Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1997-2-3
|
pubmed:abstractText |
Effects of p110, the catalytic subunit of PI-3 kinase, on induction of TPA response element-driven promoter by EGF was examined. The induction was enhanced by co-expression of the wild type of p110. The truncated p110 mutants containing the binding site for p85 but missing the catalytic activity repressed the induction. A mutant with no binding activity to p85 did not show this effect. These results suggest that PI-3 kinase is involved in signal transduction of EGF and that the truncated p110s capable of binding to p85 serves as a dominant negative reagent for PI-3 kinase.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1039-9712
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
39
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
721-8
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:8843340-Animals,
pubmed-meshheading:8843340-Enzyme Activation,
pubmed-meshheading:8843340-Epidermal Growth Factor,
pubmed-meshheading:8843340-Mutagenesis, Site-Directed,
pubmed-meshheading:8843340-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:8843340-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:8843340-Protein Conformation,
pubmed-meshheading:8843340-Rats
|
pubmed:year |
1996
|
pubmed:articleTitle |
Dominant negative effect of the truncated p110 subunit of phosphatidylinositol-3 kinase.
|
pubmed:affiliation |
Department of Applied Biological Chemistry, Faculty of Agricultural and Life Science, University of Tokyo, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|