Home
Random
Nearby
Log in
Settings
Donate
About Wikidata
Disclaimers
Search
(Q26853574)
Watch
English
In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
scientific article
In the Absence of Thioredoxins, What Are the Reductants for Peroxiredoxins in Thermotoga maritima ?
In more languages
edit
Statements
instance of
scholarly article
1 reference
stated in
PubMed
title
In the absence of thioredoxins, what are the reductants for peroxiredoxins in Thermotoga maritima?
(English)
1 reference
stated in
PubMed
main subject
cell biology
0 references
clinical chemistry
0 references
Thermotoga
1 reference
based on heuristic
inferred from title
Thermotoga maritima
object named as
Thermotoga maritima
1 reference
based on heuristic
inferred from title
author
Ahmed Haouz
series ordinal
10
0 references
Nicolas Rouhier
series ordinal
11
0 references
Arnaud Hecker
series ordinal
4
0 references
Pascalita Prosper
series ordinal
2
0 references
Jean-Pierre Jacquot
object named as
Jean-Pierre Jacquot
series ordinal
8
0 references
author name string
Jérémy Couturier
series ordinal
1
1 reference
stated in
Crossref
Alison M. Winger
series ordinal
3
1 reference
stated in
Crossref
Masakazu Hirasawa
series ordinal
5
1 reference
stated in
Crossref
David B. Knaff
series ordinal
6
1 reference
stated in
Crossref
Pierre Gans
series ordinal
7
1 reference
stated in
Crossref
Alda Navaza
series ordinal
9
1 reference
stated in
Crossref
language of work or name
English
1 reference
stated in
PubMed
publication date
1 May 2013
1 reference
stated in
PubMed
published in
Antioxidants & Redox Signaling
1 reference
stated in
PubMed
volume
18
1 reference
stated in
PubMed
issue
13
1 reference
stated in
PubMed
page(s)
1613-22
1 reference
stated in
PubMed
cites work
Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 September 2017
Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 September 2017
Subdivision of the bacterioferritin comigratory protein family of bacterial peroxiredoxins based on catalytic activity
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 September 2017
Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 September 2017
The plant multigenic family of thiol peroxidases
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 September 2017
Interrogating the molecular details of the peroxiredoxin activity of the Escherichia coli bacterioferritin comigratory protein using high-resolution mass spectrometry.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 November 2018
Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 November 2018
Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 November 2018
An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3613187
retrieved
28 November 2018
Identifiers
DOI
10.1089/ARS.2012.4739
0 references
PMC publication ID
3613187
1 reference
stated in
PubMed
PubMed publication ID
22866991
1 reference
stated in
PubMed
ResearchGate publication ID
230621769
0 references
Sitelinks
Wikipedia
(0 entries)
edit
Wikibooks
(0 entries)
edit
Wikinews
(0 entries)
edit
Wikiquote
(0 entries)
edit
Wikisource
(0 entries)
edit
Wikiversity
(0 entries)
edit
Wikivoyage
(0 entries)
edit
Wiktionary
(0 entries)
edit
Multilingual sites
(0 entries)
edit