Linked Life Data

8393158

Source:http://linkedlifedata.com/resource/pubmed/id/8393158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1993-8-25
pubmed:abstractText
The wild-type p53 gene is able to inhibit the ability of a number of oncogenes to induce transformation, but this inhibition is frequently lost when the p53 gene undergoes mutation. In this study, we generated mutated mouse p53 proteins containing conservative amino acid substitutions at residues 127 to 138 and at 140. The mutant proteins fell into three distinct classes. Class I proteins reacted well with PAb246 (246+), poorly with PAb240 (240-), bound to SV40 T antigen (T+), and inhibited the transformation of rat embryo fibroblasts by adenovirus E1a and activated ras. Class II proteins were 246-, 240+, T-, and failed to inhibit transformation. Class III proteins were 246+, 240-, but T-, and varied in their ability to inhibit transformation. The existence and properties of the Class III proteins suggest that the residues mutated in this class are important for binding to T antigen. They also lead us to conclude that the maintenance of an apparent wild-type structure is not sufficient for p53 to inhibit transformation and that the loss of T antigen binding does not necessarily result in loss of transformation inhibition. We propose the existence of a third activity important for the ability of p53 to inhibit transformation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:geneSymbol
p53, ras
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2043-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
p53 mutants with changes in conserved region II: three classes with differing antibody reactivity, SV40 T antigen binding and ability to inhibit transformation of rat cells.
pubmed:affiliation
School of Life and Health Sciences, University of Delaware, Newark 19716.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't