Glutathionylation is generally a reversible posttranslational modification that occurs to
cysteine residues that have been exposed to reactive oxygen species (P-SSG). This cyclical …

Introduction: Depending in part on the glutathione: glutathione disulfide ratio, reversible
protein glutathionylation to a mixed disulfide may occur. Reversible glutathionylation is …

Glutathionylation, covalently attaching glutathione (s) to cysteine residue (s) of a protein, has
attracted great attention in recent years. The importance of glutathionylation was initially …

Glutathione (GSH) is the most abundant antioxidant and is believed to maintain redox
potential in tissues, cells, and individual compartments. However, GSH concentrations in …

Disulfide bonds are a key determinant of protein structure and function, and highly
conserved across proteomes. They are particularly abundant in extracellular proteins …

Glutathione has traditionally been considered as an antioxidant that protects cells against
oxidative stress. Hence, the loss of reduced glutathione and formation of glutathione …

This review is the introduction to a special issue concerning, glutathione (GSH), the most
abundant low molecular weight thiol compound synthesized in cells. GSH plays critical roles …

BACKGROUND: It is now recognized that protein cysteines exist not only as free thiols or
intramolecular disulfides, that help maintain the 3D structure of proteins, but can also …

S-Glutathionylation is emerging as a novel regulatory and adoptive mechanism by which
glutathione (GSH or GSSG) conjugation can modify functionally important reactive cysteines …

Glutathionylation involves reversible protein cysteine modification that regulates the function
of numerous proteins in response to redox stimuli, thereby altering cellular processes …