/j.bbamcr.2018.10.003
204.
Wei YH, Liao SL, Wang SH, Wang CC, Yang CH. Simvastatin and ROCK Inhibitor Y-27632 Inhibit Myofibroblast Differentiation of Graves’ Ophthalmopathy-Derived Orbital Fibroblasts via RhoA-Mediated ERK and p38 Signaling Pathways. Front Endocrinol. (Lausanne). 2020;11:607968.
Not in our library10.3389/fendo.2020.607968
205.
Matoba K, et al. Rho-Kinase Blockade Attenuates Podocyte Apoptosis by Inhibiting the Notch Signaling Pathway in Diabetic Nephropathy. Int J. Mol. Sci. 2017;18:1795.
Not in our library10.3390/ijms18081795
206.
Edlund S, Landström M, Heldin CH, Aspenström P. Transforming growth factor-beta-induced mobilization of actin cytoskeleton requires signaling by small GTPases Cdc42 and RhoA. Mol. Biol. Cell. 2002;13:902-914.
Not in our library10.1091/mbc.01-08-0398
207.
Jaffe AB, Hall A. Rho GTPases: biochemistry and biology. Annu Rev. Cell Dev. Biol. 2005;21:247-269.
Not in our library10.1146/annurev.cellbio.21.020604.150721
208.
Nomikou E, Livitsanou M, Stournaras C, Kardassis D. Transcriptional and post-transcriptional regulation of the genes encoding the small GTPases RhoA, RhoB, and RhoC: implications for the pathogenesis of human diseases. Cell Mol. Life Sci. 2018;75:2111-2124.
Not in our library10.1007/s00018-018-2787-y
209.
Zhang L, et al. TRAF4 promotes TGF-β receptor signaling and drives breast cancer metastasis. Mol. Cell. 2013;51:559-572.
Not in our library10.1016/j.molcel.2013.07.014
210.
Sorrentino A, et al. The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner. Nat. Cell Biol. 2008;10:1199-1207.
Not in our library10.1038/ncb1780
211.
Yamashita M, et al. TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-beta. Mol. Cell. 2008;31:918-924.
Not in our library10.1016/j.molcel.2008.09.002
212.
Engel ME, McDonnell MA, Law BK, Moses HL. Interdependent SMAD and JNK signaling in transforming growth factor-beta-mediated transcription. J. Biol. Chem. 1999;274:37413-37420.
Not in our library10.1074/jbc.274.52.37413
213.
Atfi A, Djelloul S, Chastre E, Davis R, Gespach C. Evidence for a role of Rho-like GTPases and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) in transforming growth factor beta-mediated signaling. J. Biol. Chem. 1997;272:1429-1432.
Not in our library10.1074/jbc.272.3.1429
214.
Minden A, Lin A, Claret FX, Abo A, Karin M. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell. 1995;81:1147-1157.
Not in our library10.1016/s0092-8674(05)80019-4
215.
Coso OA, et al. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell. 1995;81:1137-1146.
Not in our library10.1016/s0092-8674(05)80018-2
216.
Mazars A, et al. Differential roles of JNK and Smad2 signaling pathways in the inhibition of c-Myc-induced cell death by TGF-beta. Oncogene. 2000;19:1277-1287.
Not in our library10.1038/sj.onc.1203420
217.
Hocevar BA, Brown TL, Howe PH. TGF-beta induces fibronectin synthesis through a c-Jun N-terminal kinase-dependent, Smad4-independent pathway. Embo j. 1999;18:1345-1356.
Not in our library10.1093/emboj/18.5.1345
218.
Zeke A, Misheva M, Reményi A, Bogoyevitch MA. JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships. Microbiol Mol. Biol. Rev. 2016;80:793-835.
Not in our library10.1128/mmbr.00043-14
219.
Yu L, Hébert MC, Zhang YE. TGF-beta receptor-activated p38 MAP kinase mediates Smad-independent TGF-beta responses. Embo j. 2002;21:3749-3759.
Not in our library10.1093/emboj/cdf366
220.
Canovas B, Nebreda AR. Diversity and versatility of p38 kinase signalling in health and disease. Nat. Rev. Mol. Cell Biol. 2021;22:346-366.
Not in our library10.1038/s41580-020-00322-w
221.
Hamidi A, et al. Polyubiquitination of transforming growth factor β (TGFβ)-associated kinase 1 mediates nuclear factor-κB activation in response to different inflammatory stimuli. J. Biol. Chem. 2012;287:123-133.
Not in our library10.1074/jbc.m111.285122
222.
Kim HJ, Kim JG, Moon MY, Park SH, Park JB. IκB kinase γ/nuclear factor-κB-essential modulator (IKKγ/NEMO) facilitates RhoA GTPase activation, which, in turn, activates Rho-associated KINASE (ROCK) to phosphorylate IKKβ in response to transforming growth factor (TGF)-β1. J. Biol. Chem. 2014;289:1429-1440.
Not in our library10.1074/jbc.m113.520130
223.
Rodriguez PL, Sahay S, Olabisi OO, Whitehead IP. ROCK I-mediated activation of NF-kappaB by RhoB. Cell Signal. 2007;19:2361-2369.
Not in our library10.1016/j.cellsig.2007.07.021
224.
Zhu X, et al. TGF-beta1-induced PI3K/Akt/NF-kappaB/MMP9 signalling pathway is activated in Philadelphia chromosome-positive chronic myeloid leukaemia hemangioblasts. J. Biochem. 2011;149:405-414.
Not in our library10.1093/jb/mvr016
225.
Capece D, et al. NF-κB: blending metabolism, immunity, and inflammation. Trends Immunol. 2022;43:757-775.
Not in our library10.1016/j.it.2022.07.004
226.
Zinatizadeh MR, et al. The Nuclear Factor Kappa B (NF-kB) signaling in cancer development and immune diseases. Genes Dis. 2021;8:287-297.
Not in our library10.1016/j.gendis.2020.06.005
227.
NF-κB: A Double-Edged Sword Controlling Inflammation · 2022
No notice
228.
Yi JY, Shin I, Arteaga CL. Type I transforming growth factor beta receptor binds to and activates phosphatidylinositol 3-kinase. J. Biol. Chem. 2005;280:10870-10876.
Not in our library10.1074/jbc.m413223200
229.
Hamidi A, et al. TGF-β promotes PI3K-AKT signaling and prostate cancer cell migration through the TRAF6-mediated ubiquitylation of p85α. Sci. Signal. 2017;10:eaal4186.
Not in our library10.1126/scisignal.aal4186
230.
Bakin AV, Tomlinson AK, Bhowmick NA, Moses HL, Arteaga CL. Phosphatidylinositol 3-kinase function is required for transforming growth factor beta-mediated epithelial to mesenchymal transition and cell migration. J. Biol. Chem. 2000;275:36803-36810.
Not in our library10.1074/jbc.m005912200
231.
Lamouille S, Derynck R. Cell size and invasion in TGF-beta-induced epithelial to mesenchymal transition is regulated by activation of the mTOR pathway. J. Cell Biol. 2007;178:437-451.
Not in our library10.1083/jcb.200611146
232.
Lamouille S, Connolly E, Smyth JW, Akhurst RJ, Derynck R. TGF-β-induced activation of mTOR complex 2 drives epithelial-mesenchymal transition and cell invasion. J. Cell Sci. 2012;125:1259-1273.
Not in our library10.1242/jcs.095299
233.
Chen XH, et al. The TGF-β-induced up-regulation of NKG2DLs requires AKT/GSK-3β-mediated stabilization of SP1. J. Cell Mol. Med. 2017;21:860-870.
Not in our library10.1111/jcmm.13025
234.
Kato M, et al. Role of the Akt/FoxO3a pathway in TGF-beta1-mediated mesangial cell dysfunction: a novel mechanism related to diabetic kidney disease. J. Am. Soc. Nephrol. 2006;17:3325-3335.
Not in our library10.1681/asn.2006070754
235.
Franke TF. PI3K/Akt: getting it right matters. Oncogene. 2008;27:6473-6488.
Not in our library10.1038/onc.2008.313
236.
Liu Y, et al. Transforming growth factor-β (TGF-β)-mediated connective tissue growth factor (CTGF) expression in hepatic stellate cells requires Stat3 signaling activation. J. Biol. Chem. 2013;288:30708-30719.
Not in our library10.1074/jbc.m113.478685
237.
Tang LY, et al. Transforming Growth Factor-β (TGF-β) Directly Activates the JAK1-STAT3 Axis to Induce Hepatic Fibrosis in Coordination with the SMAD Pathway. J. Biol. Chem. 2017;292:4302-4312.
Not in our library10.1074/jbc.m116.773085
238.
Dees C, et al. JAK-2 as a novel mediator of the profibrotic effects of transforming growth factor β in systemic sclerosis. Arthritis Rheum. 2012;64:3006-3015.
Not in our library10.1002/art.34500
239.
Philips RL, et al. The JAK-STAT pathway at 30: Much learned, much more to do. Cell. 2022;185:3857-3876.
Not in our library10.1016/j.cell.2022.09.023
240.
Lehnert SA, Akhurst RJ. Embryonic expression pattern of TGF beta type-1 RNA suggests both paracrine and autocrine mechanisms of action. Development. 1988;104:263-273.
Not in our library10.1242/dev.104.2.263
241.
Pelton RW, Nomura S, Moses HL, Hogan BL. Expression of transforming growth factor beta 2 RNA during murine embryogenesis. Development. 1989;106:759-767.
Not in our library10.1242/dev.106.4.759
242.
Pelton RW, Dickinson ME, Moses HL, Hogan BL. In situ hybridization analysis of TGF beta 3 RNA expression during mouse development: comparative studies with TGF beta 1 and beta 2. Development. 1990;110:609-620.
Not in our library10.1242/dev.110.2.609
243.
Millan FA, Denhez F, Kondaiah P, Akhurst RJ. Embryonic gene expression patterns of TGF beta 1, beta 2 and beta 3 suggest different developmental functions in vivo. Development. 1991;111:131-143.
Not in our library10.1242/dev.111.1.131
244.
Pelton RW, Saxena B, Jones M, Moses HL, Gold LI. Immunohistochemical localization of TGF beta 1, TGF beta 2, and TGF beta 3 in the mouse embryo: expression patterns suggest multiple roles during embryonic development. J. Cell Biol. 1991;115:1091-1105.
Not in our library10.1083/jcb.115.4.1091
245.
Rosa F, et al. Mesoderm induction in amphibians: the role of TGF-beta 2-like factors. Science. 1988;239:783-785.
Not in our library10.1126/science.3422517
246.
Kimelman D, Kirschner M. Synergistic induction of mesoderm by FGF and TGF-beta and the identification of an mRNA coding for FGF in the early Xenopus embryo. Cell. 1987;51:869-877.
Not in our library10.1016/0092-8674(87)90110-3
247.
Bai H, Xie YL, Gao YX, Cheng T, Wang ZZ. The balance of positive and negative effects of TGF-β signaling regulates the development of hematopoietic and endothelial progenitors in human pluripotent stem cells. Stem Cells Dev. 2013;22:2765-2776.
Not in our library10.1089/scd.2013.0008
248.
Zhang CY, et al. Transforming growth factor-β1 regulates the nascent hematopoietic stem cell niche by promoting gluconeogenesis. Leukemia. 2018;32:479-491.
Not in our library10.1038/leu.2017.198
249.
Challen GA, Boles NC, Chambers SM, Goodell MA. Distinct hematopoietic stem cell subtypes are differentially regulated by TGF-beta1. Cell Stem Cell. 2010;6:265-278.
Not in our library10.1016/j.stem.2010.02.002
250.
Xie Y, et al. Cooperative Effect of Erythropoietin and TGF-β Inhibition on Erythroid Development in Human Pluripotent Stem Cells. J. Cell Biochem. 2015;116:2735-2743.
Not in our library10.1002/jcb.25233
251.
Ng F, et al. PDGF, TGF-beta, and FGF signaling is important for differentiation and growth of mesenchymal stem cells (MSCs): transcriptional profiling can identify markers and signaling pathways important in differentiation of MSCs into adipogenic, chondrogenic, and osteogenic lineages. Blood. 2008;112:295-307.
Not in our library10.1182/blood-2007-07-103697
252.
Jian H, et al. Smad3-dependent nuclear translocation of beta-catenin is required for TGF-beta1-induced proliferation of bone marrow-derived adult human mesenchymal stem cells. Genes Dev. 2006;20:666-674.
Not in our library10.1101/gad.1388806
253.
Alliston T, Choy L, Ducy P, Karsenty G, Derynck R. TGF-beta-induced repression of CBFA1 by Smad3 decreases cbfa1 and osteocalcin expression and inhibits osteoblast differentiation. Embo j. 2001;20:2254-2272.
Not in our library10.1093/emboj/20.9.2254
254.
Liu D, Black BL, Derynck R. TGF-beta inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3. Genes Dev. 2001;15:2950-2966.
Not in our library10.1101/gad.925901
255.
Massagué J, Cheifetz S, Endo T, Nadal-Ginard B. Type beta transforming growth factor is an inhibitor of myogenic differentiation. Proc. Natl Acad. Sci. USA. 1986;83:8206-8210.
Not in our library10.1073/pnas.83.21.8206
256.
Florini JR, et al. Transforming growth factor-beta. A very potent inhibitor of myoblast differentiation, identical to the differentiation inhibitor secreted by Buffalo rat liver cells. J. Biol. Chem. 1986;261:16509-16513.
Not in our library10.1016/s0021-9258(18)66595-0
257.
Zhu S, Goldschmidt-Clermont PJ, Dong C. Transforming growth factor-beta-induced inhibition of myogenesis is mediated through Smad pathway and is modulated by microtubule dynamic stability. Circ. Res. 2004;94:617-625.
Not in our library10.1161/01.res.0000118599.25944.d5
258.
Choy L, Derynck R. Transforming growth factor-beta inhibits adipocyte differentiation by Smad3 interacting with CCAAT/enhancer-binding protein (C/EBP) and repressing C/EBP transactivation function. J. Biol. Chem. 2003;278:9609-9619.
Not in our library10.1074/jbc.m212259200
259.
Choy L, Skillington J, Derynck R. Roles of autocrine TGF-beta receptor and Smad signaling in adipocyte differentiation. J. Cell Biol. 2000;149:667-682.
Not in our library10.1083/jcb.149.3.667
260.
Kurpinski K, et al. Transforming growth factor-beta and notch signaling mediate stem cell differentiation into smooth muscle cells. Stem Cells. 2010;28:734-742.
Not in our library10.1002/stem.319
261.
Seyedin SM, et al. Cartilage-inducing factor-A. Apparent identity to transforming growth factor-beta. J. Biol. Chem. 1986;261:5693-5695.
Not in our library10.1016/s0021-9258(17)38436-3
262.
Leonard CM, et al. Role of transforming growth factor-beta in chondrogenic pattern formation in the embryonic limb: stimulation of mesenchymal condensation and fibronectin gene expression by exogenenous TGF-beta and evidence for endogenous TGF-beta-like activity. Dev. Biol. 1991;145:99-109.
Not in our library10.1016/0012-1606(91)90216-p
263.
Reiss M, Sartorelli AC. Regulation of growth and differentiation of human keratinocytes by type beta transforming growth factor and epidermal growth factor. Cancer Res. 1987;47:6705-6709.
Not in our library
264.
Masui T, et al. Type beta transforming growth factor is the primary differentiation-inducing serum factor for normal human bronchial epithelial cells. Proc. Natl Acad. Sci. USA. 1986;83:2438-2442.
Not in our library10.1073/pnas.83.8.2438
265.
Yu X, et al. The Cytokine TGF-β Promotes the Development and Homeostasis of Alveolar Macrophages. Immunity. 2017;47:903-912.e904.
Not in our library10.1016/j.immuni.2017.10.007
266.
Clark AT, Young RJ, Bertram JF. In vitro studies on the roles of transforming growth factor-beta 1 in rat metanephric development. Kidney Int. 2001;59:1641-1653.
Not in our library10.1046/j.1523-1755.2001.0590051641.x
267.
Sanvito F, et al. TGF-beta 1 influences the relative development of the exocrine and endocrine pancreas in vitro. Development. 1994;120:3451-3462.
Not in our library10.1242/dev.120.12.3451
268.
Böttinger EP, et al. Expression of a dominant-negative mutant TGF-beta type II receptor in transgenic mice reveals essential roles for TGF-beta in regulation of growth and differentiation in the exocrine pancreas. Embo j. 1997;16:2621-2633.
Not in our library10.1093/emboj/16.10.2621
269.
Huojia M, et al. TGF-beta3 induces ectopic mineralization in fetal mouse dental pulp during tooth germ development. Dev. Growth Differ. 2005;47:141-152.
Not in our library10.1111/j.1440-169x.2005.00790.x
270.
Yi JJ, Barnes AP, Hand R, Polleux F, Ehlers MD. TGF-beta signaling specifies axons during brain development. Cell. 2010;142:144-157.
Not in our library10.1016/j.cell.2010.06.010
271.
Stipursky J, Gomes FC. TGF-beta1/SMAD signaling induces astrocyte fate commitment in vitro: implications for radial glia development. Glia. 2007;55:1023-1033.
Not in our library10.1002/glia.20522
272.
Farkas LM, Dünker N, Roussa E, Unsicker K, Krieglstein K. Transforming growth factor-beta(s) are essential for the development of midbrain dopaminergic neurons in vitro and in vivo. J. Neurosci. 2003;23:5178-5186.
Not in our library10.1523/jneurosci.23-12-05178.2003
273.
Chleilat E, et al. TGF-β Signaling Regulates Development of Midbrain Dopaminergic and Hindbrain Serotonergic Neuron Subgroups. Neuroscience. 2018;381:124-137.
Not in our library10.1016/j.neuroscience.2018.04.019
274.
Effects of Transforming Growth Factor Beta 1 in Cerebellar Development: Role in Synapse Formation · 2016
Not checked
275.
Morris AD, Lewis GM, Kucenas S. Perineurial Glial Plasticity and the Role of TGF-β in the Development of the Blood-Nerve Barrier. J. Neurosci. 2017;37:4790-4807.
Not in our library10.1523/jneurosci.2875-16.2017
276.
de Sampaio e Spohr TC, Martinez R, da Silva EF, Neto VM, Gomes FC. Neuro-glia interaction effects on GFAP gene: a novel role for transforming growth factor-beta1. Eur. J. Neurosci. 2002;16:2059-2069.
Not in our library10.1046/j.1460-9568.2002.02283.x
277.
Miettinen PJ, Ebner R, Lopez AR, Derynck R. TGF-beta induced transdifferentiation of mammary epithelial cells to mesenchymal cells: involvement of type I receptors. J. Cell Biol. 1994;127:2021-2036.
Not in our library10.1083/jcb.127.6.2021
278.
Lamouille S, Xu J, Derynck R. Molecular mechanisms of epithelial-mesenchymal transition. Nat. Rev. Mol. Cell Biol. 2014;15:178-196.
Not in our library10.1038/nrm3758
279.
Jalali A, Zhu X, Liu C, Nawshad A. Induction of palate epithelial mesenchymal transition by transforming growth factor β3 signaling. Dev. Growth Differ. 2012;54:633-648.
Not in our library10.1111/j.1440-169x.2012.01364.x
280.
Nawshad A, Hay ED. TGFbeta3 signaling activates transcription of the LEF1 gene to induce epithelial mesenchymal transformation during mouse palate development. J. Cell Biol. 2003;163:1291-1301.
Not in our library10.1083/jcb.200306024
281.
Pelton RW, Hogan BL, Miller DA, Moses HL. Differential expression of genes encoding TGFs beta 1, beta 2, and beta 3 during murine palate formation. Dev. Biol. 1990;141:456-460.
Not in our library10.1016/0012-1606(90)90401-4
282.
Fitzpatrick DR, Denhez F, Kondaiah P, Akhurst RJ. Differential expression of TGF beta isoforms in murine palatogenesis. Development. 1990;109:585-595.
Not in our library10.1242/dev.109.3.585
283.
Brunet CL, Sharpe PM, Ferguson MW. Inhibition of TGF-beta 3 (but not TGF-beta 1 or TGF-beta 2) activity prevents normal mouse embryonic palate fusion. Int J. Dev. Biol. 1995;39:345-355.
Not in our library
284.
Sabbineni H, Verma A, Somanath PR. Isoform-specific effects of transforming growth factor beta on endothelial-to-mesenchymal transition. J. Cell Physiol. 2018;233:8418-8428.
Not in our library10.1002/jcp.26801
285.
Molin DG, et al. Expression patterns of Tgfbeta1-3 associate with myocardialisation of the outflow tract and the development of the epicardium and the fibrous heart skeleton. Dev. Dyn. 2003;227:431-444.
Not in our library10.1002/dvdy.10314
286.
Dickson MC, Slager HG, Duffie E, Mummery CL, Akhurst RJ. RNA and protein localisations of TGF beta 2 in the early mouse embryo suggest an involvement in cardiac development. Development. 1993;117:625-639.
Not in our library10.1242/dev.117.2.625
287.
Akhurst RJ, Lehnert SA, Faissner A, Duffie E. TGF beta in murine morphogenetic processes: the early embryo and cardiogenesis. Development. 1990;108:645-656.
Not in our library10.1242/dev.108.4.645
288.
Camenisch TD, et al. Temporal and distinct TGFbeta ligand requirements during mouse and avian endocardial cushion morphogenesis. Dev. Biol. 2002;248:170-181.
Not in our library10.1006/dbio.2002.0731
289.
Potts JD, Runyan RB. Epithelial-mesenchymal cell transformation in the embryonic heart can be mediated, in part, by transforming growth factor beta. Dev. Biol. 1989;134:392-401.
Not in our library10.1016/0012-1606(89)90111-5
290.
Azhar M, et al. Ligand-specific function of transforming growth factor beta in epithelial-mesenchymal transition in heart development. Dev. Dyn. 2009;238:431-442.
Not in our library10.1002/dvdy.21854
291.
Nakajima Y, Yamagishi T, Nakamura H, Markwald RR, Krug EL. An autocrine function for transforming growth factor (TGF)-beta3 in the transformation of atrioventricular canal endocardium into mesenchyme during chick heart development. Dev. Biol. 1998;194:99-113.
Not in our library10.1006/dbio.1997.8807
292.
Compton LA, Potash DA, Mundell NA, Barnett JV. Transforming growth factor-beta induces loss of epithelial character and smooth muscle cell differentiation in epicardial cells. Dev. Dyn. 2006;235:82-93.
Not in our library10.1002/dvdy.20629
293.
Austin AF, Compton LA, Love JD, Brown CB, Barnett JV. Primary and immortalized mouse epicardial cells undergo differentiation in response to TGFbeta. Dev. Dyn. 2008;237:366-376.
Not in our library10.1002/dvdy.21421
294.
Liu M, et al. Transforming Growth Factor-induced Protein Promotes NF-κB-mediated Angiogenesis during Postnatal Lung Development. Am. J. Respir. Cell Mol. Biol. 2021;64:318-330.
Not in our library10.1165/rcmb.2020-0153oc
295.
Ahmed S, Liu CC, Nawshad A. Mechanisms of palatal epithelial seam disintegration by transforming growth factor (TGF) beta3. Dev. Biol. 2007;309:193-207.
Not in our library10.1016/j.ydbio.2007.06.018
296.
Dunker N, Schmitt K, Krieglstein K. TGF-beta is required for programmed cell death in interdigital webs of the developing mouse limb. Mech. Dev. 2002;113:111-120.
Not in our library10.1016/s0925-4773(02)00015-1
297.
Krieglstein K, et al. Reduction of endogenous transforming growth factors beta prevents ontogenetic neuron death. Nat. Neurosci. 2000;3:1085-1090.
Not in our library10.1038/80598
298.
Dunker N, Schuster N, Krieglstein K. TGF-beta modulates programmed cell death in the retina of the developing chick embryo. Development. 2001;128:1933-1942.
Not in our library10.1242/dev.128.11.1933
299.
Schuster N, Dunker N, Krieglstein K. Transforming growth factor-beta induced cell death in the developing chick retina is mediated via activation of c-jun N-terminal kinase and downregulation of the anti-apoptotic protein Bcl-X(L). Neurosci. Lett. 2002;330:239-242.
Not in our library10.1016/s0304-3940(02)00801-7
300.
Braunger BM, et al. TGF-β signaling protects retinal neurons from programmed cell death during the development of the mammalian eye. J. Neurosci. 2013;33:14246-14258.
Not in our library10.1523/jneurosci.0991-13.2013
301.
Chronic Wound Healing by Amniotic Membrane: TGF-β and EGF Signaling Modulation in Re-epithelialization · 2021
Not checked
302.
McMullen H, et al. Spatial and temporal expression of transforming growth factor-beta isoforms during ovine excisional and incisional wound repair. Wound Repair Regen. 1995;3:141-156.
Not in our library10.1046/j.1524-475x.1995.30206.x
303.
Gold LI, Sung JJ, Siebert JW, Longaker MT. Type I (RI) and type II (RII) receptors for transforming growth factor-beta isoforms are expressed subsequent to transforming growth factor-beta ligands during excisional wound repair. Am. J. Pathol. 1997;150:209-222.
Not in our library
304.
Mustoe TA, et al. Accelerated healing of incisional wounds in rats induced by transforming growth factor-beta. Science. 1987;237:1333-1336.
Not in our library10.1126/science.2442813
305.
Postlethwaite AE, Keski-Oja J, Moses HL, Kang AH. Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta. J. Exp. Med. 1987;165:251-256.
Not in our library10.1084/jem.165.1.251
306.
Pierce GF, et al. Platelet-derived growth factor and transforming growth factor-beta enhance tissue repair activities by unique mechanisms. J. Cell Biol. 1989;109:429-440.
Not in our library10.1083/jcb.109.1.429
307.
Puolakkainen PA, et al. Acceleration of wound healing in aged rats by topical application of transforming growth factor-beta(1). Wound Repair Regen. 1995;3:330-339.
Not in our library10.1046/j.1524-475x.1995.t01-1-30314.x
308.
Wahl SM, et al. Transforming growth factor type beta induces monocyte chemotaxis and growth factor production. Proc. Natl Acad. Sci. USA. 1987;84:5788-5792.
Not in our library10.1073/pnas.84.16.5788
309.
Rappolee DA, Mark D, Banda MJ, Werb Z. Wound macrophages express TGF-alpha and other growth factors in vivo: analysis by mRNA phenotyping. Science. 1988;241:708-712.
Not in our library10.1126/science.3041594
310.
Kane CJ, Hebda PA, Mansbridge JN, Hanawalt PC. Direct evidence for spatial and temporal regulation of transforming growth factor beta 1 expression during cutaneous wound healing. J. Cell Physiol. 1991;148:157-173.
Not in our library10.1002/jcp.1041480119
311.
Zambruno G, et al. Transforming growth factor-beta 1 modulates beta 1 and beta 5 integrin receptors and induces the de novo expression of the alpha v beta 6 heterodimer in normal human keratinocytes: implications for wound healing. J. Cell Biol. 1995;129:853-865.
Not in our library10.1083/jcb.129.3.853
312.
Jeong HW, Kim IS. TGF-beta1 enhances betaig-h3-mediated keratinocyte cell migration through the alpha3beta1 integrin and PI3K. J. Cell Biochem. 2004;92:770-780.
Not in our library10.1002/jcb.20110
313.
Bandyopadhyay B, et al. A “traffic control” role for TGFbeta3: orchestrating dermal and epidermal cell motility during wound healing. J. Cell Biol. 2006;172:1093-1105.
Not in our library10.1083/jcb.200507111
314.
Heimark RL, Twardzik DR, Schwartz SM. Inhibition of endothelial regeneration by type-beta transforming growth factor from platelets. Science. 1986;233:1078-1080.
Not in our library10.1126/science.3461562
315.
Roberts AB, et al. Transforming growth factor type beta: rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro. Proc. Natl Acad. Sci. USA. 1986;83:4167-4171.
Not in our library10.1073/pnas.83.12.4167
316.
Development of gene-switch transgenic mice that inducibly express transforming growth factor β1 in the epidermis · 1999
Not checked
317.
Lynch SE, Colvin RB, Antoniades HN. Growth factors in wound healing. Single and synergistic effects on partial thickness porcine skin wounds. J. Clin. Invest. 1989;84:640-646.
Not in our library10.1172/jci114210
318.
Madri JA, Pratt BM, Tucker AM. Phenotypic modulation of endothelial cells by transforming growth factor-beta depends upon the composition and organization of the extracellular matrix. J. Cell Biol. 1988;106:1375-1384.
Not in our library10.1083/jcb.106.4.1375
319.
Iruela-Arispe ML, Sage EH. Endothelial cells exhibiting angiogenesis in vitro proliferate in response to TGF-beta 1. J. Cell Biochem. 1993;52:414-430.
