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.

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.

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.

ATP enters the endoplasmic reticulum (ER) lumen through an SLC35B1/AXER-dependentCaATiER mechanism, and ATP usage in the ER renders 'anti-Warburg' effect by increasing ATP regeneration from OxPhos while decreasing glycolysis.

Structural, computational and functional approaches reveal the role of an extended acidic chamber near the nucleotide binding site in activation of P2X3 receptor channels by divalent-bound ATP.

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

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.