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Methylglyoxal and Its Adducts: Induction, Repair, and Association with Disease

Seigmund Wai Tsuen Lai, Edwin De Jesus Lopez Gonzalez, Tala Zoukari and 2 more

Chemical Research in Toxicology · 2022 · Review

doi:10.1021/acs.chemrestox.2c00160

Abstract

Metabolism is an essential part of life that provides energy for cell growth. During metabolic flux, reactive electrophiles are produced that covalently modify macromolecules, leading to detrimental cellular effects. Methylglyoxal (MG) is an abundant electrophile formed from lipid, protein, and glucose metabolism at intracellular levels of 1-4 μM. MG covalently modifies DNA, RNA, and protein, forming advanced glycation end products (MG-AGEs). MG and MG-AGEs are associated with the onset and progression of many pathologies including diabetes, cancer, and liver and kidney disease. Regulating MG and MG-AGEs is a potential strategy to prevent disease, and they may also have utility as biomarkers to predict disease risk, onset, and progression. Here, we review recent advances and knowledge surrounding MG, including its production and elimination, mechanisms of MG-AGEs formation, the physiological impact of MG and MG-AGEs in disease onset and progression, and the latter in the context of its receptor RAGE. We also discuss methods for measuring MG and MG-AGEs and their clinical application as prognostic biomarkers to allow for early detection and intervention prior to disease onset. Finally, we consider relevant clinical applications and current therapeutic strategies aimed at targeting MG, MG-AGEs, and RAGE to ultimately improve patient outcomes.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 25, 2026. Paragraph numbers are ours, so an answer can point at one.

Introduction

Metabolism encompasses all of the reactions cells use to convert food into energy and is essential to sustain life. Changes in metabolic flux result from increased food intake, dysregulation of metabolite uptake, and up- and downregulation of proteins involved in metabolic pathways. Altered metabolism is associated with diabetes, cancer, liver, and kidney disease; however, how this drives disease onset and progression is not clear. A proposed mechanism is through changes in cellular physiology caused by reactive electrophiles produced during metabolic flux. Electrophiles are electron-pair-deficient molecules that react with nucleophilic sites within macromolecules to alter the structure and function. An abundant electrophile produced from metabolic flux is methylglyoxal (MG), which is formed intracellularly at levels of 1–4 μM. MG covalently modifies nucleophilic sites within nucleic and amino acids, forming advanced glycation end products (MG-AGEs).

Our understanding of the role of MG and MG-AGEs as potential drivers of disease has advanced because of the foundational work by Larry Marnett and other pioneers in the field of chemical toxicology. Marnett described the impact of reactive electrophiles, including malondialdehyde, base propenal, and hydroxynonenal on protein and DNA structure and function.− This work provided the framework to investigate the impact of electrophile stress using chemical tools, analytical methods, biochemistry assays, and models for animal studies. Measuring and targeting electrophiles, their associated byproducts, and receptors has important implications as biomarkers and etiological agents of disease. In this review, we discuss the formation of MG, MG-AGEs, the physiological impact of these molecules on cellular function, and their association with disease.

MG Production

MG (2-oxopropanal or pyruvaldehyde) was discovered in the late 19th century as a byproduct of glucose, protein, and lipid metabolism.− MG is proposed to exert its cellular effect through the formation of MG-AGEs on nucleic acids and protein, leading to changes in macromolecular stability and function.,− MG is predominantly produced as a byproduct of glycolysis during degradation of the triose phosphate intermediates, dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P) (Figure 1A). This occurs through two mechanisms: (1) nonenzymatic breakdown of G3P and DHAP, causing loss of the α-carbonyl group and phosphate, or (2) enzymatic conversion of G3P and DHAP into MG, mediated by enzymes such as MG synthase (MS) and triose phosphate isomerase (TPI) (Figure 1A).− Sources of DHAP include the conversion of glucose to fructose and fructose 1,6-bisphosphate via sorbitol dehydrogenase and phosphofructokinase, respectively, which are then converted to DHAP via aldolase B. DHAP is also formed from metabolism of triacylglycerol into glycerol-3-phosphate via glycerol kinase (GK), followed by l-glycerol-3-phosphate oxidase (G3PO) or glycerol-3-phosphate dehydrogenase (G3PDH) (Figure 1A).,

MG is also produced from lipid, ketone, and protein metabolism.,, Triacylglycerol is hydrolyzed to fatty acids, which form acetol and acetone, giving rise to MG through acetol mono-oxygenase (AMOO) (Figure 1B). Ketone metabolism also produces MG through cytochrome P450, AMOO, and myeloperoxidase (MP) (Figure 1C)., Finally, MG is formed from glycine and threonine metabolism to aminoacetone through threonine dehydrogenase (TDH). Aminoacetone is then converted to MG through semicarbazide-sensitive amine oxidase (SSAO) (Figure 1D).,

Collectively, this demonstrates that MG and its precursors and cofactors are abundant molecules associated with several metabolic pathways. It is important to note that MG abundance and its rate of formation also largely depends on the state of metabolic flux, the specific organism or tissue being studied, as well as physiological milieu. However, it has been estimated that intracellular MG levels range from 1 to 4 μM. However, due to MG’s reactive nature, it has been postulated that MG’s biological half-life is relatively short, and it is therefore likely that the actual amount produced is higher than current estimates. As a small molecule, MG is cell permeant and thus is able to diffuse through cell membranes from the extracellular space.

MG Regulation

Given that MG is reactive and can have detrimental impacts on cellular function, there are multiple mechanisms by which it is detoxified.

MG Detoxification via the Glyoxalase System

One of the most prominent ways cells detoxify MG is through the glyoxalase pathway, a highly evolutionarily conserved system that involves the activity of two enzymes: glyoxalase 1 (GLO1) and glyoxalase 2 (GLO2). MG reacts nonenzymatically with glutathione (GSH) to form a hemithioacetal, which is recognized by GLO1 and converted into S-d-lactoylglutathione (Figure 2A). GLO2 then converts S-d-lactoylglutathione into d-lactate, regenerating GSH (Figure 2A). The rate-limiting step of this pathway is GLO1 recognition of the hemithioacetal. Recent work demonstrated a novel role for S-d-lactoylglutathione as a source of protein post-translational modifications, a process inhibited by GLO2.

GLO1 overexpression protects cells from the accumulation of reactive oxygen species (ROS), glucose-driven apoptosis, and dysfunction arising from angiogenesis and diabetes.− Recently, Alkb homologue 7 (ALKBH7) has been proposed to regulate GLO1 as Alkbh7–/– mice have elevated Glo1 expression and MG-protein adducts. In addition, DJ-1, also known as PARK7, is a gene implicated in Parkinson’s disease that detoxifies MG through a GSH-independent glyoxalase mechanism, converting MG to lactic acid., Clinical trials involving obese patients have implicated combinatory treatment of hesperetin and trans-resveratrol in inducing GLO1 expression and activity, which was found to lower their glucose levels and improve overall vascular function.

A recent study was among the first to successfully create a viable GLO1 knockout mouse without significant detrimental side effects., However, the loss of GLO1 has not been fully characterized in mammalian models. A putative Glo1 knockout mouse model was revealed to maintain a normal, healthy phenotype owing to gene duplication prior to gene trapping, preserving the wild-type phenotype. It was subsequently reported that aldehyde dehydrogenases (ALDH) and aldose reductases (AR), reviewed below, compensated for and mitigated the loss of GLO1. A similar finding implicating compensatory mechanisms for GLO1 has been reported in studies of GLO1 knockout zebrafish (D. rerio), which upregulated ALDH activity, partially compensating for the loss of GLO1. The loss of GLO1 in yeast (S. cerevisiae) resulted in hypersensitivity to MG and decreased cell survival and proliferation., In addition, the loss of GLO1 in fruit flies (D. melanogaster) led to obesity and prolonged lifespan and appeared to recapitulate some diabetic phenotypes, including hyperglycemia. In vitro, a GLO1 knockout in HEK293T increased MG-AGEs, specifically MG-hydroimidazolone (MG-H1). Further studies in primary human aortic endothelial cells revealed that GLO1 knockdown increased MG levels and subsequent inflammation, apoptosis, and dysfunction that led to vascular damage and impaired function. Taken together, this highlights the importance of the glyoxalase system as an indispensable mechanism for detoxifying MG.

MG Detoxification via Oxidation

ALDHs are a class of nicotinamide adenine dinucleotide (NAD) and NAD phosphate (NADP)-dependent enzymes that oxidizes aldehydes to form carboxylic acids. ALDHs help detoxify aldehydes, a process that, if left unregulated, can be detrimental. For example, single-nucleotide polymorphisms, particularly ALDH2 rs672 G>A, and ALDH mutations are associated with an enhanced risk of heart disease, muscular dystrophy, and Alzheimer’s disease.,

The E1, E2, and E3 isozymes of ALDH react with MG and oxidize it into pyruvate in an NAD-dependent manner (Figure 2D). Likewise, 2-oxoaldehyde dehydrogenase (2-ODH) converts MG to pyruvate but in an NADP-dependent manner (Figure 2E). The loss of Aldh in murine models enhanced aldehydic adduct formation, cardiovascular and motor dysfunction, and tissue damage.Aldh overexpression mitigated the effects of oxidative stress and ROS in various organs, both of which are upregulated following MG accumulation., Similar to GLO1 knockout cells, glo1 knockout in zebrafish moderately increased MG levels and significantly heightened Aldh activity, supporting the role of ALDH as an additional compensatory mechanism in the event the glyoxalase system is impaired.

MG Detoxification via Reduction

Aldose reductase (AR) is a 36 kDa enzyme encoded by the human ALR2 gene and is part of the aldo-keto reductase enzyme family. The canonical role of AR is to reduce aldehydes into their respective sugar alcohols via the polyol pathway. AR activity is dependent on NADPH and exhibits a higher substrate selectivity and preference than ALDH, particularly for MG, thus making it more efficient at MG breakdown than ALDH., AR is associated with the development of diabetic complications, such as cardiovascular and renal diseases (reviewed in ref). In addition, AR gene polymorphisms are associated with the risk of developing diabetic complications such as retinopathy, nephropathy,, and neuropathy. For example, a CA dinucleotide polymorphism located in the 5′ promoter region of the ALR2 gene is correlated with diabetic retinopathy. A similar biallelic polymorphism (C-106T) also in the promoter region of ALR2 increased the risk of nephropathy, which was further enhanced if an individual carried both risk alleles. Patients with diabetic neuropathy have significantly lower frequency of the Z+2 allele than healthy controls. Therefore, AR polymorphisms appear to be closely related to the development of diabetic complications. AR-mediated MG detoxification operates in two distinct pathways: (1) GSH dependent in which the hemithioacetal formed between the nonenzymatic reaction with GSH and MG is converted by AR and NADPH to a lactaldehyde (Figure 2B) and (2) GSH independent in which MG reacts with AR and NADPH to form acetol (Figure 2C). Further AR-mediated metabolism of the lactaldehyde and acetol forms propanediol (Figure 2B and 2C). It is important to note that MG reduction by AR is significantly increased in the presence of GSH. In Schwann cells with GLO1 knockout, AR inhibition increased intracellular MG levels and elevated sensitivity to MG. This suggests that not only is AR-mediated detoxification of MG important for MG elimination, both in the presence and in the absence of GSH, but also it is a compensatory mechanism if the glyoxalase system is impaired. However, the effects of AR overexpression have not been fully elucidated in the context of MG detoxification. AR overexpression was found to contribute to drug resistance in cancers, neural atrophy, and inflammation,, contributing to a slew of disorders such as those impacting the eye and nerves. Given its ubiquitous nature, pursuing AR overexpression to promote MG breakdown may not be clinically apt.

MG-AGEs on DNA and Protein

The electrophilic properties of MG drive its reaction with nucleophiles within macromolecules, forming covalent adducts. These adducts have been described for DNA and protein, and extensive work has been performed to determine the impact of these modifications on macromolecular function. Here, we will discuss the main adducts formed on DNA and protein, the pathways cells use to remove these adducts, and the impact of adducts on macromolecular function.−

MG-Nucleic Acid Adducts

The primary target for MG modification in DNA is deoxyguanosine (dG). A 20-fold excess of MG with dG resulted in the formation of a cyclic dihydroimidazolone 1,N2-(1,2-dihydroxy-2-methyl)ethano-dG (cMG-dG) (Figure 3A). Additional adducts were later characterized including a product with 2-MG equivalents, N2-(1-carboxyethyl)-7-1-hydroxy-2-oxopropyl-dG (MG-CEdG) and N2-(1-carboxyethyl)-2′-dG (CEdG), which was formed at less than stoichiometric amounts of MG (Figure 3A).,, Although these adducts are formed in vitro, CEdG is the only adduct observed in genomic DNA. This is proposed to occur because cMG-dG is unstable and degrades to generate hydrated MG and dG. This hydrated form of MG only modifies dG at the N2 position, driving CEdG production. cMG-dG does not directly convert to CEdG, as was previously hypothesized. In addition to DNA, we hypothesize that MG modifies guanosine nucleotides in RNA to form N2-(1-carboxyethyl)-guanosine (CEG) (Figure 3B).

Regulation of MG Adducts—DNA Repair

DNA adducts induce genomic instability, impact transcription, and are mutagenic. To prevent this, cells have multiple DNA repair pathways, including nucleotide excision repair (NER), base excision repair (BER), and mismatch repair (MMR). Each pathway varies in damage recognition and removal. The repair pathway activated depends on the chemistry of the lesion and how it perturbs the DNA structure; each repair pathway employs different proteins that have specific interactions with the DNA to trigger the repair pathway. For instance, the NER pathway is the primary pathway cells use to repair bulky DNA adducts that induce helical distortions, while BER repairs small lesions that do not significantly distort the helix, and MMR removes mispaired bases in the genome. The primary pathway for the removal of MG-DNA adducts is not clear, but both BER and NER are proposed to play a role because shuttle vectors modified with MG have persistent DNA adducts when replicated in cells deficient in XPG, a protein involved in both BER and NER.

DNA repair efficiency is impacted by protein expression and activity and is regulated by complex mechanisms. Hyperglycemia, which increases the levels of MG-DNA adducts, may also play a role in regulating DNA repair. Ciminera et al. recently showed that high glucose decreased the expression of proteins in the NER pathway, leading to accumulation of MG-DNA adducts corresponding to decreased functional repair. The authors suggested that high glucose may downregulate NER protein expression through a HIF-1α-dependent mechanism.

When cells are unable to efficiently repair DNA damage, it leads to persistent lesions that may cause genomic instability and mutations (Figure 4A). CEdG is associated with single-strand DNA breaks and increased mutation frequency. In S. cerevisiae D7, MG induced both mitotic gene conversion and reverse point mutations with a dose-dependent response in mutation frequency. Forward selection analysis for mutations in the hypoxanthine phosphoribosyl transferase (HPRT) gene also revealed MG to be a mutagen in Chinese hamster lung cells and T-cell lymphocytes., Mutagenesis in T cells was observed with both a single high-dose MG treatment (1 mM) and multiple low-dose MG treatments (0.1 mM).

To define the specific mutations induced by MG, Tamae et al. utilized MG-modified shuttle vectors. The MG-adduct density was quantified, and the shuttle vectors were transfected into XPG-proficient or -deficient human fibroblasts, a protein involved in both BER and NER. A linear, dose-dependent increase in mutations was observed in the supF tRNA marker gene. However, there was a maximal elevated mutation frequency in the XPG-deficient fibroblast cells at varying adduct densities up to 5-fold background levels. Specific sites in the supF gene were preferentially modified, suggesting that there may be sites more susceptible to MG modification. These results were recapitulated by Murata-Kamiya et al., who showed that MG-modified shuttle vectors had guanine transversions when replicated in COS-7 fibroblast cells. Further characterization of these mutations via sequencing analysis revealed that multibase deletions and base-pair substitutions were predominant in the mutant signature with the latter being primarily G:C → C:G and G:C → T:A transversions in the supF gene of the shuttle vector (Figure 4A).E. coli deficient in NER also showed increased levels of MG-induced mutations. In addition, treatment of human melanoma WM-2664 cells with MG induced the formation of CEdG adducts, which had mutagenic properties in E. coli and were a substrate for DinB DNA polymerase, a known contributor to mutagenesis.

MG-Protein Adduct Formation

In addition to DNA, MG modifies amino acids including lysine, arginine, and cysteine, forming protein adducts that can impact the structure and function (Figure 3C). Initially, Takahashi found that high MG concentrations modified free amine-containing amino acids, specifically lysine and arginine, and hypothesized that thiol-containing amino acids could be modified as well. This was later confirmed by Lo et al., who demonstrated that MG modifies cysteine, forming a reversible hemithioacetal, later named carboxyethyl cysteine (CEC). Physiological MG concentrations modify proteins, particularly BSA, producing the fluorescent imidazole derivative MG-H1 (Nδ-(5-hydro-5-methyl-4-imidazolon-2-yl)ornithine). MG-H1 is the predominant adduct, but two other hydroimidazolones also form: MG-H2 (2-amino-5-(2-amino-5-hydro-5-methyl-4-imidazolon-1-yl)pentanoic acid) and the significantly less abundant MG-H3 (2-amino-5-(2-amino-4-hydro-4-methyl-5-imidazolon-1-yl)pentanoic acid). MG-H3 can be hydrolyzed to form carboxyethyl arginine (CEA). It was previously hypothesized that MG-H1 is resistant to hydrolysis, but McEwen et al. recently demonstrated that it is also hydrolyzed to form CEA. MG also modifies Nα-acetyllysine, forming a glycosylamine, Nε-carboxyethyllysine (CEL) (Figure 3C). CEL is found in lens protein and is associated with age. While there is significant CEL formation in vitro, MG-H1 is the most abundant amino acid adduct in clinical samples, approximately 10 times greater than CEL.

Adducted amino acids can undergo a secondary modification, resulting in macromolecule cross-linking. MG forms the protein dimers lysine–lysine (MOLD) and lysine–arginine (MODIC) (Figure 3D). Cross-linking also occurs between DNA and polymerases, which is proposed to occur through a dG–lysine bond.,

Impact of MG-AGEs on Protein Structure and Function

MG modification of amino acids disrupts the enzymatic activity and protein structure., Endothelial cells exposed to hyperglycemia had increased cellular MG concentrations and protein MG-AGEs. Proteomics analysis revealed that 17% of proteins had low-level MG modification including those involved in protein synthesis, protein folding, kinase signaling, glycolysis, and gluconeogenesis. The proteins with the highest number of modifications were pyruvate kinase M, β-actin, α-enolase, and heat shock protein (HSP) 90-β. HSPs are chaperone proteins that are elevated in response to stress, and in addition to HSP90-β, MG also modifies HSP6, HSP27, and α-crystallin (protein with HSP domains). This interrupts their interactions with other proteins and impairs chaperone function.− Collagen modified with MG shows a decreased ability to adhere to mesangial cells. Human serum albumin is also a target for MG modification. There is a hot spot of modification at Arg410, which is located in drug binding site II and in the active site for esterase activity. HIF-1α modification by MG decreases heterodimer formation and promoter binding. This is a potential mechanism for the decreased DNA repair protein expression in cells grown in high glucose observed by Ciminera et al. as DNA repair proteins are targets for HIF-1α transcription activity. Recently, work from Marnett demonstrated that histones are targets for MG modification, potentially regulating gene expression. Histone modification by MG has also been associated with changes in chromatin architecture related to disease.

RAGE Activation and Signaling by MG-AGEs

In addition to changing DNA and protein expression and stability, MG-AGEs are proposed to impact cell function by binding to and activating the receptor for AGEs (RAGE). RAGE is an immunoglobulin transmembrane pattern-recognition receptor that is expressed on a range of cells, including endothelial,, immune,, skeletal muscle, and cancer cells.− RAGE is generally present in three primary forms, as a full-length membrane-bound receptor (flRAGE), as a soluble product (sRAGE) created by ADAM10-mediated cleavage of flRAGE, and as a splice variant known as endogenous secretory RAGE (esRAGE). Binding of MG-AGEs to RAGE has been investigated both with free modified amino acids and with modified proteins such as albumin. Xie et al. found that CEL does not bind to RAGE, but protein with CEL modifications does. However, nuclear magnetic resonance (NMR) studies revealed that CEL-containing peptides bind specifically to a positively charged moiety of the V domain of RAGE. Additional NMR studies demonstrated that MG-derived hydroimidazolones (MG-H1–3) bind to a positively charged pocket of the V domain of RAGE, similar to CEL. MG-modified albumin (MG-BSA) also binds to RAGE to cause signal transduction; treatment of A549 adenocarcinoma cells with MG-BSA caused an upregulation of JNK phosphorylation in a RAGE-dependent mechanism.

