期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 21, 期 21, 页码 -出版社
MDPI
DOI: 10.3390/ijms21218113
关键词
S-glutathionylation; redox modification; protein post-translational modification; GSH; GSSG; oxidative stress
资金
- Office of the Provost and Academic Vice President
- Department of Chemistry of John Carroll University
S-glutathionylation, the post-translational modification forming mixed disulfides between protein reactive thiols and glutathione, regulates redox-based signaling events in the cell and serves as a protective mechanism against oxidative damage. S-glutathionylation alters protein function, interactions, and localization across physiological processes, and its aberrant function is implicated in various human diseases. In this review, we discuss the current understanding of the molecular mechanisms of S-glutathionylation and describe the changing levels of expression of S-glutathionylation in the context of aging, cancer, cardiovascular, and liver diseases.
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