{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T03:15:15Z","timestamp":1791429315095,"version":"4.3.3"},"reference-count":50,"publisher":"Elsevier BV","issue":"1-2","license":[{"start":{"date-parts":[[2012,6,1]],"date-time":"2012-06-01T00:00:00Z","timestamp":1338508800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of the Neurological Sciences"],"published-print":{"date-parts":[[2012,6]]},"DOI":"10.1016\/j.jns.2012.02.018","type":"journal-article","created":{"date-parts":[[2012,3,11]],"date-time":"2012-03-11T12:01:31Z","timestamp":1331467291000},"page":"1-5","source":"Crossref","is-referenced-by-count":292,"title":["Advanced glycation end products and neurodegenerative diseases: Mechanisms and perspective"],"prefix":"10.1016","volume":"317","author":[{"given":"Jinlong","family":"Li","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danian","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ling","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yunting","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhongling","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jns.2012.02.018_bb0005","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.nbd.2010.08.015","article-title":"The elimination of accumulated and aggregated proteins: a role for aggrephagy in neurodegeneration","volume":"43","author":"Yamamoto","year":"2011","journal-title":"Neurobiol Dis"},{"key":"10.1016\/j.jns.2012.02.018_bb0010","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1007\/978-1-60327-029-8_17","article-title":"Redox homeostasis and cellular stress response in aging and neurodegeneration","volume":"610","author":"Calabrese","year":"2010","journal-title":"Methods Mol Biol"},{"key":"10.1016\/j.jns.2012.02.018_bb0015","first-page":"699","article-title":"The aging brain, metals and oxygen free radicals","volume":"46","author":"Samson","year":"2000","journal-title":"Cell Mol Biol (Noisy-le-Grand)"},{"key":"10.1016\/j.jns.2012.02.018_bb0020","doi-asserted-by":"crossref","first-page":"4904","DOI":"10.1046\/j.1432-1327.2000.01595.x","article-title":"Glutathione, oxidative stress and neurodegeneration","volume":"267","author":"Schulz","year":"2000","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.jns.2012.02.018_bb0025","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1002\/path.2682","article-title":"The sour side of neurodegenerative disorders: the effects of protein glycation","volume":"221","author":"Vicente","year":"2010","journal-title":"J Pathol"},{"key":"10.1016\/j.jns.2012.02.018_bb0030","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1016\/j.neurobiolaging.2009.04.016","article-title":"Advanced glycation endproducts and their receptor RAGE in Alzheimer's disease","volume":"32","author":"Srikanth","year":"2011","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.jns.2012.02.018_bb0035","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1007\/s00726-007-0606-0","article-title":"Advanced glycation end-products (AGEs): involvement in aging and in neurodegenerative diseases","volume":"35","author":"Grillo","year":"2008","journal-title":"Amino Acids"},{"key":"10.1016\/j.jns.2012.02.018_bb0040","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1042\/bst0210549","article-title":"Mechanism for the formation of methylglyoxal from triosephosphates","volume":"21","author":"Richard","year":"1993","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/j.jns.2012.02.018_bb0045","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1016\/0306-3623(95)02054-3","article-title":"Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification \u2014 a role in pathogenesis and antiproliferative chemotherapy","volume":"27","author":"Thornalley","year":"1996","journal-title":"Gen Pharmacol"},{"key":"10.1016\/j.jns.2012.02.018_bb0050","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1139\/y06-077","article-title":"Methylglyoxal, oxidative stress, and hypertension","volume":"84","author":"Chang","year":"2006","journal-title":"Can J Physiol Pharmacol"},{"key":"10.1016\/j.jns.2012.02.018_bb0055","doi-asserted-by":"crossref","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":"10.1016\/j.jns.2012.02.018_bb0060","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/0304-4165(84)90131-4","article-title":"The