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thioredoxin glutathione reductase Structure and mechanism of mammalian reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Synthesis and biological evaluation of

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10.1016/j.freeradbiomed.2012.06.025 [DOI] [PMC free article] [PubMed] [Google Scholar] Fu L., Xu B

thioredoxin glutathione reductase Structure and mechanism of mammalian reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Synthesis and biological evaluation of

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Immunity 8 , 255264 (1998)

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thioredoxin glutathione reductase Structure and mechanism of mammalian reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Synthesis and biological evaluation of

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thioredoxin glutathione reductase Structure and mechanism of mammalian reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Synthesis and biological evaluation of

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