RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/11333909http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11333909http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11333909http://www.w3.org/2000/01/rdf-schema#comment"The human immunodeficiency virus type 1 (HIV-1) and human T-cell leukemia virus type 1 (HTLV-1) capsid proteins (CA) display similar structures formed by two independently folded N-terminal (NTD) and C-terminal (CTD) domains. To characterize the functions harbored by the HTLV-1 CA domains in particle formation, 12 sites scattered throughout the protein were mutated. The effects of the mutations on Gag membrane binding, proteolytic processing, and virus-like particle secretion were analyzed. It appears that the NTD is the major partner of indirect or direct Gag-Gag interactions. In particular, most of the NTD mutations impaired virion morphogenesis, and no mutation located in the NTD could be fully rescued by coexpression of wild-type Gag. In contrast, the CTD seems not to be involved in Gag-Gag interactions. Nevertheless, an unknown function required for particle formation is located in the CTD. Thus, despite an overall structural similarity between the HIV-1 and HTLV-1 CA proteins, their NTDs and CTDs exhibit different functions."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.org/dc/terms/identifier"doi:10.1128/jvi.75.11.5277-5287.2001"xsd:string
http://purl.uniprot.org/citations/11333909http://purl.org/dc/terms/identifier"doi:10.1128/jvi.75.11.5277-5287.2001"xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Mamoun R.Z."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Mamoun R.Z."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Bouamr F."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Bouamr F."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Lalanne J."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Lalanne J."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Rayne F."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/author"Rayne F."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/pages"5277-5287"xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/pages"5277-5287"xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/title"The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/title"The NH2-terminal domain of the human T-cell leukemia virus type 1 capsid protein is involved in particle formation."xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/volume"75"xsd:string
http://purl.uniprot.org/citations/11333909http://purl.uniprot.org/core/volume"75"xsd:string
http://purl.uniprot.org/citations/11333909http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11333909
http://purl.uniprot.org/citations/11333909http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11333909