{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,31]],"date-time":"2026-10-31T04:12:47Z","timestamp":1793419967098,"version":"4.5.0"},"reference-count":182,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,6,1]],"date-time":"2015-06-01T00:00:00Z","timestamp":1433116800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"name":"National Institute of Health","award":["HL55477"],"award-info":[{"award-number":["HL55477"]}]},{"name":"National Institute of Health","award":["HL59378"],"award-info":[{"award-number":["HL59378"]}]},{"name":"National Institute of Health","award":["HL65660"],"award-info":[{"award-number":["HL65660"]}]},{"name":"National Institute of Health","award":["HL78825"],"award-info":[{"award-number":["HL78825"]}]},{"name":"National Institute of Health","award":["GM103492"],"award-info":[{"award-number":["GM103492"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2015,6]]},"DOI":"10.1016\/j.cbi.2014.12.028","type":"journal-article","created":{"date-parts":[[2015,1,2]],"date-time":"2015-01-02T01:45:38Z","timestamp":1420163138000},"page":"261-273","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":146,"special_numbering":"C","title":["Oxidative and reductive metabolism of lipid-peroxidation derived carbonyls"],"prefix":"10.1016","volume":"234","author":[{"given":"Mahavir","family":"Singh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aniruddh","family":"Kapoor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aruni","family":"Bhatnagar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2014.12.028_b0005","doi-asserted-by":"crossref","first-page":"936486","DOI":"10.1155\/2012\/936486","article-title":"Reactive oxygen species in health and disease","volume":"2012","author":"Alfadda","year":"2012","journal-title":"J. Biomed. Biotechnol."},{"key":"10.1016\/j.cbi.2014.12.028_b0010","first-page":"1240","article-title":"Oxidative stress and mitochondrial dysfunction in Alzheimer\u2019s disease","volume":"2014","author":"Wang","year":"1842","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2014.12.028_b0015","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0891-5849(91)90192-6","article-title":"Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes","volume":"11","author":"Esterbauer","year":"1991","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0020","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1172\/JCI200318022","article-title":"Endogenous generation of reactive oxidants and electrophiles and their reactions with DNA and protein","volume":"111","author":"Marnett","year":"2003","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.cbi.2014.12.028_b0025","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1021\/tx700235t","article-title":"Protein damage by reactive electrophiles: targets and consequences","volume":"21","author":"Liebler","year":"2008","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0030","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF02536034","article-title":"Mechanisms of free radical oxidation of unsaturated lipids","volume":"30","author":"Porter","year":"1995","journal-title":"Lipids"},{"key":"10.1016\/j.cbi.2014.12.028_b0035","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/j.freeradbiomed.2009.05.032","article-title":"Lipid peroxidation: physiological levels and dual biological effects","volume":"47","author":"Niki","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0040","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S0022-2275(20)38899-4","article-title":"Autoxidation of polyunsaturated esters in water: chemical structure and biological activity of the products","volume":"8","author":"Schauenstein","year":"1967","journal-title":"J. Lipid Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0045","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0378-4347(00)82957-6","article-title":"Determination of the lipid peroxidation product trans-4-hydroxy-2-nonenal in biological samples by high-performance liquid chromatography and combined capillary column gas chromatography\u2013negative-ion chemical ionisation mass spectrometry","volume":"488","author":"Selley","year":"1989","journal-title":"J. Chromatogr."},{"key":"10.1016\/j.cbi.2014.12.028_b0050","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1080\/10715760600592962","article-title":"Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes","volume":"40","author":"Gil","year":"2006","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0055","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0378-4347(96)00446-X","article-title":"Determination of the lipid peroxidation product (E)-4-hydroxy-2-nonenal in clinical samples by gas chromatography\u2013negative-ion chemical ionisation mass spectrometry of the O-pentafluorobenzyl oxime","volume":"691","author":"Selley","year":"1997","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"10.1016\/j.cbi.2014.12.028_b0060","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1002\/(SICI)1097-4652(199911)181:2<295::AID-JCP11>3.0.CO;2-I","article-title":"4-Hydroxynonenal induces dysfunction and apoptosis of cultured endothelial cells","volume":"181","author":"Herbst","year":"1999","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.cbi.2014.12.028_b0065","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1080\/10715760802691455","article-title":"Elevated oxidative stress, iron accumulation around microvessels and increased 4-hydroxynonenal immunostaining in zone 1 of the liver acinus in hypercholesterolemic rabbits","volume":"43","author":"Ong","year":"2009","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0070","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1161\/01.ATV.9.4.538","article-title":"Modification of low density lipoprotein with 4-hydroxynonenal induces uptake by macrophages","volume":"9","author":"Hoff","year":"1989","journal-title":"Arteriosclerosis"},{"key":"10.1016\/j.cbi.2014.12.028_b0075","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1021\/tx000007u","article-title":"HNE-derived 2-pentylpyrroles are generated during oxidation of LDL, are more prevalent in blood plasma from patients with renal disease or atherosclerosis, and are present in atherosclerotic plaques","volume":"13","author":"Salomon","year":"2000","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0080","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1161\/CIRCRESAHA.109.200568","article-title":"Aldose reductase protects against early atherosclerotic lesion formation in apolipoprotein E-null mice","volume":"105","author":"Srivastava","year":"2009","journal-title":"Circ. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0085","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1021\/tx600295j","article-title":"Long-lived 4-oxo-2-enal-derived apparent lysine michael adducts are actually the isomeric 4-ketoamides","volume":"20","author":"Zhu","year":"2007","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0090","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1179\/135100007X162176","article-title":"Mass spectrometric evidence for long-lived protein adducts of 4-oxo-2-nonenal","volume":"12","author":"Zhu","year":"2007","journal-title":"Redox Rep."