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Reactive oxygen species, antioxidants, and the mammalian thioredoxin system.
Physiological functions of thioredoxin and thioredoxin reductase.
All mammalian thioredoxin reduct enzyme isozymes are homologous to glutathione reductase and contain a conserved C-terminal elongation with a cysteine-selenocysteine sequence forming a redox-active selenenylsulfide/selenolthiol active site and are inhibited by goldthioglucose and other clinically used drugs.
Focus on mammalian thioredoxin reductases--important selenoproteins with versatile functions.
- Elias S. J. Arnér
- BiologyBiochimica et biophysica acta
- 1 June 2009
Mammalian deoxyribonucleoside kinases.
The thioredoxin system in cancer.
Preparation and assay of mammalian thioredoxin and thioredoxin reductase.
Selenocysteine in proteins-properties and biotechnological use.
The thioredoxin reductase inhibitor auranofin triggers apoptosis through a Bax/Bak-dependent process that involves peroxiredoxin 3 oxidation.
Thioredoxin Glutathione Reductase from Schistosoma mansoni: An Essential Parasite Enzyme and a Key Drug Target
Investigating the potential of a unique, selenium-containing parasite enzyme thioredoxin glutathione reductase (TGR) as a drug target indicates that parasite TGR meets all the major criteria to be a key target for antischistosomal chemotherapy.