In addition to AGEs, RAGE is bound by structurally diverse ligands, including phosphatidylserine, high-mobility group box-1 (HMGB1) protein, S100b, lipopolysaccharides,, and nucleic acids. RAGE activates JAK/STAT, PI3K/AKT/mTOR, and MAPK/ERK, leading to NFκB activation (Figure 4B). This upregulates ER stress, ROS production, inflammation, and oxidative damage (Figure 4B)., The NFκB cascade plays a significant role in mediating cellular responses including inflammation, apoptosis, and cellular survival and proliferation. Therefore, AGE-dependent activation of the NFκB pathway via RAGE contributes to numerous disease pathologies.,,

The signaling cascade triggered by RAGE activation is influenced by cell type. For instance, RAGE activation can be detrimental to normal cell growth but advantageous for malignant cell growth. In cancer, increased RAGE expression is correlated with a worse clinical prognosis, which is supported by AGE/RAGE signaling, driving survival, proliferation, migration, angiogenesis, and metastasis. Therefore, AGE/RAGE signaling is proposed to be a therapeutic target to prevent cancer onset and progression.

MG and MG-AGEs in Disease

MG and MG-AGEs are associated with the pathogenesis of numerous diseases including cancer, diabetes, and cardiac disease.− Here, we discuss the clinical relevance of MG and MG-AGEs in different human diseases and the impact of MG-AGEs in the context of RAGE (Figure 5).

MG and MG-AGEs in Cardiovascular Disease

Patients with heart failure secondary to diabetes have increased MG-AGEs on actin and myosin in heart muscle when compared to nonfailing controls or heart failure in individuals without diabetes. These modifications interfere with protein interaction with muscle and disrupt calcium sensitivity, both processes that are critical for proper cardiac function. In a study of comorbidity with HIV infection, a positive association between MG in the heart and plasma and an enhanced risk for heart failure was observed. Moreover, higher plasma MG levels were consistently associated with fatal cardiovascular events in individuals with type 1 diabetes (T1D). A similar finding was also made in individuals with type 2 diabetes (T2D) with elevated plasma MG associated with higher risk for atherosclerosis and high blood pressure, spurring interest in its utility as a predictive biomarker for heart disease.

In mice, MG-AGEs in the heart were associated with worse outcomes following myocardial infarction, specifically negative cardiac remodeling and cardiac dysfunction. In hypertensive rats, elevated aortic and plasma levels of MG and MG-AGEs were associated with oxidative stress, endothelial dysfunction, high blood pressure, and altered vasculature. These findings have since been recapitulated in patients with diabetes; elevated plasma and serum MG-AGEs were associated with microvascular complications, higher blood pressure, and markers of atherosclerosis and coronary heart disease.−

The AGE/RAGE axis, which describes the interplay between AGE production, binding to RAGE, and RAGE activation, has been associated with coronary artery disease resulting from hyperglycemia due to insulin resistance from T2D.− AGEs are proposed to lead to cardiac dysfunction by cross-linking low-density lipoproteins and extracellular matrix proteins such as collagen and elastin, causing stiffening of the blood vessel lining. Blockade of the AGE/RAGE axis via administration of sRAGE in mice demonstrated a dose-dependent drop in markers of atherosclerosis development. Taken together, this suggests that MG-AGEs may serve as an early indicator of impending atherosclerosis development and reduced heart function.

MG and MG-AGEs in Neurological Disease

MG and MG-AGEs are associated with the development of neurological disorders such as Alzheimer’s disease (AD), cerebral atrophy, polyneuropathies, and Parkinson’s disease (PD).− In humans, there is a negative association between serum MG levels and memory, overall executive function, and lower gray matter volume., This suggests that MG is associated with subsequent neurodegeneration and cognitive decline, particularly in older people. In AD, MG and MG-AGEs are posited to accumulate in β-amyloid plaque deposits and neurofibrillarytangles., In neuroblastoma cells, MG was neurotoxic and associated with increased ROS levels, triggering neuronal damage commonly seen in PD. In nerve biopsies of patients with vasculitic polyneuropathy, increased MG-AGEs, RAGE, and NFκB expression were detected in neural mononuclear cells and vessels.−

How MG and MG-AGEs drive cognitive decline and neurodegeneration is not known; however, they are proposed to trigger mitochondrial damage and inflammation in a RAGE-dependent manner. Older mice have elevated MG-AGEs in their cerebral cortices and hippocampi, leading to mitochondrial dysfunction. This observation was recapitulated in rats with streptozotocin-induced AD, which exhibited persistent activation of the MG/AGE/RAGE/NOX-2 pathway. Transgenic mouse models mimicking AD have increased expression and activation of RAGE in astrocytes, particularly those in the hippocampus, a key memory controller. The brains of patients with AD have nearly 2-fold higher MG levels than control individuals, with MG being 5–7 times higher in cerebrospinal fluid than in plasma. Likewise, AD patients have significantly higher hippocampi MG-AGEs, a finding recapitulated in the nigra neurons of PD patients. Furthermore, MG-AGEs are elevated in adipose tissue of patients with neuropathy, AD, or neural aging.− MG and MG-AGEs accumulate in glia and astrocytes, which have an increased expression of RAGE positively correlated with age.,− This suggests a possible link between elevated MG levels, increased MG-AGE production and accumulation, and their dispersal via the cerebrospinal fluid system, driving RAGE activation on cells throughout the central nervous system and driving disease onset and progression.

MG and MG-AGEs in Skeletomuscular Disease

Recent studies have highlighted the impact of MG and MG-AGEs on the skeletomuscular system. MG promotes bone degeneration; in both in vivo rat and in vitro models, MG led to osteoclastogenesis, a step in the osteoporosis development., In the macrophage cell line RAW264.7, MG activated c-Jun N-terminal kinases, suggesting MG propagates improper bone remodeling via the JNK pathway. Patients with diabetes are prone to developing pseudoarthrosis in which their ability to heal bone fractures is delayed. Diabetic mice exposed to MG and given a bone defect exhibited significantly delayed bone healing and osteoblast differentiation in a dose-dependent manner as opposed to nondiabetic control mice. Interestingly, they also had elevated levels of serum and bone MG-AGEs. This suggests that MG detoxification may mitigate bone degeneration and loss in patients with diabetes. Limonene, an antioxidative terpene, also mitigates the effects of MG on diabetic osteopathy; pretreatment of murine osteoblast cell line MC3T3-E1 with limonene reduced endoplasmic reticulum stress, ROS release, and cell death, which was recapitulated using spironolactone., However, the precise mechanism of this protective effect by both limonene and spironolactone is not fully elucidated.

Canonically, RAGE signaling in skeletal muscle is involved in normal skeletomuscular function and maintenance; however, depending on the ligand, RAGE activation also causes wasting, inflammation, and skeletal muscle aging.,, These effects are proposed to occur by AGE-mediated aging and cross-linking of critical components of the extracellular matrix such as collagen and the basal lamina., Collectively, this leaves the individual prone to developing overt skeletomuscular atrophy, sarcopenia, and osteoporosis., In myoblast cells, MG-AGEs increased oxidative stress and reduced myotube formation while upregulating RAGE expression and activation. In diabetic mice, skeletal muscle and plasma have significantly higher MG-AGEs compared to controls, suggesting a link between MG-AGE production and accumulation in the skeletal muscle. These findings were corroborated in vitro with MG treatment of C2C12 mouse myotube cells, resulting in higher levels of MG-AGEs. A mechanism for AGE/RAGE-mediated pathogenesis of myopathy occurred via AMPK-downregulation of the Akt cascade, exacerbating skeletomuscular dysfunction and subsequent loss.

MG and MG-AGEs in Renal Disease

Kidney disease is associated with hyperglycemia and metabolic dysfunction, suggesting an association with MG and MG-AGEs. Tezuka et al. conducted an observational study with 150 individuals at different stages of chronic kidney disease (CKD) with the goal of measuring plasma MG levels. They found plasma MG was positively associated with CKD, thus identifying MG as a potential tool for estimating kidney disease prognosis and stage. Rats treated with MG intragastrically had increased expression of mRNA of pro-inflammatory and oxidative pathways in the kidney transcriptome. This data was further supported by proteomic and metabolomic analyses which revealed heightened secretion of extracellular matrix components and membrane phospholipids in MG-treated rats, both of which are indispensable for proper kidney function., Furthermore, Glo1-deficient nondiabetic mice had altered kidney morphology akin to that of diabetic nephropathy, suggesting that MG contributes to the damage that is observed in CKD. Similarly, Glo1 overexpression in diabetic mice and rats mitigated MG-AGE production and subsequent oxidative stress, diabetic kidney disease, and retinopathy., Protein cross-linking by AGEs contributes heavily to tissue damage and is a marker for organ dysfunction. Measurement of MG-AGEs has also been used to predict kidney disease prognosis and progression.− Serum MG-AGEs are significantly, positively associated with decreased renal function in humans. Individuals with T1D showed higher urinary excretion of MG-AGEs that proved useful as an indicator of early renal failure., In individuals with end-stage CKD, MG-AGEs were strongly correlated with indicators of endothelial dysfunction and inflammation.,

Recently, Lee et al. made a similar finding in humans, demonstrating that in human mesangial cell lines, MG-AGEs trigger nephropathy via upregulating RAGE expression, leading to ROS production and activation of PI3K/AKT and NFκB. RAGE suppression via small-molecule inhibition and siRNA diminished oxidative stress and inflammatory response, suggesting the MG-AGE/RAGE axis contributes to nephrotic damage and dysfunction. This was also observed in rats with streptozotocin-induced nephropathy, in which treatment with Moutan Cortex mitigated AGE-induced inflammation, resulting in a protective effect. MG-AGEs also act through the RAGE/JNK pathway, causing mitochondrial and ER stress dysfunction as well as an upregulation of apoptotic markers such as p53 and Bax. Furthermore, gliclazide, a therapeutic for diabetes, conferred a protective effect on renal damage and dysfunction induced by MG-AGEs and hyperglycemia through inhibition of the AGE/RAGE/ROS/NFκB cascade. It is important to note that not every AGE/RAGE interaction triggers the same pathways; Baragetti et al. identified −374 T/A polymorphisms in RAGE that increased the risk of progression to CKD. This suggests that in renal dysfunction it may be beneficial to target downstream RAGE signaling, as opposed to upstream MG-AGE/RAGE binding.

MG and MG-AGEs in Liver Disease

In rats given carbon tetrachloride (CCl4) to induce early-stage hepatitis, liver MG levels and d-lactate were elevated compared to control untreated rats. Similarly, a clinical trial conducted by Michel et al. revealed a positive correlation between elevated levels of serum MG, liver cirrhosis, and widespread inflammation. Elevated serum and circulating MG levels were correlated with worsening liver disease prognosis and increased risk of developing additional liver-related complications, such as ascites. In HepG2 cells, MG impaired mitochondria, caused cell death via apoptosis, promoted ROS production, and diminished GSH levels, a critical component of the glyoxalase detoxification system. In vivo, MG administration led to acute liver toxicity as evidenced by elevated levels of alanine aminotransferase and aspartate aminotransferase, both indicators of liver health. Taken together, this suggests that MG induces liver disease by triggering mitochondrial dysfunction and oxidative stress as a result of excess ROS production.

To determine the impact of inflammation on MG regulation, rats were treated with CCl4, which led to MG accumulation in the liver, causing decreased Glo1 expression, increased production of MG-AGEs, and RAGE activation, causing inflammation and stress. The impact of MG on decreased Glo1 expression is intriguing as it suggests a positive feedback loop in which elevated MG prevents its own detoxification while continuing to cause hepatic dysfunction. Excess MG leads to further MG-AGE production, and several studies have identified elevated levels of MG-AGEs in both the plasma and the serum of patients with liver disease and in obese mice.− Serum MG-AGEs and sRAGE in nondiabetic patients are associated with nonalcoholic fatty liver disease. In addition, liver steatosis and inflammation led to elevated levels of circulating MG-AGEs.

Activation of the MG-AGE/RAGE axis increased apoptosis and TGF-β, TNF-α, IL-8, and IFN-γ levels., Further characterization of the crosstalk between the pro- and the anti-inflammatory cytokines released as a result of the AGE/RAGE axis in liver disease is needed to understand their role in hepatic dysfunction. The upregulation of these cytokines appears to be ablated upon administration of a siRNA-targeting RAGE in primary rat hepatic stellate cells and prevented overt disease progression. Subsequent in vivo administration of RAGE siRNA in rats recapitulated these in vitro findings and delayed the development of liver fibrosis via hampered activation of NFκB. Interestingly, deletion of Ager (the gene that encodes RAGE) did not prevent development of liver steatosis, which suggests an alternate RAGE-independent mechanism of liver dysfunction mediated by MG-AGEs.,

MG and MG-AGEs in Immune Disorders

Recent studies have implicated MG as a potent immunosuppressor. Price et al. were among the first to show that increased MG inhibited T-cell proliferation and triggered a loss of both pro- and anti-inflammatory cytokines, such as IFN-γ in myeloid cells and TNF-α and IL-10 in T cells. MG also reduced metabolic activity in myeloid-derived suppressor cells, a group of regulatory immune cells of myeloid origin. This suppressive phenotype was also found in CD8+ cytotoxic T cells, which was proposed to occur via MG transfer, thus causing further immunosuppression. MG modification of histone H2A increased immunogenicity, providing some evidence that it may be involved in the autoimmune response in cancer and generation of autoantibodies.

In vitro studies on the effects of MG-AGE accumulation on immune cells revealed that MG-AGEs impaired the activation of inflammasomes in macrophages, thus hampering innate immunosurveillance. This effect was independent of MG-AGEs binding to RAGE but rather occurred through the suppression of macrophage M1 polarization, which would otherwise trigger a pro-inflammatory state prone to phagocytosing foreign or unwanted material. Jin et al. found conflicting results, noting that MG-AGEs elevated RAGE expression in macrophages, subsequently triggering macrophage polarization into a pro-inflammatory M1 phenotype through NFκB pathway activation.

RAGE is expressed on T cells and antigen-presenting cells such as macrophages, dendritic cells, and B cells, and its activation drives both innate and adaptive immune responses. For example, the RAGE cascade is critical for T-cell priming and proliferation and mediates interactions between dendritic cells and T cells during cross-priming to propagate an adaptive immune response., However, this can have adverse effects in disease. RAGE is present on macrophages and microglia, which are two major cell groups that infiltrate and attack the central nervous system, leading to multiple sclerosis. In vivo clinical studies in patients with multiple sclerosis demonstrated an increase in MG and MG-AGEs in astrocytes and cerebrospinal fluid. This suggests that circulating MG-AGEs may have a role in paracrine signaling in the body by traveling to and activating RAGE-expressing immune cells, thus exacerbating the immune attack on the nerves., In multiple sclerosis patients, plasma CEL levels were significantly higher than their control counterparts and were also correlated with rate of relapse.

MG and MG-AGEs in Cancer

Current literature suggests that MG has a hormetic effect in cancer, serving a pro-tumorigenic role in certain conditions and an antitumorigenic effect in others. A selection of studies investigating the pro- or antitumor role of MG and MG-AGEs in various cancers is summarized in Table 1. As reviewed by Leone et al., there is an inverse correlation between MG concentration and cancer growth and metastasis. Cancers preferentially use glycolysis and have enhanced glucose uptake; they produce higher levels of MG. To counteract this, cancers overexpress GLO1, which may lead to oversaturation of available GLO1, leading to MG accumulation and toxicity.− Nokin et al. demonstrated that preconditioning cells with high glucose (500 mM) or MG (2.5 mM) successfully conditioned yeast to be more tolerant and resistant to higher concentrations of MG (20 mM) and subsequent oxidative damage, an effect found to be independent of GLO1. This is posited to be due to a hormetic mechanism by MG in that at low levels MG drives cancer growth but can cause adverse effects at high levels.

Any pro-tumor effect by MG and MG-AGEs can likely be attributed to a survival mechanism; cancer adapts to withstand detrimental effects of altered metabolic flux and rather uses it to its benefit, while antitumor effects are due to overwhelming dicarbonyl stress exceeding the tumor‘s detoxification capacity (Table 1). We hypothesize this is due to the complex metabolic and physiological milieu as well as biological variation that may cause different responses to these metabolites. Therefore, the precise concentration of MG and MG-AGEs that delineates a pro- or antitumor impact is not yet clear, as there are additional biological factors to consider. Despite this, measuring blood-derived cultures of both healthy and cancer patients revealed an upregulation of MG-AGEs in those with cancer. Furthermore, the pro-cancer role of AGE/RAGE activation and its downstream signaling cascades has been well established across multiple types of cancers, showing it inhibits apoptosis and promotes autophagy, angiogenesis via VEGF, growth, inflammation, and metastasis via pathways such as AP-1, NFκB, STAT3, SMAD4, MAPK, mTOR, and PI3K.,−

MG and MG-AGEs in Diabetes

Given that glucose metabolism is central to MG production, MG is heavily implicated in diseases where glucose levels are elevated, particularly T1D and T2D. In addition to inducing oxidative stress and inflammation via AGE/RAGE signaling, elevated intracellular MG levels impaired cellular responses to insulin, particularly with ERK1/2 and AKT, a signaling pathway indispensable in regulating insulin sensitivity and glucose uptake.− Thus, excess MG contributes to insulin resistance, which is characteristic of T2D. Both serum MG and MG-AGEs are significantly elevated in individuals with T1D and T2D.,− When measured in young patients with T1D without complications, serum MG levels were significantly higher than their control nondiabetic counterparts. These findings have been recapitulated in newly diagnosed patients with T2D, supporting a link between elevated MG levels and development of either T1D or T2D.

Individuals with T1D or T2D are at a high risk of developing secondary complications. Because these complications are associated with poor glycemic control, MG and MG-AGEs are proposed to be associated with and potentially drive them through RAGE-dependent mechanisms. The association of both MG and MG-AGEs in diabetic complications such as nephropathy, cardiovascular problems, cancer, and skeletomuscular disease have been extensively covered above. In addition to these, retinopathy, neuropathy, and vascular complications are associated with MG-AGEs.−

Measuring MG and MG-AGEs

Direct MG quantification is difficult because of its reactivity; therefore, MG-AGEs are proposed to be more accurate indicators of MG production (Figure 6A). Rabbani and Thornalley pioneered a unique technique to detect and quantify MG using stable isotopic dilution liquid chromatography with tandem mass spectrometry (LC-MS/MS). Using this method, they achieved a limit of detection of 8 fmol MG and a limit of quantitation of 90 fmol MG. This approach has clinical applications by measuring MG in blood and tissue., Likewise, technologies to measure MG-AGEs have provided diagnostic and prognostic tools. Initial approaches involved the use of skin autofluorescence, a noninvasive technique that measures tissue accumulation of MG-AGEs, a technique that has proven useful in predicting development of cardiovascular disease, microvascular complications, or kidney transplant rejection. In contrast, newer methods use mass spectrometry or colorimetric and fluorometric profiling of MG-AGEs to allow for rapid measurement and analysis of clinically relevant concentrations.,−

Quantification of MG and MG-AGEs via methods such as LC-MS/MS and ELISA support the use of MG and MG-AGEs as biomarkers for diseases such as T2D, Alzheimer’s disease, chronic kidney disease, nonalcoholic fatty liver disease, atherosclerosis, and others.,,,, MG-H1 was measured in biological samples, including aortic tissue and lens protein, with a high correlation to AGE formation., Taken together, this presents a novel and quantifiable class of metabolites to aid in not only predicting disease but also informing disease state and prognosis.

