{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T11:20:39Z","timestamp":1787743239660,"version":"build-2784847793"},"reference-count":60,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T00:00:00Z","timestamp":1787702400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Clin. Diabetes Healthc."],"abstract":"<jats:p>Diabetes is characterized by chronic hyperglycemia and dyslipidemia, which impose sustained metabolic stress and drive the development of diabetic complications. In this review, we position the axis between advanced glycation end-products (AGEs) and the receptor for AGEs (RAGE) as a central hub that couples metabolic stress to persistent cellular stress and inflammatory responses. Ligand engagement of full-length membrane-bound RAGE (mRAGE) enhances reactive oxygen species (ROS) generation and activates nuclear factor kappa B (NF-\u03baB), establishing a self-amplifying feed-forward loop that promotes RAGE expression, inflammation and further AGE accumulation. RAGE exhibits marked structural heterogeneity: in addition to signaling-competent mRAGE, soluble decoy receptors\u2014including soluble RAGE (sRAGE) produced by ectodomain shedding and endogenous secretory RAGE (esRAGE) generated by alternative splicing\u2014sequester ligands and attenuate downstream signaling. Moreover, RAGE recognizes a broad ligand repertoire beyond AGEs, such as S100 proteins and high-mobility group box 1 (HMGB1), reinforcing its role as an integrator of metabolic and sterile inflammatory cues. Notably, RAGE also mediates physiological transport of oxytocin across the blood\u2013brain barrier (BBB), a process implicated in oxytocin-dependent social behaviors, without activating canonical, pro-inflammatory RAGE signaling. Accordingly, therapeutic strategies should selectively suppress pathogenic, ligand-driven RAGE signaling and\/or augment decoy RAGE activity while preserving RAGE-dependent oxytocin transport.<\/jats:p>","DOI":"10.3389\/fcdhc.2026.1854214","type":"journal-article","created":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T10:40:43Z","timestamp":1787740843000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":0,"title":["Decoding RAGE in diabetes: a pathogenic signaling hub modulated by decoy receptors in diabetic complications"],"prefix":"10.3389","volume":"7","author":[{"given":"Yupa","family":"Srithongchai","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ai","family":"Harashima","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Seiichi","family":"Munesue","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kumi","family":"Kimura","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Oshima","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mariko","family":"Tanaka","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroya","family":"Takahashi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pathitta","family":"Sakulsak","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chisato","family":"Uramoto","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nontaphat","family":"Leerach","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]},{"name":"Princess Srisavangavadhana Faculty of Medicine, Chulabhorn Royal Academy","place":["Bangkok, Thailand"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuhiko","family":"Yamamoto","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Vascular Biology, Kanazawa University Graduate School of Medical Sciences","place":["Kanazawa, Japan"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2026,8,26]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1038\/nri2925","article-title":"Type 2 diabetes as an inflammatory disease","volume":"11","author":"Donath","year":"2011","journal-title":"Nat Rev Immunol"},{"key":"B2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1042\/bj2690001","article-title":"The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life","volume":"269","author":"Thornalley","year":"1990","journal-title":"Biochem J"},{"key":"B3","doi-asserted-by":"publisher","DOI":"10.1007\/s00726-010-0783-0","article-title":"Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome","volume":"42","author":"Rabbani","year":"2012","journal-title":"Amino Acids"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2015.01.140","article-title":"Dicarbonyl stress in cell and tissue