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An overview of mammalian p38 mitogen-activated protein kinases, central regulators of cell stress and receptor signaling

Jiahuai Han, Jianfeng Wu, John Silke

F1000Research · 2020 · Review

doi:10.12688/f1000research.22092.1

Abstract

The p38 family is a highly evolutionarily conserved group of mitogen-activated protein kinases (MAPKs) that is involved in and helps co-ordinate cellular responses to nearly all stressful stimuli. This review provides a succinct summary of multiple aspects of the biology, role, and substrates of the mammalian family of p38 kinases. Since p38 activity is implicated in inflammatory and other diseases, we also discuss the clinical implications and pharmaceutical approaches to inhibit p38.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 26, 2026. Paragraph numbers are ours, so an answer can point at one.

p38 mitogen-activated protein kinases

p38α (originally named p38) was identified and cloned as a 38 kDa protein that was tyrosine-phosphorylated in response to LPS stimulation in mammalian cells,. Sequence comparison, on the day p38α was cloned, revealed that it belonged to the mitogen-activated protein kinase (MAPK) family and that a Saccharomyces cerevisiae osmotic response protein kinase HOG1 was a p38α homologue –. p38α was also named cytokine suppressive drug binding protein (CSBP) because it was identified as the target of a series of anti-inflammatory pyridinyl-imidazole compounds and as reactivating kinase (RK) because it phosphorylated and activated MK2 –. There are four members of the p38 group of MAPKs encoded by four different genes in mammals: p38α ( MAPK14, chromosome 6p21.31 in humans), p38β ( MAPK11, SAPK2b, Chr22q13.33), p38γ ( MAPK12, ERK6, SAPK3, Chr22q13.33),, and p38δ ( MAPK13, SAPK4, Serk4, Chr6p21.31),. As can be surmised from their chromosomal locations, MAPK14/p38α and MAPK13/p38δ are physically close and separated by just over 15 kb, as are MAPK12/p38β and MAPK11/p38γ, which are separated by less than 2 kb. All the p38s contain a conserved Thr–Gly–Tyr (TGY) dual phosphorylation motif within the kinase activation loop, and both Thr and Tyr phosphorylation are necessary to fully activate the kinase. However, monophosphorylated p38α Thr 180 has some kinase activity in vitro, but a different substrate specificity, when compared with dual-site phosphorylated p38α. p38 group members are expressed ubiquitously, but p38γ and p38δ are enriched in certain cell types and tissues, such as p38γ in skeletal muscle and p38δ in the salivary, pituitary, and adrenal glands. p38β shares more amino acid sequence identity with p38α (~70%), while p38γ and p38δ share ~60% identity with p38α. p38γ and p38δ also share high sequence homology with cyclin-dependent kinases (CDKs) and are sensitive to some CDK inhibitors.

Activation and inactivation of p38

p38α is involved in the response to almost all stressful stimuli, including LPS, UV light, heat shock, osmotic shock, inflammatory cytokines, T cell receptor ligation, glucose starvation, and oncogene activation,,, –. Under certain circumstances, it is also activated upon growth factor stimulation. It should be noted that the activation of p38 in some cases is cell type specific, since an activating stimulus in one cell type may inhibit p38 in other cell types. The study of p38 group members other than p38α has been less intensive; however, where it has been examined, the other p38s are frequently co-activated with p38α.

Like other MAPK signaling pathways, the activation of all p38s is mediated by a kinase cascade: MAPKKK (MAP3K), which activates MAPKK (MAP2K), which in turn activates MAPK. The MAP2K kinases MKK3 and MKK6 are the major upstream kinases for p38 activation –. Although MKK3 and MKK6 phosphorylate most p38 isoforms in vitro, selective activation and substrate specificity have been observed in vivo. MKK4 has also been reported to phosphorylate p38α and p38δ in specific cell types. A number of MAP3Ks have been reported to participate in p38 activation including TAK1, ASK1, DLK, and MEKK4,. Low-molecular-weight GTP-binding proteins in the Rho family, such as Rac1 and Cdc42, can activate p38 through binding to MEK1 or MLK1, which function as upstream activators of MAP3K,.

p38α can also be activated by MAP2K-independent mechanisms. TAB1 (TAK1-binding protein 1) directly interacts with p38α and can promote trans autophosphorylation on Thr 180 and Tyr 182 and thus full activation of p38α. A subsequent study revealed that autophosphorylation of Thr 180 and Tyr 182 requires a conserved Thr 185 residue. TAB1-dependent p38α activation has been implicated in ischemic myocardial injury and T cell anergy,. TAB1 is also claimed to play a role in Sestrin-mediated p38α activation. Another MAP2K-independent activation is mediated by ZAP70 after T cell receptor ligation. ZAP70 can directly phosphorylate p38α/β on Tyr 323, leading to autophosphorylation on Thr 180, one of the dual phosphorylation sites. As discussed, mono-Thr 180 phosphorylated p38 still has some kinase activity, and loss of ZAP70-mediated p38 activation in p38αβ Y323F double knock-in mice reduces autoimmunity and inflammation in several autoimmune disease models –. Interestingly, p38α also phosphorylates ZAP70, resulting in a decrease in the size and persistence of the T cell receptor signaling complex, and therefore acts as a feedback regulator of ZAP70.

Conversely, de-phosphorylation of both threonine and tyrosine residues in the activation loop inactivates MAPKs, and this is mainly carried out by dual-specificity phosphatases of the MAPK phosphatase (MKP)/dual specificity phosphatase (DUSP) family. Although several MKPs have been reported to dephosphorylate p38α, MKP1/DUSP1, MKP5/DUSP10, MKP8/DUSP26, and DUSP8 are more potent inhibitors of p38α and JNK than ERK. A recent report showed that DUSP12 is also a p38α phosphatase. While there are a number of p38α DUSPs, no DUSP for p38γ or p38δ has been reported, and these two p38s are resistant to several known p38α MKPs such as MKP1, 3, 5, and 7. p38α-dependent upregulation of MKP1 was reported and is believed to be part of a negative feedback loop of p38α activation. Other types of phosphatases have also been reported to target p38 MAPKs, such as CacyBP/SIP, Wip1, and PP2C,. The substrate specificity between p38 and phosphatases and the related physiological functions in vivo still need further investigation. p38γ has also been reported to be degraded by a p38/JNK/ubiquitin-proteasome-dependent pathway, which represents an additional mechanism by which p38 kinases may cross regulate each other. Yet other ways of regulating p38 are suggested from studies in Caenorhabditis elegans, where a genetic screen for resistance against bacterial infection identified RIOK-1, an atypical serine kinase and human RIO kinase homolog, as a suppressor of the p38 pathway. As RIOK-1 is a transcriptional target of the p38 pathway in C. elegans, this suggests that RIOK-1 is part of a negative feedback loop. A brief summary of the p38 pathway is shown in Figure 1.

Protein kinases

The p38 MAPK cascade does not end at p38. Members of the MAPK-activated protein kinase (MAPKAPK) family such as MK2, MK3, and MK5 (PRAK) are all p38 substrates,, –. The MKs have a broad range of substrates that extend the range of functions regulated by p38 kinases. Mitogen- and stress-activated protein kinase-1/2 (MSK1/2), which are important for CREB activation and chromosome remodeling, have also been identified as substrates of p38α. MNK1/2, kinases that phosphorylate the eukaryotic initiation factor-4e (eIF-4E), are phosphorylated by p38α,. p38α has also been reported to inactivate murine GSK3β by phosphorylating Ser 389, and since GSK3β is required for the continuous degradation of β-catenin in the Wnt signaling pathway, this can lead to an accumulation of β-catenin,. It was also reported that p38δ negatively regulates insulin secretion by catalyzing an inhibitory phosphorylation of PKD1. A number of p38 protein kinase substrates are summarized in Table 1.

Transcription factors

p38 targets a large number of transcription factors, including myocyte-specific enhancer factor 2 (MEF2) family members, cyclic AMP-dependent transcription factor 1, 2, and 6 (ATF-1/2/6), CHOP (growth arrest and DNA damage inducible gene 153, or GADD153), p53, C/EBPβ, MITF1, DDIT3, ELK1/4, NFAT, and STAT1/4. p38 phosphorylation of transcription factors predominantly leads to enhanced transcriptional activity. However, in some cases, it represses transcription, and this is summarized in Table 2. Transcription factor phosphorylation by p38 is often stimulus and cell type dependent and plays a role in the cellular response to inflammation, DNA damage, metabolic stress, and many other stresses –. The effects of p38 on transcription seem to constitute the major part of p38’s responses to stress stimuli.

Transcriptional regulators

A large number of transcriptional regulators, including epigenetic enzymes, are substrates of p38, and these are summarized in Table 3. The SWI–SNF complex subunit BAF60 is phosphorylated and inactivated by p38 during skeletal myogenesis,, and EZH2, the catalytic component of the Polycomb Repressive Complex 2 (PRC2), was also found to be phosphorylated by p38, particularly in ER-negative breast cancer samples. Besides its transcriptional function, dATF-2 is also involved in heterochromatin formation, and stress-induced phosphorylation of dATF-2 by p38 disrupts heterochromatin in Drosophila.

Other substrates

Given the wide range of responses that p38 is involved in, it is not surprising that many p38 substrates cannot be so easily categorized into groups, and these miscellaneous substrates are summarized in Table 4. Some of them are involved in metabolism such as Raptor phosphorylation by p38β, which enhances mTORC1 activity in response to arsenite-stress, and DEPTOR (mTOR-inhibitory protein) phosphorylation by p38γ and p38δ, leading to its degradation and mTOR hyperactivation. p38α phosphorylation of Tip60 at Thr 158 promotes senescence and DNA-damage-induced apoptosis,. Some p38 substrates are cell death regulators. In the ER stress response, p38α locates to the lysosome and phosphorylates the chaperone-mediated autophagy (CMA) receptor LAMP2A, leading to activation of CMA and thus protecting cells from ER stress-induced death.

