{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T18:18:29Z","timestamp":1788373109616,"version":"build-2803163510"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"3","license":[{"start":{"date-parts":[[2015,1,8]],"date-time":"2015-01-08T00:00:00Z","timestamp":1420675200000},"content-version":"vor","delay-in-days":366,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,3,21]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Reversible chemical modifications of protein cysteine residues by S-nitrosylation and S-oxidation are increasingly recognized as important regulatory mechanisms for many protein classes associated with cellular signaling and stress response. Both modifications may theoretically occur under cellular nitrosative or nitroxidative stress. Therefore, a proteomic isotope-coded approach to parallel, quantitative analysis of cysteome S-nitrosylation and S-oxidation was developed. Modifications of cysteine residues of (i) human glutathione-S-transferase P1-1 (GSTP1) and (ii) the schistosomiasis drug target thioredoxin glutathione reductase (TGR) were studied. Both S-nitrosylation (SNO) and S-oxidation to disulfide (SS) were observed for reactive cysteines, dependent on concentration of added S-nitrosocysteine (CysNO) and independent of oxygen. SNO and SS modifications of GSTP1 were quantified and compared for therapeutically relevant NO and HNO donors from different chemical classes, revealing oxidative modification for all donors. Observations on GSTP1 were extended to cell cultures, analyzed after lysis and in-gel digestion. Treatment of living neuronal cells with CysNO, to induce nitrosative stress, caused levels of S-nitrosylation and S-oxidation of GSTP1 comparable to those of cell-free studies. Cysteine modifications of PARK7\/DJ-1, peroxiredoxin-2, and other proteins were identified, quantified, and compared to overall levels of protein S-nitrosylation. The new methodology has allowed identification and quantitation of specific cysteome modifications, demonstrating that nitroxidation to protein disulfides occurs concurrently with S-nitrosylation to protein-SNO in recombinant proteins and living cells under nitrosative stress.<\/jats:p>","DOI":"10.1021\/cb400547u","type":"journal-article","created":{"date-parts":[[2014,1,7]],"date-time":"2014-01-07T14:25:50Z","timestamp":1389104750000},"page":"821-830","source":"Crossref","is-referenced-by-count":34,"title":["Proteomic Profiling of Nitrosative Stress: Protein\n                    <i>S-<\/i>\n                    Oxidation Accompanies\n                    <i>S-<\/i>\n                    Nitrosylation"],"prefix":"10.1021","volume":"9","author":[{"given":"Yue-Ting","family":"Wang","sequence":"first","affiliation":[{"name":"University of Illinois at Chicago , , 833 S. Wood Street , , ,","place":["Chicago, Illinois, United States, 60612-7231"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sujeewa C.","family":"Piyankarage","sequence":"additional","affiliation":[{"name":"University of Illinois at Chicago , , 833 S. Wood Street , , ,","place":["Chicago, Illinois, United States, 60612-7231"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David L.","family":"Williams","sequence":"additional","affiliation":[{"name":"Rush University Medical Center , , 1653 W. Congress Parkway , , ,","place":["Chicago, Illinois, United States, 60612"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gregory R. J.","family":"Thatcher","sequence":"additional","affiliation":[{"name":"University of Illinois at Chicago , , 833 S. Wood Street , , ,","place":["Chicago, Illinois, United States, 60612-7231"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,1,7]]},"reference":[{"key":"2026090213562045300_cit1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1515\/BC.2004.001","article-title":"The chemistry\nof nitrosative stress induced by nitric oxide and reactive nitrogen\noxide species. Putting perspective on stressful biological situations","volume":"385","author":"Ridnour","year":"2004","journal-title":"Biol. Chem."},{"key":"2026090213562045300_cit2","doi-asserted-by":"crossref","first-page":"26497","DOI":"10.1074\/jbc.R113.461368","article-title":"Causes and consequences\nof cysteine S-glutathionylation","volume":"288","author":"Grek","year":"2013","journal-title":"J. Biol. Chem."