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http://purl.uniprot.org/citations/10758161http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10758161http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10758161http://www.w3.org/2000/01/rdf-schema#comment"Hypoxia-inducible factor 1 (HIF-1) is a transcription factor that mediates cellular and systemic homeostatic responses to reduced O(2) availability in mammals, including angiogenesis, erythropoiesis, and glycolysis. HIF-1 activity is controlled by the O(2)-regulated expression of the HIF-1alpha subunit. Under nonhypoxic conditions, HIF-1alpha protein is subject to ubiquitination and proteasomal degradation. Here we report that missense mutations and/or deletions involving several different regions of HIF-1alpha result in constitutive expression and transcriptional activity in nonhypoxic cells. We demonstrate that hypoxia results in decreased ubiquitination of HIF-1alpha and that missense mutations increase HIF-1alpha expression under nonhypoxic conditions by blocking ubiquitination."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.org/dc/terms/identifier"doi:10.1073/pnas.080072497"xsd:string
http://purl.uniprot.org/citations/10758161http://purl.org/dc/terms/identifier"doi:10.1073/pnas.080072497"xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/author"Sutter C.H."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/author"Sutter C.H."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/author"Semenza G.L."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/author"Semenza G.L."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/author"Laughner E."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/author"Laughner E."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/pages"4748-4753"xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/pages"4748-4753"xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/title"Hypoxia-inducible factor 1alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/title"Hypoxia-inducible factor 1alpha protein expression is controlled by oxygen-regulated ubiquitination that is disrupted by deletions and missense mutations."xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/10758161http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/10758161http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10758161
http://purl.uniprot.org/citations/10758161http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10758161
http://purl.uniprot.org/citations/10758161http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10758161
http://purl.uniprot.org/citations/10758161http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10758161