{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T17:20:40Z","timestamp":1787505640875,"version":"build-2736575974"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31600823"],"award-info":[{"award-number":["31600823"]}],"id":[{"id":"10.13039\/501100001809","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":[[2024,3]]},"DOI":"10.1016\/j.cbi.2024.110896","type":"journal-article","created":{"date-parts":[[2024,1,30]],"date-time":"2024-01-30T11:47:01Z","timestamp":1706615221000},"page":"110896","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":8,"special_numbering":"C","title":["Aldo-keto reductases 7A subfamily: A mini review"],"prefix":"10.1016","volume":"391","author":[{"given":"Mengli","family":"Zhao","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiajin","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongyu","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingdong","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7316-5151","authenticated-orcid":false,"given":"Dan","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"Pt 3","key":"10.1016\/j.cbi.2024.110896_bib1","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1042\/bj3260625","article-title":"Comparative anatomy of the aldo-keto reductase superfamily","volume":"326","author":"Jez","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2024.110896_bib2","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.cbi.2014.09.024","article-title":"The aldo-keto reductases (AKRs): overview","volume":"234","author":"Penning","year":"2015","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2024.110896_bib3","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1146\/annurev.pharmtox.47.120505.105337","article-title":"Aldo-keto reductases and bioactivation\/detoxication","volume":"47","author":"Jin","year":"2007","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.cbi.2024.110896_bib4","doi-asserted-by":"crossref","first-page":"2767","DOI":"10.2741\/2006","article-title":"Role of aldo-keto reductases in development of prostate and breast cancer","volume":"11","author":"Jin","year":"2006","journal-title":"Front. Biosci."},{"issue":"6","key":"10.1016\/j.cbi.2024.110896_bib5","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/S0006-2952(97)84253-0","article-title":"A new nomenclature for the aldo-keto reductase superfamily","volume":"54","author":"Jez","year":"1997","journal-title":"Biochem. Pharmacol."},{"issue":"21","key":"10.1016\/j.cbi.2024.110896_bib6","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-keto reductases","volume":"90","author":"Ellis","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.cbi.2024.110896_bib7","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/S0009-2797(02)00193-X","article-title":"The aldo-keto reductase superfamily homepage","volume":"143\u2013144","author":"Hyndman","year":"2003","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2024.110896_bib8","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","author":"Hinshelwood","year":"2003","journal-title":"Chem. Biol. Interact."},{"issue":"Pt 1","key":"10.1016\/j.cbi.2024.110896_bib9","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-keto 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."},{"issue":"Pt 3","key":"10.1016\/j.cbi.2024.110896_bib10","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1042\/bj20020342","article-title":"Novel homodimeric and heterodimeric rat gamma-hydroxybutyrate synthases that associate with the Golgi apparatus define a distinct subclass of aldo-keto reductase 7 family proteins","volume":"366","author":"Kelly","year":"2002","journal-title":"Biochem. J."},{"issue":"7","key":"10.1016\/j.cbi.2024.110896_bib11","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-keto reductase superfamily, AKR7A3","volume":"20","author":"Knight","year":"1999","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.cbi.2024.110896_bib12","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S0009-2797(02)00173-4","article-title":"Substrate specificity of mouse aldo-keto reductase AKR7A5","volume":"143\u2013144","author":"Hinshelwood","year":"2003","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2024.110896_bib13","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1146\/annurev.pharmtox.47.120505.105337","article-title":"Aldo-keto reductases and bioactivation\/detoxication","volume":"47","author":"Jin","year":"2007","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"issue":"1","key":"10.1016\/j.cbi.2024.110896_bib14","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.cbi.2011.09.007","article-title":"Human aldo-keto 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."