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. 2022 Nov 10;54(11):1927–1939. doi: 10.1038/s12276-022-00879-w

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — a Heatmap for global gene expression with group clusters (n = 3). b Volcano map of DEGs in the SA group vs. the control group (upregulation: 75 genes and downregulation: 32 genes). DEGs with FC (fold change) ≥ 2 were accepted as positive DEGs. c Pathway enrichment bubble map based on the KEGG enrichment analysis. A rich factor indicates a higher degree of enrichment, a larger p value (−log10) indicates a higher statistical significance, and a larger bubble indicates a higher degree of enrichment. d GO enrichment of those DEGs. A rich factor indicates a higher degree of enrichment, a larger p value (−log10) indicates a higher statistical significance, and a larger bubble indicates a higher degree of enrichment, BP: biological process, CC: cellular component. e Molecular docking for estimating the binding site of IRE1α and SA. The three-dimensional (3D) structures of IRE1α and SA were subjected to molecular docking, and the binding site was obtained according to the software scoring system. Upper left panel: SA was located in the cavity formed by the IRE1α 3D structure, upper right panel: magnification of the cavity; lower left panel: binding site of SA and IRE1α, lower left panel: magnification showing the hydrogen bonds (yellow dot line) formed between SA and IRE1α. f DARTS assay for confirmation of IRE1α and SA binding. Protease was used to digest IRE1α protein. With the addition of SA, the digestion of IRE1α was significantly blocked at each concentration of protease compared with the DMSO group.