Pharmaceutical manipulation of cAMP levels exerts beneficial effects through the regulation
of the exchange protein activated by cAMP (EPAC) and protein kinase A (PKA) signalling …

Cancer remains a global health problem and approximately 1.7 million new cancer cases
are diagnosed every year worldwide. Although diverse molecules are currently being …

Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channels control neuronal
and cardiac electrical rhythmicity. There are four homologous isoforms (HCN1–4) sharing a …

Allostery is an essential regulatory mechanism of biological function. Allosteric sites are also
pharmacologically relevant as they are often targeted with higher selectivity than orthosteric …

Classical uncompetitive inhibitors are potent pharmacological modulators of enzyme
function. Since they selectively target enzyme–substrate complexes (E: S), their inhibitory …

Protein kinase G (PKG) is a major receptor of cGMP and controls signaling pathways often
distinct from those regulated by cAMP. Hence, the selective activation of PKG by cGMP …

Exchange proteins directly activated by cAMP (EPAC) as guanine nucleotide exchange
factors mediate the effects of the pivotal second messenger cAMP, thereby regulating a wide …

Protein Kinase A (PKA) is the major receptor for the cyclic adenosine monophosphate
(cAMP) secondary messenger in eukaryotes. cAMP binds to two tandem cAMP-binding …

Intrinsic disorder provides a means of maximizing allosteric coupling in proteins. However,
the mechanisms by which the disorder functions in allostery remain to be elucidated. Small …

Allostery is a ubiquitous mechanism to control biological function and arises from the
coupling of inhibitory and binding equilibria. The extent of coupling reflects the inactive vs …