},{"issue":"11","key":"10.1016\/j.cbi.2024.110896_bib15","doi-asserted-by":"crossref","first-page":"3821","DOI":"10.1016\/S0021-9258(17)40325-5","article-title":"Purification and properties of NADPH-dependent aldehyde reductase from human liver","volume":"252","author":"Wermuth","year":"1977","journal-title":"J. Biol. Chem."},{"issue":"18","key":"10.1016\/j.cbi.2024.110896_bib16","doi-asserted-by":"crossref","first-page":"16285","DOI":"10.1074\/jbc.M110808200","article-title":"The crystal structure of rat liver AKR7A1. A dimeric member of the aldo-keto reductase superfamily","volume":"277","author":"Kozma","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.cbi.2024.110896_bib17","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1021\/tx7004458","article-title":"Protection against aflatoxin B1-induced cytotoxicity by expression of the cloned aflatoxin B1-aldehyde reductases rat AKR7A1 and human AKR7A3","volume":"21","author":"Bodreddigari","year":"2008","journal-title":"Chem. Res. Toxicol."},{"issue":"1\u20133","key":"10.1016\/j.cbi.2024.110896_bib18","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0014-5793(02)02982-4","article-title":"Characterisation of a novel mouse liver aldo-keto reductase AKR7A5","volume":"523","author":"Hinshelwood","year":"2002","journal-title":"FEBS Lett."},{"issue":"5","key":"10.1016\/j.cbi.2024.110896_bib19","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1111\/j.1742-4658.2007.05679.x","article-title":"Neuroglobin and cytoglobin expression in mice. Evidence for a correlation with reactive oxygen species scavenging","volume":"274","author":"Fordel","year":"2007","journal-title":"FEBS J."},{"issue":"4","key":"10.1016\/j.cbi.2024.110896_bib20","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.tiv.2014.02.010","article-title":"Aldo-keto reductase 7A5 (AKR7A5) attenuates oxidative stress and reactive aldehyde toxicity in V79-4 cells","volume":"28","author":"Li","year":"2014","journal-title":"Toxicol. Vitro"},{"issue":"48","key":"10.1016\/j.cbi.2024.110896_bib21","doi-asserted-by":"crossref","first-page":"83469","DOI":"10.18632\/oncotarget.12726","article-title":"AKR7A3 suppresses tumorigenicity and chemoresistance in hepatocellular carcinoma through attenuation of ERK, c-Jun and NF-\u03baB signaling pathways","volume":"8","author":"Chow","year":"2017","journal-title":"Oncotarget"},{"issue":"1\u20132","key":"10.1016\/j.cbi.2024.110896_bib22","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.2024.110896_bib23","doi-asserted-by":"crossref","first-page":"997","DOI":"10.2147\/JHC.S323743","article-title":"Regulation network and prognostic significance of aldo-keto reductase (AKR) superfamily genes in hepatocellular carcinoma","volume":"8","author":"Dai","year":"2021","journal-title":"J. Hepatocell. Carcinoma"},{"issue":"28","key":"10.1016\/j.cbi.2024.110896_bib24","article-title":"The role of cytochromes p450 and aldo-keto reductases in prognosis of breast carcinoma patients","volume":"93","author":"Hlav\u00e1\u010d","year":"2014","journal-title":"Medicine (Baltim.)"},{"issue":"3","key":"10.1016\/j.cbi.2024.110896_bib25","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1124\/pharmrev.120.000122","article-title":"Aldo-keto reductases and cancer drug resistance","volume":"73","author":"Penning","year":"2021","journal-title":"Pharmacol. Rev."},{"issue":"1","key":"10.1016\/j.cbi.2024.110896_bib26","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s10528-019-09936-y","article-title":"Characterization and analysis of mammalian AKR7A gene promoters: implications for transcriptional regulation","volume":"58","author":"Rajib","year":"2020","journal-title":"Biochem. Genet."},{"issue":"4","key":"10.1016\/j.cbi.2024.110896_bib27","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1093\/carcin\/bgg016","article-title":"Characterization of the rat aflatoxin B1 aldehyde reductase gene, AKR7A1. Structure and chromosomal localization of AKR7A1 as well as identification of antioxidant response elements in the gene promoter","volume":"24","author":"Ellis","year":"2003","journal-title":"Carcinogenesis"},{"key":"10.1016\/j.cbi.2024.110896_bib28","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.cbi.2014.10.019","article-title":"Nrf2-mediated adaptive response to methyl glyoxal in HepG2 cells involves the induction of AKR7A2","volume":"234","author":"Li","year":"2015","journal-title":"Chem. Biol. Interact."},{"issue":"17","key":"10.1016\/j.cbi.2024.110896_bib29","first-page":"3887","article-title":"Resistance to aflatoxin B1 is associated with the expression of a novel aldo-keto reductase which has catalytic activity towards a cytotoxic aldehyde-containing metabolite of the toxin","volume":"53","author":"Hayes","year":"1993","journal-title":"Cancer Res."