{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T19:12:58Z","timestamp":1791141178530,"version":"4.1.0"},"reference-count":119,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2012,4,1]],"date-time":"2012-04-01T00:00:00Z","timestamp":1333238400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2012,4,1]],"date-time":"2012-04-01T00:00:00Z","timestamp":1333238400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,9,9]],"date-time":"2020-09-09T00:00:00Z","timestamp":1599609600000},"content-version":"vor","delay-in-days":3083,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["mcponline.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular & Cellular Proteomics"],"published-print":{"date-parts":[[2012,4]]},"DOI":"10.1074\/mcp.r111.013037","type":"journal-article","created":{"date-parts":[[2011,12,9]],"date-time":"2011-12-09T02:29:07Z","timestamp":1323397747000},"page":"R111.013037","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":84,"title":["Regulatory Control or Oxidative Damage? Proteomic Approaches to Interrogate the Role of Cysteine Oxidation Status in Biological Processes"],"prefix":"10.1016","volume":"11","author":[{"given":"Jason M.","family":"Held","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bradford W.","family":"Gibson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/mcp.R111.013037_bib1","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1126\/science.284.5414.651","article-title":"Fas-induced caspase denitrosylation","volume":"284","author":"Mannick","year":"1999","journal-title":"Science"},{"key":"10.1074\/mcp.R111.013037_bib2","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1126\/science.1158265","article-title":"Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins","volume":"320","author":"Benhar","year":"2008","journal-title":"Science"},{"key":"10.1074\/mcp.R111.013037_bib3","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/j.cub.2011.01.008","article-title":"Redox-responsive zinc finger fidelity switch in homing endonuclease and intron promiscuity in oxidative stress","volume":"21","author":"Robbins","year":"2011","journal-title":"Curr. Biol"},{"key":"10.1074\/mcp.R111.013037_bib4","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0006-291X(02)02770-5","article-title":"Multiple roles of cysteine in biocatalysis","volume":"300","author":"Giles","year":"2003","journal-title":"Biochem. Biophys. Res. Commun"},{"key":"10.1074\/mcp.R111.013037_bib5","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1073\/pnas.0812149106","article-title":"Quantifying the global cellular thiol-disulfide status","volume":"106","author":"Hansen","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib6","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1016\/j.cell.2005.04.011","article-title":"A disulfide relay system in the intermembrane space of mitochondria that mediates protein import","volume":"121","author":"Mesecke","year":"2005","journal-title":"Cell"},{"key":"10.1074\/mcp.R111.013037_bib7","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1016\/S1097-2765(02)00696-2","article-title":"The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum","volume":"10","author":"Tu","year":"2002","journal-title":"Mol. Cell"},{"key":"10.1074\/mcp.R111.013037_bib8","first-page":"43","article-title":"Reaction rates of superoxide radicals with the essential amino acids","volume":"65","author":"Bielski","year":"1978","journal-title":"Ciba Found Symp"},{"key":"10.1074\/mcp.R111.013037_bib9","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/S0891-5849(00)00506-2","article-title":"Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate","volume":"30","author":"Peskin","year":"2001","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib10","doi-asserted-by":"crossref","first-page":"7094","DOI":"10.1021\/ja00335a038","article-title":"Kinetics of ozonation. 2. Amino acids and model compounds in water and comparisons to rates in nonpolar solvents","volume":"106","author":"Pryor","year":"1984","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/mcp.R111.013037_bib11","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1002\/jps.20253","article-title":"Kinetics and mechanism of the reaction of cysteine and hydrogen peroxide in aqueous solution","volume":"94","author":"Luo","year":"2005","journal-title":"J. Pharm. Sci"},{"key":"10.1074\/mcp.R111.013037_bib12","doi-asserted-by":"crossref","first-page":"4244","DOI":"10.1016\/S0021-9258(20)64313-7","article-title":"Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide","volume":"266","author":"Radi","year":"1991","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib13","doi-asserted-by":"crossref","first-page":"4799","DOI":"10.1021\/bi035946a","article-title":"Kinetic