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1 eIF-4F, eIF-iso4F, and eIF-4B promoted PABP activity thr
3 anslation initiation factors eIF-4A, eIF-4B, eIF-4F, eIF-iso4F, and eIF-2 and the poly(A)-binding pro
7 how that the proteins bound to the mRNA cap (eIF-4F) and poly(A) tail (Pab1p) are physically associat
8 the two isoforms of the cap-binding complex (eIF-4F and eIF-iso4F) and eIF-4B, bind to the poly(A)-bi
11 mRNAs, which possess little requirement for eIF-4F but do not initiate by internal ribosome binding.
12 IF-4E), preventing formation of a functional eIF-4F complex essential for cap-dependent initiation of
15 data show that the binding of eIF-(iso)4F or eIF-4F to cap analogue enhanced their binding affinity t
16 ransfer, and it was determined that the PABP/eIF-4F complex could bind both poly(A) and 5' cap simult
19 ading to an increase in the formation of the eIF-4F initiation complex, relieves the translation repr
22 ving Akt1/mTOR complex 1 signaling (and thus eIF-4F-mediated translation initiation) from suppression
25 ribosome scanning and ribosome jumping when eIF-4F is abundant but exclusively uses a ribosome jumpi
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