(Q40527027)

English

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].

scientific article published on 9 August 2004

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scholarly article

1 reference

Europe PubMed Central

21 September 2017

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]. (English)

1 reference

Europe PubMed Central

21 September 2017

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Jonathan M. Gleadle

6

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Europe PubMed Central

21 September 2017

Peter J. Ratcliffe

7

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Europe PubMed Central

21 September 2017

2

object named as

Ya-Min Tian

1 reference

Europe PubMed Central

21 September 2017

1

object named as

Ineke P Stolze

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Europe PubMed Central

21 September 2017

Rebecca J Appelhoff

3

object named as

Rebecca J Appelhoff

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Europe PubMed Central

21 September 2017

author name string

Helen Turley

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Europe PubMed Central

21 September 2017

Charles C Wykoff

5

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Europe PubMed Central

21 September 2017

language of work or name

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publication date

9 August 2004

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Europe PubMed Central

21 September 2017

number of pages

7

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

21 September 2017

279

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Europe PubMed Central

21 September 2017

42719-42725

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Europe PubMed Central

21 September 2017

41

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Europe PubMed Central

21 September 2017

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

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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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Substrate requirements of the oxygen-sensing asparaginyl hydroxylase factor-inhibiting hypoxia-inducible factor

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Hypoxia-inducible factor-1 (HIF-1) promotes its degradation by induction of HIF-alpha-prolyl-4-hydroxylases.

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HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation

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Expression of the gene encoding the proapoptotic Nip3 protein is induced by hypoxia

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A conserved family of prolyl-4-hydroxylases that modify HIF

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HIFalpha targeted for VHL-mediated destruction by proline hydroxylation: implications for O2 sensing

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

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Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation

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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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C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

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

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Identifiers

10.1074/JBC.M406713200

1 reference

Europe PubMed Central

21 September 2017

1 reference

Europe PubMed Central

21 September 2017

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