<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Paulech J</submitter><funding>Lundbeck Foundation</funding><pagination>609-20</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4349981</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(3)</volume><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 &lt; 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</pubmed_abstract><journal>Molecular &amp; cellular proteomics : MCP</journal><pubmed_title>Global analysis of myocardial peptides containing cysteines with irreversible sulfinic and sulfonic acid post-translational modifications.</pubmed_title><pmcid>PMC4349981</pmcid><funding_grant_id>R83-2011-8143</funding_grant_id><pubmed_authors>Engholm-Keller K</pubmed_authors><pubmed_authors>Paulech J</pubmed_authors><pubmed_authors>Liddy KA</pubmed_authors><pubmed_authors>White MY</pubmed_authors><pubmed_authors>Cordwell SJ</pubmed_authors></additional><is_claimable>false</is_claimable><name>Global analysis of myocardial peptides containing cysteines with irreversible sulfinic and sulfonic acid post-translational modifications.</name><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 &lt; 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</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Mar</publication><modification>2026-04-16T21:17:00.439Z</modification><creation>2019-03-27T01:47:34Z</creation></dates><accession>S-EPMC4349981</accession><cross_references><pubmed>25561502</pubmed><doi>10.1074/mcp.M114.044347</doi><doi>10.1074/mcp.m114.044347</doi></cross_references></HashMap>