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. 2024 Dec 28;14:31210. doi: 10.1038/s41598-024-82514-4

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Fig. 5 — INTL1 is the receptor for LF binding in HepG2 cells. (A) Western blot images showing the interactions of LF and the known receptors (LRP1, INTL1, and TLR4) for LF (upper, anti-LF) and the interaction of LF and TRAF2 (lower, anti-TRAF2) by Co-IP. (B) Western blot images showing the downregulation of LRP1 by LRP1-specific shRNAs (sh-LRP1) and the effects of LRP1 downregulation on p38 MAPK, JNK, and ERK phosphorylation. (C) Western blot images showing the downregulation of INTL1 by INTL1-specific shRNAs (sh-INTL1) and the effects of INTL1 downregulation on p38 MAPK, JNK, and ERK phosphorylation. The relative protein levels were determined after β-actin normalization.