analysis of the reactions of hypobromous acid with protein components: implications for cellular damage and use of 3-bromotyrosine as a marker of oxidative stress","volume":"43","author":"Pattison","year":"2004","journal-title":"Biochemistry"},{"key":"10.1074\/mcp.R111.013037_bib14","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1080\/09553007914550831","article-title":"Reaction of azide radicals with amino acids and proteins","volume":"36","author":"Land","year":"1979","journal-title":"Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med"},{"key":"10.1074\/mcp.R111.013037_bib15","doi-asserted-by":"crossref","first-page":"278","DOI":"10.2307\/3573266","article-title":"Selective free radical reactions with proteins and enzymes: reactions of inorganic radical anions with amino acids","volume":"49","author":"Adams","year":"1972","journal-title":"Radiat. Res"},{"key":"10.1074\/mcp.R111.013037_bib16","doi-asserted-by":"crossref","first-page":"96","DOI":"10.2307\/3573375","article-title":"Transient radicals of DNA bases by pulse radiolysis. Effects of cysteine and cysteamine as radioprotectors","volume":"49","author":"Nucifora","year":"1972","journal-title":"Radiat. Res"},{"key":"10.1074\/mcp.R111.013037_bib17","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/1011-1344(91)80008-6","article-title":"Activity of thiols as singlet molecular oxygen quenchers","volume":"9","author":"Devasagayam","year":"1991","journal-title":"J. Photochem. Photobiol. B"},{"key":"10.1074\/mcp.R111.013037_bib18","doi-asserted-by":"crossref","first-page":"1882","DOI":"10.1126\/science.1130481","article-title":"Cell signaling. H2O2, a necessary evil for cell signaling","volume":"312","author":"Rhee","year":"2006","journal-title":"Science"},{"key":"10.1074\/mcp.R111.013037_bib19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.freeradbiomed.2008.03.011","article-title":"Redox-based regulation of signal transduction: principles, pitfalls, and promises","volume":"45","author":"Janssen-Heininger","year":"2008","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib20","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1074\/jbc.274.2.842","article-title":"Kinetics of peroxynitrite reaction with amino acids and human serum albumin","volume":"274","author":"Alvarez","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib21","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1021\/tx0155451","article-title":"Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds","volume":"14","author":"Pattison","year":"2001","journal-title":"Chem. Res. Toxicol"},{"key":"10.1074\/mcp.R111.013037_bib22","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1039\/b307576c","article-title":"Reactive species formed on proteins exposed to singlet oxygen","volume":"3","author":"Davies","year":"2004","journal-title":"Photochem. Photobiol. Sci"},{"key":"10.1074\/mcp.R111.013037_bib23","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.bbapap.2004.08.007","article-title":"The oxidative environment and protein damage","volume":"1703","author":"Davies","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/mcp.R111.013037_bib24","doi-asserted-by":"crossref","first-page":"1465","DOI":"10.1111\/j.1742-4658.2010.07576.x","article-title":"Cysteine residues exposed on protein surfaces are the dominant intramitochondrial thiol and may protect against oxidative damage","volume":"277","author":"Requejo","year":"2010","journal-title":"FEBS J"},{"key":"10.1074\/mcp.R111.013037_bib25","doi-asserted-by":"crossref","first-page":"ra72","DOI":"10.1126\/scisignal.2000464","article-title":"H2S signals through protein S-sulfhydration","volume":"2","author":"Mustafa","year":"2009","journal-title":"Sci. Signal"},{"key":"10.1074\/mcp.R111.013037_bib26","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1038\/nature02075","article-title":"ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin","volume":"425","author":"Biteau","year":"2003","journal-title":"Nature"},{"key":"10.1074\/mcp.R111.013037_bib27","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1126\/science.1080273","article-title":"Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation","volume":"300","author":"Woo","year":"2003","journal-title":"Science"},{"key":"10.1074\/mcp.R111.013037_bib28","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/0891-5849(94)90008-6","article-title":"Cellular reducing equivalents and oxidative