},{"key":"10.1016\/j.cbi.2014.12.028_b0095","doi-asserted-by":"crossref","first-page":"11864","DOI":"10.1021\/ja503604t","article-title":"Stable histone adduction by 4-oxo-2-nonenal: a potential link between oxidative stress and epigenetics","volume":"136","author":"Galligan","year":"2014","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2014.12.028_b0100","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1021\/tx980003d","article-title":"Structural characterization of a 4-hydroxy-2-alkenal-derived fluorophore that contributes to lipoperoxidation-dependent protein cross-linking in aging and degenerative disease","volume":"11","author":"Xu","year":"1998","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0105","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1021\/tx020105a","article-title":"Model studies on protein side chain modification by 4-oxo-2-nonenal","volume":"16","author":"Zhang","year":"2003","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0110","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1021\/tx0300030","article-title":"Mass spectroscopic characterization of protein modification by 4-hydroxy-2-(E)-nonenal and 4-oxo-2-(E)-nonenal","volume":"16","author":"Liu","year":"2003","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0115","doi-asserted-by":"crossref","first-page":"42098","DOI":"10.1074\/jbc.M308167200","article-title":"A novel lipid hydroperoxide-derived cyclic covalent modification to histone H4","volume":"278","author":"Oe","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0120","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1002\/jms.847","article-title":"Novel lipid hydroperoxide-derived hemoglobin histidine adducts as biomarkers of oxidative stress","volume":"40","author":"Yocum","year":"2005","journal-title":"J. Mass Spectrom."},{"key":"10.1016\/j.cbi.2014.12.028_b0125","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1021\/tx050080q","article-title":"4-Oxo-2-nonenal is both more neurotoxic and more protein reactive than 4-hydroxy-2-nonenal","volume":"18","author":"Lin","year":"2005","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0130","doi-asserted-by":"crossref","first-page":"19943","DOI":"10.1074\/jbc.M110.187047","article-title":"Lipid peroxidation modification of protein generates Nepsilon-(4-oxononanoyl)lysine as a pro-inflammatory ligand","volume":"286","author":"Shibata","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0135","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/S1388-1981(01)00100-7","article-title":"Aldehydic lipid peroxidation products derived from linoleic acid","volume":"1531","author":"Spiteller","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2014.12.028_b0140","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1021\/tx000101a","article-title":"Characterization of 4-oxo-2-nonenal as a novel product of lipid peroxidation","volume":"13","author":"Lee","year":"2000","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0145","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1021\/tx030009p","article-title":"Characterization of 2\u2032-deoxycytidine adducts derived from 4-oxo-2-nonenal, a novel lipid peroxidation product","volume":"16","author":"Pollack","year":"2003","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0150","doi-asserted-by":"crossref","first-page":"10127","DOI":"10.1074\/jbc.M600178200","article-title":"Endogenous lipid hydroperoxide-mediated DNA-adduct formation in min mice","volume":"281","author":"Williams","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0155","first-page":"95","article-title":"Fate and effects of acrolein","volume":"144","author":"Ghilarducci","year":"1995","journal-title":"Rev. Environ. Contam. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0160","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1172\/JCI119176","volume":"99","author":"Anderson","year":"1997","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.cbi.2014.12.028_b0165","doi-asserted-by":"crossref","first-page":"4882","DOI":"10.1073\/pnas.95.9.4882","article-title":"Protein-bound acrolein: potential markers for oxidative stress","volume":"95","author":"Uchida","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cbi.2014.12.028_b0170","series-title":"Toxicological Review of Acrolein (Cas No. 107-02-08) in Support of Summary Information on the Integrated Risk Information System (Iris)","author":"De Woskin","year":"2003"},{"key":"10.1016\/j.cbi.2014.12.028_b0175","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1196\/annals.1333.046","article-title":"Acrolein modifies apolipoprotein A\u2013I in the human artery wall","volume":"1043","author":"Shao","year":"2005","journal-title":"Ann. NY. Acad. Sci."},{"key":"10.1016\/j.cbi.2014.12.028_b0180","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.atherosclerosis.2012.12.020","article-title":"Acrolein-conjugated low-density lipoprotein induces macrophage foam cell formation","volume":"227","author":"Watanabe","year":"2013","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.cbi.2014.12.028_b0185","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1016\/j.freeradbiomed.2010.08.001","article-title":"Malondialdehyde\u2013acetaldehyde adduct is the dominant epitope after MDA modification of proteins in atherosclerosis","volume":"49","author":"Duryee","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0190","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1016\/j.jacc.2011.07.017","article-title":"Human oxidation-specific antibodies reduce foam cell formation and atherosclerosis progression","volume":"58","author":"Tsimikas","year":"2011","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.cbi.2014.12.028_b0195","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1016\/j.atherosclerosis.2012.08.006","article-title":"The levels of MDA\u2013LDL in circulating immune complexes predict myocardial infarction in the VADT study","volume":"224","author":"Lopes-Virella","year":"2012","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.cbi.2014.12.028_b0200","doi-asserted-by":"crossref","first-page":"1955","DOI":"10.1161\/01.CIR.103.15.1955","article-title":"Elevated levels of oxidized low density lipoprotein show a positive relationship with the severity of acute coronary syndromes","volume":"103","author":"Ehara","year":"2001","journal-title":"Circulation"},{"key":"10.1016\/j.cbi.2014.12.028_b0205","doi-asserted-by":"crossref","first-page":"24787","DOI":"10.1074\/jbc.274.35.24787","article-title":"Structural identification of a novel pro-inflammatory epoxyisoprostane phospholipid in mildly oxidized low density lipoprotein","volume":"274","author":"Watson","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0210","doi-asserted-by":"crossref","first-page":"2248","DOI":"10.1161\/01.ATV.20.10.2248","article-title":"Determinants of bioactivity of oxidized phospholipids. Specific oxidized fatty acyl groups at the sn-2 position","volume":"20","author":"Subbanagounder","year":"2000","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.cbi.2014.12.028_b0215","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1056\/NEJMoa043175","article-title":"Oxidized phospholipids, Lp(a) lipoprotein, and coronary artery disease","volume":"353","author":"Tsimikas","year":"2005","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0220","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1056\/NEJMp058118","article-title":"A role for oxidized phospholipids