{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fu L"],"funding":["Beijing Municipal Excellent Talents Foundation","National Key R&D Program of China","Beijing Nova Program","National Natural Science Foundation of China","NCI NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["e76"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6342663"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["95(1)"],"pubmed_abstract":["Oxidation of a protein cysteinyl thiol (Cys-SH) to S-sulfenic acid (Cys-SOH) by a reactive oxygen species (e.g., hydrogen peroxide), which is termed protein S-sulfenylation, is a reversible post-translational modification that plays a crucial role in redox regulation of protein function in various biological processes. Due to its intrinsically labile nature, protein S-sulfenylation cannot be directly detected or analyzed. Chemoselective probing has been the method of choice for analyzing S-sulfenylated proteins either in vitro or in situ, as it allows stabilization and direct detection of this transient oxidative intermediate. However, it remains challenging to globally pinpoint the specific S-sulfenylated cysteine sites on complex proteomes and to quantify their dynamic changes upon oxida"],"journal":["Current protocols in protein science"],"pubmed_title":["Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe."],"pmcid":["PMC6342663"],"funding_grant_id":["R01 GM087638","R01 GM102187","R01 CA227849","81573395","31500666","31770885","R01 CA174864","2017000021223ZK16","2016YFA0501303","171100001117014"],"pubmed_authors":["Yang J","Liu K","Carroll KS","Ferreira RB","Fu L"],"additional_accession":[]},"is_claimable":false,"name":"Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.","description":"Oxidation of a protein cysteinyl thiol (Cys-SH) to S-sulfenic acid (Cys-SOH) by a reactive oxygen species (e.g., hydrogen peroxide), which is termed protein S-sulfenylation, is a reversible post-translational modification that plays a crucial role in redox regulation of protein function in various biological processes. Due to its intrinsically labile nature, protein S-sulfenylation cannot be directly detected or analyzed. Chemoselective probing has been the method of choice for analyzing S-sulfenylated proteins either in vitro or in situ, as it allows stabilization and direct detection of this transient oxidative intermediate. However, it remains challenging to globally pinpoint the specific S-sulfenylated cysteine sites on complex proteomes and to quantify their dynamic changes upon oxida","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Feb","modification":"2025-04-19T16:36:01.171Z","creation":"2020-05-22T08:45:10Z"},"accession":"S-EPMC6342663","cross_references":{"pubmed":["30312022"],"doi":["10.1002/cpps.76"]}}