Thioredoxin reductase as a pathophysiological factor and drug target

Human cytosolic thioredoxin reductase (TrxR), a homodimeric protein containing 1 selenocysteine and 1 FAD per subunit of 55 kDa, catalyses the NADPH‐dependent reduction of thioredoxin disulfide and of numerous other oxidized cell constituents. As a general reducing enzyme with little substrate speci...

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Veröffentlicht in:	European journal of biochemistry 2000-10, Vol.267 (20), p.6118-6125
Hauptverfasser:	Becker, Katja, Gromer, Stephan, Schirmer, R. Heiner, Müller, Sylke
Format:	Artikel
Sprache:	eng
Schlagworte:	antioxidant systems aurothioglucose carmustine Chronic Disease Dimerization diselenide drug resistance Epstein–Barr virus Humans leprosy malaria Neoplasms - drug therapy Neoplasms - physiopathology Protein Subunits rheumatoid arthritis Selenium - physiology selenium metabolism Thioredoxin-Disulfide Reductase - chemistry Thioredoxin-Disulfide Reductase - metabolism Thioredoxins - metabolism
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