Glutathione and intracellular thiol-containing proteins (GSH (for glutathione))

Glutathione is a tripeptide composed of glutamate, cysteine, and glycine and is the most abundant low-molecular-mass thiol in animal cells. It acts as the major cellular antioxidant, maintaining redox homeostasis by detoxifying reactive oxygen species (ROS) and reactive nitrogen species (RNS), conjugating and inactivating electrophilic xenobiotics and endogenous products, and protecting protein thiol groups through reversible S-glutathionylation. Intracellular thiol-containing proteins (especially those with reactive cysteine residues) participate in redox regulation, and their post-translational modification (e.g., by glutathionylation) is critical in regulating protein function and cellular signaling. Dysregulation of these redox systems is linked to a wide spectrum of diseases, including cancer, neurodegeneration, and inflammatory conditions[1][2][3][4]. Note: - The entry "intracellular thiol-containing proteins and glutathione" is *not* the standard form for a single molecular target; glutathione (GSH) is a well-defined small molecule, but "intracellular thiol-containing proteins" represents a broad class of proteins. If possible, targets should be specified as either "Glutathione" or, for protein targets, the specific protein/receptor (e.g., "Protein disulfide isomerase"). This entry is too broad for precise mapping and may be considered non-specific or "incorrect" as a single therapeutic target entity.

Other names

Reduced glutathioneGSHprotein thiolsthiol-containing proteins

Enhancement or inhibition of glutathione synthesis; Modulation of protein S-glutathionylation; Alteration of redox balance; Detoxification of xenobiotics by conjugation