Embryo development

p38α is required for embryo development, since the mouse Mapk14 –/– embryo dies between embryonic days (E) 10.5 and 12.5 –. Mutant mice with a single Thr 180 to Ala mutation or with the double T180A Y182F mutation are also embryonic lethal,. Surprisingly, given the importance of the dual phosphorylation for complete p38 activation, substitution of Tyr 182 with Phe results in mice that have reduced p38 signaling but are nevertheless viable, although this is consistent with previous studies showing that the p38 phosphorylated on Thr 180 alone retains some activity in vitro. Histological analysis demonstrates that p38α is required for placental angiogenesis, but not embryonic cardiovascular development, and tetraploid rescue of the placental defect in Mapk14 –/– embryos confirmed that p38α is essential for extraembryonic development,. Given the important role that p38 and MK2 plays in regulating TNF-induced cell death –, it is intriguing that the Mapk14 –/– embryonic lethal phenotype is very similar to that observed in other mice with defects in the TNF death pathway. Caspase-8, FADD, and cFLIP knock-out mice also die at E10.5, and this is due to TNF-dependent endothelial cell death and disruption of the vasculature in the yolk sac,. Other p38 isoforms are not necessary for embryo development, but p38α and p38β have overlapping functions, as Mapk14 loxp/loxpMapk11 –/–Sox2-Cre embryos die before E16.5 with spina bifida that correlates with neural hyperproliferation and increased apoptosis in the liver, which was not observed in Mapk14 ∆/∆ Sox2-Cre embryos. Remarkably, p38α appears to have a very specific function during embryogenesis because when p38α was replaced by p38β in the Mapk14 chromosomal locus, which thereby placed p38β under the control of the endogenous p38α promoter, it was unable to rescue the embryonic lethality induced by loss of p38α.

Immune responses

p38 is activated by many inflammatory stimuli, and its activity is important for inflammatory responses. Macrophage-specific deletion of Mapk14 inhibits inflammatory cytokine production and protects mice from CLP-induced sepsis. p38α controls the production of inflammatory cytokines, such as TNF and IL-6, at many levels. It directly phosphorylates transcription factors, such as MEF2C,, and regulators of mRNA stability, such as hnRNPK-homology (KH) type splicing regulatory protein (KSRP). MEF2C appears to play an anti-inflammatory role in endothelial cells in vivo. Via MK2/MK3, p38 also upregulates cytokine mRNA transcription by the serum response transcription factor (SRF), and similarly, via MK2/MK3, p38 regulates mRNA stability by phosphorylating and inactivating TTP/Zfp36, a protein that promotes rapid turnover of AU-rich mRNAs, many of which are cytokine mRNAs,. p38 activation also induces the expression of inflammatory mediators such as COX-2, MMP9, iNOS, and VCAM-1, which are involved in tissue remodeling and oxidation regulation –. The p38 pathway also regulates adaptive immunity. p38α participates in antigen processing in CD8 + cDCs, and ZAP70-mediated p38α/β activation is important for T cell homeostasis and function. In B cells, p38α is important for CD40-induced gene expression and proliferation of B cells, and the p38α–MEF2c axis is believed to be necessary for germinal center B (GCB) cell proliferation and survival,. Excessive activation of p38α has been observed in many inflammatory diseases, such as inflammatory bowel disease (IBD), asthma, rheumatoid arthritis, and steatohepatitis –. The other members of the p38 family also play roles in immune responses. For example, p38γ and p38δ are required for neutrophil migration to damaged liver in non-alcoholic fatty liver disease and inhibition of eukaryotic elongation factor 2 in LPS-induced liver damage. p38δ is required for neutrophil accumulation in acute lung injury. These observations, and the role that p38s play in TNF production, led to enormous pharmaceutical efforts to develop p38 inhibitors to treat chronic inflammatory diseases. However, unfortunately, these drugs were not efficacious in these diseases.

Cell cycle

p38 has been implicated in G1 and G2/M phases of the cell cycle in several studies. The addition of activated recombinant p38α caused mitotic arrest in vitro, and an inhibitor of p38α/β suppressed activation of the checkpoint by nocodazole in NIH3T3 cells. G1 arrest caused by Cdc42 overexpression is also dependent on p38α in NIH3T3 cells. Besides, p38γ is specially required for gamma-irradiation-induced G2 arrest. The link between p38 and cell cycle control has been proposed through the regulation of several p38 substrates. Both p38α and p38γ regulate cell cycle progression via Rb but in opposite directions,. HBP1 represses the expression of cell cycle regulatory genes during cell cycle arrest in a p38-dependent manner; p53 and p21 activation by p38α prevented G1 progression through blockade of CDK activity,. The p38 pathway is also involved in cell cycle progress, as it is essential for self-renewal of mouse male germline stem cells and its regulation of G1-length plays a role in cell size uniformity.

Cell differentiation

Participation of p38 in cell differentiation has been reported in certain cell types. p38α activity is essential for neuronal differentiation in PC-12 cells and EPO-induced differentiation in SKT6 cells,. Treatment of 3T3-L1 fibroblasts with specific p38α/β inhibitors prevents their differentiation into adipocytes by reducing C/EBPβ phosphorylation, and p38α-dependent phosphorylation of MEF2C and BAF60 is critical for myogenic differentiation,. Intestinal epithelial cell-specific deletion of p38α also influences goblet cell differentiation in a Notch-dependent manner.

Cell metabolism

p38 group members participate in many cellular events related to metabolism. The p38β–PRAK axis specifically phosphorylates Rheb and suppresses mTORC1 activity under energy depletion conditions. DEPTOR, an inhibitor of mTORC, can be phosphorylated by p38γ and p38δ, leading to its degradation. Meanwhile, p38δ directly phosphorylated p62 to enhance mTORC1 activity in response to amino acids. In brown adipocytes, p38α functions as a central mediator in β-adrenergic-induced UCP1 expression,, while in white adipocytes, p38α inactivation leads to elevated white-to-beige adipocyte reprogramming and resistance to diet-induced obesity,. In hepatocytes, p38α controls lipolysis and protects against nutritional steatohepatitis. Thus, mice with hepatocyte-specific loss of p38α developed more severe steatohepatitis than wild type mice when fed high-fat or -cholesterol diets. Intriguingly, macrophage specific deletion of p38 had the opposite effect in the same high-fat diets and resulted in less steatohepatitis than in wild type mice, which probably reflects the inflammatory role of p38 in macrophages. p38α also directly phosphorylates Xbp1s to enhance its nuclear migration for maintaining glucose homeostasis in obesity. However, p38α also functions as a negative regulator of AMPK signaling in maintaining gluconeogenesis, and hepatic p38α could be a drug target for hyperglycemia. It was also reported that p38γ directly phosphorylated p62 under imidazole propionate stimulation to promote mTORC1 activity in hepatocytes. Interestingly, AMPK also triggers the recruitment of p38α to scaffold protein TAB1 for p38α autoactivation in human T cells.

Cell senescence

p38α appears to play a pivotal role in senescence. Constitutive activation of the p38 pathway by active MKK3 or MKK6 induces senescence in several cell types,, and p38α activity is responsible for senescence induced by multiple stimuli, such as telomere shortening,, H 2O 2 exposure,, and chronic oncogene activation,,. p38α/β-specific inhibitors have been successfully used to prevent cellular senescence in cultivated human corneal endothelial cells. Since cellular senescence is considered a defense strategy against oncogene activation, the p38 pathway plays important roles in tumorigenesis. Meanwhile, p38α activity is important for senescence-associated secretory phenotype (SASP), and its inhibition markedly reduces the secretion of most SASP factors, suggesting multiple roles for the p38 pathway in senescence –.

Cell survival and death

The role of the p38 pathway in cell fate is cell type and stimulus dependent. For example, p38α becomes activated upon NGF withdrawal in PC-12 cells, and p38α activated by overexpression of MKK3 induced apoptosis in NGF differentiated PC-12 cells. Similarly, inhibition of p38 with PD169316 blocked NGF withdrawal-induced apoptosis in PC-12 cells,. The interplay between the p38 pathway and caspases, the central regulators/executors of apoptosis, is complicated because p38α activity can be elevated in a caspase-dependent manner in death stimulus treated cells,, and caspase activity can also be elevated in MKK6E (dominant active form) overexpressed cells,. In contrast, inhibition of caspase-8 and caspase-3 by p38α-mediated phosphorylation in neutrophils was also reported. Recent studies show that p38-activated MK2 directly phosphorylates RIPK1 in TNF-treated cells or pathogen-infected cells, limiting TNF-induced cell death –. This represents an interesting link between cytokine production induced by TNF and cell death because TNF-induced MK2/MK3 phosphorylation of tristetraprolin/Zfp36 inactivates it and leads to increased stability of cytokine mRNAs. Aberrant p38α activity is observed in many tumor cells, and inhibition of p38α/β enhances cell death in these cells,.

Perspectives

p38 is one of the most researched of all proteins, let alone kinases, and a search in PubMed for p38 MAPK or p38 kinase returns more than 36,000 publications, which is a higher number than some proteins listed in a review of the "top 10" most studied genes. By contrast, searches for the kinases Raf and Src return about 17,000 and 25,000 hits, respectively. In 2018, there were more than 2,000 publications that mention p38, and it is clearly impractical to summarize such a vast amount of literature. As might be surmised from the preceding commentary, the studies are on a wide range of topics; however, the publications are more concentrated in some areas than others. The role of the p38 pathway in cancers (>10,000) –, inflammation (>8,000) –, and infections (>3,600), was intensively studied. About 1,600 publications include the specific term "p38 inhibitor". This reflects the previously mentioned enormous interest of the pharmaceutical industry in developing p38 inhibitors to treat chronic inflammatory diseases, such as rheumatoid arthritis. Yet other publications report natural products that can activate or inhibit p38, with the ultimate aim of using them clinically –. In 2011, the European Commission approved Esbriet (pirfenidone), which was described as a p38γ inhibitor, for the treatment of idiopathic pulmonary fibrosis. However, when this drug was approved by the FDA in 2014 for treating the same disease, it was described as a compound that acts on multiple pathways. In 2008, there were 27 clinical trials listed testing the use of p38 inhibitors in inflammatory disease settings, while a search today for p38 inhibitors in clinicaltrials.gov returns 44 studies for conditions as diverse as pain, asthma, cognitive impairment, rheumatoid arthritis, cancer, myelodysplastic syndrome, and depression ( Table 5). This indicates that there remains clinical interest in targeting the pathway and that there is therefore a need for more specific inhibitors of each of the p38 group members and more basic research to fully understand how the pathway, especially how each member of the p38 family, is utilized and regulated.