in atherosclerosis","volume":"353","author":"Berliner","year":"2005","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0225","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1146\/annurev.pharmtox.47.120505.105337","article-title":"Aldo\u2013keto reductases and bioactivation\/detoxication","volume":"47","author":"Jin","year":"2007","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.cbi.2014.12.028_b0230","doi-asserted-by":"crossref","first-page":"2517","DOI":"10.1073\/pnas.91.7.2517","article-title":"Three-dimensional structure of rat liver 3 alpha-hydroxysteroid\/dihydrodiol dehydrogenase: a member of the aldo\u2013keto reductase superfamily","volume":"91","author":"Hoog","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cbi.2014.12.028_b0235","doi-asserted-by":"crossref","first-page":"9547","DOI":"10.1016\/S0021-9258(18)60566-6","article-title":"The aldo\u2013keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases","volume":"264","author":"Bohren","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0240","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1159\/000015265","article-title":"The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33\u2192p32","volume":"84","author":"Fujii","year":"1999","journal-title":"Cytogenet. Cell Genet."},{"key":"10.1016\/j.cbi.2014.12.028_b0245","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1006\/geno.1999.5915","article-title":"Characterization of the human aldehyde reductase gene and promoter","volume":"60","author":"Barski","year":"1999","journal-title":"Genomics"},{"key":"10.1016\/j.cbi.2014.12.028_b0250","doi-asserted-by":"crossref","first-page":"1480","DOI":"10.1124\/dmd.113.051904","article-title":"Tissue distribution, ontogeny, and chemical induction of aldo\u2013keto reductases in mice","volume":"41","author":"Pratt-Hyatt","year":"2013","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.cbi.2014.12.028_b0255","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1128\/jb.100.1.110-116.1969","article-title":"Identification of reduced nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase in a Rhodotorula strain","volume":"100","author":"Watson","year":"1969","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.cbi.2014.12.028_b0260","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1042\/bj1390205","article-title":"Some properties and a suggested reclassification of mevaldate reductase","volume":"139","author":"Beedle","year":"1974","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0265","doi-asserted-by":"crossref","first-page":"19510","DOI":"10.1074\/jbc.M110.110247","article-title":"Ascorbate synthesis pathway: dual role of ascorbate in bone homeostasis","volume":"285","author":"Gabbay","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0270","first-page":"1787","article-title":"In vivo role of aldehyde reductase","volume":"2012","author":"Takahashi","year":"1820","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2014.12.028_b0275","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbrc.2014.08.072","article-title":"Reductive detoxification of acrolein as a potential role for aldehyde reductase (AKR1A) in mammals","author":"Kurahashi","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.cbi.2014.12.028_b0280","first-page":"273","article-title":"Effect of AKR1A1 knock-down on H2; O2; and 4-hydroxynonenal-induced cytotoxicity in human 1321N1 astrocytoma cells","volume":"29","author":"Li","year":"2013","journal-title":"Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi"},{"key":"10.1016\/j.cbi.2014.12.028_b0285","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1007\/978-1-4615-2904-0_27","article-title":"The aldo\u2013keto reductases: an overview","volume":"328","author":"Flynn","year":"1993","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.cbi.2014.12.028_b0290","doi-asserted-by":"crossref","first-page":"20764","DOI":"10.1073\/pnas.0705659105","article-title":"Structural basis for the high all-trans-retinaldehyde reductase activity of the tumor marker AKR1B10","volume":"104","author":"Gallego","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cbi.2014.12.028_b0295","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1007\/s00018-003-3402-3","article-title":"All in the family: aldose reductase and closely related aldo\u2013keto reductases","volume":"61","author":"Petrash","year":"2004","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.cbi.2014.12.028_b0300","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1007\/978-1-4615-4735-8_54","article-title":"Structure-function studies of FR-1. A growth factor-inducible aldo\u2013keto reductase","volume":"463","author":"Petrash","year":"1999","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.cbi.2014.12.028_b0305","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/0304-4165(85)90213-2","article-title":"Interrelationships among human aldo\u2013keto reductases: immunochemical, kinetic and structural properties","volume":"840","author":"Srivastava","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2014.12.028_b0310","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1021\/bi981794l","article-title":"Structural and kinetic determinants of aldehyde reduction by aldose reductase","volume":"38","author":"Srivastava","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2014.12.028_b0315","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1006\/bbrc.1995.2835","article-title":"Lipid peroxidation product, 4-hydroxynonenal and its conjugate with GSH are excellent substrates of bovine lens aldose reductase","volume":"217","author":"Srivastava","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.cbi.2014.12.028_b0320","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/S0021-9150(01)00454-3","article-title":"Identification of biochemical pathways for the metabolism of oxidized low-density lipoprotein derived aldehyde-4-hydroxy trans-2-nonenal in vascular smooth muscle cells","volume":"158","author":"Srivastava","year":"2001","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.cbi.2014.12.028_b0325","doi-asserted-by":"crossref","first-page":"53395","DOI":"10.1074\/jbc.M403416200","article-title":"Aldose reductase-catalyzed reduction of aldehyde phospholipids","volume":"279","author":"Srivastava","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0330","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1042\/BJ20061743","article-title":"Substrate specificity and catalytic efficiency of aldo\u2013keto reductases with phospholipid aldehydes","volume":"405","author":"Spite","year":"2007","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0335","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1172\/JCI4711","article-title":"Aldose reductase functions as a detoxification system for lipid peroxidation products in vasculitis","volume":"103","author":"Rittner","year":"1999","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.cbi.2014.12.028_b0340","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0167-5273(97)00085-5","article-title":"Platelet aggregability and occurrence of restenosis following coronary angioplasty","volume":"60","author":"Goel","year":"1997","journal-title":"Int. J. Cardiol."