{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T04:38:46Z","timestamp":1790483926670,"version":"4.1.0"},"reference-count":39,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicology"],"published-print":{"date-parts":[[2006,8]]},"DOI":"10.1016\/j.tox.2006.04.054","type":"journal-article","created":{"date-parts":[[2006,5,10]],"date-time":"2006-05-10T11:16:05Z","timestamp":1147259765000},"page":"1-11","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":38,"title":["Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme"],"prefix":"10.1016","volume":"225","author":[{"given":"Ingrid","family":"Billaut-Laden","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Delphine","family":"Allorge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aur\u00e9lie","family":"Crunelle-Thibaut","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emmanuel","family":"Rat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christelle","family":"Cauffiez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dany","family":"Chevalier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicole","family":"Houdret","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Marc","family":"Lo-Guidice","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Franck","family":"Broly","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.tox.2006.04.054_bib1","first-page":"56","article-title":"Cloning and expression of human liver rhodanese cDNA","volume":"231","author":"Aita","year":"1997","journal-title":"BBRC"},{"key":"10.1016\/j.tox.2006.04.054_bib2","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1051\/vetres:2001110","article-title":"Tissue and intracellular distribution of rhodanese and mercaptopyruvate sulphurtransferase in ruminants and birds","volume":"32","author":"Al-Qarawi","year":"2001","journal-title":"Vet. Res."},{"key":"10.1016\/j.tox.2006.04.054_bib3","doi-asserted-by":"crossref","first-page":"1465","DOI":"10.3382\/ps.0731465","article-title":"Rhodanese (thiosulfate: cyanide sulfurtransferase) distribution in the digestive tract of chicken","volume":"73","author":"Aminlari","year":"1994","journal-title":"Poult. Sci."},{"key":"10.1016\/j.tox.2006.04.054_bib4","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1006\/taap.1994.1009","article-title":"The cyanide-metabolizing enzyme rhodanese in different parts of the respiratory systems of sheep and dog","volume":"124","author":"Aminlari","year":"1994","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.tox.2006.04.054_bib5","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/S1096-4959(02)00005-2","article-title":"Rhodanese distribution in porcine (Sus scrofa) tissues","volume":"132","author":"Aminlari","year":"2002","journal-title":"Comp. Biochem. Physiol. B. Biochem. Mol. Biol."},{"key":"10.1016\/j.tox.2006.04.054_bib6","first-page":"369","article-title":"Seeking a better job for an underemployed enzyme: rhodanese","volume":"11","author":"Cerletti","year":"1986","journal-title":"TIBS"},{"key":"10.1016\/j.tox.2006.04.054_bib7","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1177\/153537020322800413","article-title":"Gastrointestinal and microbial responses to sulfate-supplemented drinking water in mice","volume":"228","author":"Deplancke","year":"2003","journal-title":"Exp. Biol. Med."},{"key":"10.1016\/j.tox.2006.04.054_bib8","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1007\/s004390100505","article-title":"Nomenclature for the description of human sequence variations","volume":"109","author":"Den Dunnen","year":"2001","journal-title":"Hum. Genet."},{"key":"10.1016\/j.tox.2006.04.054_bib9","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/S0006-2952(01)00657-8","article-title":"Oxidation of hydrogen sulfide and methanethiol to thiosulfate by rat tissues: a specialized function of the colonic mucosa","volume":"62","author":"Furne","year":"2001","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.tox.2006.04.054_bib10","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1093\/nar\/20.6.1425","article-title":"Improved method for high efficiency transformation of intact yeast cells","volume":"20","author":"Gietz","year":"1992","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.tox.2006.04.054_bib11","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1002\/1097-4547(20000901)61:5<570::AID-JNR12>3.0.CO;2-V","article-title":"Endogenous generation of cyanide in neuronal tissue: involvement of a peroxidase system","volume":"61","author":"Gunasekar","year":"2000","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.tox.2006.04.054_bib12","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/0003-9861(78)90189-3","article-title":"Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidney","volume":"185","author":"Jarabak","year":"1978","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.tox.2006.04.054_bib13","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1111\/j.1600-0404.1985.tb00857.x","article-title":"Cyanide metabolism in motor neuron disease","volume":"72","author":"Kato","year":"1985","journal-title":"Acta Neurol. Scand."