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http://purl.uniprot.org/citations/11641274http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11641274http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11641274http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11641274http://www.w3.org/2000/01/rdf-schema#comment"Hypoxia-inducible factor 1 (HIF-1) is a master regulator of oxygen homeostasis that controls angiogenesis, erythropoiesis, and glycolysis via transcriptional activation of target genes under hypoxic conditions. O(2)-dependent binding of the von Hippel-Lindau (VHL) tumor suppressor protein targets the HIF-1alpha subunit for ubiquitination and proteasomal degradation. The activity of the HIF-1alpha transactivation domains is also O(2) regulated by a previously undefined mechanism. Here, we report the identification of factor inhibiting HIF-1 (FIH-1), a protein that binds to HIF-1alpha and inhibits its transactivation function. In addition, we demonstrate that FIH-1 binds to VHL and that VHL also functions as a transcriptional corepressor that inhibits HIF-1alpha transactivation function by recruiting histone deacetylases. Involvement of VHL in association with FIH-1 provides a unifying mechanism for the modulation of HIF-1alpha protein stabilization and transcriptional activation in response to changes in cellular O(2) concentration."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.org/dc/terms/identifier"doi:10.1101/gad.924501"xsd:string
http://purl.uniprot.org/citations/11641274http://purl.org/dc/terms/identifier"doi:10.1101/gad.924501"xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/author"Hirota K."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/author"Hirota K."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/author"Semenza G.L."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/author"Semenza G.L."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/author"Mahon P.C."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/author"Mahon P.C."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/pages"2675-2686"xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/pages"2675-2686"xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/title"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/title"FIH-1: a novel protein that interacts with HIF-1alpha and VHL to mediate repression of HIF-1 transcriptional activity."xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/11641274http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/11641274http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11641274
http://purl.uniprot.org/citations/11641274http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11641274
http://purl.uniprot.org/citations/11641274http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11641274