| pubmed-article:16611898 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16611898 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:16611898 | lifeskim:mentions | umls-concept:C1659441 | lld:lifeskim |
| pubmed-article:16611898 | lifeskim:mentions | umls-concept:C1537068 | lld:lifeskim |
| pubmed-article:16611898 | lifeskim:mentions | umls-concept:C1422036 | lld:lifeskim |
| pubmed-article:16611898 | lifeskim:mentions | umls-concept:C0597526 | lld:lifeskim |
| pubmed-article:16611898 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:16611898 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:16611898 | pubmed:dateCreated | 2006-4-13 | lld:pubmed |
| pubmed-article:16611898 | pubmed:abstractText | The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a homotrimer of gp120/gp41 heterodimers to support virus entry. During the process of virus entry, an individual HIV-1 envelope glycoprotein trimer binds the cellular receptors CD4 and CCR5/CXCR4 and mediates the fusion of the viral and the target cellular membranes. By studying the function of heterotrimers between wild-type and nonfunctional mutant envelope glycoproteins, we found that two wild-type subunits within an envelope glycoprotein trimer are required to support virus entry. Complementation between HIV-1 envelope glycoprotein mutants defective in different functions to allow virus entry was not evident. These results assist our understanding of the mechanisms whereby the HIV-1 envelope glycoproteins mediate virus entry and membrane fusion and guide attempts to inhibit these processes. | lld:pubmed |
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| pubmed-article:16611898 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16611898 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16611898 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16611898 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16611898 | pubmed:month | May | lld:pubmed |
| pubmed-article:16611898 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16611898 | pubmed:author | pubmed-author:SodroskiJosep... | lld:pubmed |
| pubmed-article:16611898 | pubmed:author | pubmed-author:YangXinzhenX | lld:pubmed |
| pubmed-article:16611898 | pubmed:author | pubmed-author:LeeSandraS | lld:pubmed |
| pubmed-article:16611898 | pubmed:author | pubmed-author:RenXinpingX | lld:pubmed |
| pubmed-article:16611898 | pubmed:author | pubmed-author:KurtevaSvetla... | lld:pubmed |
| pubmed-article:16611898 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16611898 | pubmed:volume | 80 | lld:pubmed |
| pubmed-article:16611898 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16611898 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16611898 | pubmed:pagination | 4388-95 | lld:pubmed |
| pubmed-article:16611898 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:16611898 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16611898 | pubmed:articleTitle | Subunit stoichiometry of human immunodeficiency virus type 1 envelope glycoprotein trimers during virus entry into host cells. | lld:pubmed |
| pubmed-article:16611898 | pubmed:affiliation | Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, 44 Binney Street, JFB 824, Boston, Massachusetts 02115, USA. xinzhen_yang@dfci.harvard.edu | lld:pubmed |
| pubmed-article:16611898 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16611898 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16611898 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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