One consequence of the massive pharmaceutical effort over the last 20 years is a large number of very specific, well-tolerated, and readily bioavailable drugs that can enable such basic research. For example, one study using a boutique panel of kinase inhibitors was able to demonstrate that 11 potent and specific p38 inhibitors synergized with Smac-mimetic drugs to kill a subset of AML leukemias, providing the strongest evidence implicating p38 in Smac-mimetic-induced killing. Since several of these p38 inhibitors had already been clinically trialed, this presents an opportunity to fast-track such combinations into the clinic. In our opinion, it is likely that this is where the future of p38 research and p38 inhibitors lies, in revealing the intricate web of inter-connections and inter-dependencies of this core and central regulator of cell stress. We also believe that greater efforts to genetically assess the role of p38 and p38 isoforms in the pathophysiology of inflammatory and other diseases need to be made in order to push forward the clinical application of our burgeoning knowledge.

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  37. 37.

    Mittelstadt PR Yamaguchi H Appella E: T cell receptor-mediated activation of p38{alpha} by mono-phosphorylation of the activation loop results in altered substrate specificity. J Biol Chem. 2009;284(23):15469–15474.

    Not in our library10.1074/jbc.m901004200

  38. 38.

    Jirmanova L Sarma DN Jankovic D: Genetic disruption of p38alpha Tyr323 phosphorylation prevents T-cell receptor-mediated p38alpha activation and impairs interferon-gamma production. Blood. 2009;113(10):2229–2237.

    Not in our library10.1182/blood-2008-04-153304

  39. 39.

    Jirmanova L Giardino Torchia ML: Lack of the T cell-specific alternative p38 activation pathway reduces autoimmunity and inflammation. Blood. 2011;118(12):3280–3289.

    Not in our library10.1182/blood-2011-01-333039

  40. 40.
    Unique properties of TCR-activated p38 are necessary for NFAT-dependent T-cell activation. · 2018
    Not checked
  41. 41.

    Giardino Torchia ML Dutta D: Intensity and duration of TCR signaling is limited by p38 phosphorylation of ZAP-70 T293 and destabilization of the signalosome. Proc Natl Acad Sci U S A. 2018;115(9):2174–2179.

    Not in our library10.1073/pnas.1713301115

  42. 42.

    Sun H Charles CH Lau LF: MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell. 1993;75(3):487–493.

    Not in our library10.1016/0092-8674(93)90383-2

  43. 43.

    Nunes-Xavier C Roma-Mateo C Rios P: Dual-specificity MAP kinase phosphatases as targets of cancer treatment. Anticancer Agents Med Chem. 2011;11(1):109–132.

    Not in our library10.2174/187152011794941190

  44. 44.
    Dual-Specificity Phosphatase 12 Targets p38 MAP Kinase to Regulate Macrophage Response to Intracellular Bacterial Infection · 2017
    Not checked
  45. 45.

    Tanoue T Yamamoto T Maeda R: A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs. J Biol Chem. 2001;276(28):26629–26639.

    Not in our library10.1074/jbc.m101981200

  46. 46.

    Manetsch M Che W Seidel P: MKP-1: a negative feedback effector that represses MAPK-mediated pro-inflammatory signaling pathways and cytokine secretion in human airway smooth muscle cells. Cell Signal. 2012;24(4):907–913.

    Not in our library10.1016/j.cellsig.2011.12.013

  47. 47.

    Topolska-Wos AM Rosinska S Filipek A: MAP kinase p38 is a novel target of CacyBP/SIP phosphatase. Amino Acids. 2017;49(6):1069–1076.

    Not in our library10.1007/s00726-017-2404-7

  48. 48.

    Liu G Hu X Sun B: Phosphatase Wip1 negatively regulates neutrophil development through p38 MAPK-STAT1. Blood. 2013;121(3):519–529.

    Not in our library10.1182/blood-2012-05-432674

  49. 49.

    Takekawa M Maeda T Saito H: Protein phosphatase 2Calpha inhibits the human stress-responsive p38 and JNK MAPK pathways. EMBO J. 1998;17(16):4744–4752.

    Not in our library10.1093/emboj/17.16.4744

  50. 50.

    Maeda T Wurgler-Murphy SM Saito H: A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature. 1994;369(6477):242–245.

    Not in our library10.1038/369242a0

  51. 51.

    Qi X Pohl NM Loesch M: p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-proteasome pathways in regulating Ras transformation and stress response. J Biol Chem. 2007;282(43):31398–31408.

    Not in our library10.1074/jbc.m703857200

  52. 52.
    RIOK-1 Is a Suppressor of the p38 MAPK Innate Immune Pathway in Caenorhabditis elegans · 2018
    Not checked
  53. 53.

    Bird TA Schule HD Delaney P: The interleukin-1-stimulated protein kinase that phosphorylates heat shock protein hsp27 is activated by MAP kinase. FEBS Lett. 1994;338(1):31–36.

    Not in our library10.1016/0014-5793(94)80111-8

  54. 54.

    McLaughlin MM Kumar S McDonnell PC: Identification of mitogen-activated protein (MAP) kinase-activated protein kinase-3, a novel substrate of CSBP p38 MAP kinase. J Biol Chem. 1996;271(14):8488–8492.

    Not in our library10.1074/jbc.271.14.8488

  55. 55.

    New L Jiang Y Zhao M: PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J. 1998;17(12):3372–3384.

    Not in our library10.1093/emboj/17.12.3372

  56. 56.

    Deak M Clifton AD Lucocq LM: Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 1998;17(15):4426–4441.

    Not in our library10.1093/emboj/17.15.4426

  57. 57.

    Waskiewicz AJ Flynn A Proud CG: Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2. EMBO J. 1997;16(8):1909–1920.

    Not in our library10.1093/emboj/16.8.1909

  58. 58.

    Fukunaga R Hunter T: MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 1997;16(8):1921–1933.

    Not in our library10.1093/emboj/16.8.1921

  59. 59.

    Thornton TM Pedraza-Alva G Deng B: Phosphorylation by p38 MAPK as an alternative pathway for GSK3beta inactivation. Science. 2008;320(5876):667–670.

    Not in our library10.1126/science.1156037

  60. 60.

    Bikkavilli RK Feigin ME Malbon CC: p38 mitogen-activated protein kinase regulates canonical Wnt-beta-catenin signaling by inactivation of GSK3beta. J Cell Sci. 2008;121(Pt 21):3598–3607.

    Not in our library10.1242/jcs.032854

  61. 61.
    Regulation of PKD by the MAPK p38δ in Insulin Secretion and Glucose Homeostasis · 2009
    No notice
  62. 62.

    Han J Jiang Y Li Z: Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature. 1997;386(6622):296–299.

    Not in our library10.1038/386296a0

  63. 63.

    Tan Y Rouse J Zhang A: FGF and stress regulate CREB and ATF-1 via a pathway involving p38 MAP kinase and MAPKAP kinase-2. EMBO J. 1996;15(17):4629–4642.

    Not in our library

  64. 64.

    Barsyte-Lovejoy D Galanis A Sharrocks AD: Specificity determinants in MAPK signaling to transcription factors. J Biol Chem. 2002;277(12):9896–9903.

    Not in our library10.1074/jbc.m108145200

  65. 65.

    Hazzalin CA Cano E Cuenda A: p38/RK is essential for stress-induced nuclear responses: JNK/SAPKs and c-Jun/ATF-2 phosphorylation are insufficient. Curr Biol. 1996;6(8):1028–1031.

    Not in our library10.1016/s0960-9822(02)00649-8

  66. 66.

    Whitmarsh AJ Yang SH Su MS: Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors. Mol Cell Biol. 1997;17(5):2360–2371.

    Not in our library10.1128/mcb.17.5.2360

  67. 67.

    Janknecht R Hunter T: Convergence of MAP kinase pathways on the ternary complex factor Sap-1a. EMBO J. 1997;16(7):1620–1627.

    Not in our library10.1093/emboj/16.7.1620

  68. 68.

    Wang XZ Ron D: Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP Kinase. Science. 1996;272(5266):1347–1349.

    Not in our library10.1126/science.272.5266.1347

  69. 69.

    Bulavin DV Saito S Hollander MC: Phosphorylation of human p53 by p38 kinase coordinates N-terminal phosphorylation and apoptosis in response to UV radiation. EMBO J. 1999;18(23):6845–6854.

    Not in our library10.1093/emboj/18.23.6845

  70. 70.

    Huang C Ma WY Maxiner A: p38 kinase mediates UV-induced phosphorylation of p53 protein at serine 389. J Biol Chem. 1999;274(18):12229–12235.

    Not in our library10.1074/jbc.274.18.12229

  71. 71.

    Galibert MD Carreira S Goding CR: The Usf-1 transcription factor is a novel target for the stress-responsive p38 kinase and mediates UV-induced Tyrosinase expression. EMBO J. 2001;20(17):5022–5031.

    Not in our library10.1093/emboj/20.17.5022

  72. 72.

