Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence (Q24683648)

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Language	Label	Description	Also known as
English	Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence	scientific article

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scholarly article

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

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L-selenocysteine

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based on heuristic

inferred from title

3

object named as

A Holmgren

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author name string

L Zhong

1

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E S Arnér

2

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language of work or name

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publication date

23 May 2000

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Proceedings of the National Academy of Sciences of the United States of America

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97

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11

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5854-9

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Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Refined structure of glutathione reductase at 1.54 A resolution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Convergent evolution of similar function in two structurally divergent enzymes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Cloning, sequencing and functional expression of a novel human thioredoxin reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Contrasting patterns of regulation of the antioxidant selenoproteins, thioredoxin reductase, and glutathione peroxidase, in cancer cells

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Reassessment of Ellman's reagent

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Thioredoxin and glutaredoxin systems

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

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://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

7 April 2017

Regulation of human thioredoxin reductase expression and activity by 3'-untranslated region selenocysteine insertion sequence and mRNA instability elements

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 September 2017

Redox regulation of cellular activation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 September 2017

A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 September 2017

Cloning and sequencing of a human thioredoxin reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 September 2017

Mechanism and structure of thioredoxin reductase from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 September 2017

Functional expression of rat thioredoxin reductase: selenocysteine insertion sequence element is essential for the active enzyme

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

30 May 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

30 May 2018

Thioredoxin reductase activity is decreased by selenium deficiency

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

30 May 2018

Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

30 May 2018

Mitochondrial thioredoxin reductase in bovine adrenal cortex its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 November 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 November 2018

A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=18523

28 November 2018

Rat liver thioredoxin and thioredoxin reductase: purification and characterization

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Cellular thioredoxin reductase activity is regulated by selenium

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Purification of mitochondrial thioredoxin reductase and its involvement in the redox regulation of membrane permeability

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighboring cysteine residue

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Preparation and assay of mammalian thioredoxin and thioredoxin reductase

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Thioredoxin reductase from Plasmodium falciparum: evidence for interaction between the C-terminal cysteine residues and the active site disulfide-dithiol

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

1-Chloro-2,4-dinitrobenzene is an irreversible inhibitor of human thioredoxin reductase. Loss of thioredoxin disulfide reductase activity is accompanied by a large increase in NADPH oxidase activity

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/10801974

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1073/PNAS.100114897

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2000PNAS...97.5854Z

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PMC publication ID

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PubMed publication ID

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ResearchGate publication ID

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