dysfunction contributing to ageing and disease","volume":"458","author":"Rabbani","year":"2015","journal-title":"Biochem Biophys Res Commun"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.1016\/s0021-9258(18)42138-2","article-title":"Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins","volume":"267","author":"Neeper","year":"1992","journal-title":"J Biol Chem"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1016\/s0021-9258(18)42137-0","article-title":"Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface","volume":"267","author":"Schmidt","year":"1992","journal-title":"J Biol Chem"},{"key":"B7","doi-asserted-by":"publisher","DOI":"10.1055\/s-2000-13204","article-title":"RAGE: a multiligand receptor contributing to the cellular response in diabetic vasculopathy and inflammation","volume":"26","author":"Schmidt","year":"2000","journal-title":"Semin Thromb Hemost"},{"key":"B8","doi-asserted-by":"publisher","DOI":"10.3389\/fendo.2013.00105","article-title":"RAGE-mediated inflammation, type 2 diabetes, and diabetic vascular complication","volume":"4","author":"Yamamoto","year":"2013","journal-title":"Front Endocrinol (Lausanne)"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M801465200","article-title":"Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42","volume":"283","author":"Hudson","year":"2008","journal-title":"J Biol Chem"},{"key":"B10","doi-asserted-by":"publisher","DOI":"10.1038\/414813a","article-title":"Biochemistry and molecular cell biology of diabetic complications","volume":"414","author":"Brownlee","year":"2001","journal-title":"Nature"},{"key":"B11","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M001235200","article-title":"The receptor for advanced glycation end products is induced by the glycation products themselves and tumor necrosis factor-\u03b1 through nuclear factor-\u03baB, and by 17\u03b2-estradiol through Sp-1 in human vascular endothelial cells","volume":"275","author":"Tanaka","year":"2000","journal-title":"J Biol Chem"},{"key":"B12","doi-asserted-by":"publisher","DOI":"10.1038\/labinvest.3780116","article-title":"Interaction of the receptor for advanced glycation end products (RAGE) with transthyretin triggers nuclear transcription factor \u03baB (NF-\u03baB) activation","volume":"80","author":"Sousa","year":"2000","journal-title":"Lab Invest"},{"key":"B13","doi-asserted-by":"publisher","DOI":"10.1096\/fj.08-109033","article-title":"A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10)","volume":"22","author":"Raucci","year":"2008","journal-title":"FASEB J"},{"key":"B14","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20051573","article-title":"Identification of mouse orthologue of endogenous secretory receptor for advanced glycation end-products: structure, function and expression","volume":"396","author":"Harashima","year":"2006","journal-title":"Biochem J"},{"key":"B15","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20021371","article-title":"Novel splice variants of the receptor for advanced glycation end-products expressed in human vascular endothelial cells and pericytes, and their putative roles in diabetes-induced vascular injury","volume":"370","author":"Yonekura","year":"2003","journal-title":"Biochem J"},{"key":"B16","doi-asserted-by":"publisher","DOI":"10.1038\/35008121","article-title":"Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage","volume":"404","author":"Nishikawa","year":"2000","journal-title":"Nature"},{"key":"B17","doi-asserted-by":"publisher","DOI":"10.1126\/science.1103160","article-title":"Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes","volume":"306","author":"Ozcan","year":"2004","journal-title":"Science"},{"key":"B18","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1007\/BF00808119","article-title":"Methylglyoxal, glyoxalases and the development of diabetic complications","volume":"6","author":"Thornalley","year":"1994","journal-title":"Amino Acids"},{"key":"B19","doi-asserted-by":"publisher","DOI":"10.1254\/jphs.CPJ04005X","article-title":"Roles of the receptor for advanced glycation endproducts in diabetes-induced vascular injury","volume":"97","author":"Yonekura","year":"2005","journal-title":"J Pharmacol Sci"},{"key":"B20","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.1002253","article-title":"Septic shock is associated with receptor