},{"issue":"Pt 1","key":"10.1016\/j.cbi.2024.110896_bib30","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1042\/bj2920013","article-title":"A novel aldehyde reductase with activity towards a metabolite of aflatoxin B1 is expressed in rat liver during carcinogenesis and following the administration of an anti-oxidant","volume":"292","author":"Judah","year":"1993","journal-title":"Biochem. J."},{"issue":"1","key":"10.1016\/j.cbi.2024.110896_bib31","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1111\/j.1574-6968.2003.tb11503.x","article-title":"A novel aldo-keto reductase from Escherichia coli can increase resistance to methylglyoxal toxicity","volume":"218","author":"Grant","year":"2003","journal-title":"FEMS Microbiol. Lett."},{"issue":"Pt 1","key":"10.1016\/j.cbi.2024.110896_bib32","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1042\/bj3000117","article-title":"Regulation of aflatoxin B1-metabolizing aldehyde reductase and glutathione S-transferase by chemoprotectors","volume":"300","author":"McLellan","year":"1994","journal-title":"Biochem. J."},{"issue":"11","key":"10.1016\/j.cbi.2024.110896_bib33","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1016\/S0006-2952(01)00771-7","article-title":"Expression of rat aldehyde reductase AKR7A1: influence of age and sex and tissue-specific inducibility","volume":"62","author":"Grant","year":"2001","journal-title":"Biochem. Pharmacol."},{"issue":"4","key":"10.1016\/j.cbi.2024.110896_bib34","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1002\/prot.340110407","article-title":"Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons","volume":"11","author":"Nicholls","year":"1991","journal-title":"Proteins: Struct., Funct., Bioinf."},{"issue":"7","key":"10.1016\/j.cbi.2024.110896_bib35","doi-asserted-by":"crossref","first-page":"4536","DOI":"10.1074\/jbc.M207293200","article-title":"Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element. Degradation of Nrf2 by the 26 S proteasome","volume":"278","author":"Nguyen","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"Pt 2","key":"10.1016\/j.cbi.2024.110896_bib36","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.2024.110896_bib37","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/S0009-2797(02)00186-2","article-title":"The high resolution crystal structure of rat liver AKR7A1: understanding the substrate specificites of the AKR7 family","volume":"143","author":"Kozma","year":"2003","journal-title":"Chem. Biol. Interact."},{"issue":"1","key":"10.1016\/j.cbi.2024.110896_bib38","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-keto reductase","volume":"148","author":"Gardner","year":"2004","journal-title":"Toxicol. Lett."},{"issue":"5","key":"10.1016\/j.cbi.2024.110896_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0097678","article-title":"Evaluation of toxicogenomics approaches for assessing the risk of nongenotoxic carcinogenicity in rat liver","volume":"9","author":"Eichner","year":"2014","journal-title":"PLoS One"},{"issue":"10","key":"10.1016\/j.cbi.2024.110896_bib40","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1177\/0960327117751234","article-title":"Identification of aldo-keto reductase (AKR7A1) and glutathione S-transferase pi (GSTP1) as novel renal damage biomarkers following exposure to mercury","volume":"37","author":"Shin","year":"2018","journal-title":"Hum. Exp. Toxicol."},{"issue":"13","key":"10.1016\/j.cbi.2024.110896_bib41","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1242\/jcs.146365","article-title":"TFEB at a glance","volume":"129","author":"Napolitano","year":"2016","journal-title":"J. Cell Sci."},{"issue":"4","key":"10.1016\/j.cbi.2024.110896_bib42","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1002\/hep.24493","article-title":"Aldo\u2010keto reductase\u20107A protects liver cells and tissues from acetaminophen\u2010induced oxidative stress and hepatotoxicity","volume":"54","author":"Ahmed","year":"2011","journal-title":"Hepatology"},{"issue":"36","key":"10.1016\/j.cbi.2024.110896_bib43","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-keto reductase AKR7A2","volume":"282","author":"Lyon","year":"2007","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.cbi.2024.110896_bib44","doi-asserted-by":"crossref","first-page":"1056","DOI":"10.1046\/j.1432-1327.1999.00826.x","article-title":"Cloning and expression of succinic semialdehyde reductase from human brain. Identity with aflatoxin B sub(1) aldehyde reductase","volume":"265","author":"Schaller","year":"1999","journal-title":"Eur. J. Biochem."