autoxidation of glyceraldehyde and other simple monosaccharides under physiological conditions catalysed by buffer ions","volume":"797","author":"Thornalley","year":"1984","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jns.2012.02.018_bb0065","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0009-2797(97)00157-9","article-title":"Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors","volume":"111\u2013112","author":"Thornalley","year":"1998","journal-title":"Chem Biol Interact"},{"key":"10.1016\/j.jns.2012.02.018_bb0070","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/S0378-4347(99)00113-9","article-title":"3-Deoxyglucosone: metabolism, analysis, biological activity, and clinical implication","volume":"731","author":"Niwa","year":"1999","journal-title":"J Chromatogr B Biomed Sci Appl"},{"key":"10.1016\/j.jns.2012.02.018_bb0075","doi-asserted-by":"crossref","first-page":"2232","DOI":"10.2174\/092986710791331086","article-title":"RAGE: a multi-ligand receptor unveiling novel insights in health and disease","volume":"17","author":"Alexiou","year":"2010","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.jns.2012.02.018_bb0080","doi-asserted-by":"crossref","first-page":"14998","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":"10.1016\/j.jns.2012.02.018_bb0085","doi-asserted-by":"crossref","first-page":"998","DOI":"10.1046\/j.0022-3042.2002.00796.x","article-title":"N-Glycans on the receptor for advanced glycation end products influence amphoterin binding and neurite outgrowth","volume":"80","author":"Srikrishna","year":"2002","journal-title":"J Neurochem"},{"key":"10.1016\/j.jns.2012.02.018_bb0090","doi-asserted-by":"crossref","first-page":"3923","DOI":"10.1007\/s00018-009-0121-4","article-title":"Ectodomain shedding of the receptor for advanced glycation end products: a novel therapeutic target for Alzheimer's disease","volume":"66","author":"Zhang","year":"2009","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.jns.2012.02.018_bb0095","doi-asserted-by":"crossref","first-page":"876","DOI":"10.1007\/s00109-005-0688-7","article-title":"Understanding RAGE, the receptor for advanced glycation end products","volume":"83","author":"Bierhaus","year":"2005","journal-title":"J Mol Med (Berl)"},{"key":"10.1016\/j.jns.2012.02.018_bb0100","doi-asserted-by":"crossref","first-page":"16498","DOI":"10.1074\/jbc.272.26.16498","article-title":"Characterization and functional analysis of the promoter of RAGE, the receptor for advanced glycation end products","volume":"272","author":"Li","year":"1997","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jns.2012.02.018_bb0105","doi-asserted-by":"crossref","first-page":"2639","DOI":"10.1096\/fj.08-126383","article-title":"RAGE regulates BACE1 and Abeta generation via NFAT1 activation in Alzheimer's disease animal model","volume":"23","author":"Cho","year":"2009","journal-title":"FASEB J"},{"key":"10.1016\/j.jns.2012.02.018_bb0110","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1007\/s12640-010-9231-x","article-title":"Extracellular HMGB1 released by NMDA treatment confers neuronal apoptosis via RAGE-p38 MAPK\/ERK signaling pathway","volume":"20","author":"Kim","year":"2011","journal-title":"Neurotox Res"},{"key":"10.1016\/j.jns.2012.02.018_bb0115","doi-asserted-by":"crossref","first-page":"38635","DOI":"10.1074\/jbc.M202515200","article-title":"Receptor for advanced glycation end products (RAGE) signaling induces CREB-dependent chromogranin expression during neuronal differentiation","volume":"277","author":"Huttunen","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jns.2012.02.018_bb0120","doi-asserted-by":"crossref","first-page":"23233","DOI":"10.1074\/jbc.M110.117457","article-title":"Advanced glycation end product (AGE)-receptor for AGE (RAGE) signaling and up-regulation of Egr-1 in hypoxic macrophages","volume":"285","author":"Xu","year":"2010","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jns.2012.02.018_bb0125","doi-asserted-by":"crossref","first-page":"34457","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":"10.1016\/j.jns.2012.02.018_bb0130","doi-asserted-by":"crossref","first-page":"1175","DOI":"10.1172\/JCI8593","article-title":"A