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 …