biostudies-literatureFu LBeijing Municipal Excellent Talents FoundationNational Key R&D Program of ChinaBeijing Nova ProgramNational Natural Science Foundation of ChinaNCI NIH HHSNational Institutes of HealthNIGMS NIH HHSe76https://www.ebi.ac.uk/biostudies/studies/S-EPMC6342663biostudies-literatureUnknown95(1)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 oxidaCurrent protocols in protein scienceProteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.PMC6342663R01 GM087638R01 GM102187R01 CA227849815733953150066631770885R01 CA1748642017000021223ZK162016YFA0501303171100001117014Yang JLiu KCarroll KSFerreira RBFu LfalseProteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.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 oxida2019-01-01T00:00:00Z2019 Feb2025-04-19T16:36:01.171Z2020-05-22T08:45:10ZS-EPMC63426633031202210.1002/cpps.76