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• W4241837504 endingPage "2900" @default.
• W4241837504 startingPage "2896" @default.
• W4241837504 abstract "Eukaryotic initiation factor 4F (eIF-4F) is a three-subunit complex that binds the 5' cap structure (m7GpppX, where X is any nucleotide) of eukaryotic mRNAs. This factor facilitates ribosome binding by unwinding the secondary structure in the mRNA 5' noncoding region. The limiting component of the 4F complex is believed to be the 24-kDa cap-binding phosphoprotein, eIF-4E. In this report, we describe the phosphorylation of eIF-4E in response to expression of the tyrosine kinase oncoproteins pp60v-src and pp60c-src527F. The results suggest that eIF-4E functions as a downstream target of the phosphorylation cascade induced by tyrosine-specific protein kinases as well as by effectors of the mitogenic response." @default.
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• W4241837504 creator A5034728158 @default.
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• W4241837504 date "1991-05-01" @default.
• W4241837504 modified "2023-10-17" @default.
• W4241837504 title "Phosphorylation of eukaryotic translation initiation factor 4E is increased in Src-transformed cell lines" @default.
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• W4241837504 doi "https://doi.org/10.1128/mcb.11.5.2896-2900.1991" @default.
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