},{"key":"2026090213562045300_cit3","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/S0165-6147(00)88968-3","article-title":"NO, nitrosonium\nions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology:\na chemist\u2019s perspective","volume":"16","author":"Butler","year":"1995","journal-title":"Trends Pharmacol.\nSci."},{"key":"2026090213562045300_cit4","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1038\/nrm1569","article-title":"Protein S-nitrosylation:\npurview and parameters","volume":"6","author":"Hess","year":"2005","journal-title":"Nat. Rev. Mol. Cell.\nBiol."},{"key":"2026090213562045300_cit5","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/s00109-012-0878-z","article-title":"Enzymatic mechanisms\nregulating protein S-nitrosylation: implications in health and disease","volume":"90","author":"Anand","year":"2012","journal-title":"J. Mol. Med. (Berlin)"},{"key":"2026090213562045300_cit6","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1038\/nsb0498-247","article-title":"Oxidative modifications in nitrosative stress","volume":"5","author":"Stamler","year":"1998","journal-title":"Nat. Struct. Biol."},{"key":"2026090213562045300_cit7","first-page":"S98","article-title":"Nitroxidation: the dominant process\nof reactive nitrogen species chemistry under biological conditions","volume":"37","author":"Lancaster","year":"2004","journal-title":"Free Radical Biol. Med."},{"key":"2026090213562045300_cit8","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1080\/10715760500073931","article-title":"Post-translational\ndisulfide modifications in cell signaling-role of inter-protein, intra-protein,\nS-glutathionyl, and S-cysteaminyl disulfide modifications in signal\ntransmission","volume":"39","author":"O\u2019Brian","year":"2005","journal-title":"Free Radical Res."},{"key":"2026090213562045300_cit9","doi-asserted-by":"crossref","first-page":"7626","DOI":"10.1158\/0008-5472.CAN-09-0493","article-title":"Nitrosative stress-induced S-glutathionylation of protein\ndisulfide isomerase leads to activation of the unfolded protein response","volume":"69","author":"Townsend","year":"2009","journal-title":"Cancer Res."},{"key":"2026090213562045300_cit10","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.freeradbiomed.2009.10.026","article-title":"Reaction between nitric oxide, glutathione,\nand oxygen in the presence and absence of protein: How are S-nitrosothiols\nformed?","volume":"48","author":"Keszler","year":"2010","journal-title":"Free Radical Biol. Med."},{"key":"2026090213562045300_cit11","doi-asserted-by":"crossref","first-page":"PL1","DOI":"10.1126\/stke.2001.86.pl1","article-title":"The biotin switch\nmethod for the detection of S-nitrosylated proteins","volume":"2001","author":"Jaffrey","year":"2001","journal-title":"Sci. STKE"},{"key":"2026090213562045300_cit12","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1016\/j.freeradbiomed.2007.12.032","article-title":"Copper dependence\nof the biotin switch assay: modified assay for measuring cellular\nand blood nitrosated proteins","volume":"44","author":"Wang","year":"2008","journal-title":"Free Radical\nBiol. Med."},{"key":"2026090213562045300_cit13","doi-asserted-by":"crossref","first-page":"8197","DOI":"10.1073\/pnas.0707723105","article-title":"Quantifying changes\nin the thiol redox proteome upon oxidative stress in vivo","volume":"105","author":"Leichert","year":"2008","journal-title":"Proc. Natl. Acad. Sci. 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Biol.\nChem."},{"key":"2026090213562045300_cit17","first-page":"4313","article-title":"Glutathione-associated enzymes in\nanticancer drug resistance","volume":"54","author":"Tew","year":"1994","journal-title":"Cancer Res."},{"key":"2026090213562045300_cit18","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1038\/cdd.2010.80","article-title":"Glutathione transferases as mediators\nof signaling pathways involved in cell proliferation and cell death","volume":"17","author":"Laborde","year":"2010","journal-title":"Cell Death Differ."},{"key":"2026090213562045300_cit19","doi-asserted-by":"crossref","first-page":"e206","DOI":"10.1371\/journal.pmed.0040206","article-title":"Thioredoxin glutathione reductase\nfrom Schistosoma mansoni: an essential parasite enzyme\nand a key drug target","volume":"4","author":"Kuntz","year":"2007","journal-title":"PLoS Med."