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. 2024 Nov 28;14:29627. doi: 10.1038/s41598-024-81304-2

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© The Author(s) 2024

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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Fig. 2 — Effects of S-allylmercaptocysteine (SAMC) on phosphoproteome in HC11 cells treated with lipopolysaccharide (LPS). (a) Workflow of phosphoproteomic analysis. (b) The proportion of phosphorylated amino acid residues in detected phosphopeptides (pSer = phosphorylated serine, pThr = phosphorylated threonine, pTyr = phosphorylated tyrosine). (c) The proportion of phosphopeptides increased by LPS stimulation (≥ 1.5-fold, 10.7%) and the proportions of these phosphopeptides increased (≥ 1.5-fold, 5.2%) or decreased (≤ 0.75-fold, 69.8%) by SAMC treatment. (d, e) The heat map of the phosphopeptides affected by LPS and SAMC in Fig. 2c (d) and the phosphorylation level of protein kinases in the TLR signaling pathway (e). LPS and SAMC columns show the log2 fold changes of the phosphopeptide abundance in LPS-treated cells vs. control and in LPS- and SAMC- treated cells vs. LPS alone-treated cells, respectively.