Targeting MG and MG-AGEs and Preventing Their formation

The prevalence of MG and MG-AGEs during both normal and disease states makes regulating their levels an attractive target to mitigate disease severity and progression. Aside from the canonical pathways involved in MG detoxification, recent advances have generated considerable interest in approaches to selectively target MG and MG-AGEs to offset their associated damage and effects (Figure 6B, Table 2). While there are pharmacological approaches to preventing MG and MG-AGE formation and accumulation, their potential for clinical application requires additional investigation. Alternatively, nonpharmacological approaches such as diet and exercise may have utility in decreasing MG and MG-AGE formation by regulating metabolic flux.

Targeting RAGE

Pharmacological targeting of RAGE has been explored using antibody and small-molecule-based methods. Blocking RAGE activation by treating endothelial cells with anti-RAGE antibodies decreased the oxidative damage caused by RAGE activation, highlighting its potential as a therapeutic approach. Since then, RAGE inhibition using compounds such as FPS-ZM1 or azeliragon in a murine model of acute lung injury reduced RAGE activation and expression and decreased inflammation and damage. Similar findings have been reported in murine models of Alzheimer’s disease as well, finding that azeliragon was nontoxic in rats and helped reduced Alzheimer’s injury and progression. Additional human clinical trial evidence has supported the use of azeliragon in ameliorating the deleterious effects associated with RAGE activation, yielding promising results and demonstrating its safety profile and tolerance in humans., Although the precise mechanism by which azeliragon acts has not been fully elucidated, it is proposed to be a RAGE antagonist. Similar findings have been reported in studies of GM-1111, a semisynthetic glycosaminoglycan ether, which was found to inhibit interactions between RAGE and its ligands, such as S100B, HMGB-1, and CML-BSA, an AGE. In addition, other inhibitors and approaches to targeting RAGE have been developed. They are shown in Figure 6B and summarized in Table 3. However, due to RAGE’s ubiquitous nature, there is a risk of off-target toxicity and unwanted side effects that could result from indiscriminate RAGE targeting.

Conclusion

All living organisms perform metabolism, a process vital for life. Despite its necessity in sustaining life, metabolic perturbations underlie the pathology of many diseases. The mechanisms leading this are not clear, but MG, MG-AGEs, and RAGE are shown to play a critical role in many metabolism-driven diseases. Elucidation of their role in promoting disease onset and progression has been increasingly appreciated and studied as an invaluable asset to aid in our understanding of how and why certain diseases develop.

Despite many significant clinical advances in the treatment of human disease, there remains a gap in knowledge allowing us to predict and intervene to prevent or treat diseases early rather than after irreversible damage has occurred. Furthermore, there is a shortage of clinically relevant and quantifiable biomarkers of disease that would aid in the process. Current ways of predicting disease, such as the measurement of HbA1c in diabetes, only allow physicians to see a snapshot in time. On the other hand, metabolism is a process that can be continually monitored, and metabolism flux can be studied as it occurs. Therefore, we believe that the study of metabolites and their role in disease as progressors and predictors may yield a slew of novel viable biomarker candidates for clinical application. As such, further characterization of the biochemistry and interactions of MG, MG-AGEs, and RAGE is critical to study how their role in the body can be exploited for therapeutic benefit.

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    Chen J.; Huang W.; Cheng C.-H.; Zhou L.; Jiang G.-B.; Hu Y.-Y. Association Between Aldehyde Dehydrogenase-2 Polymorphisms and Risk of Alzheimer’s Disease and Parkinson’s Disease: A Meta-Analysis Based on 5,315 Individuals. Front. Neurol. 2019, 10, 290.

    Not in our library10.3389/fneur.2019.00290

  58. 58.

    Izaguirre G.; Kikonyogo A.; Pietruszko R. Methylglyoxal as Substrate and Inhibitor of Human Aldehyde Dehydrogenase: Comparison of Kinetic Properties among the Three Isozymes. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 1998, 119 (4), 747–754..

    Not in our library10.1016/s0305-0491(98)00051-0

  59. 59.

    Vander Jagt D. L.; Hunsaker L. A. Methylglyoxal Metabolism and Diabetic Complications: Roles of Aldose Reductase, Glyoxalase-I, Betaine Aldehyde Dehydrogenase and 2-Oxoaldehyde Dehydrogenase. Chem. Biol. Interact. 2003, 143–144, 341–351..

    Not in our library10.1016/s0009-2797(02)00212-0

  60. 60.

    Chen C.-H.; Ferreira J. C. B.; Gross E. R.; Mochly-Rosen D. Targeting Aldehyde Dehydrogenase 2: New Therapeutic Opportunities. Physiol. Rev. 2014, 94 (1), 1–34..

    Not in our library10.1152/physrev.00017.2013

  61. 61.

    Desai K. M.; Chang T.; Wang H.; Banigesh A.; Dhar A.; Liu J.; Untereiner A.; Wu L. Oxidative Stress and Aging: Is Methylglyoxal the Hidden Enemy?. Can. J. Physiol. Pharmacol. 2010, 88 (3), 273–284..

    Not in our library10.1139/y10-001

  62. 62.
    Elevated 4-hydroxynonenal induces hyperglycaemia via Aldh3a1 loss in zebrafish and associates with diabetes progression in humans · 2020
    Not checked
  63. 63.

    Srivastava S. K.; Ramana K. V.; Bhatnagar A. Role of Aldose Reductase and Oxidative Damage in Diabetes and the Consequent Potential for Therapeutic Options. Endocr. Rev. 2005, 26 (3), 380–392..

    Not in our library10.1210/er.2004-0028

  64. 64.

    Vander Jagt D. L.; Robinson B.; Taylor K. K.; Hunsaker L. A. Reduction of Trioses by NADPH-Dependent Aldo-Keto Reductases. Aldose Reductase, Methylglyoxal, and Diabetic Complications. J. Biol. Chem. 1992, 267 (7), 4364–4369..

    Not in our library10.1016/s0021-9258(18)42844-x

  65. 65.

    Jannapureddy S.; Sharma M.; Yepuri G.; Schmidt A. M.; Ramasamy R. Aldose Reductase: An Emerging Target for Development of Interventions for Diabetic Cardiovascular Complications. Front. Endocrinol. 2021, 12, 636267.

    Not in our library10.3389/fendo.2021.636267

  66. 66.

    Demaine A.; Cross D.; Millward A. Polymorphisms of the Aldose Reductase Gene and Susceptibility to Retinopathy in Type 1 Diabetes Mellitus. Invest. Ophthalmol. Vis. Sci. 2000, 41 (13), 4064–4068.

    Not in our library

  67. 67.

    Moczulski D. K.; Scott L.; Antonellis A.; Rogus J. J.; Rich S. S.; Warram J. H.; Krolewski A. S. Aldose Reductase Gene Polymorphisms and Susceptibility to Diabetic Nephropathy in Type 1 Diabetes Mellitus. Diabet. Med. J. Br. Diabet. Assoc. 2000, 17 (2), 111–118..

    Not in our library10.1046/j.1464-5491.2000.00225.x

  68. 68.

    Shah V. O.; Scavini M.; Nikolic J.; Sun Y.; Vai S.; Griffith J. K.; Dorin R. I.; Stidley C.; Yacoub M.; Vander Jagt D. L.; Eaton R. P.; Zager P. G. Z-2 Microsatellite Allele Is Linked to Increased Expression of the Aldose Reductase Gene in Diabetic Nephropathy. J. Clin. Endocrinol. Metab. 1998, 83 (8), 2886–2891..

    Not in our library10.1210/jcem.83.8.5028

  69. 69.

    Heesom A. E.; Millward A.; Demaine A. G. Susceptibility to Diabetic Neuropathy in Patients with Insulin Dependent Diabetes Mellitus Is Associated with a Polymorphism at the 5′ End of the Aldose Reductase Gene. J. Neurol. Neurosurg. Psychiatry 1998, 64 (2), 213–216..

    Not in our library10.1136/jnnp.64.2.213

  70. 70.

    Vander Jagt D. L.; Hassebrook R. K.; Hunsaker L. A.; Brown W. M.; Royer R. E. Metabolism of the 2-Oxoaldehyde Methylglyoxal by Aldose Reductase and by Glyoxalase-I: Roles for Glutathione in Both Enzymes and Implications for Diabetic Complications. Chem. Biol. Interact. 2001, 130–132 (1–3), 549–562..

    Not in our library10.1016/s0009-2797(00)00298-2

  71. 71.

    Morgenstern J.; Fleming T.; Schumacher D.; Eckstein V.; Freichel M.; Herzig S.; Nawroth P. Loss of Glyoxalase 1 Induces Compensatory Mechanism to Achieve Dicarbonyl Detoxification in Mammalian Schwann Cells. J. Biol. Chem. 2017, 292 (8), 3224–3238..

    Not in our library10.1074/jbc.m116.760132

  72. 72.

    Lee K. W.; Ko B. C.; Jiang Z.; Cao D.; Chung S. S. Overexpression of Aldose Reductase in Liver Cancers May Contribute to Drug Resistance. Anticancer. Drugs 2001, 12 (2), 129–132..

    Not in our library10.1097/00001813-200102000-00005

  73. 73.

    Chang K.-C.; Shieh B.; Petrash J. M. Aldose Reductase Mediates Retinal Microglia Activation. Biochem. Biophys. Res. Commun. 2016, 473 (2), 565–571..

    Not in our library10.1016/j.bbrc.2016.03.122

  74. 74.

    Srivastava S. K.; Yadav U. C. S.; Reddy A. B. M.; Saxena A.; Tammali R.; Shoeb M.; Ansari N. H.; Bhatnagar A.; Petrash M. J.; Srivastava S.; Ramana K. V. Aldose Reductase Inhibition Suppresses Oxidative Stress-Induced Inflammatory Disorders. Chem. Biol. Interact. 2011, 191 (1–3), 330–338..

    Not in our library10.1016/j.cbi.2011.02.023

  75. 75.

    Vikramadithyan R. K.; Hu Y.; Noh H.-L.; Liang C.-P.; Hallam K.; Tall A. R.; Ramasamy R.; Goldberg I. J. Human Aldose Reductase Expression Accelerates Diabetic Atherosclerosis in Transgenic Mice. J. Clin. Invest. 2005, 115 (9), 2434–2443..

    Not in our library10.1172/jci24819

  76. 76.

    Yagihashi S.; Yamagishi S. I.; Wada Ri R.; Baba M.; Hohman T. C.; Yabe-Nishimura C.; Kokai Y. Neuropathy in Diabetic Mice Overexpressing Human Aldose Reductase and Effects of Aldose Reductase Inhibitor. Brain J. Neurol. 2001, 124 (12), 2448–2458..

    Not in our library10.1093/brain/124.12.2448

  77. 77.

    Ahmed N.; Thornalley P. J.; Dawczynski J.; Franke S.; Strobel J.; Stein G.; Haik G. M. Methylglyoxal-Derived Hydroimidazolone Advanced Glycation End-Products of Human Lens Proteins. Invest. Ophthalmol. Vis. Sci. 2003, 44 (12), 5287–5292..

    Not in our library10.1167/iovs.03-0573

  78. 78.

    Lo T. W.; Westwood M. E.; McLellan A. C.; Selwood T.; Thornalley P. J. Binding and Modification of Proteins by Methylglyoxal under Physiological Conditions. A Kinetic and Mechanistic Study with N Alpha-Acetylarginine, N Alpha-Acetylcysteine, and N Alpha-Acetyllysine, and Bovine Serum Albumin. J. Biol. Chem. 1994, 269 (51), 32299–32305..

    Not in our library10.1016/s0021-9258(18)31635-1

  79. 79.

    Li Y.; Cohenford M. A.; Dutta U.; Dain J. A. The Structural Modification of DNA Nucleosides by Nonenzymatic Glycation: An in Vitro Study Based on the Reactions of Glyoxal and Methylglyoxal with 2′-Deoxyguanosine. Anal. Bioanal. Chem. 2008, 390 (2), 679–688..

    Not in our library10.1007/s00216-007-1682-4

  80. 80.

    Schneider M.; Quistad G. B.; Casida J. E. N2,7-Bis(1-Hydroxy-2-Oxopropyl)-2′-Deoxyguanosine: Identical Noncyclic Adducts with 1,3-Dichloropropene Epoxides and Methylglyoxal. Chem. Res. Toxicol. 1998, 11 (12), 1536–1542..

    Not in our library10.1021/tx9801256

  81. 81.

    al-Abed Y.; Schleicher E.; Voelter W.; Liebich H.; Papoulis A.; Bucala R. Identification of N2-(1-Carboxymethyl)Guanine (CMG) as a Guanine Advanced Glycation End Product. Bioorg. Med. Chem. Lett. 1998, 8 (16), 2109–2110..

    Not in our library10.1016/s0960-894x(98)00398-9

  82. 82.

    Schärer O. D. Chemistry and Biology of DNA Repair. Angew. Chem., Int. Ed. Engl. 2003, 42 (26), 2946–2974..

    Not in our library10.1002/anie.200200523

  83. 83.

    Schärer O. D. Nucleotide Excision Repair in Eukaryotes. Cold Spring Harb. Perspect. Biol. 2013, 5 (10), a012609.

    Not in our library10.1101/cshperspect.a012609

  84. 84.

    Maynard S.; Schurman S. H.; Harboe C.; de Souza-Pinto N. C.; Bohr V. A. Base Excision Repair of Oxidative DNA Damage and Association with Cancer and Aging. Carcinogenesis 2008, 30 (1), 2–10..

    Not in our library10.1093/carcin/bgn250

  85. 85.

    Li G.-M. Mechanisms and Functions of DNA Mismatch Repair. Cell Res. 2008, 18 (1), 85–98..

    Not in our library10.1038/cr.2007.115

  86. 86.

    Tamae D.; Lim P.; Wuenschell G. E.; Termini J. Mutagenesis and Repair Induced by the DNA Advanced Glycation End Product N2–1-(Carboxyethyl)-2′-Deoxyguanosine in Human Cells. Biochemistry 2011, 50 (12), 2321–2329..

    Not in our library10.1021/bi101933p

  87. 87.

    Ciminera A. K.; Shuck S. C.; Termini J. Elevated Glucose Increases Genomic Instability by Inhibiting Nucleotide Excision Repair. Life Sci. Alliance 2021, 4 (10), e202101159.

    Not in our library10.26508/lsa.202101159

  88. 88.

    Pischetsrieder M.; Seidel W.; Münch G.; Schinzel R. N(2)-(1-Carboxyethyl)Deoxyguanosine, a Nonenzymatic Glycation Adduct of DNA, Induces Single-Strand Breaks and Increases Mutation Frequencies. Biochem. Biophys. Res. Commun. 1999, 264 (2), 544–549..

    Not in our library10.1006/bbrc.1999.1528

  89. 89.

    Bronzetti G.; Corsi C.; Chiaro D. D.; Boccardo P.; Vellosi R.; Rossi F.; Paolini M.; Forti G. C. Methylglyoxal: Genotoxicity Studies and Its Effect in Vivo on the Hepatic Microsomal Mono-Oxygenase System of the Mouse. Mutagenesis 1987, 2 (4), 275–277..

    Not in our library10.1093/mutage/2.4.275

  90. 90.

    Cajelli E.; Canonero R.; Martelli A.; Brambilla G. Methylglyoxal-Induced Mutation to 6-Thioguanine Resistance in V79 Cells. Mutat. Res. 1987, 190 (1), 47–50..

    Not in our library10.1016/0165-7992(87)90081-9

  91. 91.

    Hou S. M.; Nori P.; Fang J. L.; Vaca C. E. Methylglyoxal Induces Hprt Mutation and DNA Adducts in Human T-Lymphocytes in Vitro. Environ. Mol. Mutagen. 1995, 26 (4), 286–291..

    Not in our library10.1002/em.2850260404

  92. 92.

    Bessho T. Nucleotide Excision Repair 3′ Endonuclease XPG Stimulates the Activity of Base Excision Repairenzyme Thymine Glycol DNA Glycosylase. Nucleic Acids Res. 1999, 27 (4), 979–983..

    Not in our library10.1093/nar/27.4.979

  93. 93.

    Murata-Kamiya N.; Kamiya H.; Kaji H.; Kasai H. Methylglyoxal Induces G:C to C:G and G:C to T:A Transversions in the SupF Gene on a Shuttle Vector Plasmid Replicated in Mammalian Cells. Mutat. Res. 2000, 468 (2), 173–182..

    Not in our library10.1016/s1383-5718(00)00044-9

  94. 94.

    Murata-Kamiya N.; Kaji H.; Kasai H. Deficient Nucleotide Excision Repair Increases Base-Pair Substitutions but Decreases TGGC Frameshifts Induced by Methylglyoxal in Escherichia Coli. Mutat. Res. 1999, 442 (1), 19–28..

    Not in our library10.1016/s1383-5718(99)00054-6

  95. 95.

    Yuan B.; Cao H.; Jiang Y.; Hong H.; Wang Y. Efficient and Accurate Bypass of N2-(1-Carboxyethyl)-2′-Deoxyguanosine by DinB DNA Polymerase in Vitro and in Vivo. Proc. Natl. Acad. Sci. U. S. A. 2008, 105 (25), 8679–8684..

    Not in our library10.1073/pnas.0711546105

  96. 96.

    Takahashi K. The Reaction of Phenylglyoxal with Arginine Residues in Proteins. J. Biol. Chem. 1968, 243 (23), 6171–6179..

    Not in our library10.1016/s0021-9258(18)94475-3

  97. 97.

    Klöpfer A.; Spanneberg R.; Glomb M. A. Formation of Arginine Modifications in a Model System of Nα-Tert-Butoxycarbonyl (Boc)-Arginine with Methylglyoxal. J. Agric. Food Chem. 2011, 59 (1), 394–401..

    Not in our library10.1021/jf103116c

  98. 98.

    McEwen J. M.; Fraser S.; Guir A. L. S.; Dave J.; Scheck R. A. Synergistic Sequence Contributions Bias Glycation Outcomes. Nat. Commun. 2021, 12 (1), 3316.

    Not in our library10.1038/s41467-021-23625-8

  99. 99.

    Ahmed M. U.; Brinkmann Frye E.; Degenhardt T. P.; Thorpe S. R.; Baynes J. W. N-Epsilon-(Carboxyethyl)Lysine, a Product of the Chemical Modification of Proteins by Methylglyoxal, Increases with Age in Human Lens Proteins. Biochem. J. 1997, 324 (2), 565–570..

    Not in our library10.1042/bj3240565

  100. 100.

    Thornalley P. J.; Battah S.; Ahmed N.; Karachalias N.; Agalou S.; Babaei-Jadidi R.; Dawnay A. Quantitative Screening of Advanced Glycation Endproducts in Cellular and Extracellular Proteins by Tandem Mass Spectrometry. Biochem. J. 2003, 375 (3), 581–592..

    Not in our library10.1042/bj20030763

  101. 101.

    Meade S. J.; Miller A. G.; Gerrard J. A. The Role of Dicarbonyl Compounds in Non-Enzymatic Crosslinking: A Structure-Activity Study. Bioorg. Med. Chem. 2003, 11 (6), 853–862..

    Not in our library10.1016/s0968-0896(02)00564-3

  102. 102.

    Murata-Kamiya N.; Kamiya H. Methylglyoxal, an Endogenous Aldehyde, Crosslinks DNA Polymerase and the Substrate DNA. Nucleic Acids Res. 2001, 29 (16), 3433–3438..

    Not in our library10.1093/nar/29.16.3433

  103. 103.

    Petrova K. V.; Millsap A. D.; Stec D. F.; Rizzo C. J. Characterization of the Deoxyguanosine-Lysine Cross-Link of Methylglyoxal. Chem. Res. Toxicol. 2014, 27 (6), 1019–1029..

    Not in our library10.1021/tx500068v

  104. 104.

    Leoncini G.; Maresca M.; Ronchi S.; Bonsignore A. Studies on the Inactivation of Glyceraldehyde-3-Phosphate Dehydrogenase by Methylglyoxal. Experientia 1981, 37 (5), 443–444..

    Not in our library10.1007/bf01986121

  105. 105.

    Mira M. L.; Martinho F.; Azevedo M. S.; Manso C. F. Oxidative Inhibition of Red Blood Cell ATPases by Glyceraldehyde. Biochim. Biophys. Acta 1991, 1060 (3), 257–261..

    Not in our library10.1016/s0005-2728(05)80315-9

  106. 106.