    Gomez del Arco P Martinez-Martinez S Maldonado JL: A role for the p38 MAP kinase pathway in the nuclear shuttling of NFATp. J Biol Chem. 2000;275(18):13872–13878.

    Not in our library10.1074/jbc.275.18.13872

  73. 73.

    Rampalli S Li L Mak E: p38 MAPK signaling regulates recruitment of Ash2L-containing methyltransferase complexes to specific genes during differentiation. Nat Struct Mol Biol. 2007;14(12):1150–1156.

    Not in our library10.1038/nsmb1316

  74. 74.

    Ramsauer K Sadzak I Porras A: p38 MAPK enhances STAT1-dependent transcription independently of Ser-727 phosphorylation. Proc Natl Acad Sci U S A. 2002;99(20):12859–12864.

    Not in our library10.1073/pnas.192264999

  75. 75.

    Lee J Sun C Zhou Y: p38 MAPK-mediated regulation of Xbp1s is crucial for glucose homeostasis. Nat Med. 2011;17(10):1251–1260.

    Not in our library10.1038/nm.2449

  76. 76.

    Lin KC Moroishi T Meng Z: Regulation of Hippo pathway transcription factor TEAD by p38 MAPK-induced cytoplasmic translocation. Nat Cell Biol. 2017;19(8):996–1002.

    Not in our library10.1038/ncb3581

  77. 77.

    Pierrat B Correia JS Mary JL: RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK). J Biol Chem. 1998;273(45):29661–29671.

    Not in our library10.1074/jbc.273.45.29661

  78. 78.

    Kaur R Liu X Gjoerup O: Activation of p21-activated kinase 6 by MAP kinase kinase 6 and p38 MAP kinase. J Biol Chem. 2005;280(5):3323–3330.

    Not in our library10.1074/jbc.m406701200

  79. 79.

    Jones DR Bultsma Y Keune WJ: Nuclear PtdIns5P as a transducer of stress signaling: an in vivo role for PIP4Kbeta. Mol Cell. 2006;23(5):685–695.

    Not in our library10.1016/j.molcel.2006.07.014

  80. 80.

    Saurin AT Durgan J Cameron AJ: The regulated assembly of a PKCepsilon complex controls the completion of cytokinesis. Nat Cell Biol. 2008;10(8):891–901.

    Not in our library10.1038/ncb1749

  81. 81.

    Cuenda A Cohen P Buee-Scherrer V: Activation of stress-activated protein kinase-3 (SAPK3) by cytokines and cellular stresses is mediated via SAPKK3 (MKK6); comparison of the specificities of SAPK3 and SAPK2 (RK/p38). EMBO J. 1997;16(2):295–305.

    Not in our library10.1093/emboj/16.2.295

  82. 82.

    Qiao L MacDougald OA Shao J: CCAAT/enhancer-binding protein alpha mediates induction of hepatic phosphoenolpyruvate carboxykinase by p38 mitogen-activated protein kinase. J Biol Chem. 2006;281(34):24390–24397.

    Not in our library10.1074/jbc.m603038200

  83. 83.

    Engelman JA Lisanti MP Scherer PE: Specific inhibitors of p38 mitogen-activated protein kinase block 3T3-L1 adipogenesis. J Biol Chem. 1998;273(48):32111–32120.

    Not in our library10.1074/jbc.273.48.32111

  84. 84.

    Williamson EA Williamson IK Chumakov AM: CCAAT/enhancer binding protein epsilon: changes in function upon phosphorylation by p38 MAP kinase. Blood. 2005;105(10):3841–3847.

    Not in our library10.1182/blood-2004-09-3708

  85. 85.

    Morillo SM Abanto EP Roman MJ: Nerve growth factor-induced cell cycle reentry in newborn neurons is triggered by p38 MAPK-dependent E2F4 phosphorylation. Mol Cell Biol. 2012;32(14):2722–2737.

    Not in our library10.1128/mcb.00239-12

  86. 86.

    Lee H Bai W: Regulation of estrogen receptor nuclear export by ligand-induced and p38-mediated receptor phosphorylation. Mol Cell Biol. 2002;22(16):5835–5845.

    Not in our library10.1128/mcb.22.16.5835-5845.2002

  87. 87.

    Tanos T Marinissen MJ Leskow FC: Phosphorylation of c-Fos by members of the p38 MAPK family. Role in the AP-1 response to UV light. J Biol Chem. 2005;280(19):18842–18852.

    Not in our library10.1074/jbc.m500620200

  88. 88.

    Ho KK McGuire VA Koo CY: Phosphorylation of FOXO3a on Ser-7 by p38 promotes its nuclear localization in response to doxorubicin. J Biol Chem. 2012;287(2):1545–1555.

    Not in our library10.1074/jbc.m111.284224

  89. 89.

    Miller AL Webb MS Copik AJ: p38 Mitogen-activated protein kinase (MAPK) is a key mediator in glucocorticoid-induced apoptosis of lymphoid cells: correlation between p38 MAPK activation and site-specific phosphorylation of the human glucocorticoid receptor at serine 211. Mol Endocrinol. 2005;19(6):1569–1583.

    Not in our library10.1210/me.2004-0528

  90. 90.

    Macfarlane WM Smith SB James RF: The p38/reactivating kinase mitogen-activated protein kinase cascade mediates the activation of the transcription factor insulin upstream factor 1 and insulin gene transcription by high glucose in pancreatic beta-cells. J Biol Chem. 1997;272(33):20936–20944.

    Not in our library10.1074/jbc.272.33.20936

  91. 91.

    Katz S Aronheim A: Differential targeting of the stress mitogen-activated protein kinases to the c-Jun dimerization protein 2. Biochem J. 2002;368(Pt 3):939–945.

    Not in our library10.1042/bj20021127

  92. 92.

    Humar M Loop T Schmidt R: The mitogen-activated protein kinase p38 regulates activator protein 1 by direct phosphorylation of c-Jun. Int J Biochem Cell Biol. 2007;39(12):2278–2288.

    Not in our library10.1016/j.biocel.2007.06.013

  93. 93.

    Sii-Felice K Pouponnot C Gillet S: MafA transcription factor is phosphorylated by p38 MAP kinase. FEBS Lett. 2005;579(17):3547–3554.

    Not in our library10.1016/j.febslet.2005.04.086

  94. 94.

    Zhao M New L Kravchenko VV: Regulation of the MEF2 family of transcription factors by p38. Mol Cell Biol. 1999;19(1):21–30.

    Not in our library10.1128/mcb.19.1.21

  95. 95.

    Mansky KC Sankar U Han J: Microphthalmia transcription factor is a target of the p38 MAPK pathway in response to receptor activator of NF-kappa B ligand signaling. J Biol Chem. 2002;277(13):11077–11083.

    Not in our library10.1074/jbc.m111696200

  96. 96.

    Suelves M Lluis F Ruiz V: Phosphorylation of MRF4 transactivation domain by p38 mediates repression of specific myogenic genes. EMBO J. 2004;23(2):365–375.

    Not in our library10.1038/sj.emboj.7600056

  97. 97.

    Matsumoto M Kogawa M Wada S: Essential role of p38 mitogen-activated protein kinase in cathepsin K gene expression during osteoclastogenesis through association of NFATc1 and PU.1. J Biol Chem. 2004;279(44):45969–45979.

    Not in our library10.1074/jbc.m408795200

  98. 98.

    Yang TT Xiong Q Enslen H: Phosphorylation of NFATc4 by p38 mitogen-activated protein kinases. Mol Cell Biol. 2002;22(11):3892–3904.

    Not in our library10.1128/mcb.22.11.3892-3904.2002

  99. 99.

    Sekine Y Takagahara S Hatanaka R: p38 MAPKs regulate the expression of genes in the dopamine synthesis pathway through phosphorylation of NR4A nuclear receptors. J Cell Sci. 2011;124(Pt 17):3006–3016.

    Not in our library10.1242/jcs.085902

  100. 100.

    Li L Liu Y Chen HZ: Impeding the interaction between Nur77 and p38 reduces LPS-induced inflammation. Nat Chem Biol. 2015;11(5):339–346.

    Not in our library10.1038/nchembio.1788

  101. 101.

    Ortuno MJ Ruiz-Gaspa S Rodriguez-Carballo E: p38 regulates expression of osteoblast-specific genes by phosphorylation of osterix. J Biol Chem. 2010;285(42):31985–31994.

    Not in our library10.1074/jbc.m110.123612

  102. 102.

    Mikkola I Bruun JA Bjorkoy G: Phosphorylation of the transactivation domain of Pax6 by extracellular signal-regulated kinase and p38 mitogen-activated protein kinase. J Biol Chem. 1999;274(21):15115–15126.

    Not in our library10.1074/jbc.274.21.15115

  103. 103.

    Barger PM Browning AC Garner AN: p38 mitogen-activated protein kinase activates peroxisome proliferator-activated receptor alpha: a potential role in the cardiac metabolic stress response. J Biol Chem. 2001;276(48):44495–44501.

    Not in our library10.1074/jbc.m105945200

  104. 104.

    Hayes SA Huang X Kambhampati S: p38 MAP kinase modulates Smad-dependent changes in human prostate cell adhesion. Oncogene. 2003;22(31):4841–4850.

    Not in our library10.1038/sj.onc.1206730

  105. 105.

    Ryu KJ Park SM Park SH: p38 Stabilizes Snail by Suppressing DYRK2-Mediated Phosphorylation That Is Required for GSK3beta-betaTrCP-Induced Snail Degradation. Cancer Res. 2019;79(16):4135–4148.

    Not in our library10.1158/0008-5472.can-19-0049

  106. 106.

    Kovarik P Stoiber D Eyers PA: Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-gamma uses a different signaling pathway. Proc Natl Acad Sci U S A. 1999;96(24):13956–61.

    Not in our library10.1073/pnas.96.24.13956

  107. 107.

    Visconti R Gadina M Chiariello M: Importance of the MKK6/p38 pathway for interleukin-12-induced STAT4 serine phosphorylation and transcriptional activity. Blood. 2000;96(5):1844–52.

