(Q43848623)

English

Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium

scientific article published on 8 January 2002

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scholarly article

1 reference

Europe PubMed Central

27 November 2017

Methylseleninate is a substrate rather than an inhibitor of mammalian thioredoxin reductase. Implications for the antitumor effects of selenium (English)

1 reference

Europe PubMed Central

27 November 2017

methylselenol reductase activity

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

methylseleninic acid reductase activity

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

1 reference

ChEBI release 2020-05-28

1 reference

based on heuristic

inferred from title

author name string

Stephan Gromer

1

1 reference

Europe PubMed Central

27 November 2017

Jurgen H Gross

2

1 reference

Europe PubMed Central

27 November 2017

language of work or name

0 references

publication date

8 January 2002

1 reference

Europe PubMed Central

27 November 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

27 November 2017

277

1 reference

Europe PubMed Central

27 November 2017

12

1 reference

Europe PubMed Central

27 November 2017

9701-9706

1 reference

Europe PubMed Central

27 November 2017

Selenium inhibition of the neoplastic transformation in preneoplastic mammary cell populations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

The importance of selenium to human health

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Anticarcinogenic effects of selenium

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Selenium metabolism, selenoproteins and mechanisms of cancer prevention: complexities with thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Physiological functions of thioredoxin and thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Thioredoxin reductase as a pathophysiological factor and drug target

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

News and views on thioredoxin reductases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Human placenta thioredoxin reductase. Isolation of the selenoenzyme, steady state kinetics, and inhibition by therapeutic gold compounds

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

The 58 kDa mouse selenoprotein is a BCNU-sensitive thioredoxin reductase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Random silent mutagenesis in the initial triplets of the coding region: a technique for adapting human glutathione reductase-encoding cDNA to expression in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Recombinant putative glutathione reductase of Plasmodium falciparum exhibits thioredoxin reductase activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Human placenta thioredoxin reductase: preparation and inhibitor studies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

The nature of the acid-volatile selenium in the liver of the male rat.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Methylseleninic acid, a potent growth inhibitor of synchronized mouse mammary epithelial tumor cells in vitro

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

The CXXC motif: a rheostat in the active site.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Purification of human thioredoxin reductase: properties and characterization by absorption and circular dichroism spectroscopy.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: biosynthesis and characterization of (Se)2-thioredoxin.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Intracellular reduction of selenite into glutathione peroxidase. Evidence for involvement of NADPH and not glutathione as the reductant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Selenium in biology: facts and medical perspectives

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Preparation and assay of mammalian thioredoxin and thioredoxin reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Identification of hydrogen selenide and other volatile selenols by derivatization with 1-fluoro-2,4-dinitrobenzene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Determination of thioredoxin reductase activity in rat liver supernatant

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Function of thioredoxin reductase as a peroxynitrite reductase using selenocystine or ebselen

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Selenite incubated with NADPH and mammalian thioredoxin reductase yields selenide, which inhibits lipoxygenase and changes the electron spin resonance spectrum of the active site iron

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109234200

21 January 2018

Identifiers

10.1074/JBC.M109234200

1 reference

Europe PubMed Central

27 November 2017

1 reference

Europe PubMed Central

27 November 2017

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