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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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Functional plasticity of a peroxidase allows evolution of diverse disulfide reducing pathways PNAS The thioredoxin reductase thioredoxin system: Novel redox targets for cancer therapy Highly Selective OffOn Fluorescent Probe for Imaging Thioredoxin Reductase in Living Cells Journal of the American Chemical Society Three dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine dependent enzyme PNAS
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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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