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Secondary metabolites rocaglates produced by plants lead to a plant‒fungus tug-of-war, utilizing unique amino acid substitutions in eIF4A, a target of the compounds.

Interactions of eIF4A and eIF4E with specific amino-acids in the N-terminal domain of DEAD-box helicase Ded1 enhance bulk polysome assembly and translation of reporter mRNAs with structured leaders in vivo.

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.

Human ferritin light chain (FTL) mRNA translation is regulated via its 5'-untranslated region (5'-UTR) by three mechanisms: RNA folding, iron response protein binding, and eukaryotic translation initiation factor eIF3 binding.

The ES6S region of the small subunit ribosome makes a place for the threading and secondary structure unwinding of mRNA, which regulates genome-wide translation.

The molecular microenvironment of coronaviral replicase complexes provides functional and spatial links between conserved cellular processes and viral RNA synthesis, and highlights potential targets for the development of novel antivirals.

A new in vitro approach allows measurement of the efficiency of the early steps of translation initiation on every messenger RNA in yeast simultaneously.

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.

Ded1p and eIF4A, two RNA helicases that function in eukaryotic translation initiation, interact physically with each other and with the scaffolding protein eIF4G.