},{"key":"10.1016\/j.tox.2006.04.054_bib14","first-page":"373","article-title":"The activity of cysteine desulphhydrase and rhodanase in animal tissues","volume":"9","author":"Koj","year":"1962","journal-title":"Acta Biochim. Pol."},{"key":"10.1016\/j.tox.2006.04.054_bib15","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1111\/j.1572-0241.1998.083_c.x","article-title":"Fecal hydrogen sulfide production in ulcerative colitis","volume":"93","author":"Levine","year":"1998","journal-title":"Am. J. Gastroenterol."},{"key":"10.1016\/j.tox.2006.04.054_bib16","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1172\/JCI7712","article-title":"Detoxification of hydrogen sulfide and methanethiol in the cecal mucosa","volume":"104","author":"Levitt","year":"1999","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.tox.2006.04.054_bib17","doi-asserted-by":"crossref","first-page":"8220","DOI":"10.1016\/S0021-9258(17)37182-X","article-title":"The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg186 or Lys249","volume":"269","author":"Luo","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tox.2006.04.054_bib18","first-page":"245","article-title":"Conversion of the \u03b1-keto analog of cysteine to pyruvate and sulfur","volume":"12","author":"Meister","year":"1953","journal-title":"Fed. Proc."},{"key":"10.1016\/j.tox.2006.04.054_bib19","doi-asserted-by":"crossref","first-page":"16230","DOI":"10.1074\/jbc.270.27.16230","volume":"270","author":"Nagahara","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tox.2006.04.054_bib20","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s004180050286","article-title":"Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis","volume":"110","author":"Nagahara","year":"1998","journal-title":"Histochem. Cell. Biol."},{"key":"10.1016\/j.tox.2006.04.054_bib21","first-page":"1277","article-title":"Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification","volume":"14","author":"Nagahara","year":"1999","journal-title":"Histol. Histopathol."},{"key":"10.1016\/j.tox.2006.04.054_bib22","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.bbaexp.2004.09.007","article-title":"A point mutation in a silencer module reduces the promoter activity for the human mercaptopyruvate sulfurtransferase","volume":"1680","author":"Nagahara","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.tox.2006.04.054_bib23","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/S1096-4959(03)00003-4","article-title":"Distribution of rhodanese in tissues of goat (Capra hircus)","volume":"134","author":"Nazifi","year":"2003","journal-title":"Comp. Biochem. Physiol. B. Biochem. Mol. Biol."},{"key":"10.1016\/j.tox.2006.04.054_bib24","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1002\/jbt.2570080202","article-title":"Immobilized rhodanese: some aspects of anion inhibition kinetics and modulation by cations","volume":"8","author":"Nok","year":"1993","journal-title":"J. Biochem. Toxicol."},{"key":"10.1016\/j.tox.2006.04.054_bib25","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1136\/gut.50.2.201","article-title":"Mucosal protection against sulphide: importance of the enzyme rhodanese","volume":"50","author":"Picton","year":"2002","journal-title":"Gut"},{"key":"10.1016\/j.tox.2006.04.054_bib26","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1038\/273124a0","article-title":"The covalent and tertiary structure of bovine liver rhodanese","volume":"273","author":"Ploegman","year":"1978","journal-title":"Nature"},{"key":"10.1016\/j.tox.2006.04.054_bib27","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0076-6879(96)72008-6","article-title":"Yeast expression of animal and plant P450s in optimized redox environments","volume":"272","author":"Pompon","year":"1996","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.tox.2006.04.054_bib28","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1016\/0016-5085(93)91016-B","article-title":"Reducing