Not in our library10.1002/jcb.240520406
320.
Lu SL, et al. Overexpression of transforming growth factor beta1 in head and neck epithelia results in inflammation, angiogenesis, and epithelial hyperproliferation. Cancer Res. 2004;64:4405-4410.
Not in our library10.1158/0008-5472.can-04-1032
321.
Cox DA, Kunz S, Cerletti N, McMaster GK, Burk RR. Wound healing in aged animals-effects of locally applied transforming growth factor beta 2 in different model systems. Exs. 1992;61:287-295.
Not in our library10.1007/978-3-0348-7001-6_46
322.
Frank S, et al. Regulation of vascular endothelial growth factor expression in cultured keratinocytes. Implications for normal and impaired wound healing. J. Biol. Chem. 1995;270:12607-12613.
Not in our library10.1074/jbc.270.21.12607
323.
Pertovaara L, et al. Vascular endothelial growth factor is induced in response to transforming growth factor-beta in fibroblastic and epithelial cells. J. Biol. Chem. 1994;269:6271-6274.
Not in our library10.1016/s0021-9258(17)37365-9
324.
Strutz F, et al. TGF-beta 1 induces proliferation in human renal fibroblasts via induction of basic fibroblast growth factor (FGF-2). Kidney Int. 2001;59:579-592.
Not in our library10.1046/j.1523-1755.2001.059002579.x
325.
Battegay EJ, Raines EW, Seifert RA, Bowen-Pope DF, Ross R. TGF-beta induces bimodal proliferation of connective tissue cells via complex control of an autocrine PDGF loop. Cell. 1990;63:515-524.
Not in our library10.1016/0092-8674(90)90448-n
326.
Ignotz RA, Massagué J. Transforming growth factor-beta stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix. J. Biol. Chem. 1986;261:4337-4345.
Not in our library10.1016/s0021-9258(17)35666-1
327.
Clark RA, McCoy GA, Folkvord JM, McPherson JM. TGF-beta 1 stimulates cultured human fibroblasts to proliferate and produce tissue-like fibroplasia: a fibronectin matrix-dependent event. J. Cell Physiol. 1997;170:69-80.
Not in our library10.1002/(sici)1097-4652(199701)170:1<69::aid-jcp8>3.0.co;2-j
328.
Murata H, et al. TGF-beta3 stimulates and regulates collagen synthesis through TGF-beta1-dependent and independent mechanisms. J. Invest Dermatol. 1997;108:258-262.
Not in our library10.1111/1523-1747.ep12286451
329.
Tyrone JW, et al. Transforming growth factor beta3 promotes fascial wound healing in a new animal model. Arch. Surg. 2000;135:1154-1159.
Not in our library10.1001/archsurg.135.10.1154
330.
Edwards DR, et al. Transforming growth factor beta modulates the expression of collagenase and metalloproteinase inhibitor. Embo j. 1987;6:1899-1904.
Not in our library10.1002/j.1460-2075.1987.tb02449.x
331.
Lund LR, et al. Transforming growth factor-beta is a strong and fast acting positive regulator of the level of type-1 plasminogen activator inhibitor mRNA in WI-38 human lung fibroblasts. Embo j. 1987;6:1281-1286.
Not in our library10.1002/j.1460-2075.1987.tb02365.x
332.
Overall CM, Wrana JL, Sodek J. Independent regulation of collagenase, 72-kDa progelatinase, and metalloendoproteinase inhibitor expression in human fibroblasts by transforming growth factor-beta. J. Biol. Chem. 1989;264:1860-1869.
Not in our library10.1016/s0021-9258(18)94267-5
333.
Wright JK, Cawston TE, Hazleman BL. Transforming growth factor beta stimulates the production of the tissue inhibitor of metalloproteinases (TIMP) by human synovial and skin fibroblasts. Biochim. Biophys. Acta. 1991;1094:207-210.
Not in our library10.1016/0167-4889(91)90010-u
334.
Shah M, Foreman DM, Ferguson MW. Neutralisation of TGF-beta 1 and TGF-beta 2 or exogenous addition of TGF-beta 3 to cutaneous rat wounds reduces scarring. J. Cell Sci. 1995;108:985-1002.
Not in our library10.1242/jcs.108.3.985
335.
Montesano R, Orci L. Transforming growth factor beta stimulates collagen-matrix contraction by fibroblasts: implications for wound healing. Proc. Natl Acad. Sci. USA. 1988;85:4894-4897.
Not in our library10.1073/pnas.85.13.4894
336.
Meckmongkol TT, Harmon R, McKeown-Longo P, Van De Water L. The fibronectin synergy site modulates TGF-beta-dependent fibroblast contraction. Biochem Biophys. Res Commun. 2007;360:709-714.
Not in our library10.1016/j.bbrc.2007.06.121
337.
Desmoulière A, Geinoz A, Gabbiani F, Gabbiani G. Transforming growth factor-beta 1 induces alpha-smooth muscle actin expression in granulation tissue myofibroblasts and in quiescent and growing cultured fibroblasts. J. Cell Biol. 1993;122:103-111.
Not in our library10.1083/jcb.122.1.103
338.
Jakowlew SB, et al. Transforming growth factor-beta (TGF-beta) isoforms in rat liver regeneration: messenger RNA expression and activation of latent TGF-beta. Cell Regul. 1991;2:535-548.
Not in our library10.1091/mbc.2.7.535
339.
Armendariz-Borunda J, et al. Transforming growth factor beta gene expression is transiently enhanced at a critical stage during liver regeneration after CCl4 treatment. Lab Invest. 1993;69:283-294.
Not in our library
340.
Braun L, et al. Transforming growth factor beta mRNA increases during liver regeneration: a possible paracrine mechanism of growth regulation. Proc. Natl Acad. Sci. USA. 1988;85:1539-1543.
Not in our library10.1073/pnas.85.5.1539
341.
Nishikawa Y, Wang M, Carr BI. Changes in TGF-beta receptors of rat hepatocytes during primary culture and liver regeneration: increased expression of TGF-beta receptors associated with increased sensitivity to TGF-beta-mediated growth inhibition. J. Cell Physiol. 1998;176:612-623.
Not in our library10.1002/(sici)1097-4652(199809)176:3<612::aid-jcp18>3.0.co;2-0
342.
Grasl-Kraupp B, et al. Levels of transforming growth factor beta and transforming growth factor beta receptors in rat liver during growth, regression by apoptosis and neoplasia. Hepatology. 1998;28:717-726.
Not in our library10.1002/hep.510280318
343.
Riesle E, et al. Increased expression of transforming growth factor beta s after acute oedematous pancreatitis in rats suggests a role in pancreatic repair. Gut. 1997;40:73-79.
Not in our library10.1136/gut.40.1.73
344.
Friess H, et al. Enhanced expression of TGF-betas and their receptors in human acute pancreatitis. Ann. Surg. 1998;227:95-104.
Not in our library10.1097/00000658-199801000-00014
345.
Gress T, et al. Enhancement of transforming growth factor beta 1 expression in the rat pancreas during regeneration from caerulein-induced pancreatitis. Eur. J. Clin. Invest. 1994;24:679-685.
Not in our library10.1111/j.1365-2362.1994.tb01060.x
346.
Wan M, et al. Injury-activated transforming growth factor β controls mobilization of mesenchymal stem cells for tissue remodeling. Stem Cells. 2012;30:2498-2511.
Not in our library10.1002/stem.1208
347.
Bax NA, et al. In vitro epithelial-to-mesenchymal transformation in human adult epicardial cells is regulated by TGFβ-signaling and WT1. Basic Res Cardiol. 2011;106:829-847.
Not in our library10.1007/s00395-011-0181-0
348.
Redini F, Galera P, Mauviel A, Loyau G, Pujol JP. Transforming growth factor beta stimulates collagen and glycosaminoglycan biosynthesis in cultured rabbit articular chondrocytes. FEBS Lett. 1988;234:172-176.
Not in our library10.1016/0014-5793(88)81327-9
349.
Malemud CJ, Killeen W, Hering TM, Purchio AF. Enhanced sulfated-proteoglycan core protein synthesis by incubation of rabbit chondrocytes with recombinant transforming growth factor-beta 1. J. Cell Physiol. 1991;149:152-159.
Not in our library10.1002/jcp.1041490119
350.
Buss A, et al. TGF-beta1 and TGF-beta2 expression after traumatic human spinal cord injury. Spinal Cord. 2008;46:364-371.
Not in our library10.1038/sj.sc.3102148
351.
Lehrmann E, et al. Microglia and macrophages are major sources of locally produced transforming growth factor-beta1 after transient middle cerebral artery occlusion in rats. Glia. 1998;24:437-448.
Not in our library10.1002/(sici)1098-1136(199812)24:4<437::aid-glia9>3.0.co;2-x
352.
Hannon GJ, Beach D. p15INK4B is a potential effector of TGF-beta-induced cell cycle arrest. Nature. 1994;371:257-261.
Not in our library10.1038/371257a0
353.
Datto MB, et al. Transforming growth factor beta induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism. Proc. Natl Acad. Sci. USA. 1995;92:5545-5549.
Not in our library10.1073/pnas.92.12.5545
354.
Rich JN, Zhang M, Datto MB, Bigner DD, Wang XF. Transforming growth factor-beta-mediated p15(INK4B) induction and growth inhibition in astrocytes is SMAD3-dependent and a pathway prominently altered in human glioma cell lines. J. Biol. Chem. 1999;274:35053-35058.
Not in our library10.1074/jbc.274.49.35053
355.
Seoane J, Le HV, Shen L, Anderson SA, Massagué J. Integration of Smad and forkhead pathways in the control of neuroepithelial and glioblastoma cell proliferation. Cell. 2004;117:211-223.
Not in our library10.1016/s0092-8674(04)00298-3
356.
Gomis RR, Alarcón C, Nadal C, Van Poznak C, Massagué J. C/EBPbeta at the core of the TGFbeta cytostatic response and its evasion in metastatic breast cancer cells. Cancer Cell. 2006;10:203-214.
Not in our library10.1016/j.ccr.2006.07.019
357.
Feng XH, Lin X, Derynck R. Smad2, Smad3 and Smad4 cooperate with Sp1 to induce p15(Ink4B) transcription in response to TGF-beta. Embo j. 2000;19:5178-5193.
Not in our library10.1093/emboj/19.19.5178
358.
Pardali K, et al. Role of Smad proteins and transcription factor Sp1 in p21(Waf1/Cip1) regulation by transforming growth factor-beta. J. Biol. Chem. 2000;275:29244-29256.
Not in our library10.1074/jbc.m909467199
359.
Reynisdóttir I, Polyak K, Iavarone A, Massagué J. Kip/Cip and Ink4 Cdk inhibitors cooperate to induce cell cycle arrest in response to TGF-beta. Genes Dev. 1995;9:1831-1845.
Not in our library10.1101/gad.9.15.1831
360.
Reynisdóttir I, Massagué J. The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2. Genes Dev. 1997;11:492-503.
Not in our library10.1101/gad.11.4.492
361.
Kamesaki H, Nishizawa K, Michaud GY, Cossman J, Kiyono T. TGF-beta 1 induces the cyclin-dependent kinase inhibitor p27Kip1 mRNA and protein in murine B cells. J. Immunol. 1998;160:770-777.
Not in our library10.4049/jimmunol.160.2.770
362.
Scandura JM, Boccuni P, Massagué J, Nimer SD. Transforming growth factor beta-induced cell cycle arrest of human hematopoietic cells requires p57KIP2 up-regulation. Proc. Natl Acad. Sci. USA. 2004;101:15231-15236.
Not in our library10.1073/pnas.0406771101
363.
Chen CR, Kang Y, Siegel PM, Massagué J. E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression. Cell. 2002;110:19-32.
Not in our library10.1016/s0092-8674(02)00801-2
364.
Yagi K, et al. c-myc is a downstream target of the Smad pathway. J. Biol. Chem. 2002;277:854-861.
Not in our library10.1074/jbc.m104170200
365.
Kang Y, Chen CR, Massagué J. A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells. Mol. Cell. 2003;11:915-926.
Not in our library10.1016/s1097-2765(03)00109-6
366.
Lasorella A, Noseda M, Beyna M, Yokota Y, Iavarone A. Id2 is a retinoblastoma protein target and mediates signalling by Myc oncoproteins. Nature. 2000;407:592-598.
Not in our library10.1038/35036504
367.
Siegel PM, Shu W, Massagué J. Mad upregulation and Id2 repression accompany transforming growth factor (TGF)-beta-mediated epithelial cell growth suppression. J. Biol. Chem. 2003;278:35444-35450.
Not in our library10.1074/jbc.m301413200
368.
Seoane J, et al. TGFbeta influences Myc, Miz-1 and Smad to control the CDK inhibitor p15INK4b. Nat. Cell Biol. 2001;3:400-408.
Not in our library10.1038/35070086
369.
Seoane J, Le HV, Massagué J. Myc suppression of the p21(Cip1) Cdk inhibitor influences the outcome of the p53 response to DNA damage. Nature. 2002;419:729-734.
Not in our library10.1038/nature01119
370.
Prabhu S, Ignatova A, Park ST, Sun XH. Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins. Mol. Cell Biol. 1997;17:5888-5896.
Not in our library10.1128/mcb.17.10.5888
371.
Asirvatham AJ, Carey JP, Chaudhary J. ID1-, ID2-, and ID3-regulated gene expression in E2A positive or negative prostate cancer cells. Prostate. 2007;67:1411-1420.
Not in our library10.1002/pros.20633
372.
Iavarone A, Massagué J. E2F and histone deacetylase mediate transforming growth factor beta repression of cdc25A during keratinocyte cell cycle arrest. Mol. Cell Biol. 1999;19:916-922.
Not in our library10.1128/mcb.19.1.916
373.
Bhowmick NA, et al. TGF-beta-induced RhoA and p160ROCK activation is involved in the inhibition of Cdc25A with resultant cell-cycle arrest. Proc. Natl Acad. Sci. USA. 2003;100:15548-15553.
Not in our library10.1073/pnas.2536483100
374.
Ray D, et al. Transforming growth factor beta facilitates beta-TrCP-mediated degradation of Cdc25A in a Smad3-dependent manner. Mol. Cell Biol. 2005;25:3338-3347.
Not in our library10.1128/mcb.25.8.3338-3347.2005
375.
Leof EB, et al. Induction of c-sis mRNA and activity similar to platelet-derived growth factor by transforming growth factor beta: a proposed model for indirect mitogenesis involving autocrine activity. Proc. Natl Acad. Sci. USA. 1986;83:2453-2457.
Not in our library10.1073/pnas.83.8.2453
376.
Wildey GM, Patil S, Howe PH. Smad3 potentiates transforming growth factor beta (TGFbeta)-induced apoptosis and expression of the BH3-only protein Bim in WEHI 231 B lymphocytes. J. Biol. Chem. 2003;278:18069-18077.
Not in our library10.1074/jbc.m211958200
377.
Ramjaun AR, Tomlinson S, Eddaoudi A. & Downward, J. Upregulation of two BH3-only proteins, Bmf and Bim, during TGF beta-induced apoptosis. Oncogene. 2007;26:970-981.
Not in our library10.1038/sj.onc.1209852
378.
Yoshimoto T, et al. Involvement of smad2 and Erk/Akt cascade in TGF-β1-induced apoptosis in human gingival epithelial cells. Cytokine. 2015;75:165-173.
Not in our library10.1016/j.cyto.2015.03.011
379.
Schiffer M, et al. Apoptosis in podocytes induced by TGF-beta and Smad7. J. Clin. Invest. 2001;108:807-816.
Not in our library10.1172/jci200112367
380.
Francis JM, et al. Transforming growth factor-beta 1 induces apoptosis independently of p53 and selectively reduces expression of Bcl-2 in multipotent hematopoietic cells. J. Biol. Chem. 2000;275:39137-39145.
Not in our library10.1074/jbc.m007212200
381.
Schulz R, Vogel T, Dressel R, Krieglstein K. TGF-beta superfamily members, ActivinA and TGF-beta1, induce apoptosis in oligodendrocytes by different pathways. Cell Tissue Res. 2008;334:327-338.
Not in our library10.1007/s00441-008-0714-5
382.
Larisch S, et al. A novel mitochondrial septin-like protein, ARTS, mediates apoptosis dependent on its P-loop motif. Nat. Cell Biol. 2000;2:915-921.
Not in our library10.1038/35046566
383.
Perlman R, Schiemann WP, Brooks MW, Lodish HF, Weinberg RA. TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation. Nat. Cell Biol. 2001;3:708-714.
Not in our library10.1038/35087019
384.
Arsura M, Wu M, Sonenshein GE. TGF beta 1 inhibits NF-kappa B/Rel activity inducing apoptosis of B cells: transcriptional activation of I kappa B alpha. Immunity. 1996;5:31-40.
Not in our library10.1016/s1074-7613(00)80307-6
385.
Arsura M, FitzGerald MJ, Fausto N, Sonenshein GE. Nuclear factor-kappaB/Rel blocks transforming growth factor beta1-induced apoptosis of murine hepatocyte cell lines. Cell Growth Differ. 1997;8:1049-1059.
Not in our library
386.
Arsura M, et al. Transient activation of NF-kappaB through a TAK1/IKK kinase pathway by TGF-beta1 inhibits AP-1/SMAD signaling and apoptosis: implications in liver tumor formation. Oncogene. 2003;22:412-425.
Not in our library10.1038/sj.onc.1206132
387.
Yoo J, et al. Transforming growth factor-beta-induced apoptosis is mediated by Smad-dependent expression of GADD45b through p38 activation. J. Biol. Chem. 2003;278:43001-43007.
Not in our library10.1074/jbc.m307869200
388.
Schiffer M, Mundel P, Shaw AS, Böttinger EP. A novel role for the adaptor molecule CD2-associated protein in transforming growth factor-beta-induced apoptosis. J. Biol. Chem. 2004;279:37004-37012.
Not in our library10.1074/jbc.m403534200
389.
Conery AR, et al. Akt interacts directly with Smad3 to regulate the sensitivity to TGF-beta induced apoptosis. Nat. Cell Biol. 2004;6:366-372.
Not in our library10.1038/ncb1117
390.
Remy I, Montmarquette A, Michnick SW. PKB/Akt modulates TGF-beta signalling through a direct interaction with Smad3. Nat. Cell Biol. 2004;6:358-365.
Not in our library10.1038/ncb1113
391.
Valderrama-Carvajal H, et al. Activin/TGF-beta induce apoptosis through Smad-dependent expression of the lipid phosphatase SHIP. Nat. Cell Biol. 2002;4:963-969.
Not in our library10.1038/ncb885
392.
Bender H, Wang Z, Schuster N, Krieglstein K. TIEG1 facilitates transforming growth factor-beta-mediated apoptosis in the oligodendroglial cell line OLI-neu. J. Neurosci. Res. 2004;75:344-352.
Not in our library10.1002/jnr.10856
393.
Wang Z, Spittau B, Behrendt M, Peters B, Krieglstein K. Human TIEG2/KLF11 induces oligodendroglial cell death by downregulation of Bcl-XL expression. J. Neural Transm. (Vienna). 2007;114:867-875.
Not in our library10.1007/s00702-007-0635-6
394.
Chalaux E, et al. A zinc-finger transcription factor induced by TGF-beta promotes apoptotic cell death in epithelial Mv1Lu cells. FEBS Lett. 1999;457:478-482.
Not in our library10.1016/s0014-5793(99)01051-0
395.
Poulsen KT, et al. TGF beta 2 and TGF beta 3 are potent survival factors for midbrain dopaminergic neurons. Neuron. 1994;13:1245-1252.
Not in our library10.1016/0896-6273(94)90062-0
396.
Roussa E, Farkas LM, Krieglstein K. TGF-beta promotes survival on mesencephalic dopaminergic neurons in cooperation with Shh and FGF-8. Neurobiol. Dis. 2004;16:300-310.
Not in our library10.1016/j.nbd.2004.03.006
397.
Krieglstein K, Farkas L, Unsicker K. TGF-beta regulates the survival of ciliary ganglionic neurons synergistically with ciliary neurotrophic factor and neurotrophins. J. Neurobiol. 1998;37:563-572.
Not in our library10.1002/(sici)1097-4695(199812)37:4<563::aid-neu5>3.0.co;2-a
398.
Bye N, Zieba M, Wreford NG, Nichols NR. Resistance of the dentate gyrus to induced apoptosis during ageing is associated with increases in transforming growth factor-beta1 messenger RNA. Neuroscience. 2001;105:853-862.
Not in our library10.1016/s0306-4522(01)00236-6
399.
Shin I, Bakin AV, Rodeck U, Brunet A, Arteaga CL. Transforming growth factor beta enhances epithelial cell survival via Akt-dependent regulation of FKHRL1. Mol. Biol. Cell. 2001;12:3328-3339.
Not in our library10.1091/mbc.12.11.3328
400.
Lanvin O, et al. TGF-beta1 modulates Fas (APO-1/CD95)-mediated apoptosis of human pre-B cell lines. Eur. J. Immunol. 2003;33:1372-1381.
Not in our library10.1002/eji.200323761
401.
Huang Y, et al. Transforming growth factor-beta 1 suppresses serum deprivation-induced death of A549 cells through differential effects on c-Jun and JNK activities. J. Biol. Chem. 2000;275:18234-18242.
Not in our library10.1074/jbc.m909431199
402.
Saile B, Matthes N, El Armouche H, Neubauer K, Ramadori G. The bcl, NFkappaB and p53/p21WAF1 systems are involved in spontaneous apoptosis and in the anti-apoptotic effect of TGF-beta or TNF-alpha on activated hepatic stellate cells. Eur. J. Cell Biol. 2001;80:554-561.
Not in our library10.1078/0171-9335-00182
403.
Letterio JJ, Roberts AB. Regulation of immune responses by TGF-beta. Annu Rev. Immunol. 1998;16:137-161.
Not in our library10.1146/annurev.immunol.16.1.137
404.
Thomas DA, Massagué J. TGF-beta directly targets cytotoxic T cell functions during tumor evasion of immune surveillance. Cancer Cell. 2005;8:369-380.
Not in our library10.1016/j.ccr.2005.10.012
405.
Ahmadzadeh M, Rosenberg SA. TGF-beta 1 attenuates the acquisition and expression of effector function by tumor antigen-specific human memory CD8 T cells. J. Immunol. 2005;174:5215-5223.
Not in our library10.4049/jimmunol.174.9.5215
406.
Genestier L, Kasibhatla S, Brunner T, Green DR. Transforming growth factor beta1 inhibits Fas ligand expression and subsequent activation-induced cell death in T cells via downregulation of c-Myc. J. Exp. Med. 1999;189:231-239.
Not in our library10.1084/jem.189.2.231
407.
Chen CH, et al. Transforming growth factor beta blocks Tec kinase phosphorylation, Ca2+ influx, and NFATc translocation causing inhibition of T cell differentiation. J. Exp. Med. 2003;197:1689-1699.
Not in our library10.1084/jem.20021170
408.
Gorelik L, Constant S, Flavell RA. Mechanism of transforming growth factor beta-induced inhibition of T helper type 1 differentiation. J. Exp. Med. 2002;195:1499-1505.
Not in our library10.1084/jem.20012076
409.
Gorelik L, Fields PE, Flavell RA. Cutting edge: TGF-beta inhibits Th type 2 development through inhibition of GATA-3 expression. J. Immunol. 2000;165:4773-4777.
Not in our library10.4049/jimmunol.165.9.4773
410.
Heath VL, Murphy EE, Crain C, Tomlinson MG, O’Garra A. TGF-beta1 down-regulates Th2 development and results in decreased IL-4-induced STAT6 activation and GATA-3 expression. Eur. J. Immunol. 2000;30:2639-2649.
Not in our library10.1002/1521-4141(200009)30:9<2639::aid-immu2639>3.0.co;2-7
411.
Chen W, et al. Conversion of peripheral CD4+CD25- naive T cells to CD4+CD25+ regulatory T cells by TGF-beta induction of transcription factor Foxp3. J. Exp. Med. 2003;198:1875-1886.
Not in our library10.1084/jem.20030152
412.
Fantini MC, et al. Cutting edge: TGF-beta induces a regulatory phenotype in CD4+CD25- T cells through Foxp3 induction and down-regulation of Smad7. J. Immunol. 2004;172:5149-5153.
Not in our library10.4049/jimmunol.172.9.5149
413.
Zheng SG, Wang J, Wang P, Gray JD, Horwitz DA. IL-2 is essential for TGF-beta to convert naive CD4+CD25- cells to CD25+Foxp3+ regulatory T cells and for expansion of these cells. J. Immunol. 2007;178:2018-2027.
Not in our library10.4049/jimmunol.178.4.2018
414.
Davidson TS, DiPaolo RJ, Andersson J, Shevach EM. Cutting Edge: IL-2 is essential for TGF-beta-mediated induction of Foxp3+ T regulatory cells. J. Immunol. 2007;178:4022-4026.
Not in our library10.4049/jimmunol.178.7.4022
415.
Sawamukai N, et al. Cell-autonomous role of TGFβ and IL-2 receptors in CD4+ and CD8+ inducible regulatory T-cell generation during GVHD. Blood. 2012;119:5575-5583.
Not in our library10.1182/blood-2011-07-367987
416.
Rich S, Seelig M, Lee HM, Lin J. Transforming growth factor beta 1 costimulated growth and regulatory function of staphylococcal enterotoxin B-responsive CD8+ T cells. J. Immunol. 1995;155:609-618.
Not in our library10.4049/jimmunol.155.2.609
417.
Dardalhon V, et al. IL-4 inhibits TGF-beta-induced Foxp3+ T cells and, together with TGF-beta, generates IL-9+ IL-10+ Foxp3(-) effector T cells. Nat. Immunol. 2008;9:1347-1355.
Not in our library10.1038/ni.1677
418.
Chang HC, et al. The transcription factor PU.1 is required for the development of IL-9-producing T cells and allergic inflammation. Nat. Immunol. 2010;11:527-534.
Not in our library10.1038/ni.1867
419.
Goswami R, et al. STAT6-dependent regulation of Th9 development. J. Immunol. 2012;188:968-975.
Not in our library10.4049/jimmunol.1102840
420.
Veldhoen M, et al. Transforming growth factor-beta ‘reprograms’ the differentiation of T helper 2 cells and promotes an interleukin 9-producing subset. Nat. Immunol. 2008;9:1341-1346.
Not in our library10.1038/ni.1659
421.
Manel N, Unutmaz D, Littman DR. The differentiation of human T(H)-17 cells requires transforming growth factor-beta and induction of the nuclear receptor RORgammat. Nat. Immunol. 2008;9:641-649.
Not in our library10.1038/ni.1610
422.
Volpe E, et al. A critical function for transforming growth factor-beta, interleukin 23 and proinflammatory cytokines in driving and modulating human T(H)-17 responses. Nat. Immunol. 2008;9:650-657.
Not in our library10.1038/ni.1613
423.
Kehrl JH, Thevenin C, Rieckmann P, Fauci AS. Transforming growth factor-beta suppresses human B lymphocyte Ig production by inhibiting synthesis and the switch from the membrane form to the secreted form of Ig mRNA. J. Immunol. 1991;146:4016-4023.
Not in our library10.4049/jimmunol.146.11.4016
424.
Rehmann JA, LeBien TW. Transforming growth factor-beta regulates normal human pre-B cell differentiation. Int Immunol. 1994;6:315-322.
Not in our library10.1093/intimm/6.2.315
425.
Bouchard C, Fridman WH, Sautès C. Mechanism of inhibition of lipopolysaccharide-stimulated mouse B-cell responses by transforming growth factor-beta 1. Immunol. Lett. 1994;40:105-110.
Not in our library10.1016/0165-2478(94)90180-5
426.
Lebman DA, Lee FD, Coffman RL. Mechanism for transforming growth factor beta and IL-2 enhancement of IgA expression in lipopolysaccharide-stimulated B cell cultures. J. Immunol. 1990;144:952-959.
Not in our library10.4049/jimmunol.144.3.952
427.
Pro- and Anti- Effects of Immunoglobulin A- Producing B Cell in Tumors and Its Triggers · 2021
Not checked
428.
SARS-CoV-2 in severe COVID-19 induces a TGF-β-dominated chronic immune response that does not target itself · 2021
No notice
429.
Balkwill F, Montfort A, Capasso M. B regulatory cells in cancer. Trends Immunol. 2013;34:169-173.
Not in our library10.1016/j.it.2012.10.007
430.
Immunosuppressive Mechanisms of Regulatory B Cells · 2021
No notice
431.
Shang J, Zha H, Sun Y. Phenotypes, Functions, and Clinical Relevance of Regulatory B Cells in Cancer. Front Immunol. 2020;11:582657.