    Irshad Z.; Xue M.; Ashour A.; Larkin J. R.; Thornalley P. J.; Rabbani N. Activation of the Unfolded Protein Response in High Glucose Treated Endothelial Cells Is Mediated by Methylglyoxal. Sci. Rep. 2019, 9 (1), 7889.

    Not in our library10.1038/s41598-019-44358-1

  107. 107.

    Muranova L. K.; Perfilov M. M.; Serebryakova M. V.; Gusev N. B. Effect of Methylglyoxal Modification on the Structure and Properties of Human Small Heat Shock Protein HspB6 (Hsp20). Cell Stress Chaperones 2016, 21 (4), 617–629..

    Not in our library10.1007/s12192-016-0686-4

  108. 108.

    Nagaraj R. H.; Oya-Ito T.; Padayatti P. S.; Kumar R.; Mehta S.; West K.; Levison B.; Sun J.; Crabb J. W.; Padival A. K. Enhancement of Chaperone Function of Alpha-Crystallin by Methylglyoxal Modification. Biochemistry 2003, 42 (36), 10746–10755..

    Not in our library10.1021/bi034541n

  109. 109.

    Padival A. K.; Crabb J. W.; Nagaraj R. H. Methylglyoxal Modifies Heat Shock Protein 27 in Glomerular Mesangial Cells. FEBS Lett. 2003, 551 (1–3), 113–118..

    Not in our library10.1016/s0014-5793(03)00874-3

  110. 110.

    Sakamoto H.; Mashima T.; Yamamoto K.; Tsuruo T. Modulation of Heat-Shock Protein 27 (Hsp27) Anti-Apoptotic Activity by Methylglyoxal Modification. J. Biol. Chem. 2002, 277 (48), 45770–45775..

    Not in our library10.1074/jbc.m207485200

  111. 111.

    Pozzi A.; Zent R.; Chetyrkin S.; Borza C.; Bulus N.; Chuang P.; Chen D.; Hudson B.; Voziyan P. Modification of Collagen IV by Glucose or Methylglyoxal Alters Distinct Mesangial Cell Functions. J. Am. Soc. Nephrol. JASN 2009, 20 (10), 2119–2125..

    Not in our library10.1681/asn.2008080900

  112. 112.

    Ahmed N.; Dobler D.; Dean M.; Thornalley P. J. Peptide Mapping Identifies Hotspot Site of Modification in Human Serum Albumin by Methylglyoxal Involved in Ligand Binding and Esterase Activity. J. Biol. Chem. 2005, 280 (7), 5724–5732..

    Not in our library10.1074/jbc.m410973200

  113. 113.

    Ceradini D. J.; Yao D.; Grogan R. H.; Callaghan M. J.; Edelstein D.; Brownlee M.; Gurtner G. C. Decreasing Intracellular Superoxide Corrects Defective Ischemia-Induced New Vessel Formation in Diabetic Mice. J. Biol. Chem. 2008, 283 (16), 10930–10938..

    Not in our library10.1074/jbc.m707451200

  114. 114.
    Reversible histone glycation is associated with disease-related changes in chromatin architecture · 2019
    No notice
  115. 115.

    Jeong J.; Lee J.; Lim J.; Cho S.; An S.; Lee M.; Yoon N.; Seo M.; Lim S.; Park S. Soluble RAGE Attenuates AngII-Induced Endothelial Hyperpermeability by Disrupting HMGB1-Mediated Crosstalk between AT1R and RAGE. Exp. Mol. Med. 2019, 51 (9), 1–15..

    Not in our library10.1038/s12276-019-0312-5

  116. 116.
    The receptor RAGE: Bridging inflammation and cancer · 2009
    No notice
  117. 117.

    Kierdorf K.; Fritz G. RAGE Regulation and Signaling in Inflammation and Beyond. J. Leukoc. Biol. 2013, 94 (1), 55–68..

    Not in our library10.1189/jlb.1012519

  118. 118.

    Hansen L.; Joseph G.; Valdivia A.; Taylor W. R. Satellite Cell Expression of RAGE (Receptor for Advanced Glycation End Products) Is Important for Collateral Vessel Formation. J. Am. Heart Assoc. 2021, 10 (21), e022127.

    Not in our library10.1161/jaha.120.022127

  119. 119.

    Chen M.-C.; Chen K.-C.; Chang G.-C.; Lin H.; Wu C.-C.; Kao W.-H.; Teng C.-L. J.; Hsu S.-L.; Yang T.-Y. RAGE Acts as an Oncogenic Role and Promotes the Metastasis of Human Lung Cancer. Cell Death Dis. 2020, 11 (4), 265.

    Not in our library10.1038/s41419-020-2432-1

  120. 120.

    Kang R.; Loux T.; Tang D.; Schapiro N. E.; Vernon P.; Livesey K. M.; Krasinskas A.; Lotze M. T.; Zeh H. J. 3rd. The Expression of the Receptor for Advanced Glycation Endproducts (RAGE) Is Permissive for Early Pancreatic Neoplasia. Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (18), 7031–7036..

    Not in our library10.1073/pnas.1113865109

  121. 121.

    Pusterla T.; Nèmeth J.; Stein I.; Wiechert L.; Knigin D.; Marhenke S.; Longerich T.; Kumar V.; Arnold B.; Vogel A.; Bierhaus A.; Pikarsky E.; Hess J.; Angel P. Receptor for Advanced Glycation Endproducts (RAGE) Is a Key Regulator of Oval Cell Activation and Inflammation-Associated Liver Carcinogenesis in Mice. Hepatol. Baltim. Md 2013, 58 (1), 363–373..

    Not in our library10.1002/hep.26395

  122. 122.
    RAGE (Receptor for Advanced Glycation Endproducts), RAGE Ligands, and their role in Cancer and Inflammation · 2009
    No notice
  123. 123.

    Xie J.; Reverdatto S.; Frolov A.; Hoffmann R.; Burz D. S.; Shekhtman A. Structural Basis for Pattern Recognition by the Receptor for Advanced Glycation End Products (RAGE. J. Biol. Chem. 2008, 283 (40), 27255–27269..

    Not in our library10.1074/jbc.m801622200

  124. 124.

    Xue J.; Rai V.; Singer D.; Chabierski S.; Xie J.; Reverdatto S.; Burz D. S.; Schmidt A. M.; Hoffmann R.; Shekhtman A. Advanced Glycation End Product Recognition by the Receptor for AGEs. Structure 2011, 19 (5), 722–732..

    Not in our library10.1016/j.str.2011.02.013

  125. 125.

    Xue J.; Ray R.; Singer D.; Böhme D.; Burz D. S.; Rai V.; Hoffmann R.; Shekhtman A. The Receptor for Advanced Glycation End Products (RAGE) Specifically Recognizes Methylglyoxal-Derived AGEs. Biochemistry 2014, 53 (20), 3327–3335..

    Not in our library10.1021/bi500046t

  126. 126.

    He M.; Kubo H.; Morimoto K.; Fujino N.; Suzuki T.; Takahasi T.; Yamada M.; Yamaya M.; Maekawa T.; Yamamoto Y.; Yamamoto H. Receptor for Advanced Glycation End Products Binds to Phosphatidylserine and Assists in the Clearance of Apoptotic Cells. EMBO Rep. 2011, 12 (4), 358–364..

    Not in our library10.1038/embor.2011.28

  127. 127.

    Tian J.; Avalos A. M.; Mao S.-Y.; Chen B.; Senthil K.; Wu H.; Parroche P.; Drabic S.; Golenbock D.; Sirois C.; Hua J.; An L. L.; Audoly L.; La Rosa G.; Bierhaus A.; Naworth P.; Marshak-Rothstein A.; Crow M. K.; Fitzgerald K. A.; Latz E.; Kiener P. A.; Coyle A. J. Toll-like Receptor 9-Dependent Activation by DNA-Containing Immune Complexes Is Mediated by HMGB1 and RAGE. Nat. Immunol. 2007, 8 (5), 487–496..

    Not in our library10.1038/ni1457

  128. 128.

    Huttunen H. J.; Kuja-Panula J.; Sorci G.; Agneletti A. L.; Donato R.; Rauvala H. Coregulation of Neurite Outgrowth and Cell Survival by Amphoterin and S100 Proteins through Receptor for Advanced Glycation End Products (RAGE) Activation. J. Biol. Chem. 2000, 275 (51), 40096–40105..

    Not in our library10.1074/jbc.m006993200

  129. 129.

    Yamamoto Y.; Harashima A.; Saito H.; Tsuneyama K.; Munesue S.; Motoyoshi S.; Han D.; Watanabe T.; Asano M.; Takasawa S.; Okamoto H.; Shimura S.; Karasawa T.; Yonekura H.; Yamamoto H. Septic Shock Is Associated with Receptor for Advanced Glycation End Products Ligation of LPS. J. Immunol. 2011, 186 (5), 3248–3257..

    Not in our library10.4049/jimmunol.1002253

  130. 130.

    Sirois C. M.; Jin T.; Miller A. L.; Bertheloot D.; Nakamura H.; Horvath G. L.; Mian A.; Jiang J.; Schrum J.; Bossaller L.; Pelka K.; Garbi N.; Brewah Y.; Tian J.; Chang C.; Chowdhury P. S.; Sims G. P.; Kolbeck R.; Coyle A. J.; Humbles A. A.; Xiao T. S.; Latz E. RAGE Is a Nucleic Acid Receptor That Promotes Inflammatory Responses to DNA. J. Exp. Med. 2013, 210 (11), 2447–2463..

    Not in our library10.1084/jem.20120201

  131. 131.

    Huang J. S.; Guh J. Y.; Chen H. C.; Hung W. C.; Lai Y. H.; Chuang L. Y. Role of Receptor for Advanced Glycation End-Product (RAGE) and the JAK/STAT-Signaling Pathway in AGE-Induced Collagen Production in NRK-49F Cells. J. Cell. Biochem. 2001, 81 (1), 102–113..

    Not in our library10.1002/1097-4644(20010401)81:1<102::aid-jcb1027>3.0.co;2-y

  132. 132.

    Qin Q.; Niu J.; Wang Z.; Xu W.; Qiao Z.; Gu Y. Heparanase Induced by Advanced Glycation End Products (AGEs) Promotes Macrophage Migration Involving RAGE and PI3K/AKT Pathway. Cardiovasc. Diabetol. 2013, 12, 37.

    Not in our library10.1186/1475-2840-12-37

  133. 133.

    Zhu P.; Ren M.; Yang C.; Hu Y.-X.; Ran J.-M.; Yan L. Involvement of RAGE, MAPK and NF-KB Pathways in AGEs-Induced MMP-9 Activation in HaCaT Keratinocytes. Exp. Dermatol 2012, 21 (2), 123–129..

    Not in our library10.1111/j.1600-0625.2011.01408.x

  134. 134.

    Tóbon-Velasco J. C.; Cuevas E.; Torres-Ramos M. A. Receptor for AGEs (RAGE) as Mediator of NF-KB Pathway Activation in Neuroinflammation and Oxidative Stress. CNS Neurol. Disord. Drug Targets 2014, 13 (9), 1615–1626..

    Not in our library10.2174/1871527313666140806144831

  135. 135.

    Chen Y.-H.; Chen Z.-W.; Li H.-M.; Yan X.-F.; Feng B. AGE/RAGE-Induced EMP Release via the NOX-Derived ROS Pathway. J. Diabetes Res. 2018, 2018, 6823058.

    Not in our library10.1155/2018/6823058

  136. 136.

    Lin L.; Park S.; Lakatta E. G. RAGE Signaling in Inflammation and Arterial Aging. Front. Biosci. (Landmark Ed.) 2009, 14 (4), 1403–1413..

    Not in our library10.2741/3315

  137. 137.

    Taniguchi K.; Karin M. NF-KB, Inflammation, Immunity and Cancer: Coming of Age. Nat. Rev. Immunol. 2018, 18 (5), 309–324..

    Not in our library10.1038/nri.2017.142

  138. 138.

    Lappas M.; Permezel M.; Rice G. E. Advanced Glycation Endproducts Mediate Pro-Inflammatory Actions in Human Gestational Tissues via Nuclear Factor-KappaB and Extracellular Signal-Regulated Kinase 1/2. J. Endocrinol 2007, 193 (2), 269–277..

    Not in our library10.1677/joe-06-0081

  139. 139.

    Park S.; Yoon S.-J.; Tae H.-J.; Shim C. Y. RAGE and Cardiovascular Disease. Front. Biosci. (Landmark Ed.) 2011, 16 (2), 486–497..

    Not in our library10.2741/3700

  140. 140.

    Bao J.-M.; He M.-Y.; Liu Y.-W.; Lu Y.-J.; Hong Y.-Q.; Luo H.-H.; Ren Z.-L.; Zhao S.-C.; Jiang Y. AGE/RAGE/Akt Pathway Contributes to Prostate Cancer Cell Proliferation by Promoting Rb Phosphorylation and Degradation. Am. J. Cancer Res. 2015, 5 (5), 1741–1750.

    Not in our library

  141. 141.

    Ko S.-Y.; Ko H.-A.; Shieh T.-M.; Chang W.-C.; Chen H.-I.; Chang S.-S.; Lin I.-H. Cell Migration Is Regulated by AGE-RAGE Interaction in Human Oral Cancer Cells in Vitro. PloS One 2014, 9 (10), e110542.

    Not in our library10.1371/journal.pone.0110542

  142. 142.

    Muthyalaiah Y. S.; Jonnalagadda B.; John C. M.; Arockiasamy S. Impact of Advanced Glycation End Products (AGEs) and Its Receptor (RAGE) on Cancer Metabolic Signaling Pathways and Its Progression. Glycoconj. J. 2021, 38 (6), 717–734..

    Not in our library10.1007/s10719-021-10031-x

  143. 143.

    Schalkwijk C. G.; Stehouwer C. D. A. Methylglyoxal, a Highly Reactive Dicarbonyl Compound, in Diabetes, Its Vascular Complications, and Other Age-Related Diseases. Physiol. Rev. 2020, 100 (1), 407–461..

    Not in our library10.1152/physrev.00001.2019

  144. 144.

    Leone A.; Nigro C.; Nicolò A.; Prevenzano I.; Formisano P.; Beguinot F.; Miele C. The Dual-Role of Methylglyoxal in Tumor Progression - Novel Therapeutic Approaches. Front. Oncol. 2021, 11, 645686.

    Not in our library10.3389/fonc.2021.645686

  145. 145.

    Hernandez-Castillo C.; Shuck S. C. Diet and Obesity-Induced Methylglyoxal Production and Links to Metabolic Disease. Chem. Res. Toxicol. 2021, 34 (12), 2424–2440..

    Not in our library10.1021/acs.chemrestox.1c00221

  146. 146.

    Yamagishi S.; Matsui T.; Fukami K. Role of Receptor for Advanced Glycation End Products (RAGE) and Its Ligands in Cancer Risk. Rejuvenation Res. 2015, 18 (1), 48–56..

    Not in our library10.1089/rej.2014.1625

  147. 147.

    Papadaki M.; Holewinski R. J.; Previs S. B.; Martin T. G.; Stachowski M. J.; Li A.; Blair C. A.; Moravec C. S.; Van Eyk J. E.; Campbell K. S.; Warshaw D. M.; Kirk J. A. Diabetes with Heart Failure Increases Methylglyoxal Modifications in the Sarcomere, Which Inhibit Function. JCI Insight 2018, 3 (20), 121264.

    Not in our library10.1172/jci.insight.121264

  148. 148.
    A Link Between Methylglyoxal and Heart Failure During HIV-1 Infection · 2021
    Not checked
  149. 149.

    Hanssen N. M. J.; Scheijen J. L. J. M.; Jorsal A.; Parving H.-H.; Tarnow L.; Rossing P.; Stehouwer C. D. A.; Schalkwijk C. G. Higher Plasma Methylglyoxal Levels Are Associated With Incident Cardiovascular Disease in Individuals With Type 1 Diabetes: A 12-Year Follow-up Study. Diabetes 2017, 66 (8), 2278–2283..

    Not in our library10.2337/db16-1578

  150. 150.

    Ogawa S.; Nakayama K.; Nakayama M.; Mori T.; Matsushima M.; Okamura M.; Senda M.; Nako K.; Miyata T.; Ito S. Methylglyoxal Is a Predictor in Type 2 Diabetic Patients of Intima-Media Thickening and Elevation of Blood Pressure. Hypertension 2010, 56 (3), 471–476..

    Not in our library10.1161/hypertensionaha.110.156786

  151. 151.

    Blackburn N. J. R.; Vulesevic B.; McNeill B.; Cimenci C. E.; Ahmadi A.; Gonzalez-Gomez M.; Ostojic A.; Zhong Z.; Brownlee M.; Beisswenger P. J.; Milne R. W.; Suuronen E. J. Methylglyoxal-Derived Advanced Glycation End Products Contribute to Negative Cardiac Remodeling and Dysfunction Post-Myocardial Infarction. Basic Res. Cardiol. 2017, 112 (5), 57.

    Not in our library10.1007/s00395-017-0646-x

  152. 152.

    Wang X.; Desai K.; Chang T.; Wu L. Vascular Methylglyoxal Metabolism and the Development of Hypertension. J. Hypertens 2005, 23 (8), 1565–1573..

    Not in our library10.1097/01.hjh.0000173778.85233.1b

  153. 153.

    Hanssen N. M. J.; Beulens J. W. J.; van Dieren S.; Scheijen J. L. J. M.; van der A D. L.; Spijkerman A. M. W.; van der Schouw Y. T.; Stehouwer C. D. A.; Schalkwijk C. G. Plasma Advanced Glycation End Products Are Associated with Incident Cardiovascular Events in Individuals with Type 2 Diabetes: A Case-Cohort Study with a Median Follow-up of 10 Years (EPIC-NL). Diabetes 2015, 64 (1), 257–265..

    Not in our library10.2337/db13-1864

  154. 154.

    Aso Y.; Inukai T.; Tayama K.; Takemura Y. Serum Concentrations of Advanced Glycation Endproducts Are Associated with the Development of Atherosclerosis as Well as Diabetic Microangiopathy in Patients with Type 2 Diabetes. Acta Diabetol 2000, 37 (2), 87–92..

    Not in our library10.1007/s005920070025

  155. 155.

    Kilhovd B. K.; Juutilainen A.; Lehto S.; Rönnemaa T.; Torjesen P. A.; Birkeland K. I.; Berg T. J.; Hanssen K. F.; Laakso M. High Serum Levels of Advanced Glycation End Products Predict Increased Coronary Heart Disease Mortality in Nondiabetic Women but Not in Nondiabetic Men: A Population-Based 18-Year Follow-up Study. Arterioscler. Thromb. Vasc. Biol. 2005, 25 (4), 815–820..

    Not in our library10.1161/01.atv.0000158380.44231.fe

  156. 156.

    Chiarelli F.; de Martino M.; Mezzetti A.; Catino M.; Morgese G.; Cuccurullo F.; Verrotti A. Advanced Glycation End Products in Children and Adolescents with Diabetes: Relation to Glycemic Control and Early Microvascular Complications. J. Pediatr. 1999, 134 (4), 486–491..

    Not in our library10.1016/s0022-3476(99)70208-8

  157. 157.

    Miura J.; Yamagishi S.-i.; Uchigata Y.; Takeuchi M.; Yamamoto H.; Makita Z.; Iwamoto Y. Serum Levels of Non-Carboxymethyllysine Advanced Glycation Endproducts Are Correlated to Severity of Microvascular Complications in Patients with Type 1 Diabetes. J. Diabetes Its Complications 2003, 17 (1), 16–21..

    Not in our library10.1016/s1056-8727(02)00183-6

  158. 158.

    Ramasamy R.; Yan S. F.; Schmidt A. M. Receptor for AGE (RAGE): Signaling Mechanisms in the Pathogenesis of Diabetes and Its Complications. Ann. N.Y. Acad. Sci. 2011, 1243, 88–102..

    Not in our library10.1111/j.1749-6632.2011.06320.x

  159. 159.
    The role of advanced glycation end-products in the development of coronary artery disease in patients with and without diabetes mellitus: a review · 2018
    No notice
  160. 160.

    Hegab Z.; Gibbons S.; Neyses L.; Mamas M. A. Role of Advanced Glycation End Products in Cardiovascular Disease. World J. Cardiol. 2012, 4 (4), 90–102..

