Source:http://linkedlifedata.com/resource/pubmed/id/20605095
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
15
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pubmed:dateCreated |
2010-7-16
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pubmed:abstractText |
Li-Fraumeni syndrome, a hereditary disorder characterized by familial clusters of early-onset multiple tumors, is caused by mutation of the TP53 gene, which encodes the p53 tumor suppressor protein. Mutation of Arg337 to histidine in the tetramerization domain of p53 is most frequently observed in Li-Fraumeni syndrome. This mutation is reported to destabilize the tetrameric structure of p53. We designed and synthesized calix[6]arene derivatives, which have six imidazole or pyrazole groups at the upper rim. In this study, we report, for the first time, the enhancement of the in vivo transcriptional activity of the most common Li-Fraumeni p53 mutant by imidazole-calix[6]arene through stabilization of the oligomer formation.
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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 |
Aug
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pubmed:issn |
1464-3405
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2010 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4412-5
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pubmed:meshHeading |
pubmed-meshheading:20605095-Calixarenes,
pubmed-meshheading:20605095-Humans,
pubmed-meshheading:20605095-Li-Fraumeni Syndrome,
pubmed-meshheading:20605095-Molecular Conformation,
pubmed-meshheading:20605095-Mutation,
pubmed-meshheading:20605095-Protein Multimerization,
pubmed-meshheading:20605095-Protein Stability,
pubmed-meshheading:20605095-Thermodynamics,
pubmed-meshheading:20605095-Transcription, Genetic,
pubmed-meshheading:20605095-Transition Temperature,
pubmed-meshheading:20605095-Tumor Suppressor Protein p53
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pubmed:year |
2010
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pubmed:articleTitle |
Enhancement of transcriptional activity of mutant p53 tumor suppressor protein through stabilization of tetramer formation by calix[6]arene derivatives.
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pubmed:affiliation |
Laboratory of Biological Chemistry, Department of Chemistry, Faculty of Science, Hokkaido University, Kita-ku, Sapporo 060-0810, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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