A model reveals how translation of an mRNA leader could provide resistance to global downregulation of 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.

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

The regulatory role of thousands of upstream open-reading frames were measured and used to determine the relative influences of sequence, structural, and positional features on translation regulation and nonsense-mediated decay.

Most of the mRNAs whose translation is resistant to the stress-induced repression of protein synthesis contain upstream open reading frames that are efficiently translated under normal conditions.

Building on previous work which showed that the small molecule ISRIB potently blocks the integrated stress response (Sidrauski et al., 2013), we report on ISRIB's remarkable specificity and fast action in vivo, underscoring its proposed direct effect on translation.

Rather than being a protein coding unit, an mRNA molecule can serve a purely regulatory function to inhibit protein synthesis of its corresponding gene.

Thousands of "noncoding" RNAs, 5' "untranslated" regions, and pseudogenes in humans are actually translated, and some of these are likely to express functional proteins.

A mutant impaired for ribosome recycling exhibits translational reprogramming wherein strong mRNAs outcompete weak mRNAs, also observed when preinitiation complexes are diminished by eIF2α phosphorylation or 40S ribosomal subunit depletion.