stress","volume":"17","author":"Kehrer","year":"1994","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib29","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1038\/nchembio.85","article-title":"Reconciling the chemistry and biology of reactive oxygen species","volume":"4","author":"Winterbourn","year":"2008","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/mcp.R111.013037_bib30","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1089\/ars.2010.3561","article-title":"Redox biology: computational approaches to the investigation of functional cysteine residues","volume":"15","author":"Marino","year":"2011","journal-title":"Antioxid. Redox. Signal"},{"key":"10.1074\/mcp.R111.013037_bib31","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.freeradbiomed.2008.05.004","article-title":"Thiol chemistry and specificity in redox signaling","volume":"45","author":"Winterbourn","year":"2008","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib32","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/S0092-8674(02)01048-6","article-title":"A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation","volume":"111","author":"Delaunay","year":"2002","journal-title":"Cell"},{"key":"10.1074\/mcp.R111.013037_bib33","doi-asserted-by":"crossref","first-page":"8875","DOI":"10.1073\/pnas.0503251102","article-title":"A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway","volume":"102","author":"Vivancos","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib34","doi-asserted-by":"crossref","first-page":"6704","DOI":"10.1016\/S0021-9258(18)48299-3","article-title":"Identification and reactivity of the catalytic site of pig liver thioltransferase","volume":"262","author":"Gan","year":"1987","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib35","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1016\/0092-8674(95)90210-4","article-title":"Why is DsbA such an oxidizing disulfide catalyst?","volume":"83","author":"Grauschopf","year":"1995","journal-title":"Cell"},{"key":"10.1074\/mcp.R111.013037_bib36","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1016\/j.bbagen.2009.06.003","article-title":"Is the oxidative stress theory of aging dead?","volume":"1790","author":"P\u00e9rez","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/mcp.R111.013037_bib37","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/ng1295-376","article-title":"Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase","volume":"11","author":"Li","year":"1995","journal-title":"Nat. Genet"},{"key":"10.1074\/mcp.R111.013037_bib38","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1212\/WNL.53.6.1239","article-title":"Mice lacking cytosolic copper\/zinc superoxide dismutase display a distinctive motor axonopathy","volume":"53","author":"Shefner","year":"1999","journal-title":"Neurology"},{"key":"10.1074\/mcp.R111.013037_bib39","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/S0002-9440(10)65162-0","article-title":"Hindlimb motor neurons require Cu\/Zn superoxide dismutase for maintenance of neuromuscular junctions","volume":"155","author":"Flood","year":"1999","journal-title":"Am. J. Pathol"},{"key":"10.1074\/mcp.R111.013037_bib40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.canlet.2006.10.029","article-title":"Dual role of hydrogen peroxide in cancer: possible relevance to cancer chemoprevention and therapy","volume":"252","author":"L\u00f3pez-L\u00e1zaro","year":"2007","journal-title":"Cancer Lett"},{"key":"10.1074\/mcp.R111.013037_bib41","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/S0003-2697(03)00296-3","article-title":"Essential cysteine-alkylation strategies to monitor structurally altered estrogen receptor as found in oxidant-stressed breast cancers","volume":"320","author":"Meza","year":"2003","journal-title":"Anal. Biochem"},{"key":"10.1074\/mcp.R111.013037_bib42","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.ijms.2004.06.004","article-title":"Determining cysteine oxidation status using differential alkylation","volume":"236","author":"Schilling","year":"2004","journal-title":"Int. J. Mass Spectrom"},{"key":"10.1074\/mcp.R111.013037_bib43","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0076-6879(98)90007-6","article-title":"Disulfide bond catalysts in Escherichia coli","volume":"290","author":"Zander","year":"1998","journal-title":"Methods Enzymol"},{"key":"10.1074\/mcp.R111.013037_bib44","doi-asserted-by":"crossref","first-page":"5157","DOI":"10.1093\/emboj\/19.19.5157","article-title":"H2O2 sensing through oxidation of the Yap1 transcription factor","volume":"19","author":"Delaunay","year":"2000","journal-title":"EMBO J"},{"key":"10.1074\/mcp.R111.013037_bib45","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.ab.2006.08.020","article-title":"Detection