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.

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

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.

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.