{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,7]],"date-time":"2026-05-07T10:55:37Z","timestamp":1778151337521,"version":"3.51.4"},"reference-count":32,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,5,1]],"date-time":"2019-05-01T00:00:00Z","timestamp":1556668800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["17K11151"],"award-info":[{"award-number":["17K11151"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2019,5]]},"DOI":"10.1016\/j.cbi.2019.03.026","type":"journal-article","created":{"date-parts":[[2019,3,26]],"date-time":"2019-03-26T14:33:47Z","timestamp":1553610827000},"page":"12-20","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":10,"special_numbering":"C","title":["Rabbit dehydrogenase\/reductase SDR family member 11 (DHRS11): Its identity with acetohexamide reductase with broad substrate specificity and inhibitor sensitivity, different from human DHRS11"],"prefix":"10.1016","volume":"305","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0578-9672","authenticated-orcid":false,"given":"Satoshi","family":"Endo","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Namiki","family":"Miyagi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5304-5443","authenticated-orcid":false,"given":"Toshiyuki","family":"Matsunaga","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akira","family":"Ikari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2019.03.026_bib1","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.cbi.2008.10.040","article-title":"The SDR (short-chain dehydrogenase\/reductase and related enzymes) nomenclature initiative","volume":"178","author":"Persson","year":"2009","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2019.03.026_bib2","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.cbi.2012.11.009","article-title":"Classification and nomenclature of the superfamily of short-chain dehydrogenases\/reductases (SDRs)","volume":"202","author":"Persson","year":"2013","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2019.03.026_bib3","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.bbrc.2016.01.190","article-title":"Human dehydrogenase\/reductase (SDR family) member 11 is a novel type of 17\u03b2-hydroxysteroid dehydrogenase","volume":"472","author":"Endo","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.cbi.2019.03.026_bib4","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/s12014-018-9189-x","article-title":"Proteomics-based insights into mitogen-activated protein kinase inhibitor resistance of cerebral melanoma metastases","volume":"15","author":"Zila","year":"2018","journal-title":"Clin. Proteonomics"},{"key":"10.1016\/j.cbi.2019.03.026_bib5","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1248\/bpb.23.155","article-title":"Catalytic properties for naphthoquinones and partial primary structure of rabbit heart acetohexamide reductase","volume":"23","author":"Imamura","year":"2000","journal-title":"Biol. Pharm. Bull."},{"key":"10.1016\/j.cbi.2019.03.026_bib6","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1093\/oxfordjournals.jbchem.a021291","article-title":"Purification and catalytic properties of a novel acetohexamide-reducing enzyme from rabbit heart","volume":"119","author":"Imamura","year":"1996","journal-title":"J. Biochem."},{"key":"10.1016\/j.cbi.2019.03.026_bib7","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1093\/oxfordjournals.jbchem.a021643","article-title":"Characterization of acetohexamide reductases purified from rabbit liver, kidney, and heart: structural requirements for substrates and inhibitors","volume":"121","author":"Imamura","year":"1997","journal-title":"J. Biochem."},{"key":"10.1016\/j.cbi.2019.03.026_bib8","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/0378-1119(94)00843-H","article-title":"Cloning and expression of the cDNA encoding rabbit liver carbonyl reductase","volume":"154","author":"Gonzalez","year":"1995","journal-title":"Gene"},{"key":"10.1016\/j.cbi.2019.03.026_bib9","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/S0009-2797(02)00210-7","article-title":"Cloning, expression and tissue distribution of a tetrameric form of pig carbonyl reductase","volume":"143\u2013144","author":"Usami","year":"2003","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2019.03.026_bib10","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1093\/oxfordjournals.jbchem.a022266","article-title":"Purification and catalytic properties of a tetrameric carbonyl reductase from rabbit heart","volume":"125","author":"Imamura","year":"1999","journal-title":"J. Biochem."},{"key":"10.1016\/j.cbi.2019.03.026_bib11","series-title":"Molecular Cloning: A Laboratory Manual","author":"Sambrook","year":"1989"},{"key":"10.1016\/j.cbi.2019.03.026_bib12","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/j.abb.2010.08.010","article-title":"Properties and tissue distribution of a novel aldo-keto reductase encoding in a rat gene (Akr1b10)","volume":"503","author":"Endo","year":"2010","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.03.026_bib13","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.cbi.2019.03.026_bib14","doi-asserted-by":"crossref","first-page":"13201","DOI":"10.1021\/jp035478e","article-title":"The filling potential method:\u2009 A method for estimating the free energy surface for protein\u2212ligand docking","volume":"107","author":"Fukunishi","year":"2003","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.cbi.2019.03.026_bib15","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.jmgm.2005.04.004","article-title":"Similarities among receptor pockets and among compounds: analysis and application to in silico ligand screening","volume":"24","author":"Fukunishi","year":"2005","journal-title":"J. Mol. Graph. Model."},{"key":"10.1016\/j.cbi.2019.03.026_bib16","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1021\/acs.jcim.5b00319","article-title":"Computational study of drug binding affinity to influenza A neuraminidase using smooth reaction path generation (SRPG) method","volume":"55","author":"Nguyen","year":"2015","journal-title":"J. Chem. Inf. Model."