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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1994-8-5
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pubmed:abstractText |
Protein tyrosine kinases play key roles in cellular physiology. Specific inhibitors of these enzymes are important laboratory tools and may prove to be novel therapeutic agents. In this report we describe a new class of tyrosine kinase inhibitor, synthetic oligodeoxynucleotides (ODNs). An ODN is described which specifically inhibits p210bcr-abl tyrosine kinase autophosphorylation in vitro with a Ki of 0.5 microM. Inhibition is non-competitive with respect to ATP. The effects upon inhibitory activity of ODN structure modifications are described. The inhibition described is not mediated by classical antisense mechanisms and represents an example of the recently recognized aptameric properties of ODNs.
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pubmed:commentsCorrections |
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2150-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8029025-3T3 Cells,
pubmed-meshheading:8029025-Animals,
pubmed-meshheading:8029025-Base Sequence,
pubmed-meshheading:8029025-Cell Line,
pubmed-meshheading:8029025-DNA,
pubmed-meshheading:8029025-Fusion Proteins, bcr-abl,
pubmed-meshheading:8029025-Mice,
pubmed-meshheading:8029025-Molecular Sequence Data,
pubmed-meshheading:8029025-Oligodeoxyribonucleotides,
pubmed-meshheading:8029025-Phosphorylation
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pubmed:year |
1994
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pubmed:articleTitle |
Aptameric inhibition of p210bcr-abl tyrosine kinase autophosphorylation by oligodeoxynucleotides of defined sequence and backbone structure.
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pubmed:affiliation |
Clinical Pharmacology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.
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pubmed:publicationType |
Journal Article
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