for advanced glycation end products ligation of LPS","volume":"186","author":"Yamamoto","year":"2011","journal-title":"J Immunol"},{"key":"B21","doi-asserted-by":"publisher","first-page":"467","DOI":"10.3233\/JAD-161152","article-title":"Activation of macrophages and microglia by interferon-gamma and lipopolysaccharide increases methylglyoxal production: a new mechanism in the development of vascular complications and cognitive decline in type 2 diabetes mellitus?","volume":"59","author":"Dhananjayan","year":"2017","journal-title":"Journal of Alzheimer's Disease"},{"key":"B22","doi-asserted-by":"publisher","first-page":"23137","DOI":"10.1074\/jbc.M110.133827","article-title":"Homodimerization is essential for the receptor for advanced glycation end products (RAGE)-mediated signal transduction","volume":"285","author":"Zong","year":"2010","journal-title":"Journal of Biological Chemistry"},{"key":"B23","doi-asserted-by":"publisher","first-page":"1509","DOI":"10.1016\/j.str.2016.06.021","article-title":"Change in the molecular dimension of a RAGE-ligand complex triggers RAGE signaling","volume":"24","author":"Xue","year":"2016","journal-title":"Structure"},{"key":"B24","doi-asserted-by":"publisher","DOI":"10.1038\/srep22450","article-title":"Small molecule inhibition of ligand-stimulated RAGE-DIAPH1 signal transduction","volume":"6","author":"Manigrasso","year":"2016","journal-title":"Sci Rep"},{"key":"B25","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbamcr.2023.119573","article-title":"Reactive oxygen species and cell signaling","volume":"1871","author":"Averill-Bates","year":"2024","journal-title":"Biochim Biophys Acta Mol Cell Res"},{"key":"B26","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuint.2019.03.012","article-title":"The receptor for advanced glycation end products (RAGE) and DIAPH1: implications for vascular and neuroinflammatory dysfunction in disorders of the central nervous system","volume":"126","author":"MacLean","year":"2019","journal-title":"Neurochem Int"},{"key":"B27","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.abf7084","article-title":"Small-molecule antagonism of the interaction of the RAGE cytoplasmic domain with DIAPH1 reduces diabetic complications in mice","volume":"13","author":"Manigrasso","year":"2021","journal-title":"Sci Transl Med"},{"key":"B28","doi-asserted-by":"publisher","DOI":"10.1002\/oby.23774","article-title":"Pharmacological antagonism of receptor for advanced glycation end products signaling promotes thermogenesis and healthy body mass and composition","volume":"31","author":"Wilson","year":"2023","journal-title":"Obes (Silver Spring)"},{"key":"B29","doi-asserted-by":"publisher","first-page":"1221","DOI":"10.1016\/j.chembiol.2025.09.004","article-title":"RAGE-mediated activation of the formin DIAPH1 and human macrophage inflammation are inhibited by a small molecule antagonist","volume":"32","author":"Theophall","year":"2025","journal-title":"Cell Chem Biol"},{"key":"B30","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1042\/BJ20140084","article-title":"cAMP ameliorates inflammation by modulation of macrophage receptor for advanced glycation end-products","volume":"463","author":"Motoyoshi","year":"2014","journal-title":"Biochem J"},{"key":"B31","doi-asserted-by":"publisher","DOI":"10.1096\/fj.201701553RR","article-title":"JNK and ATF4 as two important platforms for tumor necrosis factor-\u03b1-stimulated shedding of receptor for advanced glycation end products","volume":"33","author":"Miyoshi","year":"2019","journal-title":"FASEB J"},{"key":"B32","doi-asserted-by":"publisher","DOI":"10.1161\/01.atv.0000251533.18013.67","article-title":"Endogenous secretory receptor for advanced glycation endproducts levels are correlated with serum pentosidine and CML in patients with type 1 diabetes","volume":"27","author":"Miura","year":"2007","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"B33","doi-asserted-by":"publisher","DOI":"10.1038\/modpathol.3800450","article-title":"Expression profiling of endogenous secretory receptor for advanced glycation end products in human organs","volume":"18","author":"Cheng","year":"2005","journal-title":"Mod Pathol"},{"key":"B34","doi-asserted-by":"publisher","first-page":"2116","DOI":"10.2337\/db12-1528","article-title":"sRAGE and risk of diabetes, cardiovascular