of reversible protein thiol modifications in tissues","volume":"358","author":"Rogers","year":"2006","journal-title":"Anal. Biochem"},{"key":"10.1074\/mcp.R111.013037_bib46","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1139\/v76-200","article-title":"The hydrolysis of maleimide in alkaline solution","volume":"54","author":"Barradas","year":"1976","journal-title":"Can. J. Chem"},{"key":"10.1074\/mcp.R111.013037_bib47","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1016\/j.freeradbiomed.2007.12.032","article-title":"Copper dependence of the biotin switch assay: modified assay for measuring cellular and blood nitrosated proteins","volume":"44","author":"Wang","year":"2008","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib48","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.cbpa.2010.10.006","article-title":"Chemical methods to detect S-nitrosation","volume":"15","author":"Wang","year":"2011","journal-title":"Curr. Opin. Chem. Biol"},{"key":"10.1074\/mcp.R111.013037_bib49","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1021\/cb900302u","article-title":"Water-soluble triarylphosphines as biomarkers for protein S-nitrosation","volume":"5","author":"Bechtold","year":"2010","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/mcp.R111.013037_bib50","doi-asserted-by":"crossref","first-page":"17982","DOI":"10.1073\/pnas.0404762101","article-title":"Widespread sulfenic acid formation in tissues in response to hydrogen peroxide","volume":"101","author":"Saurin","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib51","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/S0003-9861(02)00468-X","article-title":"Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis","volume":"406","author":"Lind","year":"2002","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/mcp.R111.013037_bib52","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/j.bbagen.2006.01.006","article-title":"In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization","volume":"1760","author":"Reynaert","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/mcp.R111.013037_bib53","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/35055104","article-title":"Protein S-nitrosylation: a physiological signal for neuronal nitric oxide","volume":"3","author":"Jaffrey","year":"2001","journal-title":"Nat. Cell. Biol"},{"key":"10.1074\/mcp.R111.013037_bib54","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1016\/j.freeradbiomed.2006.05.025","article-title":"Methodological vexation about thiol oxidation versus S-nitrosation \u2013 a commentary on \u201cAn ascorbate-dependent artifact that interferes with the interpretation of the biotin-switch assay\u201d","volume":"41","author":"Gladwin","year":"2006","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib55","doi-asserted-by":"crossref","first-page":"3224","DOI":"10.1021\/pr0701456","article-title":"A novel approach to identify proteins modified by nitric oxide: the HIS-TAG switch method","volume":"6","author":"Camerini","year":"2007","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.R111.013037_bib56","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/nbt.1545","article-title":"Proteomic analysis of S-nitrosylation and denitrosylation by resin-assisted capture","volume":"27","author":"Forrester","year":"2009","journal-title":"Nat Biotechnol"},{"key":"10.1074\/mcp.R111.013037_bib57","doi-asserted-by":"crossref","first-page":"22040","DOI":"10.1074\/jbc.M703591200","article-title":"Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling","volume":"282","author":"Hurd","year":"2007","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib58","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.1002\/pmic.200601007","article-title":"Differential protein labeling with thiol-reactive infrared DY-680 and DY-780 maleimides and analysis by two-dimensional gel electrophoresis","volume":"7","author":"Riederer","year":"2007","journal-title":"Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib59","first-page":"181","article-title":"Protein-thiol oxidation, from single proteins to proteome-wide analyses","volume":"476","author":"Le Moan","year":"2008","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/mcp.R111.013037_bib60","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1042\/BJ20100633","article-title":"Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation","volume":"430","author":"Chouchani","year":"2010","journal-title":"Biochem. J"},{"key":"10.1074\/mcp.R111.013037_bib61","doi-asserted-by":"crossref","first-page":"e333","DOI":"10.1371\/journal.pbio.0020333","article-title":"Protein