{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yang J"],"funding":["NICHD NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["1022-37"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4608369"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(7)"],"pubmed_abstract":["Protein S-sulfenylation is the reversible oxidative modification of cysteine thiol groups to form cysteine S-sulfenic acids. Mapping the specific sites of protein S-sulfenylation onto complex proteomes is crucial to understanding the molecular mechanisms controlling redox signaling and regulation. This protocol describes global, in situ, site-specific analysis of protein S-sulfenylation using sulfenic acid-specific chemical probes and mass spectrometry (MS)-based proteomics. The major steps in this protocol are as follows: (i) optimization of conditions for selective labeling of cysteine S-sulfenic acids in intact cells with the commercially available dimedone-based probe, DYn-2; (ii) tagging the modified cysteines with a functionalized biotin reagent containing a cleavable linker via Cu(I"],"journal":["Nature protocols"],"pubmed_title":["Global, in situ, site-specific analysis of protein S-sulfenylation."],"pmcid":["PMC4608369"],"funding_grant_id":["R01 GM102187","R01 CA174864","R01GM102187","R01 HD064727","U24CA159988","U24 CA159988"],"pubmed_authors":["Yang J","Gupta V","Porter NA","Carroll KS","Liebler DC","Tallman KA"],"additional_accession":[]},"is_claimable":false,"name":"Global, in situ, site-specific analysis of protein S-sulfenylation.","description":"Protein S-sulfenylation is the reversible oxidative modification of cysteine thiol groups to form cysteine S-sulfenic acids. Mapping the specific sites of protein S-sulfenylation onto complex proteomes is crucial to understanding the molecular mechanisms controlling redox signaling and regulation. This protocol describes global, in situ, site-specific analysis of protein S-sulfenylation using sulfenic acid-specific chemical probes and mass spectrometry (MS)-based proteomics. The major steps in this protocol are as follows: (i) optimization of conditions for selective labeling of cysteine S-sulfenic acids in intact cells with the commercially available dimedone-based probe, DYn-2; (ii) tagging the modified cysteines with a functionalized biotin reagent containing a cleavable linker via Cu(I","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Jul","modification":"2025-04-04T13:25:38.009Z","creation":"2019-03-27T02:00:11Z"},"accession":"S-EPMC4608369","cross_references":{"pubmed":["26086405"],"doi":["10.1038/nprot.2015.062"]}}