Not in our library10.3389/fimmu.2020.582657
432.
Wang L, Fu Y, Chu Y. Regulatory B Cells. Adv. Exp. Med. Biol. 2020;1254:87-103.
Not in our library10.1007/978-981-15-3532-1_8
433.
Smad3 promotes cancer progression by inhibiting E4BP4-mediated NK cell development · 2017
No notice
434.
Trotta R, et al. TGF-beta utilizes SMAD3 to inhibit CD16-mediated IFN-gamma production and antibody-dependent cellular cytotoxicity in human NK cells. J. Immunol. 2008;181:3784-3792.
Not in our library10.4049/jimmunol.181.6.3784
435.
Castriconi R, et al. Transforming growth factor beta 1 inhibits expression of NKp30 and NKG2D receptors: consequences for the NK-mediated killing of dendritic cells. Proc. Natl Acad. Sci. USA. 2003;100:4120-4125.
Not in our library10.1073/pnas.0730640100
436.
Fujii R, et al. An IL-15 superagonist/IL-15Rα fusion complex protects and rescues NK cell-cytotoxic function from TGF-β1-mediated immunosuppression. Cancer Immunol. Immunother. 2018;67:675-689.
Not in our library10.1007/s00262-018-2121-4
437.
Piskurich JF, Wang Y, Linhoff MW, White LC, Ting JP. Identification of distinct regions of 5’ flanking DNA that mediate constitutive, IFN-gamma, STAT1, and TGF-beta-regulated expression of the class II transactivator gene. J. Immunol. 1998;160:233-240.
Not in our library10.4049/jimmunol.160.1.233
438.
Nandan D, Reiner NE. TGF-beta attenuates the class II transactivator and reveals an accessory pathway of IFN-gamma action. J. Immunol. 1997;158:1095-1101.
Not in our library10.4049/jimmunol.158.3.1095
439.
Shaul ME, et al. Tumor-associated neutrophils display a distinct N1 profile following TGFβ modulation: A transcriptomics analysis of pro- vs. antitumor TANs. Oncoimmunology. 2016;5:e1232221.
Not in our library10.1080/2162402x.2016.1232221
440.
Geissmann F, et al. TGF-beta 1 prevents the noncognate maturation of human dendritic Langerhans cells. J. Immunol. 1999;162:4567-4575.
Not in our library10.4049/jimmunol.162.8.4567
441.
Takeuchi M, Alard P, Streilein JW. TGF-beta promotes immune deviation by altering accessory signals of antigen-presenting cells. J. Immunol. 1998;160:1589-1597.
Not in our library10.4049/jimmunol.160.4.1589
442.
Espevik T, et al. Inhibition of cytokine production by cyclosporin A and transforming growth factor beta. J. Exp. Med. 1987;166:571-576.
Not in our library10.1084/jem.166.2.571
443.
Bogdan C, Paik J, Vodovotz Y, Nathan C. Contrasting mechanisms for suppression of macrophage cytokine release by transforming growth factor-beta and interleukin-10. J. Biol. Chem. 1992;267:23301-23308.
Not in our library10.1016/s0021-9258(18)50091-0
444.
Nelson BJ, Ralph P, Green SJ, Nacy CA. Differential susceptibility of activated macrophage cytotoxic effector reactions to the suppressive effects of transforming growth factor-beta 1. J. Immunol. 1991;146:1849-1857.
Not in our library10.4049/jimmunol.146.6.1849
445.
Vodovotz Y, Bogdan C, Paik J, Xie QW, Nathan C. Mechanisms of suppression of macrophage nitric oxide release by transforming growth factor beta. J. Exp. Med. 1993;178:605-613.
Not in our library10.1084/jem.178.2.605
446.
Oswald IP, Gazzinelli RT, Sher A, James SL. IL-10 synergizes with IL-4 and transforming growth factor-beta to inhibit macrophage cytotoxic activity. J. Immunol. 1992;148:3578-3582.
Not in our library10.4049/jimmunol.148.11.3578
447.
Tridandapani S, et al. TGF-beta 1 suppresses [correction of supresses] myeloid Fc gamma receptor function by regulating the expression and function of the common gamma-subunit. J. Immunol. 2003;170:4572-4577.
Not in our library10.4049/jimmunol.170.9.4572
448.
Mantovani A, Sozzani S, Locati M, Allavena P, Sica A. Macrophage polarization: tumor-associated macrophages as a paradigm for polarized M2 mononuclear phagocytes. Trends Immunol. 2002;23:549-555.
Not in our library10.1016/s1471-4906(02)02302-5
449.
Fridlender ZG, et al. Polarization of tumor-associated neutrophil phenotype by TGF-beta: “N1” versus “N2” TAN. Cancer Cell. 2009;16:183-194.
Not in our library10.1016/j.ccr.2009.06.017
450.
Sagiv JY, et al. Phenotypic diversity and plasticity in circulating neutrophil subpopulations in cancer. Cell Rep. 2015;10:562-573.
Not in our library10.1016/j.celrep.2014.12.039
451.
Larsson J, et al. Abnormal angiogenesis but intact hematopoietic potential in TGF-beta type I receptor-deficient mice. Embo j. 2001;20:1663-1673.
Not in our library10.1093/emboj/20.7.1663
452.
Oshima M, Oshima H, Taketo MM. TGF-beta receptor type II deficiency results in defects of yolk sac hematopoiesis and vasculogenesis. Dev. Biol. 1996;179:297-302.
Not in our library10.1006/dbio.1996.0259
453.
Shull MM, et al. Targeted disruption of the mouse transforming growth factor-beta 1 gene results in multifocal inflammatory disease. Nature. 1992;359:693-699.
Not in our library10.1038/359693a0
454.
McLennan IS, Poussart Y, Koishi K. Development of skeletal muscles in transforming growth factor-beta 1 (TGF-beta1) null-mutant mice. Dev. Dyn. 2000;217:250-256.
Not in our library10.1002/(sici)1097-0177(200003)217:3<250::aid-dvdy3>3.0.co;2-f
455.
Sanford LP, et al. TGFbeta2 knockout mice have multiple developmental defects that are non-overlapping with other TGFbeta knockout phenotypes. Development. 1997;124:2659-2670.
Not in our library10.1242/dev.124.13.2659
456.
Foitzik K, Paus R, Doetschman T, Dotto GP. The TGF-beta2 isoform is both a required and sufficient inducer of murine hair follicle morphogenesis. Dev. Biol. 1999;212:278-289.
Not in our library10.1006/dbio.1999.9325
457.
Bartram U, et al. Double-outlet right ventricle and overriding tricuspid valve reflect disturbances of looping, myocardialization, endocardial cushion differentiation, and apoptosis in TGF-beta(2)-knockout mice. Circulation. 2001;103:2745-2752.
Not in our library10.1161/01.cir.103.22.2745
458.
Jiao K, et al. Tgfbeta signaling is required for atrioventricular cushion mesenchyme remodeling during in vivo cardiac development. Development. 2006;133:4585-4593.
Not in our library10.1242/dev.02597
459.
Kaartinen V, et al. Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction. Nat. Genet. 1995;11:415-421.
Not in our library10.1038/ng1295-415
460.
Proetzel G, et al. Transforming growth factor-beta 3 is required for secondary palate fusion. Nat. Genet. 1995;11:409-414.
Not in our library10.1038/ng1295-409
461.
Lindsay ME, et al. Loss-of-function mutations in TGFB2 cause a syndromic presentation of thoracic aortic aneurysm. Nat. Genet. 2012;44:922-927.
Not in our library10.1038/ng.2349
462.
Boileau C, et al. TGFB2 mutations cause familial thoracic aortic aneurysms and dissections associated with mild systemic features of Marfan syndrome. Nat. Genet. 2012;44:916-921.
Not in our library10.1038/ng.2348
463.
Al Maskari R, et al. A missense TGFB2 variant p.(Arg320Cys) causes a paradoxical and striking increase in aortic TGFB1/2 expression. Eur. J. Hum. Genet. 2016;25:157-160.
Not in our library10.1038/ejhg.2016.143
464.
Rienhoff HY, et al. A mutation in TGFB3 associated with a syndrome of low muscle mass, growth retardation, distal arthrogryposis and clinical features overlapping with Marfan and Loeys-Dietz syndrome. Am. J. Med Genet A. 2013;161a:2040-2046.
Not in our library10.1002/ajmg.a.36056
465.
Mutations in a TGF-β Ligand, TGFB3, Cause Syndromic Aortic Aneurysms and Dissections · 2015
No notice
466.
Kuechler A, et al. Exome sequencing identifies a novel heterozygous TGFB3 mutation in a disorder overlapping with Marfan and Loeys-Dietz syndrome. Mol. Cell Probes. 2015;29:330-334.
Not in our library10.1016/j.mcp.2015.07.003
467.
Loeys BL, et al. Aneurysm syndromes caused by mutations in the TGF-beta receptor. N. Engl. J. Med. 2006;355:788-798.
Not in our library10.1056/nejmoa055695
468.
Hara H, et al. Activation of TGF-β signaling in an aortic aneurysm in a patient with Loeys-Dietz syndrome caused by a novel loss-of-function variant of TGFBR1. Hum. Genome Var. 2019;6:6.
Not in our library10.1038/s41439-019-0038-x
469.
Tran-Fadulu V, et al. Analysis of multigenerational families with thoracic aortic aneurysms and dissections due to TGFBR1 or TGFBR2 mutations. J. Med Genet. 2009;46:607-613.
Not in our library10.1136/jmg.2008.062844
470.
Kirmani S, et al. Germline TGF-beta receptor mutations and skeletal fragility: a report on two patients with Loeys-Dietz syndrome. Am. J. Med Genet A. 2010;152a:1016-1019.
Not in our library10.1002/ajmg.a.33356
471.
Cousin MA, et al. Functional validation reveals the novel missense V419L variant in TGFBR2 associated with Loeys-Dietz syndrome (LDS) impairs canonical TGF-β signaling. Cold Spring Harb. Mol. Case Stud. 2017;3:a001727.
Not in our library10.1101/mcs.a001727
472.
Luo X, et al. Identification of a Pathogenic TGFBR2 Variant in a Patient With Loeys-Dietz Syndrome. Front Genet. 2020;11:479.
Not in our library10.3389/fgene.2020.00479
473.
Cannaerts E, et al. Novel pathogenic SMAD2 variants in five families with arterial aneurysm and dissection: further delineation of the phenotype. J. Med Genet. 2019;56:220-227.
Not in our library10.1136/jmedgenet-2018-105304
474.
Granadillo JL, et al. Variable cardiovascular phenotypes associated with SMAD2 pathogenic variants. Hum. Mutat. 2018;39:1875-1884.
Not in our library10.1002/humu.23627
475.
A mutation update on the LDS-associated genes TGFB2/3 and SMAD2/3 · 2018
No notice
476.
van de Laar IM, et al. Mutations in SMAD3 cause a syndromic form of aortic aneurysms and dissections with early-onset osteoarthritis. Nat. Genet. 2011;43:121-126.
Not in our library10.1038/ng.744
477.
van de Laar IM, et al. Phenotypic spectrum of the SMAD3-related aneurysms-osteoarthritis syndrome. J. Med Genet. 2012;49:47-57.
Not in our library10.1136/jmedgenet-2011-100382
478.
Aubart M, et al. Early-onset osteoarthritis, Charcot-Marie-Tooth like neuropathy, autoimmune features, multiple arterial aneurysms and dissections: an unrecognized and life threatening condition. PLoS One. 2014;9:e96387.
Not in our library10.1371/journal.pone.0096387
479.
Chung BH, et al. Hand and fibrillin-1 deposition abnormalities in Loeys-Dietz syndrome-expanding the clinical spectrum. Am. J. Med Genet A. 2014;164a:461-466.
Not in our library10.1002/ajmg.a.36246
480.
Barnett CP, Chitayat D, Bradley TJ, Wang Y, Hinek A. Dexamethasone normalizes aberrant elastic fiber production and collagen 1 secretion by Loeys-Dietz syndrome fibroblasts: a possible treatment? Eur. J. Hum. Genet. 2011;19:624-633.
Not in our library10.1038/ejhg.2010.259
481.
Loeys BL, et al. A syndrome of altered cardiovascular, craniofacial, neurocognitive and skeletal development caused by mutations in TGFBR1 or TGFBR2. Nat. Genet. 2005;37:275-281.
Not in our library10.1038/ng1511
482.
Maleszewski JJ, Miller DV, Lu J, Dietz HC, Halushka MK. Histopathologic findings in ascending aortas from individuals with Loeys-Dietz syndrome (LDS). Am. J. Surg. Pathol. 2009;33:194-201.
Not in our library10.1097/pas.0b013e31817f3661
483.
Sellheyer K, et al. Inhibition of skin development by overexpression of transforming growth factor beta 1 in the epidermis of transgenic mice. Proc. Natl Acad. Sci. USA. 1993;90:5237-5241.
Not in our library10.1073/pnas.90.11.5237
484.
Ito Y, et al. Overexpression of Smad2 reveals its concerted action with Smad4 in regulating TGF-beta-mediated epidermal homeostasis. Dev. Biol. 2001;236:181-194.
Not in our library10.1006/dbio.2001.0332
485.
Erlebacher A, Derynck R. Increased expression of TGF-beta 2 in osteoblasts results in an osteoporosis-like phenotype. J. Cell Biol. 1996;132:195-210.
Not in our library10.1083/jcb.132.1.195
486.
Flügel-Koch C, Ohlmann A, Piatigorsky J, Tamm ER. Disruption of anterior segment development by TGF-beta1 overexpression in the eyes of transgenic mice. Dev. Dyn. 2002;225:111-125.
Not in our library10.1002/dvdy.10144
487.
Vicencio AG, et al. Conditional overexpression of bioactive transforming growth factor-beta1 in neonatal mouse lung: a new model for bronchopulmonary dysplasia? Am. J. Respir. Cell Mol. Biol. 2004;31:650-656.
Not in our library10.1165/rcmb.2004-0092oc
488.
Zeng X, Gray M, Stahlman MT, Whitsett JA. TGF-beta1 perturbs vascular development and inhibits epithelial differentiation in fetal lung in vivo. Dev. Dyn. 2001;221:289-301.
Not in our library10.1002/dvdy.1140
489.
Jhappan C, et al. Targeting expression of a transforming growth factor beta 1 transgene to the pregnant mammary gland inhibits alveolar development and lactation. Embo j. 1993;12:1835-1845.
Not in our library10.1002/j.1460-2075.1993.tb05832.x
490.
Pierce DF, et al. Inhibition of mammary duct development but not alveolar outgrowth during pregnancy in transgenic mice expressing active TGF-beta 1. Genes Dev. 1993;7:2308-2317.
Not in our library10.1101/gad.7.12a.2308
491.
Buggiano V, et al. Impairment of mammary lobular development induced by expression of TGFbeta1 under the control of WAP promoter does not suppress tumorigenesis in MMTV-infected transgenic mice. Int J. Cancer. 2001;92:568-576.
Not in our library10.1002/ijc.1232
492.
Hall BE, et al. Conditional overexpression of TGF-beta1 disrupts mouse salivary gland development and function. Lab Invest. 2010;90:543-555.
Not in our library10.1038/labinvest.2010.5
493.
Wyss-Coray T, et al. Increased central nervous system production of extracellular matrix components and development of hydrocephalus in transgenic mice overexpressing transforming growth factor-beta 1. Am. J. Pathol. 1995;147:53-67.
Not in our library
494.
Saito T, et al. Domain-specific mutations of a transforming growth factor (TGF)-beta 1 latency-associated peptide cause Camurati-Engelmann disease because of the formation of a constitutively active form of TGF-beta 1. J. Biol. Chem. 2001;276:11469-11472.
Not in our library10.1074/jbc.c000859200
495.
Janssens K, ten Dijke P, Ralston SH, Bergmann C, Van Hul W. Transforming growth factor-beta 1 mutations in Camurati-Engelmann disease lead to increased signaling by altering either activation or secretion of the mutant protein. J. Biol. Chem. 2003;278:7718-7724.
Not in our library10.1074/jbc.m208857200
496.
Wallace, S. E. & Wilcox, W. R. In GeneReviews(®) (eds. M. P. Adam et al.) (University of Washington, Seattle Copyright © 1993-2023, University of Washington, Seattle. GeneReviews is a registered trademark of the University of Washington, Seattle. All rights reserved., 1993).
Not in our library
497.
Janssens K, et al. Mutations in the gene encoding the latency-associated peptide of TGF-beta 1 cause Camurati-Engelmann disease. Nat. Genet. 2000;26:273-275.
Not in our library10.1038/81563
498.
McGowan NW, et al. A mutation affecting the latency-associated peptide of TGFbeta1 in Camurati-Engelmann disease enhances osteoclast formation in vitro. J. Clin. Endocrinol. Metab. 2003;88:3321-3326.
Not in our library10.1210/jc.2002-020564
499.
Tang Y, et al. TGF-beta1-induced migration of bone mesenchymal stem cells couples bone resorption with formation. Nat. Med. 2009;15:757-765.
Not in our library10.1038/nm.1979
500.
Schmid P, et al. TGF-beta s and TGF-beta type II receptor in human epidermis: differential expression in acute and chronic skin wounds. J. Pathol. 1993;171:191-197.
Not in our library10.1002/path.1711710307
501.
Pastar I, et al. Attenuation of the transforming growth factor beta-signaling pathway in chronic venous ulcers. Mol. Med. 2010;16:92-101.
Not in our library10.2119/molmed.2009.00149
502.
Kim BC, et al. Fibroblasts from chronic wounds show altered TGF-beta-signaling and decreased TGF-beta Type II receptor expression. J. Cell Physiol. 2003;195:331-336.
Not in our library10.1002/jcp.10301
503.
Cowin AJ, et al. Effect of healing on the expression of transforming growth factor beta(s) and their receptors in chronic venous leg ulcers. J. Invest Dermatol. 2001;117:1282-1289.
Not in our library10.1046/j.0022-202x.2001.01501.x
504.
Bitar MS, Labbad ZN. Transforming growth factor-beta and insulin-like growth factor-I in relation to diabetes-induced impairment of wound healing. J. Surg. Res. 1996;61:113-119.
Not in our library10.1006/jsre.1996.0090
505.
Jude EB, Blakytny R, Bulmer J, Boulton AJ, Ferguson MW. Transforming growth factor-beta 1, 2, 3 and receptor type I and II in diabetic foot ulcers. Diabet. Med. 2002;19:440-447.
Not in our library10.1046/j.1464-5491.2002.00692.x
506.
Liu J, et al. Regenerative phenotype in mice with a point mutation in transforming growth factor beta type I receptor (TGFBR1). Proc. Natl Acad. Sci. USA. 2011;108:14560-14565.
Not in our library10.1073/pnas.1111056108
507.
Tredget EB, et al. Transforming growth factor-beta and its effect on reepithelialization of partial-thickness ear wounds in transgenic mice. Wound Repair Regen. 2005;13:61-67.
Not in our library10.1111/j.1067-1927.2005.130108.x
508.
Chan T, et al. Development, characterization, and wound healing of the keratin 14 promoted transforming growth factor-beta1 transgenic mouse. Wound Repair Regen. 2002;10:177-187.
Not in our library10.1046/j.1524-475x.2002.11101.x
509.
Brown RL, Ormsby I, Doetschman TC, Greenhalgh DG. Wound healing in the transforming growth factor-beta-deficient mouse. Wound Repair Regen. 1995;3:25-36.
Not in our library10.1046/j.1524-475x.1995.30108.x
510.
Crowe MJ, Doetschman T, Greenhalgh DG. Delayed wound healing in immunodeficient TGF-beta 1 knockout mice. J. Invest Dermatol. 2000;115:3-11.
Not in our library10.1046/j.1523-1747.2000.00010.x
511.
Amendt C, Mann A, Schirmacher P, Blessing M. Resistance of keratinocytes to TGFbeta-mediated growth restriction and apoptosis induction accelerates re-epithelialization in skin wounds. J. Cell Sci. 2002;115:2189-2198.
Not in our library10.1242/jcs.115.10.2189
512.
Owens P, Engelking E, Han G, Haeger SM, Wang XJ. Epidermal Smad4 deletion results in aberrant wound healing. Am. J. Pathol. 2010;176:122-133.
Not in our library10.2353/ajpath.2010.090081
513.
Ashcroft GS, et al. Mice lacking Smad3 show accelerated wound healing and an impaired local inflammatory response. Nat. Cell Biol. 1999;1:260-266.
Not in our library10.1038/12971
514.
Ghahary A, Shen YJ, Scott PG, Tredget EE. Immunolocalization of TGF-beta 1 in human hypertrophic scar and normal dermal tissues. Cytokine. 1995;7:184-190.
Not in our library10.1006/cyto.1995.1025
515.
Schmid P, Itin P, Cherry G, Bi C, Cox DA. Enhanced expression of transforming growth factor-beta type I and type II receptors in wound granulation tissue and hypertrophic scar. Am. J. Pathol. 1998;152:485-493.
Not in our library
516.
Wang R, et al. Hypertrophic scar tissues and fibroblasts produce more transforming growth factor-beta1 mRNA and protein than normal skin and cells. Wound Repair Regen. 2000;8:128-137.
Not in our library10.1046/j.1524-475x.2000.00128.x
517.
Chin GS, et al. Differential expression of transforming growth factor-beta receptors I and II and activation of Smad 3 in keloid fibroblasts. Plast. Reconstr. Surg. 2001;108:423-429.
Not in our library10.1097/00006534-200108000-00022
518.
Xia W, Phan TT, Lim IJ, Longaker MT, Yang GP. Complex epithelial-mesenchymal interactions modulate transforming growth factor-beta expression in keloid-derived cells. Wound Repair Regen. 2004;12:546-556.
Not in our library10.1111/j.1067-1927.2004.012507.x
519.
Younai S, et al. Modulation of collagen synthesis by transforming growth factor-beta in keloid and hypertrophic scar fibroblasts. Ann. Plast. Surg. 1994;33:148-151.
Not in our library10.1097/00000637-199408000-00005
520.
Chodon T, Sugihara T, Igawa HH, Funayama E, Furukawa H. Keloid-derived fibroblasts are refractory to Fas-mediated apoptosis and neutralization of autocrine transforming growth factor-beta1 can abrogate this resistance. Am. J. Pathol. 2000;157:1661-1669.
Not in our library10.1016/s0002-9440(10)64803-1
521.
Colwell AS, Phan TT, Kong W, Longaker MT, Lorenz PH. Hypertrophic scar fibroblasts have increased connective tissue growth factor expression after transforming growth factor-beta stimulation. Plast. Reconstr. Surg. 2005;116:1387-1390.
Not in our library10.1097/01.prs.0000182343.99694.28
522.
Bettinger DA, Yager DR, Diegelmann RF, Cohen IK. The effect of TGF-beta on keloid fibroblast proliferation and collagen synthesis. Plast. Reconstr. Surg. 1996;98:827-833.
Not in our library10.1097/00006534-199610000-00012
523.
Fujiwara M, Muragaki Y, Ooshima A. Upregulation of transforming growth factor-beta1 and vascular endothelial growth factor in cultured keloid fibroblasts: relevance to angiogenic activity. Arch. Dermatol Res. 2005;297:161-169.
Not in our library10.1007/s00403-005-0596-2
524.
Hoyt DG, Lazo JS. Alterations in pulmonary mRNA encoding procollagens, fibronectin and transforming growth factor-beta precede bleomycin-induced pulmonary fibrosis in mice. J. Pharm. Exp. Ther. 1988;246:765-771.
Not in our library
525.
Westergren-Thorsson G, et al. Altered expression of small proteoglycans, collagen, and transforming growth factor-beta 1 in developing bleomycin-induced pulmonary fibrosis in rats. J. Clin. Invest. 1993;92:632-637.
Not in our library10.1172/jci116631
526.
Broekelmann TJ, Limper AH, Colby TV, McDonald JA. Transforming growth factor beta 1 is present at sites of extracellular matrix gene expression in human pulmonary fibrosis. Proc. Natl Acad. Sci. USA. 1991;88:6642-6646.
Not in our library10.1073/pnas.88.15.6642
527.
Coker RK, et al. Localisation of transforming growth factor beta1 and beta3 mRNA transcripts in normal and fibrotic human lung. Thorax. 2001;56:549-556.
Not in our library10.1136/thorax.56.7.549
528.
Corrin B, et al. Immunohistochemical localization of transforming growth factor-beta 1 in the lungs of patients with systemic sclerosis, cryptogenic fibrosing alveolitis and other lung disorders. Histopathology. 1994;24:145-150.
Not in our library10.1111/j.1365-2559.1994.tb01293.x
529.
Utsugi M, et al. C-Jun-NH2-terminal kinase mediates expression of connective tissue growth factor induced by transforming growth factor-beta1 in human lung fibroblasts. Am. J. Respir. Cell Mol. Biol. 2003;28:754-761.
Not in our library10.1165/rcmb.4892
530.
Togami K, Yamaguchi K, Chono S, Tada H. Evaluation of permeability alteration and epithelial-mesenchymal transition induced by transforming growth factor-β(1) in A549, NCI-H441, and Calu-3 cells: Development of an in vitro model of respiratory epithelial cells in idiopathic pulmonary fibrosis. J. Pharm. Toxicol. Methods. 2017;86:19-27.
Not in our library10.1016/j.vascn.2017.02.023
531.
Roy SG, Nozaki Y, Phan SH. Regulation of alpha-smooth muscle actin gene expression in myofibroblast differentiation from rat lung fibroblasts. Int J. Biochem Cell Biol. 2001;33:723-734.
Not in our library10.1016/s1357-2725(01)00041-3
532.
Kim KK, et al. Alveolar epithelial cell mesenchymal transition develops in vivo during pulmonary fibrosis and is regulated by the extracellular matrix. Proc. Natl Acad. Sci. USA. 2006;103:13180-13185.
Not in our library10.1073/pnas.0605669103
533.
Lee CG, et al. Early growth response gene 1-mediated apoptosis is essential for transforming growth factor beta1-induced pulmonary fibrosis. J. Exp. Med. 2004;200:377-389.
Not in our library10.1084/jem.20040104
534.
Sime PJ, Xing Z, Graham FL, Csaky KG, Gauldie J. Adenovector-mediated gene transfer of active transforming growth factor-beta1 induces prolonged severe fibrosis in rat lung. J. Clin. Invest. 1997;100:768-776.
Not in our library10.1172/jci119590
535.
D’Alessandro-Gabazza CN, et al. Development and preclinical efficacy of novel transforming growth factor-β1 short interfering RNAs for pulmonary fibrosis. Am. J. Respir. Cell Mol. Biol. 2012;46:397-406.
Not in our library10.1165/rcmb.2011-0158oc
536.
Li M, et al. Epithelium-specific deletion of TGF-β receptor type II protects mice from bleomycin-induced pulmonary fibrosis. J. Clin. Invest. 2011;121:277-287.
Not in our library10.1172/jci42090
537.
Xu L, et al. Transforming growth factor β3 attenuates the development of radiation-induced pulmonary fibrosis in mice by decreasing fibrocyte recruitment and regulating IFN-γ/IL-4 balance. Immunol. Lett. 2014;162:27-33.
Not in our library10.1016/j.imlet.2014.06.010
538.
Zhao J, et al. Smad3 deficiency attenuates bleomycin-induced pulmonary fibrosis in mice. Am. J. Physiol. Lung Cell Mol. Physiol. 2002;282:L585-L593.
Not in our library10.1152/ajplung.00151.2001
539.
Nakao A, et al. Transient gene transfer and expression of Smad7 prevents bleomycin-induced lung fibrosis in mice. J. Clin. Invest. 1999;104:5-11.
Not in our library10.1172/jci6094
540.
Yamamoto T, et al. Expression of transforming growth factor-beta isoforms in human glomerular diseases. Kidney Int. 1996;49:461-469.
Not in our library10.1038/ki.1996.65
541.
Shihab FS, et al. Transforming growth factor-beta and matrix protein expression in acute and chronic rejection of human renal allografts. J. Am. Soc. Nephrol. 1995;6:286-294.
Not in our library10.1681/asn.v62286
542.
Yoshioka K, et al. Transforming growth factor-beta protein and mRNA in glomeruli in normal and diseased human kidneys. Lab Invest. 1993;68:154-163.
Not in our library
543.
Iwano M, et al. Intraglomerular expression of transforming growth factor-beta 1 (TGF-beta 1) mRNA in patients with glomerulonephritis: quantitative analysis by competitive polymerase chain reaction. Clin. Exp. Immunol. 1994;97:309-314.
Not in our library10.1111/j.1365-2249.1994.tb06086.x
544.
Grande J, Melder D, Zinsmeister A, Killen P. Transforming growth factor-beta 1 induces collagen IV gene expression in NIH-3T3 cells. Lab Invest. 1993;69:387-395.
