eIF3, despite being a general translation initiation factor, functions in mRNA-specific regulation, having a profound impact on the synthesis and activation of the MAPK pathway components and ribosomal proteins.

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.

Binding of the translation initiation factor eIF3 to the messenger RNAs encoding the T cell receptor subunits alpha and beta is required to drive a short burst in their translation and promote a strong T cell response.

The N-terminal domain (NTD) of the initiation factor eIF5 bound to the 40S subunit at the precise location vacated by eIF1 promotes tRNAi accommodation at AUG codons.

Eukaryotic translation initiation factor 4A is stimulated by the ribosomal pre-initiation complex and promotes the recruitment of mRNAs regardless of their degree of structure.

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.

The ribosome bound structure of a new IRES reveals novel architecture features used by viruses to hijack cellular translation.

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.

The eIF3 translation initiation complex exerts specific regulation on neuronal protein levels by targeting mRNAs with GC-rich 5' UTR.