},{"key":"2026090213562045300_cit20","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1080\/10715760500073931","article-title":"Post-translational disulfide modifications in cell signaling--role\nof inter-protein, intra-protein, S-glutathionyl, and S-cysteaminyl\ndisulfide modifications in signal transmission","volume":"39","author":"O\u2019Brian","year":"2005","journal-title":"Free Radical Res."},{"key":"2026090213562045300_cit21","doi-asserted-by":"crossref","first-page":"E600","DOI":"10.1073\/pnas.1110736108","article-title":"Site-specific and redox-controlled S-nitrosation of\nthioredoxin","volume":"108","author":"Barglow","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090213562045300_cit22","doi-asserted-by":"crossref","first-page":"1378","DOI":"10.1002\/ange.201007175","article-title":"Quantification of\nprotein sulfenic acid modifications using isotope-coded dimedone and\niododimedone","volume":"123","author":"Seo","year":"2011","journal-title":"Angew. Chem."},{"key":"2026090213562045300_cit23","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/nbt.1545","article-title":"Proteomic analysis of S-nitrosylation\nand denitrosylation by resin-assisted capture","volume":"27","author":"Forrester","year":"2009","journal-title":"Nat. Biotechnol."},{"key":"2026090213562045300_cit24","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1074\/jbc.M805586200","article-title":"Novel role for glutathione S-transferase pi. Regulator\nof protein S-glutathionylation following oxidative and nitrosative\nstress","volume":"284","author":"Townsend","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2026090213562045300_cit25","doi-asserted-by":"crossref","first-page":"3780","DOI":"10.1073\/pnas.0400181101","article-title":"Activation of the\nantioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation\nmediated by heterodimerization with pi GST","volume":"101","author":"Manevich","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090213562045300_cit26","doi-asserted-by":"crossref","first-page":"4811","DOI":"10.1021\/bi002513o","article-title":"Structural\nand functional consequences of inactivation of human glutathione S-transferase\nP1-1 mediated by the catechol metabolite of equine estrogens, 4-hydroxyequilenin","volume":"40","author":"Chang","year":"2001","journal-title":"Biochemistry (Moscow)"},{"key":"2026090213562045300_cit27","doi-asserted-by":"crossref","first-page":"14428","DOI":"10.1073\/pnas.93.25.14428","article-title":"The chemistry\nof the S-nitrosoglutathione\/glutathione system","volume":"93","author":"Singh","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026090213562045300_cit28","doi-asserted-by":"crossref","first-page":"e127","DOI":"10.1371\/journal.pntd.0000127","article-title":"Quantitative\nhigh-throughput screen identifies inhibitors of the Schistosoma mansoni\nredox cascade","volume":"2","author":"Simeonov","year":"2008","journal-title":"PLoS Negl. Trop. Dis."},{"key":"2026090213562045300_cit29","doi-asserted-by":"crossref","first-page":"5870","DOI":"10.1021\/bi200107n","article-title":"Investigations of\nthe catalytic mechanism of thioredoxin glutathione reductase from\nSchistosoma mansoni","volume":"50","author":"Huang","year":"2011","journal-title":"Biochemistry (Moscow)"},{"key":"2026090213562045300_cit30","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1002\/prot.21986","article-title":"Glutathione reductase\nand thioredoxin reductase at the crossroad: the structure of Schistosoma\nmansoni thioredoxin glutathione reductase","volume":"72","author":"Angelucci","year":"2008","journal-title":"Proteins"},{"key":"2026090213562045300_cit31","doi-asserted-by":"crossref","first-page":"962","DOI":"10.1089\/ars.2012.4543","article-title":"Is S-nitrosocysteine a true surrogate\nfor nitric oxide?","volume":"17","author":"Hickok","year":"2012","journal-title":"Antioxid. Redox Signaling"},{"key":"2026090213562045300_cit32","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1039\/cc9960000927","article-title":"Reactivity of\nthionitrate esters: putative intermediates in nitrovasodilator activity","author":"Artz","year":"1996","journal-title":"Chem. Commun."