    Not in our library10.4330/wjc.v4.i4.90

  161. 161.

    Park L.; Raman K. G.; Lee K. J.; Lu Y.; Ferran L. J. J.; Chow W. S.; Stern D.; Schmidt A. M. Suppression of Accelerated Diabetic Atherosclerosis by the Soluble Receptor for Advanced Glycation Endproducts. Nat. Med. 1998, 4 (9), 1025–1031..

    Not in our library10.1038/2012

  162. 162.

    Srikanth V.; Westcott B.; Forbes J.; Phan T. G.; Beare R.; Venn A.; Pearson S.; Greenaway T.; Parameswaran V.; Münch G. Methylglyoxal, Cognitive Function and Cerebral Atrophy in Older People. J. Gerontol. A. Biol. Sci. Med. Sci. 2013, 68 (1), 68–73..

    Not in our library10.1093/gerona/gls100

  163. 163.

    Hipkiss A. R. On the Relationship between Energy Metabolism, Proteostasis, Aging and Parkinson’s Disease: Possible Causative Role of Methylglyoxal and Alleviative Potential of Carnosine. Aging Dis. 2017, 8 (3), 334–345..

    Not in our library10.14336/ad.2016.1030

  164. 164.

    Gomes R.; Sousa Silva M.; Quintas A.; Cordeiro C.; Freire A.; Pereira P.; Martins A.; Monteiro E.; Barroso E.; Ponces Freire A. Argpyrimidine, a Methylglyoxal-Derived Advanced Glycation End-Product in Familial Amyloidotic Polyneuropathy. Biochem. J. 2005, 385 (2), 339–345..

    Not in our library10.1042/bj20040833

  165. 165.

    Li J.; Liu D.; Sun L.; Lu Y.; Zhang Z. Advanced Glycation End Products and Neurodegenerative Diseases: Mechanisms and Perspective. J. Neurol. Sci. 2012, 317 (1–2), 1–5..

    Not in our library10.1016/j.jns.2012.02.018

  166. 166.

    Beeri M. S.; Moshier E.; Schmeidler J.; Godbold J.; Uribarri J.; Reddy S.; Sano M.; Grossman H. T.; Cai W.; Vlassara H.; Silverman J. M. Serum Concentration of an Inflammatory Glycotoxin, Methylglyoxal, Is Associated with Increased Cognitive Decline in Elderly Individuals. Mech. Ageing Dev. 2011, 132 (11–12), 583–587..

    Not in our library10.1016/j.mad.2011.10.007

  167. 167.

    Krautwald M.; Münch G. Advanced Glycation End Products as Biomarkers and Gerontotoxins - A Basis to Explore Methylglyoxal-Lowering Agents for Alzheimer’s Disease?. Exp. Gerontol. 2010, 45 (10), 744–751..

    Not in our library10.1016/j.exger.2010.03.001

  168. 168.

    Kimura T.; Takamatsu J.; Araki N.; Goto M.; Kondo A.; Miyakawa T.; Horiuchi S. Are Advanced Glycation End-Products Associated with Amyloidosis in Alzheimer’s Disease?. Neuroreport 1995, 6 (6), 866–868..

    Not in our library10.1097/00001756-199504190-00010

  169. 169.

    Xie B.; Lin F.; Peng L.; Ullah K.; Wu H.; Qing H.; Deng Y. Methylglyoxal Increases Dopamine Level and Leads to Oxidative Stress in SH-SY5Y Cells. Acta Biochim. Biophys. Sin. 2014, 46 (11), 950–956..

    Not in our library10.1093/abbs/gmu094

  170. 170.

    Haslbeck K.-M.; Bierhaus A.; Erwin S.; Kirchner A.; Nawroth P.; Schlötzer U.; Neundörfer B.; Heuss D. Receptor for Advanced Glycation Endproduct (RAGE)-Mediated Nuclear Factor-KappaB Activation in Vasculitic Neuropathy. Muscle Nerve 2004, 29 (6), 853–860..

    Not in our library10.1002/mus.20039

  171. 171.

    Haslbeck K. M.; Schleicher E. D.; Friess U.; Kirchner A.; Neundörfer B.; Heuss D. N(Epsilon)-Carboxymethyllysine in Diabetic and Non-Diabetic Polyneuropathies. Acta Neuropathol. (Berl.) 2002, 104 (1), 45–52..

    Not in our library10.1007/s00401-002-0518-8

  172. 172.

    Haslbeck K. M.; Neundörfer B.; Schlötzer-Schrehardtt U.; Bierhaus A.; Schleicher E.; Pauli E.; Haslbeck M.; Hecht M.; Nawroth P.; Heuss D. Activation of the RAGE Pathway: A General Mechanism in the Pathogenesis of Polyneuropathies?. Neurol. Res. 2007, 29 (1), 103–110..

    Not in our library10.1179/174313206x152564

  173. 173.

    Haslbeck K.-M.; Schleicher E.; Bierhaus A.; Nawroth P.; Haslbeck M.; Neundörfer B.; Heuss D. The AGE/RAGE/NF-(Kappa)B Pathway May Contribute to the Pathogenesis of Polyneuropathy in Impaired Glucose Tolerance (IGT). Exp. Clin. Endocrinol. Diabetes Off. J. Ger. Soc. Endocrinol. Ger. Diabetes Assoc. 2005, 113 (5), 288–291..

    Not in our library10.1055/s-2005-865600

  174. 174.

    Derk J.; MacLean M.; Juranek J.; Schmidt A. M. The Receptor for Advanced Glycation Endproducts (RAGE) and Mediation of Inflammatory Neurodegeneration. J. Alzheimers Dis. Parkinsonism 2018, 8 (1), 421.

    Not in our library10.4172/2161-0460.1000421

  175. 175.

    Akhter F.; Chen D.; Akhter A.; Yan S. F.; Yan S. S. Age-Dependent Accumulation of Dicarbonyls and Advanced Glycation Endproducts (AGEs) Associates with Mitochondrial Stress. Free Radic. Biol. Med. 2021, 164, 429–438..

    Not in our library10.1016/j.freeradbiomed.2020.12.021

  176. 176.

    Moreira A. P.; Vizuete A. F. K.; Zin L. E. F.; de Marques C. O.; Pacheco R. F.; Leal M. B.; Gonçalves C.-A. The Methylglyoxal/RAGE/NOX-2 Pathway Is Persistently Activated in the Hippocampus of Rats with STZ-Induced Sporadic Alzheimer’s Disease. Neurotox. Res. 2022, 40 (2), 395–409..

    Not in our library10.1007/s12640-022-00476-9

  177. 177.

    Choi B.-R.; Cho W.-H.; Kim J.; Lee H. J.; Chung C.; Jeon W. K.; Han J.-S. Increased Expression of the Receptor for Advanced Glycation End Products in Neurons and Astrocytes in a Triple Transgenic Mouse Model of Alzheimer’s Disease. Exp. Mol. Med. 2014, 46 (2), e75.

    Not in our library10.1038/emm.2013.147

  178. 178.

    Kuhla B.; Lüth H.-J.; Haferburg D.; Boeck K.; Arendt T.; Münch G. Methylglyoxal, Glyoxal, and Their Detoxification in Alzheimer’s Disease. Ann. N.Y. Acad. Sci. 2005, 1043, 211–216..

    Not in our library10.1196/annals.1333.026

  179. 179.

    Fan X.; Sell D. R.; Hao C.; Liu S.; Wang B.; Wesson D. W.; Siedlak S.; Zhu X.; Kavanagh T. J.; Harrison F. E.; Monnier V. M. Vitamin C Is a Source of Oxoaldehyde and Glycative Stress in Age-Related Cataract and Neurodegenerative Diseases. Aging Cell 2020, 19 (7), e13176.

    Not in our library10.1111/acel.13176

  180. 180.

    Jono T.; Kimura T.; Takamatsu J.; Nagai R.; Miyazaki K.; Yuzuriha T.; Kitamura T.; Horiuchi S. Accumulation of Imidazolone, Pentosidine and N(Epsilon)-(Carboxymethyl)Lysine in Hippocampal CA4 Pyramidal Neurons of Aged Human Brain. Pathol. Int. 2002, 52 (9), 563–571..

    Not in our library10.1046/j.1320-5463.2002.01390.x

  181. 181.

    Aubert C. E.; Michel P.-L.; Gillery P.; Jaisson S.; Fonfrede M.; Morel F.; Hartemann A.; Bourron O. Association of Peripheral Neuropathy with Circulating Advanced Glycation End Products, Soluble Receptor for Advanced Glycation End Products and Other Risk Factors in Patients with Type 2 Diabetes. Diabetes Metab. Res. Rev. 2014, 30 (8), 679–685..

    Not in our library10.1002/dmrr.2529

  182. 182.
    Role of Methylglyoxal in Alzheimer’s Disease · 2014
    No notice
  183. 183.

    Wetzels S.; Vanmierlo T.; Scheijen J. L. J. M.; van Horssen J.; Amor S.; Somers V.; Schalkwijk C. G.; Hendriks J. J. A.; Wouters K. Methylglyoxal-Derived Advanced Glycation Endproducts Accumulate in Multiple Sclerosis Lesions. Front. Immunol. 2019, 10, 855.

    Not in our library10.3389/fimmu.2019.00855

  184. 184.

    Shibata N.; Hirano A.; Hedley-Whyte E. T.; Dal Canto M. C.; Nagai R.; Uchida K.; Horiuchi S.; Kawaguchi M.; Yamamoto T.; Kobayashi M. Selective Formation of Certain Advanced Glycation End Products in Spinal Cord Astrocytes of Humans and Mice with Superoxide Dismutase-1 Mutation. Acta Neuropathol. (Berl.) 2002, 104 (2), 171–178..

    Not in our library10.1007/s00401-002-0537-5

  185. 185.

    Kim J.; Waldvogel H. J.; Faull R. L. M.; Curtis M. A.; Nicholson L. F. B. The RAGE Receptor and Its Ligands Are Highly Expressed in Astrocytes in a Grade-Dependant Manner in the Striatum and Subependymal Layer in Huntington’s Disease. J. Neurochem. 2015, 134 (5), 927–942..

    Not in our library10.1111/jnc.13178

  186. 186.

    Suzuki A.; Yabu A.; Nakamura H. Advanced Glycation End Products in Musculoskeletal System and Disorders. Methods 2020, 203, 179–186..

    Not in our library10.1016/j.ymeth.2020.09.012

  187. 187.

    Lee K. M.; Lee C. Y.; Zhang G.; Lyu A.; Yue K. K. M. Methylglyoxal Activates Osteoclasts through JNK Pathway Leading to Osteoporosis. Chem. Biol. Interact. 2019, 308, 147–154..

    Not in our library10.1016/j.cbi.2019.05.026

  188. 188.
    Key Triggers of Osteoclast-Related Diseases and Available Strategies for Targeted Therapies: A Review · 2017
    Not checked
  189. 189.

    Jiao H.; Xiao E.; Graves D. T. Diabetes and Its Effect on Bone and Fracture Healing. Curr. Osteoporos. Rep. 2015, 13 (5), 327–335..

    Not in our library10.1007/s11914-015-0286-8

  190. 190.

    Aikawa T.; Matsubara H.; Ugaji S.; Shirakawa J.; Nagai R.; Munesue S.; Harashima A.; Yamamoto Y.; Tsuchiya H. Contribution of Methylglyoxal to Delayed Healing of Bone Injury in Diabetes. Mol. Med. Rep. 2017, 16 (1), 403–409..

    Not in our library10.3892/mmr.2017.6589

  191. 191.

    Suh K. S.; Chon S.; Choi E. M. Limonene Attenuates Methylglyoxal-Induced Dysfunction in MC3T3-E1 Osteoblastic Cells. Food Agric. Immunol. 2017, 28 (6), 1256–1268..

    Not in our library10.1080/09540105.2017.1337082

  192. 192.

    Park S. Y.; Suh K. S.; Jung W.-W.; Chin S. O. Spironolactone Attenuates Methylglyoxal-Induced Cellular Dysfunction in MC3T3-E1 Osteoblastic Cells. J. Korean Med. Sci. 2021, 36 (38), e265.

    Not in our library10.3346/jkms.2021.36.e265

  193. 193.

    Riuzzi F.; Sorci G.; Sagheddu R.; Chiappalupi S.; Salvadori L.; Donato R. RAGE in the Pathophysiology of Skeletal Muscle. J. Cachexia Sarcopenia Muscle 2018, 9 (7), 1213–1234..

    Not in our library10.1002/jcsm.12350

  194. 194.

    Mey J. T.; Haus J. M. Dicarbonyl Stress and Glyoxalase-1 in Skeletal Muscle: Implications for Insulin Resistance and Type 2 Diabetes. Front. Cardiovasc. Med. 2018, 5, 117.

    Not in our library10.3389/fcvm.2018.00117

  195. 195.

    Svensson R. B.; Smith S. T.; Moyer P. J.; Magnusson S. P. Effects of Maturation and Advanced Glycation on Tensile Mechanics of Collagen Fibrils from Rat Tail and Achilles Tendons. Acta Biomater. 2018, 70, 270–280..

    Not in our library10.1016/j.actbio.2018.02.005

  196. 196.

    Pastino A. K.; Greco T. M.; Mathias R. A.; Cristea I. M.; Schwarzbauer J. E. Stimulatory Effects of Advanced Glycation Endproducts (AGEs) on Fibronectin Matrix Assembly. Matrix Biol. J. Int. Soc. Matrix Biol. 2017, 59, 39–53..

    Not in our library10.1016/j.matbio.2016.07.003

  197. 197.

    Olson L. C.; Redden J. T.; Schwartz Z.; Cohen D. J.; McClure M. J. Advanced Glycation End-Products in Skeletal Muscle Aging. Bioengineering (Basel) 2021, 8 (11), 168.

    Not in our library10.3390/bioengineering8110168

  198. 198.

    Baig M. H.; Jan A. T.; Rabbani G.; Ahmad K.; Ashraf J. M.; Kim T.; Min H. S.; Lee Y. H.; Cho W.-K.; Ma J. Y.; Lee E. J.; Choi I. Methylglyoxal and Advanced Glycation End Products: Insight of the Regulatory Machinery Affecting the Myogenic Program and of Its Modulation by Natural Compounds. Sci. Rep. 2017, 7 (1), 5916.

    Not in our library10.1038/s41598-017-06067-5

  199. 199.

    Chiu C.-Y.; Yang R.-S.; Sheu M.-L.; Chan D.-C.; Yang T.-H.; Tsai K.-S.; Chiang C.-K.; Liu S.-H. Advanced Glycation End-Products Induce Skeletal Muscle Atrophy and Dysfunction in Diabetic Mice via a RAGE-Mediated, AMPK-down-Regulated, Akt Pathway. J. Pathol. 2016, 238 (3), 470–482..

    Not in our library10.1002/path.4674

  200. 200.

    Tezuka Y.; Nakaya I.; Nakayama K.; Nakayama M.; Yahata M.; Soma J. Methylglyoxal as a Prognostic Factor in Patients with Chronic Kidney Disease. Nephrology (Carlton) 2019, 24 (9), 943–950..

    Not in our library10.1111/nep.13526

  201. 201.
    The effect of dicarbonyl stress on the development of kidney dysfunction in metabolic syndrome – a transcriptomic and proteomic approach · 2019
    Not checked
  202. 202.

    Chi Y.; Gupta R. K. Alterations in Heart and Kidney Membrane Phospholipids in Hypertension as Observed by 31P Nuclear Magnetic Resonance. Lipids 1998, 33 (10), 1023–1030..

    Not in our library10.1007/s11745-998-0301-z

  203. 203.

    Giacco F.; Du X.; D’Agati V. D.; Milne R.; Sui G.; Geoffrion M.; Brownlee M. Knockdown of Glyoxalase 1 Mimics Diabetic Nephropathy in Nondiabetic Mice. Diabetes 2014, 63 (1), 291–299..

    Not in our library10.2337/db13-0316

  204. 204.

    Berner A. K.; Brouwers O.; Pringle R.; Klaassen I.; Colhoun L.; McVicar C.; Brockbank S.; Curry J. W.; Miyata T.; Brownlee M.; Schlingemann R. O.; Schalkwijk C.; Stitt A. W. Protection against Methylglyoxal-Derived AGEs by Regulation of Glyoxalase 1 Prevents Retinal Neuroglial and Vasodegenerative Pathology. Diabetologia 2012, 55 (3), 845–854..

    Not in our library10.1007/s00125-011-2393-0

  205. 205.

    Goldin A.; Beckman J. A.; Schmidt A. M.; Creager M. A. Advanced Glycation End Products: Sparking the Development of Diabetic Vascular Injury. Circulation 2006, 114 (6), 597–605..

    Not in our library10.1161/circulationaha.106.621854

  206. 206.

    Beisswenger P. J.; Howell S. K.; Russell G. B.; Miller M. E.; Rich S. S.; Mauer M. Early Progression of Diabetic Nephropathy Correlates with Methylglyoxal-Derived Advanced Glycation End Products. Diabetes Care 2013, 36 (10), 3234–3239..

    Not in our library10.2337/dc12-2689

  207. 207.

    Beisswenger P. J.; Drummond K. S.; Nelson R. G.; Howell S. K.; Szwergold B. S.; Mauer M. Susceptibility to Diabetic Nephropathy Is Related to Dicarbonyl and Oxidative Stress. Diabetes 2005, 54 (11), 3274–3281..

    Not in our library10.2337/diabetes.54.11.3274

  208. 208.

    Waris S.; Winklhofer-Roob B. M.; Roob J. M.; Fuchs S.; Sourij H.; Rabbani N.; Thornalley P. J. Increased DNA Dicarbonyl Glycation and Oxidation Markers in Patients with Type 2 Diabetes and Link to Diabetic Nephropathy. J. Diabetes Res. 2015, 2015, 915486.

    Not in our library10.1155/2015/915486

  209. 209.

    Ito K.; Sakata N.; Nagai R.; Shirakawa J.-I.; Watanabe M.; Mimata A.; Abe Y.; Yasuno T.; Sasatomi Y.; Miyake K.; Ueki N.; Hamauchi A.; Nakashima H. High Serum Level of Methylglyoxal-Derived AGE, Nδ-(5-Hydro-5-Methyl-4-Imidazolone-2-Yl)-Ornithine, Independently Relates to Renal Dysfunction. Clin. Exp. Nephrol. 2017, 21 (3), 398–406..

    Not in our library10.1007/s10157-016-1301-9

  210. 210.

    Forbes J. M.; Le Bagge S.; Righi S.; Fotheringham A. K.; Gallo L. A.; McCarthy D. A.; Leung S.; Baskerville T.; Nisbett J.; Morton A.; Teasdale S.; D’Silva N.; Barrett H.; Jones T.; Couper J.; Donaghue K.; Isbel N.; Johnson D. W.; Donnellan L.; Deo P.; Akison L. K.; Moritz K. M.; O’Moore-Sullivan T. Advanced Glycation End Products as Predictors of Renal Function in Youth with Type 1 Diabetes. Sci. Rep. 2021, 11 (1), 9422.

    Not in our library10.1038/s41598-021-88786-4

  211. 211.

    Perkins B. A.; Rabbani N.; Weston A.; Adaikalakoteswari A.; Lee J. A.; Lovblom L. E.; Cardinez N.; Thornalley P. J. High Fractional Excretion of Glycation Adducts Is Associated with Subsequent Early Decline in Renal Function in Type 1 Diabetes. Sci. Rep. 2020, 10 (1), 12709.

    Not in our library10.1038/s41598-020-69350-y

  212. 212.

    Martens R. J. H.; Broers N. J. H.; Canaud B.; Christiaans M. H. L.; Cornelis T.; Gauly A.; Hermans M. M. H.; Konings C. J. A. M.; van der Sande F. M.; Scheijen J. L. J. M.; Stifft F.; Wirtz J. J. J. M.; Kooman J. P.; Schalkwijk C. G. Relations of Advanced Glycation Endproducts and Dicarbonyls with Endothelial Dysfunction and Low-Grade Inflammation in Individuals with End-Stage Renal Disease in the Transition to Renal Replacement Therapy: A Cross-Sectional Observational Study. PloS One 2019, 14 (8), e0221058.

