C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation (Q24291783)

positive regulation of protein catabolic process

GOA release 2020-03-11

1 reference

Hypoxia-inducible factor prolyl hydroxylase CELE_F22E12.4

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

P Jaakkola

14

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Peter J. Ratcliffe

20

object named as

P J Ratcliffe

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author name string

A C Epstein

1

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J M Gleadle

2

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L A McNeill

3

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K S Hewitson

4

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J O'Rourke

5

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D R Mole

6

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M Mukherji

7

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E Metzen

8

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M I Wilson

9

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A Dhanda

10

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Y M Tian

11

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N Masson

12

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D L Hamilton

13

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R Barstead

15

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J Hodgkin

16

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P H Maxwell

17

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C W Pugh

18

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C J Schofield

ALSCRIPT: a tool to format multiple sequence alignments

19

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publication date

5 October 2001

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language of work or name

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107

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issue

1

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page(s)

43-54

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cites work

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HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1alpha degradation

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Hypoxia inducible factor-alpha binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein

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Lethal paralysis of Caenorhabditis elegans by Pseudomonas aeruginosa

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Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2

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The 2‐His‐1‐Carboxylate Facial Triad — An Emerging Structural Motif in Mononuclear Non‐Heme Iron(II) Enzymes

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Regulation of hypoxia-inducible factor 1α is mediated by an O 2 -dependent degradation domain via the ubiquitin-proteasome pathway

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Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide. Implications for oxygen sensing and signaling

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

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7 January 2021

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

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Hypoxia-inducible factor 1 levels vary exponentially over a physiologically relevant range of O2 tension

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7 January 2021

The Caenorhabditis elegans hif-1 gene encodes a bHLH-PAS protein that is required for adaptation to hypoxia

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Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex

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Prolyl 4-hydroxylases and their protein disulfide isomerase subunit

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SM-20 is a novel mitochondrial protein that causes caspase-dependent cell death in nerve growth factor-dependent neurons

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Studies on the active site of deacetoxycephalosporin C synthase

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

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The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

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Activation of the HIF pathway in cancer

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Oxygen-regulated and transactivating domains in endothelial PAS protein 1: comparison with hypoxia-inducible factor-1alpha.

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Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein

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Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes

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Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes

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Perspectives on oxygen sensing

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HIF-1: mediator of physiological and pathophysiological responses to hypoxia

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Hypoxia-inducible factor 1alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations

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Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein

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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

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Comparative sequence analysis of the VHL tumor suppressor gene

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Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase

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Signal transduction. How do cells sense oxygen?

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11595184

1 reference

Consolidated OpenCitations Corpus – April 2017