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http://purl.uniprot.org/citations/9651361http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9651361http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9651361http://www.w3.org/2000/01/rdf-schema#comment"Hepatitis C virus (HCV) core protein, a component of viral nucleocapsid, has been shown to modulate cellular and viral promoter activities. To identify potential cellular targets for HCV core protein, a human liver cDNA library was screened for core-interacting proteins using the yeast two-hybrid system. Among the proteins identified was heterogeneous nuclear ribonucleoprotein K (hnRNP K), which has been demonstrated to be a transcriptional regulator. The interaction of HCV core protein with hnRNP K was confirmed by glutathione S-transferase fusion protein binding assay, protein-protein blotting assay, and coimmunoprecipitation in vitro and in vivo. Additionally, these two proteins were shown to be partially colocalized in the nucleus. The hnRNP K-binding site in HCV core protein was mapped to the region from amino acid residues 25-91, a hydrophilic area near the N terminus. The HCV core protein-binding domain was located within amino acid residues 250 to 392, which contain the three proline-rich domains, of hnRNP K. Furthermore, HCV core protein relieved the suppression effect of hnRNP K on the activity of the human thymidine kinase gene promoter. The specific binding of HCV core protein to hnRNP K suggests that multiple functions of hnRNP K may be disrupted by the core protein during HCV infection and thus explains, in part, the pathogenesis of HCV."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.28.17651"xsd:string
http://purl.uniprot.org/citations/9651361http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.28.17651"xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Matsumoto M."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Matsumoto M."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Schneider R."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Schneider R."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Hwang S.B."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Hwang S.B."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Chou H.-C."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Chou H.-C."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Lai M.M.C."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Lai M.M.C."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Lee A.S."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Lee A.S."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Hsieh T.-Y."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/author"Hsieh T.-Y."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/pages"17651-17659"xsd:string
http://purl.uniprot.org/citations/9651361http://purl.uniprot.org/core/pages"17651-17659"xsd:string