rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2007-5-2
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pubmed:abstractText |
Recently, artificial ribonucleases (aRNases)--conjugates of oligodeoxyribonucleotides and peptide (LR)(4)-G-amide--were designed and assessed in terms of the activity and specificity of RNA cleavage. The conjugates were shown to cleave RNA at Pyr-A and G-X sequences. Variations of oligonucleotide length and sequence, peptide and linker structure led to the development of conjugates exhibiting G-X cleavage specificity only. The most efficient catalyst is built of nonadeoxyribonucleotide of unique sequence and peptide (LR)(4)-G-NH(2) connected by the linker of three abasic deoxyribonucleotides (conjugate pep-9). Investigation of the cleavage specificity of conjugate pep-9 showed that the compound is the first single-stranded guanine-specific aRNase, which mimics RNase T1. Rate enhancement of RNA cleavage at G-X linkages catalysed by pep-9 is 10(8) compared to non-catalysed reaction, pep-9 cleaves these linkages only 10(5)-fold less efficiently than RNase T1 (k(cat_RNase T1)/k(cat)_(pep)(-9) = 10(5)).
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-11433033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-12462971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-12654263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-1373237,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-1379732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-15047859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-15250719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-15625232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-16615805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-1985896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-220499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-2866795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-30474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-3331337,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-409999,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-4508150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-5416897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-7707372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-8386773,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-8604321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-9528657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17389642-9931000
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2356-67
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
|
pubmed:year |
2007
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pubmed:articleTitle |
RNase T1 mimicking artificial ribonuclease.
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pubmed:affiliation |
Institute of Chemical Biology and Fundamental Medicine SB RAS, Novosibirsk, Russia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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