{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T00:41:41Z","timestamp":1791333701392,"version":"4.3.1"},"reference-count":36,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2011,8,1]],"date-time":"2011-08-01T00:00:00Z","timestamp":1312156800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The International Journal of Biochemistry & Cell Biology"],"published-print":{"date-parts":[[2011,8]]},"DOI":"10.1016\/j.biocel.2011.04.002","type":"journal-article","created":{"date-parts":[[2011,4,18]],"date-time":"2011-04-18T13:06:13Z","timestamp":1303131973000},"page":"1079-1085","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"title":["Thiol-based redox signalling: Rust never sleeps"],"prefix":"10.1016","volume":"43","author":[{"given":"Merridee A.","family":"Wouters","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Siiri","family":"Iismaa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samuel W.","family":"Fan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naomi L.","family":"Haworth","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biocel.2011.04.002_bib0005","doi-asserted-by":"crossref","first-page":"19683","DOI":"10.1073\/pnas.0609283103","article-title":"Mechanism of allosteric regulation of transglutaminase 2 by GTP","volume":"103","author":"Begg","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.biocel.2011.04.002_bib0010","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1089\/ars.2009.2510","article-title":"Disulfides as redox switches: from molecular mechanisms to functional significance","volume":"12","author":"Wouters","year":"2010","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biocel.2011.04.002_bib0015","doi-asserted-by":"crossref","first-page":"4419","DOI":"10.2174\/092986709789712880","article-title":"Protein cysteine modifications: (1) medicinal chemistry for proteomics","volume":"16","author":"Nagahara","year":"2009","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.biocel.2011.04.002_bib0020","doi-asserted-by":"crossref","first-page":"51","DOI":"10.2174\/157016409787847448","article-title":"Oxidation proteomics: the role of thiol modifications","volume":"6","author":"Riederer","year":"2009","journal-title":"Curr Proteomics"},{"key":"10.1016\/j.biocel.2011.04.002_bib0025","series-title":"Proc Natl Acad Sci U S A","first-page":"444","article-title":"S-Nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds","author":"Stamler","year":"1992"},{"key":"10.1016\/j.biocel.2011.04.002_bib0030","doi-asserted-by":"crossref","first-page":"19773","DOI":"10.1074\/jbc.M701363200","article-title":"S-nitrosylation-induced conformational change in Blackfin tuna myoglobin","volume":"282","author":"Schreiter","year":"2007","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biocel.2011.04.002_bib0035","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1073\/pnas.0508412103","article-title":"SNOSID, a proteomic method for identification of cysteine S-nitrosylation sites in complex protein mixtures","volume":"103","author":"Hao","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.biocel.2011.04.002_bib0040","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.niox.2005.03.005","article-title":"The solid-state molecular structure of the S-nitroso derivative of l-cysteine ethyl ester hydrochloride","volume":"12","author":"Yi","year":"2005","journal-title":"Nitric Oxide"},{"key":"10.1016\/j.biocel.2011.04.002_bib0045","doi-asserted-by":"crossref","first-page":"16459","DOI":"10.1021\/bi9816711","article-title":"Crystal structure of the S-nitroso form of liganded human hemoglobin","volume":"37","author":"Chan","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.biocel.2011.04.002_bib0050","doi-asserted-by":"crossref","first-page":"1496","DOI":"10.1126\/science.1523409","article-title":"Oxidized redox state of glutathione in the endoplasmic reticulum","volume":"257","author":"Hwang","year":"1992","journal-title":"Science"},{"key":"10.1016\/j.biocel.2011.04.002_bib0055","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/S0969-2126(98)00074-4","article-title":"A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications","volume":"6","author":"Rossjohn","year":"1998","journal-title":"Structure"},{"key":"10.1016\/j.biocel.2011.04.002_bib0060","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/S0969-2126(01)00154-X","article-title":"Thioredoxin\u2014a fold for all reasons","volume":"3","author":"Martin","year":"1995","journal-title":"Structure"},{"key":"10.1016\/j.biocel.2011.04.002_bib0065","doi-asserted-by":"crossref","first-page":"2076","DOI":"10.1016\/j.febslet.2010.02.073","article-title":"Chloride intracellular channel 1 (CLIC1): sensor and effector during oxidative stress","volume":"584","author":"Averaimo","year":"2010","journal-title":"FEBS Lett"},{"key":"10.1016\/j.biocel.2011.04.002_bib0070","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1006\/jmbi.1994.1108","article-title":"The nuclear magnetie resonance solution structure of the mixed disulfide between Escherichia coli Glutaredoxin(C14S) and glutathione","volume":"235","author":"Bushweller","year":"1994","journal-title":"J Mol Biol"},{"key":"10.1016\/j.biocel.2011.04.002_bib0075","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S0014-5793(00)02022-6","article-title":"Crystal structure of S-glutathiolated carbonic anhydrase III","volume":"482","author":"Mallis","year":"2000","journal-title":"FEBS Lett"},{"key":"10.1016\/j.biocel.2011.04.002_bib0080","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S0092-8674(01)00300-2","article-title":"Structural basis of the redox switch in the OxyR transcription factor","volume":"105","author":"Choi","year":"2001","journal-title":"Cell"},{"key":"10.1016\/j.biocel.2011.04.002_bib0085","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1042\/BJ20070379","article-title":"Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I","volume":"407","author":"de\u00a0Hemptinne","year":"2007","journal-title":"Biochem J"},{"key":"10.1016\/j.biocel.2011.04.002_bib0090","doi-asserted-by":"crossref","first-page":"e10399","DOI":"10.1371\/journal.pone.0010399","article-title":"Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation","volume":"5","author":"Birkenmeier","year":"2010","journal-title":"PLoS