Publication | Open Access
Highly Functionalized Terpyridines as Competitive Inhibitors of AKAP–PKA Interactions
50
Citations
17
References
2013
Year
Heart FailureGood FitMolecular BiologyPharmaceutical ChemistryMolecular PharmacologySignaling PathwayHighly Functionalized TerpyridinesProtein DegradationCell SignalingInhibitory ActivityMolecular SignalingProtein FunctionMolecular PhysiologyBiochemistryBiomolecular InteractionPharmacologyProtein PhosphorylationSignal Transductionα-Helix MimeticsNatural SciencesProtein KinaseCellular BiochemistryMedicineSmall MoleculesDrug Discovery
A good fit: Interactions between A-kinase anchoring proteins (AKAPs) and protein kinase A (PKA) play key roles in a plethora of physiologically relevant processes whose dysregulation causes or is associated with diseases such as heart failure. Terpyridines have been developed as α-helix mimetics for the inhibition of such interactions and are the first biologically active, nonpeptidic compounds that block the AKAP binding site of PKA.
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