},{"key":"10.1016\/j.cbi.2014.12.028_b0345","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1161\/01.ATV.20.7.1745","article-title":"Involvement of aldose reductase in vascular smooth muscle cell growth and lesion formation after arterial injury","volume":"20","author":"Ruef","year":"2000","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.cbi.2014.12.028_b0350","doi-asserted-by":"crossref","first-page":"17652","DOI":"10.1074\/jbc.M600270200","article-title":"Mitogenic responses of vascular smooth muscle cells to lipid peroxidation-derived aldehyde 4-hydroxy-trans-2-nonenal (HNE): role of aldose reductase-catalyzed reduction of the HNE-glutathione conjugates in regulating cell growth","volume":"281","author":"Ramana","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0355","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1530\/jrf.0.0830835","article-title":"Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens","volume":"83","author":"Taragnat","year":"1988","journal-title":"J. Reprod. Fertil."},{"issue":"Pt. 2","key":"10.1016\/j.cbi.2014.12.028_b0360","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1042\/bj3120609","article-title":"Tissue-specific expression of two aldose reductase-like genes in mice: abundant expression of mouse vas deferens protein and fibroblast growth factor-regulated protein in the adrenal gland","volume":"312","author":"Lau","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0365","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1677\/joe.0.1600147","article-title":"Cyclic AMP regulates expression of the gene coding for a mouse vas deferens protein related to the aldo\u2013keto reductase superfamily in human and murine adrenocortical cells","volume":"160","author":"Aigueperse","year":"1999","journal-title":"J. Endocrinol."},{"key":"10.1016\/j.cbi.2014.12.028_b0370","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1530\/REP-07-0022","article-title":"AKR1B7 (mouse vas deferens protein) is dispensable for mouse development and reproductive success","volume":"134","author":"Baumann","year":"2007","journal-title":"Reproduction"},{"key":"10.1016\/j.cbi.2014.12.028_b0375","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1111\/and.12018","article-title":"Identification of a role for a mouse sperm surface aldo\u2013keto reductase (AKR1B7) and its human analogue in the detoxification of the reactive aldehyde, acrolein","volume":"45","author":"Jagoe","year":"2013","journal-title":"Andrologia"},{"key":"10.1016\/j.cbi.2014.12.028_b0380","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1016\/S0009-2797(00)00244-1","article-title":"Physiological functions and hormonal regulation of mouse vas deferens protein (AKR1B7) in steroidogenic tissues","volume":"130\u2013132","author":"Martinez","year":"2001","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0385","doi-asserted-by":"crossref","first-page":"1996","DOI":"10.1210\/en.2006-1707","article-title":"A novel inhibitory protein in adipose tissue, the aldo\u2013keto reductase AKR1B7: its role in adipogenesis","volume":"148","author":"Tirard","year":"2007","journal-title":"Endocrinology"},{"key":"10.1016\/j.cbi.2014.12.028_b0390","doi-asserted-by":"crossref","first-page":"5704","DOI":"10.1210\/en.2004-0552","article-title":"Activation of the glucocorticoid receptor or liver X receptors interferes with growth hormone-induced akr1b7 gene expression in rat hepatocytes","volume":"145","author":"Kotokorpi","year":"2004","journal-title":"Endocrinology"},{"key":"10.1016\/j.cbi.2014.12.028_b0395","doi-asserted-by":"crossref","first-page":"1886","DOI":"10.1248\/bpb.33.1886","article-title":"Rat aldose reductase-like protein (AKR1B14) efficiently reduces the lipid peroxidation product 4-oxo-2-nonenal","volume":"33","author":"Endo","year":"2010","journal-title":"Biol. Pharm. Bull."},{"key":"10.1016\/j.cbi.2014.12.028_b0400","doi-asserted-by":"crossref","first-page":"148","DOI":"10.3389\/fphar.2012.00148","article-title":"Aldo\u2013keto reductases 1B in endocrinology and metabolism","volume":"3","author":"Pastel","year":"2012","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.cbi.2014.12.028_b0405","doi-asserted-by":"crossref","first-page":"8604","DOI":"10.1016\/S0021-9258(17)37237-X","article-title":"A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase","volume":"269","author":"Donohue","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0410","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1515\/bc.2010.144","article-title":"Murine aldo\u2013keto reductase family 1 subfamily B: identification of AKR1B8 as an ortholog of human AKR1B10","volume":"391","author":"Joshi","year":"2010","journal-title":"Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0415","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.cbi.2011.02.004","article-title":"Human aldo\u2013keto reductases 1B1 and 1B10: a comparative study on their enzyme activity toward electrophilic carbonyl compounds","volume":"191","author":"Shen","year":"2011","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0420","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.cbi.2008.10.021","article-title":"Role of human aldo\u2013keto-reductase AKR1B10 in the protection against toxic aldehydes","volume":"178","author":"Martin","year":"2009","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0425","doi-asserted-by":"crossref","first-page":"2890","DOI":"10.1074\/jbc.M006655200","article-title":"The reactive oxygen species- and michael acceptor-inducible human aldo\u2013keto reductase AKR1C1 reduces the \u03b1, \u03b2-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene","volume":"276","author":"Burczynski","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0430","doi-asserted-by":"crossref","first-page":"20162","DOI":"10.1074\/jbc.270.34.20162","article-title":"Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases","volume":"270","author":"Khanna","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0435","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1093\/oxfordjournals.jbchem.a022211","article-title":"Identification of a principal mRNA species for human 3alpha-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity","volume":"124","author":"Matsuura","year":"1998","journal-title":"J. Biochem."},{"key":"10.1016\/j.cbi.2014.12.028_b0440","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1746-1596-9-42","article-title":"AKR1C3 overexpression may serve as a promising biomarker for prostate cancer progression","volume":"9","author":"Tian","year":"2014","journal-title":"Diagn. Pathol."},{"key":"10.1016\/j.cbi.2014.12.028_b0445","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.neuint.2012.10.007","article-title":"Aldo\u2013keto reductases mediate constitutive and inducible protection against aldehyde toxicity in human neuroblastoma SH-SY5Y cells","volume":"62","author":"Lyon","year":"2013","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.cbi.2014.12.028_b0450","doi-asserted-by":"crossref","first-page":"35095","DOI":"10.1074\/jbc.273.52.35095","article-title":"Coexpression of the KCNA3B gene product with Kv1.5 leads to a novel A-type potassium channel","volume":"273","author":"Leicher","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0455","article-title":"The aldo\u2013keto reductases (AKRs): overview","author":"Penning","year":"2014","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0460","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.bbrc.2007.05.102","article-title":"NADPH binding to beta-subunit regulates inactivation of voltage-gated K(+) channels","volume":"359","author":"Tipparaju","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.cbi.2014.12.028_b0465","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1007\/s00424-012-1093-z","article-title":"Interactions between the C-terminus of Kv1.5 and Kvbeta regulate pyridine nucleotide-dependent changes in channel gating","volume":"463","author":"Tipparaju","year":"2012","journal-title":"Pflugers Arch."