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.

In C. elegans and mouse neurons, the balance between poly(ADP-ribose) glycohydrolases and poly(ADP-ribose) polymerases regulates axon regeneration downstream of DLK-1/MAPKKK signaling.

NDR kinase Orb6 prevents RNP granule assembly and translational repression by promoting Sts5 association with 14-3-3 protein Rad24 to spatially control polarized cell growth.

ARH3 is an enzyme that hydrolyses serine ADP-ribosylation, a recently uncovered post-translational protein modification.

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.

Amino-acid induced Sec body formation is mediated by PARP16 dependent MARylation of Sec16, a component of the endoplasmic reticulum exit site.

Cryo-electron microscopy reconstructions of two microtubule-bound transport kinesins at 7 Å resolution reveal how microtubule track binding stimulates ADP release, primes the active site for ATP binding and enables force generation.

By moving between DNA segments like a child swinging on monkey bars, poly(ADP-ribose) polymerase 1 explores possible DNA damage sites more effectively.

Combining powerful simulation methods uncovers the structural and dynamical changes driving G protein activation in atomic detail, revealing the allosteric network that triggers GDP release and reconciling diverse experimental data.