Significance: Over the past several years, oxidative post-translational modifications of
protein cysteines have been recognized for their critical roles in physiology and …

Reversible protein S-glutathionylation (protein-SSG) is an important post-translational
modification, providing protection of protein cysteines from irreversible oxidation and serving …

This Special Issue of Antioxidants on Glutathione (GSH) and Glutaredoxin (Grx) was
designed to collect review articles and original research studies focused on advancing the …

Protein-S-glutathionylation is a post-translational modification involving the conjugation of
glutathione to protein thiols, which can modulate the activity and structure of key cellular …

The tripeptide glutathione (GSH) and its oxidized form glutathione disulfide (GSSG)
constitute a key redox couple in cells. In particular, they partner protein thiols in reversible …

Reversible posttranslational modifications on specific amino acid residues can efficiently
regulate protein functions. O-Phosphorylation is the prototype and analogue to the rapidly …

To understand the physiological function of glutaredoxin, a thiotransferase catalyzing the
reduction of mixed disulfides of protein and glutathione, we generated a line of knockout …

S-glutathionylation is a reversible post-translational modification that continues to gain
eminence as a redox regulatory mechanism of protein activity and associated cellular …

Redox homeostasis governs a number of critical cellular processes. In turn, imbalances in
pathways that control oxidative and reductive conditions have been linked to a number of …

Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the
reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH …