Optogenetics is a non-invasive way to study cAMP signaling in sperm cells, which is able to control sperm motility and fertilization.

β₃-AR signalling via cGMP in cardiomyocytes is regulated via phosphodiesterase 2 and 5 degradation, it is potentially cardioprotective, but dysregulated in heart failure through signal redistribution and higher phosphodiesterase activity.

UV-Vis- and IR-spectroscopy provides insights into the light-induced enzyme activity of a rhodopsin guanylyl cyclase by tracking the substrate turnover with atomic resolution in real-time and correlating it with the structural changes of the protein.

A new FRET-based cAMP biosensor with nanomolar sensitivity makes it possible to measure cAMP dynamics in miniscule subcellular compartments like cilia and flagella.

Nanodomain clustering of cAMP effectors represents a novel mechanism of cAMP compartmentation within an oscillatory signaling circuit.

A minimal subset of two to three residues in cyclic nucleotide binding (CNB) domains controls nucleoside vs. cyclic nucleotide specificity, repurposing PKA of certain pathogens for novel nucleoside signaling pathways or sensing.

Poxin enzymes are a diverse family of insect and viral 2′3′-cGAMP nucleases, which evolved from self-cleaving RNA virus accessory proteases.

The crystal structure of a mammalian protein kinase G reveals contacts between the regulatory and catalytic domains, indicates how cGMP binding alters domain conformations and thus domain:domain interactions, and informs a model for enzyme auto-inhibition and cooperative activation.

Live cell imaging shows that the cAMP-sensor Epac2, a target of major antidiabetic drugs, is central to fusion pore control during insulin granule exocytosis.

Experimental and computational approaches reveal how ligand binding is coupled to voltage sensing in a HCN channels.