thiol modifications visualized in vivo","volume":"2","author":"Leichert","year":"2004","journal-title":"PLoS Biol"},{"key":"10.1074\/mcp.R111.013037_bib62","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1038\/13690","article-title":"Quantitative analysis of complex protein mixtures using isotope-coded affinity tags","volume":"17","author":"Gygi","year":"1999","journal-title":"Nat. Biotechnol"},{"key":"10.1074\/mcp.R111.013037_bib63","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1021\/pr049887e","article-title":"Isotope-coded affinity tag (ICAT) approach to redox proteomics: identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures","volume":"3","author":"Sethuraman","year":"2004","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.R111.013037_bib64","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1074\/mcp.T300011-MCP200","article-title":"Isotope-coded affinity tag approach to identify and quantify oxidant-sensitive protein thiols","volume":"3","author":"Sethuraman","year":"2004","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib65","doi-asserted-by":"crossref","first-page":"3789","DOI":"10.1021\/pr800233r","article-title":"Quantitative analysis of redox-sensitive proteome with DIGE and ICAT","volume":"7","author":"Fu","year":"2008","journal-title":"J. Proteome Res"},{"key":"10.1074\/mcp.R111.013037_bib66","doi-asserted-by":"crossref","first-page":"8197","DOI":"10.1073\/pnas.0707723105","article-title":"Quantifying changes in the thiol redox proteome upon oxidative stress in vivo","volume":"105","author":"Leichert","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib67","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1089\/ars.2010.3203","article-title":"Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans","volume":"14","author":"Kumsta","year":"2011","journal-title":"Antioxid. Redox. Signal"},{"key":"10.1074\/mcp.R111.013037_bib68","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.jasms.2006.09.023","article-title":"Identification of redox sensitive thiols of protein disulfide isomerase using isotope coded affinity technology and mass spectrometry","volume":"18","author":"Kozarova","year":"2007","journal-title":"J. Am. Soc. Mass Spectrom"},{"key":"10.1074\/mcp.R111.013037_bib69","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.freeradbiomed.2006.12.012","article-title":"Quantification of oxidative posttranslational modifications of cysteine thiols of p21ras associated with redox modulation of activity using isotope-coded affinity tags and mass spectrometry","volume":"42","author":"Sethuraman","year":"2007","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib70","doi-asserted-by":"crossref","first-page":"20556","DOI":"10.1074\/jbc.M109.015651","article-title":"Heme regulatory motifs in heme oxygenase-2 form a thiol\/disulfide redox switch that responds to the cellular redox state","volume":"284","author":"Yi","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib71","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1074\/mcp.M900643-MCP200","article-title":"Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach","volume":"9","author":"Held","year":"2010","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib72","doi-asserted-by":"crossref","first-page":"7601","DOI":"10.1074\/jbc.M110.190108","article-title":"Quantitative mapping of reversible mitochondrial Complex I cysteine oxidation in a Parkinson disease mouse model","volume":"286","author":"Danielson","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib73","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1093\/bioinformatics\/btq054","article-title":"Skyline: an open source document editor for creating and analyzing targeted proteomics experiments","volume":"26","author":"MacLean","year":"2010","journal-title":"Bioinformatics"},{"key":"10.1074\/mcp.R111.013037_bib74","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M110.005645","article-title":"Evaluation of Large Scale Quantitative Proteomic Assay Development Using Peptide Affinity-based Mass Spectrometry","volume":"10","author":"Whiteaker","year":"2011","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib75","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1074\/mcp.M500331-MCP200","article-title":"Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins","volume":"5","author":"Anderson","year":"2006","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib76","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1038\/nrm2395","article-title":"Transcriptional control of human p53-regulated