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Hydroxylation of HIF-1: oxygen sensing at the molecular level

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Hydroxylation of HIF-1: oxygen sensing at the molecular level (English)

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Gregg L Semenza

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language of work or name

English

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publication date

August 2004

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Physiology

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volume

19

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page(s)

176-82

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cites work

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Hearts from rodents exposed to intermittent hypoxia or erythropoietin are protected against ischemia-reperfusion injury

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Defective vascularization of HIF-1alpha-null embryos is not associated with VEGF deficiency but with mesenchymal cell death

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

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Surviving ischemia: adaptive responses mediated by hypoxia-inducible factor 1

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Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on 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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The antimycotic ciclopirox olamine induces HIF-1alpha stability, VEGF expression, and angiogenesis

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Perspectives on oxygen sensing

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Cardia bifida, defective heart development and abnormal neural crest migration in embryos lacking hypoxia-inducible factor-1alpha

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HIF-1alpha is essential for myeloid cell-mediated inflammation

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Impaired physiological responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1alpha

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Transcription factor HIF-1 is a necessary mediator of the pasteur effect in mammalian cells.

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Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells

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

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

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

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Temporal, spatial, and oxygen-regulated expression of hypoxia-inducible factor-1 in the lung

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

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Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor

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

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

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Cellular and developmental control of O2 homeostasis by hypoxia-inducible factor 1 alpha

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Abnormal B lymphocyte development and autoimmunity in hypoxia-inducible factor 1alpha -deficient chimeric mice

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

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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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Defective carotid body function and impaired ventilatory responses to chronic hypoxia in mice partially deficient for hypoxia-inducible factor 1 alpha

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

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

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Purification and characterization of hypoxia-inducible factor 1

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DOI

10.1152/PHYSIOL.00001.2004

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3875338

OpenCitations bibliographic resource ID

3875338

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3875338

PubMed publication ID

15304631

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3875338

(Q28276549)

Hydroxylation of HIF-1: oxygen sensing at the molecular level

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