    Not in our library

  108. 108.

    Hong J Zhou J Fu J: Phosphorylation of serine 68 of Twist1 by MAPKs stabilizes Twist1 protein and promotes breast cancer cell invasiveness. Cancer Res. 2011;71(11):3980–90.

    Not in our library10.1158/0008-5472.can-10-2914

  109. 109.

    Simone C Forcales SV Hill DA: p38 pathway targets SWI-SNF chromatin-remodeling complex to muscle-specific loci. Nat Genet. 2004;36(7):738–43.

    Not in our library10.1038/ng1378

  110. 110.

    Forcales SV Albini S Giordani L: Signal-dependent incorporation of MyoD-BAF60c into Brg1-based SWI/SNF chromatin-remodelling complex. EMBO J. 2012;31(2):301–16.

    Not in our library10.1038/emboj.2011.391

  111. 111.
    p38-mediated phosphorylation at T367 induces EZH2 cytoplasmic localization to promote breast cancer metastasis · 2018
    Not checked
  112. 112.

    Seong KH Li D Shimizu H: Inheritance of stress-induced, ATF-2-dependent epigenetic change. Cell. 2011;145(7):1049–1061.

    Not in our library10.1016/j.cell.2011.05.029

  113. 113.

    Wu XN Wang XK Wu SQ: Phosphorylation of Raptor by p38beta participates in arsenite-induced mammalian target of rapamycin complex 1 (mTORC1) activation. J Biol Chem. 2011;286(36):31501–31511.

    Not in our library10.1074/jbc.m111.233122

  114. 114.
    p38γ and δ promote heart hypertrophy by targeting the mTOR-inhibitory protein DEPTOR for degradation · 2016
    Not checked
  115. 115.

    Zheng H Seit-Nebi A Han X: A posttranslational modification cascade involving p38, Tip60, and PRAK mediates oncogene-induced senescence. Mol Cell. 2013;50(5):699–710.

    Not in our library10.1016/j.molcel.2013.04.013

  116. 116.

    Xu Y Liao R Li N: Phosphorylation of Tip60 by p38alpha regulates p53-mediated PUMA induction and apoptosis in response to DNA damage. Oncotarget. 2014;5(24):12555–12572.

    Not in our library10.18632/oncotarget.2717

  117. 117.
    Phosphorylation of LAMP2A by p38 MAPK couples ER stress to chaperone-mediated autophagy · 2017
    No notice
  118. 118.

    Allen M Svensson L Roach M: Deficiency of the stress kinase p38alpha results in embryonic lethality: characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells. J Exp Med. 2000;191(5):859–870.

    Not in our library10.1084/jem.191.5.859

  119. 119.

    Tamura K Sudo T Senftleben U: Requirement for p38alpha in erythropoietin expression: a role for stress kinases in erythropoiesis. Cell. 2000;102(2):221–231.

    Not in our library10.1016/s0092-8674(00)00027-1

  120. 120.

    Adams RH Porras A Alonso G: Essential role of p38alpha MAP kinase in placental but not embryonic cardiovascular development. Mol Cell. 2000;6(1):109–116.

    Not in our library10.1016/s1097-2765(05)00014-6

  121. 121.

    Mudgett JS Ding J Guh-Siesel L: Essential role for p38alpha mitogen-activated protein kinase in placental angiogenesis. Proc Natl Acad Sci U S A. 2000;97(19):10454–10459.

    Not in our library10.1073/pnas.180316397

  122. 122.

    Wong ES Le Guezennec X Demidov ON: p38MAPK controls expression of multiple cell cycle inhibitors and islet proliferation with advancing age. Dev Cell. 2009;17(1):142–149.

    Not in our library10.1016/j.devcel.2009.05.009

  123. 123.

    Brichkina A Bertero T Loh HM: p38MAPK builds a hyaluronan cancer niche to drive lung tumorigenesis. Genes Dev. 2016;30(23):2623–2636.

    Not in our library10.1101/gad.290346.116

  124. 124.

    Rao PS Satelli A Zhang S: RNF2 is the target for phosphorylation by the p38 MAPK and ERK signaling pathways. Proteomics. 2009;9(10):2776–2787.

    Not in our library10.1002/pmic.200800847

  125. 125.

    Ma H Liu Z Zhong CQ: Inactivation of Cyclic AMP Response Element Transcription Caused by Constitutive p38 Activation Is Mediated by Hyperphosphorylation-Dependent CRTC2 Nucleocytoplasmic Transport. Mol Cell Biol. 2019;39(9):e00554–18.

    Not in our library10.1128/mcb.00554-18

  126. 126.

    Page JL Wang X Sordillo LM: MEKK1 signaling through p38 leads to transcriptional inactivation of E47 and repression of skeletal myogenesis. J Biol Chem. 2004;279(30):30966–30972.

    Not in our library10.1074/jbc.m402224200

  127. 127.

    Lluis F Ballestar E Suelves M: E47 phosphorylation by p38 MAPK promotes MyoD/E47 association and muscle-specific gene transcription. EMBO J. 2005;24(5):974–84.

    Not in our library10.1038/sj.emboj.7600528

  128. 128.

    Xiu M Kim J Sampson E: The transcriptional repressor HBP1 is a target of the p38 mitogen-activated protein kinase pathway in cell cycle regulation. Mol Cell Biol. 2003;23(23):8890–901.

    Not in our library10.1128/mcb.23.23.8890-8901.2003

  129. 129.

    Cuadrado A Lafarga V Cheung PCF: A new p38 MAP kinase-regulated transcriptional coactivator that stimulates p53-dependent apoptosis. EMBO J. 2007;26(8):2115–26.

    Not in our library10.1038/sj.emboj.7601657

  130. 130.

    Puigserver P Rhee J Lin J: Cytokine stimulation of energy expenditure through p38 MAP kinase activation of PPARgamma coactivator-1. Mol Cell. 2001;8(5):971–82.

    Not in our library10.1016/s1097-2765(01)00390-2

  131. 131.

    Delston RB Matatall KA Sun Y: p38 phosphorylates Rb on Ser567 by a novel, cell cycle-independent mechanism that triggers Rb-Hdm2 interaction and apoptosis. Oncogene. 2011;30(5):588–99.

    Not in our library10.1038/onc.2010.442

  132. 132.

    Gianni M Parrella E Raska I Jr: P38MAPK-dependent phosphorylation and degradation of SRC-3/AIB1 and RARalpha-mediated transcription. EMBO J. 2006;25(4):739–751.

    Not in our library10.1038/sj.emboj.7600981

  133. 133.

    Goloudina A Yamaguchi H Chervyakova DB: Regulation of human Cdc25A stability by Serine 75 phosphorylation is not sufficient to activate a S phase checkpoint. Cell Cycle. 2003;2(5):473–478.

    Not in our library10.4161/cc.2.5.482

  134. 134.

    Lemaire M Froment C Boutros R: CDC25B phosphorylation by p38 and MK-2. Cell Cycle. 2006;5(15):1649–1653.

    Not in our library10.4161/cc.5.15.3006

  135. 135.

    Casanovas O Miro F Estanyol JM: Osmotic stress regulates the stability of cyclin D1 in a p38SAPK2-dependent manner. J Biol Chem. 2000;275(45):35091–35097.

    Not in our library10.1074/jbc.m006324200

  136. 136.

    Casanovas O Jaumot M Paules AB: P38SAPK2 phosphorylates cyclin D3 at Thr-283 and targets it for proteasomal degradation. Oncogene. 2004;23(45):7537–7544.

    Not in our library10.1038/sj.onc.1208040

  137. 137.

    Joaquin M Gubern A Gonzalez-Nunez D: The p57 CDKi integrates stress signals into cell-cycle progression to promote cell survival upon stress. EMBO J. 2012;31(13):2952–64.

    Not in our library10.1038/emboj.2012.122

  138. 138.

    Min H Ghatnekar GS Ghatnekar AV: 2-Methoxyestradiol induced Bax phosphorylation and apoptosis in human retinoblastoma cells via p38 MAPK activation. Mol Carcinog. 2012;51(7):576–85.

    Not in our library10.1002/mc.20825

  139. 139.

    Cai B Chang SH Becker EBE: p38 MAP kinase mediates apoptosis through phosphorylation of BimEL at Ser-65. J Biol Chem. 2006;281(35):25215–22.

    Not in our library10.1074/jbc.m512627200

  140. 140.

    Alvarado-Kristensson M Melander F Leandersson K: p38-MAPK signals survival by phosphorylation of caspase-8 and caspase-3 in human neutrophils. J Exp Med. 2004;199(4):449–58.

    Not in our library10.1084/jem.20031771

  141. 141.

    Seifert A Clarke PR: p38alpha- and DYRK1A-dependent phosphorylation of caspase-9 at an inhibitory site in response to hyperosmotic stress. Cell Signal. 2009;21(11):1626–33.

    Not in our library10.1016/j.cellsig.2009.06.009

  142. 142.

    Chandrasekaran S Tan TX Hall JR: Stress-stimulated mitogen-activated protein kinases control the stability and activity of the Cdt1 DNA replication licensing factor. Mol Cell Biol. 2011;31(22):4405–16.

    Not in our library10.1128/mcb.06163-11

  143. 143.

    Yang Q Li W She H: Stress induces p38 MAPK-mediated phosphorylation and inhibition of Drosha-dependent cell survival. Mol Cell. 2015;57(4):721–734.

    Not in our library10.1016/j.molcel.2015.01.004

  144. 144.

    Danckwardt S Gantzert AS Macher-Goeppinger S: p38 MAPK controls prothrombin expression by regulated RNA 3' end processing. Mol Cell. 2011;41(3):298–310.

    Not in our library10.1016/j.molcel.2010.12.032

  145. 145.

