Amino Acids · 2012 · 50 citations · 24 references
PharmacyMedicinal ChemistryPharmacologyCancer PharmacologyDrug DesignDrug DiscoveryEnzyme InhibitionLigand BindingPotency OptimizationBinding Mode AnalysisBinding Mode OptimizationBiological Activity FeaturesKinase Inhibitor Library DesignKinase InhibitorsProtein Kinase InhibitorsX-ray Diffraction AnalysisX-ray Spectral Analysis
In this study we identified two heterocyclic compounds (5 and 6) as potent and specific inhibitors of CK1δ (IC(50) = 0.040 and 0.042 μM, respectively). Whereas compound 5 exhibited fivefold higher affinity towards CK1δ than to CK1ε (IC(50) CK1ε = 0.199 μM), compound 6 also inhibited CK1ε (IC(50) = 0.0326 μM) in the same range as CK1δ. Selected compound 5 was screened over 442 kinases identifying 5 as a highly potent and selective inhibitor of CK1δ. X-ray analysis of 5 bound to CK1δ demonstrated its binding mode. In addition, characterization of 5 and 6 in a cell biological approach revealed the ability of both compounds to inhibit proliferation of tumor cell lines in a dose and cell line specific manner. In summary, our optimizations lead to the development of new highly selective CK1δ and ε specific inhibitors with biological activity.
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Isolation of a human prostate carcinoma cell line (DU 145)
Kenneth R. Stone, Don D. Mickey, Heidi Wunderli et al. · International Journal of Cancer · 1978 · 1.2K citations
Classification of human colorectal adenocarcinoma cell lines.
Albert Leibovitz, James C. Stinson, William B. McCombs et al. · PubMed · 1976 · 958 citations
Characterization of a newly derived human sarcoma cell line (HT-1080)
Suraiya Rasheed, Walter A. Nelson‐Rees, Eva M. Toth et al. · Cancer · 1974 · 689 citations