{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T04:31:23Z","timestamp":1791433883877,"version":"4.3.3"},"reference-count":56,"publisher":"American Chemical Society (ACS)","issue":"11","license":[{"start":{"date-parts":[[2014,9,26]],"date-time":"2014-09-26T00:00:00Z","timestamp":1411689600000},"content-version":"vor","delay-in-days":24,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_ccby_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000341","name":"Arthritis Research UK","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000341","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000836","name":"University Of Liverpool","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000836","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,11,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The molecular mechanisms underlying skeletal muscle aging and associated sarcopenia have been linked to an altered oxidative status of redox-sensitive proteins. Reactive oxygen and reactive nitrogen species (ROS\/RNS) generated by contracting skeletal muscle are necessary for optimal protein function, signaling, and adaptation. To investigate the redox proteome of aging gastrocnemius muscles from adult and old male mice, we developed a label-free quantitative proteomic approach that includes a differential cysteine labeling step. The approach allows simultaneous identification of up- and downregulated proteins between samples in addition to the identification and relative quantification of the reversible oxidation state of susceptible redox cysteine residues. Results from muscles of adult and old mice indicate significant changes in the content of chaperone, glucose metabolism, and cytoskeletal regulatory proteins, including Protein DJ-1, cAMP-dependent protein kinase type II, 78 kDa glucose regulated protein, and a reduction in the number of redox-responsive proteins identified in muscle of old mice. Results demonstrate skeletal muscle aging causes a reduction in redox-sensitive proteins involved in the generation of precursor metabolites and energy metabolism, indicating a loss in the flexibility of the redox energy response. Data is available via ProteomeXchange with identifier PXD001054.<\/jats:p>","DOI":"10.1021\/pr5006394","type":"journal-article","created":{"date-parts":[[2014,9,2]],"date-time":"2014-09-02T09:08:23Z","timestamp":1409648903000},"page":"5008-5021","source":"Crossref","is-referenced-by-count":112,"title":["Differential Cysteine Labeling\nand Global Label-Free\nProteomics Reveals an Altered Metabolic State in Skeletal Muscle Aging"],"prefix":"10.1021","volume":"13","author":[{"given":"Brian","family":"McDonagh","sequence":"first","affiliation":[{"name":"University of Liverpool , , , ,","place":["Liverpool, United Kingdom, L69 3GA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Giorgos K.","family":"Sakellariou","sequence":"additional","affiliation":[{"name":"University of Liverpool , , , ,","place":["Liverpool, United Kingdom, L69 3GA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neil T.","family":"Smith","sequence":"additional","affiliation":[{"name":"University of Liverpool , , , ,","place":["Liverpool, United Kingdom, L69 3GA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philip","family":"Brownridge","sequence":"additional","affiliation":[{"name":"University of Liverpool , , , ,","place":["Liverpool, United Kingdom, L69 3GA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Malcolm J.","family":"Jackson","sequence":"additional","affiliation":[{"name":"University of Liverpool , , , ,","place":["Liverpool, United Kingdom, L69 3GA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,9,2]]},"reference":[{"key":"2026090206134907700_cit1","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1016\/j.freeradbiomed.2005.07.009","article-title":"Microdialysis studies\nof extracellular reactive oxygen species in skeletal muscle: factors\ninfluencing the reduction of cytochrome c and hydroxylation of salicylate","volume":"39","author":"Close","year":"2005","journal-title":"Free Radical Biol. 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Cell Biol."},{"key":"2026090206134907700_cit25","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1021\/bi0520737","article-title":"Direct evidence\nfor the formation of a complex between 1-cysteine peroxiredoxin and\nglutathione S-transferase pi with activity changes in both enzymes","volume":"45","author":"Ralat","year":"2006","journal-title":"Biochemistry"},{"key":"2026090206134907700_cit26","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1096\/fj.00-0199com","article-title":"Transgene\noverexpression of alphaB Crystallin confers\nsimultaneous protection against cardiomyocyte apoptosis and necrosis\nduring myocardial ischemia and reperfusion","volume":"15","author":"Ray","year":"2001","journal-title":"FASEB J."},{"key":"2026090206134907700_cit27","doi-asserted-by":"crossref","first-page":"7293","DOI":"10.1074\/jbc.M113.520403","article-title":"A redox-resistant\nsirtuin-1 mutant protects against hepatic metabolic and oxidant stress","volume":"289","author":"Shao","year":"2014","journal-title":"J. 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Chem."},{"key":"2026090206134907700_cit30","doi-asserted-by":"crossref","first-page":"8106","DOI":"10.1074\/jbc.M113.511535","article-title":"Targeted metabolomics connects thioredoxin-interacting\nprotein (TXNIP) to mitochondrial fuel selection and regulation of\nspecific oxidoreductase enzymes in skeletal muscle","volume":"289","author":"DeBalsi","year":"2014","journal-title":"J. Biol. Chem."},{"key":"2026090206134907700_cit31","doi-asserted-by":"crossref","first-page":"10810","DOI":"10.1073\/pnas.0404161101","article-title":"Nitrosative stress linked to sporadic\nParkinson\u2019s disease: S-nitrosylation of parkin regulates its\nE3 ubiquitin ligase activity","volume":"101","author":"Yao","year":"2004","journal-title":"Proc. Natl. Acad.\nSci. U.S.A."},{"key":"2026090206134907700_cit32","doi-asserted-by":"crossref","first-page":"514847","DOI":"10.1155\/2012\/514847","article-title":"Application\nof iTRAQ reagents to relatively quantify\nthe reversible redox state of cysteine residues","volume":"2012","author":"McDonagh","year":"2012","journal-title":"Int. J. 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Toxicol."},{"key":"2026090206134907700_cit55","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.mce.2012.06.019","article-title":"AMPK regulation\nof fatty acid metabolism\nand mitochondrial biogenesis: implications for obesity","volume":"366","author":"O\u2019Neill","year":"2013","journal-title":"Mol. Cell. Endocrinol."},{"key":"2026090206134907700_cit56","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.phrs.2004.10.012","article-title":"Altered redox status in patients\nwith diabetes mellitus type I","volume":"51","author":"Gil-del Valle","year":"2005","journal-title":"Pharmacol. Res."}],"container-title":["Journal of Proteome Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/pr5006394","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/jprobs\/article-pdf\/13\/11\/5008\/13545147\/pr5006394.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/jprobs\/article-pdf\/13\/11\/5008\/13545147\/pr5006394.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T10:14:00Z","timestamp":1788344040000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/jprobs\/article\/13\/11\/5008\/1339677\/Differential-Cysteine-Labeling-and-Global-Label"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,9,2]]},"references-count":56,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2014,9,2]]},"published-print":{"date-parts":[[2014,11,7]]}},"URL":"https:\/\/doi.org\/10.1021\/pr5006394","relation":{},"ISSN":["1535-3893","1535-3907"],"issn-type":[{"value":"1535-3893","type":"print"},{"value":"1535-3907","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,9,2]]}}}