    Lu C Shi Y Wang Z: Serum starvation induces H2AX phosphorylation to regulate apoptosis via p38 MAPK pathway. FEBS Lett. 2008;582(18):2703–8.

    Not in our library10.1016/j.febslet.2008.06.051

  146. 146.

    Zhong SP Ma WY Dong Z: ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10. J Biol Chem. 2000;275(28):20980–4.

    Not in our library10.1074/jbc.m909934199

  147. 147.

    Lafarga V Cuadrado A Lopez de Silanes I: p38 Mitogen-activated protein kinase- and HuR-dependent stabilization of p21 Cip1 mRNA mediates the G 1/S checkpoint. Mol Cell Biol. 2009;29(16):4341–4351.

    Not in our library10.1128/mcb.00210-09

  148. 148.

    Briata P Forcales SV Ponassi M: p38-dependent phosphorylation of the mRNA decay-promoting factor KSRP controls the stability of select myogenic transcripts. Mol Cell. 2005;20(6):891–903.

    Not in our library10.1016/j.molcel.2005.10.021

  149. 149.
    A novel whole-cell lysate kinase assay identifies substrates of the p38 MAPK in differentiating myoblasts · 2012
    Not checked
  150. 150.

    Al-Ayoubi AM Zheng H Liu Y: Mitogen-activated protein kinase phosphorylation of splicing factor 45 (SPF45) regulates SPF45 alternative splicing site utilization, proliferation, and cell adhesion. Mol Cell Biol. 2012;32(14):2880–2893.

    Not in our library10.1128/mcb.06327-11

  151. 151.

    Mace G Miaczynska M Zerial M: Phosphorylation of EEA1 by p38 MAP kinase regulates mu opioid receptor endocytosis. EMBO J. 2005;24(18):3235–3246.

    Not in our library10.1038/sj.emboj.7600799

  152. 152.

    Cavalli V Vilbois F Corti M: The stress-induced MAP kinase p38 regulates endocytic trafficking via the GDI:Rab5 complex. Mol Cell. 2001;7(2):421–432.

    Not in our library10.1016/s1097-2765(01)00189-7

  153. 153.

    Kelkar N Standen CL Davis RJ: Role of the JIP4 scaffold protein in the regulation of mitogen-activated protein kinase signaling pathways. Mol Cell Biol. 2005;25(7):2733–2743.

    Not in our library10.1128/mcb.25.7.2733-2743.2005

  154. 154.

    Cheung PC Campbell DG Nebreda AR: Feedback control of the protein kinase TAK1 by SAPK2a/p38alpha. EMBO J. 2003;22(21):5793–5805.

    Not in our library10.1093/emboj/cdg552

  155. 155.

    Mendoza H Campbell DG Burness K: Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex. Biochem J. 2008;409(3):711–722.

    Not in our library10.1042/bj20071149

  156. 156.

    Zakrzewska M Opalinski L Haugsten EM: Crosstalk between p38 and Erk 1/2 in Downregulation of FGF1-Induced Signaling. Int J Mol Sci. 2019;20(8):1826.

    Not in our library10.3390/ijms20081826

  157. 157.

    Winograd-Katz SE Levitzki A: Cisplatin induces PKB/Akt activation and p38 MAPK phosphorylation of the EGF receptor. Oncogene. 2006;25(56):7381–7390.

    Not in our library10.1038/sj.onc.1209737

  158. 158.

    Sørensen V Zhen Y Zakrzewska M: Phosphorylation of fibroblast growth factor (FGF) receptor 1 at Ser777 by p38 mitogen-activated protein kinase regulates translocation of exogenous FGF1 to the cytosol and nucleus. Mol Cell Biol. 2008;28(12):4129–4141.

    Not in our library10.1128/mcb.02117-07

  159. 159.

    Gasser A Cheng X Gilmore ES: Two Nedd4-binding motifs underlie modulation of sodium channel Na v1.6 by p38 MAPK. J Biol Chem. 2010;285(34):26149–26161.

    Not in our library10.1074/jbc.m109.098681

  160. 160.

    Khaled AR Moor AN Li A: Trophic factor withdrawal: p38 mitogen-activated protein kinase activates NHE1, which induces intracellular alkalinization. Mol Cell Biol. 2001;21(22):7545–7557.

    Not in our library10.1128/mcb.21.22.7545-7557.2001

  161. 161.

    Börsch-Haubold AG Bartoli F Asselin J: Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. J Biol Chem. 1998;273(8):4449–4458.

    Not in our library10.1074/jbc.273.8.4449

  162. 162.

    Xu P Derynck R: Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation. Mol Cell. 2010;37(4):551–566.

    Not in our library10.1016/j.molcel.2010.01.034

  163. 163.

    Hedges JC Yamboliev IA Ngo M: p38 mitogen-activated protein kinase expression and activation in smooth muscle. Am J Physiol. 1998;275(2):C527–534.

    Not in our library10.1152/ajpcell.1998.275.2.c527

  164. 164.

    Ku NO Azhar S Omary MB: Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: modulation by a keratin 1-like disease causing mutation. J Biol Chem. 2002;277(13):10775–10782.

    Not in our library10.1074/jbc.m107623200

  165. 165.

    Barascu A Le Chalony C Pennarun G: Oxidative stress induces an ATM-independent senescence pathway through p38 MAPK-mediated lamin B1 accumulation. EMBO J. 2012;31(5):1080–1094.

    Not in our library10.1038/emboj.2011.492

  166. 166.

    Huang C Borchers CH Schaller MD: Phosphorylation of paxillin by p38MAPK is involved in the neurite extension of PC-12 cells. J Cell Biol. 2004;164(4):593–602.

    Not in our library10.1083/jcb.200307081

  167. 167.

    Parker CG Hunt J Diener K: Identification of stathmin as a novel substrate for p38 delta. Biochem Biophys Res Commun. 1998;249(3):791–796.

    Not in our library10.1006/bbrc.1998.9250

  168. 168.

    Sabio G Arthur JS Kuma Y: p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP. EMBO J. 2005;24(6):1134–1145.

    Not in our library10.1038/sj.emboj.7600578

  169. 169.

    Reynolds CH Nebreda AR Gibb GM: Reactivating kinase/p38 phosphorylates tau protein in vitro. J Neurochem. 1997;69(1):191–198.

    Not in our library10.1046/j.1471-4159.1997.69010191.x

  170. 170.

    Ittner A Chua SW Bertz J: Site-specific phosphorylation of tau inhibits amyloid-β toxicity in Alzheimer's mice. Science. 2016;354(6314):904–908.

    Not in our library10.1126/science.aah6205

  171. 171.

    Hall EH Balsbaugh JL Rose KL: Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK. Mol Cell Proteomics. 2010;9(12):2853–2863.

    Not in our library10.1074/mcp.m110.003665

  172. 172.

    Kuma Y Campbell DG Cuenda A: Identification of glycogen synthase as a new substrate for stress-activated protein kinase 2b/p38beta. Biochem J. 2004;379(Pt 1):133–139.

    Not in our library10.1042/bj20031559

  173. 173.

    Chen J Ren Y Gui C: Phosphorylation of Parkin at serine 131 by p38 MAPK promotes mitochondrial dysfunction and neuronal death in mutant A53T α-synuclein model of Parkinson's disease. Cell Death Dis. 2018;9(6):700.

    Not in our library10.1038/s41419-018-0722-7

  174. 174.

    Makni-Maalej K Boussetta T Hurtado-Nedelec M: The TLR7/8 agonist CL097 primes N-formyl-methionyl-leucyl-phenylalanine-stimulated NADPH oxidase activation in human neutrophils: critical role of p47phox phosphorylation and the proline isomerase Pin1. J Immunol. 2012;189(9):4657–4665.

    Not in our library10.4049/jimmunol.1201007

  175. 175.

    Linares JF Duran A Reina-Campos M: Amino Acid Activation of mTORC1 by a PB1-Domain-Driven Kinase Complex Cascade. Cell Rep. 2015;12(8):1339–1352.

    Not in our library10.1016/j.celrep.2015.07.045

  176. 176.

    Koh A Molinaro A Stahlman M: Microbially Produced Imidazole Propionate Impairs Insulin Signaling through mTORC1. Cell. 2018;175(4):947–961.e917.

    Not in our library10.1016/j.cell.2018.09.055

  177. 177.

    Lee SH Park Y Yoon SK: Osmotic stress inhibits proteasome by p38 MAPK-dependent phosphorylation. J Biol Chem. 2010;285(53):41280–41289.

    Not in our library10.1074/jbc.m110.182188

  178. 178.

    Khurana A Nakayama K Williams S: Regulation of the ring finger E3 ligase Siah2 by p38 MAPK. J Biol Chem. 2006;281(46):35316–35326.

    Not in our library10.1074/jbc.m606568200

  179. 179.

    Lalaoui N Hanggi K Brumatti G: Targeting p38 or MK2 Enhances the Anti-Leukemic Activity of Smac-Mimetics. Cancer Cell. 2016;30(3):499–500.

    Not in our library10.1016/j.ccell.2016.08.009

  180. 180.
    MK2 Phosphorylates RIPK1 to Prevent TNF-Induced Cell Death · 2017
    No notice
  181. 181.

    Dondelinger Y Delanghe T Rojas-Rivera D: MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death. Nat Cell Biol. 2017;19(10):1237–1247.

    Not in our library10.1038/ncb3608

  182. 182.

    Menon MB Gropengiesser J Fischer J: p38 MAPK/MK2-dependent phosphorylation controls cytotoxic RIPK1 signalling in inflammation and infection. Nat Cell Biol. 2017;19(10):1248–1259.

    Not in our library10.1038/ncb3614

  183. 183.

    Silke J Rickard JA Gerlic M: The diverse role of RIP kinases in necroptosis and inflammation. Nat Immunol. 2015;16(7):689–697.

    Not in our library10.1038/ni.3206

  184. 184.