},{"key":"10.1016\/j.cbi.2014.12.028_b0470","doi-asserted-by":"crossref","first-page":"8840","DOI":"10.1021\/bi800301b","article-title":"Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel","volume":"47","author":"Tipparaju","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2014.12.028_b0475","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.cbi.2011.01.032","article-title":"Catalytic reduction of carbonyl groups in oxidized PAPC by Kvbeta2 (AKR6)","volume":"191","author":"Xie","year":"2011","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0480","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.cbi.2008.10.016","article-title":"Kinetics of nucleotide binding to the beta-subunit (AKR6A2) of the voltage-gated potassium (Kv) channel","volume":"178","author":"Barski","year":"2009","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0485","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0009-2797(02)00173-4","article-title":"Substrate specificity of mouse aldo\u2013keto reductase AKR7A5","volume":"143\u2013144","author":"Hinshelwood","year":"2003","journal-title":"Chem. Biol. Interact."},{"issue":"Pt 1","key":"10.1016\/j.cbi.2014.12.028_b0490","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1042\/bj3320021","article-title":"Molecular cloning, expression and catalytic activity of a human AKR7 member of the aldo\u2013keto reductase superfamily: evidence that the major 2-carboxybenzaldehyde reductase from human liver is a homologue of rat aflatoxin B1-aldehyde reductase","volume":"332","author":"Ireland","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0495","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1093\/carcin\/20.7.1215","article-title":"CDNA cloning, expression and activity of a second human aflatoxin B1-metabolizing member of the aldo\u2013keto reductase superfamily, AKR7A3","volume":"20","author":"Knight","year":"1999","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.cbi.2014.12.028_b0500","first-page":"957","article-title":"Chemoprevention of aflatoxin B1 hepatocarcinogenesis by coumarin, a natural benzopyrone that is a potent inducer of aflatoxin B1-aldehyde reductase, the glutathione S-transferase A5 and P1 subunits, and NAD(P)H:quinone oxidoreductase in rat liver","volume":"60","author":"Kelly","year":"2000","journal-title":"Cancer Res."},{"issue":"Pt. 2","key":"10.1016\/j.cbi.2014.12.028_b0505","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1042\/bj3480389","article-title":"Purification from rat liver of a novel constitutively expressed member of the aldo\u2013keto reductase 7 family that is widely distributed in extrahepatic tissues","volume":"348","author":"Kelly","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0510","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0014-5793(02)02982-4","article-title":"Characterisation of a novel mouse liver aldo\u2013keto reductase AKR7A5","volume":"523","author":"Hinshelwood","year":"2002","journal-title":"FEBS Lett."},{"issue":"Pt 2","key":"10.1016\/j.cbi.2014.12.028_b0515","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1042\/bj3120535","article-title":"Substrate specificity of an aflatoxin-metabolizing aldehyde reductase","volume":"312","author":"Ellis","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0520","first-page":"3887","article-title":"Resistance to aflatoxin B1 is associated with the expression of a novel aldo\u2013keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin","volume":"53","author":"Hayes","year":"1993","journal-title":"Cancer Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0525","doi-asserted-by":"crossref","first-page":"10350","DOI":"10.1073\/pnas.90.21.10350","article-title":"An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin B1 defines a subfamily of aldo\u2013keto reductases","volume":"90","author":"Ellis","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cbi.2014.12.028_b0530","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.toxlet.2003.12.056","article-title":"Detoxication of the environmental pollutant acrolein by a rat liver aldo\u2013keto reductase","volume":"148","author":"Gardner","year":"2004","journal-title":"Toxicol. Lett."},{"key":"10.1016\/j.cbi.2014.12.028_b0535","doi-asserted-by":"crossref","first-page":"25986","DOI":"10.1074\/jbc.M702465200","article-title":"Synthesis and catabolism of gamma-hydroxybutyrate in SH-SY5Y human neuroblastoma cells: role of the aldo\u2013keto reductase AKR7A2","volume":"282","author":"Lyon","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"Pt. 2","key":"10.1016\/j.cbi.2014.12.028_b0540","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1042\/bj3430487","article-title":"Major differences exist in the function and tissue-specific expression of human aflatoxin B1 aldehyde reductase and the principal human aldo\u2013keto reductase AKR1 family members","volume":"343","author":"O\u2019Connor","year":"1999","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0545","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0006-8993(01)02897-9","article-title":"Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease","volume":"916","author":"Picklo","year":"2001","journal-title":"Brain Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0550","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.1016\/j.neuro.2012.08.015","article-title":"Inducible protection of human astrocytoma 1321N1 cells against hydrogen peroxide and aldehyde toxicity by 7-hydroxycoumarin is associated with the upregulation of aldo\u2013keto reductases","volume":"33","author":"Li","year":"2012","journal-title":"Neurotoxicology"},{"key":"10.1016\/j.cbi.2014.12.028_b0555","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cbi.2011.09.007","article-title":"Human aldo\u2013keto reductase AKR7A2 protects against the cytotoxicity and mutagenicity of reactive aldehydes and lowers intracellular reactive oxygen species in hamster V79-4 cells","volume":"195","author":"Li","year":"2012","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0560","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.tox.2006.06.013","article-title":"Mouse aldo\u2013keto reductase AKR7A5 protects V79 cells against 4-hydroxynonenal-induced apoptosis","volume":"226","author":"Li","year":"2006","journal-title":"Toxicology"},{"key":"10.1016\/j.cbi.2014.12.028_b0565","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.tiv.2014.02.010","article-title":"Aldo\u2013keto reductase 7A5 (AKR7A5) attenuates oxidative stress and reactive aldehyde toxicity in V79-4 cells","volume":"28","author":"Li","year":"2014","journal-title":"Toxicol. In Vitro"},{"key":"10.1016\/j.cbi.2014.12.028_b0570","first-page":"421","article-title":"Eukaryotic aldehyde dehydrogenase (ALDH) genes: human polymorphisms, and recommended nomenclature based on divergent evolution and chromosomal mapping","volume":"9","author":"Vasiliou","year":"1999","journal-title":"Pharmacogenetics"},{"issue":"2003","key":"10.1016\/j.cbi.2014.12.028_b0575","first-page":"5","article-title":"Aldehyde dehydrogenase gene superfamily: the 2002 update","volume":"143\u2013144","author":"Sophos","year":"2002","journal-title":"Chem. Biol. Interact."