Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains (Q24337743)

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English	Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains	scientific article

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20 January 2020

Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains (English)

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20 January 2020

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peptidyl-histidine dioxygenase activity

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

peptidyl-histidine hydroxylation

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

1 reference

GOA release 2020-03-11

Hypoxia inducible factor 1 subunit alpha inhibitor

1 reference

GOA release 2020-03-11

ankyrin repeat binding

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GOA release 2020-03-11

Rasheduzzaman Chowdhury

2

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20 January 2020

Christopher J. Schofield

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20 January 2020

Refaat B. Hamed

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20 January 2020

Michael A McDonough

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20 January 2020

Benedikt M. Kessler

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20 January 2020

Matthew Cockman

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20 January 2020

Peter J. Ratcliffe

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20 January 2020

Timothy D W Claridge

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Timothy D W Claridge

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20 January 2020

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Ming Yang

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20 January 2020

Wei Ge

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20 January 2020

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23 February 2011

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20 January 2020

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20 January 2020

278

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20 January 2020

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20 January 2020

1086-1097

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20 January 2020

Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3569879

19 March 2017

Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen

1 reference

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19 March 2017

MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3569879

19 March 2017

Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways

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19 March 2017

ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism

1 reference

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19 March 2017

Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor

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19 March 2017

Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)

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19 March 2017

Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha

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19 March 2017

Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the beta-carbon of asparagine-803

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3569879

19 March 2017

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

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19 March 2017

Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)

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19 March 2017

Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold

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19 March 2017

Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein

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19 March 2017

X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates

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19 March 2017

Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases

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19 March 2017

Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

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19 March 2017

Hypoxia-dependent sequestration of an oxygen sensor by a widespread structural motif can shape the hypoxic response--a predictive kinetic model

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27 September 2017

FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins.

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27 September 2017

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

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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].

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Asparaginyl beta-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function.

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21 January 2018

Auto-hydroxylation of FIH-1: an Fe(ii), alpha-ketoglutarate-dependent human hypoxia sensor.

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21 January 2018

Differences in hydroxylation and binding of Notch and HIF-1alpha demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1).

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Identifiers

10.1111/J.1742-4658.2011.08022.X

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Europe PubMed Central

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20 January 2020

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20 January 2020

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