Recombinant expression of mammalian selenocysteine-containing thioredoxin reductase and other selenoproteins in Escherichia coli (Q34566277)

3 August 2017

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title

Recombinant expression of mammalian selenocysteine-containing thioredoxin reductase and other selenoproteins in Escherichia coli (English)

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3 August 2017

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Elias S J Arnér

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3 August 2017

language of work or name

English

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publication date

1 January 2002

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3 August 2017

published in

Methods in Enzymology

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3 August 2017

volume

347

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3 August 2017

page(s)

226-235

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Physiological functions of thioredoxin and thioredoxin reductase

3 August 2017

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Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation

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Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue.

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High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes

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Overexpression of wild type and SeCys/Cys mutant of human thioredoxin reductase in E. coli: the role of selenocysteine in the catalytic activity

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Substituting selenocysteine for catalytic cysteine 41 enhances enzymatic activity of plant phospholipid hydroperoxide glutathione peroxidase expressed in Escherichia coli

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7 January 2021

Genetic probing of the interaction between the translation factor SelB and its mRNA binding element in Escherichia coli

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7 January 2021

Role of stoichiometry between mRNA, translation factor SelB and selenocysteyl-tRNA in selenoprotein synthesis

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7 January 2021

The path of unspecific incorporation of selenium in Escherichia coli

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Identifiers

DOI

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3 August 2017

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