pubmed-article:18322015 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C0475463 | lld:lifeskim |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C0913822 | lld:lifeskim |
pubmed-article:18322015 | lifeskim:mentions | umls-concept:C0913823 | lld:lifeskim |
pubmed-article:18322015 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:18322015 | pubmed:dateCreated | 2008-3-12 | lld:pubmed |
pubmed-article:18322015 | pubmed:abstractText | Most antibodies induced by HIV-1 are ineffective at preventing initiation or spread of infection because they are either nonneutralizing or narrowly isolate-specific. Rare, "broadly neutralizing" antibodies have been detected that recognize relatively conserved regions on the envelope glycoprotein. Using stringently characterized, homogeneous preparations of trimeric HIV-1 envelope protein in relevant conformations, we have analyzed the molecular mechanism of neutralization by two of these antibodies, 2F5 and 4E10. We find that their epitopes, in the membrane-proximal segment of the envelope protein ectodomain, are exposed only on a form designed to mimic an intermediate state during viral entry. These results help explain the rarity of 2F5- and 4E10-like antibody responses and suggest a strategy for eliciting them. | lld:pubmed |
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pubmed-article:18322015 | pubmed:language | eng | lld:pubmed |
pubmed-article:18322015 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18322015 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:18322015 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18322015 | pubmed:month | Mar | lld:pubmed |
pubmed-article:18322015 | pubmed:issn | 1091-6490 | lld:pubmed |
pubmed-article:18322015 | pubmed:author | pubmed-author:ReyF AFA | lld:pubmed |
pubmed-article:18322015 | pubmed:author | pubmed-author:ChenBingB | lld:pubmed |
pubmed-article:18322015 | pubmed:author | pubmed-author:MorelliMarcoM | lld:pubmed |
pubmed-article:18322015 | pubmed:author | pubmed-author:ChengYifanY | lld:pubmed |
pubmed-article:18322015 | pubmed:author | pubmed-author:Rits-VollochS... | lld:pubmed |
pubmed-article:18322015 | pubmed:author | pubmed-author:PengHanqinH | lld:pubmed |
pubmed-article:18322015 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:18322015 | pubmed:day | 11 | lld:pubmed |
pubmed-article:18322015 | pubmed:volume | 105 | lld:pubmed |
pubmed-article:18322015 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18322015 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18322015 | pubmed:pagination | 3739-44 | lld:pubmed |
pubmed-article:18322015 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:18322015 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18322015 | pubmed:articleTitle | A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. | lld:pubmed |
pubmed-article:18322015 | pubmed:affiliation | Laboratory of Molecular Medicine, Children's Hospital, and Department of Pediatrics, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA. | lld:pubmed |
pubmed-article:18322015 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18322015 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
pubmed-article:18322015 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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