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Protein kinases are involved in many essential cellular processes and their deregulation can lead to a variety of diseases, including cancer. The pharmaceutical industry has invested heavily in the identification of kinase inhibitors to modulate these disease-promoting pathways, resulting in several successful drugs. However, the field is challenging as it is difficult to identify novel selective inhibitors with good pharmacokinetic/pharmacodynamic properties. In addition, resistance to kinase inhibitor treatment frequently arises. The identification of non-ATP site targeting ('allosteric') inhibitors, the identification of kinase activators and the expansion of kinase target space to include the less studied members of the family, including atypical- and pseudo-kinases, are potential avenues to overcome these challenges. In this perspective, the opportunities and challenges of following these approaches and others will be discussed.

Original publication

DOI

10.4155/fmc.13.216

Type

Journal article

Journal

Future Med Chem

Publication Date

04/2014

Volume

6

Pages

541 - 561

Keywords

Allosteric Regulation, Allosteric Site, Binding Sites, Databases, Protein, Humans, Molecular Docking Simulation, Pharmacokinetics, Protein Kinase Inhibitors, Protein Kinases, Protein Structure, Tertiary, Surface Plasmon Resonance