Anton A. Komar

TL;DR: A yeast two-hybrid analysis revealed that Pdcd4 associates with the eukaryotic translation initiation factors eIF4AI and eIF 4AII, and the mechanism by which PdCD4 inhibits translation appears to involve inhibition of eif4A helicase, interference with eIF2A association-dissociation from eIF3G, and inhibition ofeIF4A binding to the C-terminal domain of eIF5G.

TL;DR: The data suggest that kinetics of protein translation can affect the in vivo protein‐folding pathway, leading to increased levels of protein misfolding.

TL;DR: This review presents examples in which the competitive action of IRES-transacting factors plays a pivotal role in IRes-mediated translation and thereby controls cell-fate decisions leading to either pro-survival stress adaptation or cell death.

TL;DR: Findings indicate that translation kinetics might direct the co-translational folding pathway and that translational pausing at rare codons might provide a time delay to enable independent and sequential folding of the defined portions of the nascent polypeptide emerging from the ribosome.

TL;DR: It is shown that synonymous codon variants in the gene encoding gamma-B crystallin, a mammalian eye-lens protein, modulate the rates of translation and cotranslational folding of protein domains monitored in real time by Förster resonance energy transfer and fluorescence-intensity changes.