| pubmed-article:14505569 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C0014662 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C0682323 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C1418407 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C1424881 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C1825938 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:14505569 | lifeskim:mentions | umls-concept:C2717976 | lld:lifeskim |
| pubmed-article:14505569 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:14505569 | pubmed:dateCreated | 2003-9-24 | lld:pubmed |
| pubmed-article:14505569 | pubmed:abstractText | HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a process requiring membrane fission. The primary late assembly (L) domain in the p6 region of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component of the class E vacuolar protein sorting (Vps) machinery. We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a subunit of the yeast class E Vps protein complex ESCRT-III. AIP1 also binds to the L domain in EIAV p9, and this binding correlates perfectly with L domain function. These observations identify AIP1 as a component of the viral budding machinery, which serves to link a distinct region in the L domain of HIV-1 p6 and EIAV p9 to ESCRT-III. | lld:pubmed |
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| pubmed-article:14505569 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14505569 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14505569 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14505569 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:14505569 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:14505569 | pubmed:author | pubmed-author:GöttlingerHei... | lld:pubmed |
| pubmed-article:14505569 | pubmed:author | pubmed-author:StrackBettina... | lld:pubmed |
| pubmed-article:14505569 | pubmed:author | pubmed-author:CalistriArian... | lld:pubmed |
| pubmed-article:14505569 | pubmed:author | pubmed-author:PopovaElenaE | lld:pubmed |
| pubmed-article:14505569 | pubmed:author | pubmed-author:CraigStewartS | lld:pubmed |
| pubmed-article:14505569 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14505569 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:14505569 | pubmed:volume | 114 | lld:pubmed |
| pubmed-article:14505569 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14505569 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14505569 | pubmed:pagination | 689-99 | lld:pubmed |
| pubmed-article:14505569 | pubmed:dateRevised | 2009-12-18 | lld:pubmed |
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| pubmed-article:14505569 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14505569 | pubmed:articleTitle | AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. | lld:pubmed |
| pubmed-article:14505569 | pubmed:affiliation | Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA. | lld:pubmed |
| pubmed-article:14505569 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14505569 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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