Cue2 is an endonuclease that cleaves mRNA in the A site of the lagging ribosome upon ribosome collision events.

Rqc2-mediated modification of ribosome-stalled nascent chains with "CAT tails" promotes formation of insoluble aggregates suggesting that proteins can become specifically marked for aggregation.

An eukaryotic specific system cooperates with the ribosome quality control pathway to maintain the reading frame during translation of slowly translated sequences.

The structure of the VemP-stalled ribosome reveals a helix-double turn-helix conformation of the nascent chain within the ribosomal tunnel, illustrating how secondary structure formation directly at the peptidyltransferase center of the ribosome can induce translational arrest.

Although puromycin staining is often used to examine subcellular translation, puromycin-labeled proteins are rapidly released from ribosomes even in the presence of elongation inhibitors, which may confound translation site localization.

Collision between ribosomes can cause dissociation of stalled ribosomes from messenger RNAs during the process of mRNA translation.

Cyclic peptide natural products didemnin B and ternatin-4 bind the same hydrophobic pocket of eEF1A to inhibit mRNA translation but exhibit kinetic differences that influence rate-limiting conformational changes underpinning aminoacyl-tRNA selection.

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

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

Quantitative protein and ribosome 'accounting' in T cells highlights a gap in our understanding of how activated T cells sufficiently replicate their proteome during rapid cell division driven by infection.