ONE"},{"key":"10.1016\/j.biocel.2011.04.002_bib0095","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1038\/nature01680","article-title":"Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate","volume":"423","author":"Salmeen","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.biocel.2011.04.002_bib0100","doi-asserted-by":"crossref","first-page":"5204","DOI":"10.1074\/jbc.M110.172973","article-title":"Cell cycle sensing of oxidative stress in Saccharomyces cerevisiae by oxidation of a specific cysteine residue in the transcription factor Swi6p","volume":"286","author":"Chiu","year":"2011","journal-title":"J Biol Chem"},{"key":"10.1016\/j.biocel.2011.04.002_bib0105","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1071\/CH09456","article-title":"Estimating relative disulfide energies: an accurate ab initio potential energy surface","volume":"63","author":"Haworth","year":"2010","journal-title":"Aust J Chem"},{"key":"10.1016\/j.biocel.2011.04.002_bib0110","doi-asserted-by":"crossref","first-page":"484","DOI":"10.2174\/138920307782411464","article-title":"\u201cForbidden\u201d disulfides: their role as redox switches","volume":"8","author":"Wouters","year":"2007","journal-title":"Curr Protein Pept Sci"},{"key":"10.1016\/j.biocel.2011.04.002_bib0115","doi-asserted-by":"crossref","first-page":"1745","DOI":"10.1002\/pro.175","article-title":"Conformational changes in redox pairs of protein structures","volume":"18","author":"Fan","year":"2009","journal-title":"Protein Sci"},{"key":"10.1016\/j.biocel.2011.04.002_bib0120","doi-asserted-by":"crossref","first-page":"13661","DOI":"10.1021\/jp806465e","article-title":"Factors governing electron capture by small disulfide loops in two-cysteine peptides","volume":"112","author":"Dumont","year":"2008","journal-title":"J Phys Chem B"},{"key":"10.1016\/j.biocel.2011.04.002_bib0125","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1073\/pnas.97.2.623","article-title":"Specific chemical and structural damage to proteins produced by synchrotron radiation","volume":"97","author":"Weik","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.biocel.2011.04.002_bib0130","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1089\/ars.2008.2420","article-title":"Structural and functional characterization of the oxidoreductase \u03b1-DsbA1 from Wolbachia pipientis","volume":"11","author":"Kurz","year":"2009","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biocel.2011.04.002_bib0135","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1089\/ars.2006.8.1419","article-title":"Zinc coordination environments in proteins as redox sensors and signal transducers","volume":"8","author":"Maret","year":"2006","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biocel.2011.04.002_bib0140","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1126\/science.1158868","article-title":"Metamorphic proteins","volume":"320","author":"Murzin","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.biocel.2011.04.002_bib0145","first-page":"4609","article-title":"Cooperative DNA binding of the human HoxB5 (Hox-2.1) protein is under redox regulation in vitro","volume":"13","author":"Galang","year":"1993","journal-title":"Mol Cell Biol"},{"key":"10.1016\/j.biocel.2011.04.002_bib0150","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1089\/152308603770310338","article-title":"Formation of disulfide bond in p53 correlates with inhibition of DNA binding and tetramerization","volume":"5","author":"Sun","year":"2003","journal-title":"Antioxid Redox Signal"},{"key":"10.1016\/j.biocel.2011.04.002_bib0155","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1038\/ni815","article-title":"Disulfide exchange in domain 2 of CD4 is required for entry of HIV-I","volume":"3","author":"Matthias","year":"2002","journal-title":"Nat Immunol"},{"key":"10.1016\/j.biocel.2011.04.002_bib0160","doi-asserted-by":"crossref","first-page":"13932","DOI":"10.1073\/pnas.0606411103","article-title":"Disulfide isomerization switches tissue factor from coagulation to cell signaling","volume":"103","author":"Ahamed","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.biocel.2011.04.002_bib0165","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1126\/science.1105143","article-title":"Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme","volume":"307","author":"Xu","year":"2005","journal-title":"Science"},{"key":"10.1016\/j.biocel.2011.04.002_bib0170","doi-asserted-by":"crossref","first-page":"8506","DOI":"10.1073\/pnas.132142799","article-title":"All intermediates of the arsenate reductase mechanism, including an intramolecular dynamic disulfide cascade","volume":"99","author":"Messens","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.biocel.2011.04.002_bib0175","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1083\/jcb.200402120","article-title":"Monitoring disulfide bond formation in the eukaryotic cytosol","volume":"166","author":"Ostergaard","year":"2004","journal-title":"J Cell Biol"},{"key":"10.1016\/j.biocel.2011.04.002_bib0180","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1016\/j.jmb.2005.09.002","article-title":"Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically","volume":"353","author":"Lu","year":"2005","journal-title":"J Mol Biol"}],"container-title":["The International Journal of Biochemistry & Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1357272511000926?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1357272511000926?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T06:43:05Z","timestamp":1761201785000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1357272511000926"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,8]]},"references-count":36,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2011,8]]}},"alternative-id":["S1357272511000926"],"URL":"https:\/\/doi.org\/10.1016\/j.biocel.2011.04.002","relation":{},"ISSN":["1357-2725"],"issn-type":[{"value":"1357-2725","type":"print"}],"subject":[],"published":{"date-parts":[[2011,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Thiol-based redox signalling: Rust never sleeps","name":"articletitle","label":"Article Title"},{"value":"The International Journal of Biochemistry & Cell Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biocel.2011.04.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Crown copyright \u00a9 2011 Published by Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}