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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.

The integrated stress response is able to rapidly shut down the synthesis of proteins in eukaryotic cells.

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.

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

Mining electron cryomicroscopy data reveals new ribosomal interactions that preclude translation to potentially regulate gene expression.

A compound that prevents stressors such as UV light and viral infection from downregulating protein synthesis inside cells improves memory performance in mice.

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.

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.

Genetically induced conformational modulation of eIF2B activates the Integrated Stress Response by impairing nucleotide exchange.

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