| http://purl.uniprot.org/citations/18842592 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18842592 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18842592 | http://www.w3.org/2000/01/rdf-schema#comment | "Human APOBEC3G (hA3G) is a cytidine deaminase active on HIV single-stranded DNA. Small angle x-ray scattering and molecular envelope restorations predicted a C-terminal dimeric model for RNA-depleted hA3G in solution. Each subunit was elongated, suggesting that individual domains of hA3G are solvent-exposed and therefore may interact with other macromolecules even as isolated substructures. In this study, co-immunoprecipitation and in-cell quenched fluorescence resonance energy transfer assays reveal that hA3G forms RNA-independent oligomers through interactions within its C terminus. Residues 209-336 were necessary and sufficient for homoligomerization. N-terminal domains of hA3G were unable to multimerize but remained functional for Gag and viral infectivity factor (Vif) interactions when expressed apart from the C terminus. These findings corroborate the small angle x-ray scattering structural model and are instructive for development of high throughput screens that target specific domains and their functions to identify HIV/AIDS therapeutics."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m803726200"xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m803726200"xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Liu X."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Liu X."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Smith H.C."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Smith H.C."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Bennett R.P."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Bennett R.P."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Salter J.D."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Salter J.D."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Wedekind J.E."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/author | "Wedekind J.E."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/pages | "33329-33336"xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/pages | "33329-33336"xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/title | "APOBEC3G subunits self-associate via the C-terminal deaminase domain."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/title | "APOBEC3G subunits self-associate via the C-terminal deaminase domain."xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/volume | "283"xsd:string |
| http://purl.uniprot.org/citations/18842592 | http://purl.uniprot.org/core/volume | "283"xsd:string |