{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T22:57:30Z","timestamp":1790463450199,"version":"4.1.0"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2018,4,1]],"date-time":"2018-04-01T00:00:00Z","timestamp":1522540800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The Journal of Steroid Biochemistry and Molecular Biology"],"published-print":{"date-parts":[[2018,4]]},"DOI":"10.1016\/j.jsbmb.2017.11.011","type":"journal-article","created":{"date-parts":[[2017,11,24]],"date-time":"2017-11-24T21:03:01Z","timestamp":1511557381000},"page":"117-126","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"special_numbering":"C","title":["Characterization of equine GST A3-3 as a steroid isomerase"],"prefix":"10.1016","volume":"178","author":[{"given":"Helena","family":"Lindstr\u00f6m","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shawna M.","family":"Peer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy H.","family":"Ing","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bengt","family":"Mannervik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jsbmb.2017.11.011_bib0005","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1093\/toxsci\/49.2.156","article-title":"Concise review of the glutathione S-transferases and their significance to toxicology","volume":"49","author":"Eaton","year":"1999","journal-title":"Toxicol. Sci."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0010","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.bioeng.2006.05.020","article-title":"Glutathione transferases in the genomics era: new insights and perspectives","volume":"23","author":"Frova","year":"2006","journal-title":"Biomol. Eng."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0015","series-title":"Molecular Toxicology","first-page":"303","author":"Josephy","year":"2006"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0020","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1093\/emboj\/18.5.1321","article-title":"Regulation of JNK signaling by GSTp","volume":"18","author":"Adler","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0025","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1038\/cdd.2010.80","article-title":"Glutathione transferases as mediators of signaling pathways involved in cell proliferation and cell death","volume":"17","author":"Laborde","year":"2010","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0030","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.freeradbiomed.2011.04.013","article-title":"The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer","volume":"51","author":"Tew","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0035","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1042\/bj3110739","article-title":"Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase","volume":"311","author":"Meyer","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0040","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/S0092-8674(00)80374-8","article-title":"Cloning and crystal structure of hematopoietic prostaglandin D synthase","volume":"90","author":"Kanaoka","year":"1997","journal-title":"Cell"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0045","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0076-6879(05)01017-7","article-title":"Human glutathione transferase A3-3 active as steroid double-bond isomerase","volume":"401","author":"Raffalli-Mathieu","year":"2005","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0050","doi-asserted-by":"crossref","first-page":"33061","DOI":"10.1074\/jbc.M104539200","article-title":"Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones","volume":"276","author":"Johansson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0055","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1042\/BJ20080397","article-title":"Targeting human glutathione transferase A3-3 attenuates progesterone production in human steroidogenic cells","volume":"414","author":"Raffalli-Mathieu","year":"2008","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0060","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1042\/BJ20100839","article-title":"Porcine glutathione transferase Alpha 2-2 is a human GST A3-3 analogue that catalyses steroid double-bond isomerization","volume":"431","author":"Fedulova","year":"2010","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0065","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.bbagen.2006.06.015","article-title":"Differences between bovine and human steroid double-bond isomerase activities of Alpha-class glutathione transferases selectively expressed in steroidogenic tissues","volume":"1770","author":"Raffalli-Mathieu","year":"2007","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0070","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1095\/biolreprod56.4.789","article-title":"The role of cytochrome P450 17\u03b1-hydroxylase and 3\u03b2-hydroxysteroid dehydrogenase in the integration of gonadal and adrenal steroidogenesis via the \u03945 and \u03944 pathways of steroidogenesis in mammals","volume":"56","author":"Conley","year":"1997","journal-title":"Biol. Reprod."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0075","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/j.jsbmb.2014.07.003","article-title":"Dexamethasone acutely down-regulates genes involved in steroidogenesis in stallion testes","volume":"143","author":"Ing","year":"2014","journal-title":"J. Steroid Biochem. Mol. Biol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0080","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.ab.2011.01.024","article-title":"Quantitative and selective polymerase chain reaction analysis of highly similar human alpha-class glutathione transferases","volume":"412","author":"Larsson","year":"2011","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0085","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1042\/bj3300827","article-title":"Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4","volume":"330","author":"Board","year":"1998","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0090","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1007\/BF02254963","article-title":"Zoo-FISH delineates conserved chromosomal segments in horse and man","volume":"4","author":"Raudsepp","year":"1996","journal-title":"Chromosome Res."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0095","doi-asserted-by":"crossref","first-page":"9909","DOI":"10.1016\/S0021-9258(18)33960-7","article-title":"Binary combinations of four protein subunits with different catalytic specificities explain the relationship between six basic glutathione S-transferases in rat liver cytosol","volume":"257","author":"Mannervik","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0100","series-title":"Proteomics Protoc. Handb.","first-page":"571","article-title":"Protein identification and analysis tools on the ExPASy server","author":"Gasteiger","year":"2005"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0105","doi-asserted-by":"crossref","first-page":"7202","DOI":"10.1073\/pnas.82.21.7202","article-title":"Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties","volume":"82","author":"Mannervik","year":"1985","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0110","series-title":"Conjugation Reactions in Drug Biotransformation","first-page":"101","article-title":"Glutathione conjugation: reaction mechanism of glutathione S-tranferase","author":"Mannervik","year":"1978"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0115","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1006\/jmbi.1993.1376","article-title":"Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes","volume":"232","author":"Sinning","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0120","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1111\/j.1432-1033.1994.tb18666.x","article-title":"X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function","volume":"220","author":"Dirr","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0125","doi-asserted-by":"crossref","first-page":"16648","DOI":"10.1074\/jbc.M201062200","article-title":"Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3","volume":"277","author":"Johansson","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0130","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.abb.2010.12.015","article-title":"Characterization