nickel and glutathione Toxicity of Glutathione-Binding Metals: A Review of Targets Mechanisms binding to nickel or glutathione

RNF8-and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites

Inhibition of thioredoxin reductase by auranofin induces apoptosis in adriamycin-resistant human K562 chronic myeloid leukemia cells

Moreover, it is employed in the preservation of protein-dithiols by the protein disulfide reductase (glutathione) (EC 1.8.4.2), an enzyme that catalyzes the chemical reaction: This enzyme acts on different substrates, such as insulin, which is inactivated by cleavage of the disulfide bridge, or on protein disulfide, in which the reduction to protein-dithiol restores the catalytic activity, protecting the cell from oxidant stress

Rheb protein binds CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamoylase, and dihydroorotase) protein in a GTP- and effector domain-dependent manner and influences its cellular localization and carbamoyl-phosphate synthetase (CPSase) activity

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