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

LncRNA Neat1, with paraspeckle proteins, controls translational induction of (lymph)angiogenic and cardioprotective factors by the IRES-dependent mechanism in mouse cardiomyocytes submitted to hypoxia.

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.

Ribosomal profiling reveals that translational repression is an important mechanism for cell cycle control and can complement protein degradation.

A key cellular stress granule protein, G3BP1, is critical for efficient norovirus infection, representing the first pan-norovirus, pro-viral factor identified to date.

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.

PRMT5 participates in ovarian granulosa cell lineage maintenance by regulating Wt1 IRES-dependent translation.

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.

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.

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.