genetic dichotomy model for the inheritance of Alzheimer's disease and common age-related disorders","volume":"104","author":"Tanzi","year":"1999","journal-title":"J Clin Invest"},{"key":"10.1016\/j.jns.2012.02.018_bb0135","first-page":"1121","article-title":"The role of cerebral amyloid beta accumulation in common forms of Alzheimer disease","volume":"115","author":"Gandy","year":"2005","journal-title":"J Clin Invest"},{"key":"10.1016\/j.jns.2012.02.018_bb0140","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/0006-8993(94)90156-2","article-title":"Differential expression of advanced glycosylation end-products in neurons of different species","volume":"641","author":"Li","year":"1994","journal-title":"Brain Res"},{"key":"10.1016\/j.jns.2012.02.018_bb0145","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0925-4439(96)00062-2","article-title":"Influence of advanced glycation end-products and AGE-inhibitors on nucleation-dependent polymerization of beta-amyloid peptide","volume":"1360","author":"Munch","year":"1997","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jns.2012.02.018_bb0150","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.freeradbiomed.2010.05.005","article-title":"Advanced glycation end products enhance amyloid precursor protein expression by inducing reactive oxygen species","volume":"49","author":"Ko","year":"2010","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.jns.2012.02.018_bb0155","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1016\/j.neurobiolaging.2009.04.021","article-title":"Apolipoprotein E: implications for AD neurobiology, epidemiology and risk assessment","volume":"32","author":"Schipper","year":"2011","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.jns.2012.02.018_bb0160","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0304-3940(97)00266-8","article-title":"Enhanced binding of advanced glycation endproducts (AGE) by the ApoE4 isoform links the mechanism of plaque deposition in Alzheimer's disease","volume":"226","author":"Li","year":"1997","journal-title":"Neurosci Lett"},{"key":"10.1016\/j.jns.2012.02.018_bb0165","doi-asserted-by":"crossref","first-page":"1658","DOI":"10.1046\/j.1471-4159.1995.65041658.x","article-title":"Tau protein from Alzheimer's disease patients is glycated at its tubulin-binding domain","volume":"65","author":"Ledesma","year":"1995","journal-title":"J Neurochem"},{"key":"10.1016\/j.jns.2012.02.018_bb0170","article-title":"AGEs induce Alzheimer-like tau pathology and memory deficit via RAGE-mediated GSK-3 activation","author":"Li","year":"2011","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.jns.2012.02.018_bb0175","doi-asserted-by":"crossref","first-page":"2055","DOI":"10.1016\/S0140-6736(09)60492-X","article-title":"Parkinson's disease","volume":"373","author":"Lees","year":"2009","journal-title":"Lancet"},{"key":"10.1016\/j.jns.2012.02.018_bb0180","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1097\/00005072-199603000-00001","article-title":"Neuropathology of Parkinson's disease","volume":"55","author":"Forno","year":"1996","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1016\/j.jns.2012.02.018_bb0185","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0197-4580(02)00065-9","article-title":"Staging of brain pathology related to sporadic Parkinson's disease","volume":"24","author":"Braak","year":"2003","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.jns.2012.02.018_bb0190","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1126\/science.1143780","article-title":"Sirtuin 2 inhibitors rescue alpha-synuclein-mediated toxicity in models of Parkinson's disease","volume":"317","author":"Outeiro","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.jns.2012.02.018_bb0195","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.bbapap.2008.11.016","article-title":"The modification of alpha-synuclein by dicarbonyl compounds inhibits its fibril-forming process","volume":"1794","author":"Lee","year":"2009","journal-title":"Biochim Biophys Acta"},{"issue":"Suppl 2","key":"10.1016\/j.jns.2012.02.018_bb0200","doi-asserted-by":"crossref","first-page":"211","DOI":"10.3233\/JAD-2011-101965","article-title":"Role