{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,28]],"date-time":"2026-07-28T02:45:23Z","timestamp":1785206723336,"version":"3.55.0"},"reference-count":43,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2010,3,1]],"date-time":"2010-03-01T00:00:00Z","timestamp":1267401600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,3,1]],"date-time":"2010-03-01T00:00:00Z","timestamp":1267401600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","metabolismjournal.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Metabolism"],"published-print":{"date-parts":[[2010,3]]},"DOI":"10.1016\/j.metabol.2009.07.028","type":"journal-article","created":{"date-parts":[[2009,9,30]],"date-time":"2009-09-30T04:57:35Z","timestamp":1254286655000},"page":"325-332","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":27,"title":["2-Deoxy-d-ribose induces cellular damage by increasing oxidative stress and protein glycation in a pancreatic \u03b2-cell line"],"prefix":"10.1016","volume":"59","author":[{"given":"Gwanpyo","family":"Koh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dae-Ho","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeong-taek","family":"Woo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.metabol.2009.07.028_bib1","doi-asserted-by":"crossref","first-page":"42351","DOI":"10.1074\/jbc.R400019200","article-title":"Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet beta cells in diabetes","volume":"279","author":"Robertson","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.metabol.2009.07.028_bib2","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.freeradbiomed.2005.04.030","article-title":"Diabetes, glucose toxicity, and oxidative stress: a case of double jeopardy for the pancreatic islet beta cell","volume":"41","author":"Robertson","year":"2006","journal-title":"Free Radic Biol Med"},{"key":"10.1016\/j.metabol.2009.07.028_bib3","doi-asserted-by":"crossref","first-page":"405","DOI":"10.2337\/diab.40.4.405","article-title":"Role of oxidative stress in development of complications in diabetes","volume":"40","author":"Baynes","year":"1991","journal-title":"Diabetes"},{"key":"10.1016\/j.metabol.2009.07.028_bib4","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1021\/jf60015a004","article-title":"Dehydrated foods: chemistry of browning reactions in model systems","volume":"1","author":"Hodge","year":"1953","journal-title":"Agric Food Chem"},{"key":"10.1016\/j.metabol.2009.07.028_bib5","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2337\/diabetes.48.1.1","article-title":"Role of oxidative stress in diabetic complications: a new perspective on an old paradigm","volume":"48","author":"Baynes","year":"1999","journal-title":"Diabetes"},{"key":"10.1016\/j.metabol.2009.07.028_bib6","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1038\/414813a","article-title":"Biochemistry and molecular cell biology of diabetic complications","volume":"414","author":"Brownlee","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.metabol.2009.07.028_bib7","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1196\/annals.1333.092","article-title":"Post-Amadori AGE inhibition as a therapeutic target for diabetic complications: a rational approach to second-generation Amadorin design","volume":"1043","author":"Khalifah","year":"2005","journal-title":"Ann N Y Acad Sci"},{"key":"10.1016\/j.metabol.2009.07.028_bib8","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/s000110050495","article-title":"Biological effects of aminoguanidine: an update","volume":"48","author":"Nilsson","year":"1999","journal-title":"Inflamm Res"},{"key":"10.1016\/j.metabol.2009.07.028_bib9","doi-asserted-by":"crossref","first-page":"1671","DOI":"10.1007\/s00018-005-5082-7","article-title":"Pyridoxamine as a multifunctional pharmaceutical: targeting pathogenic glycation and oxidative damage","volume":"62","author":"Voziyan","year":"2005","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.metabol.2009.07.028_bib10","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1042\/bj2450243","article-title":"Glucose autoxidation and protein modification. The potential role of \u2018autoxidative glycosylation\u2019 in diabetes","volume":"245","author":"Wolff","year":"1987","journal-title":"Biochem J"},{"key":"10.1016\/j.metabol.2009.07.028_bib11","doi-asserted-by":"crossref","first-page":"676","DOI":"10.2337\/diab.43.5.676","article-title":"Glycation, glycoxidation, and cross-linking of collagen by glucose. Kinetics, mechanisms, and inhibition of late stages of the Maillard reaction","volume":"43","author":"Fu","year":"1994","journal-title":"Diabetes"},{"key":"10.1016\/j.metabol.2009.07.028_bib12","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1126\/science.12192669","article-title":"Reaction of monosaccharides with proteins: possible evolutionary significance","volume":"213","author":"Bunn","year":"1981","journal-title":"Science"},{"key":"10.1016\/j.metabol.2009.07.028_bib13","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1172\/JCI118496","article-title":"Chronic exposure of betaTC-6 cells to supraphysiologic concentrations of glucose decreases binding of the RIPE3b1 insulin gene transcription activator","volume":"97","author":"Poitout","year":"1996","journal-title":"J Clin