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http://purl.uniprot.org/citations/12464182http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12464182http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12464182http://www.w3.org/2000/01/rdf-schema#comment"Hypoxia-inducible factor 1 (HIF-1) plays a central role in cellular adaptation to changes in oxygen availability. Recently, prolyl hydroxylation was identified as a key regulatory event that targets the HIF-1alpha subunit for proteasomal degradation via the pVHL ubiquitination complex. In this report, we reveal an important function for ARD1 in mammalian cells as a protein acetyltransferase by direct binding to HIF-1alpha to regulate its stability. We present further evidence showing that ARD1-mediated acetylation enhances interaction of HIF-1alpha with pVHL and HIF-1alpha ubiquitination, suggesting that the acetylation of HIF-1alpha by ARD1 is critical to proteasomal degradation. Therefore, we have concluded that the role of ARD1 in the acetylation of HIF-1alpha provides a key regulatory mechanism underlying HIF-1alpha stability."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)01085-1"xsd:string
http://purl.uniprot.org/citations/12464182http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)01085-1"xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Kim S.-H."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Kim S.-H."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Kim K.-W."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Kim K.-W."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Lee K.-J."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Lee K.-J."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Ahn M.-Y."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Ahn M.-Y."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Bae M.-H."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Bae M.-H."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Bae M.-K."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Bae M.-K."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Jeong J.-W."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Jeong J.-W."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Yoo M.-A."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Yoo M.-A."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Sohn T.-K."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Sohn T.-K."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Song E.-J."xsd:string
http://purl.uniprot.org/citations/12464182http://purl.uniprot.org/core/author"Song E.-J."xsd:string