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- W2520347846 abstract "Significance Protein synthesis initiates in eukaryotes when the 40S ribosomal subunit, loaded with initiator tRNA, attaches to the 5′ end of the mRNA, scans the 5′ UTR, and selects the AUG start codon. Ribosome attachment and scanning are impeded by structures in the 5′ UTR that can be resolved by RNA helicases Ded1 and eukaryotic translation initiation factor 4A (eIF4A), with cofactors eIF4B and eIF4G. We show that eIF4B can stimulate translation independently of eIF4A and that eIF4B, eIF4A, and Ded1 are preferentially required for translating long mRNAs, burdened with 5′ UTR structures, that inefficiently form the closed-loop intermediate with the mRNA ends joined by eIF4G. In contrast, eIF4G appears to be most crucial for closed-loop assembly on short, highly translated, and unstructured mRNAs." @default.
- W2520347846 created "2016-09-23" @default.
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- W2520347846 date "2016-09-06" @default.
- W2520347846 modified "2023-09-27" @default.
- W2520347846 title "eIF4B stimulates translation of long mRNAs with structured 5′ UTRs and low closed-loop potential but weak dependence on eIF4G" @default.
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- W2520347846 doi "https://doi.org/10.1073/pnas.1612398113" @default.
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