},{"issue":"11","key":"10.1016\/j.cbi.2024.110896_bib45","doi-asserted-by":"crossref","first-page":"7636","DOI":"10.1016\/S0021-9258(18)53003-9","article-title":"Isolation and characterization of recombinant mitochondrial 4-aminobutyrate aminotransferase","volume":"268","author":"Park","year":"1993","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.cbi.2024.110896_bib46","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1038\/ng727","article-title":"Pharmacologic rescue of lethal seizures in mice deficient in succinate semialdehyde dehydrogenase","volume":"29","author":"Hogema","year":"2001","journal-title":"Nat. Genet."},{"issue":"2","key":"10.1016\/j.cbi.2024.110896_bib47","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1111\/j.1471-4159.1980.tb06272.x","article-title":"Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase","volume":"35","author":"Hoffman","year":"1980","journal-title":"J. Neurochem."},{"issue":"2","key":"10.1016\/j.cbi.2024.110896_bib48","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1186\/1479-7364-3-2-106","article-title":"Comparative genomics of aldehyde dehydrogenase 5a1 (succinate semialdehyde dehydrogenase) and accumulation of gamma-hydroxybutyrate associated with its deficiency","volume":"3","author":"Malaspina","year":"2009","journal-title":"Hum. Genom."},{"issue":"30","key":"10.1016\/j.cbi.2024.110896_bib49","doi-asserted-by":"crossref","first-page":"4765","DOI":"10.1038\/sj.onc.1206684","article-title":"Aflatoxin B1 aldehyde reductase (Afar) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells","volume":"22","author":"Praml","year":"2003","journal-title":"Oncogene"},{"issue":"2","key":"10.1016\/j.cbi.2024.110896_bib50","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1074\/mcp.M113.035600","article-title":"Analysis of the human tissue-specific expression by genome-wide integration of transcriptomics and antibody-based proteomics","volume":"13","author":"Fagerberg","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"issue":"4","key":"10.1016\/j.cbi.2024.110896_bib51","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1111\/cts.13205","article-title":"Non-synonymous alterations in AKR7A3 and ABCA6 correlate with bleeding in aged patients treated with rivaroxaban","volume":"15","author":"Zhao","year":"2022","journal-title":"Clin. Transl. Sci."},{"issue":"Pt 2","key":"10.1016\/j.cbi.2024.110896_bib52","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-keto reductase 7 family that is widely distributed in extrahepatic tissues","volume":"348","author":"Kelly","year":"2000","journal-title":"Biochem. J."},{"issue":"9","key":"10.1016\/j.cbi.2024.110896_bib53","doi-asserted-by":"crossref","first-page":"3194","DOI":"10.1210\/endo.141.9.7685","article-title":"Androgen-regulated expression of a novel member of the aldo-keto reductase superfamily in regrowing rat prostate","volume":"141","author":"Nishi","year":"2000","journal-title":"Endocrinology"},{"issue":"2\u20133","key":"10.1016\/j.cbi.2024.110896_bib54","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.tox.2006.06.013","article-title":"Mouse aldo-keto reductase AKR7A5 protects V79 cells against 4-hydroxynonenal-induced apoptosis","volume":"226","author":"Li","year":"2006","journal-title":"Toxicology"},{"issue":"6","key":"10.1016\/j.cbi.2024.110896_bib55","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1021\/bi051610k","article-title":"Crystal structure of mouse succinic semialdehyde reductase AKR7A5: structural basis for substrate specificity","volume":"45","author":"Zhu","year":"2006","journal-title":"Biochemistry"},{"issue":"5","key":"10.1016\/j.cbi.2024.110896_bib56","doi-asserted-by":"crossref","first-page":"2853","DOI":"10.1167\/iovs.13-13487","article-title":"Aldose reductase inhibition prevents endotoxin-induced inflammatory responses in retinal microglia","volume":"55","author":"Chang","year":"2014","journal-title":"Invest. Ophthalmol. Vis. Sci."}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279724000425?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279724000425?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T19:50:27Z","timestamp":1762113027000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279724000425"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,3]]},"references-count":56,"alternative-id":["S0009279724000425"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2024.110896","relation":{},"ISSN":["0009-2797"],"issn-type":[{"value":"0009-2797","type":"print"}],"subject":[],"published":{"date-parts":[[2024,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Aldo-keto reductases 7A subfamily: A mini review","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2024.110896","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"110896"}}