disease, and death","volume":"62","author":"Selvin","year":"2013","journal-title":"Diabetes"},{"key":"B35","doi-asserted-by":"publisher","first-page":"785","DOI":"10.2217\/bmm-2020-0856","article-title":"Modulation of soluble receptor for advanced glycation end products isoforms and advanced glycation end products in long-living individuals","volume":"11","author":"Scavello","year":"2021","journal-title":"Biomarkers in Medicine"},{"key":"B36","doi-asserted-by":"publisher","first-page":"2379","DOI":"10.2337\/db11-0291","article-title":"Total soluble and endogenous secretory receptor for advanced glycation end products as predictive biomarkers of coronary heart disease risk in patients with type 2 diabetes: an analysis from the CARDS trial","volume":"60","author":"Colhoun","year":"2011","journal-title":"Diabetes"},{"key":"B37","doi-asserted-by":"publisher","first-page":"1891","DOI":"10.2337\/dc15-0925","article-title":"Relationship between levels of advanced glycation end products and their soluble receptor and adverse outcomes in adults with type 2 diabetes","volume":"38","author":"Thomas","year":"2015","journal-title":"Diabetes Care"},{"key":"B38","doi-asserted-by":"publisher","DOI":"10.3389\/fnins.2022.858070","article-title":"Oxytocin dynamics in the body and brain regulated by the receptor for advanced glycation end-products, CD38, CD157, and nicotinamide riboside","volume":"16","author":"Higashida","year":"2022","journal-title":"Front Neurosci"},{"key":"B39","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1146\/annurev-psych-010213-115110","article-title":"Oxytocin pathways and the evolution of human behavior","volume":"65","author":"Carter","year":"2014","journal-title":"Annu Rev Psychol"},{"key":"B40","doi-asserted-by":"publisher","DOI":"10.1038\/nature05526","article-title":"CD38 is critical for social behaviour by regulating oxytocin secretion","volume":"446","author":"Jin","year":"2007","journal-title":"Nature"},{"key":"B41","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1038\/s42003-019-0325-6","article-title":"Vascular RAGE transports oxytocin into the brain to elicit its maternal bonding behaviour in mice","volume":"2","author":"Yamamoto","year":"2019","journal-title":"Commun Biol"},{"key":"B42","doi-asserted-by":"publisher","first-page":"70","DOI":"10.1038\/s42003-020-0799-2","article-title":"RAGE regulates oxytocin transport into the brain","volume":"3","author":"Yamamoto","year":"2020","journal-title":"Commun Biol"},{"key":"B43","doi-asserted-by":"publisher","DOI":"10.1111\/jne.12963","article-title":"Transport of oxytocin to the brain after peripheral administration by membrane-bound or soluble forms of receptors for advanced glycation end-products","volume":"33","author":"Munesue","year":"2021","journal-title":"J Neuroendocrinol"},{"key":"B44","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2025.152004","article-title":"Complement component C4a binds to oxytocin and modulates plasma oxytocin concentrations and social behavior in male mice","volume":"771","author":"Yamamoto","year":"2025","journal-title":"Biochem Biophys Res Commun"},{"key":"B45","doi-asserted-by":"publisher","first-page":"4683","DOI":"10.1210\/jc.2014-2206","article-title":"Decreased circulating levels of oxytocin in obesity and newly diagnosed type 2 diabetic patients","volume":"99","author":"Qian","year":"2014","journal-title":"Journal of Clinical Endocrinology & Metabolism"},{"key":"B46","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1002\/dmrr.2577","article-title":"Oxytocin levels are lower in premenopausal women with type 1 diabetes mellitus compared with matched controls","volume":"31","author":"Kujath","year":"2015","journal-title":"Diabetes\/Metabolism Research and Reviews"},{"key":"B47","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1186\/s40478-023-01606-w","article-title":"Reduction of oxytocin-containing neurons and enhanced glymphatic activity in the hypothalamic paraventricular nucleus of patients with type 2 diabetes mellitus","volume":"11","author":"Correa-da-Silva","year":"2023","journal-title":"Acta Neuropathologica Communications"},{"key":"B48","doi-asserted-by":"publisher","DOI":"10.1172\/JCI58642","article-title":"A multimodal RAGE-specific inhibitor reduces amyloid \u03b2-mediated brain disorder in a mouse model of Alzheimer