genes","volume":"9","author":"Riley","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/mcp.R111.013037_bib77","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1146\/annurev.pharmtox.46.120604.141122","article-title":"Nuclear and mitochondrial compartmentation of oxidative stress and redox signaling","volume":"46","author":"Hansen","year":"2006","journal-title":"Annu. Rev. Pharmacol. Toxicol"},{"key":"10.1074\/mcp.R111.013037_bib78","doi-asserted-by":"crossref","first-page":"35265","DOI":"10.1074\/jbc.M805287200","article-title":"Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation","volume":"283","author":"Chen","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib79","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1006\/abio.2000.4623","article-title":"Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH","volume":"283","author":"Kim","year":"2000","journal-title":"Anal. Biochem"},{"key":"10.1074\/mcp.R111.013037_bib80","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.bbabio.2008.03.029","article-title":"Targeting lipophilic cations to mitochondria","volume":"1777","author":"Murphy","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/mcp.R111.013037_bib81","doi-asserted-by":"crossref","first-page":"17048","DOI":"10.1074\/jbc.M110797200","article-title":"Specific modification of mitochondrial protein thiols in response to oxidative stress: a proteomics approach","volume":"277","author":"Lin","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib82","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1016\/j.cbpa.2008.07.028","article-title":"Expanding the functional diversity of proteins through cysteine oxidation","volume":"12","author":"Reddie","year":"2008","journal-title":"Curr. Opin. Chem. Biol"},{"key":"10.1074\/mcp.R111.013037_bib83","doi-asserted-by":"crossref","first-page":"1473","DOI":"10.1074\/mcp.M700065-MCP200","article-title":"Protein sulfenation as a redox sensor: proteomics studies using a novel biotinylated dimedone analogue","volume":"6","author":"Charles","year":"2007","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib84","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1021\/bc050257s","article-title":"Synthesis of chemical probes to map sulfenic acid modifications on proteins","volume":"16","author":"Poole","year":"2005","journal-title":"Bioconjug. Chem"},{"key":"10.1074\/mcp.R111.013037_bib85","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1039\/b719986d","article-title":"A chemical approach for detecting sulfenic acid-modified proteins in living cells","volume":"4","author":"Reddie","year":"2008","journal-title":"Mol. Biosyst"},{"key":"10.1074\/mcp.R111.013037_bib86","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1021\/cb900105q","article-title":"Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells","volume":"4","author":"Leonard","year":"2009","journal-title":"ACS Chem. Biol"},{"key":"10.1074\/mcp.R111.013037_bib87","doi-asserted-by":"crossref","first-page":"1342","DOI":"10.1002\/anie.201007175","article-title":"Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone","volume":"50","author":"Seo","year":"2011","journal-title":"Angew Chem. Int. Ed. Engl"},{"key":"10.1074\/mcp.R111.013037_bib88","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1016\/j.jasms.2007.05.013","article-title":"Characterization by tandem mass spectrometry of stable cysteine sulfenic acid in a cysteine switch peptide of matrix metalloproteinases","volume":"18","author":"Shetty","year":"2007","journal-title":"J. Am. Soc. Mass Spectrom"},{"key":"10.1074\/mcp.R111.013037_bib89","doi-asserted-by":"crossref","first-page":"16163","DOI":"10.1073\/pnas.0903015106","article-title":"Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies","volume":"106","author":"Seo","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib90","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1016\/j.freeradbiomed.2010.06.020","article-title":"Cys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines","volume":"49","author":"Yusuf","year":"2010","journal-title":"Free Radic. Biol. Med"},{"key":"10.1074\/mcp.R111.013037_bib91","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M500212-MCP200","article-title":"The utility of N,N-biotinyl glutathione disulfide in the study of protein S-glutathiolation","volume":"5","author":"Brennan","year":"2006","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/mcp.R111.013037_bib92","doi-asserted-by":"crossref","first-page":"11121","DOI":"10.1021\/bi0007674","article-title":"Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation","volume":"39","author":"Sullivan","year":"2000","journal-title":"Biochemistry"},{"key":"10.1074\/mcp.R111.013037_bib93","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1002\/bms.1200220602","article-title":"Mass