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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-7-2
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pubmed:abstractText |
Dimerization initiation site (DIS) of the human immunodeficiency virus type 1 (HIV-1) genome has been identified as a primary sequence that can form a stem-loop structure with a self-complementary sequence in the loop and a bulge in the stem. A DIS RNA fragment spontaneously forms a kissing dimer and is converted into an extended-duplex dimer by supplement of nucleocapsid protein NCp7. This two-step dimerization reaction can be also executed by a heat treatment instead of the binding proteins. However, it has not identified whether mechanisms of the conformational conversion by two different treatments are identical or not. In the present study, we used a series of DIS RNA oligonucleotides and the conformations of two extended-duplex dimers produced by the two different treatments were compared by the analysis of NMR spectra in the imino proton region. It was found that the effects of the two kinds of treatments are quite similar and the conformations of the two extended-duplex dimers are identical. These findings suggest that the conversion mechanisms DIS RNA by NCp7 and heat treatments are similar.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Capsid Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, gag,
http://linkedlifedata.com/resource/pubmed/chemical/NCP7 protein, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/Oligoribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/gag Gene Products, Human...
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pubmed:status |
MEDLINE
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pubmed:author |
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
155-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12836311-Base Sequence,
pubmed-meshheading:12836311-Capsid,
pubmed-meshheading:12836311-Capsid Proteins,
pubmed-meshheading:12836311-Dimerization,
pubmed-meshheading:12836311-Gene Products, gag,
pubmed-meshheading:12836311-Genome, Viral,
pubmed-meshheading:12836311-HIV-1,
pubmed-meshheading:12836311-Hot Temperature,
pubmed-meshheading:12836311-Models, Genetic,
pubmed-meshheading:12836311-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:12836311-Nucleic Acid Conformation,
pubmed-meshheading:12836311-Oligoribonucleotides,
pubmed-meshheading:12836311-RNA, Double-Stranded,
pubmed-meshheading:12836311-RNA, Viral,
pubmed-meshheading:12836311-Viral Proteins,
pubmed-meshheading:12836311-Virus Replication,
pubmed-meshheading:12836311-gag Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2001
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pubmed:articleTitle |
Conformational change of dimerization initiation site of HIV-1 genomic RNA by NCp7 or heat treatment.
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pubmed:affiliation |
Department of Industrial Chemistry, Faculty of Engineering, Chiba Institute of Technology, 2-17-1 Tsudanuma, Narashino-shi, Chiba, Japan.
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pubmed:publicationType |
Journal Article
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