Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.

An ancient complex comprising the eukaryotic elongation factor-1A and aminoacylated tRNA is shown to be the target of a cyclic heptapeptide and two unrelated natural products with potent anticancer activity.

Cyclic peptide natural products didemnin B and ternatin-4 bind the same hydrophobic pocket of eEF1A to inhibit mRNA translation but exhibit kinetic differences that influence rate-limiting conformational changes underpinning aminoacyl-tRNA selection.

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.

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.

Both exogenous and endogenous genes can be highly activated in cells by a new dCas9-based activator, CRISPR-assisted trans enhancer, that can be used to activate genes for biomedical applications.

Junction Mapper is a powerful new semi-automated software that provides a fingerprint of cell–cell contact morphometry and receptor density alterations.

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.

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.