sulfur compounds of the colon impair colonocyte nutrition: implications for ulcerative colitis","volume":"104","author":"Roediger","year":"1993","journal-title":"Gastroenterology"},{"key":"10.1016\/j.tox.2006.04.054_bib29","doi-asserted-by":"crossref","first-page":"3990","DOI":"10.3748\/wjg.v11.i26.3990","article-title":"Hydrogen sulfide protects colon cancer cells from chemopreventative agent \u03b2-phenylethyl isotiocyanate induced apoptosis","volume":"11","author":"Rose","year":"2005","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.tox.2006.04.054_bib30","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1016\/S0021-9258(19)42997-9","article-title":"An expanded mechanism for rhodanese catalysis","volume":"249","author":"Schlesinger","year":"1974","journal-title":"J Biol Chem"},{"key":"10.1016\/j.tox.2006.04.054_bib31","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.3891\/acta.chem.scand.07-1129","article-title":"Crystalline rhodanese. Purification and physiochemical examination","volume":"7","author":"S\u00f6rbo","year":"1953","journal-title":"Acta Chen. Scand."},{"key":"10.1016\/j.tox.2006.04.054_bib32","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/0006-3002(57)90201-9","article-title":"Enzymic transfer of sulfur from mercaptopyruvate to sulfate or sulfinates","volume":"24","author":"S\u00f6rbo","year":"1957","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.tox.2006.04.054_bib33","series-title":"Cyanide in Biology","first-page":"371","article-title":"The role of myeloperoxidase in phagocytosis, with special regard to HCN formation","author":"Stelmaszynska","year":"1981"},{"key":"10.1016\/j.tox.2006.04.054_bib34","doi-asserted-by":"crossref","first-page":"5967","DOI":"10.1016\/S0021-9258(19)39277-4","article-title":"The detection of kinetic intermediate(s) during refolding of rhodanese","volume":"265","author":"Tandon","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tox.2006.04.054_bib35","doi-asserted-by":"crossref","first-page":"27841","DOI":"10.1074\/jbc.273.43.27841","article-title":"Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression","volume":"273","author":"Trevino","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.tox.2006.04.054_bib36","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1248\/jhs.46.343","article-title":"Cyanide and thiocyanate levels in blood and saliva of healthy adult volunteers","volume":"46","author":"Tsuge","year":"2000","journal-title":"J. Health Sci."},{"key":"10.1016\/j.tox.2006.04.054_bib37","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/1357-2725(94)00089-T","article-title":"Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice","volume":"27","author":"Vazquez","year":"1995","journal-title":"Int. J. Biochem. Cell. Biol."},{"key":"10.1016\/j.tox.2006.04.054_bib38","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1096\/fj.02-0211hyp","article-title":"Two's company, three's a crowd: can H2S be the third endogenous gaseous transmitter?","volume":"16","author":"Wang","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.tox.2006.04.054_bib39","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0021-9258(19)77248-2","article-title":"B-mercaptopyruvate, a substrate for rhodanese","volume":"205","author":"Wood","year":"1953","journal-title":"J. Biol. Chem."}],"container-title":["Toxicology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300483X06002447?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300483X06002447?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,3]],"date-time":"2025-10-03T22:54:42Z","timestamp":1759532082000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300483X06002447"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,8]]},"references-count":39,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2006,8]]}},"alternative-id":["S0300483X06002447"],"URL":"https:\/\/doi.org\/10.1016\/j.tox.2006.04.054","relation":{},"ISSN":["0300-483X"],"issn-type":[{"value":"0300-483X","type":"print"}],"subject":[],"published":{"date-parts":[[2006,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme","name":"articletitle","label":"Article Title"},{"value":"Toxicology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.tox.2006.04.054","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2006 Elsevier Ireland Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}