Not in our library
545.
Nakamura T, Miller D, Ruoslahti E, Border WA. Production of extracellular matrix by glomerular epithelial cells is regulated by transforming growth factor-beta 1. Kidney Int. 1992;41:1213-1221.
Not in our library10.1038/ki.1992.183
546.
Kagami S, et al. Transforming growth factor-beta (TGF-beta) stimulates the expression of beta1 integrins and adhesion by rat mesangial cells. Exp. Cell Res. 1996;229:1-6.
Not in our library10.1006/excr.1996.0336
547.
Okuda S, Languino LR, Ruoslahti E, Border WA. Elevated expression of transforming growth factor-beta and proteoglycan production in experimental glomerulonephritis. Possible role in expansion of the mesangial extracellular matrix. J. Clin. Invest. 1990;86:453-462.
Not in our library10.1172/jci114731
548.
Marti HP, Lee L, Kashgarian M, Lovett DH. Transforming growth factor-beta 1 stimulates glomerular mesangial cell synthesis of the 72-kd type IV collagenase. Am. J. Pathol. 1994;144:82-94.
Not in our library
549.
Zeisberg M, Maeshima Y, Mosterman B, Kalluri R. Renal fibrosis. Extracellular matrix microenvironment regulates migratory behavior of activated tubular epithelial cells. Am. J. Pathol. 2002;160:2001-2008.
Not in our library10.1016/s0002-9440(10)61150-9
550.
Yang J, Liu Y. Dissection of key events in tubular epithelial to myofibroblast transition and its implications in renal interstitial fibrosis. Am. J. Pathol. 2001;159:1465-1475.
Not in our library10.1016/s0002-9440(10)62533-3
551.
Kopp JB, et al. Transgenic mice with increased plasma levels of TGF-beta 1 develop progressive renal disease. Lab Invest. 1996;74:991-1003.
Not in our library
552.
Mozes MM, Böttinger EP, Jacot TA, Kopp JB. Renal expression of fibrotic matrix proteins and of transforming growth factor-beta (TGF-beta) isoforms in TGF-beta transgenic mice. J. Am. Soc. Nephrol. 1999;10:271-280.
Not in our library10.1681/asn.v102271
553.
Nagy P, Schaff Z, Lapis K. Immunohistochemical detection of transforming growth factor-beta 1 in fibrotic liver diseases. Hepatology. 1991;14:269-273.
Not in our library10.1002/hep.1840140211
554.
Castilla A, Prieto J, Fausto N. Transforming growth factors beta 1 and alpha in chronic liver disease. Effects of interferon alfa therapy. N. Engl. J. Med. 1991;324:933-940.
Not in our library10.1056/nejm199104043241401
555.
Czaja MJ, et al. In vitro and in vivo association of transforming growth factor-beta 1 with hepatic fibrosis. J. Cell Biol. 1989;108:2477-2482.
Not in our library10.1083/jcb.108.6.2477
556.
Sakaguchi E, et al. Th1 down-regulation at the single-lymphocyte level in HCV-related liver cirrhosis and the effect of TGF-beta on Th1 response: possible implications for the development of hepatoma. Hepatol. Res. 2002;24:282.
Not in our library10.1016/s1386-6346(02)00090-6
557.
Ueberham E, et al. Conditional tetracycline-regulated expression of TGF-beta1 in liver of transgenic mice leads to reversible intermediary fibrosis. Hepatology. 2003;37:1067-1078.
Not in our library10.1053/jhep.2003.50196
558.
Sanderson N, et al. Hepatic expression of mature transforming growth factor beta 1 in transgenic mice results in multiple tissue lesions. Proc. Natl Acad. Sci. USA. 1995;92:2572-2576.
Not in our library10.1073/pnas.92.7.2572
559.
El-Youssef M, Mu Y, Huang L, Stellmach V, Crawford SE. Increased expression of transforming growth factor-beta1 and thrombospondin-1 in congenital hepatic fibrosis: possible role of the hepatic stellate cell. J. Pediatr. Gastroenterol. Nutr. 1999;28:386-392.
Not in our library10.1097/00005176-199904000-00008
560.
Teekakirikul P, et al. Cardiac fibrosis in mice with hypertrophic cardiomyopathy is mediated by non-myocyte proliferation and requires Tgf-β. J. Clin. Invest. 2010;120:3520-3529.
Not in our library10.1172/jci42028
561.
Kania G, et al. Heart-infiltrating prominin-1+/CD133+ progenitor cells represent the cellular source of transforming growth factor beta-mediated cardiac fibrosis in experimental autoimmune myocarditis. Circ. Res. 2009;105:462-470.
Not in our library10.1161/circresaha.109.196287
562.
Zhao W, Zhao T, Chen Y, Ahokas RA, Sun Y. Oxidative stress mediates cardiac fibrosis by enhancing transforming growth factor-beta1 in hypertensive rats. Mol. Cell Biochem. 2008;317:43-50.
Not in our library10.1007/s11010-008-9803-8
563.
Lijnen PJ, Petrov VV, Fagard RH. Induction of cardiac fibrosis by transforming growth factor-beta(1). Mol. Genet Metab. 2000;71:418-435.
Not in our library10.1006/mgme.2000.3032
564.
Kuwahara F, et al. Transforming growth factor-beta function blocking prevents myocardial fibrosis and diastolic dysfunction in pressure-overloaded rats. Circulation. 2002;106:130-135.
Not in our library10.1161/01.cir.0000020689.12472.e0
565.
Sakata Y, et al. Transforming growth factor-beta receptor antagonism attenuates myocardial fibrosis in mice with cardiac-restricted overexpression of tumor necrosis factor. Basic Res Cardiol. 2008;103:60-68.
Not in our library10.1007/s00395-007-0689-5
566.
Hagler MA, et al. TGF-β signalling and reactive oxygen species drive fibrosis and matrix remodelling in myxomatous mitral valves. Cardiovasc Res. 2013;99:175-184.
Not in our library10.1093/cvr/cvt083
567.
Spriewald BM, Ensminger SM, Billing JS, Morris PJ, Wood KJ. Increased expression of transforming growth factor-beta and eosinophil infiltration is associated with the development of transplant arteriosclerosis in long-term surviving cardiac allografts. Transplantation. 2003;76:1105-1111.
Not in our library10.1097/01.tp.0000076467.83192.42
568.
Bobik A, et al. Distinct patterns of transforming growth factor-beta isoform and receptor expression in human atherosclerotic lesions. Colocalization implicates TGF-beta in fibrofatty lesion development. Circulation. 1999;99:2883-2891.
Not in our library10.1161/01.cir.99.22.2883
569.
Li J, et al. Endothelial Cell Apoptosis Induces TGF-β Signaling-Dependent Host Endothelial-Mesenchymal Transition to Promote Transplant Arteriosclerosis. Am. J. Transpl. 2015;15:3095-3111.
Not in our library10.1111/ajt.13406
570.
Chang SH, et al. Transforming growth factor-β-mediated CD44/STAT3 signaling contributes to the development of atrial fibrosis and fibrillation. Basic Res Cardiol. 2017;112:58.
Not in our library10.1007/s00395-017-0647-9
571.
Seeland U, et al. Myocardial fibrosis in transforming growth factor-beta(1) (TGF-beta(1)) transgenic mice is associated with inhibition of interstitial collagenase. Eur. J. Clin. Invest. 2002;32:295-303.
Not in our library10.1046/j.1365-2362.2002.00985.x
572.
Cucoranu I, et al. NAD(P)H oxidase 4 mediates transforming growth factor-beta1-induced differentiation of cardiac fibroblasts into myofibroblasts. Circ. Res. 2005;97:900-907.
Not in our library10.1161/01.res.0000187457.24338.3d
573.
Blyszczuk P, et al. Transforming growth factor-β-dependent Wnt secretion controls myofibroblast formation and myocardial fibrosis progression in experimental autoimmune myocarditis. Eur. Heart J. 2017;38:1413-1425.
Not in our library10.1093/eurheartj/ehw116
574.
Song S, et al. Foxm1 is a critical driver of TGF-β-induced EndMT in endothelial cells through Smad2/3 and binds to the Snail promoter. J. Cell Physiol. 2019;234:9052-9064.
Not in our library10.1002/jcp.27583
575.
Zeisberg EM, et al. Endothelial-to-mesenchymal transition contributes to cardiac fibrosis. Nat. Med. 2007;13:952-961.
Not in our library10.1038/nm1613
576.
Varga J, Rosenbloom J, Jimenez SA. Transforming growth factor beta (TGF beta) causes a persistent increase in steady-state amounts of type I and type III collagen and fibronectin mRNAs in normal human dermal fibroblasts. Biochem J. 1987;247:597-604.
Not in our library10.1042/bj2470597
577.
Goto K, et al. Development and progression of immobilization-induced skin fibrosis through overexpression of transforming growth factor-ß1 and hypoxic conditions in a rat knee joint contracture model. Connect Tissue Res. 2017;58:586-596.
Not in our library10.1080/03008207.2017.1284823
578.
Zhang X, et al. Roles of TGF-β/Smad signaling pathway in pathogenesis and development of gluteal muscle contracture. Connect Tissue Res. 2015;56:9-17.
Not in our library10.3109/03008207.2014.964400
579.
Yoshikawa H, et al. Role of TGF-beta1 in the development of pancreatic fibrosis in Otsuka Long-Evans Tokushima Fatty rats. Am. J. Physiol. Gastrointest. Liver Physiol. 2002;282:G549-G558.
Not in our library10.1152/ajpgi.00323.2001
580.
Vogelmann R, Ruf D, Wagner M, Adler G, Menke A. Effects of fibrogenic mediators on the development of pancreatic fibrosis in a TGF-beta1 transgenic mouse model. Am. J. Physiol. Gastrointest. Liver Physiol. 2001;280:G164-G172.
Not in our library10.1152/ajpgi.2001.280.1.g164
581.
Van Laethem JL, Robberecht P, Résibois A, Devière J. Transforming growth factor beta promotes development of fibrosis after repeated courses of acute pancreatitis in mice. Gastroenterology. 1996;110:576-582.
Not in our library10.1053/gast.1996.v110.pm8566606
582.
Shek FW, et al. Expression of transforming growth factor-beta 1 by pancreatic stellate cells and its implications for matrix secretion and turnover in chronic pancreatitis. Am. J. Pathol. 2002;160:1787-1798.
Not in our library10.1016/s0002-9440(10)61125-x
583.
Yao JC, et al. TGF-β signaling in myeloproliferative neoplasms contributes to myelofibrosis without disrupting the hematopoietic niche. J. Clin. Invest. 2022;132:e154092.
Not in our library10.1172/jci154092
584.
Ponce CC, de Lourdes FCM, Ihara SS, Silva MR. The relationship of the active and latent forms of TGF-β1 with marrow fibrosis in essential thrombocythemia and primary myelofibrosis. Med Oncol. 2012;29:2337-2344.
Not in our library10.1007/s12032-011-0144-1
585.
Shen M, Liu X, Zhang H, Guo SW. Transforming growth factor β1 signaling coincides with epithelial-mesenchymal transition and fibroblast-to-myofibroblast transdifferentiation in the development of adenomyosis in mice. Hum. Reprod. 2016;31:355-369.
Not in our library10.1093/humrep/dev314
586.
Koski H, Konttinen YT, Gu XH, Hietanen J, Malmström M. Transforming growth factor beta 2 in labial salivary glands in Sjögren’s syndrome. Ann. Rheum. Dis. 1995;54:744-747.
Not in our library10.1136/ard.54.9.744
587.
di Mola FF, et al. Transforming growth factor-betas and their signaling receptors are coexpressed in Crohn’s disease. Ann. Surg. 1999;229:67-75.
Not in our library10.1097/00000658-199901000-00009
588.
Gómez-Bernal F, et al. Transforming growth factor beta 1 is associated with subclinical carotid atherosclerosis in patients with systemic lupus erythematosus. Arthritis Res Ther. 2023;25:64.
Not in our library10.1186/s13075-023-03046-2
589.
Liu B, et al. Aberrant TGF-β1 signaling contributes to the development of primary biliary cirrhosis in murine model. World J. Gastroenterol. 2013;19:5828-5836.
Not in our library10.3748/wjg.v19.i35.5828
590.
Chida T, et al. Critical role of CREBH-mediated induction of transforming growth factor β2 by hepatitis C virus infection in fibrogenic responses in hepatic stellate cells. Hepatology. 2017;66:1430-1443.
Not in our library10.1002/hep.29319
591.
Mehta AK, Doherty T, Broide D, Croft M. Tumor necrosis factor family member LIGHT acts with IL-1β and TGF-β to promote airway remodeling during rhinovirus infection. Allergy. 2018;73:1415-1424.
Not in our library10.1111/all.13390
592.
Ahodantin J, et al. Type I interferons and TGF-β cooperate to induce liver fibrosis during HIV-1 infection under antiretroviral therapy. JCI Insight. 2022;7:e152738.
Not in our library10.1172/jci.insight.152738
593.
Huang L, et al. CD8+ T cells with high TGF‑β1 expression cause lymph node fibrosis following HIV infection. Mol. Med Rep. 2018;18:77-86.
Not in our library10.3892/mmr.2018.8964
594.
Kulkarni AB, et al. Transforming growth factor beta 1 null mutation in mice causes excessive inflammatory response and early death. Proc. Natl Acad. Sci. USA. 1993;90:770-774.
Not in our library10.1073/pnas.90.2.770
595.
Kulkarni AB, et al. Transforming growth factor-beta 1 null mice. An animal model for inflammatory disorders. Am. J. Pathol. 1995;146:264-275.
Not in our library
596.
Dang H, et al. SLE-like autoantibodies and Sjögren’s syndrome-like lymphoproliferation in TGF-beta knockout mice. J. Immunol. 1995;155:3205-3212.
Not in our library10.4049/jimmunol.155.6.3205
597.
Laouar Y, et al. TGF-beta signaling in dendritic cells is a prerequisite for the control of autoimmune encephalomyelitis. Proc. Natl Acad. Sci. USA. 2008;105:10865-10870.
Not in our library10.1073/pnas.0805058105
598.
Hahm KB, et al. Loss of transforming growth factor beta signalling in the intestine contributes to tissue injury in inflammatory bowel disease. Gut. 2001;49:190-198.
Not in our library10.1136/gut.49.2.190
599.
Schramm C, et al. Impairment of TGF-beta signaling in T cells increases susceptibility to experimental autoimmune hepatitis in mice. Am. J. Physiol. Gastrointest. Liver Physiol. 2003;284:G525-G535.
Not in our library10.1152/ajpgi.00286.2002
600.
Ramalingam R, et al. Dendritic cell-specific disruption of TGF-beta receptor II leads to altered regulatory T cell phenotype and spontaneous multiorgan autoimmunity. J. Immunol. 2012;189:3878-3893.
Not in our library10.4049/jimmunol.1201029
601.
Ihara S, et al. TGF-beta Signaling in Dendritic Cells Governs Colonic Homeostasis by Controlling Epithelial Differentiation and the Luminal Microbiota. J. Immunol. 2016;196:4603-4613.
Not in our library10.4049/jimmunol.1502548
602.
Gorelik L, Flavell RA. Abrogation of TGFbeta signaling in T cells leads to spontaneous T cell differentiation and autoimmune disease. Immunity. 2000;12:171-181.
Not in our library10.1016/s1074-7613(00)80170-3
603.
Turner JA, et al. Regulatory T Cell-Derived TGF-β1 Controls Multiple Checkpoints Governing Allergy and Autoimmunity. Immunity. 2020;53:1202-1214.e1206.
Not in our library10.1016/j.immuni.2020.10.002
604.
Hahm KB, et al. Loss of TGF-beta signaling contributes to autoimmune pancreatitis. J. Clin. Invest. 2000;105:1057-1065.
Not in our library10.1172/jci8337
605.
Gómez-Bernal F, et al. Serum Levels of Transforming Growth Factor Beta 1 in Systemic Lupus Erythematosus Patients. Biomolecules. 2022;13:73.
Not in our library10.3390/biom13010073
606.
Manolova I, Gerenova J, Ivanova M. Serum levels of transforming growth factor-β1 (TGF-β1) in patients with systemic lupus erythematosus and Hashimoto’s thyroiditis. Eur. Cytokine Netw. 2013;24:69-74.
Not in our library10.1684/ecn.2013.0331
607.
Becker-Merok A, Eilertsen G, Nossent JC. Levels of transforming growth factor-beta are low in systemic lupus erythematosus patients with active disease. J. Rheumatol. 2010;37:2039-2045.
Not in our library10.3899/jrheum.100180
608.
Lomelí-Nieto JA, et al. Transforming growth factor beta isoforms and TGF-βR1 and TGF-βR2 expression in systemic sclerosis patients. Clin. Exp. Med. 2023;23:471-481.
Not in our library10.1007/s10238-022-00841-0
609.
Dziadzio M, Smith RE, Abraham DJ, Black CM, Denton CP. Circulating levels of active transforming growth factor beta1 are reduced in diffuse cutaneous systemic sclerosis and correlate inversely with the modified Rodnan skin score. Rheumatol. (Oxf.). 2005;44:1518-1524.
Not in our library10.1093/rheumatology/kei088
610.
Kulozik M, Hogg A, Lankat-Buttgereit B, Krieg T. Co-localization of transforming growth factor beta 2 with alpha 1(I) procollagen mRNA in tissue sections of patients with systemic sclerosis. J. Clin. Invest. 1990;86:917-922.
Not in our library10.1172/jci114793
611.
Kubo M, Ihn H, Yamane K, Tamaki K. Upregulated expression of transforming growth factor-beta receptors in dermal fibroblasts of skin sections from patients with systemic sclerosis. J. Rheumatol. 2002;29:2558-2564.
Not in our library
612.
Taketazu F, et al. Enhanced expression of transforming growth factor-beta s and transforming growth factor-beta type II receptor in the synovial tissues of patients with rheumatoid arthritis. Lab Invest. 1994;70:620-630.
Not in our library
613.
Szekanecz Z, et al. Increased synovial expression of transforming growth factor (TGF)-beta receptor endoglin and TGF-beta 1 in rheumatoid arthritis: possible interactions in the pathogenesis of the disease. Clin. Immunol. Immunopathol. 1995;76:187-194.
Not in our library10.1006/clin.1995.1114
614.
Mieliauskaite D, Venalis P, Dumalakiene I, Venalis A, Distler J. Relationship between serum levels of TGF-beta1 and clinical parameters in patients with rheumatoid arthritis and Sjögren’s syndrome secondary to rheumatoid arthritis. Autoimmunity. 2009;42:356-358.
Not in our library10.1080/08916930902831977
615.
He J, et al. Clinical significance of the expression levels of serum transforming growth factor-β and CXC type chemokine ligand 13 in primary Sjogren’s syndrome patients. Clin. Rheumatol. 2023;42:3283-3288.
Not in our library10.1007/s10067-023-06783-6
616.
Ogawa N, et al. Analysis of transforming growth factor beta and other cytokines in autoimmune exocrinopathy (Sjögren’s syndrome). J. Interferon Cytokine Res. 1995;15:759-767.
Not in our library10.1089/jir.1995.15.759
617.
Kader HA, et al. Protein microarray analysis of disease activity in pediatric inflammatory bowel disease demonstrates elevated serum PLGF, IL-7, TGF-beta1, and IL-12p40 levels in Crohn’s disease and ulcerative colitis patients in remission versus active disease. Am. J. Gastroenterol. 2005;100:414-423.
Not in our library10.1111/j.1572-0241.2005.40819.x
618.
Kanazawa S, et al. VEGF, basic-FGF, and TGF-beta in Crohn’s disease and ulcerative colitis: a novel mechanism of chronic intestinal inflammation. Am. J. Gastroenterol. 2001;96:822-828.
Not in our library10.1111/j.1572-0241.2001.03527.x
619.
Babyatsky MW, Rossiter G, Podolsky DK. Expression of transforming growth factors alpha and beta in colonic mucosa in inflammatory bowel disease. Gastroenterology. 1996;110:975-984.
Not in our library10.1053/gast.1996.v110.pm8613031
620.
Stadnicki A, Machnik G, Klimacka-Nawrot E, Wolanska-Karut A, Labuzek K. Transforming growth factor-beta1 and its receptors in patients with ulcerative colitis. Int Immunopharmacol. 2009;9:761-766.
Not in our library10.1016/j.intimp.2009.02.014
621.
Wiercińska-Drapało A, Flisiak R, Prokopowicz D. Effect of ulcerative colitis activity on plasma concentration of transforming growth factor beta1. Cytokine. 2001;14:343-346.
Not in our library10.1006/cyto.2001.0901
622.
Chowdhury A, Fukuda R, Fukumoto S. Growth factor mRNA expression in normal colorectal mucosa and in uninvolved mucosa from ulcerative colitis patients. J. Gastroenterol. 1996;31:353-360.
Not in our library10.1007/bf02355024
623.
Bayer EM, et al. Transforming growth factor-beta1 in autoimmune hepatitis: correlation of liver tissue expression and serum levels with disease activity. J. Hepatol. 1998;28:803-811.
Not in our library10.1016/s0168-8278(98)80230-4
624.
Sakaguchi K, et al. Serum level of transforming growth factor-beta1 (TGF-beta1) and the expression of TGF-beta receptor type II in peripheral blood mononuclear cells in patients with autoimmune hepatitis. Hepatogastroenterology. 2004;51:1780-1783.
Not in our library
625.
Vural P, Degirmencioglu S, Erden S, Gelincik A. The relationship between transforming growth factor-beta1, vascular endothelial growth factor, nitric oxide and Hashimoto’s thyroiditis. Int Immunopharmacol. 2009;9:212-215.
Not in our library10.1016/j.intimp.2008.11.003
626.
Akinci B, et al. Hashimoto’s thyroiditis, but not treatment of hypothyroidism, is associated with altered TGF-beta1 levels. Arch. Med Res. 2008;39:397-401.
Not in our library10.1016/j.arcmed.2007.12.001
627.
Ohtsuka K, Gray JD, Stimmler MM, Toro B, Horwitz DA. Decreased production of TGF-beta by lymphocytes from patients with systemic lupus erythematosus. J. Immunol. 1998;160:2539-2545.
Not in our library10.4049/jimmunol.160.5.2539
628.
Del Zotto B, et al. TGF-beta1 production in inflammatory bowel disease: differing production patterns in Crohn’s disease and ulcerative colitis. Clin. Exp. Immunol. 2003;134:120-126.
Not in our library10.1046/j.1365-2249.2003.02250.x
629.
Ohtsuka K, Gray JD, Stimmler MM, Horwitz DA. The relationship between defects in lymphocyte production of transforming growth factor-beta1 in systemic lupus erythematosus and disease activity or severity. Lupus. 1999;8:90-94.
Not in our library10.1191/096120399678847489
630.
Kotlarz D, et al. Human TGF-β1 deficiency causes severe inflammatory bowel disease and encephalopathy. Nat. Genet. 2018;50:344-348.
Not in our library10.1038/s41588-018-0063-6
631.
Bai B, et al. Molecular mechanism of the TGF‑β/Smad7 signaling pathway in ulcerative colitis. Mol. Med Rep. 2022;25:116.
Not in our library10.3892/mmr.2022.12632
632.
Elbeldi-Ferchiou A, et al. Resistance to exogenous TGF-β effects in patients with systemic lupus erythematosus. J. Clin. Immunol. 2011;31:574-583.
Not in our library10.1007/s10875-011-9531-9
633.
Naviglio S, et al. Severe inflammatory bowel disease associated with congenital alteration of transforming growth factor beta signaling. J. Crohns Colitis. 2014;8:770-774.
Not in our library10.1016/j.crohns.2014.01.013
634.
Peres RS, et al. TGF-β signalling defect is linked to low CD39 expression on regulatory T cells and methotrexate resistance in rheumatoid arthritis. J. Autoimmun. 2018;90:49-58.
Not in our library10.1016/j.jaut.2018.01.004
635.
Rekik R, et al. Impaired TGF-β signaling in patients with active systemic lupus erythematosus is associated with an overexpression of IL-22. Cytokine. 2018;108:182-189.
Not in our library10.1016/j.cyto.2018.04.011
636.
Yalcin AD, Bisgin A, Gorczynski RM. IL-8, IL-10, TGF-β, and GCSF levels were increased in severe persistent allergic asthma patients with the anti-IgE treatment. Mediators Inflamm. 2012;2012:720976.
Not in our library10.1155/2012/720976
637.
Yamaguchi M, et al. Sputum levels of transforming growth factor-beta1 in asthma: relation to clinical and computed tomography findings. J. Investig. Allergol. Clin. Immunol. 2008;18:202-206.
Not in our library
638.
Manuyakorn W, et al. Serum TGF-beta1 in atopic asthma. Asian Pac. J. Allergy Immunol. 2008;26:185-189.
Not in our library
639.
Redington AE, et al. Transforming growth factor-beta 1 in asthma. Measurement in bronchoalveolar lavage fluid. Am. J. Respir. Crit. Care Med. 1997;156:642-647.
Not in our library10.1164/ajrccm.156.2.9605065
640.
Balzar S, et al. Increased TGF-beta2 in severe asthma with eosinophilia. J. Allergy Clin. Immunol. 2005;115:110-117.
Not in our library10.1016/j.jaci.2004.09.034
641.
Torrego A, Hew M, Oates T, Sukkar M, Fan Chung K. Expression and activation of TGF-beta isoforms in acute allergen-induced remodelling in asthma. Thorax. 2007;62:307-313.
Not in our library10.1136/thx.2006.063487
642.
Vignola AM, et al. Transforming growth factor-beta expression in mucosal biopsies in asthma and chronic bronchitis. Am. J. Respir. Crit. Care Med. 1997;156:591-599.
Not in our library10.1164/ajrccm.156.2.9609066
643.
Jiang K, et al. Changes in interleukin-17 and transforming growth factor beta 1 levels in serum and bronchoalveolar lavage fluid and their clinical significance among children with asthma. Transl. Pediatr. 2013;2:154-159.
Not in our library10.3978/j.issn.2224-4336.2013.10.03
644.
Vignola AM, et al. Release of transforming growth factor-beta (TGF-beta) and fibronectin by alveolar macrophages in airway diseases. Clin. Exp. Immunol. 1996;106:114-119.
Not in our library10.1046/j.1365-2249.1996.d01-811.x
645.
Minshall EM, et al. Eosinophil-associated TGF-beta1 mRNA expression and airways fibrosis in bronchial asthma. Am. J. Respir. Cell Mol. Biol. 1997;17:326-333.
Not in our library10.1165/ajrcmb.17.3.2733
646.
Ohno I, et al. Transforming growth factor beta 1 (TGF beta 1) gene expression by eosinophils in asthmatic airway inflammation. Am. J. Respir. Cell Mol. Biol. 1996;15:404-409.
Not in our library10.1165/ajrcmb.15.3.8810646
647.
Xie S, Sukkar MB, Issa R, Khorasani NM, Chung KF. Mechanisms of induction of airway smooth muscle hyperplasia by transforming growth factor-beta. Am. J. Physiol. Lung Cell Mol. Physiol. 2007;293:L245-L253.
Not in our library10.1152/ajplung.00068.2007
648.
Berger P, et al. Tryptase-stimulated human airway smooth muscle cells induce cytokine synthesis and mast cell chemotaxis. Faseb j. 2003;17:2139-2141.
Not in our library10.1096/fj.03-0041fje
649.
Janulaityte I, Januskevicius A, Kalinauskaite-Zukauske V, Bajoriuniene I, Malakauskas K. In Vivo Allergen-Activated Eosinophils Promote Collagen I and Fibronectin Gene Expression in Airway Smooth Muscle Cells via TGF-β1 Signaling Pathway in Asthma. Int J. Mol. Sci. 2020;21:1837.
Not in our library10.3390/ijms21051837
650.
Januskevicius A, et al. Eosinophils enhance WNT-5a and TGF-β1 genes expression in airway smooth muscle cells and promote their proliferation by increased extracellular matrix proteins production in asthma. BMC Pulm. Med. 2016;16:94.
Not in our library10.1186/s12890-016-0254-9
651.
Bottoms SE, Howell JE, Reinhardt AK, Evans IC, McAnulty RJ. Tgf-Beta isoform specific regulation of airway inflammation and remodelling in a murine model of asthma. PLoS One. 2010;5:e9674.
Not in our library10.1371/journal.pone.0009674
652.
Gagliardo R, et al. The role of transforming growth factor-β1 in airway inflammation of childhood asthma. Int J. Immunopathol. Pharm. 2013;26:725-738.
Not in our library10.1177/039463201302600316
653.
