Interactions between serines and molecules of ADP-ribose play an important role in signaling that the DNA in a cell has been damaged and needs to be repaired.

Serine residues in proteins are the primary targets for PARP-dependent ADP-ribosylation signalling upon DNA damage.

MgADP binding to the high-affinity 'consensus' ATPase active site of SUR1 and remodeling of the L0-loop (lasso region) overrides tonic ATP inhibition of KATP channels.

A phylum-specific ATP synthase subunit is needed for proper mitochondrial function and stability of the complex in Toxoplasma gondii.

The accumulation of its product, cytidine triphosphate, encourages the enzyme CTP synthetase (CtpS) to form large-scale polymers and inhibits the enzyme's activity.

Construction of a first atomic model for an intact bacterial ATP synthase allows for a structural understanding of the roles of individual amino acids in the mechanism of ATP synthesis.

ATM plays an important role in maintaining the fidelity of DNA repair through the regulation of ARP8 phosphorylation to prevent the chromosome abnormality.

Mitochondrial flashes counteract the imbalance of ATP supply-and-demand and constitute an auto-regulator of ATP homeostasis in the heart.

A flip of the dimer asymmetry following the first ATP hydrolysis provides a mechanistic model for client remodeling by the mitochondrial Hsp90, TRAP1.

Single-particle cryo-electron microscopy reveals the first subnanometer structure of ATP-sensitive potassium (K_ATP) channels, which provides insight into the structural mechanisms of channel assembly and gating.