},{"issue":"2001","key":"10.1016\/j.cbi.2014.12.028_b0580","first-page":"323","article-title":"Aldehyde dehydrogenase gene superfamily: the 2000 update","volume":"130\u2013132","author":"Sophos","year":"2000","journal-title":"Chem. Biol. Interact."},{"issue":"1999","key":"10.1016\/j.cbi.2014.12.028_b0585","first-page":"255","article-title":"Aldehyde dehydrogenase gene superfamily. The 1998 update","volume":"463","author":"Ziegler","year":"1998","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.cbi.2014.12.028_b0590","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1081\/DMR-120034001","article-title":"Role of human aldehyde dehydrogenases in endobiotic and xenobiotic metabolism","volume":"36","author":"Vasiliou","year":"2004","journal-title":"Drug Metab. Rev."},{"key":"10.1016\/j.cbi.2014.12.028_b0595","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.stem.2007.08.014","article-title":"ALDH1 is a marker of normal and malignant human mammary stem cells and a predictor of poor clinical outcome","volume":"1","author":"Ginestier","year":"2007","journal-title":"Cell Stem Cell"},{"key":"10.1016\/j.cbi.2014.12.028_b0600","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1158\/1078-0432.CCR-09-1630","article-title":"Aldehyde dehydrogenase 1-positive cancer stem cells mediate metastasis and poor clinical outcome in inflammatory breast cancer","volume":"16","author":"Charafe-Jauffret","year":"2010","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0605","doi-asserted-by":"crossref","first-page":"e10277","DOI":"10.1371\/journal.pone.0010277","article-title":"Distinct expression levels and patterns of stem cell marker, aldehyde dehydrogenase isoform 1 (ALDH1), in human epithelial cancers","volume":"5","author":"Deng","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2014.12.028_b0610","doi-asserted-by":"crossref","first-page":"3186","DOI":"10.1158\/1535-7163.MCT-10-0563","article-title":"Targeting aldehyde dehydrogenase cancer stem cells in ovarian cancer","volume":"9","author":"Landen","year":"2010","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.cbi.2014.12.028_b0615","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1002\/(SICI)1097-010X(199809\/10)282:1\/2<12::AID-JEZ4>3.0.CO;2-Q","article-title":"Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens","volume":"282","author":"King","year":"1998","journal-title":"J. Exp. Zool."},{"key":"10.1016\/j.cbi.2014.12.028_b0620","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1167\/iovs.04-0120","article-title":"Role of aldehyde dehydrogenase isozymes in the defense of rat lens and human lens epithelial cells against oxidative stress","volume":"46","author":"Choudhary","year":"2005","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.cbi.2014.12.028_b0625","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1080\/15287390802706371","article-title":"Molecular cloning and oxidative modification of human lens ALDH1A1: implication in impaired detoxification of lipid aldehydes","volume":"72","author":"Xiao","year":"2009","journal-title":"J. Toxicol. Environ. Health A"},{"key":"10.1016\/j.cbi.2014.12.028_b0630","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1158\/1541-7786.MCR-08-0393","article-title":"Aldehyde dehydrogenase 1 is a tumor stem cell-associated marker in lung cancer","volume":"7","author":"Jiang","year":"2009","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0635","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1038\/modpathol.2009.35","article-title":"ALDH1 expression correlates with favorable prognosis in ovarian cancers","volume":"22","author":"Chang","year":"2009","journal-title":"Mod. Pathol."},{"key":"10.1016\/j.cbi.2014.12.028_b0640","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1093\/jnci\/djp535","article-title":"Prognostic significance of tumorigenic cells with mesenchymal features in pancreatic adenocarcinoma","volume":"102","author":"Rasheed","year":"2010","journal-title":"J. Natl Cancer Inst."},{"key":"10.1016\/j.cbi.2014.12.028_b0645","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1158\/1055-9965.EPI-09-0865","article-title":"Aldehyde dehydrogenase 1 A1-positive cell population is enriched in tumor-initiating cells and associated with progression of bladder cancer","volume":"19","author":"Su","year":"2010","journal-title":"Cancer Epidemiol. Biomarkers Prev."},{"key":"10.1016\/j.cbi.2014.12.028_b0650","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1038\/labinvest.2009.127","article-title":"ALDH1A1 is a marker for malignant prostate stem cells and predictor of prostate cancer patients\u2019 outcome","volume":"90","author":"Li","year":"2010","journal-title":"Lab. Invest."},{"key":"10.1016\/j.cbi.2014.12.028_b0655","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.cbi.2011.10.007","article-title":"The enzymatic activity of human aldehyde dehydrogenases 1A2 and 2 (ALDH1A2 and ALDH2) is detected by Aldefluor, inhibited by diethylaminobenzaldehyde and has significant effects on cell proliferation and drug resistance","volume":"195","author":"Moreb","year":"2012","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0660","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/s00280-001-0412-4","volume":"49","author":"Sladek","year":"2002","journal-title":"Cancer Chemother. Pharmacol."},{"key":"10.1016\/j.cbi.2014.12.028_b0665","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1111\/j.1530-0277.2000.tb02068.x","article-title":"High salivary acetaldehyde after a moderate dose of alcohol in ALDH2-deficient subjects: strong evidence for the local carcinogenic action of acetaldehyde","volume":"24","author":"Vakevainen","year":"2000","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0670","doi-asserted-by":"crossref","first-page":"6239","DOI":"10.1523\/JNEUROSCI.4956-07.2008","article-title":"Age-dependent neurodegeneration accompanying memory loss in transgenic mice defective in mitochondrial aldehyde dehydrogenase 2 activity","volume":"28","author":"Ohsawa","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.cbi.2014.12.028_b0675","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1152\/physrev.00017.2013","article-title":"Targeting aldehyde dehydrogenase 2: new therapeutic opportunities","volume":"94","author":"Chen","year":"2014","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.cbi.2014.12.028_b0680","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/S0969-2126(97)00224-4","article-title":"Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion","volume":"5","author":"Steinmetz","year":"1997","journal-title":"Structure"},{"key":"10.1016\/j.cbi.2014.12.028_b0685","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1079\/PNS2003327","article-title":"Overview of the role of alcohol dehydrogenase and aldehyde dehydrogenase and their variants in the genesis of alcohol-related pathology","volume":"63","author":"Crabb","year":"2004","journal-title":"Proc. Nutr. Soc."