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http://purl.uniprot.org/citations/28794491http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28794491http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28794491http://www.w3.org/2000/01/rdf-schema#comment"Ebola virus causes devastating hemorrhagic fever outbreaks for which no approved therapeutic exists. The viral nucleocapsid, which is minimally composed of the proteins NP, VP35, and VP24, represents an attractive target for drug development; however, the molecular determinants that govern the interactions and functions of these three proteins are still unknown. Through a series of mutational analyses, in combination with biochemical and bioinformatics approaches, we identified a region on VP24 that was critical for its interaction with NP. Importantly, we demonstrated that the interaction between VP24 and NP was required for both nucleocapsid assembly and genome packaging. Not only does this study underscore the critical role that these proteins play in the viral replication cycle, but it also identifies a key interaction interface on VP24 that may serve as a novel target for antiviral therapeutic intervention."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.org/dc/terms/identifier"doi:10.1038/s41598-017-08167-8"xsd:string
http://purl.uniprot.org/citations/28794491http://purl.org/dc/terms/identifier"doi:10.1038/s41598-017-08167-8"xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Banadyga L."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Banadyga L."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Ebihara H."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Ebihara H."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Groseth A."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Groseth A."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Hoenen T."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Hoenen T."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Ambroggio X."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Ambroggio X."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Dunham E."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/author"Dunham E."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/name"Sci. Rep."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/name"Sci. Rep."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/pages"7698"xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/pages"7698"xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/title"Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging."xsd:string
http://purl.uniprot.org/citations/28794491http://purl.uniprot.org/core/title"Ebola virus VP24 interacts with NP to facilitate nucleocapsid assembly and genome packaging."xsd:string