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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
|
pubmed:dateCreated |
1998-6-18
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pubmed:abstractText |
We have previously shown that transactivation by tumor suppressor protein p53 can be inhibited in vivo at elevated protein concentrations. In this study we characterize the structural requirements of this function. We show that oligomerization domain of p53 is involved in loss of transactivation at high protein concentrations: mutants not able to oligomerize are neither able to suppress transactivation, although these transactivating properties can be untouched.
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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
|
pubmed:month |
May
|
pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
7
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pubmed:volume |
16
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2413-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9620560-DNA Mutational Analysis,
pubmed-meshheading:9620560-Protein Binding,
pubmed-meshheading:9620560-Protein Conformation,
pubmed-meshheading:9620560-Recombinant Proteins,
pubmed-meshheading:9620560-Transcriptional Activation,
pubmed-meshheading:9620560-Tumor Suppressor Protein p53
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pubmed:year |
1998
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pubmed:articleTitle |
Oligomerization of p53 is necessary to inhibit its transcriptional transactivation property at high protein concentration.
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pubmed:affiliation |
Institute of Molecular and Cell Biology, Estonian Biocentre, Tartu University.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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