Eukaryotic translation initiation factor 3 (eIF3) is required to stabilize the binding of mRNA at the exit channel of the small ribosomal subunit and acts at the entry channel to accelerate mRNA recruitment to the translation preinitiation complex.

Ribosome production is unexpectedly integrated into innate cell-intrinsic responses that regulate double strand DNA-sensing and inflammatory cytokine induction in infected and uninfected cells.

A pattern recognition receptor called toll-like receptor 13 detects pathogens in a manner that is different to that seen in other pathogen sensors.

The messenger RNA encoding La-related protein-4 (LARP4) contains a short region of instability whose codon clusters are sensitive to low abundance tRNAs that when elevated increase LARP4 activity for poly(A) lengthening of ribosomal protein mRNAs and other mRNAs.

Embryonic development requires autophagy-dependent degradation of ribosomal RNAs.

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-EM structures of 70S•RelA ribosome complexes reveal how cognate deacyl-tRNA activates RelA.

A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.

Mass spectrometry analysis of purified pre-ribosomal RNAs shows that stable ribosomal RNA domains independently recruit assembly factors, and the cryo-EM structure of the 5' ETS ribonucleoprotein reveals regulatory conformational switches.

Cancer-associated changes in small nucleolar RNAs and site-specific pseudouridine modifications impact ribosome activity.