{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Paulech J"],"funding":["Lundbeck Foundation"],"pagination":["609-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4349981"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(3)"],"pubmed_abstract":["Cysteine (Cys) oxidation is a crucial post-translational modification (PTM) associated with redox signaling and oxidative stress. As Cys is highly reactive to oxidants it forms a range of post-translational modifications, some that are biologically reversible (e.g. disulfides, Cys sulfenic acid) and others (Cys sulfinic [Cys-SO2H] and sulfonic [Cys-SO3H] acids) that are considered \"irreversible.\" We developed an enrichment method to isolate Cys-SO2H/SO3H-containing peptides from complex tissue lysates that is compatible with tandem mass spectrometry (MS/MS). The acidity of these post-translational modification (pKa Cys-SO3H < 0) creates a unique charge distribution when localized on tryptic peptides at acidic pH that can be utilized for their purification. The method is based on electrosta"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Global analysis of myocardial peptides containing cysteines with irreversible sulfinic and sulfonic acid post-translational modifications."],"pmcid":["PMC4349981"],"funding_grant_id":["R83-2011-8143"],"pubmed_authors":["Engholm-Keller K","Paulech J","Liddy KA","White MY","Cordwell SJ"],"additional_accession":[]},"is_claimable":false,"name":"Global analysis of myocardial peptides containing cysteines with irreversible sulfinic and sulfonic acid post-translational modifications.","description":"Cysteine (Cys) oxidation is a crucial post-translational modification (PTM) associated with redox signaling and oxidative stress. As Cys is highly reactive to oxidants it forms a range of post-translational modifications, some that are biologically reversible (e.g. disulfides, Cys sulfenic acid) and others (Cys sulfinic [Cys-SO2H] and sulfonic [Cys-SO3H] acids) that are considered \"irreversible.\" We developed an enrichment method to isolate Cys-SO2H/SO3H-containing peptides from complex tissue lysates that is compatible with tandem mass spectrometry (MS/MS). The acidity of these post-translational modification (pKa Cys-SO3H < 0) creates a unique charge distribution when localized on tryptic peptides at acidic pH that can be utilized for their purification. The method is based on electrosta","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Mar","modification":"2026-04-16T21:17:00.439Z","creation":"2019-03-27T01:47:34Z"},"accession":"S-EPMC4349981","cross_references":{"pubmed":["25561502"],"doi":["10.1074/mcp.M114.044347","10.1074/mcp.m114.044347"]}}