| http://purl.uniprot.org/citations/19327811 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19327811 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19327811 | http://www.w3.org/2000/01/rdf-schema#comment | "The human immunodeficiency virus type 1 (HIV-1) matrix (MA) protein represents the N-terminal domain of the HIV-1 precursor Gag (PrGag) protein and carries an N-terminal myristate (Myr) group. HIV-1 MA fosters PrGag membrane binding, as well as assembly of envelope (Env) proteins into virus particles, and recent studies have shown that HIV-1 MA preferentially directs virus assembly at plasma membrane sites enriched in cholesterol and phosphatidylinositol-(4,5)-bisphosphate (PI[4,5]P(2)). To characterize the membrane binding of MA and PrGag proteins, we have examined how Myr-MA proteins, and proteins composed of Myr-MA and its neighbor Gag capsid (CA) protein associate on membranes containing cholesterol and PI[4,5]P(2). Our results indicate that Myr-MA assembles as a hexamer of trimers on such membranes, and imply that MA trimers interconnect CA hexamer rings in immature virus particles. Our observations suggest a model for the organization of PrGag proteins, and for MA-Env protein interactions."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.virol.2009.02.048"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.virol.2009.02.048"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/author | "Barklis E."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/author | "Barklis E."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/author | "Alfadhli A."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/author | "Alfadhli A."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/author | "Barklis R.L."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/author | "Barklis R.L."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/name | "Virology"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/name | "Virology"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/pages | "466-472"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/pages | "466-472"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/title | "HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/title | "HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate."xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/volume | "387"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://purl.uniprot.org/core/volume | "387"xsd:string |
| http://purl.uniprot.org/citations/19327811 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19327811 |
| http://purl.uniprot.org/citations/19327811 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19327811 |
| http://purl.uniprot.org/citations/19327811 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19327811 |
| http://purl.uniprot.org/citations/19327811 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19327811 |