| pubmed-article:16227301 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16227301 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:16227301 | lifeskim:mentions | umls-concept:C0080194 | lld:lifeskim |
| pubmed-article:16227301 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16227301 | lifeskim:mentions | umls-concept:C1533157 | lld:lifeskim |
| pubmed-article:16227301 | lifeskim:mentions | umls-concept:C0599013 | lld:lifeskim |
| pubmed-article:16227301 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:16227301 | pubmed:dateCreated | 2005-10-17 | lld:pubmed |
| pubmed-article:16227301 | pubmed:abstractText | We recently described the isolation and structural characterization of 2'-fluoropyrimidine-substituted RNA aptamers that bind to gp120 of R5 strains of human immunodeficiency virus type 1 and thereby potently neutralize the infectivity of phylogenetically diverse R5 strains. Here we investigate the physical basis of their antiviral action. We show that both N-linked oligosaccharides and the variable loops V1/V2 and V3 are not required for binding of one aptamer, B40, to gp120. Using surface plasmon resonance binding analyses, we show that the aptamer binds to the CCR5-binding site on gp120 in a relatively CD4-independent manner, providing a mechanistic explanation for its neutralizing potency. | lld:pubmed |
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| pubmed-article:16227301 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16227301 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16227301 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16227301 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16227301 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:16227301 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:16227301 | pubmed:author | pubmed-author:WyattRichardR | lld:pubmed |
| pubmed-article:16227301 | pubmed:author | pubmed-author:JamesWilliamW | lld:pubmed |
| pubmed-article:16227301 | pubmed:author | pubmed-author:LeaSusan MSM | lld:pubmed |
| pubmed-article:16227301 | pubmed:author | pubmed-author:TangMinM | lld:pubmed |
| pubmed-article:16227301 | pubmed:author | pubmed-author:KhatiMakobets... | lld:pubmed |
| pubmed-article:16227301 | pubmed:author | pubmed-author:DeyAntu KAK | lld:pubmed |
| pubmed-article:16227301 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16227301 | pubmed:volume | 79 | lld:pubmed |
| pubmed-article:16227301 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16227301 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16227301 | pubmed:pagination | 13806-10 | lld:pubmed |
| pubmed-article:16227301 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:16227301 | pubmed:meshHeading | pubmed-meshheading:16227301... | lld:pubmed |
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| pubmed-article:16227301 | pubmed:meshHeading | pubmed-meshheading:16227301... | lld:pubmed |
| pubmed-article:16227301 | pubmed:meshHeading | pubmed-meshheading:16227301... | lld:pubmed |
| pubmed-article:16227301 | pubmed:meshHeading | pubmed-meshheading:16227301... | lld:pubmed |
| pubmed-article:16227301 | pubmed:meshHeading | pubmed-meshheading:16227301... | lld:pubmed |
| pubmed-article:16227301 | pubmed:meshHeading | pubmed-meshheading:16227301... | lld:pubmed |
| pubmed-article:16227301 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16227301 | pubmed:articleTitle | An aptamer that neutralizes R5 strains of human immunodeficiency virus type 1 blocks gp120-CCR5 interaction. | lld:pubmed |
| pubmed-article:16227301 | pubmed:affiliation | Laboratory of Molecular Biophysics, Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom. | lld:pubmed |
| pubmed-article:16227301 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16227301 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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