Linked Life Data

8548757

Source:http://linkedlifedata.com/resource/pubmed/id/8548757

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-2-16
pubmed:abstractText
The tetramerization domain of p53 is required for efficient tumor suppressor activity. This domain, however, also allows wild-type p53 to heterooligomerize with dominant negative tumor-derived p53 mutants. We explored the feasibility of substituting the native tetramerization domain of wild-type p53 with an engineered leucine zipper that assembles as a four-stranded coiled coil. The engineered zipper drove p53 tetramerization in vitro and p53 function in vivo. Furthermore, it alleviated transdominant inhibition by tumor-derived p53 mutants, implying that dominant negative mutants act by hetero-oligomerizing with wild-type p53. The ability of the engineered zipper to drive tetramerization was critical for p53 function, since p53 dimers, formed by substituting the p53 tetramerization domain with a native leucine zipper, were weak tumor suppressors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
158-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
An engineered four-stranded coiled coil substitutes for the tetramerization domain of wild-type p53 and alleviates transdominant inhibition by tumor-derived p53 mutants.
pubmed:affiliation
Department of Molecular Oncology, Wistar Institute, Philadelphia, PA 19104-4268, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.