},{"key":"2026090213562045300_cit33","doi-asserted-by":"crossref","first-page":"1160","DOI":"10.1021\/tx060061w","article-title":"Nitroxidative,\nnitrosative, and nitrative stress: kinetic predictions of reactive\nnitrogen species chemistry under biological conditions","volume":"19","author":"Lancaster","year":"2006","journal-title":"Chem. Res. Toxicol."},{"key":"2026090213562045300_cit34","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/nsb0498-267","article-title":"Enzyme\ninactivation through sulfhydryl oxidation by physiologic NO-carriers","volume":"5","author":"Becker","year":"1998","journal-title":"Nat. Struct. Biol."},{"key":"2026090213562045300_cit35","doi-asserted-by":"crossref","first-page":"1122","DOI":"10.1016\/j.freeradbiomed.2004.06.013","article-title":"Nitrates and NO release:\nContemporary aspects in biological and medicinal chemistry","volume":"37","author":"Thatcher","year":"2004","journal-title":"Free Radical Biol. Med."},{"key":"2026090213562045300_cit36","doi-asserted-by":"crossref","first-page":"16526","DOI":"10.1021\/ja106552p","article-title":"Dual mechanisms of HNO generation by a nitroxyl prodrug\nof the diazeniumdiolate (NONOate) class","volume":"132","author":"Andrei","year":"2010","journal-title":"J.\nAm. Chem. Soc."},{"key":"2026090213562045300_cit37","doi-asserted-by":"crossref","first-page":"2230","DOI":"10.1158\/1535-7163.MCT-07-0069","article-title":"Colon cancer\nchemoprevention by a novel NO chimera that shows anti-inflammatory\nand antiproliferative activity in vitro and in vivo","volume":"6","author":"Hagos","year":"2007","journal-title":"Mol. Cancer Ther."},{"key":"2026090213562045300_cit38","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1021\/ml300002m","article-title":"NOSH-Aspirin: A novel nitric oxide\u2013hydrogen\nsulfide-releasing hybrid: A new class of anti-inflammatory pharmaceuticals","volume":"3","author":"Kodela","year":"2012","journal-title":"ACS Med. Chem. Lett."},{"key":"2026090213562045300_cit39","doi-asserted-by":"crossref","first-page":"5362","DOI":"10.1021\/bi973153g","article-title":"Reaction between S-nitrosothiols\nand thiols: generation of nitroxyl (HNO) and subsequent chemistry","volume":"37","author":"Wong","year":"1998","journal-title":"Biochemistry (Moscow)"},{"key":"2026090213562045300_cit40","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.niox.2006.01.010","article-title":"Nitroxidation, nitration, and oxidation\nof a BODIPY fluorophore by RNOS and ROS","volume":"15","author":"Nicolescu","year":"2006","journal-title":"Nitric\nOxide"},{"key":"2026090213562045300_cit41","doi-asserted-by":"crossref","first-page":"1548","DOI":"10.1002\/pmic.200700322","article-title":"MassMatrix: a database\nsearch program for rapid characterization of proteins and peptides\nfrom tandem mass spectrometry data","volume":"9","author":"Xu","year":"2009","journal-title":"Proteomics"},{"key":"2026090213562045300_cit42","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/j.chembiol.2008.10.013","article-title":"Nitrosothiol reactivity profiling identifies S-nitrosylated\nproteins with unexpected stability","volume":"15","author":"Paige","year":"2008","journal-title":"Chem. Biol."},{"key":"2026090213562045300_cit43","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1089\/ars.2010.3481","article-title":"The role of cysteine oxidation in\nDJ-1 function and dysfunction","volume":"15","author":"Wilson","year":"2011","journal-title":"Antioxid. Redox\nSignaling"},{"key":"2026090213562045300_cit44","doi-asserted-by":"crossref","first-page":"e54087","DOI":"10.1371\/journal.pone.0054087","article-title":"Monomer DJ-1 and its N-terminal sequence are necessary for mitochondrial\nlocalization of DJ-1 mutants","volume":"8","author":"Maita","year":"2013","journal-title":"PLoS One"},{"key":"2026090213562045300_cit45","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1128\/MCB.01350-12","article-title":"Oxidized DJ-1 inhibits p53 by sequestering p53 from promoters in\na DNA-binding affinity-dependent manner","volume":"33","author":"Kato","year":"2013","journal-title":"Mol.\nCell. Biol."