disease","volume":"122","author":"Deane","year":"2012","journal-title":"J Clin Invest"},{"key":"B49","doi-asserted-by":"publisher","DOI":"10.14283\/jpad.2018.18","article-title":"Development of Azeliragon, an oral small molecule antagonist of RAGE, for Alzheimer\u2019s disease","volume":"5","author":"Burstein","year":"2018","journal-title":"J\u00a0Prev Alzheimers Dis"},{"key":"B50","doi-asserted-by":"publisher","first-page":"1536","DOI":"10.1212\/WNL.0000000000000364","article-title":"Clinical trial of an inhibitor of RAGE-A\u03b2 interactions in Alzheimer disease","volume":"82","author":"Galasko","year":"2014","journal-title":"Neurology"},{"key":"B51","unstructured":"vTv Therapeutics Announces Topline Results from the First STEADFAST Phase 3 Study Evaluating Azeliragon in People with Mild Alzheimer\u2019s Disease\n          \n          \n          2018"},{"key":"B52","doi-asserted-by":"publisher","first-page":"2015","DOI":"10.1200\/JCO.2026.44.1_suppl.2015","article-title":"Azeliragon, a RAGE inhibitor, plus temozolomide and radiotherapy in patients with newly diagnosed glioblastoma: Final results from a dose-finding phase in the CAN-201 NDG trial","volume":"44","author":"Garcia","year":"2026","journal-title":"Journal of Clinical Oncology"},{"key":"B53","doi-asserted-by":"publisher","DOI":"10.3892\/ol.2018.7902","article-title":"In vitro anticancer effects of a RAGE inhibitor discovered using a structure-based drug design system","volume":"15","author":"El-Far","year":"2018","journal-title":"Oncol Lett"},{"key":"B54","doi-asserted-by":"publisher","DOI":"10.1111\/cas.12133","article-title":"Low molecular weight heparin suppresses receptor for advanced glycation end products-mediated expression of Malignant phenotype in human fibrosarcoma cells","volume":"104","author":"Takeuchi","year":"2013","journal-title":"Cancer Sci"},{"key":"B55","doi-asserted-by":"publisher","DOI":"10.2337\/db06-0221","article-title":"RAGE control of diabetic nephropathy in a mouse model: effects of RAGE gene disruption and administration of low-molecular weight heparin","volume":"55","author":"Myint","year":"2006","journal-title":"Diabetes"},{"key":"B56","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2026.153540","article-title":"Integrated discovery of SBLR876: a potent RAGE inhibitor mitigating AGE-RAGE-NF-\u03baB-mediated cytotoxicity and inflammation in diabetic kidney disease","volume":"746","author":"Al Shahrani","year":"2026","journal-title":"Biochem Biophys Res Commun"},{"key":"B57","doi-asserted-by":"publisher","DOI":"10.1002\/cmdc.202500503","article-title":"Development of new benzo[b]thiophene-2-carboxamide derivatives as advanced glycation end-products receptor (RAGE) antagonists","volume":"21","author":"Bonin","year":"2026","journal-title":"ChemMedChem"},{"key":"B58","doi-asserted-by":"publisher","DOI":"10.1164\/ajrccm-conference.2024.209.1_MeetingAbstracts.A1376","article-title":"A first-in-human study of ARO-RAGE, a novel inhaled RNA-interference therapy for asthma","volume":"209","author":"O'Carroll","year":"2024","journal-title":"Am J Respir Crit Care Med"},{"key":"B59","volume-title":"Study of ARO-RAGE in healthy subjects and subjects with asthma (ARORAGE-1001). Identifier: NCT05276570","year":""},{"key":"B60","doi-asserted-by":"publisher","DOI":"10.1042\/BST0311417","article-title":"Quantitative screening of protein biomarkers of early glycation, advanced glycation, oxidation and nitrosation in cellular and extracellular proteins by tandem mass spectrometry multiple reaction monitoring","volume":"31","author":"Ahmed","year":"2003","journal-title":"Biochem Soc Trans"}],"container-title":["Frontiers in Clinical Diabetes and Healthcare"],"original-title":[],"link":[{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fcdhc.2026.1854214\/full","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T10:40:44Z","timestamp":1787740844000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.frontiersin.org\/articles\/10.3389\/fcdhc.2026.1854214\/full"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,26]]},"references-count":60,"alternative-id":["10.3389\/fcdhc.2026.1854214"],"URL":"https:\/\/doi.org\/10.3389\/fcdhc.2026.1854214","relation":{},"ISSN":["2673-6616"],"issn-type":[{"value":"2673-6616","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,8,26]]},"article-number":"1854214"}}