Báo cáo khoa học: The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions
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The leader proteinase (Lpro) of foot-and-mouth disease virus (FMDV) ini-tially cleaves itself from the polyprotein. Subsequently, Lprocleaves thehost proteins eukaryotic initiation factor (eIF) 4GI and 4GII. This preventsprotein synthesis from capped cellular mRNAs; the viral RNA is still trans-lated, initiating from an internal ribosome entry site. Lprocleaves eIF4GIbetween residues G674 and R675. We showed previously, however, thatLprobinds to residues 640–669 of eIF4GI. Binding was substantiallyimproved when the eIF4GI fragment contained the eIF4E binding site andeIF4E was present in the binding assay....
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Báo cáo khoa học: The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions
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Báo cáo khoa học: The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions
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