| http://purl.uniprot.org/citations/17350572 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17350572 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17350572 | http://www.w3.org/2000/01/rdf-schema#comment | "ALIX/AIP1 functions in enveloped virus budding, endosomal protein sorting, and many other cellular processes. Retroviruses, including HIV-1, SIV, and EIAV, bind and recruit ALIX through YPX(n)L late-domain motifs (X = any residue; n = 1-3). Crystal structures reveal that human ALIX is composed of an N-terminal Bro1 domain and a central domain that is composed of two extended three-helix bundles that form elongated arms that fold back into a "V." The structures also reveal conformational flexibility in the arms that suggests that the V domain may act as a flexible hinge in response to ligand binding. YPX(n)L late domains bind in a conserved hydrophobic pocket on the second arm near the apex of the V, whereas CHMP4/ESCRT-III proteins bind a conserved hydrophobic patch on the Bro1 domain, and both interactions are required for virus budding. ALIX therefore serves as a flexible, extended scaffold that connects retroviral Gag proteins to ESCRT-III and other cellular-budding machinery."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2007.01.035"xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cell.2007.01.035"xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Hill C.P."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Hill C.P."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Robinson H."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Robinson H."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Zhai Q."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Zhai Q."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Sundquist W.I."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Sundquist W.I."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Chung H.Y."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Chung H.Y."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Fisher R.D."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/author | "Fisher R.D."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/pages | "841-852"xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/pages | "841-852"xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/title | "Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding."xsd:string |
| http://purl.uniprot.org/citations/17350572 | http://purl.uniprot.org/core/title | "Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding."xsd:string |