pubmed-article:15037073 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C1704689 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0292147 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0525021 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0887839 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0597551 | lld:lifeskim |
pubmed-article:15037073 | lifeskim:mentions | umls-concept:C0917728 | lld:lifeskim |
pubmed-article:15037073 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:15037073 | pubmed:dateCreated | 2004-3-23 | lld:pubmed |
pubmed-article:15037073 | pubmed:abstractText | In spite of recent efforts to elucidate the nuclear import pathway of the human immunodeficiency virus type 1 (HIV-1) integrase protein (IN), its exact route as well as the domains that mediate its import are still unknown. Here, we show that a synthetic peptide bearing the amino acid residues 161-173 of the HIV-1 IN is able to mediate active import of covalently attached bovine serum albumin molecules into nuclei of permeabilized cells and therefore was designated as nuclear localization signal-IN (NLS(IN)). A peptide bearing residues 161-173 in the reversed order showed low karyophilic properties. Active nuclear import was demonstrated by using fluorescence microscopy and a quantitative ELISA-based assay system. Nuclear import was blocked by addition of the NLS(IN) peptide, as well as by a peptide bearing the NLS of the simian virus 40 T-antigen (NLS-SV40). The NLS(IN) peptide partially inhibited nuclear import mediated by the full-length recombinant HIV-1 IN protein, indicating that the sequence of the NLS(IN) is involved in mediating nuclear import of the IN protein. The NLS(IN) as well as the full-length IN protein interacted specifically with importin alpha, binding of which was blocked by the NLS(IN) peptide itself as well as by the NLS-SV40. | lld:pubmed |
pubmed-article:15037073 | pubmed:language | eng | lld:pubmed |
pubmed-article:15037073 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15037073 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:15037073 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15037073 | pubmed:month | Mar | lld:pubmed |
pubmed-article:15037073 | pubmed:issn | 0022-2836 | lld:pubmed |
pubmed-article:15037073 | pubmed:author | pubmed-author:LoyterAbraham... | lld:pubmed |
pubmed-article:15037073 | pubmed:author | pubmed-author:GraessmannAdo... | lld:pubmed |
pubmed-article:15037073 | pubmed:author | pubmed-author:Armon-OmerAye... | lld:pubmed |
pubmed-article:15037073 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15037073 | pubmed:day | 5 | lld:pubmed |
pubmed-article:15037073 | pubmed:volume | 336 | lld:pubmed |
pubmed-article:15037073 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15037073 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15037073 | pubmed:pagination | 1117-28 | lld:pubmed |
pubmed-article:15037073 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:15037073 | pubmed:meshHeading | pubmed-meshheading:15037073... | lld:pubmed |
pubmed-article:15037073 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15037073 | pubmed:articleTitle | A synthetic peptide bearing the HIV-1 integrase 161-173 amino acid residues mediates active nuclear import and binding to importin alpha: characterization of a functional nuclear localization signal. | lld:pubmed |
pubmed-article:15037073 | pubmed:affiliation | Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel. | lld:pubmed |
pubmed-article:15037073 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15037073 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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