Eusebio M, Kraszula L, Kupczyk M, Kuna P, Pietruczuk M. The effects of interleukin-10 or TGF-beta on anti-CD3/CD28 induced activation of CD8+CD28- and CD8+CD28+ T cells in allergic asthma. J. Biol. Regul. Homeost. Agents. 2013;27:681-692.
Not in our library
654.
Hung CH, et al. Altered pattern of monocyte differentiation and monocyte-derived TGF-β1 in severe asthma. Sci. Rep. 2018;8:919.
Not in our library10.1038/s41598-017-19105-z
655.
Ma Y, et al. Immunization against TGF-β1 reduces collagen deposition but increases sustained inflammation in a murine asthma model. Hum. Vaccin Immunother. 2016;12:1876-1885.
Not in our library10.1080/21645515.2016.1145849
656.
Scherf W, Burdach S, Hansen G. Reduced expression of transforming growth factor beta 1 exacerbates pathology in an experimental asthma model. Eur. J. Immunol. 2005;35:198-206.
Not in our library10.1002/eji.200425209
657.
In vivo disruption of TGF-beta signaling by Smad7 in airway epithelium alleviates allergic asthma but aggravates lung carcinogenesis in mouse. · 2010
Not checked
658.
Gao P, et al. Functional effects of TGF-β1 on mesenchymal stem cell mobilization in cockroach allergen-induced asthma. J. Immunol. 2014;192:4560-4570.
Not in our library10.4049/jimmunol.1303461
659.
Nemeth K, et al. Bone marrow stromal cells use TGF-beta to suppress allergic responses in a mouse model of ragweed-induced asthma. Proc. Natl Acad. Sci. USA. 2010;107:5652-5657.
Not in our library10.1073/pnas.0910720107
660.
Musiol S, et al. TGF-β1 Drives Inflammatory Th Cell But Not Treg Cell Compartment Upon Allergen Exposure. Front Immunol. 2021;12:763243.
Not in our library10.3389/fimmu.2021.763243
661.
Whitehead GS, et al. A neutrophil/TGF-β axis limits the pathogenicity of allergen-specific CD4+ T cells. JCI Insight. 2022;7:e150251.
Not in our library10.1172/jci.insight.150251
662.
Yang ZC, et al. Transforming growth factor-β1 induces bronchial epithelial cells to mesenchymal transition by activating the Snail pathway and promotes airway remodeling in asthma. Mol. Med Rep. 2013;8:1663-1668.
Not in our library10.3892/mmr.2013.1728
663.
Hackett TL, et al. Induction of epithelial-mesenchymal transition in primary airway epithelial cells from patients with asthma by transforming growth factor-beta1. Am. J. Respir. Crit. Care Med. 2009;180:122-133.
Not in our library10.1164/rccm.200811-1730oc
664.
Stumm CL, et al. Lung remodeling in a mouse model of asthma involves a balance between TGF-β1 and BMP-7. PLoS One. 2014;9:e95959.
Not in our library10.1371/journal.pone.0095959
665.
Enhanced asthma-related fibroblast to myofibroblast transition is the result of profibrotic TGF-β/Smad2/3 pathway intensification and antifibrotic TGF-β/Smad1/5/(8)9 pathway impairment · 2020
Not checked
666.
Ciprandi G, De Amici M, Tosca M, Marseglia G. Serum transforming growth factor-beta levels depend on allergen exposure in allergic rhinitis. Int Arch. Allergy Immunol. 2010;152:66-70.
Not in our library10.1159/000260085
667.
Salib RJ, Kumar S, Wilson SJ, Howarth PH. Nasal mucosal immunoexpression of the mast cell chemoattractants TGF-beta, eotaxin, and stem cell factor and their receptors in allergic rhinitis. J. Allergy Clin. Immunol. 2004;114:799-806.
Not in our library10.1016/j.jaci.2004.07.010
668.
Salib RJ. Transforming growth factor-beta gene expression studies in nasal mucosal biopsies in naturally occurring allergic rhinitis. Ann. R. Coll. Surg. Engl. 2007;89:563-573.
Not in our library10.1308/003588407x202164
669.
Ouyang Y, Nakao A, Han D, Zhang L. Transforming growth factor-β1 promotes nasal mucosal mast cell chemotaxis in murine experimental allergic rhinitis. ORL J. Otorhinolaryngol. Relat. Spec. 2012;74:117-123.
Not in our library10.1159/000328587
670.
Ouyang Y, et al. TGF-beta signaling may play a role in the development of goblet cell hyperplasia in a mouse model of allergic rhinitis. Allergol. Int. 2010;59:313-319.
Not in our library10.2332/allergolint.10-sc-0172
671.
Wang M, Gu Z, Yang J, Zhao H, Cao Z. Changes among TGF-β1(+) Breg cells and helper T cell subsets in a murine model of allergic rhinitis with prolonged OVA challenge. Int Immunopharmacol. 2019;69:347-357.
Not in our library10.1016/j.intimp.2019.01.009
672.
Yang M, Yang C, Mine Y. Multiple T cell epitope peptides suppress allergic responses in an egg allergy mouse model by the elicitation of forkhead box transcription factor 3- and transforming growth factor-beta-associated mechanisms. Clin. Exp. Allergy. 2010;40:668-678.
Not in our library10.1111/j.1365-2222.2009.03442.x
673.
Barletta B, et al. Probiotic VSL#3-induced TGF-β ameliorates food allergy inflammation in a mouse model of peanut sensitization through the induction of regulatory T cells in the gut mucosa. Mol. Nutr. Food Res. 2013;57:2233-2244.
Not in our library10.1002/mnfr.201300028
674.
Pérez-Machado MA, et al. Reduced transforming growth factor-beta1-producing T cells in the duodenal mucosa of children with food allergy. Eur. J. Immunol. 2003;33:2307-2315.
Not in our library10.1002/eji.200323308
675.
Park HH, et al. TGF-β secreted by human umbilical cord blood-derived mesenchymal stem cells ameliorates atopic dermatitis by inhibiting secretion of TNF-α and IgE. Stem Cells. 2020;38:904-916.
Not in our library10.1002/stem.3183
676.
Sumiyoshi K, et al. Transforming growth factor-beta1 suppresses atopic dermatitis-like skin lesions in NC/Nga mice. Clin. Exp. Allergy. 2002;32:309-314.
Not in our library10.1046/j.1365-2222.2002.01221.x
677.
Kim HS, et al. Human umbilical cord blood mesenchymal stem cell-derived PGE2 and TGF-β1 alleviate atopic dermatitis by reducing mast cell degranulation. Stem Cells. 2015;33:1254-1266.
Not in our library10.1002/stem.1913
678.
Lee HJ, Lee HP, Ha SJ, Byun DG, Kim JW. Spontaneous expression of mRNA for IL-10, GM-CSF, TGF-beta, TGF-alpha, and IL-6 in peripheral blood mononuclear cells from atopic dermatitis. Ann. Allergy Asthma Immunol. 2000;84:553-558.
Not in our library10.1016/s1081-1206(10)62522-7
679.
Peng WM, Maintz L, Allam JP, Novak N. Attenuated TGF-β1 responsiveness of dendritic cells and their precursors in atopic dermatitis. Eur. J. Immunol. 2013;43:1374-1382.
Not in our library10.1002/eji.201242955
680.
Shafi, T. et al. Investigating dysregulation of TGF-β1/SMAD3 signaling in Atopic Dermatitis: A Molecular and Immunohistochemical Analysis. Clin. Exp. Immunol.10.1093/cei/uxad130 (2023).
Not in our library10.1093/cei/uxad130
681.
Akbarshahi H, Sam A, Chen C, Rosendahl AH, Andersson R. Early activation of pulmonary TGF-β1/Smad2 signaling in mice with acute pancreatitis-associated acute lung injury. Mediat. Inflamm. 2014;2014:148029.
Not in our library10.1155/2014/148029
682.
Hori Y, et al. Macrophage-derived transforming growth factor-beta1 induces hepatocellular injury via apoptosis in rat severe acute pancreatitis. Surgery. 2000;127:641-649.
Not in our library10.1067/msy.2000.105499
683.
van Laethem JL, et al. Localization of transforming growth factor beta 1 and its latent binding protein in human chronic pancreatitis. Gastroenterology. 1995;108:1873-1881.
Not in our library10.1016/0016-5085(95)90152-3
684.
Kanamaru Y, et al. Blockade of TGF-beta signaling in T cells prevents the development of experimental glomerulonephritis. J. Immunol. 2001;166:2818-2823.
Not in our library10.4049/jimmunol.166.4.2818
685.
Kitamura M, Sütö T, Yokoo T, Shimizu F, Fine LG. Transforming growth factor-beta 1 is the predominant paracrine inhibitor of macrophage cytokine synthesis produced by glomerular mesangial cells. J. Immunol. 1996;156:2964-2971.
Not in our library10.4049/jimmunol.156.8.2964
686.
Zhang W, et al. Staphylococcus aureus Infection Initiates Hypoxia-Mediated Transforming Growth Factor-β1 Upregulation to Trigger Osteomyelitis. mSystems. 2022;7:e0038022.
Not in our library10.1128/msystems.00380-22
687.
Brandes ME, Allen JB, Ogawa Y, Wahl SM. Transforming growth factor beta 1 suppresses acute and chronic arthritis in experimental animals. J. Clin. Invest. 1991;87:1108-1113.
Not in our library10.1172/jci115073
688.
Yan J, et al. Obesity- and aging-induced excess of central transforming growth factor-β potentiates diabetic development via an RNA stress response. Nat. Med. 2014;20:1001-1008.
Not in our library10.1038/nm.3616
689.
Weiss R, Lifshitz V, Frenkel D. TGF-β1 affects endothelial cell interaction with macrophages and T cells leading to the development of cerebrovascular amyloidosis. Brain Behav. Immun. 2011;25:1017-1024.
Not in our library10.1016/j.bbi.2010.11.012
690.
Grammas P, Ovase R. Cerebrovascular transforming growth factor-beta contributes to inflammation in the Alzheimer’s disease brain. Am. J. Pathol. 2002;160:1583-1587.
Not in our library10.1016/s0002-9440(10)61105-4
691.
Rendón-Ramirez EJ, et al. TGF-β Blood Levels Distinguish Between Influenza A (H1N1)pdm09 Virus Sepsis and Sepsis due to Other Forms of Community-Acquired Pneumonia. Viral Immunol. 2015;28:248-254.
Not in our library10.1089/vim.2014.0123
692.
Transforming Growth Factor-β: Activation by Neuraminidase and Role in Highly Pathogenic H5N1 Influenza Pathogenesis · 2010
No notice
693.
Furuya Y, et al. Prevention of Influenza Virus-Induced Immunopathology by TGF-β Produced during Allergic Asthma. PLoS Pathog. 2015;11:e1005180.
Not in our library10.1371/journal.ppat.1005180
694.
Richer MJ, Straka N, Fang D, Shanina I, Horwitz MS. Regulatory T-cells protect from type 1 diabetes after induction by coxsackievirus infection in the context of transforming growth factor-beta. Diabetes. 2008;57:1302-1311.
Not in our library10.2337/db07-1460
695.
Shi Y, et al. Regulatory T cells protect mice against coxsackievirus-induced myocarditis through the transforming growth factor beta-coxsackie-adenovirus receptor pathway. Circulation. 2010;121:2624-2634.
Not in our library10.1161/circulationaha.109.893248
696.
Beckham JD, Tuttle K, Tyler KL. Reovirus activates transforming growth factor beta and bone morphogenetic protein signaling pathways in the central nervous system that contribute to neuronal survival following infection. J. Virol. 2009;83:5035-5045.
Not in our library10.1128/jvi.02433-08
697.
Stanifer ML, et al. Reovirus intermediate subviral particles constitute a strategy to infect intestinal epithelial cells by exploiting TGF-β dependent pro-survival signaling. Cell Microbiol. 2016;18:1831-1845.
Not in our library10.1111/cmi.12626
698.
Chen Y, et al. Mechanism of exosomes from adipose-derived mesenchymal stem cells on sepsis-induced acute lung injury by promoting TGF-β secretion in macrophages. Surgery. 2023;174:1208-1219.
Not in our library10.1016/j.surg.2023.06.017
699.
Sanfilippo AM, Furuya Y, Roberts S, Salmon SL, Metzger DW. Allergic Lung Inflammation Reduces Tissue Invasion and Enhances Survival from Pulmonary Pneumococcal Infection in Mice, Which Correlates with Increased Expression of Transforming Growth Factor β1 and SiglecF(low) Alveolar Macrophages. Infect. Immun. 2015;83:2976-2983.
Not in our library10.1128/iai.00142-15
700.
Wang B, et al. Induction of TGF-beta1 and TGF-beta1-dependent predominant Th17 differentiation by group A streptococcal infection. Proc. Natl Acad. Sci. USA. 2010;107:5937-5942.
Not in our library10.1073/pnas.0904831107
701.
Nakane A, et al. Transforming growth factor beta is protective in host resistance against Listeria monocytogenes infection in mice. Infect. Immun. 1996;64:3901-3904.
Not in our library10.1128/iai.64.9.3901-3904.1996
702.
Zhong Y, Cantwell A, Dube PH. Transforming growth factor beta and CD25 are important for controlling systemic dissemination following Yersinia enterocolitica infection of the gut. Infect. Immun. 2010;78:3716-3725.
Not in our library10.1128/iai.00203-10
703.
Shao X, Rivera J, Niang R, Casadevall A, Goldman DL. A dual role for TGF-beta1 in the control and persistence of fungal pneumonia. J. Immunol. 2005;175:6757-6763.
Not in our library10.4049/jimmunol.175.10.6757
704.
Omer FM, Riley EM. Transforming growth factor beta production is inversely correlated with severity of murine malaria infection. J. Exp. Med. 1998;188:39-48.
Not in our library10.1084/jem.188.1.39
705.
Namangala B, Sugimoto C, Inoue N. Effects of exogenous transforming growth factor beta on Trypanosoma congolense infection in mice. Infect. Immun. 2007;75:1878-1885.
Not in our library10.1128/iai.01452-06
706.
Buzoni-Gatel D, et al. Murine ileitis after intracellular parasite infection is controlled by TGF-beta-producing intraepithelial lymphocytes. Gastroenterology. 2001;120:914-924.
Not in our library10.1053/gast.2001.22432a
707.
Cekanaviciute E, et al. Astrocytic TGF-β signaling limits inflammation and reduces neuronal damage during central nervous system Toxoplasma infection. J. Immunol. 2014;193:139-149.
Not in our library10.4049/jimmunol.1303284
708.
Zhao M, et al. The Effect of TGF-β on Treg Cells in Adverse Pregnancy Outcome upon Toxoplasma gondii Infection. Front Microbiol. 2017;8:901.
Not in our library10.3389/fmicb.2017.00901
709.
Xu X, et al. TGF-β1 improving abnormal pregnancy outcomes induced by Toxoplasma gondii infection: Regulating NKG2D/DAP10 and killer subset of decidual NK cells. Cell Immunol. 2017;317:9-17.
Not in our library10.1016/j.cellimm.2017.04.004
710.
Heitmann L, et al. TGF-β-responsive myeloid cells suppress type 2 immunity and emphysematous pathology after hookworm infection. Am. J. Pathol. 2012;181:897-906.
Not in our library10.1016/j.ajpath.2012.05.032
711.
Wu HP, et al. Plasma transforming growth factor-beta1 level in patients with severe community-acquired pneumonia and association with disease severity. J. Formos. Med Assoc. 2009;108:20-27.
Not in our library10.1016/s0929-6646(09)60028-0
712.
de Pablo R, et al. Sepsis-induced acute respiratory distress syndrome with fatal outcome is associated to increased serum transforming growth factor beta-1 levels. Eur. J. Intern Med. 2012;23:358-362.
Not in our library10.1016/j.ejim.2011.10.001
713.
Gauthier T, et al. TGF-β uncouples glycolysis and inflammation in macrophages and controls survival during sepsis. Sci. Signal. 2023;16:eade0385.
Not in our library10.1126/scisignal.ade0385
714.
Ahmad S, Choudhry MA, Shankar R, Sayeed MM. Transforming growth factor-beta negatively modulates T-cell responses in sepsis. FEBS Lett. 1997;402:213-218.
Not in our library10.1016/s0014-5793(96)01535-9
715.
Lowrance JH, O’Sullivan FX, Caver TE, Waegell W, Gresham HD. Spontaneous elaboration of transforming growth factor beta suppresses host defense against bacterial infection in autoimmune MRL/lpr mice. J. Exp. Med. 1994;180:1693-1703.
Not in our library10.1084/jem.180.5.1693
716.
Li N, et al. Influenza viral neuraminidase primes bacterial coinfection through TGF-β-mediated expression of host cell receptors. Proc. Natl Acad. Sci. USA. 2015;112:238-243.
Not in our library10.1073/pnas.1414422112
717.
Zhang M, et al. TGF-β1 promoted the infection of bovine mammary epithelial cells by Staphylococcus aureus through increasing expression of cells’ fibronectin and integrin β1. Vet. Microbiol. 2019;237:108420.
Not in our library10.1016/j.vetmic.2019.108420
718.
Owyang SY, et al. Dendritic cell-derived TGF-β mediates the induction of mucosal regulatory T-cell response to Helicobacter infection essential for maintenance of immune tolerance in mice. Helicobacter. 2020;25:e12763.
Not in our library10.1111/hel.12763
719.
Beswick EJ, Pinchuk IV, Earley RB, Schmitt DA, Reyes VE. Role of gastric epithelial cell-derived transforming growth factor beta in reduced CD4+ T cell proliferation and development of regulatory T cells during Helicobacter pylori infection. Infect. Immun. 2011;79:2737-2745.
Not in our library10.1128/iai.01146-10
720.
Liu Y, Islam EA, Jarvis GA, Gray-Owen SD, Russell MW. Neisseria gonorrhoeae selectively suppresses the development of Th1 and Th2 cells, and enhances Th17 cell responses, through TGF-β-dependent mechanisms. Mucosal. Immunol. 2012;5:320-331.
Not in our library10.1038/mi.2012.12
721.
Balkhi MY, Sinha A, Natarajan K. Dominance of CD86, transforming growth factor- beta 1, and interleukin-10 in Mycobacterium tuberculosis secretory antigen-activated dendritic cells regulates T helper 1 responses to mycobacterial antigens. J. Infect. Dis. 2004;189:1598-1609.
Not in our library10.1086/383328
722.
Roberts T, Beyers N, Aguirre A, Walzl G. Immunosuppression during active tuberculosis is characterized by decreased interferon- gamma production and CD25 expression with elevated forkhead box P3, transforming growth factor- beta, and interleukin-4 mRNA levels. J. Infect. Dis. 2007;195:870-878.
Not in our library10.1086/511277
723.
Denney L, Branchett W, Gregory LG, Oliver RA, Lloyd CM. Epithelial-derived TGF-β1 acts as a pro-viral factor in the lung during influenza A infection. Mucosal. Immunol. 2018;11:523-535.
Not in our library10.1038/mi.2017.77
724.
Thomas BJ, et al. Transforming growth factor-beta enhances rhinovirus infection by diminishing early innate responses. Am. J. Respir. Cell Mol. Biol. 2009;41:339-347.
Not in our library10.1165/rcmb.2008-0316oc
725.
Lewis GM, Macal M, Hesser CR, Zuñiga EI. Constitutive but not inducible attenuation of transforming growth factor β signaling increases natural killer cell responses without directly affecting dendritic cells early after persistent viral infection. J. Virol. 2015;89:3343-3355.
Not in our library10.1128/jvi.03076-14
726.
Marcoe JP, et al. TGF-β is responsible for NK cell immaturity during ontogeny and increased susceptibility to infection during mouse infancy. Nat. Immunol. 2012;13:843-850.
Not in our library10.1038/ni.2388
727.
Kekow J, et al. Transforming growth factor beta and noncytopathic mechanisms of immunodeficiency in human immunodeficiency virus infection. Proc. Natl Acad. Sci. USA. 1990;87:8321-8325.
Not in our library10.1073/pnas.87.21.8321
728.
Kekow J, et al. Transforming growth factor-beta and suppression of humoral immune responses in HIV infection. J. Clin. Invest. 1991;87:1010-1016.
Not in our library10.1172/jci115059
729.
Bedke N, et al. Transforming growth factor-beta promotes rhinovirus replication in bronchial epithelial cells by suppressing the innate immune response. PLoS One. 2012;7:e44580.
Not in our library10.1371/journal.pone.0044580
730.
Grunwell JR, et al. TGF-β1 Suppresses the Type I IFN Response and Induces Mitochondrial Dysfunction in Alveolar Macrophages. J. Immunol. 2018;200:2115-2128.
Not in our library10.4049/jimmunol.1701325
731.
Witkowski M, et al. Untimely TGFβ responses in COVID-19 limit antiviral functions of NK cells. Nature. 2021;600:295-301.
Not in our library10.1038/s41586-021-04142-6
732.
Moriuchi M, Moriuchi H. Cell-type-dependent effect of transforming growth factor beta, a major cytokine in breast milk, on human immunodeficiency virus type 1 infection of mammary epithelial MCF-7 cells or macrophages. J. Virol. 2004;78:13046-13052.
Not in our library10.1128/jvi.78.23.13046-13052.2004
733.
Yim LY, et al. Transforming Growth Factor β Signaling Promotes HIV-1 Infection in Activated and Resting Memory CD4(+) T Cells. J. Virol. 2023;97:e0027023.
Not in our library10.1128/jvi.00270-23
734.
Cheung KW, et al. α(4)β(7)(+) CD4(+) Effector/Effector Memory T Cells Differentiate into Productively and Latently Infected Central Memory T Cells by Transforming Growth Factor β1 during HIV-1 Infection. J. Virol. 2018;92:e01510-e01517.
Not in our library10.1128/jvi.01510-17
735.
Moriuchi M, Moriuchi H. Transforming growth factor-beta enhances human T-cell leukemia virus type I infection. J. Med Virol. 2002;67:427-430.
Not in our library10.1002/jmv.10074
736.
Lin W, et al. HIV increases HCV replication in a TGF-beta1-dependent manner. Gastroenterology. 2008;134:803-811.
Not in our library10.1053/j.gastro.2008.01.005
737.
Trinh QD, et al. TGF-β1 Promotes Zika Virus Infection in Immortalized Human First-Trimester Trophoblasts via the Smad Pathway. Cells. 2022;11:3026.
Not in our library10.3390/cells11193026
738.
Pham NTK, et al. The Epithelial-to-Mesenchymal Transition-Like Process Induced by TGF-β1 Enhances Rubella Virus Binding and Infection in A549 Cells via the Smad Pathway. Microorganisms. 2021;9:662.
Not in our library10.3390/microorganisms9030662
739.
Flynn RJ, Mulcahy G. The roles of IL-10 and TGF-beta in controlling IL-4 and IFN-gamma production during experimental Fasciola hepatica infection. Int J. Parasitol. 2008;38:1673-1680.
Not in our library10.1016/j.ijpara.2008.05.008
740.
Pang N, et al. TGF-β/Smad signaling pathway regulates Th17/Treg balance during Echinococcus multilocularis infection. Int Immunopharmacol. 2014;20:248-257.
Not in our library10.1016/j.intimp.2014.02.038
741.
Barbosa BF, et al. IL10, TGF beta1, and IFN gamma modulate intracellular signaling pathways and cytokine production to control Toxoplasma gondii infection in BeWo trophoblast cells. Biol. Reprod. 2015;92:82.
Not in our library10.1095/biolreprod.114.124115
742.
Barral-Netto M, et al. Transforming growth factor-beta in leishmanial infection: a parasite escape mechanism. Science. 1992;257:545-548.
Not in our library10.1126/science.1636092
743.
Walther M, et al. Upregulation of TGF-beta, FOXP3, and CD4+CD25+ regulatory T cells correlates with more rapid parasite growth in human malaria infection. Immunity. 2005;23:287-296.
Not in our library10.1016/j.immuni.2005.08.006
744.
Tsutsui N, Kamiyama T. Transforming growth factor beta-induced failure of resistance to infection with blood-stage Plasmodium chabaudi in mice. Infect. Immun. 1999;67:2306-2311.
Not in our library10.1128/iai.67.5.2306-2311.1999
745.
Akhurst RJ, Fee F, Balmain A. Localized production of TGF-beta mRNA in tumour promoter-stimulated mouse epidermis. Nature. 1988;331:363-365.
Not in our library10.1038/331363a0
746.
Cui W, et al. Concerted action of TGF-beta 1 and its type II receptor in control of epidermal homeostasis in transgenic mice. Genes Dev. 1995;9:945-955.
Not in our library10.1101/gad.9.8.945
747.
Fowlis DJ, Cui W, Johnson SA, Balmain A, Akhurst RJ. Altered epidermal cell growth control in vivo by inducible expression of transforming growth factor beta 1 in the skin of transgenic mice. Cell Growth Differ. 1996;7:679-687.
Not in our library
748.
Boulanger CA, Smith GH. Reducing mammary cancer risk through premature stem cell senescence. Oncogene. 2001;20:2264-2272.
Not in our library10.1038/sj.onc.1204312
749.
Siegel PM, Shu W, Cardiff RD, Muller WJ, Massagué J. Transforming growth factor beta signaling impairs Neu-induced mammary tumorigenesis while promoting pulmonary metastasis. Proc. Natl Acad. Sci. USA. 2003;100:8430-8435.
Not in our library10.1073/pnas.0932636100
750.
Weeks BH, He W, Olson KL, Wang XJ. Inducible expression of transforming growth factor beta1 in papillomas causes rapid metastasis. Cancer Res. 2001;61:7435-7443.
Not in our library
751.
Gobbi H, et al. Transforming growth factor-beta and breast cancer risk in women with mammary epithelial hyperplasia. J. Natl Cancer Inst. 1999;91:2096-2101.
Not in our library10.1093/jnci/91.24.2096
752.
Goudie DR, et al. Multiple self-healing squamous epithelioma is caused by a disease-specific spectrum of mutations in TGFBR1. Nat. Genet. 2011;43:365-369.
Not in our library10.1038/ng.780
753.
Goudie D. Multiple Self-Healing Squamous Epithelioma (MSSE): A Digenic Trait Associated with Loss of Function Mutations in TGFBR1 and Variants at a Second Linked Locus on the Long Arm of Chromosome 9. Genes (Basel). 2020;11:1410.
Not in our library10.3390/genes11121410
754.
Lu SL, et al. HNPCC associated with germline mutation in the TGF-beta type II receptor gene. Nat. Genet. 1998;19:17-18.
Not in our library10.1038/ng0598-17
755.
Woodford-Richens K, et al. Analysis of genetic and phenotypic heterogeneity in juvenile polyposis. Gut. 2000;46:656-660.
Not in our library10.1136/gut.46.5.656
756.
Howe JR, et al. The prevalence of MADH4 and BMPR1A mutations in juvenile polyposis and absence of BMPR2, BMPR1B, and ACVR1 mutations. J. Med Genet. 2004;41:484-491.
Not in our library10.1136/jmg.2004.018598
757.
Engle SJ, et al. Transforming growth factor beta1 suppresses nonmetastatic colon cancer at an early stage of tumorigenesis. Cancer Res. 1999;59:3379-3386.
Not in our library
758.
Glick AB, et al. Loss of expression of transforming growth factor beta in skin and skin tumors is associated with hyperproliferation and a high risk for malignant conversion. Proc. Natl Acad. Sci. USA. 1993;90:6076-6080.
Not in our library10.1073/pnas.90.13.6076
759.
Forrester E, et al. Effect of conditional knockout of the type II TGF-beta receptor gene in mammary epithelia on mammary gland development and polyomavirus middle T antigen induced tumor formation and metastasis. Cancer Res. 2005;65:2296-2302.
Not in our library10.1158/0008-5472.can-04-3272
760.
Muñoz NM, et al. Transforming growth factor beta receptor type II inactivation induces the malignant transformation of intestinal neoplasms initiated by Apc mutation. Cancer Res. 2006;66:9837-9844.
Not in our library10.1158/0008-5472.can-06-0890
761.
Ijichi H, et al. Aggressive pancreatic ductal adenocarcinoma in mice caused by pancreas-specific blockade of transforming growth factor-beta signaling in cooperation with active Kras expression. Genes Dev. 2006;20:3147-3160.
Not in our library10.1101/gad.1475506
762.
Lu SL, et al. Loss of transforming growth factor-beta type II receptor promotes metastatic head-and-neck squamous cell carcinoma. Genes Dev. 2006;20:1331-1342.
Not in our library10.1101/gad.1413306
763.
Bian Y, et al. Progressive tumor formation in mice with conditional deletion of TGF-beta signaling in head and neck epithelia is associated with activation of the PI3K/Akt pathway. Cancer Res. 2009;69:5918-5926.
Not in our library10.1158/0008-5472.can-08-4623
764.
