Substitutions in general translation initiation factor eIF1A found as recurring somatic mutations in uveal melanoma destabilize the closed conformation of the preinitiation complex at the start codon and increase discrimination against suboptimal initiation codons genome-wide.

A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.

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.

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.

Eliminating eukaryotic initiation factor 2 (eIF2) from wild-type budding yeast had little impact on translation of individual mRNAs, including those with regulatory upstream open-reading frames, even when canonical initiation factor eIF2 activity was impaired.

Ribosome collisions along an mRNA are shown to recruit factors that prevent additional ribosomes from initiating translation on that mRNA, thereby providing time to resolve the collision.

The hepatitis C virus IRES binds and remodels preassembled eukaryotic translation preinitiation complexes, using specific initiation factor protein within a "bacterial-like" mode of initiation that can function in both stressed and unstressed cells.

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.

Yeast RNA helicase Ded1 stimulates ribosome recruitment of structure-laden native mRNAs in a reconstituted system by interactions between domains in Ded1 and initiation factor eIF4G that stabilizes a Ded1-eIF4F complex.

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.