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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1990-8-16
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pubmed:abstractText |
We have designed a hammerhead-type RNA system which consists of three RNA fragments for normal and modified complexes which contain a non-cleavable substrate with 2'-O-methylcytidine and a guanosine-to-inosine replaced enzyme. Examination of the RNA-cleaving activity and conformational properties of the complexes suggests that the 2-amino group of a conserved guanosine residue in the loop region plays an important role for maintaining both the activity and loop conformation.
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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 |
Jul
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
150-2
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:1694789-Base Sequence,
pubmed-meshheading:1694789-Chemical Phenomena,
pubmed-meshheading:1694789-Chemistry,
pubmed-meshheading:1694789-Guanosine,
pubmed-meshheading:1694789-Magnetic Resonance Spectroscopy,
pubmed-meshheading:1694789-Molecular Sequence Data,
pubmed-meshheading:1694789-Nucleic Acid Conformation,
pubmed-meshheading:1694789-RNA,
pubmed-meshheading:1694789-RNA, Catalytic,
pubmed-meshheading:1694789-RNA, Ribosomal
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pubmed:year |
1990
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pubmed:articleTitle |
The role of a conserved guanosine residue in the hammerhead-type RNA enzyme.
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pubmed:affiliation |
Faculty of Pharmaceutical Sciences, Osaka University, Japan.
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pubmed:publicationType |
Journal Article
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