Guasch G, et al. Loss of TGFbeta signaling destabilizes homeostasis and promotes squamous cell carcinomas in stratified epithelia. Cancer Cell. 2007;12:313-327.
Not in our library10.1016/j.ccr.2007.08.020
765.
Go C, et al. Aberrant cell cycle progression contributes to the early-stage accelerated carcinogenesis in transgenic epidermis expressing the dominant negative TGFbetaRII. Oncogene. 2000;19:3623-3631.
Not in our library10.1038/sj.onc.1203701
766.
Amendt C, Schirmacher P, Weber H, Blessing M. Expression of a dominant negative type II TGF-beta receptor in mouse skin results in an increase in carcinoma incidence and an acceleration of carcinoma development. Oncogene. 1998;17:25-34.
Not in our library10.1038/sj.onc.1202161
767.
Kanzler S, et al. Hepatocellular expression of a dominant-negative mutant TGF-beta type II receptor accelerates chemically induced hepatocarcinogenesis. Oncogene. 2001;20:5015-5024.
Not in our library10.1038/sj.onc.1204544
768.
Hahm KB, et al. Conditional loss of TGF-beta signalling leads to increased susceptibility to gastrointestinal carcinogenesis in mice. Aliment Pharm. Ther. 2002;16:115-127.
Not in our library10.1046/j.1365-2036.16.s2.3.x
769.
Biswas S, et al. Transforming growth factor beta receptor type II inactivation promotes the establishment and progression of colon cancer. Cancer Res. 2004;64:4687-4692.
Not in our library10.1158/0008-5472.can-03-3255
770.
Gorska AE, et al. Transgenic mice expressing a dominant-negative mutant type II transforming growth factor-beta receptor exhibit impaired mammary development and enhanced mammary tumor formation. Am. J. Pathol. 2003;163:1539-1549.
Not in our library10.1016/s0002-9440(10)63510-9
771.
Zhu Y, Richardson JA, Parada LF, Graff JM. Smad3 mutant mice develop metastatic colorectal cancer. Cell. 1998;94:703-714.
Not in our library10.1016/s0092-8674(00)81730-4
772.
Wolfraim LA, et al. Loss of Smad3 in acute T-cell lymphoblastic leukemia. N. Engl. J. Med. 2004;351:552-559.
Not in our library10.1056/nejmoa031197
773.
Takaku K, et al. Gastric and duodenal polyps in Smad4 (Dpc4) knockout mice. Cancer Res. 1999;59:6113-6117.
Not in our library
774.
Bardeesy N, et al. Smad4 is dispensable for normal pancreas development yet critical in progression and tumor biology of pancreas cancer. Genes Dev. 2006;20:3130-3146.
Not in our library10.1101/gad.1478706
775.
Alberici P, et al. Smad4 haploinsufficiency in mouse models for intestinal cancer. Oncogene. 2006;25:1841-1851.
Not in our library10.1038/sj.onc.1209226
776.
Xu X, et al. Haploid loss of the tumor suppressor Smad4/Dpc4 initiates gastric polyposis and cancer in mice. Oncogene. 2000;19:1868-1874.
Not in our library10.1038/sj.onc.1203504
777.
Braun L, Dürst M, Mikumo R, Crowley A, Robinson M. Regulation of growth and gene expression in human papillomavirus-transformed keratinocytes by transforming growth factor-beta: implications for the control of papillomavirus infection. Mol. Carcinog. 1992;6:100-111.
Not in our library10.1002/mc.2940060205
778.
Souza RF, et al. A transforming growth factor beta 1 receptor type II mutation in ulcerative colitis-associated neoplasms. Gastroenterology. 1997;112:40-45.
Not in our library10.1016/s0016-5085(97)70217-8
779.
Kim BG, et al. Smad4 signalling in T cells is required for suppression of gastrointestinal cancer. Nature. 2006;441:1015-1019.
Not in our library10.1038/nature04846
780.
Matsuzaki K, et al. Chronic inflammation associated with hepatitis C virus infection perturbs hepatic transforming growth factor beta signaling, promoting cirrhosis and hepatocellular carcinoma. Hepatology. 2007;46:48-57.
Not in our library10.1002/hep.21672
781.
Inflammation-mediated genetic and epigenetic alterations drive cancer development in the neighboring epithelium upon stromal abrogation of TGF-β signaling. · 2013
Not checked
782.
Glick AB, Weinberg WC, Wu IH, Quan W, Yuspa SH. Transforming growth factor beta 1 suppresses genomic instability independent of a G1 arrest, p53, and Rb. Cancer Res. 1996;56:3645-3650.
Not in our library
783.
Katakura Y, Nakata E, Miura T, Shirahata S. Transforming growth factor beta triggers two independent-senescence programs in cancer cells. Biochem Biophys. Res Commun. 1999;255:110-115.
Not in our library10.1006/bbrc.1999.0129
784.
Bhowmick NA, et al. TGF-beta signaling in fibroblasts modulates the oncogenic potential of adjacent epithelia. Science. 2004;303:848-851.
Not in our library10.1126/science.1090922
785.
Moustakas A, Kardassis D. Regulation of the human p21/WAF1/Cip1 promoter in hepatic cells by functional interactions between Sp1 and Smad family members. Proc. Natl Acad. Sci. USA. 1998;95:6733-6738.
Not in our library10.1073/pnas.95.12.6733
786.
Kang SH, et al. Rapid induction of p21WAF1 but delayed down-regulation of Cdc25A in the TGF-beta-induced cell cycle arrest of gastric carcinoma cells. Br. J. Cancer. 1999;80:1144-1149.
Not in our library10.1038/sj.bjc.6690478
787.
Damdinsuren B, et al. TGF-beta1-induced cell growth arrest and partial differentiation is related to the suppression of Id1 in human hepatoma cells. Oncol. Rep. 2006;15:401-408.
Not in our library
788.
Hishikawa K, et al. Connective tissue growth factor induces apoptosis in human breast cancer cell line MCF-7. J. Biol. Chem. 1999;274:37461-37466.
Not in our library10.1074/jbc.274.52.37461
789.
Zhang H, et al. Involvement of programmed cell death 4 in transforming growth factor-beta1-induced apoptosis in human hepatocellular carcinoma. Oncogene. 2006;25:6101-6112.
Not in our library10.1038/sj.onc.1209634
790.
Kim SG, et al. Transforming growth factor-beta 1 induces apoptosis through Fas ligand-independent activation of the Fas death pathway in human gastric SNU-620 carcinoma cells. Mol. Biol. Cell. 2004;15:420-434.
Not in our library10.1091/mbc.e03-04-0201
791.
Jang CW, et al. TGF-beta induces apoptosis through Smad-mediated expression of DAP-kinase. Nat. Cell Biol. 2002;4:51-58.
Not in our library10.1038/ncb731
792.
David CJ, et al. TGF-β Tumor Suppression through a Lethal EMT. Cell. 2016;164:1015-1030.
Not in our library10.1016/j.cell.2016.01.009
793.
Tachibana I, et al. Overexpression of the TGFbeta-regulated zinc finger encoding gene, TIEG, induces apoptosis in pancreatic epithelial cells. J. Clin. Invest. 1997;99:2365-2374.
Not in our library10.1172/jci119418
794.
Kim BC, Mamura M, Choi KS, Calabretta B, Kim SJ. Transforming growth factor beta 1 induces apoptosis through cleavage of BAD in a Smad3-dependent mechanism in FaO hepatoma cells. Mol. Cell Biol. 2002;22:1369-1378.
Not in our library10.1128/mcb.22.5.1369-1378.2002
795.
Chipuk JE, Bhat M, Hsing AY, Ma J, Danielpour D. Bcl-xL blocks transforming growth factor-beta 1-induced apoptosis by inhibiting cytochrome c release and not by directly antagonizing Apaf-1-dependent caspase activation in prostate epithelial cells. J. Biol. Chem. 2001;276:26614-26621.
Not in our library10.1074/jbc.m100913200
796.
Spender LC, et al. TGF-beta induces apoptosis in human B cells by transcriptional regulation of BIK and BCL-XL. Cell Death Differ. 2009;16:593-602.
Not in our library10.1038/cdd.2008.183
797.
Ohgushi M, et al. Transforming growth factor beta-dependent sequential activation of Smad, Bim, and caspase-9 mediates physiological apoptosis in gastric epithelial cells. Mol. Cell Biol. 2005;25:10017-10028.
Not in our library10.1128/mcb.25.22.10017-10028.2005
798.
Saltzman A, et al. Transforming growth factor-beta-mediated apoptosis in the Ramos B-lymphoma cell line is accompanied by caspase activation and Bcl-XL downregulation. Exp. Cell Res. 1998;242:244-254.
Not in our library10.1006/excr.1998.4096
799.
Kanamaru C, Yasuda H, Fujita T. Involvement of Smad proteins in TGF-beta and activin A-induced apoptosis and growth inhibition of liver cells. Hepatol. Res. 2002;23:211-219.
Not in our library10.1016/s1386-6346(01)00175-9
800.
Bakhshayesh M, Zaker F, Hashemi M, Katebi M, Solaimani M. TGF- β1-mediated apoptosis associated with SMAD-dependent mitochondrial Bcl-2 expression. Clin. Lymphoma Myeloma Leuk. 2012;12:138-143.
Not in our library10.1016/j.clml.2011.12.001
801.
Cui W, Kemp CJ, Duffie E, Balmain A, Akhurst RJ. Lack of transforming growth factor-beta 1 expression in benign skin tumors of p53null mice is prognostic for a high risk of malignant conversion. Cancer Res. 1994;54:5831-5836.
Not in our library
802.
Cui W, et al. TGFbeta1 inhibits the formation of benign skin tumors, but enhances progression to invasive spindle carcinomas in transgenic mice. Cell. 1996;86:531-542.
Not in our library10.1016/s0092-8674(00)80127-0
803.
Capocasale RJ, et al. Reduced surface expression of transforming growth factor beta receptor type II in mitogen-activated T cells from Sézary patients. Proc. Natl Acad. Sci. USA. 1995;92:5501-5505.
Not in our library10.1073/pnas.92.12.5501
804.
Kadin ME, et al. Loss of receptors for transforming growth factor beta in human T-cell malignancies. Proc. Natl Acad. Sci. USA. 1994;91:6002-6006.
Not in our library10.1073/pnas.91.13.6002
805.
Fukai Y, et al. Reduced expression of transforming growth factor-beta receptors is an unfavorable prognostic factor in human esophageal squamous cell carcinoma. Int J. Cancer. 2003;104:161-166.
Not in our library10.1002/ijc.10929
806.
Tanaka S, Mori M, Mafune K, Ohno S, Sugimachi K. A dominant negative mutation of transforming growth factor-beta receptor type II gene in microsatellite stable oesophageal carcinoma. Br. J. Cancer. 2000;82:1557-1560.
Not in our library10.1054/bjoc.1999.1178
807.
Souza RF, et al. Alterations of transforming growth factor-beta 1 receptor type II occur in ulcerative colitis-associated carcinomas, sporadic colorectal neoplasms, and esophageal carcinomas, but not in gastric neoplasms. Hum. Cell. 1996;9:229-236.
Not in our library
808.
Myeroff LL, et al. A transforming growth factor beta receptor type II gene mutation common in colon and gastric but rare in endometrial cancers with microsatellite instability. Cancer Res. 1995;55:5545-5547.
Not in our library
809.
Grady WM, et al. Mutation of the type II transforming growth factor-beta receptor is coincident with the transformation of human colon adenomas to malignant carcinomas. Cancer Res. 1998;58:3101-3104.
Not in our library
810.
Salovaara R, et al. Frequent loss of SMAD4/DPC4 protein in colorectal cancers. Gut. 2002;51:56-59.
Not in our library10.1136/gut.51.1.56
811.
Takagi Y, et al. Somatic alterations of the DPC4 gene in human colorectal cancers in vivo. Gastroenterology. 1996;111:1369-1372.
Not in our library10.1053/gast.1996.v111.pm8898652
812.
Goggins M, et al. Genetic alterations of the transforming growth factor beta receptor genes in pancreatic and biliary adenocarcinomas. Cancer Res. 1998;58:5329-5332.
Not in our library
813.
Venkatasubbarao K, et al. Novel mutations in the polyadenine tract of the transforming growth factor beta type II receptor gene are found in a subpopulation of human pancreatic adenocarcinomas. Genes Chromosomes Cancer. 1998;22:138-144.
Not in our library10.1002/(sici)1098-2264(199806)22:2<138::aid-gcc8>3.0.co;2-y
814.
Imai Y, Tsurutani N, Oda H, Inoue T, Ishikawa T. Genetic instability and mutation of the TGF-beta-receptor-II gene in ampullary carcinomas. Int J. Cancer. 1998;76:407-411.
Not in our library10.1002/(sici)1097-0215(19980504)76:3<407::aid-ijc19>3.0.co;2-7
815.
Lazzereschi D, et al. Human malignant thyroid tumors displayed reduced levels of transforming growth factor beta receptor type II messenger RNA and protein. Cancer Res. 1997;57:2071-2076.
Not in our library
816.
Kim IY, et al. Loss of expression of transforming growth factor-beta receptors is associated with poor prognosis in prostate cancer patients. Clin. Cancer Res. 1998;4:1625-1630.
Not in our library
817.
Guo Y, Jacobs SC, Kyprianou N. Down-regulation of protein and mRNA expression for transforming growth factor-beta (TGF-beta1) type I and type II receptors in human prostate cancer. Int J. Cancer. 1997;71:573-579.
Not in our library10.1002/(sici)1097-0215(19970516)71:4<573::aid-ijc11>3.0.co;2-d
818.
Gobbi H, et al. Loss of expression of transforming growth factor beta type II receptor correlates with high tumour grade in human breast in-situ and invasive carcinomas. Histopathology. 2000;36:168-177.
Not in our library10.1046/j.1365-2559.2000.00841.x
819.
Lynch MA, et al. Mutational analysis of the transforming growth factor beta receptor type II gene in human ovarian carcinoma. Cancer Res. 1998;58:4227-4232.
Not in our library
820.
Chen T, et al. Novel inactivating mutations of transforming growth factor-beta type I receptor gene in head-and-neck cancer metastases. Int J. Cancer. 2001;93:653-661.
Not in our library10.1002/ijc.1381
821.
Wang D, et al. Mutation and downregulation of the transforming growth factor beta type II receptor gene in primary squamous cell carcinomas of the head and neck. Carcinogenesis. 1997;18:2285-2290.
Not in our library10.1093/carcin/18.11.2285
822.
Qiu W, Schönleben F, Li X, Su GH. Disruption of transforming growth factor beta-Smad signaling pathway in head and neck squamous cell carcinoma as evidenced by mutations of SMAD2 and SMAD4. Cancer Lett. 2007;245:163-170.
Not in our library10.1016/j.canlet.2006.01.003
823.
Xie W, et al. Frequent alterations of Smad signaling in human head and neck squamous cell carcinomas: a tissue microarray analysis. Oncol. Res. 2003;14:61-73.
Not in our library10.3727/000000003108748612
824.
Sun L, et al. Expression of transforming growth factor beta type II receptor leads to reduced malignancy in human breast cancer MCF-7 cells. J. Biol. Chem. 1994;269:26449-26455.
Not in our library10.1016/s0021-9258(18)47215-8
825.
Steiner MS. & Barrack, E. R. Transforming growth factor-beta 1 overproduction in prostate cancer: effects on growth in vivo and in vitro. Mol. Endocrinol. 1992;6:15-25.
Not in our library10.1210/mend.6.1.1738367
826.
Chang HL, et al. Increased transforming growth factor beta expression inhibits cell proliferation in vitro, yet increases tumorigenicity and tumor growth of Meth A sarcoma cells. Cancer Res. 1993;53:4391-4398.
Not in our library
827.
Kleeff J, et al. The TGF-beta signaling inhibitor Smad7 enhances tumorigenicity in pancreatic cancer. Oncogene. 1999;18:5363-5372.
Not in our library10.1038/sj.onc.1202909
828.
Datto MB, Hu PP, Kowalik TF, Yingling J, Wang XF. The viral oncoprotein E1A blocks transforming growth factor beta-mediated induction of p21/WAF1/Cip1 and p15/INK4B. Mol. Cell Biol. 1997;17:2030-2037.
Not in our library10.1128/mcb.17.4.2030
829.
Missero C. Ramon y Cajal, S. & Dotto, G. P. Escape from transforming growth factor beta control and oncogene cooperation in skin tumor development. Proc. Natl Acad. Sci. USA. 1991;88:9613-9617.
Not in our library10.1073/pnas.88.21.9613
830.
Kurokawa M, et al. The oncoprotein Evi-1 represses TGF-beta signalling by inhibiting Smad3. Nature. 1998;394:92-96.
Not in our library10.1038/27945
831.
Alexandrow MG, Kawabata M, Aakre M, Moses HL. Overexpression of the c-Myc oncoprotein blocks the growth-inhibitory response but is required for the mitogenic effects of transforming growth factor beta 1. Proc. Natl Acad. Sci. USA. 1995;92:3239-3243.
Not in our library10.1073/pnas.92.8.3239
832.
Schlegel NC, et al. Id2 suppression of p15 counters TGF-beta-mediated growth inhibition of melanoma cells. Pigment Cell Melanoma Res. 2009;22:445-453.
Not in our library10.1111/j.1755-148x.2009.00571.x
833.
Ewen ME, Oliver CJ, Sluss HK, Miller SJ, Peeper D. S. p53-dependent repression of CDK4 translation in TGF-beta-induced G1 cell-cycle arrest. Genes Dev. 1995;9:204-217.
Not in our library10.1101/gad.9.2.204
834.
Kretzschmar M, Doody J, Timokhina I, Massague J. A mechanism of repression of TGFbeta/ Smad signaling by oncogenic Ras. Genes Dev. 1999;13:804-816.
Not in our library10.1101/gad.13.7.804
835.
Dalal BI, Keown PA, Greenberg AH. Immunocytochemical localization of secreted transforming growth factor-beta 1 to the advancing edges of primary tumors and to lymph node metastases of human mammary carcinoma. Am. J. Pathol. 1993;143:381-389.
Not in our library
836.
Walker RA, Dearing SJ. Transforming growth factor beta 1 in ductal carcinoma in situ and invasive carcinomas of the breast. Eur. J. Cancer. 1992;28:641-644.
Not in our library10.1016/s0959-8049(05)80116-9
837.
Friess H, et al. Enhanced expression of transforming growth factor beta isoforms in pancreatic cancer correlates with decreased survival. Gastroenterology. 1993;105:1846-1856.
Not in our library10.1016/0016-5085(93)91084-u
838.
Wagner M, Kleeff J, Friess H, Büchler MW, Korc M. Enhanced expression of the type II transforming growth factor-beta receptor is associated with decreased survival in human pancreatic cancer. Pancreas. 1999;19:370-376.
Not in our library10.1097/00006676-199911000-00008
839.
Tateishi M, et al. The progression of invasiveness regarding the role of transforming growth factor beta receptor type II in gastric cancer. Eur. J. Surg. Oncol. 2000;26:377-380.
Not in our library10.1053/ejso.1999.0902
840.
Welch DR, Fabra A, Nakajima M. Transforming growth factor beta stimulates mammary adenocarcinoma cell invasion and metastatic potential. Proc. Natl Acad. Sci. USA. 1990;87:7678-7682.
Not in our library10.1073/pnas.87.19.7678
841.
Tang B, et al. TGF-beta switches from tumor suppressor to prometastatic factor in a model of breast cancer progression. J. Clin. Invest. 2003;112:1116-1124.
Not in our library10.1172/jci200318899
842.
Oft M, Heider KH, Beug H. TGFbeta signaling is necessary for carcinoma cell invasiveness and metastasis. Curr. Biol. 1998;8:1243-1252.
Not in our library10.1016/s0960-9822(07)00533-7
843.
Han G, et al. Distinct mechanisms of TGF-beta1-mediated epithelial-to-mesenchymal transition and metastasis during skin carcinogenesis. J. Clin. Invest. 2005;115:1714-1723.
Not in our library10.1172/jci24399
844.
Caulín C, Scholl FG, Frontelo P, Gamallo C, Quintanilla M. Chronic exposure of cultured transformed mouse epidermal cells to transforming growth factor-beta 1 induces an epithelial-mesenchymal transdifferentiation and a spindle tumoral phenotype. Cell Growth Differ. 1995;6:1027-1035.
Not in our library
845.
Cheng JC, Auersperg N, Leung PC. TGF-beta induces serous borderline ovarian tumor cell invasion by activating EMT but triggers apoptosis in low-grade serous ovarian carcinoma cells. PLoS One. 2012;7:e42436.
Not in our library10.1371/journal.pone.0042436
846.
Qiao B, Johnson NW, Gao J. Epithelial-mesenchymal transition in oral squamous cell carcinoma triggered by transforming growth factor-beta1 is Snail family-dependent and correlates with matrix metalloproteinase-2 and -9 expressions. Int J. Oncol. 2010;37:663-668.
Not in our library10.3892/ijo_00000715
847.
Vincent T, et al. A SNAIL1-SMAD3/4 transcriptional repressor complex promotes TGF-beta mediated epithelial-mesenchymal transition. Nat. Cell Biol. 2009;11:943-950.
Not in our library10.1038/ncb1905
848.
Arrick BA, et al. Altered metabolic and adhesive properties and increased tumorigenesis associated with increased expression of transforming growth factor beta 1. J. Cell Biol. 1992;118:715-726.
Not in our library10.1083/jcb.118.3.715
849.
Tu WH, et al. The loss of TGF-beta signaling promotes prostate cancer metastasis. Neoplasia. 2003;5:267-277.
Not in our library10.1016/s1476-5586(03)80058-1
850.
Huntley SP, et al. Attenuated type II TGF-beta receptor signalling in human malignant oral keratinocytes induces a less differentiated and more aggressive phenotype that is associated with metastatic dissemination. Int J. Cancer. 2004;110:170-176.
Not in our library10.1002/ijc.20111
851.
Hoosein NM, et al. Differential sensitivity of subclasses of human colon carcinoma cell lines to the growth inhibitory effects of transforming growth factor-beta 1. Exp. Cell Res. 1989;181:442-453.
Not in our library10.1016/0014-4827(89)90101-8
852.
Takaku K, et al. Intestinal tumorigenesis in compound mutant mice of both Dpc4 (Smad4) and Apc genes. Cell. 1998;92:645-656.
Not in our library10.1016/s0092-8674(00)81132-0
853.
Tumour-derived TGF-β1 modulates myofibroblast differentiation and promotes HGF/SF-dependent invasion of squamous carcinoma cells · 2004
No notice
854.
Stuelten CH, et al. Transient tumor-fibroblast interactions increase tumor cell malignancy by a TGF-Beta mediated mechanism in a mouse xenograft model of breast cancer. PLoS One. 2010;5:e9832.
Not in our library10.1371/journal.pone.0009832
855.
Löhr M, et al. Transforming growth factor-beta1 induces desmoplasia in an experimental model of human pancreatic carcinoma. Cancer Res. 2001;61:550-555.
Not in our library
856.
Igarashi A, Okochi H, Bradham DM, Grotendorst GR. Regulation of connective tissue growth factor gene expression in human skin fibroblasts and during wound repair. Mol. Biol. Cell. 1993;4:637-645.
Not in our library10.1091/mbc.4.6.637
857.
Chantry D, Turner M, Abney E, Feldmann M. Modulation of cytokine production by transforming growth factor-beta. J. Immunol. 1989;142:4295-4300.
Not in our library10.4049/jimmunol.142.12.4295
858.
Sieuwerts AM, Klijn JG, Henzen-Logmans SC, Foekens JA. Cytokine-regulated urokinase-type-plasminogen-activator (uPA) production by human breast fibroblasts in vitro. Breast Cancer Res Treat. 1999;55:9-20.
Not in our library10.1023/a:1006190729866
859.
Cheng N, et al. Loss of TGF-beta type II receptor in fibroblasts promotes mammary carcinoma growth and invasion through upregulation of TGF-alpha-, MSP- and HGF-mediated signaling networks. Oncogene. 2005;24:5053-5068.
Not in our library10.1038/sj.onc.1208685
860.
Zeisberg EM, Potenta S, Xie L, Zeisberg M, Kalluri R. Discovery of endothelial to mesenchymal transition as a source for carcinoma-associated fibroblasts. Cancer Res. 2007;67:10123-10128.
Not in our library10.1158/0008-5472.can-07-3127
861.
Go C, Li P, Wang XJ. Blocking transforming growth factor beta signaling in transgenic epidermis accelerates chemical carcinogenesis: a mechanism associated with increased angiogenesis. Cancer Res. 1999;59:2861-2868.
Not in our library
862.
Ueki N, et al. Excessive production of transforming growth-factor beta 1 can play an important role in the development of tumorigenesis by its action for angiogenesis: validity of neutralizing antibodies to block tumor growth. Biochim Biophys. Acta. 1992;1137:189-196.
Not in our library10.1016/0167-4889(92)90201-l
863.
Padua D, et al. TGFbeta primes breast tumors for lung metastasis seeding through angiopoietin-like 4. Cell. 2008;133:66-77.
Not in our library10.1016/j.cell.2008.01.046
864.
Haak-Frendscho M, Wynn TA, Czuprynski CJ, Paulnock D. Transforming growth factor-beta 1 inhibits activation of macrophage cell line RAW 264.7 for cell killing. Clin. Exp. Immunol. 1990;82:404-410.
Not in our library10.1111/j.1365-2249.1990.tb05461.x
865.
Torre-Amione G, et al. A highly immunogenic tumor transfected with a murine transforming growth factor type beta 1 cDNA escapes immune surveillance. Proc. Natl Acad. Sci. USA. 1990;87:1486-1490.
Not in our library10.1073/pnas.87.4.1486
866.
Donkor MK, Sarkar A, Li MO. Tgf-β1 produced by activated CD4(+) T Cells Antagonizes T Cell Surveillance of Tumor Development. Oncoimmunology. 2012;1:162-171.
Not in our library10.4161/onci.1.2.18481
867.
Sarkar A, Donkor MK, Li MO. T cell- but not tumor cell-produced TGF-β1 promotes the development of spontaneous mammary cancer. Oncotarget. 2011;2:1339-1351.
Not in our library10.18632/oncotarget.403
868.
Arteaga CL, et al. Anti-transforming growth factor (TGF)-beta antibodies inhibit breast cancer cell tumorigenicity and increase mouse spleen natural killer cell activity. Implications for a possible role of tumor cell/host TGF-beta interactions in human breast cancer progression. J. Clin. Invest. 1993;92:2569-2576.
Not in our library10.1172/jci116871
869.
Ghiringhelli F, et al. Tumor cells convert immature myeloid dendritic cells into TGF-beta-secreting cells inducing CD4+CD25+ regulatory T cell proliferation. J. Exp. Med. 2005;202:919-929.
Not in our library10.1084/jem.20050463
870.
Hsiao YW, et al. Interactions of host IL-6 and IFN-gamma and cancer-derived TGF-beta1 on MHC molecule expression during tumor spontaneous regression. Cancer Immunol. Immunother. 2008;57:1091-1104.
Not in our library10.1007/s00262-007-0446-5
871.
Czarniecki CW, Chiu HH, Wong GH, McCabe SM, Palladino MA. Transforming growth factor-beta 1 modulates the expression of class II histocompatibility antigens on human cells. J. Immunol. 1988;140:4217-4223.
Not in our library10.4049/jimmunol.140.12.4217
872.
Ma D, Niederkorn JY. Transforming growth factor-beta down-regulates major histocompatibility complex class I antigen expression and increases the susceptibility of uveal melanoma cells to natural killer cell-mediated cytolysis. Immunology. 1995;86:263-269.
Not in our library
873.
Bogdahn U, et al. Targeted therapy for high-grade glioma with the TGF-beta2 inhibitor trabedersen: results of a randomized and controlled phase IIb study. Neuro Oncol. 2011;13:132-142.
Not in our library10.1093/neuonc/noq142
874.
Niu NK, et al. Novel targeting of PEGylated liposomes for codelivery of TGF-β1 siRNA and four antitubercular drugs to human macrophages for the treatment of mycobacterial infection: a quantitative proteomic study. Drug Des. Devel Ther. 2015;9:4441-4470.
Not in our library10.2147/dddt.s79369
875.
Yang Z, et al. Preparation, characterization, and in-vitro cytotoxicity of nanoliposomes loaded with anti-tubercular drugs and TGF-β1 siRNA for improving spinal tuberculosis therapy. BMC Infect. Dis. 2022;22:824.
Not in our library10.1186/s12879-022-07791-8
876.
Guoyou Z, et al. Modulation of transforming growth factor-beta1 production by vector-based RNAi in hypertrophic scar fibroblasts: a therapeutic potential strategy for hypertrophic scar. J. Dermatol Sci. 2007;48:67-70.
