pubmed-article:8523579 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0019691 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0021024 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0525038 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C1948059 | lld:lifeskim |
pubmed-article:8523579 | lifeskim:mentions | umls-concept:C1720529 | lld:lifeskim |
pubmed-article:8523579 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:8523579 | pubmed:dateCreated | 1996-1-25 | lld:pubmed |
pubmed-article:8523579 | pubmed:abstractText | The second major cysteine loop of human immunodeficiency virus type 1 envelope glycoprotein gp120 contains 5 to 11 consensus N-linked glycosylation sites, which is disproportionately higher than the number of such sites found in other regions of gp120. Amino acid substitutions introduced at three of six N-linked glycosylation sites in this region of an infectious molecular clone, HXB2, resulted in severe impairment of virus infectivity. Isolation and genetic characterization of a revertant of this mutant revealed an isoleucine-for-valine substitution at position 84 in constant region 1 and an isoleucine-for-methionine substitution at position 434 in constant region 4. Further mutational analysis indicated that either isoleucine substitution was sufficient to confer the revertant phenotype. These findings demonstrate that V1/V2 not only functionally interacts with C4, as previously reported, but also interacts with C1. The observation that compensatory changes do not involve regeneration of N-linked glycosylation sites in the second major cysteine loop suggests that replication of human immunodeficiency virus type 1 in vitro is independent of the presence of a disproportionate number of N-linked glycosylation sites within this loop. | lld:pubmed |
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pubmed-article:8523579 | pubmed:language | eng | lld:pubmed |
pubmed-article:8523579 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8523579 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8523579 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8523579 | pubmed:month | Jan | lld:pubmed |
pubmed-article:8523579 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:8523579 | pubmed:author | pubmed-author:LeeT HTH | lld:pubmed |
pubmed-article:8523579 | pubmed:author | pubmed-author:EsserGG | lld:pubmed |
pubmed-article:8523579 | pubmed:author | pubmed-author:WangW KWK | lld:pubmed |
pubmed-article:8523579 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8523579 | pubmed:volume | 70 | lld:pubmed |
pubmed-article:8523579 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8523579 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8523579 | pubmed:pagination | 607-11 | lld:pubmed |
pubmed-article:8523579 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8523579 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8523579 | pubmed:articleTitle | Single amino acid substitution in constant region 1 or 4 of gp120 causes the phenotype of a human immunodeficiency virus type 1 variant with mutations in hypervariable regions 1 and 2 to revert. | lld:pubmed |
pubmed-article:8523579 | pubmed:affiliation | Department of Cancer Biology, Harvard School of Public Health, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:8523579 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8523579 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8523579 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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