},{"key":"10.1016\/j.cbi.2019.03.026_bib17","doi-asserted-by":"crossref","first-page":"W252","DOI":"10.1093\/nar\/gku340","article-title":"SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information","volume":"42","author":"Biasini","year":"2014","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.cbi.2019.03.026_bib18","doi-asserted-by":"crossref","first-page":"4048","DOI":"10.1021\/jf500615u","article-title":"Diacetyl: occurrence, analysis, and toxicity","volume":"62","author":"Shibamoto","year":"2014","journal-title":"J. Agric. Food Chem."},{"key":"10.1016\/j.cbi.2019.03.026_bib19","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1002\/biof.1408","article-title":"Isatin, an endogenous nonpeptide biofactor: a review of its molecular targets, mechanisms of actions, and their biomedical implications","volume":"44","author":"Medvedev","year":"2018","journal-title":"Biofactors"},{"key":"10.1016\/j.cbi.2019.03.026_bib20","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.2019.03.026_bib21","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1196\/annals.1433.058","article-title":"\u03b1-Dicarbonyl compounds--key intermediates for the formation of carbohydrate-based melanoidins","volume":"1126","author":"Kroh","year":"2008","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.cbi.2019.03.026_bib22","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1016\/0006-2952(80)90601-2","article-title":"Isolation and characterization of rabbit liver xenobiotic carbonyl reductases","volume":"29","author":"Felsted","year":"1980","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2019.03.026_bib23","first-page":"1153","article-title":"Reductases for aromatic aldehydes and ketones from rabbit liver. Purification and characterization","volume":"87","author":"Sawada","year":"1980","journal-title":"J. Biochem."},{"key":"10.1016\/j.cbi.2019.03.026_bib24","doi-asserted-by":"crossref","first-page":"1366","DOI":"10.1016\/j.bcp.2013.08.024","article-title":"Rabbit 3-hydroxyhexobarbital dehydrogenase is a NADPH-preferring reductase with broad substrate specificity for ketosteroids, prostaglandin D\u2082, and other endogenous and xenobiotic carbonyl compounds","volume":"86","author":"Endo","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2019.03.026_bib25","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1124\/dmd.113.056044","article-title":"Cloning and characterization of four rabbit aldo-keto reductases featuring broad substrate specificity for xenobiotic and endogenous carbonyl compounds: relationship with multiple forms of drug ketone reductases","volume":"42","author":"Endo","year":"2014","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.cbi.2019.03.026_bib26","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.abb.2012.07.012","article-title":"Characterization of rabbit aldose reductase-like protein with 3\u03b2-hydroxysteroid dehydrogenase activity","volume":"527","author":"Endo","year":"2012","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.03.026_bib27","doi-asserted-by":"crossref","first-page":"R139","DOI":"10.1530\/JME-16-0013","article-title":"Novel mechanisms for DHEA action","volume":"56","author":"Prough","year":"2016","journal-title":"J. Mol. Endocrinol."},{"key":"10.1016\/j.cbi.2019.03.026_bib28","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.jsbmb.2014.03.008","article-title":"Dehydroepiandrosterone: a neuroactive steroid","volume":"145","author":"St\u00e1rka","year":"2015","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.cbi.2019.03.026_bib29","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1210\/jcem-40-3-373","article-title":"Interaction of delta-5-androstene-3\u03b2,17\u03b2-diol with estradiol and dihydrotestosterone receptors in human myometrial and mammary cancer tissue","volume":"40","author":"Poortman","year":"1975","journal-title":"J. Clin. Endocrinol. Metab."},{"key":"10.1016\/j.cbi.2019.03.026_bib30","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.1016\/j.steroids.2012.07.014","article-title":"3D models of human ER\u03b1 and ER\u03b2 complexed with 5-androsten-3\u03b2,17\u03b2-diol","volume":"77","author":"Baker","year":"2012","journal-title":"Steroids"},{"key":"10.1016\/j.cbi.2019.03.026_bib31","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1002\/2211-5463.12506","article-title":"Multiple short-chain dehydrogenases\/reductases are regulated in pathological cardiac hypertrophy","volume":"8","author":"Roussel","year":"2018","journal-title":"FEBS Open Bio"},{"key":"10.1016\/j.cbi.2019.03.026_bib32","doi-asserted-by":"crossref","first-page":"25677","DOI":"10.1074\/jbc.M202160200","article-title":"Critical residues for structure and catalysis in short-chain dehydrogenases\/reductases","volume":"277","author":"Filling","year":"2002","journal-title":"J. Biol. Chem."}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279718310731?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279718310731?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,14]],"date-time":"2025-09-14T13:52:11Z","timestamp":1757857931000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279718310731"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,5]]},"references-count":32,"alternative-id":["S0009279718310731"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2019.03.026","relation":{},"ISSN":["0009-2797"],"issn-type":[{"value":"0009-2797","type":"print"}],"subject":[],"published":{"date-parts":[[2019,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Rabbit dehydrogenase\/reductase SDR family member 11 (DHRS11): Its identity with acetohexamide reductase with broad substrate specificity and inhibitor sensitivity, different from human DHRS11","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2019.03.026","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}