Not in our library10.1016/j.jdermsci.2007.06.009
877.
Loiselle AE, et al. Development of antisense oligonucleotide (ASO) technology against Tgf-β signaling to prevent scarring during flexor tendon repair. J. Orthop. Res. 2015;33:859-866.
Not in our library10.1002/jor.22890
878.
Jeong HS, et al. Effect of antisense TGF-beta1 oligodeoxynucleotides in streptozotocin- induced diabetic rat kidney. J. Korean Med Sci. 2004;19:374-383.
Not in our library10.3346/jkms.2004.19.3.374
879.
Isaka Y, et al. Transforming growth factor-beta 1 antisense oligodeoxynucleotides block interstitial fibrosis in unilateral ureteral obstruction. Kidney Int. 2000;58:1885-1892.
Not in our library10.1111/j.1523-1755.2000.00360.x
880.
Han DC, Hoffman BB, Hong SW, Guo J, Ziyadeh FN. Therapy with antisense TGF-beta1 oligodeoxynucleotides reduces kidney weight and matrix mRNAs in diabetic mice. Am. J. Physiol. Ren. Physiol. 2000;278:F628-F634.
Not in our library10.1152/ajprenal.2000.278.4.f628
881.
Akagi Y, et al. Inhibition of TGF-beta 1 expression by antisense oligonucleotides suppressed extracellular matrix accumulation in experimental glomerulonephritis. Kidney Int. 1996;50:148-155.
Not in our library10.1038/ki.1996.297
882.
Giaccone G, et al. A phase III study of belagenpumatucel-L, an allogeneic tumour cell vaccine, as maintenance therapy for non-small cell lung cancer. Eur. J. Cancer. 2015;51:2321-2329.
Not in our library10.1016/j.ejca.2015.07.035
883.
Olivares J, et al. Phase I trial of TGF-beta 2 antisense GM-CSF gene-modified autologous tumor cell (TAG) vaccine. Clin. Cancer Res. 2011;17:183-192.
Not in our library10.1158/1078-0432.ccr-10-2195
884.
Senzer N, et al. Phase I trial of “bi-shRNAi(furin)/GMCSF DNA/autologous tumor cell” vaccine (FANG) in advanced cancer. Mol. Ther. 2012;20:679-686.
Not in our library10.1038/mt.2011.269
885.
Rocconi RP, et al. Gemogenovatucel-T (Vigil) immunotherapy demonstrates clinical benefit in homologous recombination proficient (HRP) ovarian cancer. Gynecol. Oncol. 2021;161:676-680.
Not in our library10.1016/j.ygyno.2021.03.009
886.
Martin CJ, et al. Selective inhibition of TGFbeta1 activation overcomes primary resistance to checkpoint blockade therapy by altering tumor immune landscape. Sci. Transl. Med. 2020;12:eaay8456.
Not in our library10.1126/scitranslmed.aay8456
887.
Welsh BT, et al. Nonclinical Development of SRK-181: An Anti-Latent TGFbeta1 Monoclonal Antibody for the Treatment of Locally Advanced or Metastatic Solid Tumors. Int J. Toxicol. 2021;40:226-241.
Not in our library10.1177/1091581821998945
888.
Li A, et al. Selective targeting of GARP-LTGFbeta axis in the tumor microenvironment augments PD-1 blockade via enhancing CD8(+) T cell antitumor immunity. J. Immunother. Cancer. 2022;10:e005433.
Not in our library10.1136/jitc-2022-005433
889.
Elez E, et al. Abituzumab combined with cetuximab plus irinotecan versus cetuximab plus irinotecan alone for patients with KRAS wild-type metastatic colorectal cancer: the randomised phase I/II POSEIDON trial. Ann. Oncol. 2015;26:132-140.
Not in our library10.1093/annonc/mdu474
890.
Hussain M, et al. Differential Effect on Bone Lesions of Targeting Integrins: Randomized Phase II Trial of Abituzumab in Patients with Metastatic Castration-Resistant Prostate Cancer. Clin. Cancer Res. 2016;22:3192-3200.
Not in our library10.1158/1078-0432.ccr-15-2512
891.
Khanna D, et al. STRATUS: A Phase II Study of Abituzumab in Patients With Systemic Sclerosis-associated Interstitial Lung Disease. J. Rheumatol. 2021;48:1295-1298.
Not in our library10.3899/jrheum.191365
892.
Uhl W, Zuhlsdorf M, Koernicke T, Forssmann U, Kovar A. Safety, tolerability, and pharmacokinetics of the novel alphav-integrin antibody EMD 525797 (DI17E6) in healthy subjects after ascending single intravenous doses. Invest N. Drugs. 2014;32:347-354.
Not in our library10.1007/s10637-013-0038-5
893.
Manegold C, et al. Randomized phase II study of three doses of the integrin inhibitor cilengitide versus docetaxel as second-line treatment for patients with advanced non-small-cell lung cancer. Invest N. Drugs. 2013;31:175-182.
Not in our library10.1007/s10637-012-9842-6
894.
Vansteenkiste J, et al. Cilengitide combined with cetuximab and platinum-based chemotherapy as first-line treatment in advanced non-small-cell lung cancer (NSCLC) patients: results of an open-label, randomized, controlled phase II study (CERTO). Ann. Oncol. 2015;26:1734-1740.
Not in our library10.1093/annonc/mdv219
895.
Vermorken JB, et al. Cisplatin, 5-fluorouracil, and cetuximab (PFE) with or without cilengitide in recurrent/metastatic squamous cell carcinoma of the head and neck: results of the randomized phase I/II ADVANTAGE trial (phase II part). Ann. Oncol. 2014;25:682-688.
Not in our library10.1093/annonc/mdu003
896.
Stupp R, et al. Phase I/IIa study of cilengitide and temozolomide with concomitant radiotherapy followed by cilengitide and temozolomide maintenance therapy in patients with newly diagnosed glioblastoma. J. Clin. Oncol. 2010;28:2712-2718.
Not in our library10.1200/jco.2009.26.6650
897.
Reardon DA, et al. Randomized phase II study of cilengitide, an integrin-targeting arginine-glycine-aspartic acid peptide, in recurrent glioblastoma multiforme. J. Clin. Oncol. 2008;26:5610-5617.
Not in our library10.1200/jco.2008.16.7510
898.
Nabors LB, et al. A safety run-in and randomized phase 2 study of cilengitide combined with chemoradiation for newly diagnosed glioblastoma (NABTT 0306). Cancer. 2012;118:5601-5607.
Not in our library10.1002/cncr.27585
899.
Gilbert MR, et al. Cilengitide in patients with recurrent glioblastoma: the results of NABTC 03-02, a phase II trial with measures of treatment delivery. J. Neurooncol. 2012;106:147-153.
Not in our library10.1007/s11060-011-0650-1
900.
MacDonald TJ, et al. Phase II study of cilengitide in the treatment of refractory or relapsed high-grade gliomas in children: a report from the Children’s Oncology Group. Neuro Oncol. 2013;15:1438-1444.
Not in our library10.1093/neuonc/not058
901.
Nabors LB, et al. Two cilengitide regimens in combination with standard treatment for patients with newly diagnosed glioblastoma and unmethylated MGMT gene promoter: results of the open-label, controlled, randomized phase II CORE study. Neuro Oncol. 2015;17:708-717.
Not in our library10.1093/neuonc/nou356
902.
Khasraw M, et al. Cilengitide with metronomic temozolomide, procarbazine, and standard radiotherapy in patients with glioblastoma and unmethylated MGMT gene promoter in ExCentric, an open-label phase II trial. J. Neurooncol. 2016;128:163-171.
Not in our library10.1007/s11060-016-2094-0
903.
Stupp R, et al. Cilengitide combined with standard treatment for patients with newly diagnosed glioblastoma with methylated MGMT promoter (CENTRIC EORTC 26071-22072 study): a multicentre, randomised, open-label, phase 3 trial. Lancet Oncol. 2014;15:1100-1108.
Not in our library10.1016/s1470-2045(14)70379-1
904.
Kim KB, et al. A randomized phase II study of cilengitide (EMD 121974) in patients with metastatic melanoma. Melanoma Res. 2012;22:294-301.
Not in our library10.1097/cmr.0b013e32835312e4
905.
Friess H, et al. A randomized multi-center phase II trial of the angiogenesis inhibitor Cilengitide (EMD 121974) and gemcitabine compared with gemcitabine alone in advanced unresectable pancreatic cancer. BMC Cancer. 2006;6:285.
Not in our library10.1186/1471-2407-6-285
906.
Bradley DA, et al. Cilengitide (EMD 121974, NSC 707544) in asymptomatic metastatic castration resistant prostate cancer patients: a randomized phase II trial by the prostate cancer clinical trials consortium. Invest N. Drugs. 2011;29:1432-1440.
Not in our library10.1007/s10637-010-9420-8
907.
Alva A, et al. Phase II study of cilengitide (EMD 121974, NSC 707544) in patients with non-metastatic castration resistant prostate cancer, NCI-6735. A study by the DOD/PCF prostate cancer clinical trials consortium. Invest N. Drugs. 2012;30:749-757.
Not in our library10.1007/s10637-010-9573-5
908.
Li C, et al. Increased activation of latent TGF-β1 by αVβ3 in human Crohn’s disease and fibrosis in TNBS colitis can be prevented by cilengitide. Inflamm. Bowel Dis. 2013;19:2829-2839.
Not in our library10.1097/mib.0b013e3182a8452e
909.
Bagnato GL, et al. Dual αvβ3 and αvβ5 blockade attenuates fibrotic and vascular alterations in a murine model of systemic sclerosis. Clin. Sci. (Lond.). 2018;132:231-242.
Not in our library10.1042/cs20171426
910.
MacDonald WJ, et al. Broad spectrum integrin inhibitor GLPG-0187 bypasses immune evasion in colorectal cancer by TGF-β signaling mediated downregulation of PD-L1. Am. J. Cancer Res. 2023;13:2938-2947.
Not in our library
911.
Verschleiser B, et al. Pan-integrin inhibitor GLPG-0187 promotes T-cell killing of mismatch repair-deficient colorectal cancer cells by suppression of SMAD/TGF-β signaling. Am. J. Cancer Res. 2023;13:2878-2885.
Not in our library
912.
Belmadani S, et al. A thrombospondin-1 antagonist of transforming growth factor-beta activation blocks cardiomyopathy in rats with diabetes and elevated angiotensin II. Am. J. Pathol. 2007;171:777-789.
Not in our library10.2353/ajpath.2007.070056
913.
Ruschkowski BA, et al. Thrombospondin-1 Plays a Major Pathogenic Role in Experimental and Human Bronchopulmonary Dysplasia. Am. J. Respir. Crit. Care Med. 2022;205:685-699.
Not in our library10.1164/rccm.202104-1021oc
914.
Song S, et al. Sestrin2 remedies podocyte injury via orchestrating TSP-1/TGF-β1/Smad3 axis in diabetic kidney disease. Cell Death Dis. 2022;13:663.
Not in our library10.1038/s41419-022-05120-0
915.
Xie XS, et al. LSKL, a peptide antagonist of thrombospondin-1, attenuates renal interstitial fibrosis in rats with unilateral ureteral obstruction. Arch. Pharm. Res. 2010;33:275-284.
Not in our library10.1007/s12272-010-0213-6
916.
Lu A, Miao M, Schoeb TR, Agarwal A, Murphy-Ullrich JE. Blockade of TSP1-dependent TGF-β activity reduces renal injury and proteinuria in a murine model of diabetic nephropathy. Am. J. Pathol. 2011;178:2573-2586.
Not in our library10.1016/j.ajpath.2011.02.039
917.
Zhang Y, et al. P2Y4/TSP-1/TGF-β1/pSmad2/3 pathway contributes to acute generalized seizures induced by kainic acid. Brain Res Bull. 2019;149:106-119.
Not in our library10.1016/j.brainresbull.2019.04.004
918.
Liao F, et al. LSKL peptide alleviates subarachnoid fibrosis and hydrocephalus by inhibiting TSP1-mediated TGF-β1 signaling activity following subarachnoid hemorrhage in rats. Exp. Ther. Med. 2016;12:2537-2543.
Not in our library10.3892/etm.2016.3640
919.
Jiang N, et al. Blockade of thrombospondin-1 ameliorates high glucose-induced peritoneal fibrosis through downregulation of TGF-β1/Smad3 signaling pathway. J. Cell Physiol. 2020;235:364-379.
Not in our library10.1002/jcp.28976
920.
Narmada BC, Chia SM, Tucker-Kellogg L, Yu H. HGF regulates the activation of TGF-β1 in rat hepatocytes and hepatic stellate cells. J. Cell Physiol. 2013;228:393-401.
Not in our library10.1002/jcp.24143
921.
Kondou H, et al. A blocking peptide for transforming growth factor-beta1 activation prevents hepatic fibrosis in vivo. J. Hepatol. 2003;39:742-748.
Not in our library10.1016/s0168-8278(03)00377-5
922.
Xu X, et al. Investigating the potential of LSKL peptide as a novel hypertrophic scar treatment. Biomed. Pharmacother. 2020;124:109824.
Not in our library10.1016/j.biopha.2020.109824
923.
Kuroki H, et al. Effect of LSKL peptide on thrombospondin 1-mediated transforming growth factor β signal activation and liver regeneration after hepatectomy in an experimental model. Br. J. Surg. 2015;102:813-825.
Not in our library10.1002/bjs.9765
924.
Lu A, et al. Inhibition of Transforming Growth Factor-β Activation Diminishes Tumor Progression and Osteolytic Bone Disease in Mouse Models of Multiple Myeloma. Am. J. Pathol. 2016;186:678-690.
Not in our library10.1016/j.ajpath.2015.11.003
925.
Fu PY, et al. Far upstream element-binding protein 1 facilitates hepatocellular carcinoma invasion and metastasis. Carcinogenesis. 2020;41:950-960.
Not in our library10.1093/carcin/bgz171
926.
Gu J, et al. Irradiation induces DJ-1 secretion from esophageal squamous cell carcinoma cells to accelerate metastasis of bystander cells via a TGF-β1 positive feedback loop. J. Exp. Clin. Cancer Res. 2022;41:259.
Not in our library10.1186/s13046-022-02471-6
927.
Daniel C, et al. Antisense oligonucleotides against thrombospondin-1 inhibit activation of tgf-beta in fibrotic renal disease in the rat in vivo. Am. J. Pathol. 2003;163:1185-1192.
Not in our library10.1016/s0002-9440(10)63478-5
928.
Agin M, Yucel A, Gumus M, Yuksekkaya HA, Tumgor G. The Effect of Enteral Nutrition Support Rich in TGF-β in the Treatment of Inflammatory Bowel Disease in Childhood. Med. (Kaunas.). 2019;55:620.
Not in our library10.3390/medicina55100620
929.
Fell JM, et al. Mucosal healing and a fall in mucosal pro-inflammatory cytokine mRNA induced by a specific oral polymeric diet in paediatric Crohn’s disease. Aliment Pharm. Ther. 2000;14:281-289.
Not in our library10.1046/j.1365-2036.2000.00707.x
930.
Hartman C, et al. Nutritional supplementation with polymeric diet enriched with transforming growth factor-beta 2 for children with Crohn’s disease. Isr. Med Assoc. J. 2008;10:503-507.
Not in our library
931.
Ferreira TMR, et al. Effect of Oral Nutrition Supplements and TGF-β2 on Nutrition and Inflammatory Patterns in Patients With Active Crohn’s Disease. Nutr. Clin. Pr. 2020;35:885-893.
Not in our library10.1002/ncp.10448
932.
Borrelli O, et al. Polymeric diet alone versus corticosteroids in the treatment of active pediatric Crohn’s disease: a randomized controlled open-label trial. Clin. Gastroenterol. Hepatol. 2006;4:744-753.
Not in our library10.1016/j.cgh.2006.03.010
933.
Pigneur B, et al. Mucosal Healing and Bacterial Composition in Response to Enteral Nutrition Vs Steroid-based Induction Therapy-A Randomised Prospective Clinical Trial in Children With Crohn’s Disease. J. Crohns Colitis. 2019;13:846-855.
Not in our library10.1093/ecco-jcc/jjy207
934.
Beaupel N, et al. Preoperative oral polymeric diet enriched with transforming growth factor-beta 2 (Modulen) could decrease postoperative morbidity after surgery for complicated ileocolonic Crohn’s disease. Scand. J. Gastroenterol. 2017;52:5-10.
Not in our library10.1080/00365521.2016.1221994
935.
Okamoto A, et al. Suppression of serum IgE response and systemic anaphylaxis in a food allergy model by orally administered high-dose TGF-beta. Int Immunol. 2005;17:705-712.
Not in our library10.1093/intimm/dxh250
936.
Rekima A, et al. Long-term reduction in food allergy susceptibility in mice by combining breastfeeding-induced tolerance and TGF-β-enriched formula after weaning. Clin. Exp. Allergy. 2017;47:565-576.
Not in our library10.1111/cea.12864
937.
Penttila I. Effects of transforming growth factor-beta and formula feeding on systemic immune responses to dietary beta-lactoglobulin in allergy-prone rats. Pediatr. Res. 2006;59:650-655.
Not in our library10.1203/01.pdr.0000203149.75465.74
938.
Verhasselt V. Neonatal tolerance under breastfeeding influence: the presence of allergen and transforming growth factor-beta in breast milk protects the progeny from allergic asthma. J. Pediatr. 2010;156:S16-S20.
Not in our library10.1016/j.jpeds.2009.11.015
939.
Morita Y, et al. TGF-β Concentration in Breast Milk is Associated With the Development of Eczema in Infants. Front Pediatr. 2018;6:162.
Not in our library10.3389/fped.2018.00162
940.
Saarinen KM, Vaarala O, Klemetti P, Savilahti E. Transforming growth factor-beta1 in mothers’ colostrum and immune responses to cows’ milk proteins in infants with cows’ milk allergy. J. Allergy Clin. Immunol. 1999;104:1093-1098.
Not in our library10.1016/s0091-6749(99)70094-1
941.
Ferguson MW, et al. Prophylactic administration of avotermin for improvement of skin scarring: three double-blind, placebo-controlled, phase I/II studies. Lancet. 2009;373:1264-1274.
Not in our library10.1016/s0140-6736(09)60322-6
942.
So K, et al. Avotermin for scar improvement following scar revision surgery: a randomized, double-blind, within-patient, placebo-controlled, phase II clinical trial. Plast. Reconstr. Surg. 2011;128:163-172.
Not in our library10.1097/prs.0b013e318217429b
943.
Bush J, et al. Scar-improving efficacy of avotermin administered into the wound margins of skin incisions as evaluated by a randomized, double-blind, placebo-controlled, phase II clinical trial. Plast. Reconstr. Surg. 2010;126:1604-1615.
Not in our library10.1097/prs.0b013e3181ef8e66
944.
McCollum PT, et al. Randomized phase II clinical trial of avotermin versus placebo for scar improvement. Br. J. Surg. 2011;98:925-934.
Not in our library10.1002/bjs.7438
945.
Robson MC, et al. Safety and effect of transforming growth factor-beta(2) for treatment of venous stasis ulcers. Wound Repair Regen. 1995;3:157-167.
Not in our library10.1046/j.1524-475x.1995.30207.x
946.
Wang X, et al. Demineralized bone matrix combined bone marrow mesenchymal stem cells, bone morphogenetic protein-2 and transforming growth factor-β3 gene promoted pig cartilage defect repair. PLoS One. 2014;9:e116061.
Not in our library10.1371/journal.pone.0116061
947.
Luo Z, et al. Mechano growth factor (MGF) and transforming growth factor (TGF)-β3 functionalized silk scaffolds enhance articular hyaline cartilage regeneration in rabbit model. Biomaterials. 2015;52:463-475.
Not in our library10.1016/j.biomaterials.2015.01.001
948.
Kuruvilla AP, et al. Protective effect of transforming growth factor beta 1 on experimental autoimmune diseases in mice. Proc. Natl Acad. Sci. USA. 1991;88:2918-2921.
Not in our library10.1073/pnas.88.7.2918
949.
Srivastava V, Khanna M, Sharma S, Kumar B. Resolution of immune response by recombinant transforming growth factor-beta (rTGF-β) during influenza A virus infection. Indian J. Med Res. 2012;136:641-648.
Not in our library
950.
Phase I Study of GC1008 (Fresolimumab): A Human Anti-Transforming Growth Factor-Beta (TGFβ) Monoclonal Antibody in Patients with Advanced Malignant Melanoma or Renal Cell Carcinoma · 2014
No notice
951.
Formenti SC, et al. Focal Irradiation and Systemic TGFbeta Blockade in Metastatic Breast Cancer. Clin. Cancer Res. 2018;24:2493-2504.
Not in our library10.1158/1078-0432.ccr-17-3322
952.
Rice LM, et al. Fresolimumab treatment decreases biomarkers and improves clinical symptoms in systemic sclerosis patients. J. Clin. Invest. 2015;125:2795-2807.
Not in our library10.1172/jci77958
953.
Trachtman H, et al. A phase 1, single-dose study of fresolimumab, an anti-TGF-beta antibody, in treatment-resistant primary focal segmental glomerulosclerosis. Kidney Int. 2011;79:1236-1243.
Not in our library10.1038/ki.2011.33
954.
Lacouture ME, et al. Cutaneous keratoacanthomas/squamous cell carcinomas associated with neutralization of transforming growth factor beta by the monoclonal antibody fresolimumab (GC1008). Cancer Immunol. Immunother. 2015;64:437-446.
Not in our library10.1007/s00262-015-1653-0
955.
Bauer TM, et al. Phase I/Ib, open-label, multicenter, dose-escalation study of the anti-TGF-β monoclonal antibody, NIS793, in combination with spartalizumab in adult patients with advanced tumors. J. Immunother. Cancer. 2023;11:e007353.
Not in our library10.1136/jitc-2023-007353
956.
Denton CP, et al. Recombinant human anti-transforming growth factor beta1 antibody therapy in systemic sclerosis: a multicenter, randomized, placebo-controlled phase I/II trial of CAT-192. Arthritis Rheum. 2007;56:323-333.
Not in our library10.1002/art.22289
957.
Voelker J, et al. Anti-TGF-β1 Antibody Therapy in Patients with Diabetic Nephropathy. J. Am. Soc. Nephrol. 2017;28:953-962.
Not in our library10.1681/asn.2015111230
958.
Mascarenhas J, et al. A Phase Ib Trial of AVID200, a TGFβ 1/3 Trap, in Patients with Myelofibrosis. Clin. Cancer Res. 2023;29:3622-3632.
Not in our library10.1158/1078-0432.ccr-23-0276
959.
Li Y, et al. Neutralization of excessive levels of active TGF-β1 reduces MSC recruitment and differentiation to mitigate peritendinous adhesion. Bone Res. 2023;11:24.
Not in our library10.1038/s41413-023-00252-1
960.
Lu L, et al. The temporal effects of anti-TGF-beta1, 2, and 3 monoclonal antibody on wound healing and hypertrophic scar formation. J. Am. Coll. Surg. 2005;201:391-397.
Not in our library10.1016/j.jamcollsurg.2005.03.032
961.
Wang L, et al. Aberrant Transforming Growth Factor-β Activation Recruits Mesenchymal Stem Cells During Prostatic Hyperplasia. Stem Cells Transl. Med. 2017;6:394-404.
Not in our library10.5966/sctm.2015-0411
962.
Deng S, Zhang H, Han W, Guo C, Deng C. Transforming Growth Factor-β-Neutralizing Antibodies Improve Alveolarization in the Oxygen-Exposed Newborn Mouse Lung. J. Interferon Cytokine Res. 2019;39:106-116.
Not in our library10.1089/jir.2018.0080
963.
Nelson CA, et al. Inhibiting TGF-β activity improves respiratory function in mdx mice. Am. J. Pathol. 2011;178:2611-2621.
Not in our library10.1016/j.ajpath.2011.02.024
964.
Cook JR, et al. Dimorphic effects of transforming growth factor-β signaling during aortic aneurysm progression in mice suggest a combinatorial therapy for Marfan syndrome. Arterioscler Thromb. Vasc. Biol. 2015;35:911-917.
Not in our library10.1161/atvbaha.114.305150
965.
Wang X, et al. Aberrant TGF-β activation in bone tendon insertion induces enthesopathy-like disease. J. Clin. Invest. 2018;128:846-860.
Not in our library10.1172/jci96186
966.
Becerikli M, et al. TGF-beta pathway inhibition as the therapeutic acceleration of diabetic bone regeneration. J. Orthop. Res. 2022;40:1810-1826.
Not in our library10.1002/jor.25212
967.
Sahbani K, Cardozo CP, Bauman WA, Tawfeek HA. Inhibition of TGF-β Signaling Attenuates Disuse-induced Trabecular Bone Loss After Spinal Cord Injury in Male Mice. Endocrinology. 2022;163:bqab230.
Not in our library10.1210/endocr/bqab230
968.
Grafe I, et al. Excessive transforming growth factor-β signaling is a common mechanism in osteogenesis imperfecta. Nat. Med. 2014;20:670-675.
Not in our library10.1038/nm.3544
969.
Wahl SM, Allen JB, Costa GL, Wong HL, Dasch JR. Reversal of acute and chronic synovial inflammation by anti-transforming growth factor beta. J. Exp. Med. 1993;177:225-230.
Not in our library10.1084/jem.177.1.225
970.
Xie L, et al. Systemic neutralization of TGF-β attenuates osteoarthritis. Ann. N. Y Acad. Sci. 2016;1376:53-64.
Not in our library10.1111/nyas.13000
971.
Ferreira RR, et al. In Chagas disease, transforming growth factor beta neutralization reduces Trypanosoma cruzi infection and improves cardiac performance. Front Cell Infect. Microbiol. 2022;12:1017040.
Not in our library10.3389/fcimb.2022.1017040
972.
Bifunctional immune checkpoint-targeted antibody-ligand traps that simultaneously disable TGFβ enhance the efficacy of cancer immunotherapy · 2018
No notice
973.
Paz-Ares L, et al. Bintrafusp Alfa, a Bifunctional Fusion Protein Targeting TGF-beta and PD-L1, in Second-Line Treatment of Patients With NSCLC: Results From an Expansion Cohort of a Phase 1 Trial. J. Thorac. Oncol. 2020;15:1210-1222.
Not in our library10.1016/j.jtho.2020.03.003
974.
Kang YK, et al. Safety and Tolerability of Bintrafusp Alfa, a Bifunctional Fusion Protein Targeting TGFbeta and PD-L1, in Asian Patients with Pretreated Recurrent or Refractory Gastric Cancer. Clin. Cancer Res. 2020;26:3202-3210.
Not in our library10.1158/1078-0432.ccr-19-3806
975.
Yoo C, et al. Phase I study of bintrafusp alfa, a bifunctional fusion protein targeting TGF-beta and PD-L1, in patients with pretreated biliary tract cancer. J. Immunother. Cancer. 2020;8:e000564.
Not in our library10.1136/jitc-2020-000564
976.
Redman JM, et al. Enhanced neoepitope-specific immunity following neoadjuvant PD-L1 and TGF-beta blockade in HPV-unrelated head and neck cancer. J. Clin. Invest. 2022;132:e161400.
Not in our library10.1172/jci161400
977.
Strauss J, et al. Phase I Trial of M7824 (MSB0011359C), a Bifunctional Fusion Protein Targeting PD-L1 and TGFbeta, in Advanced Solid Tumors. Clin. Cancer Res. 2018;24:1287-1295.
Not in our library10.1158/1078-0432.ccr-17-2653
978.
Wu ZH, et al. Development of the Novel Bifunctional Fusion Protein BR102 That Simultaneously Targets PD-L1 and TGF-β for Anticancer Immunotherapy. Cancers (Basel). 2022;14:4964.
Not in our library10.3390/cancers14194964
979.
Chen X, et al. Secretion of bispecific protein of anti-PD-1 fused with TGF-beta trap enhances antitumor efficacy of CAR-T cell therapy. Mol. Ther. Oncolyt. 2021;21:144-157.
Not in our library10.1016/j.omto.2021.03.014
980.
Fukushima K, et al. The use of an antifibrosis agent to improve muscle recovery after laceration. Am. J. Sports Med. 2001;29:394-402.
Not in our library10.1177/03635465010290040201
981.
Ruehle MA, et al. Decorin-supplemented collagen hydrogels for the co-delivery of bone morphogenetic protein-2 and microvascular fragments to a composite bone-muscle injury model with impaired vascularization. Acta Biomater. 2019;93:210-221.
Not in our library10.1016/j.actbio.2019.01.045
982.
Ahmed Z, et al. Decorin blocks scarring and cystic cavitation in acute and induces scar dissolution in chronic spinal cord wounds. Neurobiol. Dis. 2014;64:163-176.
