Chemical approaches for trapping protein thiols and their oxidative modification.
- Author:
Chu-Sen HUANG
1
;
Wei-Ping ZHU
;
Yu-Fang XU
;
Xu-Hong QIAN
Author Information
1. Shanghai Key Laboratory of Chemical Biology, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Cysteine;
metabolism;
Fluorescent Dyes;
Humans;
Nitrosation;
Oxidation-Reduction;
Proteins;
chemistry;
metabolism;
Reactive Nitrogen Species;
metabolism;
Reactive Oxygen Species;
metabolism;
Sulfenic Acids;
analysis;
Sulfhydryl Compounds;
analysis;
chemistry;
metabolism
- From:
Acta Pharmaceutica Sinica
2012;47(3):280-290
- CountryChina
- Language:Chinese
-
Abstract:
Redox signal transduction, especially the oxidative modification of proein thiols, correlates with many diseases and becomes an expanding research area. However, there was rare method for quick and specific detection of protein thiols and their oxidative modification in living cells. In this article, we review the current chemical strategies for the detection and quantification of protein thiols and related cysteine oxidation. We also look into the future of the development of fluorescent probes for protein thiols and their potential application in the research of reactive cysteine proteomes and early detection of redox-related diseases.
