Glutathione is a tripeptide thiol composed of glutamate, cysteine, and glycine that functions as the principal intracellular antioxidant and redox buffer in mammalian cells. Its reactive sulfhydryl group allows it to scavenge reactive oxygen and nitrogen species directly and to serve as the electron donor for glutat…
Glutathione is a tripeptide thiol composed of glutamate, cysteine, and glycine that functions as the principal intracellular antioxidant and redox buffer in mammalian cells. Its reactive sulfhydryl group allows it to scavenge reactive oxygen and nitrogen species directly and to serve as the electron donor for glutathione peroxidases, which reduce hydrogen peroxide and lipid hydroperoxides. The ratio of reduced glutathione to its oxidized disulfide form is a widely used index of cellular oxidative status, and glutathione participates in xenobiotic detoxification through glutathione S-transferase conjugation, in the regeneration of vitamins C and E, and in the regulation of protein thiol redox states that influence signaling and gene expression. Depletion of glutathione is implicated in oxidative-stress-linked conditions spanning hepatic injury, cardiovascular and metabolic disease, neurodegeneration, and aging. Research in this area examines endogenous and dietary antioxidant systems, including phenolic compounds, flavonoids, polysaccharides, micronutrients, and methionine-derived sulfur metabolism, together with assays of total antioxidant status and protective effects in animal and cell models of induced oxidative damage. The journal publishes peer-reviewed studies on the biochemistry, measurement, and physiological significance of glutathione and related antioxidant defenses.
12 peer-reviewed articles, ranked by relevance. Each links to its DOI.
The 12 articles above have been cited 113 times in the scholarly literature. Citation data via OpenAlex and Crossref, updated Jun 2026.
A sample of recent works citing this journal's research on Glutathione, linking to each citing work.