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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Knapp, Stefan Roux, Benoit Vieth, Michal Meiler, Jens Baumann, Alexander Berdini, Valerio Engh, Richard A. Varin, Thibault Martin, Eric Moebitz, Henrik |
| Description | Author Affiliation: Martin E ( Novartis Institutes for BioMedical Research, 5300 Chiron Way, Emeryville, CA 94608-2916, USA.); Knapp S ( Target Discovery Institute and Structural Genomics Consortium, University of Oxford, NDM Research Building, Roosevelt Drive, Oxford OX3 7FZ, UK.); Engh RA ( The Norwegian Structural Biology Centre, Department of Chemistry, University of Tromsø, Tromsø, Norway.); Moebitz H ( Novartis Institutes for BioMedical Research, Novartis Pharma AG, Postfach, CH-4002 Basel, Switzerland.); Varin T ( Eli Lilly and Company, Lilly Research Laboratories, Lilly Corporate Center, DC 1931, Indianapolis, IN 46285, USA.); Roux B ( University of Chicago, Dept. of Biochemistry & Molecular Biology, 929 E. 57th St., Chicago 60637, IL, USA.); Meiler J ( Department of Chemistry, Vanderbilt University, Nashville, TN 37232, USA.); Berdini V ( Astex Pharmaceuticals, 436 Cambridge Science Park, Milton Road, Cambridge CB4 0QA, United Kingdom.); Baumann A ( DiscoveRx Corporation, 42501 Albrae Street, Suite 100, Fremont, CA 94538, USA.); Vieth M ( Eli Lilly and Company, Lilly Research Laboratories, Lilly Corporate Center, DC 1931, Indianapolis, IN 46285, USA. Electronic address: vieth_michal@lilly.com.) |
| Abstract | Recent advances in understanding the activity and selectivity of kinase inhibitors and their relationships to protein structure are presented. Conformational selection in kinases is studied from empirical, data-driven and simulation approaches. Ligand binding and its affinity are, in many cases, determined by the predetermined active and inactive conformation of kinases. Binding affinity and selectivity predictions highlight the current state of the art and advances in computational chemistry as it applies to kinase inhibitor discovery. Kinome wide inhibitor profiling and cell panel profiling lead to a better understanding of selectivity and allow for target validation and patient tailoring hypotheses. This article is part of a Special Issue entitled: Inhibitors of Protein Kinases. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Part | Pt B |
| Issue Number | 10 |
| Volume Number | 1854 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-10-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Protein Kinases Chemistry Genetics Proto-Oncogene Proteins C-abl Src-Family Kinases Amino Acid Sequence Binding Sites Computational Biology Protein Binding Protein Conformation Protein Kinase Inhibitors Metabolism Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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