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

A conformational change in the Cricket Paralysis Virus IRES upon double translocation in the ribosome uncovers an unexpected similarity with the Hepatitis C Virus IRES.

The retarding effect of a ribosome-bound internal ribosome entry site on eukaryotic protein synthesis is largely overcome following translocation of tripeptidyl-tRNA.

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.

A Internal Ribosomal Entry Site RNA has been visualised by high resolution cryoEM, trapped in the ribosome in an intermediate state of translocation.

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.

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.

Hoxa3 and Hoxa11 translation inhibitory elements block cap-dependent translation by using upstream open reading frames with distinct modes of action.

LncRNA Neat1, with paraspeckle proteins, controls translational induction of (lymph)angiogenic and cardioprotective factors by the IRES-dependent mechanism in mouse cardiomyocytes submitted to hypoxia.

Electrophysiological and structural characterizations reveal that a previously proposed ion channel responsible for sensing mechanical pain is insensitive to poking or stretching stimuli for conducting ions and may serve as a coenzyme A-binding protein instead.