{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T05:36:30Z","timestamp":1787981790947,"version":"build-2784847793"},"reference-count":48,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T00:00:00Z","timestamp":1759276800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100013209","name":"Hellenic Foundation for Research and Innovation","doi-asserted-by":"publisher","award":["HFRI-FM17-886"],"award-info":[{"award-number":["HFRI-FM17-886"]}],"id":[{"id":"10.13039\/501100013209","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Nitric Oxide"],"published-print":{"date-parts":[[2025,10]]},"DOI":"10.1016\/j.niox.2025.06.004","type":"journal-article","created":{"date-parts":[[2025,6,20]],"date-time":"2025-06-20T19:30:49Z","timestamp":1750447849000},"page":"67-75","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"special_numbering":"C","title":["3-mercaptopyruvate sulfurtransferase resides on the inner mitochondrial membrane"],"prefix":"10.1016","volume":"158","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3253-2250","authenticated-orcid":false,"given":"Antonia","family":"Katsouda","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eleni","family":"Vasilaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Markos","family":"Fountoulakis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ioanna","family":"Tremi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophia","family":"Havaki","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vassilios","family":"Myrianthopoulos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vassilis G.","family":"Gorgoulis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emmanuel","family":"Mikros","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4253-5930","authenticated-orcid":false,"given":"Andreas","family":"Papapetropoulos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.niox.2025.06.004_bib1","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1152\/physrev.00028.2021","article-title":"Physiological roles of hydrogen sulfide in mammalian cells, tissues, and organs","volume":"103","author":"Cirino","year":"2023","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.niox.2025.06.004_bib2","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1124\/pr.117.014050","article-title":"International union of basic and clinical pharmacology. CII: pharmacological modulation of H2S levels: H2s donors and H2S biosynthesis inhibitors","volume":"69","author":"Szabo","year":"2017","journal-title":"Pharmacol. Rev."},{"key":"10.1016\/j.niox.2025.06.004_bib3","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1089\/ars.2013.5309","article-title":"Production and physiological effects of hydrogen sulfide","volume":"20","author":"Kimura","year":"2014","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.niox.2025.06.004_bib4","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1111\/bph.14100","article-title":"Multiple role of 3-mercaptopyruvate sulfurtransferase: antioxidative function, H2S and polysulfide production and possible SOx production","volume":"175","author":"Nagahara","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.niox.2025.06.004_bib5","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1515\/hsz-2020-0249","article-title":"3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking","volume":"402","author":"Pedre","year":"2021","journal-title":"Biol. Chem."},{"key":"10.1016\/j.niox.2025.06.004_bib6","doi-asserted-by":"crossref","DOI":"10.1021\/acs.chemrev.7b00205","article-title":"Chemical biology of H2S signaling through persulfidation","author":"Filipovic","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.niox.2025.06.004_bib7","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1042\/BJ20110841","article-title":"Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide","volume":"439","author":"Mikami","year":"2011","journal-title":"Biochem. J."},{"key":"10.1016\/j.niox.2025.06.004_bib8","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1089\/ars.2008.2253","article-title":"3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain","volume":"11","author":"Shibuya","year":"2009","journal-title":"Antioxidants Redox Signal."},{"key":"10.1016\/j.niox.2025.06.004_bib9","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M114.605733","article-title":"Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans","author":"Fr\u00e4sdorf","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2025.06.004_bib10","doi-asserted-by":"crossref","first-page":"27395","DOI":"10.1074\/jbc.271.44.27395","article-title":"Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase: cDNA cloning, overexpression, and site- directed mutagenesis","volume":"271","author":"Nagahara","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2025.06.004_bib11","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1111\/bph.14574","article-title":"3-Mercaptopyruvate sulfurtransferase supports endothelial cell angiogenesis and bioenergetics","volume":"177","author":"Abdollahi Govar","year":"2020","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.niox.2025.06.004_bib12","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2018.11.034","article-title":"Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)\u2014hydrogen sulfide (H2S) pathway in cancer cells","volume":"154","author":"Augsburger","year":"2020","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.niox.2025.06.004_bib13","doi-asserted-by":"crossref","DOI":"10.1084\/jem.20211894","article-title":"MPST sulfurtransferase