pubmed-article:10729129 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C1706515 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C1704640 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C0314603 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C0913822 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C0913823 | lld:lifeskim |
pubmed-article:10729129 | lifeskim:mentions | umls-concept:C0331858 | lld:lifeskim |
pubmed-article:10729129 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:10729129 | pubmed:dateCreated | 2000-4-26 | lld:pubmed |
pubmed-article:10729129 | pubmed:abstractText | The incorporation of envelope (Env) glycoproteins into virions is an essential step in the retroviral replication cycle. Lentiviruses, including human immunodeficiency virus type 1 (HIV-1), encode Env glycoproteins with unusually long cytoplasmic tails, the functions of which have not been fully elucidated. In this study, we examine the effects on virus replication of a number of mutations in a helical motif (alpha-helix 2) located near the center of the HIV-1 gp41 cytoplasmic tail. We find that, in T-cell lines, small deletions in this domain disrupt the incorporation of Env glycoproteins into virions and markedly impair virus infectivity. Through the analysis of viral revertants, we demonstrate that a single amino acid change (34VI) in the matrix domain of Gag reverses the Env incorporation and infectivity defect imposed by a small deletion near the C terminus of alpha-helix 2. These results provide genetic evidence, in the context of infected T cells, for an interaction between HIV-1 matrix and the gp41 cytoplasmic tail and identify domains of both proteins involved in this putative interaction. | lld:pubmed |
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pubmed-article:10729129 | pubmed:language | eng | lld:pubmed |
pubmed-article:10729129 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10729129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10729129 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10729129 | pubmed:month | Apr | lld:pubmed |
pubmed-article:10729129 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:10729129 | pubmed:author | pubmed-author:MurakamiTT | lld:pubmed |
pubmed-article:10729129 | pubmed:author | pubmed-author:FreedE OEO | lld:pubmed |
pubmed-article:10729129 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10729129 | pubmed:volume | 74 | lld:pubmed |
pubmed-article:10729129 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10729129 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10729129 | pubmed:pagination | 3548-54 | lld:pubmed |
pubmed-article:10729129 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:10729129 | pubmed:year | 2000 | lld:pubmed |
pubmed-article:10729129 | pubmed:articleTitle | Genetic evidence for an interaction between human immunodeficiency virus type 1 matrix and alpha-helix 2 of the gp41 cytoplasmic tail. | lld:pubmed |