    Not in our library10.1371/journal.pone.0221058

  213. 213.

    Martens R. J. H.; Broers N. J. H.; Canaud B.; Christiaans M. H. L.; Cornelis T.; Gauly A.; Hermans M. M. H.; Konings C. J. A. M.; van der Sande F. M.; Scheijen J. L. J. M.; Stifft F.; Kooman J. P.; Schalkwijk C. G. Advanced Glycation Endproducts and Dicarbonyls in End-Stage Renal Disease: Associations with Uraemia and Courses Following Renal Replacement Therapy. Clin. Kidney J. 2020, 13 (5), 855–866..

    Not in our library10.1093/ckj/sfz099

  214. 214.

    Lee H.-W.; Gu M. J.; Lee J.-Y.; Lee S.; Kim Y.; Ha S. K. Methylglyoxal-Lysine Dimer, an Advanced Glycation End Product, Induces Inflammation via Interaction with RAGE in Mesangial Cells. Mol. Nutr. Food Res. 2021, 65 (13), 2000799.

    Not in our library10.1002/mnfr.202000799

  215. 215.

    Lee H.-W.; Gu M. J.; Kim Y.; Lee J.-Y.; Lee S.; Choi I.-W.; Ha S. K. Glyoxal-Lysine Dimer, an Advanced Glycation End Product, Induces Oxidative Damage and Inflammatory Response by Interacting with RAGE. Antioxidants (Basel) 2021, 10 (9), 1486.

    Not in our library10.3390/antiox10091486

  216. 216.

    Zhang M.; Feng L.; Zhu M.; Gu J.; Jiang J.; Cheng X.; Ding S.; Wu C.; Jia X. The Anti-Inflammation Effect of Moutan Cortex on Advanced Glycation End Products-Induced Rat Mesangial Cells Dysfunction and High-Glucose-Fat Diet and Streptozotocin-Induced Diabetic Nephropathy Rats. J. Ethnopharmacol. 2014, 151 (1), 591–600..

    Not in our library10.1016/j.jep.2013.11.015

  217. 217.

    Jeong S.-R.; Lee K.-W. Methylglyoxal-Derived Advanced Glycation End Product (AGE4)-Induced Apoptosis Leads to Mitochondrial Dysfunction and Endoplasmic Reticulum Stress through the RAGE/JNK Pathway in Kidney Cells. Int. J. Mol. Sci. 2021, 22 (12), 6530.

    Not in our library10.3390/ijms22126530

  218. 218.

    Yang P.-Y.; Li P.-C.; Feng B. Protective Effects of Gliclazide on High Glucose and AGEs-Induced Damage of Glomerular Mesangial Cells and Renal Tubular Epithelial Cells via Inhibiting RAGE-P22phox-NF-KB Pathway. Eur. Rev. Med. Pharmacol. Sci. 2019, 23 (20), 9099–9107..

    Not in our library10.26355/eurrev_201910_19313

  219. 219.

    Baragetti I.; Norata G. D.; Sarcina C.; Baragetti A.; Rastelli F.; Buzzi L.; Grigore L.; Garlaschelli K.; Pozzi C.; Catapano A. L. 374 T/A RAGE Polymorphism Is Associated with Chronic Kidney Disease Progression in Subjects Affected by Nephrocardiovascular Disease. PloS One 2013, 8 (4), e60089.

    Not in our library10.1371/journal.pone.0060089

  220. 220.

    Wang W.-C.; Chou C.-K.; Chuang M.-C.; Li Y.-C.; Lee J.-A. Elevated Levels of Liver Methylglyoxal and D-Lactate in Early-Stage Hepatitis in Rats. Biomed. Chromatogr. 2018, 32 (2), 4039.

    Not in our library10.1002/bmc.4039

  221. 221.

    Michel M.; Hess C.; Kaps L.; Kremer W. M.; Hilscher M.; Galle P. R.; Moehler M.; Schattenberg J. M.; Wörns M.-A.; Labenz C.; Nagel M. Elevated Serum Levels of Methylglyoxal Are Associated with Impaired Liver Function in Patients with Liver Cirrhosis. Sci. Rep. 2021, 11 (1), 20506.

    Not in our library10.1038/s41598-021-00119-7

  222. 222.

    Seo K.; Ki S. H.; Shin S. M. Methylglyoxal Induces Mitochondrial Dysfunction and Cell Death in Liver. Toxicol. Res. 2014, 30 (3), 193–198..

    Not in our library10.5487/tr.2014.30.3.193

  223. 223.

    Hollenbach M.; Thonig A.; Pohl S.; Ripoll C.; Michel M.; Zipprich A. Expression of Glyoxalase-I Is Reduced in Cirrhotic Livers: A Possible Mechanism in the Development of Cirrhosis. PloS One 2017, 12 (2), e0171260.

    Not in our library10.1371/journal.pone.0171260

  224. 224.

    Ahmed N.; Thornalley P. J.; Lüthen R.; Häussinger D.; Sebekova K.; Schinzel R.; Voelker W.; Heidland A. Processing of Protein Glycation, Oxidation and Nitrosation Adducts in the Liver and the Effect of Cirrhosis. J. Hepatol. 2004, 41 (6), 913–919..

    Not in our library10.1016/j.jhep.2004.08.007

  225. 225.

    Spanos C.; Maldonado E. M.; Fisher C. P.; Leenutaphong P.; Oviedo-Orta E.; Windridge D.; Salguero F. J.; Bermudez-Fajardo A.; Weeks M. E.; Evans C.; Corfe B. M.; Rabbani N.; Thornalley P. J.; Miller M. H.; Wang H.; Dillon J. F.; Quaglia A.; Dhawan A.; Fitzpatrick E.; Bernadette Moore J. Proteomic Identification and Characterization of Hepatic Glyoxalase 1 Dysregulation in Non-Alcoholic Fatty Liver Disease. Proteome Sci. 2018, 16, 4.

    Not in our library10.1186/s12953-018-0131-y

  226. 226.

    Wouters K.; Cento A. S.; Gaens K. H.; Teunissen M.; Scheijen J. L. J. M.; Barutta F.; Chiazza F.; Collotta D.; Aragno M.; Gruden G.; Collino M.; Schalkwijk C. G.; Mastrocola R. Deletion of RAGE Fails to Prevent Hepatosteatosis in Obese Mice Due to Impairment of Other AGEs Receptors and Detoxifying Systems. Sci. Rep. 2021, 11 (1), 17373.

    Not in our library10.1038/s41598-021-96859-7

  227. 227.

    Palma-Duran S. A.; Kontogianni M. D.; Vlassopoulos A.; Zhao S.; Margariti A.; Georgoulis M.; Papatheodoridis G.; Combet E. Serum Levels of Advanced Glycation End-Products (AGEs) and the Decoy Soluble Receptor for AGEs (SRAGE) Can Identify Non-Alcoholic Fatty Liver Disease in Age-, Sex- and BMI-Matched Normo-Glycemic Adults. Metabolism. 2018, 83, 120–127..

    Not in our library10.1016/j.metabol.2018.01.023

  228. 228.

    Bijnen M.; van Greevenbroek M. M. J.; van der Kallen C. J. H.; Scheijen J. L.; van de Waarenburg M. P. H.; Stehouwer C. D. A.; Wouters K.; Schalkwijk C. G. Hepatic Fat Content and Liver Enzymes Are Associated with Circulating Free and Protein-Bound Advanced Glycation End Products, Which Are Associated with Low-Grade Inflammation: The CODAM Study. J. Diabetes Res. 2019, 2019, 6289831.

    Not in our library10.1155/2019/6289831

  229. 229.

    Serban A. I.; Stanca L.; Geicu O. I.; Munteanu M. C.; Dinischiotu A. RAGE and TGF-B1 Cross-Talk Regulate Extracellular Matrix Turnover and Cytokine Synthesis in AGEs Exposed Fibroblast Cells. PloS One 2016, 11 (3), e0152376.

    Not in our library10.1371/journal.pone.0152376

  230. 230.

    Kim J.; Kim O. S.; Kim C.-S.; Sohn E.; Jo K.; Kim J. S. Accumulation of Argpyrimidine, a Methylglyoxal-Derived Advanced Glycation End Product, Increases Apoptosis of Lens Epithelial Cells Both in Vitro and in Vivo. Exp. Mol. Med. 2012, 44 (2), 167–175..

    Not in our library10.3858/emm.2012.44.2.012

  231. 231.

    Xia J.-R.; Chen T.-T.; Li W.-D.; Lu F.-L.; Liu J.; Cai X.-G.; Lu Q.; Yang C.-P. Inhibitory Effect of Receptor for Advanced Glycation End Product-specific Small Interfering RNAs on the Development of Hepatic Fibrosis in Primary Rat Hepatic Stellate Cells. Mol. Med. Rep. 2015, 12 (1), 569–574..

    Not in our library10.3892/mmr.2015.3342

  232. 232.

    Cai X.-G.; Xia J.-R.; Li W.-D.; Lu F.-L.; Liu J.; Lu Q.; Zhi H. Anti-Fibrotic Effects of Specific-SiRNA Targeting of the Receptor for Advanced Glycation End Products in a Rat Model of Experimental Hepatic Fibrosis. Mol. Med. Rep. 2014, 10 (1), 306–314..

    Not in our library10.3892/mmr.2014.2207

  233. 233.

    Bijnen M.; Beelen N.; Wetzels S.; Gaar J. v. d.; Vroomen M.; Wijnands E.; Scheijen J. L.; van de Waarenburg M. P. H; Gijbels M. J.; Cleutjens J. P.; Biessen E. A. L.; Stehouwer C. D. A.; Schalkwijk C. G.; Wouters K. RAGE Deficiency Does Not Affect Non-Alcoholic Steatohepatitis and Atherosclerosis in Western Type Diet-Fed Ldlr(−/−) Mice. Sci. Rep. 2018, 8 (1), 15256.

    Not in our library10.1038/s41598-018-33661-y

  234. 234.

    Price C. L.; Hassi H. O. S. A.; English N. R.; Blakemore A. I. F.; Stagg A. J.; Knight S. C. Methylglyoxal Modulates Immune Responses: Relevance to Diabetes. J. Cell. Mol. Med. 2010, 14 (6B), 1806–1815..

    Not in our library10.1111/j.1582-4934.2009.00803.x

  235. 235.

    Baumann T.; Dunkel A.; Schmid C.; Schmitt S.; Hiltensperger M.; Lohr K.; Laketa V.; Donakonda S.; Ahting U.; Lorenz-Depiereux B.; Heil J. E.; Schredelseker J.; Simeoni L.; Fecher C.; Körber N.; Bauer T.; Hüser N.; Hartmann D.; Laschinger M.; Eyerich K.; Eyerich S.; Anton M.; Streeter M.; Wang T.; Schraven B.; Spiegel D.; Assaad F.; Misgeld T.; Zischka H.; Murray P. J.; Heine A.; Heikenwälder M.; Korn T.; Dawid C.; Hofmann T.; Knolle P. A.; Höchst B. Regulatory Myeloid Cells Paralyze T Cells through Cell-Cell Transfer of the Metabolite Methylglyoxal. Nat. Immunol. 2020, 21 (5), 555–566..

    Not in our library10.1038/s41590-020-0666-9

  236. 236.

    Mir A. R.; Moinuddin; Habib S.; Khan F.; Alam K.; Ali A. Structural Changes in Histone H2A by Methylglyoxal Generate Highly Immunogenic Amorphous Aggregates with Implications in Auto-Immune Response in Cancer. Glycobiology 2016, 26 (2), 129–141..

    Not in our library10.1093/glycob/cwv082

  237. 237.

    Son S.; Hwang I.; Han S. H.; Shin J.-S.; Shin O. S.; Yu J.-W. Advanced Glycation End Products Impair NLRP3 Inflammasome-Mediated Innate Immune Responses in Macrophages. J. Biol. Chem. 2017, 292 (50), 20437–20448..

    Not in our library10.1074/jbc.m117.806307

  238. 238.
    Advanced Glycation End Products Enhance Macrophages Polarization into M1 Phenotype through Activating RAGE/NF- κ B Pathway · 2015
    No notice
  239. 239.

    Yan S. F.; Ramasamy R.; Schmidt A. M. The RAGE Axis: A Fundamental Mechanism Signaling Danger to the Vulnerable Vasculature. Circ. Res. 2010, 106 (5), 842–853..

    Not in our library10.1161/circresaha.109.212217

  240. 240.

    Moser B.; Desai D. D.; Downie M. P.; Chen Y.; Yan S. F.; Herold K.; Schmidt A. M.; Clynes R. Receptor for Advanced Glycation End Products Expression on T Cells Contributes to Antigen-Specific Cellular Expansion in Vivo. J. Immunol. 2007, 179 (12), 8051–8058..

    Not in our library10.4049/jimmunol.179.12.8051

  241. 241.

    Akirav E. M.; Preston-Hurlburt P.; Garyu J.; Henegariu O.; Clynes R.; Schmidt A. M.; Herold K. C. RAGE Expression in Human T Cells: A Link between Environmental Factors and Adaptive Immune Responses. PloS One 2012, 7 (4), e34698.

    Not in our library10.1371/journal.pone.0034698

  242. 242.

    Wetzels S.; Wouters K.; Schalkwijk C. G.; Vanmierlo T.; Hendriks J. J. A. Methylglyoxal-Derived Advanced Glycation Endproducts in Multiple Sclerosis. Int. J. Mol. Sci. 2017, 18 (2), 421.

    Not in our library10.3390/ijms18020421

  243. 243.

    Sternberg Z.; Hennies C.; Sternberg D.; Wang P.; Kinkel P.; Hojnacki D.; Weinstock-Guttman B.; Munschauer F. Diagnostic Potential of Plasma Carboxymethyllysine and Carboxyethyllysine in Multiple Sclerosis. J. Neuroinflammation 2010, 7, 72.

    Not in our library10.1186/1742-2094-7-72

  244. 244.

    Yu L.; Chen X.; Sun X.; Wang L.; Chen S. The Glycolytic Switch in Tumors: How Many Players Are Involved?. J. Cancer 2017, 8 (17), 3430–3440..

    Not in our library10.7150/jca.21125

  245. 245.

    Hosoda F.; Arai Y.; Okada N.; Shimizu H.; Miyamoto M.; Kitagawa N.; Katai H.; Taniguchi H.; Yanagihara K.; Imoto I.; Inazawa J.; Ohki M.; Shibata T. Integrated Genomic and Functional Analyses Reveal Glyoxalase I as a Novel Metabolic Oncogene in Human Gastric Cancer. Oncogene 2015, 34 (9), 1196–1206..

    Not in our library10.1038/onc.2014.57

  246. 246.

    Wang Y.; Kuramitsu Y.; Ueno T.; Suzuki N.; Yoshino S.; Iizuka N.; Akada J.; Kitagawa T.; Oka M.; Nakamura K. Glyoxalase I (GLO1) Is up-Regulated in Pancreatic Cancerous Tissues Compared with Related Non-Cancerous Tissues. Anticancer Res. 2012, 32 (8), 3219–3222.

    Not in our library

  247. 247.

    Bair W. B. 3rd; Cabello C. M.; Uchida K.; Bause A. S.; Wondrak G. T. GLO1 Overexpression in Human Malignant Melanoma. Melanoma Res. 2010, 20 (2), 85–96..

    Not in our library10.1097/cmr.0b013e3283364903

  248. 248.

    Tamori S.; Nozaki Y.; Motomura H.; Nakane H.; Katayama R.; Onaga C.; Kikuchi E.; Shimada N.; Suzuki Y.; Noike M.; Hara Y.; Sato K.; Sato T.; Yamamoto K.; Hanawa T.; Imai M.; Abe R.; Yoshimori A.; Takasawa R.; Tanuma S.-I.; Akimoto K. Glyoxalase 1 Gene Is Highly Expressed in Basal-like Human Breast Cancers and Contributes to Survival of ALDH1-Positive Breast Cancer Stem Cells. Oncotarget 2018, 9 (92), 36515–36529..

    Not in our library10.18632/oncotarget.26369

  249. 249.

    Abordo E. A.; Minhas H. S.; Thornalley P. J. Accumulation of Alpha-Oxoaldehydes during Oxidative Stress: A Role in Cytotoxicity. Biochem. Pharmacol. 1999, 58 (4), 641–648..

    Not in our library10.1016/s0006-2952(99)00132-x

  250. 250.

    Nokin M.-J.; Durieux F.; Bellier J.; Peulen O.; Uchida K.; Spiegel D. A.; Cochrane J. R.; Hutton C. A.; Castronovo V.; Bellahcène A. Hormetic Potential of Methylglyoxal, a Side-Product of Glycolysis, in Switching Tumours from Growth to Death. Sci. Rep. 2017, 7 (1), 11722.

    Not in our library10.1038/s41598-017-12119-7

  251. 251.

    Coluccio M. L.; Gentile F.; Presta I.; Donato G.; Coppedè N.; Valprapuram I.; Mignogna C.; Lavecchia A.; Figuccia F.; Garo V. M.; Fabrizio E. D.; Candeloro P.; Viglietto G.; Malara N. Tailoring Chemometric Models on Blood-Derived Cultures Secretome to Assess Personalized Cancer Risk Score. Cancers 2020, 12 (6), 1362.

    Not in our library10.3390/cancers12061362

  252. 252.

    Kang R.; Tang D.; Schapiro N. E.; Livesey K. M.; Farkas A.; Loughran P.; Bierhaus A.; Lotze M. T.; Zeh H. J. The Receptor for Advanced Glycation End Products (RAGE) Sustains Autophagy and Limits Apoptosis, Promoting Pancreatic Tumor Cell Survival. Cell Death Differ. 2010, 17 (4), 666–676..

    Not in our library10.1038/cdd.2009.149

  253. 253.

    Miki S.; Kasayama S.; Miki Y.; Nakamura Y.; Yamamoto M.; Sato B.; Kishimoto T. Expression of Receptors for Advanced Glycosylation End Products on Renal Cell Carcinoma Cells in Vitro. Biochem. Biophys. Res. Commun. 1993, 196 (2), 984–989..

    Not in our library10.1006/bbrc.1993.2346

  254. 254.

    Sakellariou S.; Fragkou P.; Levidou G.; Gargalionis A. N.; Piperi C.; Dalagiorgou G.; Adamopoulos C.; Saetta A.; Agrogiannis G.; Theohari I.; Sougioultzis S.; Tsioli P.; Karavokyros I.; Tsavaris N.; Kostakis I. D.; Zizi-Serbetzoglou A.; Vandoros G. P.; Patsouris E.; Korkolopoulou P. Clinical Significance of AGE-RAGE Axis in Colorectal Cancer: Associations with Glyoxalase-I, Adiponectin Receptor Expression and Prognosis. BMC Cancer 2016, 16, 174.

    Not in our library10.1186/s12885-016-2213-5

  255. 255.

    Waghela B. N.; Vaidya F. U.; Ranjan K.; Chhipa A. S.; Tiwari B. S.; Pathak C. AGE-RAGE Synergy Influences Programmed Cell Death Signaling to Promote Cancer. Mol. Cell. Biochem. 2021, 476 (2), 585–598..

    Not in our library10.1007/s11010-020-03928-y

  256. 256.

    Logsdon C. D.; Fuentes M. K.; Huang E. H.; Arumugam T. RAGE and RAGE Ligands in Cancer. Curr. Mol. Med. 2007, 7 (8), 777–789..

    Not in our library10.2174/156652407783220697

  257. 257.
    Receptor for Advanced Glycation End Products Acts as a Fuel to Colorectal Cancer Development · 2020
    Not checked
  258. 258.

    Riboulet-Chavey A.; Pierron A.; Durand I.; Murdaca J.; Giudicelli J.; Van Obberghen E. Methylglyoxal Impairs the Insulin Signaling Pathways Independently of the Formation of Intracellular Reactive Oxygen Species. Diabetes 2006, 55 (5), 1289–1299..

    Not in our library10.2337/db05-0857

  259. 259.

    Ng Y.; Ramm G.; Lopez J. A.; James D. E. Rapid Activation of Akt2 Is Sufficient to Stimulate GLUT4 Translocation in 3T3-L1 Adipocytes. Cell Metab. 2008, 7 (4), 348–356..

