RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/19091860http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19091860http://www.w3.org/2000/01/rdf-schema#comment"We have previously reported on the ubiquitylation and degradation of hepatitis C virus core protein. Here we demonstrate that proteasomal degradation of the core protein is mediated by two distinct mechanisms. One leads to polyubiquitylation, in which lysine residues in the N-terminal region are preferential ubiquitylation sites. The other is independent of the presence of ubiquitin. Gain- and loss-of-function analyses using lysineless mutants substantiate the hypothesis that the proteasome activator PA28gamma, a binding partner of the core, is involved in the ubiquitin-independent degradation of the core protein. Our results suggest that turnover of this multifunctional viral protein can be tightly controlled via dual ubiquitin-dependent and -independent proteasomal pathways."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.org/dc/terms/identifier"doi:10.1128/jvi.01690-08"xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Fukuda K."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Ishii K."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Matsuura Y."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Miyamura T."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Moriishi K."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Suzuki T."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Suzuki R."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Wakita T."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Shirakura M."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/author"Shoji I."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/name"J Virol"xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/pages"2389-2392"xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/title"Proteasomal turnover of hepatitis C virus core protein is regulated by two distinct mechanisms: a ubiquitin-dependent mechanism and a ubiquitin-independent but PA28gamma-dependent mechanism."xsd:string
http://purl.uniprot.org/citations/19091860http://purl.uniprot.org/core/volume"83"xsd:string
http://purl.uniprot.org/citations/19091860http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19091860
http://purl.uniprot.org/citations/19091860http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19091860
http://purl.uniprot.org/uniprot/#_B7Z8D3-mappedCitation-19091860http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19091860
http://purl.uniprot.org/uniprot/#_B3KQ25-mappedCitation-19091860http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19091860
http://purl.uniprot.org/uniprot/#_J7FRP4-mappedCitation-19091860http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19091860
http://purl.uniprot.org/uniprot/#_K9J957-mappedCitation-19091860http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19091860
http://purl.uniprot.org/uniprot/#_P61289-mappedCitation-19091860http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19091860