Invest"},{"key":"10.1016\/j.metabol.2009.07.028_bib14","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1172\/JCI119126","article-title":"Glycation-dependent, reactive oxygen species\u2013mediated suppression of the insulin gene promoter activity in HIT cells","volume":"99","author":"Matsuoka","year":"1997","journal-title":"J Clin Invest"},{"issue":"Pt 3","key":"10.1016\/j.metabol.2009.07.028_bib15","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1042\/bj3200855","article-title":"Reducing sugars trigger oxidative modification and apoptosis in pancreatic beta-cells by provoking oxidative stress through the glycation reaction","volume":"320","author":"Kaneto","year":"1996","journal-title":"Biochem J"},{"key":"10.1016\/j.metabol.2009.07.028_bib16","doi-asserted-by":"crossref","first-page":"B105","DOI":"10.1093\/geronj\/45.4.B105","article-title":"Nonenzymatic glycosylation, the Maillard reaction and the aging process","volume":"45","author":"Monnier","year":"1990","journal-title":"J Gerontol"},{"key":"10.1016\/j.metabol.2009.07.028_bib17","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.abb.2005.03.018","article-title":"Elevated cAMP level attenuates 2-deoxy-d-ribose-induced oxidative damage in pancreatic beta-cells","volume":"438","author":"Koh","year":"2005","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.metabol.2009.07.028_bib18","first-page":"936","article-title":"Evaluation of a tetrazolium-based semiautomated colorimetric assay: assessment of chemosensitivity testing","volume":"47","author":"Carmichael","year":"1987","journal-title":"Cancer Res"},{"key":"10.1016\/j.metabol.2009.07.028_bib19","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1182\/blood.V84.5.1415.bloodjournal8451415","article-title":"Annexin V for flow cytometric detection of phosphatidylserine expression on B cells undergoing apoptosis","volume":"84","author":"Koopman","year":"1994","journal-title":"Blood"},{"key":"10.1016\/j.metabol.2009.07.028_bib20","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0306-4522(01)00189-0","article-title":"Intracellular generation of free radicals and modifications of detoxifying enzymes in cultured neurons from the developing rat forebrain in response to transient hypoxia","volume":"105","author":"Lievre","year":"2001","journal-title":"Neuroscience"},{"key":"10.1016\/j.metabol.2009.07.028_bib21","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1073\/pnas.77.2.990","article-title":"Localization of mitochondria in living cells with rhodamine 123","volume":"77","author":"Johnson","year":"1980","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.metabol.2009.07.028_bib22","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/0076-6879(90)86141-H","article-title":"Determination of carbonyl content in oxidatively modified proteins","volume":"186","author":"Levine","year":"1990","journal-title":"Methods Enzymol"},{"key":"10.1016\/j.metabol.2009.07.028_bib23","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/0003-2697(77)90597-8","article-title":"The use of Girard-T reagent in a rapid and sensitive methods for measuring glyoxal and certain other alpha-dicarbonyl compounds","volume":"81","author":"Mitchel","year":"1977","journal-title":"Anal Biochem"},{"key":"10.1016\/j.metabol.2009.07.028_bib24","doi-asserted-by":"crossref","first-page":"3397","DOI":"10.1074\/jbc.M109935200","article-title":"A post-Amadori inhibitor pyridoxamine also inhibits chemical modification of proteins by scavenging carbonyl intermediates of carbohydrate and lipid degradation","volume":"277","author":"Voziyan","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.metabol.2009.07.028_bib25","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/S1471-4914(03)00031-5","article-title":"Protein carbonylation in human diseases","volume":"9","author":"Dalle-Donne","year":"2003","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.metabol.2009.07.028_bib26","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1172\/JCI115865","article-title":"Preservation of insulin mRNA levels and insulin secretion in HIT cells by avoidance of chronic exposure to high glucose concentrations","volume":"90","author":"Robertson","year":"1992","journal-title":"J Clin Invest"},{"key":"10.1016\/j.metabol.2009.07.028_bib27","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/S0006-291X(03)00310-3","article-title":"Gliclazide protects pancreatic beta-cells from damage by hydrogen peroxide","volume":"303","author":"Kimoto","year":"2003","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.metabol.2009.07.028_bib28","doi-asserted-by":"crossref","first-page":"1444","DOI":"10.1210\/en.2002-220897","article-title":"Glucagon-like peptide\u20131 inhibits apoptosis of insulin-secreting cells via a cyclic 5\u2032-adenosine monophosphate\u2013dependent protein kinase A\u2013 and a phosphatidylinositol 3-kinase\u2013dependent pathway","volume":"144","author":"Hui","year":"2003","journal-title":"Endocrinology"},{"key":"10.1016\/j.metabol.2009.07.028_bib29","doi-asserted-by":"crossref","first-page":"12363","DOI":"10.1073\/pnas.192445199","article-title":"A role for glutathione peroxidase in protecting pancreatic beta cells against oxidative stress in a model of glucose