Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

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Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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2018年學術文章

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Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

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Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

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Item

label

Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

@en

Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

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Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

@en

Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

@nl

P1476

Selective Evaluation of Thioredoxin Reductase Enzymatic Activities.

@en

P2093

Elias S J Arnér

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P2860

The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

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

Convergent evolution of similar function in two structurally divergent enzymes

Physiological functions of thioredoxin and thioredoxin reductase

2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity.

Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells

Thioredoxin reductase two modes of catalysis have evolved.

Active sites of thioredoxin reductases: why selenoproteins?

Focus on mammalian thioredoxin reductases--important selenoproteins with versatile functions.

P304

301-309

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P31

scholarly article

P356

10.1007/978-1-4939-7258-6_21

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P407

English

P478

1661

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P50

Elias Arnér

P577

2018-01-01T00:00:00Z

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P698

28917053

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