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HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels

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Europe PubMed Central

6 August 2017

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Europe PubMed Central

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HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels (English)

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Europe PubMed Central

6 August 2017

Peter J Ratcliffe

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Norma Masson

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Europe PubMed Central

PubMed ID

12829734

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6 August 2017

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English

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1 August 2003

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Europe PubMed Central

6 August 2017

Journal of Cell Science

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Europe PubMed Central

6 August 2017

116

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Europe PubMed Central

6 August 2017

3041-3049

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Europe PubMed Central

6 August 2017

Pt 15

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Europe PubMed Central

6 August 2017

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

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Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by 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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Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension

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A variant of nuclear localization signal of bipartite-type is required for the nuclear translocation of hypoxia inducible factors (1alpha, 2alpha and 3alpha)

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Histone deacetylases induce angiogenesis by negative regulation of tumor suppressor genes

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Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha

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Perspectives on oxygen sensing

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Carboxyl-terminal transactivation activity of hypoxia-inducible factor 1 alpha is governed by a von Hippel-Lindau protein-independent, hydroxylation-regulated association with p300/CBP.

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Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein

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Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway

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Activation of Hypoxia-inducible Factor-1; Definition of Regulatory Domains within the α Subunit

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

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Activation of the HIF pathway in cancer

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Post-transcriptional regulation of vascular endothelial growth factor mRNA by the product of the VHL tumor suppressor gene

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Control of the hypoxic response in Drosophila melanogaster by the basic helix-loop-helix PAS protein similar.

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

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Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression

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Overexpression of PH-4, a novel putative proline 4-hydroxylase, modulates activity of hypoxia-inducible transcription factors

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Jab1 interacts directly with HIF-1alpha and regulates its stability

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

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Activated pp60c-Src leads to elevated hypoxia-inducible factor (HIF)-1alpha expression under normoxia

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Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein

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

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Induction of hypervascularity without leakage or inflammation in transgenic mice overexpressing hypoxia-inducible factor-1alpha

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Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1

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Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling

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Oxygen sensing and molecular adaptation to hypoxia

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Hypoxia: the tumor's gateway to progression along the angiogenic pathway

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Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor suppressor protein

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The PAS superfamily: sensors of environmental and developmental signals

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

1 reference

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Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing

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Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex

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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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Inducible operation of the erythropoietin 3' enhancer in multiple cell lines: evidence for a widespread oxygen-sensing mechanism

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Induction of HIF-1alpha in response to hypoxia is instantaneous

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Angiogenesis is induced in a rabbit model of hindlimb ischemia by naked DNA encoding an HIF-1alpha/VP16 hybrid transcription factor

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Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway

1 reference

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

1 reference

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Cobalt inhibits the interaction between hypoxia-inducible factor-alpha and von Hippel-Lindau protein by direct binding to hypoxia-inducible factor-alpha

1 reference

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Insulin stimulates hypoxia-inducible factor 1 through a phosphatidylinositol 3-kinase/target of rapamycin-dependent signaling pathway

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Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL

1 reference

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Molecular basis of the VHL hereditary cancer syndrome

1 reference

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Mammalian EGLN genes have distinct patterns of mRNA expression and regulation

1 reference

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Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit

1 reference

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The transcriptional activation function of the HIF-like factor requires phosphorylation at a conserved threonine

1 reference

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Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

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Inhibitory PAS domain protein (IPAS) is a hypoxia-inducible splicing variant of the hypoxia-inducible factor-3alpha locus

1 reference

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

1 reference

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

1 reference

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1 reference

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Differential regulation of HIF-1 alpha prolyl-4-hydroxylase genes by hypoxia in human cardiovascular cells

1 reference

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Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway

1 reference

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The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma

1 reference

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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

1 reference

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von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination

1 reference

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

1 reference

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A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

1 reference

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Transactivation and inhibitory domains of hypoxia-inducible factor 1alpha. Modulation of transcriptional activity by oxygen tension

1 reference

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Software and database for the analysis of mutations in the VHL gene

1 reference

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p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1alpha (HIF-1alpha) and enhance the transcriptional activity of HIF-1.

1 reference

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Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation

1 reference

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Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha

1 reference

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Structure of a cephalosporin synthase

1 reference

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FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity

1 reference

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

1 reference

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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

1 reference

12 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1242/JCS.00655

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

1 reference

12 October 2022

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

1 reference

12 October 2022

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EPAS1 trans-activation during hypoxia requires p42/p44 MAPK

1 reference

12 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1242/JCS.00655

Identifiers

DOI

10.1242/JCS.00655

1 reference

stated in

Europe PubMed Central

6 August 2017

1 reference

Europe PubMed Central

PubMed ID

12829734

retrieved

6 August 2017

ResearchGate publication ID

10687687

0 references

(Q35164093)

HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels

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