[66] Modulation of cellular glutathione and protein thiol status during quinone metabolism
- 1 January 1990
- book chapter
- Published by Elsevier
- Vol. 186, 627-635
- https://doi.org/10.1016/0076-6879(90)86158-r
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Alterations of surface morphology caused by the metabolism of menadione in mammalian cells are associated with the oxidation of critical sulfhydryl groups in cytoskeletal proteinsBiochemical Pharmacology, 1988
- Menadione-induced bleb formation in hepatocytes is associated with the oxidation of thiol groups in actinArchives of Biochemistry and Biophysics, 1988
- Redox cycling and sulphydryl arylation; Their relative importance in the mechanism of quinone cytotoxicity to isolated hepatocytesChemico-Biological Interactions, 1988
- Formation and reduction of glutathione-protein mixed disulfides during oxidative stressBiochemical Pharmacology, 1987
- Quinone toxicity in hepatocytes without oxidative stressArchives of Biochemistry and Biophysics, 1986
- Interaction of menadione (2-methyl-1,4-naphthoquinone) with glutathioneChemico-Biological Interactions, 1985
- The covalent binding of acetaminophen to protein. Evidence for cysteine residues as major sites of arylation in vitroChemico-Biological Interactions, 1984
- Oxidation of glutathione during hydroperoxide metabolismEuropean Journal of Biochemistry, 1984
- Metabolism of hydrogen peroxide in isolated hepatocytes: Relative contributions of catalase and glutathione peroxidase in decomposition of endogenously generated H2O2Archives of Biochemistry and Biophysics, 1981
- Relationship of the single-electron reduction potential of quinones to their reduction by flavoproteinsBiochemical Pharmacology, 1980