ic-87114 has been researched along with Neoplasms* in 2 studies
1 review(s) available for ic-87114 and Neoplasms
| Article | Year |
|---|---|
Small molecule inhibitors of the PI3-kinase family.
The PI3-K family is one of the most intensely pursued classes of drug targets. This chapter reviews some of the chemical and structural features that determine the selectivity of PI3-K inhibitors, by focusing on a few key compounds that have been instrumental in guiding our understanding of how to design drugs against this family. Topics: Adenine; Androstadienes; Animals; Ataxia Telangiectasia Mutated Proteins; Cell Cycle Proteins; Chromones; DNA-Activated Protein Kinase; DNA-Binding Proteins; Humans; Morpholines; Neoplasms; Nuclear Proteins; Phosphoinositide-3 Kinase Inhibitors; Protein Kinase Inhibitors; Protein Serine-Threonine Kinases; Quinazolines; Tumor Suppressor Proteins; Wortmannin | 2010 |
1 other study(ies) available for ic-87114 and Neoplasms
| Article | Year |
|---|---|
Cancer-derived mutations in the regulatory subunit p85alpha of phosphoinositide 3-kinase function through the catalytic subunit p110alpha.
Cancer-specific mutations in the iSH2 (inter-SH2) and nSH2 (N-terminal SH2) domains of p85alpha, the regulatory subunit of phosphatidylinositide 3-kinase (PI3K), show gain of function. They induce oncogenic cellular transformation, stimulate cellular proliferation, and enhance PI3K signaling. Quantitative determinations of oncogenic activity reveal large differences between individual mutants of p85alpha. The mutant proteins are still able to bind to the catalytic subunits p110alpha and p110beta. Studies with isoform-specific inhibitors of p110 suggest that expression of p85 mutants in fibroblasts leads exclusively to an activation of p110alpha, and p110alpha is the sole mediator of p85 mutant-induced oncogenic transformation. The characteristics of the p85 mutants are in agreement with the hypothesis that the mutations weaken an inhibitory interaction between p85alpha and p110alpha while preserving the stabilizing interaction between p85alpha iSH2 and the adapter-binding domain of p110alpha. Topics: Adenine; Amino Acid Sequence; Animals; Base Sequence; Blotting, Western; Catalytic Domain; Cell Line; Cell Proliferation; Cell Transformation, Neoplastic; Cells, Cultured; Chick Embryo; Class I Phosphatidylinositol 3-Kinases; Dioxoles; Fibroblasts; Humans; Immunoprecipitation; Morpholines; Mutation; Neoplasms; Phosphatidylinositol 3-Kinases; Phosphoinositide-3 Kinase Inhibitors; Protein Binding; Protein Subunits; Pyrimidinones; Quinazolines; Thiazolidinediones; Transfection | 2010 |