(Q34049908)

30 July 2017

1 reference

title

AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase (English)

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30 July 2017

L B Poole

1

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30 July 2017

C M Reynolds

2

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30 July 2017

Z A Wood

3

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30 July 2017

P A Karplus

4

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30 July 2017

H R Ellis

5

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30 July 2017

M Li Calzi

6

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30 July 2017

language of work or name

English

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publication date

1 October 2000

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30 July 2017

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30 July 2017

volume

267

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30 July 2017

issue

20

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30 July 2017

page(s)

6126-6133

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Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes

30 July 2017

cites work

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Comparison of sequence profiles. Strategies for structural predictions using sequence information

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: genetic characterization and cloning of ahp

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

General and oxidative stress responses in Bacillus subtilis: cloning, expression, and mutation of the alkyl hydroperoxide reductase operon.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Isolation and analysis of the Xanthomonas alkyl hydroperoxide reductase gene and the peroxide sensor regulator genes ahpC and ahpF-oxyR-orfX.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Characterization of transcription organization and analysis of unique expression patterns of an alkyl hydroperoxide reductase C gene (ahpC) and the peroxide regulator operon ahpF-oxyR-orfX from Xanthomonas campestris pv. phaseoli

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

A homologue to the Escherichia coli alkyl hydroperoxide reductase AhpC is induced by osmotic upshock in Staphylococcus aureus

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Cloning of an organic solvent-resistance gene in Escherichia coli: the unexpected role of alkylhydroperoxide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Isolation and transposon mutagenesis of a Pseudomonas putida KT2442 toluene-resistant variant: involvement of an efflux system in solvent resistance

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

A flavoprotein functional as NADH oxidase from Amphibacillus xylanus Ep01: purification and characterization of the enzyme and structural analysis of its gene

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Molecular cloning and sequence analysis of the gene encoding the H2O2-forming NADH oxidase from Streptococcus mutans

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Tryptic digestion of NADH dehydrogenase from alkalophilic Bacillus

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Nucleotide sequence of the gene encoding NADH dehydrogenase from an alkalophile, Bacillus sp. strain YN-1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hy

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Purification and characterisation of NADH oxidase from Thermus aquaticus YT-1 and evidence that it functions in a peroxide-reduction system.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Peroxide reductase activity of NADH dehydrogenase of an alkaliphilic Bacillus in the presence of a 22-kDa protein component from Amphibacillus xylanus

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Reaction mechanism of Amphibacillus xylanus NADH oxidase/alkyl hydroperoxide reductase flavoprotein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavi

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity.

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Thioredoxin reductase two modes of catalysis have evolved

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome

21 January 2018

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2000.01704.X

10.1046/J.1432-1327.2000.01704.X

21 January 2018

Identifiers

DOI

1 reference

30 July 2017

1 reference