maintains mitochondrial protein import and cellular bioenergetics to attenuate obesity","volume":"219","author":"Katsouda","year":"2022","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.niox.2025.06.004_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2017.09.023","article-title":"Reduced adipose tissue H2S in obesity","author":"Katsouda","year":"2018","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.niox.2025.06.004_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.bcp.2020.113833","article-title":"Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase","volume":"176","author":"Peleli","year":"2020","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.niox.2025.06.004_bib16","doi-asserted-by":"crossref","DOI":"10.1038\/s41392-023-01547-9","article-title":"Mitochondrial dynamics in health and disease: mechanisms and potential targets","volume":"8","author":"Chen","year":"2023","journal-title":"Signal Transduct. Targeted Ther."},{"key":"10.1016\/j.niox.2025.06.004_bib17","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1016\/j.cell.2012.02.035","article-title":"Mitochondria: in sickness and in health","volume":"148","author":"Nunnari","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib18","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1146\/annurev-genom-082509-141720","article-title":"The mitochondrial proteome and human disease","volume":"11","author":"Calvo","year":"2010","journal-title":"Annu. Rev. Genom. Hum. Genet."},{"key":"10.1016\/j.niox.2025.06.004_bib19","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/nrm1426","article-title":"Mitochondrial import and the twin-pore translocase","volume":"5","author":"Rehling","year":"2004","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.niox.2025.06.004_bib20","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1016\/j.molcel.2023.02.020","article-title":"Mitochondrial protein transport: versatility of translocases and mechanisms","volume":"83","author":"Busch","year":"2023","journal-title":"Mol. Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.15252\/embj.2021109519","article-title":"Widespread use of unconventional targeting signals in mitochondrial ribosome proteins","volume":"41","author":"Bykov","year":"2022","journal-title":"EMBO J."},{"key":"10.1016\/j.niox.2025.06.004_bib22","doi-asserted-by":"crossref","first-page":"948","DOI":"10.1038\/sj.embor.embor937","article-title":"Finding the right organelle. Targeting signals in mitochondrial outer-membrane proteins","volume":"4","author":"Rapaport","year":"2003","journal-title":"EMBO Rep."},{"key":"10.1016\/j.niox.2025.06.004_bib23","doi-asserted-by":"crossref","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","author":"Nagahara","year":"1998","journal-title":"Histochem. Cell Biol."},{"key":"10.1016\/j.niox.2025.06.004_bib24","doi-asserted-by":"crossref","first-page":"6299","DOI":"10.1074\/jbc.RA120.012616","article-title":"Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations","volume":"295","author":"Yadav","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2025.06.004_bib25","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1111\/j.1365-2818.1992.tb03253.x","article-title":"An appraisal of low\u2010temperature embedding by progressive lowering of temperature into lowicryl HM20 for immunocytochemical studies","volume":"168","author":"Robertson","year":"1992","journal-title":"J Microsc"},{"key":"10.1016\/j.niox.2025.06.004_bib26","series-title":"Proceedings of the 2006 ACM\/IEEE Conference on Supercomputing","first-page":"84","article-title":"Scalable algorithms for molecular dynamics simulations on commodity clusters, SC \u201906","author":"Bowers","year":"2006"},{"key":"10.1016\/j.niox.2025.06.004_bib27","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/S0092-8674(00)80691-1","article-title":"Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20","volume":"100","author":"Abe","year":"2000","journal-title":"Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib28","doi-asserted-by":"crossref","first-page":"14406","DOI":"10.1073\/pnas.1408401111","article-title":"Pharmacologic rescue of an enzyme-trafficking defect in primary hyperoxaluria 1","volume":"111","author":"Miyata","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.niox.2025.06.004_bib29","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.devcel.2013.03.006","article-title":"A small molecule inhibitor of redox-regulated protein translocation into mitochondria","volume":"25","author":"Dabir","year":"2013","journal-title":"Dev. Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib30","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.cell.2009.07.045","article-title":"Global analysis of the mitochondrial N-Proteome identifies a processing peptidase critical for protein stability","volume":"139","author":"V\u00f6gtle","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib31","series-title":"Methods Cell Biol","first-page":"441","article-title":"Manipulation of mitochondrial genes and mtDNA heteroplasmy","author":"Bacman","year":"2020"},{"key":"10.1016\/j.niox.2025.06.004_bib32","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1134\/S0026893308040195","article-title":"Radius of gyration as an indicator of protein structure compactness","volume":"42","author":"Lobanov","year":"2008","journal-title":"Mol. Biol."