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. 2023 Jun 8;13:9297. doi: 10.1038/s41598-023-35765-6

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Shifts in thermal denaturation temperature of different eIF4A:RNA:silvestrol complexes are associated with eIF4A sensitivity to rocaglates. While relative eIF4A helicase activities of eIF4A mutant proteins expressing different rocaglate-binding aa patterns fall within a narrow range of V_max values and do not correlate with rocaglate sensitivity, comparative thermal shift analysis of the mutant proteins showed a clear association between sensitivity to rocaglates and higher thermal denaturation differentials between the eIF4A:RNA and eIF4A:RNA:silvestrol complexes. The increased stability of the rocaglate-sensitive mutants is determined by π–π-stacking interactions elicited by the corresponding aa residues at position 163. Data points represent mean values of three technical replicates. Standard errors for the helicase activities are indicated in Fig. 4A and standard errors for the Δ melting temperature are listed in Table S5. The size of the circles denotes prevalence of the aa pattern among the eIF4As included in our survey.