toxicity","volume":"99","author":"Tanaka","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.metabol.2009.07.028_bib30","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.metabol.2009.07.028_bib31","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1006\/bbrc.1999.0371","article-title":"Amadorins: novel post-Amadori inhibitors of advanced glycation reactions","volume":"257","author":"Khalifah","year":"1999","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.metabol.2009.07.028_bib32","doi-asserted-by":"crossref","first-page":"3620","DOI":"10.1016\/S0021-9258(17)43139-5","article-title":"Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site","volume":"259","author":"Graf","year":"1984","journal-title":"J Biol Chem"},{"key":"10.1016\/j.metabol.2009.07.028_bib33","doi-asserted-by":"crossref","first-page":"1297","DOI":"10.1016\/S1357-2725(99)00091-6","article-title":"Oxygen is not required for the browning and crosslinking of protein by pentoses: relevance to Maillard reactions in vivo","volume":"31","author":"Litchfield","year":"1999","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/j.metabol.2009.07.028_bib34","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.2337\/diabetes.47.7.1114","article-title":"Aminoguanidine inhibits reactive oxygen species formation, lipid peroxidation, and oxidant-induced apoptosis","volume":"47","author":"Giardino","year":"1998","journal-title":"Diabetes"},{"key":"10.1016\/j.metabol.2009.07.028_bib35","doi-asserted-by":"crossref","first-page":"7787","DOI":"10.1073\/pnas.91.16.7787","article-title":"Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress","volume":"91","author":"Yan","year":"1994","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.metabol.2009.07.028_bib36","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1681\/ASN.V781198","article-title":"Accumulation of albumin-linked and free-form pentosidine in the circulation of uremic patients with end-stage renal failure: renal implications in the pathophysiology of pentosidine","volume":"7","author":"Miyata","year":"1996","journal-title":"J Am Soc Nephrol"},{"key":"10.1016\/j.metabol.2009.07.028_bib37","doi-asserted-by":"crossref","first-page":"419","DOI":"10.3109\/07853899608999102","article-title":"Advanced glycation end-products and atherosclerosis","volume":"28","author":"Vlassara","year":"1996","journal-title":"Ann Med"},{"key":"10.1016\/j.metabol.2009.07.028_bib38","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1126\/science.6779377","article-title":"Nonenzymatic browning in vivo: possible process for aging of long-lived proteins","volume":"211","author":"Monnier","year":"1981","journal-title":"Science"},{"key":"10.1016\/j.metabol.2009.07.028_bib39","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.diabres.2004.09.004","article-title":"Advanced glycation end products\u2014role in pathology of diabetic complications","volume":"67","author":"Ahmed","year":"2005","journal-title":"Diabetes Res Clin Pract"},{"key":"10.1016\/j.metabol.2009.07.028_bib40","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1042\/bj2560205","article-title":"Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing","volume":"256","author":"Hunt","year":"1988","journal-title":"Biochem J"},{"key":"10.1016\/j.metabol.2009.07.028_bib41","doi-asserted-by":"crossref","first-page":"10017","DOI":"10.1074\/jbc.270.17.10017","article-title":"Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction","volume":"270","author":"Glomb","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/j.metabol.2009.07.028_bib42","doi-asserted-by":"crossref","first-page":"1820","DOI":"10.1271\/bbb.60.1820","article-title":"Effects of oxygen and transition metals on the advanced Maillard reaction of proteins with glucose","volume":"60","author":"Hayase","year":"1996","journal-title":"Biosci Biotechnol Biochem"},{"issue":"Pt 2","key":"10.1016\/j.metabol.2009.07.028_bib43","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1042\/bj2910529","article-title":"Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Some fundamental differences in proposed mechanisms of glucose oxidation and oxidant production","volume":"291","author":"Hunt","year":"1993","journal-title":"Biochem J"}],"container-title":["Metabolism"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0026049509003199?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0026049509003199?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,21]],"date-time":"2025-09-21T03:48:20Z","timestamp":1758426500000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0026049509003199"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,3]]},"references-count":43,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2010,3]]}},"alternative-id":["S0026049509003199"],"URL":"https:\/\/doi.org\/10.1016\/j.metabol.2009.07.028","relation":{},"ISSN":["0026-0495"],"issn-type":[{"value":"0026-0495","type":"print"}],"subject":[],"published":{"date-parts":[[2010,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"2-Deoxy-d-ribose induces cellular damage by increasing oxidative stress and protein glycation in a pancreatic \u03b2-cell line","name":"articletitle","label":"Article Title"},{"value":"Metabolism","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.metabol.2009.07.028","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}