    Not in our library10.1016/j.cmet.2008.02.008

  260. 260.
    MAPK/ERK Signaling Regulates Insulin Sensitivity to Control Glucose Metabolism in Drosophila · 2011
    No notice
  261. 261.

    Marko A. J.; Miller R. A.; Kelman A.; Frauwirth K. A. Induction of Glucose Metabolism in Stimulated T Lymphocytes Is Regulated by Mitogen-Activated Protein Kinase Signaling. PloS One 2010, 5 (11), e15425.

    Not in our library10.1371/journal.pone.0015425

  262. 262.

    Ahmed N.; Babaei-Jadidi R.; Howell S. K.; Beisswenger P. J.; Thornalley P. J. Degradation Products of Proteins Damaged by Glycation, Oxidation and Nitration in Clinical Type 1 Diabetes. Diabetologia 2005, 48 (8), 1590–1603..

    Not in our library10.1007/s00125-005-1810-7

  263. 263.

    Duran-Jimenez B.; Dobler D.; Moffatt S.; Rabbani N.; Streuli C. H.; Thornalley P. J.; Tomlinson D. R.; Gardiner N. J. Advanced Glycation End Products in Extracellular Matrix Proteins Contribute to the Failure of Sensory Nerve Regeneration in Diabetes. Diabetes 2009, 58 (12), 2893–2903..

    Not in our library10.2337/db09-0320

  264. 264.

    Wilker S. C.; Chellan P.; Arnold B. M.; Nagaraj R. H. Chromatographic Quantification of Argpyrimidine, a Methylglyoxal-Derived Product in Tissue Proteins: Comparison with Pentosidine. Anal. Biochem. 2001, 290 (2), 353–358..

    Not in our library10.1006/abio.2001.4992

  265. 265.

    Han Y.; Randell E.; Vasdev S.; Gill V.; Gadag V.; Newhook L. A.; Grant M.; Hagerty D. Plasma Methylglyoxal and Glyoxal Are Elevated and Related to Early Membrane Alteration in Young, Complication-Free Patients with Type 1 Diabetes. Mol. Cell. Biochem. 2007, 305 (1–2), 123–131..

    Not in our library10.1007/s11010-007-9535-1

  266. 266.

    Kong X.; Ma M.; Huang K.; Qin L.; Zhang H.; Yang Z.; Li X.; Su Q. Increased Plasma Levels of the Methylglyoxal in Patients with Newly Diagnosed Type 2 Diabetes 2. J. Diabetes 2014, 6 (6), 535–540..

    Not in our library10.1111/1753-0407.12160

  267. 267.

    Bellier J.; Nokin M.-J.; Lardé E.; Karoyan P.; Peulen O.; Castronovo V.; Bellahcène A. Methylglyoxal, a Potent Inducer of AGEs, Connects between Diabetes and Cancer. Diabetes Res. Clin. Pract. 2019, 148, 200–211..

    Not in our library10.1016/j.diabres.2019.01.002

  268. 268.

    Stitt A. W.; Bhaduri T.; McMullen C. B.; Gardiner T. A.; Archer D. B. Advanced Glycation End Products Induce Blood-Retinal Barrier Dysfunction in Normoglycemic Rats. Mol. Cell Biol. Res. Commun. MCBRC 2000, 3 (6), 380–388..

    Not in our library10.1006/mcbr.2000.0243

  269. 269.

    Griggs R. B.; Laird D. E.; Donahue R. R.; Fu W.; Taylor B. K. Methylglyoxal Requires AC1 and TRPA1 to Produce Pain and Spinal Neuron Activation. Front. Neurosci. 2017, 11, 679.

    Not in our library10.3389/fnins.2017.00679

  270. 270.

    Dobler D.; Ahmed N.; Song L.; Eboigbodin K. E.; Thornalley P. J. Increased Dicarbonyl Metabolism in Endothelial Cells in Hyperglycemia Induces Anoikis and Impairs Angiogenesis by RGD and GFOGER Motif Modification. Diabetes 2006, 55 (7), 1961–1969..

    Not in our library10.2337/db05-1634

  271. 271.

    Xu J.; Chen L.-J.; Yu J.; Wang H.-J.; Zhang F.; Liu Q.; Wu J. Involvement of Advanced Glycation End Products in the Pathogenesis of Diabetic Retinopathy. Cell. Physiol. Biochem. Int. J. Exp. Cell. Physiol. Biochem. Pharmacol 2018, 48 (2), 705–717..

    Not in our library10.1159/000491897

  272. 272.

    Sugimoto K.; Yasujima M.; Yagihashi S. Role of Advanced Glycation End Products in Diabetic Neuropathy. Curr. Pharm. Des. 2008, 14 (10), 953–961..

    Not in our library10.2174/138161208784139774

  273. 273.

    Bierhaus A.; Hofmann M. A.; Ziegler R.; Nawroth P. P. AGEs and Their Interaction with AGE-Receptors in Vascular Disease and Diabetes Mellitus. I. The AGE Concept. Cardiovasc. Res. 1998, 37 (3), 586–600..

    Not in our library10.1016/s0008-6363(97)00233-2

  274. 274.

    Haddad M.; Perrotte M.; Khedher M. R. B.; Demongin C.; Lepage A.; Fülöp T.; Ramassamy C. Methylglyoxal and Glyoxal as Potential Peripheral Markers for MCI Diagnosis and Their Effects on the Expression of Neurotrophic, Inflammatory and Neurodegenerative Factors in Neurons and in Neuronal Derived-Extracellular Vesicles. Int. J. Mol. Sci. 2019, 20 (19), 4906.

    Not in our library10.3390/ijms20194906

  275. 275.

    Knani I.; Bouzidi H.; Zrour S.; Bergaoui N.; Hammami M.; Kerkeni M. Methylglyoxal: A Relevant Marker of Disease Activity in Patients with Rheumatoid Arthritis. Dis. Markers 2018, 2018, 8735926.

    Not in our library10.1155/2018/8735926

  276. 276.

    Thornalley P. J.; Rabbani N. Detection of Oxidized and Glycated Proteins in Clinical Samples Using Mass Spectrometry--a User’s Perspective. Biochim. Biophys. Acta 2014, 1840 (2), 818–829..

    Not in our library10.1016/j.bbagen.2013.03.025

  277. 277.

    Conway B.; Edmundowicz D.; Matter N.; Maynard J.; Orchard T. Skin Fluorescence Correlates Strongly with Coronary Artery Calcification Severity in Type 1 Diabetes. Diabetes Technol. Ther. 2010, 12 (5), 339–345..

    Not in our library10.1089/dia.2009.0152

  278. 278.

    Gerrits E. G.; Lutgers H. L.; Kleefstra N.; Graaff R.; Groenier K. H.; Smit A. J.; Gans R. O.; Bilo H. J. Skin Autofluorescence: A Tool to Identify Type 2 Diabetic Patients at Risk for Developing Microvascular Complications. Diabetes Care 2008, 31 (3), 517–521..

    Not in our library10.2337/dc07-1755

  279. 279.

    Hartog J. W. L.; Gross S.; Oterdoom L. H.; van Ree R. M.; de Vries A. P. J.; Smit A. J.; Schouten J. P.; Nawroth P. P.; Gans R. O. B.; van Son W. J.; Bierhaus A.; Bakker S. J. L. Skin-Autofluorescence Is an Independent Predictor of Graft Loss in Renal Transplant Recipients. Transplantation 2009, 87 (7), 1069–1077..

    Not in our library10.1097/tp.0b013e31819d3173

  280. 280.

    Ammanath G.; Delachi C. G.; Karabacak S.; Ali Y.; Boehm B. O.; Yildiz U. H.; Alagappan P.; Liedberg B. Colorimetric and Fluorometric Profiling of Advanced Glycation End Products. ACS Appl. Mater. Interfaces 2022, 14 (1), 94–103..

    Not in our library10.1021/acsami.1c16261

  281. 281.

    Münch G.; Keis R.; Wessels A.; Riederer P.; Bahner U.; Heidland A.; Niwa T.; Lemke H. D.; Schinzel R. Determination of Advanced Glycation End Products in Serum by Fluorescence Spectroscopy and Competitive ELISA. Eur. J. Clin. Chem. Clin. Biochem. 1997, 35 (9), 669–677..

    Not in our library10.1515/cclm.1997.35.9.669

  282. 282.

    de Vos L. C.; Lefrandt J. D.; Dullaart R. P. F.; Zeebregts C. J.; Smit A. J. Advanced Glycation End Products: An Emerging Biomarker for Adverse Outcome in Patients with Peripheral Artery Disease. Atherosclerosis 2016, 254, 291–299..

    Not in our library10.1016/j.atherosclerosis.2016.10.012

  283. 283.

    Ahmed N.; Argirov O. K.; Minhas H. S.; Cordeiro C. A. A.; Thornalley P. J. Assay of Advanced Glycation Endproducts (AGEs): Surveying AGEs by Chromatographic Assay with Derivatization by 6-Aminoquinolyl-N-Hydroxysuccinimidyl-Carbamate and Application to Nepsilon-Carboxymethyl-Lysine- and Nepsilon-(1-Carboxyethyl)Lysine-Modified Albumin. Biochem. J. 2002, 364 (1), 1–14..

    Not in our library10.1042/bj3640001

  284. 284.

    Uchida K.; Khor O. T.; Oya T.; Osawa T.; Yasuda Y.; Miyata T. Protein Modification by a Maillard Reaction Intermediate Methylglyoxal. Immunochemical Detection of Fluorescent 5-Methylimidazolone Derivatives in Vivo. FEBS Lett. 1997, 410 (2–3), 313–318..

    Not in our library10.1016/s0014-5793(97)00610-8

  285. 285.

    Yan S. D.; Schmidt A. M.; Anderson G. M.; Zhang J.; Brett J.; Zou Y. S.; Pinsky D.; Stern D. Enhanced Cellular Oxidant Stress by the Interaction of Advanced Glycation End Products with Their Receptors/Binding Proteins. J. Biol. Chem. 1994, 269 (13), 9889–9897..

    Not in our library10.1016/s0021-9258(17)36966-1

  286. 286.

    Li J.; Wang K.; Huang B.; Li R.; Wang X.; Zhang H.; Tang H.; Chen X. The Receptor for Advanced Glycation End Products Mediates Dysfunction of Airway Epithelial Barrier in a Lipopolysaccharides-Induced Murine Acute Lung Injury Model. Int. Immunopharmacol. 2021, 93, 107419.

    Not in our library10.1016/j.intimp.2021.107419

  287. 287.

    Yang L.; Liu Y.; Wang Y.; Li J.; Liu N. Azeliragon Ameliorates Alzheimer’s Disease via the Janus Tyrosine Kinase and Signal Transducer and Activator of Transcription Signaling Pathway. Clin. Sao Paulo Braz. 2021, 76, e2348.

    Not in our library10.6061/clinics/2021/e2348

  288. 288.

    Galasko D.; Bell J.; Mancuso J. Y.; Kupiec J. W.; Sabbagh M. N.; van Dyck C.; Thomas R. G.; Aisen P. S. Clinical Trial of an Inhibitor of RAGE-Aβ Interactions in Alzheimer Disease. Neurology 2014, 82 (17), 1536–1542..

    Not in our library10.1212/wnl.0000000000000364

  289. 289.

    Sabbagh M. N.; Agro A.; Bell J.; Aisen P. S.; Schweizer E.; Galasko D. PF-04494700, an Oral Inhibitor of Receptor for Advanced Glycation End Products (RAGE), in Alzheimer Disease. Alzheimer Dis. Assoc. Disord. 2011, 25 (3), 206–212..

    Not in our library10.1097/wad.0b013e318204b550

  290. 290.

    Zhang J.; Xu X.; Rao N. V.; Argyle B.; McCoard L.; Rusho W. J.; Kennedy T. P.; Prestwich G. D.; Krueger G. Novel Sulfated Polysaccharides Disrupt Cathelicidins, Inhibit RAGE and Reduce Cutaneous Inflammation in a Mouse Model of Rosacea. PloS One 2011, 6 (2), e16658.

    Not in our library10.1371/journal.pone.0016658

  291. 291.
    Methylglyoxal, a glycolysis side-product, induces Hsp90 glycation and YAP-mediated tumor growth and metastasis · 2016
    Corrected
  292. 292.

    Nokin M.-J.; Bellier J.; Durieux F.; Peulen O.; Rademaker G.; Gabriel M.; Monseur C.; Charloteaux B.; Verbeke L.; van Laere S.; Roncarati P.; Herfs M.; Lambert C.; Scheijen J.; Schalkwijk C.; Colige A.; Caers J.; Delvenne P.; Turtoi A.; Castronovo V.; Bellahcène A. Methylglyoxal, a Glycolysis Metabolite, Triggers Metastasis through MEK/ERK/SMAD1 Pathway Activation in Breast Cancer. Breast Cancer Res. BCR 2019, 21 (1), 11.

    Not in our library10.1186/s13058-018-1095-7

  293. 293.

    Guo Y.; Zhang Y.; Yang X.; Lu P.; Yan X.; Xiao F.; Zhou H.; Wen C.; Shi M.; Lu J.; Meng Q. H. Effects of Methylglyoxal and Glyoxalase I Inhibition on Breast Cancer Cells Proliferation, Invasion, and Apoptosis through Modulation of MAPKs, MMP9, and Bcl-2. Cancer Biol. Ther. 2016, 17 (2), 169–180..

    Not in our library10.1080/15384047.2015.1121346

  294. 294.

    Sharaf H.; Matou-Nasri S.; Wang Q.; Rabhan Z.; Al-Eidi H.; Al Abdulrahman A.; Ahmed N. Advanced Glycation Endproducts Increase Proliferation, Migration and Invasion of the Breast Cancer Cell Line MDA-MB-231. Biochim. Biophys. Acta 2015, 1852 (3), 429–441..

    Not in our library10.1016/j.bbadis.2014.12.009

  295. 295.

    Lee K. J.; Yoo J. W.; Kim Y. K.; Choi J. H.; Ha T.-Y.; Gil M. Advanced Glycation End Products Promote Triple Negative Breast Cancer Cells via ERK and NF-KB Pathway. Biochem. Biophys. Res. Commun. 2018, 495 (3), 2195–2201..

    Not in our library10.1016/j.bbrc.2017.11.182

  296. 296.

    Khan M. S.; Tabrez S.; Al-Okail M. S.; Shaik G. M.; Bhat S. A.; Rehman T. M.; Husain F. M.; AlAjmi M. F. Non-Enzymatic Glycation of Protein Induces Cancer Cell Proliferation and Its Inhibition by Quercetin: Spectroscopic, Cytotoxicity and Molecular Docking Studies. J. Biomol. Struct. Dyn. 2021, 39 (3), 777–786..

    Not in our library10.1080/07391102.2020.1715838

  297. 297.

    Paul-Samojedny M.; Łasut B.; Pudełko A.; Fila-Daniłow A.; Kowalczyk M.; Suchanek-Raif R.; Zieliński M.; Borkowska P.; Kowalski J. Methylglyoxal (MGO) Inhibits Proliferation and Induces Cell Death of Human Glioblastoma Multiforme T98G and U87MG Cells. Biomed. Pharmacother. Biomedecine Pharmacother. 2016, 80, 236–243..

    Not in our library10.1016/j.biopha.2016.03.021

  298. 298.

    Nam H.-K.; Jeong S.-R.; Pyo M. C.; Ha S.-K.; Nam M.-H.; Lee K.-W. Methylglyoxal-Derived Advanced Glycation End Products (AGE4) Promote Cell Proliferation and Survival in Renal Cell Carcinoma Cells through the RAGE/Akt/ERK Signaling Pathways. Biol. Pharm. Bull. 2021, 44 (11), 1697–1706..

    Not in our library10.1248/bpb.b21-00382

  299. 299.

    Loarca L.; Sassi-Gaha S.; Artlett C. M. Two α-Dicarbonyls Downregulate Migration, Invasion, and Adhesion of Liver Cancer Cells in a P53-Dependent Manner. Dig. Liver Dis. 2013, 45 (11), 938–946..

    Not in our library10.1016/j.dld.2013.05.005

  300. 300.

    Ayoub F. M.; Allen R. E.; Thornalley P. J. Inhibition of Proliferation of Human Leukaemia 60 Cells by Methylglyoxal in Vitro. Leuk. Res. 1993, 17 (5), 397–401..

    Not in our library10.1016/0145-2126(93)90094-2

  301. 301.

    Kang Y.; Edwards L. G.; Thornalley P. J. Effect of Methylglyoxal on Human Leukaemia 60 Cell Growth: Modification of DNA G1 Growth Arrest and Induction of Apoptosis. Leuk. Res. 1996, 20 (5), 397–405..

    Not in our library10.1016/0145-2126(95)00162-x

  302. 302.

    Milanesa D. M.; Choudhury M. S.; Mallouh C.; Tazaki H.; Konno S. Methylglyoxal-Induced Apoptosis in Human Prostate Carcinoma: Potential Modality for Prostate Cancer Treatment. Eur. Urol. 2000, 37 (6), 728–734..

    Not in our library10.1159/000020226

  303. 303.

    Antognelli C.; Moretti S.; Frosini R.; Puxeddu E.; Sidoni A.; Talesa V. N. Methylglyoxal Acts as a Tumor-Promoting Factor in Anaplastic Thyroid Cancer. Cells 2019, 8 (6), 547.

    Not in our library10.3390/cells8060547

  304. 304.

    Lin J.-A.; Wu C.-H.; Yen G.-C. Methylglyoxal Displays Colorectal Cancer-Promoting Properties in the Murine Models of Azoxymethane and CT26 Isografts. Free Radic. Biol. Med. 2018, 115, 436–446..

    Not in our library10.1016/j.freeradbiomed.2017.12.020

  305. 305.

    Chen Y.; Fang L.; Li G.; Zhang J.; Li C.; Ma M.; Guan C.; Bai F.; Lyu J.; Meng Q. H. Synergistic Inhibition of Colon Cancer Growth by the Combination of Methylglyoxal and Silencing of Glyoxalase I Mediated by the STAT1 Pathway. Oncotarget 2017, 8 (33), 54838–54857..

    Not in our library10.18632/oncotarget.18601

  306. 306.

    He T.; Zhou H.; Li C.; Chen Y.; Chen X.; Li C.; Mao J.; Lyu J.; Meng Q. H. Methylglyoxal Suppresses Human Colon Cancer Cell Lines and Tumor Growth in a Mouse Model by Impairing Glycolytic Metabolism of Cancer Cells Associated with Down-Regulation of c-Myc Expression. Cancer Biol. Ther. 2016, 17 (9), 955–965..

    Not in our library10.1080/15384047.2016.1210736

  307. 307.

    Coluccio M. L.; Presta I.; Greco M.; Gervasi R.; La Torre D.; Renne M.; Voci C. P.; Lunelli L.; Donato G.; Malara N. Microenvironment Molecular Profile Combining Glycation Adducts and Cytokines Patterns on Secretome of Short-Term Blood-Derived Cultures during Tumour Progression. Int. J. Mol. Sci. 2020, 21 (13), 4711.

    Not in our library10.3390/ijms21134711

  308. 308.

    Chiavarina B.; Nokin M.-J.; Bellier J.; Durieux F.; Bletard N.; Sherer F.; Lovinfosse P.; Peulen O.; Verset L.; Dehon R.; Demetter P.; Turtoi A.; Uchida K.; Goldman S.; Hustinx R.; Delvenne P.; Castronovo V.; Bellahcène A. Methylglyoxal-Mediated Stress Correlates with High Metabolic Activity and Promotes Tumor Growth in Colorectal Cancer. Int. J. Mol. Sci. 2017, 18 (1), 213.

    Not in our library10.3390/ijms18010213

  309. 309.

    Saraiva M. A.; Borges C. M.; Florêncio M. H. Reactions of Aminoguanidine with α-Dicarbonyl Compounds Studied by Electrospray Ionization Mass Spectrometry. Eur. J. Mass Spectrom. Chichester Engl. 2012, 18 (4), 385–397..

    Not in our library10.1255/ejms.1191

  310. 310.

    Thornalley P. J. Use of Aminoguanidine (Pimagedine) to Prevent the Formation of Advanced Glycation Endproducts. Arch. Biochem. Biophys. 2003, 419 (1), 31–40..