},{"key":"10.1016\/j.cbi.2014.12.028_b0690","first-page":"677","article-title":"Alcohol and aldehyde dehydrogenase genotypes and alcoholism in Chinese men","volume":"48","author":"Thomasson","year":"1991","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.cbi.2014.12.028_b0695","doi-asserted-by":"crossref","DOI":"10.2174\/1389450115666140828142401","article-title":"Mitochondrial aldehyde dehydrogenase, a potential drug target for protection of heart and brain from ischemia\/reperfusion injury","author":"Luo","year":"2014","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.cbi.2014.12.028_b0700","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.3009539","article-title":"Aldehyde dehydrogenase-2 regulates nociception in rodent models of acute inflammatory pain","volume":"6","author":"Zambelli","year":"2014","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0705","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/0888-7543(95)80150-K","article-title":"Assignment of ALDH3 to human chromosome 17p11.2 and ALDH5 to human chromosome 9p13","volume":"25","author":"Hiraoka","year":"1995","journal-title":"Genomics"},{"key":"10.1016\/j.cbi.2014.12.028_b0710","doi-asserted-by":"crossref","first-page":"1178","DOI":"10.1016\/S0891-5849(03)00070-4","article-title":"Aldh3a1 protects human corneal epithelial cells from ultraviolet- and 4-hydroxy-2-nonenal-induced oxidative damage","volume":"34","author":"Pappa","year":"2003","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0715","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0891-5849(98)00206-8","article-title":"Inhibition of class-3 aldehyde dehydrogenase and cell growth by restored lipid peroxidation in hepatoma cell lines","volume":"26","author":"Canuto","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0720","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1006\/exer.1996.0098","article-title":"Corneal aldehyde dehydrogenase displays antioxidant properties","volume":"63","author":"Uma","year":"1996","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0725","doi-asserted-by":"crossref","first-page":"1459","DOI":"10.1016\/j.freeradbiomed.2006.08.009","article-title":"Antioxidant function of corneal ALDH3A1 in cultured stromal fibroblasts","volume":"41","author":"Lassen","year":"2006","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0730","first-page":"949","article-title":"Genetic modification of hematopoietic progenitor cells for combined resistance to 4-hydroperoxycyclophosphamide, vincristine, and daunorubicin","volume":"22","author":"Wang","year":"2001","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.cbi.2014.12.028_b0735","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/S0009-2797(02)00169-2","article-title":"Aldehyde dehydrogenase 3 expression is decreased by clofibrate via PPAR gamma induction in JM2 rat hepatoma cell line","volume":"143\u2013144","author":"Canuto","year":"2003","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0740","doi-asserted-by":"crossref","first-page":"27998","DOI":"10.1074\/jbc.M503698200","article-title":"Human aldehyde dehydrogenase 3A1 inhibits proliferation and promotes survival of human corneal epithelial cells","volume":"280","author":"Pappa","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0745","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.1016\/j.freeradbiomed.2006.01.020","article-title":"Arachidonic acid suppresses growth of human lung tumor A549 cells through down-regulation of ALDH3A1 expression","volume":"40","author":"Muzio","year":"2006","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0750","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.lungcan.2007.08.033","article-title":"ALDH1A1 and ALDH3A1 expression in lung cancers: correlation with histologic type and potential precursors","volume":"59","author":"Patel","year":"2008","journal-title":"Lung Cancer"},{"key":"10.1016\/j.cbi.2014.12.028_b0755","doi-asserted-by":"crossref","DOI":"10.1016\/j.exphem.2011.12.006","article-title":"Aldehyde dehydrogenases are regulators of hematopoietic stem cell numbers and B-cell development","volume":"40","author":"Gasparetto","year":"2012","journal-title":"Exp. Hematol."},{"key":"10.1016\/j.cbi.2014.12.028_b0760","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.freeradbiomed.2013.11.028","article-title":"Aldehyde dehydrogenase 3A1 protects airway epithelial cells from cigarette smoke-induced DNA damage and cytotoxicity","volume":"68","author":"Jang","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0765","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1042\/bj20030810","article-title":"Human aldehyde dehydrogenase 3A1 (ALDH3A1): biochemical characterization and immunohistochemical localization in the cornea","volume":"376","author":"Pappa","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2014.12.028_b0770","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.exer.2006.04.010","article-title":"ALDH3A1: a corneal crystallin with diverse functions","volume":"84","author":"Estey","year":"2007","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0775","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1016\/j.freeradbiomed.2012.02.050","article-title":"Molecular mechanisms of ALDH3A1-mediated cellular protection against 4-hydroxy-2-nonenal","volume":"52","author":"Black","year":"2012","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.cbi.2014.12.028_b0780","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/S0009-2797(00)00270-2","article-title":"Selective protection by stably transfected human ALDH3A1 (but not human ALDH1A1) against toxicity of aliphatic aldehydes in V79 cells","volume":"130\u2013132","author":"Townsend","year":"2001","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0785","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1097\/00008571-199312000-00002","article-title":"Mouse dioxin-inducible cytosolic aldehyde dehydrogenase-3: AHD4 cDNA sequence, genetic mapping, and differences in mRNA levels","volume":"3","author":"Vasiliou","year":"1993","journal-title":"Pharmacogenetics"},{"key":"10.1016\/j.cbi.2014.12.028_b0790","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0009-2797(94)03325-3","article-title":"Comparison of expression of aldehyde dehydrogenase 3 and CYP1A1 in dominant and recessive aryl hydrocarbon hydroxylase-deficient mutant mouse hepatoma cells","volume":"94","author":"Korkalainen","year":"1995","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0795","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1167\/iovs.07-1057","article-title":"Gene expression of the mouse corneal crystallin Aldh3a1: activation by Pax6, Oct1, and p300","volume":"49","author":"Davis","year":"2008","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.cbi.2014.12.028_b0800","doi-asserted-by":"crossref","first-page":"2593","DOI":"10.1038\/bjc.2014.201","article-title":"Aldehyde dehydrogenase 3A1 associates with prostate tumorigenesis","volume":"110","author":"Yan","year":"2014","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.cbi.2014.12.028_b0805","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1006\/abbi.1993.1564","article-title":"Physiological substrates for rat alcohol dehydrogenase classes: aldehydes of lipid peroxidation, omega-hydroxyfatty acids, and