},{"key":"2026090213562045300_cit46","doi-asserted-by":"crossref","first-page":"14245","DOI":"10.1074\/jbc.M806902200","article-title":"Oxidizable\nresidues mediating protein stability and cytoprotective interaction\nof DJ-1 with apoptosis signal-regulating kinase 1","volume":"284","author":"Waak","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2026090213562045300_cit47","doi-asserted-by":"crossref","first-page":"7430","DOI":"10.1021\/bi800282d","article-title":"Cysteine pKa depression by a protonated glutamic acid\nin human DJ-1","volume":"47","author":"Witt","year":"2008","journal-title":"Biochemistry (Moscow.)"},{"key":"2026090213562045300_cit48","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/j.bbrc.2005.11.058","article-title":"Roles of distinct cysteine residues in S-nitrosylation\nand dimerization of DJ-1","volume":"339","author":"Ito","year":"2006","journal-title":"Biochem. Biophys.\nRes. Commun."},{"key":"2026090213562045300_cit49","doi-asserted-by":"crossref","first-page":"179","DOI":"10.3109\/03602532.2011.552912","article-title":"Regulatory functions\nof glutathione S-transferase P1-1 unrelated to detoxification","volume":"43","author":"Tew","year":"2011","journal-title":"Drug Metab. Rev."},{"key":"2026090213562045300_cit50","doi-asserted-by":"crossref","first-page":"2024","DOI":"10.1002\/pmic.201100666","article-title":"Proteomic\nanalysis of the role of S-nitrosoglutathione reductase in lipopolysaccharide-challenged\nmice","volume":"12","author":"Ozawa","year":"2012","journal-title":"Proteomics"},{"key":"2026090213562045300_cit51","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1093\/carcin\/bgt031","article-title":"S-Nitrosoglutathione reductase deficiency increases\nmutagenesis from alkylation in mouse liver","volume":"34","author":"Leung","year":"2013","journal-title":"Carcinogenesis"},{"key":"2026090213562045300_cit52","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1227\/NEU.0b013e31823209cf","article-title":"JS-K, a glutathione S-transferase-activated nitric\noxide donor with antineoplastic activity in malignant gliomas","volume":"70","author":"Weyerbrock","year":"2012","journal-title":"Neurosurgery"},{"key":"2026090213562045300_cit53","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1089\/ars.2011.4476","article-title":"Targeting hepatoma using nitric oxide donor strategies","volume":"18","author":"Gonza\u0301lez","year":"2013","journal-title":"Antioxid. Redox Signaling"},{"key":"2026090213562045300_cit54","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1006\/abio.1998.2609","article-title":"Development of chemiluminescence-based methods for\nspecific quantitation of nitrosylated thiols","volume":"258","author":"Samouilov","year":"1998","journal-title":"Anal. Biochem."},{"key":"2026090213562045300_cit55","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1006\/prep.1999.1149","article-title":"Expression and purification of hexahistidine-tagged\nhuman glutathione S-transferase P1-1 in Escherichia coli","volume":"17","author":"Chang","year":"1999","journal-title":"Protein Expression Purif."},{"key":"2026090213562045300_cit56","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ:\n25 years of image analysis","volume":"9","author":"Schneider","year":"2012","journal-title":"Nat. Methods"}],"container-title":["ACS Chemical\nBiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/cb400547u","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/acbcct\/article-pdf\/9\/3\/821\/15708195\/cb400547u.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/acbcct\/article-pdf\/9\/3\/821\/15708195\/cb400547u.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T17:56:36Z","timestamp":1788371796000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/acbcct\/article\/9\/3\/821\/1477904\/Proteomic-Profiling-of-Nitrosative-Stress-Protein"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,1,7]]},"references-count":56,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2014,1,7]]},"published-print":{"date-parts":[[2014,3,21]]}},"URL":"https:\/\/doi.org\/10.1021\/cb400547u","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.718231110.793489487","asserted-by":"object"}]},"ISSN":["1554-8929","1554-8937"],"issn-type":[{"value":"1554-8929","type":"print"},{"value":"1554-8937","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,1,7]]}}}