of porcine alpha-class glutathione transferase A1-1","volume":"507","author":"Fedulova","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0135","doi-asserted-by":"crossref","first-page":"11698","DOI":"10.1074\/jbc.M009146200","article-title":"The role of glutathione in the isomerization of Delta(5)-androstene-3,17-dione catalyzed by human glutathione transferase A1-1","volume":"276","author":"Pettersson","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0140","series-title":"Advances in Drug Metabolism in Man","first-page":"407","article-title":"Human glutathione transferases: classification, tissue distribution, structure, and functional properties","author":"Mannervik","year":"1995"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0145","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1042\/bj3110453","article-title":"Isothiocyanates as substrates for human glutathione transferases: structure-activity studies","volume":"311","author":"Kolm","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0150","series-title":"The Leydig Cell","author":"Payne","year":"1996"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0155","doi-asserted-by":"crossref","first-page":"4440","DOI":"10.2527\/jas.2014-7903","article-title":"Temporal changes in histomorphology and gene expression in goat testes during postnatal development","volume":"92","author":"Faucette","year":"2014","journal-title":"J. Anim. Sci."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0160","doi-asserted-by":"crossref","first-page":"3267","DOI":"10.1016\/j.bbagen.2012.11.019","article-title":"Glutathione transferases, regulators of cellular metabolism and physiology, Biochim","volume":"1830","author":"Board","year":"2013","journal-title":"Biophys. Acta."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0165","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1210\/me.2006-0534","article-title":"Hormonal regulation of testicular steroid and cholesterol homeostasis","volume":"22","author":"Eacker","year":"2008","journal-title":"Mol. Endocrinol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0170","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1210\/er.2003-0030","article-title":"Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones","volume":"25","author":"Payne","year":"2004","journal-title":"Endocr. Rev."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0175","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1126\/science.113.2939.490","article-title":"An enzyme in endocrine tissues which oxidizes \u03945-3 hydroxy steroids to \u03b1, \u03b2 unsaturated ketones","volume":"113","author":"Samuels","year":"1951","journal-title":"Science"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0180","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/0006-3002(55)90079-2","article-title":"Enzymic isomerization of \u03945-3-ketosteroids","volume":"18","author":"Talalay","year":"1955","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0185","doi-asserted-by":"crossref","first-page":"9283","DOI":"10.1021\/bi201089v","article-title":"A tale of two isomerases: compact versus extended active sites in ketosteroid isomerase and phosphoglucose isomerase","volume":"50","author":"Somarowthu","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0190","series-title":"A Guide to Enzyme Catalysis and Protein Folding","first-page":"166","article-title":"Structure and mechanism in protein science","author":"Fersht","year":"1999"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0195","doi-asserted-by":"crossref","first-page":"30019","DOI":"10.1074\/jbc.M204485200","article-title":"Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase","volume":"277","author":"Pettersson","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0200","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.jmb.2010.01.023","article-title":"Structural basis for featuring of steroid isomerase activity in alpha class glutathione transferases","volume":"397","author":"Tars","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0205","doi-asserted-by":"crossref","first-page":"5790","DOI":"10.1021\/jp410810q","article-title":"Isomerization of \u03945-androstene-3,17-dione into \u03944-androstene-3,17-dione catalyzed by human glutathione transferase A3-3: a computational study identifies a dual role for glutathione","author":"Dourado","year":"2014","journal-title":"J. Phys. Chem. A"},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0210","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1021\/sb500242x","article-title":"Mapping of amino acid substitutions conferring herbicide resistance in wheat glutathione transferase","volume":"4","author":"Govindarajan","year":"2015","journal-title":"ACS Synth. Biol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0215","doi-asserted-by":"crossref","first-page":"3198","DOI":"10.1096\/fj.12-222745","article-title":"Human glutathione S-transferase A (GSTA) family genes are regulated by steroidogenic factor 1 (SF-1) and are involved in steroidogenesis","volume":"27","author":"Matsumura","year":"2013","journal-title":"FASEB J."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0220","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1038\/nrg3185","article-title":"Insights into the regulation of protein abundance from proteomic and transcriptomic analyses","volume":"13","author":"Vogel","year":"2012","journal-title":"Nat. Rev. Genet."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0225","first-page":"17","article-title":"cDNA Amplification using one-sided (anchored) PCR","author":"Dorit","year":"2001","journal-title":"Curr. Protoc. Mol. Biol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0230","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1128\/JB.186.3.595-600.2004","article-title":"Lysogeny at mid-twentieth century: p1, P2, and other experimental systems","volume":"186","author":"Bertani","year":"2004","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0235","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.ab.2011.01.041","article-title":"Experimental conditions affecting functional comparison of highly active glutathione transferases","volume":"413","author":"Fedulova","year":"2011","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jsbmb.2017.11.011_bib0240","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0022-4731(89)90296-3","article-title":"Human placental 3\u03b2-hydroxy-5-ene-steroid dehydrogenase and steroid 5\u2192 4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes","volume":"33","author":"Thomas","year":"1989","journal-title":"J. Steroid Biochem."}],"container-title":["The Journal of Steroid Biochemistry and Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960076017303606?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0960076017303606?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,18]],"date-time":"2025-10-18T00:00:48Z","timestamp":1760745648000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0960076017303606"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,4]]},"references-count":48,"alternative-id":["S0960076017303606"],"URL":"https:\/\/doi.org\/10.1016\/j.jsbmb.2017.11.011","relation":{},"ISSN":["0960-0760"],"issn-type":[{"value":"0960-0760","type":"print"}],"subject":[],"published":{"date-parts":[[2018,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Characterization of equine GST A3-3 as a steroid isomerase","name":"articletitle","label":"Article Title"},{"value":"The Journal of Steroid Biochemistry and Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jsbmb.2017.11.011","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}