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One main finding on the structural side is that the glutathione-hosting site is highly conserved, and uses the negatively charged carboxylate functions of the glycine and glutamic acid residues of glutathione as anchors for substrate recognition by positively charged amino acid residues, as well as negatively charged residues to hold the protonated amino group of the glutamic acid residue

The effects of altered GSH homeostasis vary with cell type, subcellular localization, and metabolic state

Science 287 , 443449 (2000)

Protein purification under denaturing conditions: Proteins that are expressed as an inclusion body and have been solubilized with chaotrophic agents such as guanidine-HCl or urea can be purified by modifying the protocol to include the appropriate amount of denaturant (up to 6M guanidine-HCl or up to 8M urea) in the binding, wash and elution buffers

Differential contribution of hepatitis C virus NS5A and core proteins to the induction of oxidative and nitrosative stress in human hepatocyte-derived cells