    Dillon CP Tummers B Baran K: Developmental checkpoints guarded by regulated necrosis. Cell Mol Life Sci. 2016;73(11-12):2125–2136.

    Not in our library10.1007/s00018-016-2188-z

  185. 185.

    del Barco Barrantes I Coya JM Maina F: Genetic analysis of specific and redundant roles for p38alpha and p38beta MAPKs during mouse development. Proc Natl Acad Sci U S A. 2011;108(31):12764–12769.

    Not in our library10.1073/pnas.1015013108

  186. 186.

    Kang YJ Chen J Otsuka M: Macrophage deletion of p38alpha partially impairs lipopolysaccharide-induced cellular activation. J Immunol. 2008;180(7):5075–5082.

    Not in our library10.4049/jimmunol.180.7.5075

  187. 187.

    Tiedje C Holtmann H Gaestel M: The role of mammalian MAPK signaling in regulation of cytokine mRNA stability and translation. J Interferon Cytokine Res. 2014;34(4):220–232.

    Not in our library10.1089/jir.2013.0146

  188. 188.

    Xu Z Yoshida T Wu L: Transcription factor MEF2C suppresses endothelial cell inflammation via regulation of NF-kappaB and KLF2. J Cell Physiol. 2015;230(6):1310–1320.

    Not in our library10.1002/jcp.24870

  189. 189.

    Ronkina N Menon MB Schwermann J: Stress induced gene expression: a direct role for MAPKAP kinases in transcriptional activation of immediate early genes. Nucleic Acids Res. 2011;39(7):2503–2518.

    Not in our library10.1093/nar/gkq1178

  190. 190.

    Ronkina N Shushakova N Tiedje C: The Role of TTP Phosphorylation in the Regulation of Inflammatory Cytokine Production by MK2/3. J Immunol. 2019;203(8):2291–2300.

    Not in our library10.4049/jimmunol.1801221

  191. 191.

    Guan Z Buckman SY Pentland AP: Induction of cyclooxygenase-2 by the activated MEKK1 --> SEK1/MKK4 --> p38 mitogen-activated protein kinase pathway. J Biol Chem. 1998;273(21):12901–8.

    Not in our library10.1074/jbc.273.21.12901

  192. 192.

    Badger AM Cook MN Lark MW: SB 203580 inhibits p38 mitogen-activated protein kinase, nitric oxide production, and inducible nitric oxide synthase in bovine cartilage-derived chondrocytes. J Immunol. 1998;161(1):467–73.

    Not in our library

  193. 193.

    Da Silva J Pierrat B Mary JL: Blockade of p38 mitogen-activated protein kinase pathway inhibits inducible nitric-oxide synthase expression in mouse astrocytes. J Biol Chem. 1997;272(45):28373–80.

    Not in our library10.1074/jbc.272.45.28373

  194. 194.

    Wiehler S Cuvelier SL Chakrabarti S: p38 MAP kinase regulates rapid matrix metalloproteinase-9 release from eosinophils. Biochem Biophys Res Commun. 2004;315(2):463–70.

    Not in our library10.1016/j.bbrc.2004.01.078

  195. 195.

    Zhou Y Wu J Liu C: p38alpha has an important role in antigen cross-presentation by dendritic cells. Cell Mol Immunol. 2018;15(3):246–259.

    Not in our library10.1038/cmi.2016.49

  196. 196.

    Craxton A Shu G Graves JD: p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes. J Immunol. 1998;161(7):3225–36.

    Not in our library

  197. 197.

    Khiem D Cyster JG Schwarz JJ: A p38 MAPK-MEF2C pathway regulates B-cell proliferation. Proc Natl Acad Sci U S A. 2008;105(44):17067–72.

    Not in our library10.1073/pnas.0804868105

  198. 198.

    Wilker PR Kohyama M Sandau MM: Transcription factor Mef2c is required for B cell proliferation and survival after antigen receptor stimulation. Nat Immunol. 2008;9(6):603–12.

    Not in our library10.1038/ni.1609

  199. 199.

    Zhang X Fan L Wu J: Macrophage p38α promotes nutritional steatohepatitis through M1 polarization. J Hepatol. 2019;71(1):163–174.

    Not in our library10.1016/j.jhep.2019.03.014

  200. 200.

    Otsuka M Kang YJ Ren J: Distinct effects of p38alpha deletion in myeloid lineage and gut epithelia in mouse models of inflammatory bowel disease. Gastroenterology. 2010;138(4):1255–65.1265.e1-9.

    Not in our library10.1053/j.gastro.2010.01.005

  201. 201.

    Liang L Li F Bao A: Activation of p38 mitogen-activated protein kinase in ovalbumin and ozone-induced mouse model of asthma. Respirology. 2013;18 Suppl 3:20–29.

    Not in our library10.1111/resp.12189

  202. 202.

    Gonzalez-Teran B Matesanz N Nikolic I: p38γ and p38δ Reprogram Liver Metabolism by Modulating Neutrophil Infiltration. EMBO J. 2016;35(5):536–552.

    Not in our library10.15252/embj.201591857

  203. 203.

    Gonzalez-Teran B Cortes JR Manieri E: Eukaryotic Elongation Factor 2 Controls TNF-α Translation in LPS-induced Hepatitis. J Clin Invest. 2013;123(1):164–178.

    Not in our library10.1172/jci65124

  204. 204.

    Ittner A Block H Reichel CA: Regulation of PTEN Activity by p38δ-PKD1 Signaling in Neutrophils Confers Inflammatory Responses in the Lung. J Exp Med. 2012;209(12):2229–2246.

    Not in our library10.1084/jem.20120677

  205. 205.

    Genovese MC: Inhibition of p38: has the fat lady sung? Arthritis Rheum. 2009;60(12):317–320.

    Not in our library10.1002/art.24264

  206. 206.

    Takenaka K Moriguchi T Nishida E: Activation of the protein kinase p38 in the spindle assembly checkpoint and mitotic arrest. Science. 1998;280(5363):599–602.

    Not in our library10.1126/science.280.5363.599

  207. 207.

    Molnar A Theodoras AM Zon LI: Cdc42Hs, but not Rac1, inhibits serum-stimulated cell cycle progression at G 1/S through a mechanism requiring p38/RK. J Biol Chem. 1997;272(20):13229–13235.

    Not in our library10.1074/jbc.272.20.13229

  208. 208.

    Wang X McGowan CH Zhao M: Involvement of the MKK6-p38gamma cascade in gamma-radiation-induced cell cycle arrest. Mol Cell Biol. 2000;20(13):4543–4552.

    Not in our library10.1128/mcb.20.13.4543-4552.2000

  209. 209.

    Gubern A Joaquin M Marquès M: The N-Terminal Phosphorylation of RB by p38 Bypasses Its Inactivation by CDKs and Prevents Proliferation in Cancer Cells. Mol Cell. 2016;64(1):25–36.

    Not in our library10.1016/j.molcel.2016.08.015

  210. 210.

    Yee AS Paulson EK McDevitt MA: The HBP1 transcriptional repressor and the p38 MAP kinase: unlikely partners in G1 regulation and tumor suppression. Gene. 2004;336(1):1–13.

    Not in our library10.1016/j.gene.2004.04.004

  211. 211.

    Kumari G Ulrich T Gaubatz S: A role for p38 in transcriptional elongation of p21 CIP1 in response to Aurora B inhibition. Cell Cycle. 2013;12(13):2051–2060.

    Not in our library10.4161/cc.25100

  212. 212.

    Saha K Adhikary G Kanade SR: p38δ regulates p53 to control p21 Cip1 expression in human epidermal keratinocytes. J Biol Chem. 2014;289(16):11443–11453.

    Not in our library10.1074/jbc.m113.543165

  213. 213.

    Niu Z Mu H Zhu H: p38 MAPK pathway is essential for self-renewal of mouse male germline stem cells (mGSCs). Cell Prolif. 2017;50(1):e12314.

    Not in our library10.1111/cpr.12314

  214. 214.
    Size uniformity of animal cells is actively maintained by a p38 MAPK-dependent regulation of G1-length · 2018
    Not checked
  215. 215.

    Morooka T Nishida E: Requirement of p38 mitogen-activated protein kinase for neuronal differentiation in PC12 cells. J Biol Chem. 1998;273(38):24285–24288.

    Not in our library10.1074/jbc.273.38.24285

  216. 216.

    Li Y Jiang B Ensign WY: Myogenic differentiation requires signalling through both phosphatidylinositol 3-kinase and p38 MAP kinase. Cell Signal. 2000;12(11–12):751–757.

    Not in our library10.1016/s0898-6568(00)00120-0

  217. 217.

    Cao W Medvedev AV Daniel KW: β-Adrenergic activation of p38 MAP kinase in adipocytes: cAMP induction of the uncoupling protein 1 (UCP1) gene requires p38 MAP kinase. J Biol Chem. 2001;276(29):27077–27082.

    Not in our library10.1074/jbc.m101049200

  218. 218.

    Cao W Daniel KW Robidoux J: p38 mitogen-activated protein kinase is the central regulator of cyclic AMP-dependent transcription of the brown fat uncoupling protein 1 gene. Mol Cell Biol. 2004;24(7):3057–3067.

    Not in our library10.1128/mcb.24.7.3057-3067.2004

  219. 219.
    p38α blocks brown adipose tissue thermogenesis through p38δ inhibition. · 2018
    Not checked
  220. 220.

    Zhang S Cao H Li Y: Metabolic benefits of inhibition of p38α in white adipose tissue in obesity. PLoS Biol. 2018;16(5):e2004225.

    Not in our library10.1371/journal.pbio.2004225

  221. 221.

    Jing Y Liu W Cao H: Hepatic p38α regulates gluconeogenesis by suppressing AMPK. J Hepatol. 2015;62(6):1319–1327.

    Not in our library10.1016/j.jhep.2014.12.032

  222. 222.

