Role of nonprotein thiols in enzymatic reduction of 2-nitroimidazoles
- 1 February 1988
- journal article
- research article
- Published by Elsevier in Biochemical Pharmacology
- Vol. 37 (3) , 473-479
- https://doi.org/10.1016/0006-2952(88)90217-1
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- The biological properties of reduced nitroheterocyclics and possible underlying biochemical mechanismsBiochemical Pharmacology, 1986
- Effects of glutathione depletion using buthionine sulphoximine on the cytotoxicity of nitroaromatic compounds in mammalian cells in vitroBiochemical Pharmacology, 1985
- Chemical modifiers of radiosensitivity-theory and reality: A reviewInternational Journal of Radiation Oncology*Biology*Physics, 1985
- Reductive fragmentation of 2-nitroimidazoles in the presence of nitroreductases—glyoxal formation from misonidazoleBiochemical Pharmacology, 1983
- The mechanisms of cytotoxicity and chemosensitization by misonidazole and other nitroimidazolesInternational Journal of Radiation Oncology*Biology*Physics, 1982
- Activation of misonidazole by rat liver microsomes and purified NADPH-cytochrome c reductaseBiochemical Pharmacology, 1982
- Misonidazole—A drug for trial in radiotherapy and oncologyInternational Journal of Radiation Oncology*Biology*Physics, 1979
- The Glutathione Status of CellsPublished by Elsevier ,1978
- One-electron transfer reactions in biochemical systems. VI. Changes in electron transfer mechanism of lipoamide dehydrogenase by modification of sulfhydryl groupsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1972
- The regulation of rat liver xanthine oxidase. Involvement of thiol groups in the conversion of the enzyme activity from dehydrogenase (type D) into oxidase (type O) and purification of the enzymeBiochemical Journal, 1972