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thioredoxin glutathione reductase Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
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thioredoxin glutathione reductase Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
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Disulfide bond formation in the cytoplasm of SHUFFLE cells (4 of 4) NEB Two thiol dependent redox systems. The disulfides in oxidized Trxs GSH Download Scientific Diagram Non covalent inhibitors of thioredoxin glutathione reductase with schistosomicidal activity in vivo Nature Communications Frontiers Assigning function to active site residues of Schistosoma mansoni thioredoxin glutathione reductase from analysis of transient state reductive half reactions with variant forms of the enzyme Glutaredoxin Alchetron, The Free Social Encyclopedia
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thioredoxin glutathione reductase Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
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