Yeast RNA helicase Ded1 stimulates ribosome recruitment of structure-laden native mRNAs in a reconstituted system by interactions between domains in Ded1 and initiation factor eIF4G that stabilizes a Ded1-eIF4F complex.

Ded1p and eIF4A, two RNA helicases that function in eukaryotic translation initiation, interact physically with each other and with the scaffolding protein eIF4G.

The mTOR downstream effector eukaryotic initiation factor 4E-binding protein 1 (4E-BP1) regulates mechanical nociception via translational control of synaptic transmission in the spinal cord.

Interactions of eIF4A and eIF4E with specific amino-acids in the N-terminal domain of DEAD-box helicase Ded1 enhance bulk polysome assembly and translation of reporter mRNAs with structured leaders in vivo.

Eukaryotic translation initiation factor 4A is stimulated by the ribosomal pre-initiation complex and promotes the recruitment of mRNAs regardless of their degree of structure.

Overexpression of inhibitor of Bruton's tyrosine kinase contributes to the process of tumorigenesis by amplifying translation, represents a promising target for anti-cancer therapies.

La-related protein 1 specifically and directly binds the 5' cap and first nucleotide of mRNAs encoding ribosomal proteins and translation factors, inhibiting the assembly of translation initiation factors on these messages and therefore their translation.

Utilizing a conserved mechanism, a ribosome can initiate translation from a site within the insulin receptor mRNA to maintain protein synthesis even when standard mechanisms of initiating translation have been inhibited by stress.

The yeast mRNA decapping enzyme Dcp1/Dcp2 repressses many genes whose products are required on poor carbon or nitrogen sources in nutrient-replete cells by mRNA decapping and degradation or translational repression, adding post-transcriptional controls to the transcriptional repression of these functions.

LARP1 turns off and on the translation of an essential class of mRNAs by acting as a key effecter and regulator for mTORC1.