of advanced glycation on aggregation and DNA binding properties of alpha-synuclein","volume":"24","author":"Padmaraju","year":"2011","journal-title":"J Alzheimers Dis"},{"key":"10.1016\/j.jns.2012.02.018_bb0205","doi-asserted-by":"crossref","first-page":"e9052","DOI":"10.1371\/journal.pone.0009052","article-title":"Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products","volume":"5","author":"Chen","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.jns.2012.02.018_bb0210","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1097\/01.jnen.0000179050.54522.5a","article-title":"Evidence of oxidative stress in the neocortex in incidental Lewy body disease","volume":"64","author":"Dalfo","year":"2005","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.1016\/j.jns.2012.02.018_bb0215","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0006-8993(96)00729-9","article-title":"Glycoxidation and oxidative stress in Parkinson disease and diffuse Lewy body disease","volume":"737","author":"Castellani","year":"1996","journal-title":"Brain Res"},{"key":"10.1016\/j.jns.2012.02.018_bb0220","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.neulet.2004.08.071","article-title":"The advanced glycation end-product N epsilon-(carboxymethyl)lysine level is elevated in cerebrospinal fluid of patients with amyotrophic lateral sclerosis","volume":"371","author":"Kaufmann","year":"2004","journal-title":"Neurosci Lett"},{"key":"10.1016\/j.jns.2012.02.018_bb0225","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1042\/BJ20040833","article-title":"Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy","volume":"385","author":"Gomes","year":"2005","journal-title":"Biochem J"},{"key":"10.1016\/j.jns.2012.02.018_bb0230","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/S0304-3940(02)00310-5","article-title":"Advanced glycation end products (AGE) and their receptor (RAGE) in the brain of patients with Creutzfeldt\u2013Jakob disease with prion plaques","volume":"326","author":"Sasaki","year":"2002","journal-title":"Neurosci Lett"},{"key":"10.1016\/j.jns.2012.02.018_bb0235","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1016\/j.brainresbull.2011.01.009","article-title":"Immunohistochemical localization of receptor for advanced glycation end (RAGE) products in the R6\/2 mouse model of Huntington's disease","volume":"87","author":"Anzilotti","year":"2011","journal-title":"Brain Res Bull"},{"key":"10.1016\/j.jns.2012.02.018_bb0240","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1002\/cbf.1714","article-title":"Proteomics analysis of methylglyoxal-induced neurotoxic effects in SH-SY5Y cells","volume":"29","author":"Li","year":"2011","journal-title":"Cell Biochem Funct"},{"key":"10.1016\/j.jns.2012.02.018_bb0245","doi-asserted-by":"crossref","first-page":"442","DOI":"10.2337\/dc10-1087","article-title":"Higher plasma levels of advanced glycation end products are associated with incident cardiovascular disease and all-cause mortality in type 1 diabetes: a 12-year follow-up study","volume":"34","author":"Nin","year":"2011","journal-title":"Diabetes Care"},{"key":"10.1016\/j.jns.2012.02.018_bb0250","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1515\/CCLM.2011.079","article-title":"Advanced glycation endproducts as gerontotoxins and biomarkers for carbonyl-based degenerative processes in Alzheimer's disease","volume":"49","author":"Rahmadi","year":"2011","journal-title":"Clin Chem Lab Med"}],"container-title":["Journal of the Neurological Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022510X12001013?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022510X12001013?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,1,2]],"date-time":"2022-01-02T09:56:24Z","timestamp":1641117384000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022510X12001013"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,6]]},"references-count":50,"journal-issue":{"issue":"1-2","published-print":{"date-parts":[[2012,6]]}},"alternative-id":["S0022510X12001013"],"URL":"https:\/\/doi.org\/10.1016\/j.jns.2012.02.018","relation":{},"ISSN":["0022-510X"],"issn-type":[{"value":"0022-510X","type":"print"}],"subject":[],"published":{"date-parts":[[2012,6]]}}}