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.

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.

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

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.

HIV-1 Vpr antagonises innate immune sensing of viral and non-viral stimuli by preventing activated IRF3 and NF-κB nuclear transport.

A-type potassium conductances influence the distinctive firing behaviour of irregular-spiking interneurons.

The common post-translational modification trans-4-hydroxy-L-proline is reversed by gut microbes with the help of hydroxyproline dehydratase (HypD), an enzyme that performs a radical chemical mechanism.

National Institutes of Health (NIH) grants have evolved over time, with a greater proportion of funds going to solicited projects, but inflation-adjusted costs have remained relatively stable following a brief increase during the NIH-doubling (1998-2003).

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.