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. 2020 Mar 19;43(6):1819–1830. doi: 10.3892/or.2020.7554

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Copyright: © Gao et al.

This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

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Figure 1. — Acetylation and succinylation data of proteins in breast cancer and adjacent normal tissues. (A) Numbers of protein sites whose acetylation and succinylation were identified (sum of all numbers respectively) and quantified (acetylation: 64+170+33; succinylation: 103+20+134) in cancer and adjacent normal tissues, as well as protein sites whose modification levels were upregulated (acetylation: 170; succinylation: 134) and downregulated (acetylation: 33; succinylation: 20) in breast cancer tissue. (B and C) Statistics of the changes in modification levels of quantified proteins when setting 1.5 as the significant fold change (cancer vs. normal). (D and E) All quantified protein sites and their modification levels in breast cancer and adjacent normal tissues. (F) Venn diagram of proteins with significantly higher acetylation and succinylation levels in breast cancer tissue. (G) Venn diagram of proteins with significant lower acetylation and succinylation level in breast cancer tissue.