Protein thiol group modification

Protein thiol group modification refers to a set of post-translational redox modifications of cysteine residues within proteins. The thiol (-SH) side chain of cysteine is highly reactive and susceptible to oxidation or conjugation, resulting in modifications such as disulfide bond formation, S-glutathionylation, S-nitrosylation, and others. These modifications are key for regulating protein function, signal transduction, immune responses, and adaptation to oxidative stress. Aberrant protein thiol modifications are implicated in numerous diseases due to their crucial roles in controlling enzyme activity, protein folding, and cellular redox homeostasis. Protein thiol modification is a process, not a singular molecular drug target, but is of high therapeutic interest due to its central role in health and disease.

Other names

Thiol modificationProtein thiol oxidationCysteine oxidationProtein S-glutathionylationProtein S-nitrosylation

Reversible oxidation (S-glutathionylation, S-nitrosylation, disulfide bond formation), Irreversible oxidation (sulfinic and sulfonic acid formation), Covalent adduct formation with electrophiles, Reduction via thioredoxin or glutathione systems