The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity (Q35880387)

10 August 2017

The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity (English)

1 reference

10 August 2017

8

1 reference

PMCID

3323130

10 August 2017

Christopher J. Schofield

9

1 reference

10 August 2017

Rachelle S Singleton

2

0 references

Peter J. Ratcliffe

object named as

Peter J Ratcliffe

10

0 references

Ya-Min Tian

7

object named as

Ya-Min Tian

1 reference

10 August 2017

3

Rok Sekirnik

1 reference

10 August 2017

4

David C Trudgian

1 reference

10 August 2017

1

Norma Masson

1 reference

10 August 2017

Lucy J Ambrose

5

1 reference

PMCID

3323130

10 August 2017

Melroy X Miranda

6

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10 August 2017

1 March 2012

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10 August 2017

1 reference

10 August 2017

13

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10 August 2017

3

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10 August 2017

251-257

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Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.

10 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Differential sensitivity of hypoxia inducible factor hydroxylation sites to hypoxia and hydroxylase inhibitors

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

The asparaginyl hydroxylase factor inhibiting HIF-1alpha is an essential regulator of metabolism

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Inter-connection between mitochondria and HIFs

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

The hypoxia-inducible factor-2alpha is stabilized by oxidative stress involving NOX4.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Hydrogen peroxide as an endogenous mediator and exogenous tool in cardiovascular research: issues and considerations.

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-alpha activation

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected].

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Oxygen sensing by HIF hydroxylases

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1alpha during hypoxia: a mechanism of O2 sensing

27 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3323130

JunD reduces tumor angiogenesis by protecting cells from oxidative stress

27 July 2018

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FEMBOR.2012.9

Multiple factors affecting cellular redox status and energy metabolism modulate hypoxia-inducible factor prolyl hydroxylase activity in vivo and in vitro

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FEMBOR.2012.9

Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300.

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1038%2FEMBOR.2012.9

Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22310300

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/EMBOR.2012.9

1 reference

10 August 2017

1 reference

10 August 2017

1 reference

PMCID

3323130