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http://purl.uniprot.org/citations/16956324http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16956324http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16956324http://www.w3.org/2000/01/rdf-schema#comment"A central means by which mammalian cells respond to low oxygen tension is through the activation of the transcription factor HIF-1 (hypoxia-inducible factor-1). Under normoxic conditions, HIF-1alpha (the alpha subunit of HIF-1) is targeted for rapid degradation by the ubiquitin-proteasome pathway. Under hypoxic conditions, this degradation is inhibited, thereby leading to the stabilization and activation of HIF-1alpha. Here, we report the identification of IOP1 (iron-only hydrogenase-like protein 1), a protein homologous with enzymes present in anaerobic organisms that contain a distinctive iron-sulfur cluster. IOP1 is present in a broad range of cell types. Knockdown of IOP1 using siRNA (small interfering RNA) in mammalian cells increases protein levels of HIF-1alpha under both normoxic and hypoxic conditions, and augments hypoxia-induced HRE (hypoxia response element) reporter gene and endogenous HIF-1alpha target gene expressions. We find that IOP1 knockdown up-regulates HIF-1alpha mRNA levels, thereby providing a mechanism by which knockdown induces the observed effects. The results collectively provide evidence that IOP1 is a component of the protein network that regulates HIF-1alpha in mammalian cells."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.org/dc/terms/identifier"doi:10.1042/bj20060635"xsd:string
http://purl.uniprot.org/citations/16956324http://purl.org/dc/terms/identifier"doi:10.1042/bj20060635"xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Huang J."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Zhao Q."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Zhao Q."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Song D."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Song D."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Flores A."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Flores A."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Lee F.S."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Lee F.S."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Mooney S.M."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Mooney S.M."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Shaw L.M."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/author"Shaw L.M."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/name"Biochem. J."xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/pages"341-352"xsd:string
http://purl.uniprot.org/citations/16956324http://purl.uniprot.org/core/pages"341-352"xsd:string