RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/16876117http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16876117http://www.w3.org/2000/01/rdf-schema#comment"By use of the yeast two-hybrid system, hepatitis C virus (HCV) F protein was found to interact with a cellular protein named prefoldin 2. The interaction was confirmed by confocal immunofluorescence microscopy as well as coimmunoprecipitation experiments. Prefoldin 2 is a subunit of a hexameric molecular chaperone complex, named prefoldin, which delivers nascent actin and tubulin proteins to the eukaryotic cytosolic chaperonin for facilitated folding. Functional prefoldin spontaneously assembles from its six subunits (prefoldin 1-6). In the yeast three-hybrid system, it was found that expression of HCV F protein impeded the interaction between prefoldin 1 and 2. By performing immunofluorescence experiment and non-denaturing gel electrophoresis, it was shown that expression of HCV F protein resulted in aberrant organization of tubulin cytoskeleton. Since HCV replication requires intact microtubule and actin polymerization, HCV F protein may serve as a modulator to prevent high level of HCV replication and thus contributes to viral persistence in chronic HCV infection."xsd:string
http://purl.uniprot.org/citations/16876117http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2006.07.062"xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/author"Yeh C.T."xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/author"Chao C.H."xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/author"Tsao M.L."xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/pages"271-277"xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/title"Interaction of hepatitis C virus F protein with prefoldin 2 perturbs tubulin cytoskeleton organization."xsd:string
http://purl.uniprot.org/citations/16876117http://purl.uniprot.org/core/volume"348"xsd:string
http://purl.uniprot.org/citations/16876117http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16876117
http://purl.uniprot.org/citations/16876117http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16876117
http://purl.uniprot.org/uniprot/P0C045#attribution-1AA7FCBC146707F2F6B3BFA8DC29706Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/Q9UHV9#attribution-1AA7FCBC146707F2F6B3BFA8DC29706Dhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/Q9UHV9#attribution-AAE2548AD0977E3039C4D08FB7143E23http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/O60925#attribution-AAE2548AD0977E3039C4D08FB7143E23http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/#_P0C045-mappedCitation-16876117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/#_O60925-mappedCitation-16876117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/#_Q9UHV9-mappedCitation-16876117http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/Q9UHV9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/O60925http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16876117
http://purl.uniprot.org/uniprot/P0C045http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16876117