Protein kinases and phosphatases are involved in all facets of cellular processes ranging from metabolism to neuronal survival. Thus, it is not surprising that aberrant regulation of their activity, subcellular localization, and expression contributes to pathogenesis and progression of many human diseases such as cancer, neurodegeneration, and metabolic diseases. Knowledge of the regulation and structures of a number of protein kinases has led to the development of small molecule inhibitors as therapeutics for cancer treatment. The most notable examples are the small molecule inhibitors of protein kinases that are used as therapeutics for the treatment of chronic myelogenous leukaemia including Imatinib, Nilotinib, and Dasatinib. There is no doubt that further investigations that aim at elucidating the regulation and substrate recognition of protein kinases and phosphatases will benefit the development of therapeutic strategies for the treatment and prevention of many diseases.

We invite researchers to contribute manuscripts documenting the findings of original research and review articles in enzymology of protein kinases and phosphatases. We are particularly interested in articles describing the catalytic and kinetic mechanisms, regulation, substrate recognition and inhibitor designs of protein kinases and phosphatases. Potential topics include, but are not limited to:

• Identification of protein substrates of eukaryotic and prokaryotic protein kinases and phosphatases
• Elucidation of the structural basis of substrate specificity of protein kinases and phosphatases
• Studies of the catalytic and kinetic mechanisms of protein kinases and phosphatases
• Elucidation of the regulatory and catalytic mechanisms of protein kinases and phosphatases using biophysical approaches such as analytical ultracentrifugation and nuclear magnetic resonance spectroscopy
• Structural basis of inhibition of protein kinases and phosphatases by small-molecule inhibitors
• Recent development in the design of chemosensor peptide substrates and biosensors to monitor the activity and subcellular localization of protein kinases and phosphatases in vitro and in cells
• Recent development in the design of assays for high throughput screening of small-molecule inhibitors of protein kinases and phosphatases

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