spectrometry in the analysis of glutathione conjugates","volume":"22","author":"Baillie","year":"1993","journal-title":"Biol Mass Spectrom"},{"key":"10.1074\/mcp.R111.013037_bib94","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1002\/jms.1475","article-title":"Screening and characterization of reactive metabolites using glutathione ethyl ester in combination with Q-trap mass spectrometry","volume":"44","author":"Wen","year":"2009","journal-title":"J. Mass Spectrom"},{"key":"10.1074\/mcp.R111.013037_bib95","doi-asserted-by":"crossref","first-page":"6835","DOI":"10.1021\/ac040159k","article-title":"Stable-isotope trapping and high-throughput screenings of reactive metabolites using the isotope MS signature","volume":"76","author":"Yan","year":"2004","journal-title":"Anal. Chem"},{"key":"10.1074\/mcp.R111.013037_bib96","doi-asserted-by":"crossref","first-page":"3482","DOI":"10.1002\/rcm.2223","article-title":"Application of stable isotope labeled glutathione and rapid scanning mass spectrometers in detecting and characterizing reactive metabolites","volume":"19","author":"Mutlib","year":"2005","journal-title":"Rapid Commun. Mass Spectrom"},{"key":"10.1074\/mcp.R111.013037_bib97","doi-asserted-by":"crossref","first-page":"11158","DOI":"10.1073\/pnas.201289098","article-title":"Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO","volume":"98","author":"Sun","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib98","doi-asserted-by":"crossref","first-page":"9637","DOI":"10.1074\/jbc.C100746200","article-title":"Basal and stimulated protein S-nitrosylation in multiple cell types and tissues","volume":"277","author":"Gow","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib99","doi-asserted-by":"crossref","first-page":"re1","DOI":"10.1126\/stke.2001.86.re1","article-title":"S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation","volume":"2001","author":"Lane","year":"2001","journal-title":"Sci. STKE"},{"key":"10.1074\/mcp.R111.013037_bib100","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1038\/nrm2764","article-title":"Protein denitrosylation: enzymatic mechanisms and cellular functions","volume":"10","author":"Benhar","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/mcp.R111.013037_bib101","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1096\/fasebj.12.7.561","article-title":"Redox regulation of ubiquitin-conjugating enzymes: mechanistic insights using the thiol-specific oxidant diamide","volume":"12","author":"Obin","year":"1998","journal-title":"FASEB J"},{"key":"10.1074\/mcp.R111.013037_bib102","doi-asserted-by":"crossref","first-page":"10941","DOI":"10.1128\/MCB.24.24.10941-10953.2004","article-title":"Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex","volume":"24","author":"Zhang","year":"2004","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/mcp.R111.013037_bib103","doi-asserted-by":"crossref","first-page":"10810","DOI":"10.1073\/pnas.0404161101","article-title":"Nitrosative stress linked to sporadic Parkinson\u2019s disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity","volume":"101","author":"Yao","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib104","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.molcel.2005.12.019","article-title":"Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes","volume":"21","author":"Bossis","year":"2006","journal-title":"Mol. Cell"},{"key":"10.1074\/mcp.R111.013037_bib105","doi-asserted-by":"crossref","first-page":"24484","DOI":"10.1074\/jbc.M803795200","article-title":"Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization of ISG15 and contributes to effective ISGylation","volume":"283","author":"Okumura","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib106","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1096\/fj.06-7871com","article-title":"Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation","volume":"22","author":"Xu","year":"2008","journal-title":"FASEB J"},{"key":"10.1074\/mcp.R111.013037_bib107","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1016\/j.cell.2008.04.041","article-title":"A redox-dependent pathway for regulating class II HDACs and cardiac hypertrophy","volume":"133","author":"Ago","year":"2008","journal-title":"Cell"},{"key":"10.1074\/mcp.R111.013037_bib108","doi-asserted-by":"crossref","first-page":"20974","DOI":"10.1073\/pnas.1007225107","article-title":"Oxidation-induced intramolecular disulfide bond inactivates