pd-166326 and pyrimidine

pd-166326 has been researched along with pyrimidine* in 2 studies

Other Studies

2 other study(ies) available for pd-166326 and pyrimidine

Article	Year
Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell, 2003, Mar-21, Volume: 112, Issue:6 c-Abl is normally regulated by an autoinhibitory mechanism, the disruption of which leads to chronic myelogenous leukemia. The details of this mechanism have been elusive because c-Abl lacks a phosphotyrosine residue that triggers the assembly of the autoinhibited form of the closely related Src kinases by internally engaging the SH2 domain. Crystal structures of c-Abl show that the N-terminal myristoyl modification of c-Abl 1b binds to the kinase domain and induces conformational changes that allow the SH2 and SH3 domains to dock onto it. Autoinhibited c-Abl forms an assembly that is strikingly similar to that of inactive Src kinases but with specific differences that explain the differential ability of the drug STI-571/Gleevec/imatinib (STI-571) to inhibit the catalytic activity of Abl, but not that of c-Src. Topics: Benzamides; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Imatinib Mesylate; Models, Molecular; Phosphorylation; Piperazines; Protein Binding; Protein Conformation; Proto-Oncogene Proteins c-abl; Pyridines; Pyrimidines; Recombinant Fusion Proteins; src Homology Domains; Structure-Activity Relationship	2003
Is another bcr-abl inhibitor needed for chronic myelogenous leukemia? Clinical cancer research : an official journal of the American Association for Cancer Research, 2003, Volume: 9, Issue:4 Topics: Benzamides; Fusion Proteins, bcr-abl; Humans; Imatinib Mesylate; Leukemia, Myelogenous, Chronic, BCR-ABL Positive; Piperazines; Pyridines; Pyrimidines	2003

Article

Year

Structural basis for the autoinhibition of c-Abl tyrosine kinase.

Cell, 2003, Mar-21, Volume: 112, Issue:6

c-Abl is normally regulated by an autoinhibitory mechanism, the disruption of which leads to chronic myelogenous leukemia. The details of this mechanism have been elusive because c-Abl lacks a phosphotyrosine residue that triggers the assembly of the autoinhibited form of the closely related Src kinases by internally engaging the SH2 domain. Crystal structures of c-Abl show that the N-terminal myristoyl modification of c-Abl 1b binds to the kinase domain and induces conformational changes that allow the SH2 and SH3 domains to dock onto it. Autoinhibited c-Abl forms an assembly that is strikingly similar to that of inactive Src kinases but with specific differences that explain the differential ability of the drug STI-571/Gleevec/imatinib (STI-571) to inhibit the catalytic activity of Abl, but not that of c-Src.

Topics: Benzamides; Catalysis; Crystallography, X-Ray; Enzyme Inhibitors; Imatinib Mesylate; Models, Molecular; Phosphorylation; Piperazines; Protein Binding; Protein Conformation; Proto-Oncogene Proteins c-abl; Pyridines; Pyrimidines; Recombinant Fusion Proteins; src Homology Domains; Structure-Activity Relationship

2003

Is another bcr-abl inhibitor needed for chronic myelogenous leukemia?

Clinical cancer research : an official journal of the American Association for Cancer Research, 2003, Volume: 9, Issue:4

Topics: Benzamides; Fusion Proteins, bcr-abl; Humans; Imatinib Mesylate; Leukemia, Myelogenous, Chronic, BCR-ABL Positive; Piperazines; Pyridines; Pyrimidines

2003