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

Set1 has roles in chromatin organization and transcriptome control that are largely independent of histone H3 lysine 4 methylation.

The loss of p53 in bone cells activates critical signaling pathways; these are also essential in bone cancer.

X-ray imaging reveals well-preserved internal characters in mineralized arthropods from the Paleogene, urging the reexamination of previously neglected fossil collections.

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

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.

The tumor suppressor p53 prevents tumor cell growth by employing a small RNA called miR-139-5p to inhibit the activity of an tumorigenic protein, cAMP-specific phosphodiesterase 4D.

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

Via the capacitance clamp, electrophysiologists can for the first time flexibly set an artificial membrane capacitance for neurons and other excitable cells and thereby adjust their membrane time constant independent of any conductance changes.

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.