Source:http://linkedlifedata.com/resource/pubmed/id/16879966
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
2006-8-25
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pubmed:abstractText |
Peptides deriving from the HIV-1 HXB2 Pol gene sequence were evaluated for inhibitory activity against wild-type (WT) and mutant HIV-1 integrase (IN). The most potent peptide corresponding to a region on the reverse transcriptase (RT) subunit of the Pol polyprotein showed IC(50) value of 5 and 2 microM for 3'-processing and strand transfer, respectively. These peptides, and their analogs, may potentially be used in the elucidation of structural and functional epitopes of IN involved in protein-protein and protein-small molecule interactions.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5199-202
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pubmed:meshHeading |
pubmed-meshheading:16879966-Amino Acid Sequence,
pubmed-meshheading:16879966-Gene Products, pol,
pubmed-meshheading:16879966-HIV Integrase,
pubmed-meshheading:16879966-HIV Integrase Inhibitors,
pubmed-meshheading:16879966-Humans,
pubmed-meshheading:16879966-Inhibitory Concentration 50,
pubmed-meshheading:16879966-Mutation,
pubmed-meshheading:16879966-Peptide Fragments,
pubmed-meshheading:16879966-Structure-Activity Relationship
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pubmed:year |
2006
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pubmed:articleTitle |
Inhibition of HIV-1 integrase activity by synthetic peptides derived from the HIV-1 HXB2 Pol region of the viral genome.
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pubmed:affiliation |
Department of Pharmaceutical Sciences, School of Pharmacy, University of Southern California, 1985 Zonal Avenue, Los Angeles, 90089, USA.
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pubmed:publicationType |
Journal Article
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