Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Ensemble cryo-EM visualizes how structural rearrangements poise the newly made protein and release factor RF2 to dissociate in preparation for ribosome recycling.

Cryo-EM shows a 5’ DNA site on the RFC clamp loader, in addition to the 3’ site, and biochemical study shows the 5’ site facilitates PCNA loading onto gaps, consistent with genetics indicating the 5’ DNA site facilitates gap repair.

Cryo-EM structures reveal the structural dynamics of ArfA*RF2-mediated rescue of stalled ribosomes.

Translation termination is a stochastic process that utilizes loosely coupled motions of its players to complete protein synthesis and release the newly synthesized nascent chain toward its cellular destination.

Structural, biochemical, and cellular data reveal the mechanism by which the clamp loader attaches sliding clamps at gapped and nicked DNA to support DNA damage repair.

A zebrafish model of neuroblastoma reveals that the tumor suppressor NF1 uses different mechanisms to suppress malignant transformation and to down-modulate normal neural crest cell growth during embryogenesis.

Genetic analyses illustrate the novel requirement of Ftz-f1 and Sim in adult Drosophila ovaries for regulating follicle cell differentiation and ovulation that is likely conserved in mammals.

Neurofibromatosis type 1 gene (NF1) signaling is causally linked to the acquisition of a mesenchymal gene expression program in gliomas through the regulation of the AP-1 transcription factor FOSL1.

Post-translational processing of the SKN-1A/Nrf1 transcription factor regulates proteasome expression.