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http://purl.uniprot.org/citations/19403670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19403670http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19403670http://www.w3.org/2000/01/rdf-schema#comment"Diverse members of the Paramyxovirus family of negative-strand RNA viruses effectively suppress host innate immune responses through the actions of their V proteins. The V protein mediates interference with the interferon regulatory RNA helicase MDA5 to avoid cellular antiviral responses. Analysis of the interaction interface revealed the MDA5 helicase C domain as necessary and sufficient for association with V proteins from human parainfluenza virus type 2, parainfluenza virus type 5, measles virus, mumps virus, Hendra virus, and Nipah virus. The identified approximately 130-residue region is highly homologous between MDA5 and the related antiviral helicase LGP2, but not RIG-I. Results indicate that the paramyxovirus V proteins can also associate with LGP2. The V protein interaction was found to disrupt ATP hydrolysis mediated by both MDA5 and LGP2. These findings provide a potential mechanistic basis for V protein-mediated helicase interference and identify LGP2 as a second cellular RNA helicase targeted by paramyxovirus V proteins."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00153-09"xsd:string
http://purl.uniprot.org/citations/19403670http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00153-09"xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Komuro A."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Komuro A."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Bamming D."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Bamming D."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Barber G."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Barber G."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Horvath C.M."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Horvath C.M."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Parisien J.P."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Parisien J.P."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Ramachandran A."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Ramachandran A."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Rodriguez J.J."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Rodriguez J.J."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Wojahn R.D."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/author"Wojahn R.D."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/19403670http://purl.uniprot.org/core/name"J. Virol."xsd:string