Source:http://linkedlifedata.com/resource/pubmed/id/18029752
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
51
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pubmed:dateCreated |
2007-11-21
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pubmed:abstractText |
The minus-IRES ((-)IRES), corresponding to the 3'-terminal end of the negative strand of hepatitis C virus (HCV) RNA, is well conserved among HCV subtypes. The higher order structure of (-)IRES is essential for HCV replication, because the viral RNA dependent RNA polymerase, NS5B, recognizes it as the initiation site for plus-strand synthesis of the HCV genome. To inhibit the "de novo" synthesis of plus-strand RNA molecules, we performed an in vitro selection procedure that is specific for the (-)IRES domain I. After confirming the binding convergence in the ninth RNA pool, 42 RNA clones were sequenced and analyzed. Of these, 25 clones (Family-I) had the consensus sequence, 5'-UGGAUC-3', which is complementary to the apical loop of SL-E1, an important region for NS5B recognition. Another 13 clones (Family-II) had the consensus sequence, 5'-GAGUAC-3', which is complementary to the apical loop of SL-D1. Biochemical analyses are in progress to evaluate whether these RNA aptamers have the ability to inhibit HCV replication.
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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:issn |
1746-8272
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
393-4
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pubmed:meshHeading |
pubmed-meshheading:18029752-5' Untranslated Regions,
pubmed-meshheading:18029752-Aptamers, Nucleotide,
pubmed-meshheading:18029752-Base Sequence,
pubmed-meshheading:18029752-Consensus Sequence,
pubmed-meshheading:18029752-Hepacivirus,
pubmed-meshheading:18029752-Molecular Sequence Data,
pubmed-meshheading:18029752-Nucleic Acid Conformation,
pubmed-meshheading:18029752-RNA, Viral
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pubmed:year |
2007
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pubmed:articleTitle |
Isolation of RNA aptamers specific for the HCV minus-IRES domain I.
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pubmed:affiliation |
Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan.
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pubmed:publicationType |
Journal Article
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