    Lanna A Henson SM Escors D: The kinase p38 activated by the metabolic regulator AMPK and scaffold TAB1 drives the senescence of human T cells. Nat Immunol. 2014;15(10):965–972.

    Not in our library10.1038/ni.2981

  223. 223.

    Wang W Chen JX Liao R: Sequential activation of the MEK-extracellular signal-regulated kinase and MKK3/6-p38 mitogen-activated protein kinase pathways mediates oncogenic ras-induced premature senescence. Mol Cell Biol. 2002;22(10):3389–3403.

    Not in our library10.1128/mcb.22.10.3389-3403.2002

  224. 224.

    Haq R Brenton JD Takahashi M: Constitutive p38HOG mitogen-activated protein kinase activation induces permanent cell cycle arrest and senescence. Cancer Res. 2002;62(17):5076–5082.

    Not in our library

  225. 225.

    Tivey HS Brook AJ Rokicki MJ: p38 MAPK stress signalling in replicative senescence in fibroblasts from progeroid and genomic instability syndromes. Biogerontology. 2013;14(1):47–62.

    Not in our library10.1007/s10522-012-9407-2

  226. 226.

    Naka K Tachibana A Ikeda K: Stress-induced premature senescence in hTERT-expressing ataxia telangiectasia fibroblasts. J Biol Chem. 2004;279(3):2030–2037.

    Not in our library10.1074/jbc.m309457200

  227. 227.

    Dimozi A Mavrogonatou E Sklirou A: Oxidative stress inhibits the proliferation, induces premature senescence and promotes a catabolic phenotype in human nucleus pulposus intervertebral disc cells. Eur Cell Mater. 2015;30:89–102.

    Not in our library10.22203/ecm.v030a07

  228. 228.

    Borodkina AV Shatrova AN Nikolsky NN: Role of P38 Map-Kinase in the Stress-Induced Senescence Progression of Human Endometrium-Derived Mesenchymal Stem Cells. Tsitologiia. 2016;58(6):429–435.

    Not in our library

  229. 229.

    Harada G Neng Q Fujiki T: Molecular mechanisms for the p38-induced cellular senescence in normal human fibroblast. J Biochem. 2014;156(5):283–290.

    Not in our library10.1093/jb/mvu040

  230. 230.

    Hongo A Okumura N Nakahara M: The Effect of a p38 Mitogen-Activated Protein Kinase Inhibitor on Cellular Senescence of Cultivated Human Corneal Endothelial Cells. Invest Ophthalmol Vis Sci. 2017;58(9):3325–3334.

    Not in our library10.1167/iovs.16-21170

  231. 231.

    Han J Sun P: The pathways to tumor suppression via route p38. Trends Biochem Sci. 2007;32(8):364–371.

    Not in our library10.1016/j.tibs.2007.06.007

  232. 232.

    Freund A Patil CK Campisi J: p38MAPK is a novel DNA damage response-independent regulator of the senescence-associated secretory phenotype. EMBO J. 2011;30(8):1536–1548.

    Not in our library10.1038/emboj.2011.69

  233. 233.
    The senescence-associated secretory phenotype is potentiated by feedforward regulatory mechanisms involving Zscan4 and TAK1 · 2018
    No notice
  234. 234.
    Suppression of the senescence-associated secretory phenotype (SASP) in human fibroblasts using small molecule inhibitors of p38 MAP kinase and MK2 · 2015
    No notice
  235. 235.

    Coppe JP Desprez PY Krtolica A: The senescence-associated secretory phenotype: the dark side of tumor suppression. Annu Rev Pathol. 2010;5:99–118.

    Not in our library10.1146/annurev-pathol-121808-102144

  236. 236.

    Xia Z Dickens M Raingeaud J: Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science. 1995;270(5240):1326–1331.

    Not in our library10.1126/science.270.5240.1326

  237. 237.

    Kummer JL Rao PK Heidenreich KA: Apoptosis induced by withdrawal of trophic factors is mediated by p38 mitogen-activated protein kinase. J Biol Chem. 1997;272(33):20490–20494.

    Not in our library10.1074/jbc.272.33.20490

  238. 238.

    Cahill MA Peter ME Kischkel FC: CD95 (APO-1/Fas) induces activation of SAP kinases downstream of ICE-like proteases. Oncogene. 1996;13(10):2087–2096.

    Not in our library

  239. 239.

    Huang S Jiang Y Li Z: Apoptosis signaling pathway in T cells is composed of ICE/Ced-3 family proteases and MAP kinase kinase 6b. Immunity. 1997;6(6):739–749.

    Not in our library10.1016/s1074-7613(00)80449-5

  240. 240.

    Cardone MH Salvesen GS Widmann C: The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell. 1997;90(2):315–323.

    Not in our library10.1016/s0092-8674(00)80339-6

  241. 241.

    Tan W Yu HG Luo HS: Inhibition of the p38 MAPK pathway sensitizes human gastric cells to doxorubicin treatment in vitro and in vivo. Mol Med Rep. 2014;10(6):3275–3281.

    Not in our library10.3892/mmr.2014.2598

  242. 242.

    Slawinska-Brych A Zdzisinska B Mizerska-Dudka M: Induction of apoptosis in multiple myeloma cells by a statin-thalidomide combination can be enhanced by p38 MAPK inhibition. Leuk Res. 2013;37(5):586–594.

    Not in our library10.1016/j.leukres.2013.01.022

  243. 243.

    Dolgin E: The most popular genes in the human genome. Nature. 2017;551(7681):427–431.

    Not in our library10.1038/d41586-017-07291-9

  244. 244.

    Alam MS Gaida MM Bergmann F: Selective inhibition of the p38 alternative activation pathway in infiltrating T cells inhibits pancreatic cancer progression. Nat Med. 2015;21(11):1337–1343.

    Not in our library10.1038/nm.3957

  245. 245.

    Luk ST Ng KY Zhou L: Deficiency in Embryonic Stem Cell Marker Reduced Expression 1 Activates Mitogen-Activated Protein Kinase Kinase 6-Dependent p38 Mitogen-Activated Protein Kinase Signaling to Drive Hepatocarcinogenesis. Hepatology. 2019.

    Not in our library10.1002/hep.31020

  246. 246.

    Salome M Magee A Yalla K: A Trib2-p38 axis controls myeloid leukaemia cell cycle and stress response signalling. Cell Death Dis. 2018;9(5):443.

    Not in our library10.1038/s41419-018-0467-3

  247. 247.

    Gibbs KL Kalmar B Rhymes ER: Inhibiting p38 MAPK alpha rescues axonal retrograde transport defects in a mouse model of ALS. Cell Death Dis. 2018;9(6):596.

    Not in our library10.1038/s41419-018-0624-8

  248. 248.

    Fang C Wu B Le NTT: Prions activate a p38 MAPK synaptotoxic signaling pathway. PLoS Pathog. 2018;14(9): e1007283.

    Not in our library10.1371/journal.ppat.1007283

  249. 249.
    A new hypothesis for Parkinson’s disease pathogenesis: GTPase-p38 MAPK signaling and autophagy as convergence points of etiology and genomics · 2018
    Not checked
  250. 250.

    Wang PY Hsu PI Wu DC: SUMOs Mediate the Nuclear Transfer of p38 and p-p38 during Helicobacter Pylori Infection. Int J Mol Sci. 2018;19(9):2482.

    Not in our library10.3390/ijms19092482

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    Zhang F Zhao Q Tian J: Effective Pro-Inflammatory Induced Activity of GALT, a Conserved Antigen in A. Pleuropneumoniae, Improves the Cytokines Secretion of Macrophage via p38, ERK1/2 and JNK MAPKs Signal Pathway. Front Cell Infect Microbiol. 2018;8:337.

    Not in our library10.3389/fcimb.2018.00337

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    Zhu J Yu W Liu B: Escin induces caspase-dependent apoptosis and autophagy through the ROS/p38 MAPK signalling pathway in human osteosarcoma cells in vitro and in vivo. Cell Death Dis. 2017;8(10):e3113.

    Not in our library10.1038/cddis.2017.488

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    Fan H Gao Z Ji K: The in vitro and in vivo anti-inflammatory effect of osthole, the major natural coumarin from Cnidium monnieri (L.) Cuss, via the blocking of the activation of the NF-kappaB and MAPK/p38 pathways. Phytomedicine. 2019;58:152864.

    Not in our library10.1016/j.phymed.2019.152864

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    Li Y Xu B Xu M: 6-Gingerol protects intestinal barrier from ischemia/reperfusion-induced damage via inhibition of p38 MAPK to NF-kappaB signalling. Pharmacol Res. 2017;119:137–148.

    Not in our library10.1016/j.phrs.2017.01.026

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    Isoliensinine induces apoptosis in triple-negative human breast cancer cells through ROS generation and p38 MAPK/JNK activation · 2015
    No notice
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    Bachegowda L Morrone K Winski SL: Pexmetinib: A Novel Dual Inhibitor of Tie2 and p38 MAPK with Efficacy in Preclinical Models of Myelodysplastic Syndromes and Acute Myeloid Leukemia. Cancer Res. 2016;76(16):4841–4849.

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    O'Donoghue ML Glaser R Aylward PE: Rationale and design of the LosmApimod To Inhibit p38 MAP kinase as a TherapeUtic target and moDify outcomes after an acute coronary syndromE trial. Am Heart J. 2015;169(5):622–630.e6.

    Not in our library10.1016/j.ahj.2015.02.012

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    Emami H Vucic E Subramanian S: The effect of BMS-582949, a P38 mitogen-activated protein kinase (P38 MAPK) inhibitor on arterial inflammation: a multicenter FDG-PET trial. Atherosclerosis. 2015;240(2):490–496.

    Not in our library10.1016/j.atherosclerosis.2015.03.039

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    Moran N: p38 kinase inhibitor approved for idiopathic pulmonary fibrosis. Nat Biotechnol. 2011;29(4):301.

    Not in our library10.1038/nbt0411-301

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