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Molecular Pharmacology of Cancer

One of the most effective strategies to develop selective kinase inhibitors is targeting allosteric regulatory sites as opposed to active sites, as the former are typically less conserved than the latter. Allostery is also critical to understand the long-range perturbations caused by cancer-related genetic mutations.


Our work focuses on allosteric kinase inhibitors and on methods to identify allosteric sites.  For example, our group developed an NMR-based approach to map allostery through the NMR chemical shift covariance analysis (CHESCA). Read more about CHESCA here or watch this video.


Through CHESCA and other biophysical methods, we are investigating the allosteric regulation of cyclic-nucleotide monophosphate (cNMP) dependent protein kinases (PK), such as PKA and PKG, which are allosterically activated by cAMP and cGMP, respectively. To learn more about our work on these topics please follow this PubMed link.


We have also expanded our investigations to other cNMP-dependent eukaryotic proteins, including the hyperpolarization and cyclic-nucleotide dependent (HCN) ion channels as well as the exchange protein directly activated by cAMP (EPAC). Read more about HCN here and EPAC here

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