retinoids","volume":"307","author":"Boleda","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2014.12.028_b0810","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1159\/000469238","article-title":"Catalytic properties of human liver alcohol dehydrogenase isoenzymes","volume":"37","author":"Bosron","year":"1987","journal-title":"Enzyme"},{"key":"10.1016\/j.cbi.2014.12.028_b0815","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/0888-7543(90)90535-3","article-title":"The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome","volume":"7","author":"Yasunami","year":"1990","journal-title":"Genomics"},{"key":"10.1016\/j.cbi.2014.12.028_b0820","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1016\/0006-291X(87)90779-0","article-title":"The human beta 3 alcohol dehydrogenase subunit differs from beta 1 by a Cys for Arg-369 substitution which decreases NAD(H) binding","volume":"146","author":"Burnell","year":"1987","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.cbi.2014.12.028_b0825","first-page":"85","article-title":"Classification of alcohol metabolizing enzymes and polymorphisms \u2013 specificity in Japanese","volume":"36","author":"Harada","year":"2001","journal-title":"Nihon Arukoru Yakubutsu Igakkai Zasshi"},{"key":"10.1016\/j.cbi.2014.12.028_b0830","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1111\/j.1432-1033.1994.1081b.x","article-title":"Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization","volume":"225","author":"Danielsson","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.cbi.2014.12.028_b0835","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.1097\/01.ALC.0000075823.73536.DD","article-title":"Cardiac overexpression of alcohol dehydrogenase exacerbates cardiac contractile dysfunction, lipid peroxidation, and protein damage after chronic ethanol ingestion","volume":"27","author":"Hintz","year":"2003","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0840","first-page":"301","article-title":"Site-directed mutagenesis and enzyme properties of mammalian alcohol dehydrogenases correlated with their tissue distribution","volume":"71","author":"Hoog","year":"1994","journal-title":"EXS"},{"key":"10.1016\/j.cbi.2014.12.028_b0845","doi-asserted-by":"crossref","first-page":"11222","DOI":"10.1073\/pnas.90.23.11222","article-title":"Origin of the human alcohol dehydrogenase system: implications from the structure and properties of the octopus protein","volume":"90","author":"Kaiser","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.cbi.2014.12.028_b0850","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1300\/J251v07n03_22","article-title":"Review of the molecular biology of the human alcohol dehydrogenase genes and gene products","volume":"7","author":"Cotton","year":"1988","journal-title":"Adv. Alcohol Subst. Abuse"},{"key":"10.1016\/j.cbi.2014.12.028_b0855","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1111\/j.1530-0277.1989.tb00383.x","article-title":"Nucleotide sequence of the ADH2(3) gene encoding the human alcohol dehydrogenase beta 3 subunit","volume":"13","author":"Carr","year":"1989","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0860","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1111\/j.1432-1033.1989.tb14931.x","article-title":"The genes for human alcohol dehydrogenases beta 1 and beta 2 differ by only one nucleotide","volume":"183","author":"Matsuo","year":"1989","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.cbi.2014.12.028_b0865","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1111\/j.1530-0277.2002.tb02673.x","article-title":"Alcohol dependence symptoms and alcohol dehydrogenase 2 polymorphism: Israeli Ashkenazis, Sephardics, and recent Russian immigrants","volume":"26","author":"Hasin","year":"2002","journal-title":"Alcohol. Clin. Exp. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0870","doi-asserted-by":"crossref","first-page":"1230","DOI":"10.1023\/A:1024134520823","article-title":"Alcohol dehydrogenase (ADH) isoenzymes and aldehyde dehydrogenase (ALDH) activity in the human pancreas","volume":"48","author":"Chrostek","year":"2003","journal-title":"Dig. Dis. Sci."},{"key":"10.1016\/j.cbi.2014.12.028_b0875","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/jcla.10076","article-title":"Gender-related differences in hepatic activity of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in humans","volume":"17","author":"Chrostek","year":"2003","journal-title":"J. Clin. Lab. Anal."},{"key":"10.1016\/j.cbi.2014.12.028_b0880","series-title":"Carbonyl Toxification Hypothesis of Biological Aging","author":"Yin","year":"1995"},{"key":"10.1016\/j.cbi.2014.12.028_b0885","doi-asserted-by":"crossref","first-page":"34853","DOI":"10.1074\/jbc.M005536200","article-title":"The role of alpha, beta-dicarbonyl compounds in the toxicity of short chain sugars","volume":"275","author":"Okado-Matsumoto","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2014.12.028_b0890","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1021\/bi971958i","article-title":"Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal","volume":"37","author":"Humphries","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2014.12.028_b0895","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1161\/01.RES.76.2.293","article-title":"Electrophysiological effects of 4-hydroxynonenal, an aldehydic product of lipid peroxidation, on isolated rat ventricular myocytes","volume":"76","author":"Bhatnagar","year":"1995","journal-title":"Circ. Res."},{"key":"10.1016\/j.cbi.2014.12.028_b0900","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1074\/mcp.M113.032953","article-title":"Alkylation damage by lipid electrophiles targets functional protein systems","volume":"13","author":"Codreanu","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.cbi.2014.12.028_b0905","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.cbi.2011.02.007","article-title":"Human and rodent aldo\u2013keto reductases from the AKR1B subfamily and their specificity with retinaldehyde","volume":"191","author":"Ruiz","year":"2011","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2014.12.028_b0910","doi-asserted-by":"crossref","first-page":"12172","DOI":"10.1021\/bi000796e","article-title":"Selective recognition of glutathiolated aldehydes by aldose reductase","volume":"39","author":"Ramana","year":"2000","journal-title":"Biochemistry"}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S000927971400413X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S000927971400413X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,14]],"date-time":"2025-09-14T13:38:36Z","timestamp":1757857116000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S000927971400413X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,6]]},"references-count":182,"alternative-id":["S000927971400413X"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2014.12.028","relation":{},"ISSN":["0009-2797"],"issn-type":[{"value":"0009-2797","type":"print"}],"subject":[],"published":{"date-parts":[[2015,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Oxidative and reductive metabolism of lipid-peroxidation derived carbonyls","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2014.12.028","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier Ireland Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}