Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 37, Pages 26497-26504Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R113.461368
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Funding
- National Institutes of Health [CA08660, CA117259]
- National Center for Research Resources (NCRR) [P20 RR024485-COBRE]
- South Carolina Centers of Excellence Program
- Drug Metabolism and Clinical Pharmacology Shared Resource of Hollings Cancer Center of the Medical University of South Carolina
- Swedish Research Council [524-2011-6998]
- National Institutes of Health from the NCRR Extramural Research Facilities Program [C06 RR015455]
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Post-translational S-glutathionylation occurs through the reversible addition of a proximal donor of glutathione to thiolate anions of cysteines in target proteins, where the modification alters molecular mass, charge, and structure/function and/or prevents degradation from sulfhydryl overoxidation or proteolysis. Catalysis of both the forward (glutathione S-transferase P) and reverse (glutaredoxin) reactions creates a functional cycle that can also regulate certain protein functional clusters, including those involved in redox-dependent cell signaling events. For translational application, S-glutathionylated serum proteins may be useful as biomarkers in individuals (who may also have polymorphic expression of glutathione S-transferase P) exposed to agents that cause oxidative or nitrosative stress.
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