pubmed-article:9261347 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C1332700 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C0457083 | lld:lifeskim |
pubmed-article:9261347 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9261347 | pubmed:issue | 9 | lld:pubmed |
pubmed-article:9261347 | pubmed:dateCreated | 1997-9-17 | lld:pubmed |
pubmed-article:9261347 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9261347 | pubmed:abstractText | The chemokine receptor CCR5 is the major fusion coreceptor for macrophage-tropic strains of human immunodeficiency virus type 1 (HIV-1). To define the structures of CCR5 that can support envelope (Env)-mediated membrane fusion, we analyzed the activity of homologs, chimeras, and mutants of human CCR5 in a sensitive gene reporter cell-cell fusion assay. Simian, but not murine, homologs of CCR5 were fully active as HIV-1 fusion coreceptors. Chimeras between CCR5 and divergent chemokine receptors demonstrated the existence of two distinct regions of CCR5 that could be utilized for Env-mediated fusion, the amino-terminal domain and the extracellular loops. Dual-tropic Env proteins were particularly sensitive to alterations in the CCR5 amino-terminal domain, suggesting that this domain may play a pivotal role in the evolution of coreceptor usage in vivo. We identified individual residues in both functional regions, Asp-11, Lys-197, and Asp-276, that contribute to coreceptor function. Deletion of a highly conserved cytoplasmic motif rendered CCR5 incapable of signaling but did not abrogate its ability to function as a coreceptor, implying the independence of fusion and G-protein-mediated chemokine receptor signaling. Finally, we developed a novel monoclonal antibody to CCR5 to assist in future studies of CCR5 expression. | lld:pubmed |
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pubmed-article:9261347 | pubmed:language | eng | lld:pubmed |
pubmed-article:9261347 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9261347 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9261347 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9261347 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9261347 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9261347 | pubmed:month | Sep | lld:pubmed |
pubmed-article:9261347 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:LuZ HZH | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:FRYMM | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:YUMM | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:PeiperS CSC | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:WangZ XZX | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:RuckerJJ | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:DomsR WRW | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:AccavittiM... | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:ZhangT YTY | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:TAMJ CJC | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:DoranzB JBJ | lld:pubmed |
pubmed-article:9261347 | pubmed:author | pubmed-author:SharronMM | lld:pubmed |
pubmed-article:9261347 | pubmed:issnType | Print | lld:pubmed |