Unknown

Dataset Information

0

Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.


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 oxidative stress. This unit describes how a benzothiazine-based chemoselective probe called BTD and mass spectrometry based chemoproteomics can be used to globally and site-specifically identify and quantify protein S-sulfenylation. © 2018 by John Wiley & Sons, Inc.

SUBMITTER: Fu L 

PROVIDER: S-EPMC6342663 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.

Fu Ling L   Liu Keke K   Ferreira Renan B RB   Carroll Kate S KS   Yang Jing J  

Current protocols in protein science 20181012 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-sulfe  ...[more]

Similar Datasets

| S-EPMC3823053 | biostudies-literature
| S-EPMC8341131 | biostudies-literature
| S-EPMC5910380 | biostudies-literature
| S-EPMC10649196 | biostudies-literature
| S-EPMC6684851 | biostudies-literature
| S-EPMC6207713 | biostudies-literature
| S-EPMC7509873 | biostudies-literature
| MSV000086125 | MassIVE
| S-EPMC10284117 | biostudies-literature
| S-EPMC5623068 | biostudies-literature