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Eukaryotic translation initiation factor 3 (eIF3) is required to stabilize the binding of mRNA at the exit channel of the small ribosomal subunit and acts at the entry channel to accelerate mRNA recruitment to the translation preinitiation complex.

A pattern recognition receptor called toll-like receptor 13 detects pathogens in a manner that is different to that seen in other pathogen sensors.

Alkylation stress modify mRNAs and results in translation arrest, which activates the ribosome-rescue pathway of trans translation in bacteria.

Cancer-associated changes in small nucleolar RNAs and site-specific pseudouridine modifications impact ribosome activity.

PTRF (Cavin-1) mediates metabolism-regulated ribosomal transcription in mature adipocytes, independent of its role in caveolae formation.

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.

Embryonic development requires autophagy-dependent degradation of ribosomal RNAs.

A method that involves simultaneous tracking of individual mRNAs and their associated ribosomes can be used to determine when and where individual molecules get translated in living cells.

Nascent regulatory peptides tune the translation rate through a continuous, dynamic reshaping of the functional center of the ribosome.

Ribosome profiling data from several eukaryotic species provides strong evidence that many long non-coding RNA molecules encode novel short proteins.