Activation of the integrated stress response by stalled translation elongation complexes attenuates neurodegeneration, and demonstrates a protective link between a decrease in the rate of translation initiation and defects in translation elongation.

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.

METTL18 methylates histidine 245 of ribosomal protein RPL3, retards ribosome traversal at tyrosine codons, and thus ensures nascent protein folding for proteostasis maintenance.

Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.

During initiation factor-independent RNA structure-driven translation initiation, a flexible RNA element drives the movement of a viral IRES through the ribosome's tRNA binding sites and promotes tRNA binding.

Carefully controlling the level of protein synthesis reduction and mode of translation inhibitor action reveal different and sometimes opposing phenotypic effects following proteostasis stress, wherein protection via initiation inhibition specifically depends on heat shock factor 1.

Specific amino acids in the N-terminus of the replication initiator protein DnaA inhibit translation elongation upon carbon starvation, illustrating that the identity of the N-terminal amino acids of a protein can modulate protein synthesis yield under changing conditions.

Genetic screens and functional assays utilizing reporter mRNAs triggering NGD or COMD provide a basis for understanding the unique contributions of each pathway to translation-coupled mRNA decay and contextualizes their effects in the larger cellular process of translation surveillance.

With the removal of confounding artifacts, ribosome profiling can yield insight into the mechanism of protein synthesis in bacteria at high resolution.

An ensemble of cryo-EM structures reveals how eukaryotic elongation factor 2 positions the first codon of a viral mRNA for translation.