mitogen-activated protein kinase kinase 6 by inhibiting ATP binding","volume":"107","author":"Diao","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/mcp.R111.013037_bib109","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1016\/j.cell.2004.12.041","article-title":"Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases","volume":"120","author":"Kamata","year":"2005","journal-title":"Cell"},{"key":"10.1074\/mcp.R111.013037_bib110","doi-asserted-by":"crossref","first-page":"15366","DOI":"10.1074\/jbc.273.25.15366","article-title":"Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor","volume":"273","author":"Lee","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib111","doi-asserted-by":"crossref","first-page":"20336","DOI":"10.1074\/jbc.M111899200","article-title":"Reversible inactivation of the tumor suppressor PTEN by H2O2","volume":"277","author":"Lee","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib112","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1038\/nmeth1100","article-title":"Mapping protein post-translational modifications with mass spectrometry","volume":"4","author":"Witze","year":"2007","journal-title":"Nat. Methods"},{"key":"10.1074\/mcp.R111.013037_bib113","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1007\/978-1-59745-566-4_3","article-title":"Identification of SUMO-conjugated proteins and their SUMO attachment sites using proteomic mass spectrometry","volume":"497","author":"Wohlschlegel","year":"2009","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/mcp.R111.013037_bib114","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1038\/nchembio.194","article-title":"Redox-sensitive cysteines bridge p300\/CBP-mediated acetylation and FoxO4 activity","volume":"5","author":"Dansen","year":"2009","journal-title":"Nat. Chem. Biol"},{"key":"10.1074\/mcp.R111.013037_bib115","doi-asserted-by":"crossref","first-page":"19401","DOI":"10.1074\/jbc.M312626200","article-title":"CD81 associates with 14\u20133-3 in a redox-regulated palmitoylation-dependent manner","volume":"279","author":"Clark","year":"2004","journal-title":"J. Biol. Chem"},{"key":"10.1074\/mcp.R111.013037_bib116","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S0092-8674(02)00723-7","article-title":"OxyR: a molecular code for redox-related signaling","volume":"109","author":"Kim","year":"2002","journal-title":"Cell"},{"key":"10.1074\/mcp.R111.013037_bib117","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1111\/j.1474-9726.2006.00237.x","article-title":"High oxidative damage levels in the longest-living rodent, the naked mole-rat","volume":"5","author":"Andziak","year":"2006","journal-title":"Aging Cell"},{"key":"10.1074\/mcp.R111.013037_bib118","doi-asserted-by":"crossref","first-page":"H2698","DOI":"10.1152\/ajpheart.00534.2006","article-title":"Comparison of endothelial function, O2-* and H2O2 production, and vascular oxidative stress resistance between the longest-living rodent, the naked mole rat, and mice","volume":"291","author":"Labinskyy","year":"2006","journal-title":"Am. J. Physiol. Heart Circ Physiol"},{"key":"10.1074\/mcp.R111.013037_bib119","doi-asserted-by":"crossref","first-page":"3059","DOI":"10.1073\/pnas.0809620106","article-title":"Protein stability and resistance to oxidative stress are determinants of longevity in the longest-living rodent, the naked mole-rat","volume":"106","author":"P\u00e9rez","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"}],"container-title":["Molecular & Cellular Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947620304886?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947620304886?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/mcp.R111.013037","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T00:17:15Z","timestamp":1761524235000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1535947620304886"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,4]]},"references-count":119,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2012,4]]}},"alternative-id":["S1535947620304886"],"URL":"https:\/\/doi.org\/10.1074\/mcp.r111.013037","relation":{},"ISSN":["1535-9476"],"issn-type":[{"value":"1535-9476","type":"print"}],"subject":[],"published":{"date-parts":[[2012,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Regulatory Control or Oxidative Damage? Proteomic Approaches to Interrogate the Role of Cysteine Oxidation Status in Biological Processes","name":"articletitle","label":"Article Title"},{"value":"Molecular & Cellular Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/mcp.R111.013037","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"R111.013037"}}