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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




Journal article


Future Med Chem

Publication Date





541 - 561


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