    Not in our library10.1016/j.abb.2003.08.013

  311. 311.

    Thornalley P. J.; Yurek-George A.; Argirov O. K. Kinetics and Mechanism of the Reaction of Aminoguanidine with the Alpha-Oxoaldehydes Glyoxal, Methylglyoxal, and 3-Deoxyglucosone under Physiological Conditions. Biochem. Pharmacol. 2000, 60 (1), 55–65..

    Not in our library10.1016/s0006-2952(00)00287-2

  312. 312.

    Solís-Calero C.; Ortega-Castro J.; Hernández-Laguna A.; Muñoz F. DFT Study of the Mechanism of the Reaction of Aminoguanidine with Methylglyoxal. J. Mol. Model. 2014, 20 (4), 2202.

    Not in our library10.1007/s00894-014-2202-z

  313. 313.

    Lima T. F. O.; Costa M. C.; Figueiredo I. D.; Inácio M. D.; Rodrigues M. R.; Assis R. P.; Baviera A. M.; Brunetti I. L. Curcumin, Alone or in Combination with Aminoguanidine, Increases Antioxidant Defenses and Glycation Product Detoxification in Streptozotocin-Diabetic Rats: A Therapeutic Strategy to Mitigate Glycoxidative Stress. Oxid. Med. Cell. Longevity 2020, 2020, 1036360.

    Not in our library10.1155/2020/1036360

  314. 314.

    Li W.; Hu Q.; Ren X.; He P.; Xu H.; Dai H.; Chen Z. Aminoguanidine suppresses methylglyoxal-mediated oxygen-glucose deprivation injury in human brain microvascular endothelial cells. J. Zhejiang Univ. Med. Sci. 2013, 42 (3), 261–266.

    Not in our library

  315. 315.

    Liu B.-F.; Miyata S.; Hirota Y.; Higo S.; Miyazaki H.; Fukunaga M.; Hamada Y.; Ueyama S.; Muramoto O.; Uriuhara A.; Kasuga M. Methylglyoxal Induces Apoptosis through Activation of P38 Mitogen-Activated Protein Kinase in Rat Mesangial Cells. Kidney Int. 2003, 63 (3), 947–957..

    Not in our library10.1046/j.1523-1755.2003.00829.x

  316. 316.

    Magdaleno F.; Blajszczak C. C.; Charles-Niño C. L.; Guadrón-Llanos A. M.; Vázquez-Álvarez A. O.; Miranda-Díaz A. G.; Nieto N.; Islas-Carbajal M. C.; Rincón-Sánchez A. R. Aminoguanidine Reduces Diabetes-Associated Cardiac Fibrosis. Exp. Ther. Med. 2019, 18 (4), 3125–3138..

    Not in our library10.3892/etm.2019.7921

  317. 317.

    Lo T. W.; Selwood T.; Thornalley P. J. The Reaction of Methylglyoxal with Aminoguanidine under Physiological Conditions and Prevention of Methylglyoxal Binding to Plasma Proteins. Biochem. Pharmacol. 1994, 48 (10), 1865–1870..

    Not in our library10.1016/0006-2952(94)90584-3

  318. 318.

    Hsuuw Y.-D.; Chang C.-K.; Chan W.-H.; Yu J.-S. Curcumin Prevents Methylglyoxal-Induced Oxidative Stress and Apoptosis in Mouse Embryonic Stem Cells and Blastocysts. J. Cell. Physiol. 2005, 205 (3), 379–386..

    Not in our library10.1002/jcp.20408

  319. 319.

    Chan W.; Wu H. Protective Effects of Curcumin on Methylglyoxal-Induced Oxidative DNA Damage and Cell Injury in Human Mononuclear Cells. Acta Pharmacol. Sin. 2006, 27 (9), 1192–1198..

    Not in our library10.1111/j.1745-7254.2006.00374.x

  320. 320.

    Sun Y. P.; Gu J. F.; Tan X. B.; Wang C. F.; Jia X. B.; Feng L.; Liu J. P. Curcumin Inhibits Advanced Glycation End Product-Induced Oxidative Stress and Inflammatory Responses in Endothelial Cell Damage via Trapping Methylglyoxal. Mol. Med. Rep. 2016, 13 (2), 1475–1486..

    Not in our library10.3892/mmr.2015.4725

  321. 321.

    Hu T.-Y.; Liu C.-L.; Chyau C.-C.; Hu M.-L. Trapping of Methylglyoxal by Curcumin in Cell-Free Systems and in Human Umbilical Vein Endothelial Cells. J. Agric. Food Chem. 2012, 60 (33), 8190–8196..

    Not in our library10.1021/jf302188a

  322. 322.

    Roxo D. F.; Arcaro C. A.; Gutierres V. O.; Costa M. C.; Oliveira J. O.; Lima T. F. O.; Assis R. P.; Brunetti I. L.; Baviera A. M. Curcumin Combined with Metformin Decreases Glycemia and Dyslipidemia, and Increases Paraoxonase Activity in Diabetic Rats. Diabetol. Metab. Syndr. 2019, 11, 33.

    Not in our library10.1186/s13098-019-0431-0

  323. 323.

    Jung E.; Park S.-B.; Jung W. K.; Kim H. R.; Kim J. Antiglycation Activity of Aucubin In Vitro and in Exogenous Methylglyoxal Injected Rats. Molecules 2019, 24 (20), 3653.

    Not in our library10.3390/molecules24203653

  324. 324.

    Lv L.; Shao X.; Chen H.; Ho C.-T.; Sang S. Genistein Inhibits Advanced Glycation End Product Formation by Trapping Methylglyoxal. Chem. Res. Toxicol. 2011, 24 (4), 579–586..

    Not in our library10.1021/tx100457h

  325. 325.

    Li X.; Zheng T.; Sang S.; Lv L. Quercetin Inhibits Advanced Glycation End Product Formation by Trapping Methylglyoxal and Glyoxal. J. Agric. Food Chem. 2014, 62 (50), 12152–12158..

    Not in our library10.1021/jf504132x

  326. 326.

    Do M. H.; Hur J.; Choi J.; Kim M.; Kim M. J.; Kim Y.; Ha S. K. Eucommia Ulmoides Ameliorates Glucotoxicity by Suppressing Advanced Glycation End-Products in Diabetic Mice Kidney. Nutrients 2018, 10 (3), 265.

    Not in our library10.3390/nu10030265

  327. 327.

    Bucciarelli L. G.; Wendt T.; Qu W.; Lu Y.; Lalla E.; Rong L. L.; Goova M. T.; Moser B.; Kislinger T.; Lee D. C.; Kashyap Y.; Stern D. M.; Schmidt A. M. RAGE Blockade Stabilizes Established Atherosclerosis in Diabetic Apolipoprotein E-Null Mice. Circulation 2002, 106 (22), 2827–2835..

    Not in our library10.1161/01.cir.0000039325.03698.36

  328. 328.

    La Selva M.; Beltramo E.; Pagnozzi F.; Bena E.; Molinatti P. A.; Molinatti G. M.; Porta M. Thiamine Corrects Delayed Replication and Decreases Production of Lactate and Advanced Glycation End-Products in Bovine Retinal and Human Umbilical Vein Endothelial Cells Cultured under High Glucose Conditions. Diabetologia 1996, 39 (11), 1263–1268..

    Not in our library10.1007/s001250050568

  329. 329.

    Stracke H.; Hammes H. P.; Werkmann D.; Mavrakis K.; Bitsch I.; Netzel M.; Geyer J.; Köpcke W.; Sauerland C.; Bretzel R. G.; Federlin K. F. Efficacy of Benfotiamine versus Thiamine on Function and Glycation Products of Peripheral Nerves in Diabetic Rats. Exp. Clin. Endocrinol. Diabetes Off. J. Ger. Soc. Endocrinol. Ger. Diabetes Assoc. 2001, 109 (6), 330–336..

    Not in our library10.1055/s-2001-17399

  330. 330.

    Alkhalaf A.; Klooster A.; van Oeveren W.; Achenbach U.; Kleefstra N.; Slingerland R. J.; Mijnhout G. S.; Bilo H. J. G.; Gans R. O. B.; Navis G. J.; Bakker S. J. L. A Double-Blind, Randomized, Placebo-Controlled Clinical Trial on Benfotiamine Treatment in Patients with Diabetic Nephropathy. Diabetes Care 2010, 33 (7), 1598–1601..

    Not in our library10.2337/dc09-2241

  331. 331.

    Stirban A.; Negrean M.; Stratmann B.; Gawlowski T.; Horstmann T.; Götting C.; Kleesiek K.; Mueller-Roesel M.; Koschinsky T.; Uribarri J.; Vlassara H.; Tschoepe D. Benfotiamine Prevents Macro- and Microvascular Endothelial Dysfunction and Oxidative Stress Following a Meal Rich in Advanced Glycation End Products in Individuals with Type 2 Diabetes. Diabetes Care 2006, 29 (9), 2064–2071..

    Not in our library10.2337/dc06-0531

  332. 332.

    Du X.; Edelstein D.; Brownlee M. Oral Benfotiamine plus Alpha-Lipoic Acid Normalises Complication-Causing Pathways in Type 1 Diabetes. Diabetologia 2008, 51 (10), 1930–1932..

    Not in our library10.1007/s00125-008-1100-2

  333. 333.

    Contreras C. L.; Guzman-Rosiles I.; Del Castillo D.; Gomez-Ojeda A.; Garay-Sevilla Ma. E. Advanced Glycation End Products (AGEs) and SRAGE Levels after Benfotiamine Treatment in Diabetes Mellitus Type 2. FASEB J. 2017, 31 (S1), 646.32.

    Not in our library10.1096/fasebj.31.1_supplement.646.32

  334. 334.

    Bakris G. L.; Bank A. J.; Kass D. A.; Neutel J. M.; Preston R. A.; Oparil S. Advanced Glycation End-Product Cross-Link Breakers. A Novel Approach to Cardiovascular Pathologies Related to the Aging Process. Am. J. Hypertens. 2004, 17 (12), 23S–30S..

    Not in our library10.1016/j.amjhyper.2004.08.022

  335. 335.

    Toprak C.; Yigitaslan S. Alagebrium and Complications of Diabetes Mellitus. Eurasian J. Med. 2019, 51 (3), 285–292..

    Not in our library10.5152/eurasianjmed.2019.18434

  336. 336.
    A cross-link breaker has sustained effects on arterial and ventricular properties in older rhesus monkeys · 2001
    Not checked
  337. 337.

    Zieman S. J.; Melenovsky V.; Clattenburg L.; Corretti M. C.; Capriotti A.; Gerstenblith G.; Kass D. A. Advanced Glycation Endproduct Crosslink Breaker (Alagebrium) Improves Endothelial Function in Patients with Isolated Systolic Hypertension. J. Hypertens. 2007, 25 (3), 577–583..

    Not in our library10.1097/hjh.0b013e328013e7dd

  338. 338.

    Kass D. A.; Shapiro E. P.; Kawaguchi M.; Capriotti A. R.; Scuteri A.; deGroof R. C.; Lakatta E. G. Improved Arterial Compliance by a Novel Advanced Glycation End-Product Crosslink Breaker. Circulation 2001, 104 (13), 1464–1470..

    Not in our library10.1161/hc3801.097806

  339. 339.
    Inhibition of the RAGE products increases survival in experimental models of severe sepsis and systemic infection · 2007
    No notice
  340. 340.

    Christaki E.; Opal S. M.; Keith J. C. J.; Kessimian N.; Palardy J. E.; Parejo N. A.; Tan X. Y.; Piche-Nicholas N.; Tchistiakova L.; Vlasuk G. P.; Shields K. M.; Feldman J. L.; Lavallie E. R.; Arai M.; Mounts W.; Pittman D. D. A Monoclonal Antibody against RAGE Alters Gene Expression and Is Protective in Experimental Models of Sepsis and Pneumococcal Pneumonia. Shock Augusta Ga 2011, 35 (5), 492–498..

    Not in our library10.1097/shk.0b013e31820b2e1c

  341. 341.

    Xia P.; Deng Q.; Gao J.; Yu X.; Zhang Y.; Li J.; Guan W.; Hu J.; Tan Q.; Zhou L.; Han W.; Yuan Y.; Yu Y. Therapeutic Effects of Antigen Affinity-Purified Polyclonal Anti-Receptor of Advanced Glycation End-Product (RAGE) Antibodies on Cholestasis-Induced Liver Injury in Rats. Eur. J. Pharmacol. 2016, 779, 102–110..

    Not in our library10.1016/j.ejphar.2016.03.017

  342. 342.

    Sagheddu R.; Chiappalupi S.; Salvadori L.; Riuzzi F.; Donato R.; Sorci G. Targeting RAGE as a Potential Therapeutic Approach to Duchenne Muscular Dystrophy. Hum. Mol. Genet. 2018, 27 (21), 3734–3746..

    Not in our library10.1093/hmg/ddy288

  343. 343.

    Gasparotto J.; Ribeiro C. T.; Bortolin R. C.; Somensi N.; Fernandes H. S.; Teixeira A. A.; Guasselli M. O. R.; Agani C. A. J. O.; Souza N. C.; Grings M.; Leipnitz G.; Gomes H. M.; de Bittencourt Pasquali M. A.; Dunkley P. R.; Dickson P. W.; Moreira J. C. F.; Gelain D. P. Anti-RAGE Antibody Selectively Blocks Acute Systemic Inflammatory Responses to LPS in Serum, Liver, CSF and Striatum. Brain. Behav. Immun. 2017, 62, 124–136..

    Not in our library10.1016/j.bbi.2017.01.008

  344. 344.

    Bro S.; Flyvbjerg A.; Binder C. J.; Bang C. A.; Denner L.; Olgaard K.; Nielsen L. B. A Neutralizing Antibody against Receptor for Advanced Glycation End Products (RAGE) Reduces Atherosclerosis in Uremic Mice. Atherosclerosis 2008, 201 (2), 274–280..

    Not in our library10.1016/j.atherosclerosis.2008.01.015

  345. 345.

    Brederson J.-D.; Strakhova M.; Mills C.; Barlow E.; Meyer A.; Nimmrich V.; Leddy M.; Simler G.; Schmidt M.; Jarvis M.; Lacy S. A Monoclonal Antibody against the Receptor for Advanced Glycation End Products Attenuates Inflammatory and Neuropathic Pain in the Mouse. Eur. J. Pain London Engl. 2016, 20 (4), 607–614..

    Not in our library10.1002/ejp.775

  346. 346.

    Mizumoto S.; Takahashi J.; Sugahara K. Receptor for Advanced Glycation End Products (RAGE) Functions as Receptor for Specific Sulfated Glycosaminoglycans, and Anti-RAGE Antibody or Sulfated Glycosaminoglycans Delivered in Vivo Inhibit Pulmonary Metastasis of Tumor Cells. J. Biol. Chem. 2012, 287 (23), 18985–18994..

    Not in our library10.1074/jbc.m111.313437

  347. 347.

    Arumugam T.; Ramachandran V.; Gomez S. B.; Schmidt A. M.; Logsdon C. D. S100P-Derived RAGE Antagonistic Peptide Reduces Tumor Growth and Metastasis. Clin. Cancer Res. Off. J. Am. Assoc. Cancer Res. 2012, 18 (16), 4356–4364..

    Not in our library10.1158/1078-0432.ccr-12-0221

  348. 348.

    Putranto E. W.; Murata H.; Yamamoto K.-I.; Kataoka K.; Yamada H.; Futami J.-I.; Sakaguchi M.; Huh N.-H. Inhibition of RAGE Signaling through the Intracellular Delivery of Inhibitor Peptides by PEI Cationization. Int. J. Mol. Med. 2013, 32 (4), 938–944..

    Not in our library10.3892/ijmm.2013.1467

  349. 349.

    Yan Z.; Luo H.; Xie B.; Tian T.; Li S.; Chen Z.; Liu J.; Zhao X.; Zhang L.; Deng Y.; Billiar T. R.; Jiang Y. Targeting Adaptor Protein SLP76 of RAGE as a Therapeutic Approach for Lethal Sepsis. Nat. Commun. 2021, 12 (1), 308.

    Not in our library10.1038/s41467-020-20577-3

  350. 350.

    Matsui T.; Higashimoto Y.; Nishino Y.; Nakamura N.; Fukami K.; Yamagishi S.-I. RAGE-Aptamer Blocks the Development and Progression of Experimental Diabetic Nephropathy. Diabetes 2017, 66 (6), 1683–1695..

    Not in our library10.2337/db16-1281

  351. 351.
    An Aptamer-Based Antagonist against the Receptor for Advanced Glycation End-Products (RAGE) Blocks Development of Colorectal Cancer · 2021
    Not checked
  352. 352.

    Nakamura N.; Matsui T.; Nishino Y.; Sotokawauchi A.; Higashimoto Y.; Yamagishi S.-I. Long-Term Local Injection of RAGE-Aptamer Suppresses the Growth of Malignant Melanoma in Nude Mice. J. Oncol. 2019, 2019, 7387601.

    Not in our library10.1155/2019/7387601

  353. 353.

    Han Y. T.; Choi G.-I.; Son D.; Kim N.-J.; Yun H.; Lee S.; Chang D. J.; Hong H.-S.; Kim H.; Ha H.-J.; Kim Y.-H.; Park H.-J.; Lee J.; Suh Y.-G. Ligand-Based Design, Synthesis, and Biological Evaluation of 2-Aminopyrimidines, a Novel Series of Receptor for Advanced Glycation End Products (RAGE) Inhibitors. J. Med. Chem. 2012, 55 (21), 9120–9135..

    Not in our library10.1021/jm300172z

  354. 354.

    Han Y. T.; Kim K.; Choi G.-I.; An H.; Son D.; Kim H.; Ha H.-J.; Son J.-H.; Chung S.-J.; Park H.-J.; Lee J.; Suh Y.-G. Pyrazole-5-Carboxamides, Novel Inhibitors of Receptor for Advanced Glycation End Products (RAGE. Eur. J. Med. Chem. 2014, 79, 128–142..

    Not in our library10.1016/j.ejmech.2014.03.072

  355. 355.

    Kwak T.; Drews-Elger K.; Ergonul A.; Miller P. C.; Braley A.; Hwang G. H.; Zhao D.; Besser A.; Yamamoto Y.; Yamamoto H.; El-Ashry D.; Slingerland J. M.; Lippman M. E.; Hudson B. I. Targeting of RAGE-Ligand Signaling Impairs Breast Cancer Cell Invasion and Metastasis. Oncogene 2017, 36 (11), 1559–1572..

    Not in our library10.1038/onc.2016.324

  356. 356.

    Deane R.; Singh I.; Sagare A. P.; Bell R. D.; Ross N. T.; LaRue B.; Love R.; Perry S.; Paquette N.; Deane R. J.; Thiyagarajan M.; Zarcone T.; Fritz G.; Friedman A. E.; Miller B. L.; Zlokovic B. V. A Multimodal RAGE-Specific Inhibitor Reduces Amyloid β-Mediated Brain Disorder in a Mouse Model of Alzheimer Disease. J. Clin. Invest. 2012, 122 (4), 1377–1392..

    Not in our library10.1172/jci58642

  357. 357.

    Ostergar A.; Egbert K.; Clark C.; Hall P.; Davis T.; Hirschi K. M.; Arroyo J. A.; Reynolds P. R. Semi-Synthetic Glycosaminoglycan Ethers Decrease Receptors for Advanced Glycation End-Products and Increase AXL Receptor in the Lung from Secondhand Smoke Treated Mice. FASEB J. 2018, 32 (S1), 143.5.28904019

    Not in our library10.1096/fasebj.2018.32.1_supplement.143.5

  358. 358.

    Hirschi K. M.; Lewis J. B.; Hall P. D.; Wright T. J.; Egbert K. M.; Ogden K. C.; Nelson S. M.; Clark J. C.; Milner D. C.; Arroyo J. A.; Reynolds P. R. Abrogation of RAGE Signaling Using Semi-Synthetic Glycosaminoglycan Ethers (SAGEs) Ameliorates Inflammation in Mice Exposed to Secondhand Tobacco Smoke. FASEB J. 2017, 31 (S1), 656.1.

    Not in our library10.1096/fasebj.31.1_supplement.656.1

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