},{"key":"10.1016\/j.niox.2025.06.004_bib33","doi-asserted-by":"crossref","first-page":"41566","DOI":"10.1074\/jbc.M304940200","article-title":"Proteomic analysis of the mouse liver mitochondrial inner membrane","volume":"278","author":"Da Cruz","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2025.06.004_bib34","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1161\/01.RES.72.4.921","article-title":"Mutation of N-myristoylation site converts endothelial cell nitric oxide synthase from a membrane to a cytosolic protein","volume":"72","author":"Sessa","year":"1993","journal-title":"Circ. Res."},{"key":"10.1016\/j.niox.2025.06.004_bib35","doi-asserted-by":"crossref","first-page":"W401","DOI":"10.1093\/nar\/gkv485","article-title":"The TOPCONS web server for consensus prediction of membrane protein topology and signal peptides","volume":"43","author":"Tsirigos","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.niox.2025.06.004_bib36","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0284541","article-title":"MTSviewer: a database to visualize mitochondrial targeting sequences, cleavage sites, and mutations on protein structures","volume":"18","author":"Bayne","year":"2023","journal-title":"PLoS One"},{"key":"10.1016\/j.niox.2025.06.004_bib37","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/abbi.1998.0723","article-title":"Trypsin cleavage of human cystathionine beta-synthase into an evolutionarily conserved active core: structural and functional consequences","volume":"355","author":"Kery","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.niox.2025.06.004_bib38","doi-asserted-by":"crossref","first-page":"16802","DOI":"10.1074\/jbc.M212376200","article-title":"Tumor necrosis factor-alpha-induced targeted proteolysis of cystathionine beta-synthase modulates redox homeostasis","volume":"278","author":"Zou","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.niox.2025.06.004_bib39","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1002\/j.1460-2075.1986.tb04363.x","article-title":"A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers","volume":"5","author":"Roise","year":"1986","journal-title":"EMBO J."},{"key":"10.1016\/j.niox.2025.06.004_bib40","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/j.cell.2009.08.005","article-title":"Importing mitochondrial proteins: machineries and mechanisms","volume":"138","author":"Chacinska","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib41","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/0092-8674(88)90096-7","article-title":"Mitochondrial protein import: identification of processing peptidase and of PEP, a processing enhancing protein","volume":"53","author":"Hawlitschek","year":"1988","journal-title":"Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib42","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1091\/mbc.e11-02-0169","article-title":"Mitochondrial protein turnover: role of the precursor intermediate peptidase Oct1 in protein stabilization","volume":"22","author":"V\u00f6gtle","year":"2011","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib43","doi-asserted-by":"crossref","first-page":"1747","DOI":"10.1126\/science.1080945","article-title":"Protein insertion into the mitochondrial inner membrane by a twin-pore translocase","volume":"299","author":"Rehling","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.niox.2025.06.004_bib44","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1016\/j.cell.2008.01.028","article-title":"Dissecting membrane insertion of mitochondrial \u03b2-Barrel proteins","volume":"132","author":"Kutik","year":"2008","journal-title":"Cell"},{"key":"10.1016\/j.niox.2025.06.004_bib45","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1126\/science.aah6834","article-title":"Membrane protein insertion through a mitochondrial \u03b2-barrel gate","volume":"359","author":"H\u00f6hr","year":"2018","journal-title":"Science"},{"key":"10.1016\/j.niox.2025.06.004_bib46","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/s41586-019-1680-7","article-title":"Structure of the mitochondrial import gate reveals distinct preprotein paths","volume":"575","author":"Araiso","year":"2019","journal-title":"Nature"},{"key":"10.1016\/j.niox.2025.06.004_bib47","doi-asserted-by":"crossref","first-page":"3735","DOI":"10.1038\/sj.emboj.7600389","article-title":"Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins","volume":"23","author":"Chacinska","year":"2004","journal-title":"EMBO J."},{"key":"10.1016\/j.niox.2025.06.004_bib48","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/j.molcel.2010.01.017","article-title":"Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione","volume":"37","author":"Bien","year":"2010","journal-title":"Mol. Cell"}],"container-title":["Nitric Oxide"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S108986032500059X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S108986032500059X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T12:35:23Z","timestamp":1778589323000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S108986032500059X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,10]]},"references-count":48,"alternative-id":["S108986032500059X"],"URL":"https:\/\/doi.org\/10.1016\/j.niox.2025.06.004","relation":{},"ISSN":["1089-8603"],"issn-type":[{"value":"1089-8603","type":"print"}],"subject":[],"published":{"date-parts":[[2025,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"3-mercaptopyruvate sulfurtransferase resides on the inner mitochondrial membrane","name":"articletitle","label":"Article Title"},{"value":"Nitric Oxide","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.niox.2025.06.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}