Ontology highlight
ABSTRACT:
SUBMITTER: Akter S
PROVIDER: S-EPMC6192846 | biostudies-literature | 2018 Nov
REPOSITORIES: biostudies-literature
Akter Salma S Fu Ling L Jung Youngeun Y Conte Mauro Lo ML Lawson J Reed JR Lowther W Todd WT Sun Rui R Liu Keke K Yang Jing J Carroll Kate S KS
Nature chemical biology 20180903 11
Cysteine sulfinic acid or S-sulfinylation is an oxidative post-translational modification (OxiPTM) that is known to be involved in redox-dependent regulation of protein function but has been historically difficult to analyze biochemically. To facilitate the detection of S-sulfinylated proteins, we demonstrate that a clickable, electrophilic diazene probe (DiaAlk) enables capture and site-centric proteomic analysis of this OxiPTM. Using this workflow, we revealed a striking difference between sul ...[more]