Source:http://linkedlifedata.com/resource/pubmed/id/15037073
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rdf:type | |
lifeskim:mentions |
umls-concept:C0002520,
umls-concept:C0086597,
umls-concept:C0205177,
umls-concept:C0205245,
umls-concept:C0292147,
umls-concept:C0525021,
umls-concept:C0597551,
umls-concept:C0887839,
umls-concept:C0917728,
umls-concept:C1167622,
umls-concept:C1704689,
umls-concept:C1709915,
umls-concept:C1880022,
umls-concept:C2003941
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pubmed:issue |
5
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pubmed:dateCreated |
2004-3-23
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/HIV Integrase,
http://linkedlifedata.com/resource/pubmed/chemical/Karyopherins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
336
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1117-28
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15037073-Active Transport, Cell Nucleus,
pubmed-meshheading:15037073-Amino Acid Sequence,
pubmed-meshheading:15037073-HIV Integrase,
pubmed-meshheading:15037073-HeLa Cells,
pubmed-meshheading:15037073-Humans,
pubmed-meshheading:15037073-Karyopherins,
pubmed-meshheading:15037073-Microscopy, Fluorescence,
pubmed-meshheading:15037073-Nuclear Localization Signals,
pubmed-meshheading:15037073-Peptide Fragments,
pubmed-meshheading:15037073-Protein Binding,
pubmed-meshheading:15037073-Protein Transport,
pubmed-meshheading:15037073-Recombinant Proteins
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pubmed:year |
2004
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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.
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pubmed:affiliation |
Department of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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