Hydroxylation of HIF-1: oxygen sensing at the molecular level (Q28276549)

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

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title

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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published in

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

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Partial HIF-1alpha deficiency impairs pulmonary arterial myocyte electrophysiological responses to hypoxia

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Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response

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

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Hypoxia-inducible factor 1alpha is essential for cell cycle arrest during hypoxia

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

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Intramyocardial injection of naked DNA encoding HIF-1alpha/VP16 hybrid to enhance angiogenesis in an acute myocardial infarction model in the rat.

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Role of HIF-1alpha in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis

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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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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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Cell type-specific regulation of angiogenic growth factor gene expression and induction of angiogenesis in nonischemic tissue by a constitutively active form of hypoxia-inducible factor 1.

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

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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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12 October 2022

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

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The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development

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Peptide blockade of HIFalpha degradation modulates cellular metabolism and angiogenesis

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YC-1: a potential anticancer drug targeting hypoxia-inducible factor 1.

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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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12 October 2022

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

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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

1 reference

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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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Asialoerythropoietin is a nonerythropoietic cytokine with broad neuroprotective activity in vivo.

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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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Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau

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Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch

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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

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

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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

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

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

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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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HIF1alpha is a critical regulator of secretory differentiation and activation, but not vascular expansion, in the mouse mammary gland

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

1 reference

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Purification and characterization of hypoxia-inducible factor 1

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12 October 2022

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10.1152/PHYSIOL.00001.2004

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3875338

OpenCitations bibliographic resource ID

3875338

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

3875338

Hydroxylation of HIF-1: oxygen sensing at the molecular level (Q28276549)

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Hydroxylation of HIF-1: oxygen sensing at the molecular level (Q28276549)

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