Not in our library10.1016/j.nbd.2013.12.008
983.
Qiu SS, Dotor J, Hontanilla B. Effect of P144® (Anti-TGF-β) in an “In Vivo” Human Hypertrophic Scar Model in Nude Mice. PLoS One. 2015;10:e0144489.
Not in our library10.1371/journal.pone.0144489
984.
Arce C, et al. Anti-TGFβ (Transforming Growth Factor β) Therapy With Betaglycan-Derived P144 Peptide Gene Delivery Prevents the Formation of Aortic Aneurysm in a Mouse Model of Marfan Syndrome. Arterioscler Thromb. Vasc. Biol. 2021;41:e440-e452.
Not in our library10.1161/atvbaha.121.316496
985.
Li L, et al. Postinfarction gene therapy with adenoviral vector expressing decorin mitigates cardiac remodeling and dysfunction. Am. J. Physiol. Heart Circ. Physiol. 2009;297:H1504-H1513.
Not in our library10.1152/ajpheart.00194.2009
986.
Yan W, et al. Decorin gene delivery inhibits cardiac fibrosis in spontaneously hypertensive rats by modulation of transforming growth factor-beta/Smad and p38 mitogen-activated protein kinase signaling pathways. Hum. Gene Ther. 2009;20:1190-1200.
Not in our library10.1089/hum.2008.204
987.
Hermida N, et al. A synthetic peptide from transforming growth factor-beta1 type III receptor prevents myocardial fibrosis in spontaneously hypertensive rats. Cardiovasc Res. 2009;81:601-609.
Not in our library10.1093/cvr/cvn315
988.
Nili N, et al. Decorin inhibition of PDGF-stimulated vascular smooth muscle cell function: potential mechanism for inhibition of intimal hyperplasia after balloon angioplasty. Am. J. Pathol. 2003;163:869-878.
Not in our library10.1016/s0002-9440(10)63447-5
989.
Recalde S, et al. Transforming growth factor-β inhibition decreases diode laser-induced choroidal neovascularization development in rats: P17 and P144 peptides. Invest Ophthalmol. Vis. Sci. 2011;52:7090-7097.
Not in our library10.1167/iovs.11-7300
990.
Aojula A, et al. Diffusion tensor imaging with direct cytopathological validation: characterisation of decorin treatment in experimental juvenile communicating hydrocephalus. Fluids Barriers CNS. 2016;13:9.
Not in our library10.1186/s12987-016-0033-2
991.
Botfield H, et al. Decorin prevents the development of juvenile communicating hydrocephalus. Brain. 2013;136:2842-2858.
Not in our library10.1093/brain/awt203
992.
Murillo-Cuesta S, et al. Transforming growth factor β1 inhibition protects from noise-induced hearing loss. Front Aging Neurosci. 2015;7:32.
Not in our library10.3389/fnagi.2015.00032
993.
Border WA, et al. Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Nature. 1992;360:361-364.
Not in our library10.1038/360361a0
994.
Juárez P, et al. Soluble betaglycan reduces renal damage progression in db/db mice. Am. J. Physiol. Ren. Physiol. 2007;292:F321-F329.
Not in our library10.1152/ajprenal.00264.2006
995.
Baltanás A, et al. A synthetic peptide from transforming growth factor-β1 type III receptor inhibits NADPH oxidase and prevents oxidative stress in the kidney of spontaneously hypertensive rats. Antioxid. Redox Signal. 2013;19:1607-1618.
Not in our library10.1089/ars.2012.4653
996.
Li D, et al. TGF-β1 peptide-based inhibitor P144 ameliorates renal fibrosis after ischemia-reperfusion injury by modulating alternatively activated macrophages. Cell Prolif. 2022;55:e13299.
Not in our library10.1111/cpr.13299
997.
Zhang Y, McCormick LL, Gilliam AC. Latency-associated peptide prevents skin fibrosis in murine sclerodermatous graft-versus-host disease, a model for human scleroderma. J. Invest Dermatol. 2003;121:713-719.
Not in our library10.1046/j.1523-1747.2003.12517.x
998.
Jang YO, et al. Effect of Function-Enhanced Mesenchymal Stem Cells Infected With Decorin-Expressing Adenovirus on Hepatic Fibrosis. Stem Cells Transl. Med. 2016;5:1247-1256.
Not in our library10.5966/sctm.2015-0323
999.
Kolb M, Margetts PJ, Sime PJ, Gauldie J. Proteoglycans decorin and biglycan differentially modulate TGF-beta-mediated fibrotic responses in the lung. Am. J. Physiol. Lung Cell Mol. Physiol. 2001;280:L1327-L1334.
Not in our library10.1152/ajplung.2001.280.6.l1327
1000.
Ezquerro IJ, et al. A synthetic peptide from transforming growth factor beta type III receptor inhibits liver fibrogenesis in rats with carbon tetrachloride liver injury. Cytokine. 2003;22:12-20.
Not in our library10.1016/s1043-4666(03)00101-7
1001.
In vitro restoration of T cell responses in tuberculosis and augmentation of monocyte effector function against Mycobacterium tuberculosis by natural inhibitors of transforming growth factor β · 1997
Not checked
1002.
Bandyopadhyay A, et al. Antitumor activity of a recombinant soluble betaglycan in human breast cancer xenograft. Cancer Res. 2002;62:4690-4695.
Not in our library
1003.
Liu Z, et al. An Oncolytic Adenovirus Encoding Decorin and Granulocyte Macrophage Colony Stimulating Factor Inhibits Tumor Growth in a Colorectal Tumor Model by Targeting Pro-Tumorigenic Signals and via Immune Activation. Hum. Gene Ther. 2017;28:667-680.
Not in our library10.1089/hum.2017.033
1004.
Zhang W, et al. Efficacy of an Oncolytic Adenovirus Driven by a Chimeric Promoter and Armed with Decorin Against Renal Cell Carcinoma. Hum. Gene Ther. 2020;31:651-663.
Not in our library10.1089/hum.2019.352
1005.
Yang Y, et al. Systemic Delivery of an Oncolytic Adenovirus Expressing Decorin for the Treatment of Breast Cancer Bone Metastases. Hum. Gene Ther. 2015;26:813-825.
Not in our library10.1089/hum.2015.098
1006.
Narayan V, et al. PSMA-targeting TGFbeta-insensitive armored CAR T cells in metastatic castration-resistant prostate cancer: a phase 1 trial. Nat. Med. 2022;28:724-734.
Not in our library10.1038/s41591-022-01726-1
1007.
Wang FL, et al. TGF-beta insensitive dendritic cells: an efficient vaccine for murine prostate cancer. Cancer Immunol. Immunother. 2007;56:1785-1793.
Not in our library10.1007/s00262-007-0322-3
1008.
Tian F, et al. Vaccination with transforming growth factor-beta insensitive dendritic cells suppresses pulmonary metastases of renal carcinoma in mice. Cancer Lett. 2008;271:333-341.
Not in our library10.1016/j.canlet.2008.06.025
1009.
Reid RR, et al. Reduction of hypertrophic scar via retroviral delivery of a dominant negative TGF-beta receptor II. J. Plast. Reconstr. Aesthet. Surg. 2007;60:64-72.
Not in our library10.1016/j.bjps.2005.12.026
1010.
Santini V, et al. Phase II Study of the ALK5 Inhibitor Galunisertib in Very Low-, Low-, and Intermediate-Risk Myelodysplastic Syndromes. Clin. Cancer Res. 2019;25:6976-6985.
Not in our library10.1158/1078-0432.ccr-19-1338
1011.
Nadal E, et al. A phase Ib/II study of galunisertib in combination with nivolumab in solid tumors and non-small cell lung cancer. BMC Cancer. 2023;23:708.
Not in our library10.1186/s12885-023-11153-1
1012.
Kelley RK, et al. A Phase 2 Study of Galunisertib (TGF-beta1 Receptor Type I Inhibitor) and Sorafenib in Patients With Advanced Hepatocellular Carcinoma. Clin. Transl. Gastroenterol. 2019;10:e00056.
Not in our library10.14309/ctg.0000000000000056
1013.
Faivre S, et al. Novel transforming growth factor beta receptor I kinase inhibitor galunisertib (LY2157299) in advanced hepatocellular carcinoma. Liver Int. 2019;39:1468-1477.
Not in our library10.1111/liv.14113
1014.
Yamazaki T, et al. Galunisertib plus neoadjuvant chemoradiotherapy in patients with locally advanced rectal cancer: a single-arm, phase 2 trial. Lancet Oncol. 2022;23:1189-1200.
Not in our library10.1016/s1470-2045(22)00446-6
1015.
Galunisertib plus gemcitabine vs. gemcitabine for first-line treatment of patients with unresectable pancreatic cancer · 2018
No notice
1016.
Phase 1b/2a study of galunisertib, a small molecule inhibitor of transforming growth factor-beta receptor I, in combination with standard temozolomide-based radiochemotherapy in patients with newly diagnosed malignant glioma · 2020
No notice
1017.
Brandes AA, et al. A Phase II randomized study of galunisertib monotherapy or galunisertib plus lomustine compared with lomustine monotherapy in patients with recurrent glioblastoma. Neuro Oncol. 2016;18:1146-1156.
Not in our library10.1093/neuonc/now009
1018.
Kovacs RJ, et al. Cardiac Safety of TGF-beta Receptor I Kinase Inhibitor LY2157299 Monohydrate in Cancer Patients in a First-in-Human Dose Study. Cardiovasc Toxicol. 2015;15:309-323.
Not in our library10.1007/s12012-014-9297-4
1019.
Tolcher AW, et al. A phase 1 study of anti-TGFbeta receptor type-II monoclonal antibody LY3022859 in patients with advanced solid tumors. Cancer Chemother. Pharm. 2017;79:673-680.
Not in our library10.1007/s00280-017-3245-5
1020.
Suzuki E, et al. A novel small-molecule inhibitor of transforming growth factor beta type I receptor kinase (SM16) inhibits murine mesothelioma tumor growth in vivo and prevents tumor recurrence after surgical resection. Cancer Res. 2007;67:2351-2359.
Not in our library10.1158/0008-5472.can-06-2389
1021.
Uhl M, et al. SD-208, a novel transforming growth factor beta receptor I kinase inhibitor, inhibits growth and invasiveness and enhances immunogenicity of murine and human glioma cells in vitro and in vivo. Cancer Res. 2004;64:7954-7961.
Not in our library10.1158/0008-5472.can-04-1013
1022.
Tanaka H, et al. Transforming growth factor β signaling inhibitor, SB-431542, induces maturation of dendritic cells and enhances anti-tumor activity. Oncol. Rep. 2010;24:1637-1643.
Not in our library10.3892/or_00001028
1023.
Halder SK, Beauchamp RD, Datta PK. A specific inhibitor of TGF-beta receptor kinase, SB-431542, as a potent antitumor agent for human cancers. Neoplasia. 2005;7:509-521.
Not in our library10.1593/neo.04640
1024.
Lee JE, et al. Vactosertib, TGF-β receptor I inhibitor, augments the sensitization of the anti-cancer activity of gemcitabine in pancreatic cancer. Biomed. Pharmacother. 2023;162:114716.
Not in our library10.1016/j.biopha.2023.114716
1025.
Zhang P, et al. The programmed site-specific delivery of LY3200882 and PD-L1 siRNA boosts immunotherapy for triple-negative breast cancer by remodeling tumor microenvironment. Biomaterials. 2022;284:121518.
Not in our library10.1016/j.biomaterials.2022.121518
1026.
Chen J, et al. TGF-β Signaling Activation Confers Anlotinib Resistance in Gastric Cancer. Pharm. Res. 2023;40:689-699.
Not in our library10.1007/s11095-022-03461-1
1027.
Fu K, et al. SM16, an orally active TGF-beta type I receptor inhibitor prevents myofibroblast induction and vascular fibrosis in the rat carotid injury model. Arterioscler Thromb. Vasc. Biol. 2008;28:665-671.
Not in our library10.1161/atvbaha.107.158030
1028.
Engebretsen KV, et al. Attenuated development of cardiac fibrosis in left ventricular pressure overload by SM16, an orally active inhibitor of ALK5. J. Mol. Cell Cardiol. 2014;76:148-157.
Not in our library10.1016/j.yjmcc.2014.08.008
1029.
Atis M, et al. Targeting the blood-brain barrier disruption in hypertension by ALK5/TGF-Β type I receptor inhibitor SB-431542 and dynamin inhibitor dynasore. Brain Res. 2022;1794:148071.
Not in our library10.1016/j.brainres.2022.148071
1030.
Wu D, et al. TGF-β1-PML SUMOylation-peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) form a positive feedback loop to regulate cardiac fibrosis. J. Cell Physiol. 2019;234:6263-6273.
Not in our library10.1002/jcp.27357
1031.
Ha KB, et al. EW-7197 Attenuates the Progression of Diabetic Nephropathy in db/db Mice through Suppression of Fibrogenesis and Inflammation. Endocrinol. Metab. (Seoul.). 2022;37:96-111.
Not in our library10.3803/enm.2021.1305
1032.
Nassar K, et al. A TGF-β receptor 1 inhibitor for prevention of proliferative vitreoretinopathy. Exp. Eye Res. 2014;123:72-86.
Not in our library10.1016/j.exer.2014.04.006
1033.
Maeda S, Hayashi M, Komiya S, Imamura T, Miyazono K. Endogenous TGF-beta signaling suppresses maturation of osteoblastic mesenchymal cells. Embo j. 2004;23:552-563.
Not in our library10.1038/sj.emboj.7600067
1034.
Lee AJ, et al. Sustained Delivery of SB-431542, a Type I Transforming Growth Factor Beta-1 Receptor Inhibitor, to Prevent Arthrofibrosis. Tissue Eng. Part A. 2021;27:1411-1421.
Not in our library10.1089/ten.tea.2021.0029
1035.
Anscher MS, et al. Small molecular inhibitor of transforming growth factor-beta protects against development of radiation-induced lung injury. Int J. Radiat. Oncol. Biol. Phys. 2008;71:829-837.
Not in our library10.1016/j.ijrobp.2008.02.046
1036.
Park SA, et al. EW-7197 inhibits hepatic, renal, and pulmonary fibrosis by blocking TGF-β/Smad and ROS signaling. Cell Mol. Life Sci. 2015;72:2023-2039.
Not in our library10.1007/s00018-014-1798-6
1037.
Alyoussef A. Blocking TGF-β type 1 receptor partially reversed skin tissue damage in experimentally induced atopic dermatitis in mice. Cytokine. 2018;106:45-53.
Not in our library10.1016/j.cyto.2018.02.025
1038.
Binabaj MM, et al. EW-7197 prevents ulcerative colitis-associated fibrosis and inflammation. J. Cell Physiol. 2019;234:11654-11661.
Not in our library10.1002/jcp.27823
1039.
Ko HK, et al. The role of transforming growth factor-β2 in cigarette smoke-induced lung inflammation and injury. Life Sci. 2023;320:121539.
Not in our library10.1016/j.lfs.2023.121539
1040.
Waghabi MC, et al. Pharmacological inhibition of transforming growth factor beta signaling decreases infection and prevents heart damage in acute Chagas’ disease. Antimicrob. Agents Chemother. 2009;53:4694-4701.
Not in our library10.1128/aac.00580-09
1041.
Waghabi MC, et al. SB-431542, a transforming growth factor beta inhibitor, impairs Trypanosoma cruzi infection in cardiomyocytes and parasite cycle completion. Antimicrob. Agents Chemother. 2007;51:2905-2910.
Not in our library10.1128/aac.00022-07
1042.
Mezger MC, et al. Inhibitors of Activin Receptor-like Kinase 5 Interfere with SARS-CoV-2 S-Protein Processing and Spike-Mediated Cell Fusion via Attenuation of Furin Expression. Viruses. 2022;14:1308.
Not in our library10.3390/v14061308
1043.
Xiao YQ, Liu K, Shen JF, Xu GT, Ye W. SB-431542 inhibition of scar formation after filtration surgery and its potential mechanism. Invest Ophthalmol. Vis. Sci. 2009;50:1698-1706.
Not in our library10.1167/iovs.08-1675
1044.
Hasegawa T, Nakao A, Sumiyoshi K, Tsuchihashi H, Ogawa H. SB-431542 inhibits TGF-beta-induced contraction of collagen gel by normal and keloid fibroblasts. J. Dermatol Sci. 2005;39:33-38.
Not in our library10.1016/j.jdermsci.2005.01.013
1045.
Soleimani A, et al. Novel oral transforming growth factor-β signaling inhibitor potently inhibits postsurgical adhesion band formation. J. Cell Physiol. 2020;235:1349-1357.
Not in our library10.1002/jcp.29053
1046.
Monteleone G, et al. Phase I clinical trial of Smad7 knockdown using antisense oligonucleotide in patients with active Crohn’s disease. Mol. Ther. 2012;20:870-876.
Not in our library10.1038/mt.2011.290
1047.
Monteleone G, et al. Mongersen, an oral SMAD7 antisense oligonucleotide, and Crohn’s disease. N. Engl. J. Med. 2015;372:1104-1113.
Not in our library10.1056/nejmoa1407250
1048.
Sands BE, et al. Mongersen (GED-0301) for Active Crohn’s Disease: Results of a Phase 3 Study. Am. J. Gastroenterol. 2020;115:738-745.
Not in our library10.14309/ajg.0000000000000493
1049.
Huo, D., Bi, X. Y., Zeng, J. L., Dai, D. M. & Dong, X. L. Drugs targeting TGF-β/Notch interaction attenuate hypertrophic scar formation by optic atrophy 1-mediated mitochondrial fusion. Mol. Cell Biochem.10.1007/s11010-023-04912-y (2023).
Not in our library10.1007/s11010-023-04912-y
1050.
Zhang C, et al. Mitomycin C induces pulmonary vascular endothelial-to-mesenchymal transition and pulmonary veno-occlusive disease via Smad3-dependent pathway in rats. Br. J. Pharm. 2021;178:217-235.
Not in our library10.1111/bph.15314
1051.
Meng J, et al. Treatment of Hypertensive Heart Disease by Targeting Smad3 Signaling in Mice. Mol. Ther. Methods Clin. Dev. 2020;18:791-802.
Not in our library10.1016/j.omtm.2020.08.003
1052.
Liu S, et al. Suppression of TGFβR-Smad3 pathway alleviates the syrinx induced by syringomyelia. Cell Biosci. 2023;13:98.
Not in our library10.1186/s13578-023-01048-w
1053.
Ji X, et al. Specific Inhibitor of Smad3 (SIS3) Attenuates Fibrosis, Apoptosis, and Inflammation in Unilateral Ureteral Obstruction Kidneys by Inhibition of Transforming Growth Factor β (TGF-β)/Smad3 Signaling. Med Sci. Monit. 2018;24:1633-1641.
Not in our library10.12659/msm.909236
1054.
Zhang Y, Meng XM, Huang XR, Lan HY. The preventive and therapeutic implication for renal fibrosis by targetting TGF-β/Smad3 signaling. Clin. Sci. (Lond.). 2018;132:1403-1415.
Not in our library10.1042/cs20180243
1055.
Pan W, et al. SIS3 suppresses osteoclastogenesis and ameliorates bone loss in ovariectomized mice by modulating Nox4-dependent reactive oxygen species. Biochem Pharm. 2022;195:114846.
Not in our library10.1016/j.bcp.2021.114846
1056.
Shou J, et al. SIS3, a specific inhibitor of smad3, attenuates bleomycin-induced pulmonary fibrosis in mice. Biochem Biophys. Res Commun. 2018;503:757-762.
Not in our library10.1016/j.bbrc.2018.06.072
1057.
Rudnik M, et al. Elevated Fibronectin Levels in Profibrotic CD14(+) Monocytes and CD14(+) Macrophages in Systemic Sclerosis. Front Immunol. 2021;12:642891.
Not in our library10.3389/fimmu.2021.642891
1058.
Xiang W, et al. Inhibition of SMAD3 effectively reduces ADAMTS-5 expression in the early stages of osteoarthritis. BMC Musculoskelet. Disord. 2023;24:130.
Not in our library10.1186/s12891-022-05949-8
1059.
He H, et al. Treatment for type 2 diabetes and diabetic nephropathy by targeting Smad3 signaling. Int J. Biol. Sci. 2024;20:200-217.
Not in our library10.7150/ijbs.87820
1060.
He H, et al. Smad3 Mediates Diabetic Dyslipidemia and Fatty Liver in db/db Mice by Targeting PPARδ. Int J. Mol. Sci. 2023;24:11396.
Not in our library10.3390/ijms241411396
1061.
Wu CP, et al. SIS3, a specific inhibitor of Smad3 reverses ABCB1- and ABCG2-mediated multidrug resistance in cancer cell lines. Cancer Lett. 2018;433:259-272.
Not in our library10.1016/j.canlet.2018.07.004
1062.
Chihara Y, et al. A small-molecule inhibitor of SMAD3 attenuates resistance to anti-HER2 drugs in HER2-positive breast cancer cells. Breast Cancer Res Treat. 2017;166:55-68.
Not in our library10.1007/s10549-017-4382-6
1063.
Conidi A, van den Berghe V, Huylebroeck D. Aptamers and their potential to selectively target aspects of EGF, Wnt/beta-catenin and TGFbeta-smad family signaling. Int J. Mol. Sci. 2013;14:6690-6719.
Not in our library10.3390/ijms14046690
1064.
Lim SK, Hoffmann FM. Smad4 cooperates with lymphoid enhancer-binding factor 1/T cell-specific factor to increase c-myc expression in the absence of TGF-beta signaling. Proc. Natl Acad. Sci. USA. 2006;103:18580-18585.
Not in our library10.1073/pnas.0604773103
1065.
Zhao BM, Hoffmann FM. Inhibition of transforming growth factor-beta1-induced signaling and epithelial-to-mesenchymal transition by the Smad-binding peptide aptamer Trx-SARA. Mol. Biol. Cell. 2006;17:3819-3831.
Not in our library10.1091/mbc.e05-10-0990
1066.
Huang C, et al. Expression, purification, and functional characterization of recombinant PTD-SARA. Acta Biochim Biophys. Sin. (Shanghai). 2011;43:110-117.
Not in our library10.1093/abbs/gmq122
1067.
Ji WP, Dong Y. Targeting Yes-associated Protein with Evolved Peptide Aptamers to Disrupt TGF-beta Signaling Pathway: Therapeutic Implication for Bone Tumor. Mol. Inf. 2015;34:771-777.
Not in our library10.1002/minf.201500063
1068.
Cheifetz S, et al. Heterodimeric transforming growth factor beta. Biological properties and interaction with three types of cell surface receptors. J. Biol. Chem. 1988;263:10783-10789.
Not in our library10.1016/s0021-9258(18)38039-6
1069.
Goumans MJ, et al. Balancing the activation state of the endothelium via two distinct TGF-beta type I receptors. Embo j. 2002;21:1743-1753.
Not in our library10.1093/emboj/21.7.1743
1070.
van den Bosch MH, et al. Canonical Wnt signaling skews TGF-β signaling in chondrocytes towards signaling via ALK1 and Smad 1/5/8. Cell Signal. 2014;26:951-958.
Not in our library10.1016/j.cellsig.2014.01.021
1071.
Pannu J, Nakerakanti S, Smith E, ten Dijke P, Trojanowska M. Transforming growth factor-beta receptor type I-dependent fibrogenic gene program is mediated via activation of Smad1 and ERK1/2 pathways. J. Biol. Chem. 2007;282:10405-10413.
Not in our library10.1074/jbc.m611742200
1072.
Bharathy S, Xie W, Yingling JM, Reiss M. Cancer-associated transforming growth factor beta type II receptor gene mutant causes activation of bone morphogenic protein-Smads and invasive phenotype. Cancer Res. 2008;68:1656-1666.
Not in our library10.1158/0008-5472.can-07-5089
1073.
Daly AC, Randall RA, Hill CS. Transforming growth factor beta-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth. Mol. Cell Biol. 2008;28:6889-6902.
Not in our library10.1128/mcb.01192-08
1074.
Hussein YM, Mohamed RH, El-Shahawy EE, Alzahrani SS. Interaction between TGF-β1 (869C/T) polymorphism and biochemical risk factor for prediction of disease progression in rheumatoid arthritis. Gene. 2014;536:393-397.
Not in our library10.1016/j.gene.2013.11.042
1075.
Nakao E, et al. Elevated Plasma Transforming Growth Factor β1 Levels Predict the Development of Hypertension in Normotensives: The 14-Year Follow-Up Study. Am. J. Hypertens. 2017;30:808-814.
Not in our library10.1093/ajh/hpx053
1076.
Kanzler S, et al. Prediction of progressive liver fibrosis in hepatitis C infection by serum and tissue levels of transforming growth factor-beta. J. Viral Hepat. 2001;8:430-437.
Not in our library10.1046/j.1365-2893.2001.00314.x
1077.
Wei Y, Tian Q, Zhao X, Wang X. Serum transforming growth factor beta 3 predicts future development of nonalcoholic fatty liver disease. Int J. Clin. Exp. Med. 2015;8:4545-4550.
Not in our library
1078.
Wu CY, Li L, Zhang LH. Detection of serum MCP-1 and TGF-β1 in polymyositis/dermatomyositis patients and its significance. Eur. J. Med Res. 2019;24:12.
Not in our library10.1186/s40001-019-0368-7
1079.
Boix F, et al. A high concentration of TGF-β correlates with opportunistic infection in liver and kidney transplantation. Hum. Immunol. 2021;82:414-421.
Not in our library10.1016/j.humimm.2021.03.007
1080.
Leppäpuska IM, et al. Low TGF-β1 in Wound Exudate Predicts Surgical Site Infection After Axillary Lymph Node Dissection. J. Surg. Res. 2021;267:302-308.
Not in our library10.1016/j.jss.2021.05.039
1081.
Capuano A, et al. Hepatocyte growth factor and transforming growth factor beta1 ratio at baseline can predict early response to cyclophosphamide in systemic lupus erythematosus nephritis. Arthritis Rheum. 2006;54:3633-3639.
Not in our library10.1002/art.22192
1082.
Daïen CI, et al. TGF beta1 polymorphisms are candidate predictors of the clinical response to rituximab in rheumatoid arthritis. Jt. Bone Spine. 2012;79:471-475.
Not in our library10.1016/j.jbspin.2011.10.007
1083.
Sambuelli A, et al. Serum transforming growth factor-beta1 levels increase in response to successful anti-inflammatory therapy in ulcerative colitis. Aliment Pharm. Ther. 2000;14:1443-1449.
Not in our library10.1046/j.1365-2036.2000.00861.x
1084.
Rodrigues-Junior DM, et al. Circulating extracellular vesicle-associated TGFβ3 modulates response to cytotoxic therapy in head and neck squamous cell carcinoma. Carcinogenesis. 2019;40:1452-1461.
Not in our library10.1093/carcin/bgz148
1085.
Scarpa M, et al. TGF-beta1 and IGF-1 production and recurrence of Crohn’s disease after ileo-colonic resection. J. Surg. Res. 2009;152:26-34.
Not in our library10.1016/j.jss.2008.04.014
1086.
Scarpa M, et al. TGF-beta1 and IGF-1 and anastomotic recurrence of Crohn’s disease after ileo-colonic resection. J. Gastrointest. Surg. 2008;12:1981-1990.
Not in our library10.1007/s11605-008-0641-5
1087.
Memon AA, et al. Transforming growth factor (TGF)-β levels and unprovoked recurrent venous thromboembolism. J. Thromb. Thrombolysis. 2014;38:348-354.
Not in our library10.1007/s11239-013-1047-0
1088.
Mattey DL, Nixon N, Dawes PT, Kerr J. Association of polymorphism in the transforming growth factor {beta}1 gene with disease outcome and mortality in rheumatoid arthritis. Ann. Rheum. Dis. 2005;64:1190-1194.
Not in our library10.1136/ard.2004.031674
1089.
Watanabe Y, et al. Transforming Growth Factor-β1 as a Predictor for the Development of Hepatocellular Carcinoma: A Nested Case-Controlled Study. EBioMedicine. 2016;12:68-71.
Not in our library10.1016/j.ebiom.2016.09.001
1090.
Ikeguchi M, Iwamoto A, Taniguchi K, Katano K, Hirooka Y. The gene expression level of transforming growth factor-beta (TGF-beta) as a biological prognostic marker of hepatocellular carcinoma. J. Exp. Clin. Cancer Res. 2005;24:415-421.
Not in our library
1091.
Wu X, et al. Development of a TGF-β signaling-related genes signature to predict clinical prognosis and immunotherapy responses in clear cell renal cell carcinoma. Front Oncol. 2023;13:1124080.
Not in our library10.3389/fonc.2023.1124080

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