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http://purl.uniprot.org/citations/3656418http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3656418http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3656418http://www.w3.org/2000/01/rdf-schema#comment"Purified Sindbis virus nucleocapsids were reacted with a variety of bifunctional protein-specific cross-linking agents. The products were analyzed in concentration-gradient polyacrylamide gels and amounts of various products determined. These studies indicated that available lysine residues within adjacent capsid proteins in purified intact nucleocapsids are separated by 6 A. The capsid proteins in intact nucleocapsids are cross-linked in a pattern predicted for discrete monomeric entities, rather than in dimeric or trimeric aggregates. Purified, soluble capsid protein exists in a conformation that differs from the arrangement of protein within nucleocapsids. These conformational differences suggest that topological changes may occur in the capsid protein during virus maturation. Cross-linked nucleocapsids that were treated with RNases resulted in the generation of RNA-free protein shells that retained hexagonal morphology, indicating that, together, the RNA and protein form the outer surface of the nucleocapsid. These data are used to produce a model of the Sindbis virus nucleocapsid in which the proteins are arranged quasi-equivalently in a T = 4 icosahedral shell."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.org/dc/terms/identifier"doi:10.1016/0022-2836(87)90657-7"xsd:string
http://purl.uniprot.org/citations/3656418http://purl.org/dc/terms/identifier"doi:10.1016/0022-2836(87)90657-7"xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/author"Brown D.T."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/author"Brown D.T."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/author"Coombs K."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/author"Coombs K."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/date"1987"xsd:gYear
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/pages"359-371"xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/pages"359-371"xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/title"Organization of the Sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/title"Organization of the Sindbis virus nucleocapsid as revealed by bifunctional cross-linking agents."xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/volume"195"xsd:string
http://purl.uniprot.org/citations/3656418http://purl.uniprot.org/core/volume"195"xsd:string
http://purl.uniprot.org/citations/3656418http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3656418
http://purl.uniprot.org/citations/3656418http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3656418
http://purl.uniprot.org/citations/3656418http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3656418
http://purl.uniprot.org/citations/3656418http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3656418
http://purl.uniprot.org/uniprot/P03316http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3656418
http://purl.uniprot.org/uniprot/P0DOK0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3656418