Ontology highlight
ABSTRACT:
SUBMITTER: Fu L
PROVIDER: S-EPMC6342663 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
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]