The ribosome bound structure of a new IRES reveals novel architecture features used by viruses to hijack cellular translation.

In mouse cardiomyocytes, (lymph)angiogenic growth factors are induced during early hypoxia by a translational mechanism involving a new IRES trans-acting factor, vasohibin-1.

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

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.

ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.

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.

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.

Acute hypoxia activates TRPA1 channels in cerebral artery endothelial cells to activate an early adaptive response to reduce tissue ischemic damage through vasodilation.

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

Touch information is represented with minimal noise in the somatosensory cortex during tactile exploration.