| Literature DB >> 32031597 |
Leslie B Poole1,2, Cristina M Furdui2,3, S Bruce King2,4.
Abstract
Oxidative modifications of cysteine thiols in cellular proteins are pivotal to the way signal-stimulated reactive oxygen species are sensed and elicit appropriate or sometimes pathological responses, but the dynamic and often transitory nature of these modifications offer a challenge to the investigator trying to identify such sites and the responses they elicit. A number of reagents and workflows have been developed to identify proteins undergoing oxidation and to query the timing, extent and location of such modifications, as described in this minireview. While no approach is perfect to capture all the redox information in a functioning cell, best practices described herein can enable considerable insights into the "redox world" of cells and organisms.Entities:
Keywords: chemical biology; cysteine oxidation; post translational modification; proteomics; redox methods
Year: 2020 PMID: 32031597 PMCID: PMC7477960 DOI: 10.1042/EBC20190050
Source DB: PubMed Journal: Essays Biochem ISSN: 0071-1365 Impact factor: 8.000