The minimal twister sister (TS)-like self-cleaving ribozymes, revealed by deep mutational scanning, represent some of the very few human/primate ribozymes.

A high-throughput analysis of several self-cleaving ribozymes reveals the effect of every possible mutation, and every possible pair of mutations, and how patterns in the relative activity data can be mapped to canonical and non-canonical structural elements.

Adopting RNA trinucleotides as substrates, ribozymes can catalyse the copying of structured RNA sequences, allowing self-synthesis by part of a newly evolved symbiotic ribozyme pair.

High-resolution maps and models of the bacterial ribosome provide new chemical insights into protein synthesis, and should enable the development of robust tools for cryo-EM structure modeling and refinement.

A combination of direct-electron detectors and statistical movie processing allows ribosome cryo-EM structures to be determined to resolutions that were previously only attainable by X-ray crystallography.

The size of the mRNA fragment protected by a ribosome depends on the ribosome's conformation, which enables studies of the distinct steps of decoding and translocation at single-codon resolution.

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.

Nascent regulatory peptides tune the translation rate through a continuous, dynamic reshaping of the functional center of the ribosome.

Rapidly proliferating cells are at risk of compromised cell fitness due to proteostasis collapse from perturbations that interfere with ribosome biogenesis.

Ribosome assembly is monitored to promote proteostatis through a system whereby unassembled ribosomal proteins lead to activation of heat shock factor 1 and inactivation of the RP gene activator Ifh1.