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. 2023 Jun;64(6):873–879. doi: 10.2967/jnumed.122.264597

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© 2023 by the Society of Nuclear Medicine and Molecular Imaging.

Immediate Open Access: Creative Commons Attribution 4.0 International License (CC BY) allows users to share and adapt with attribution, excluding materials credited to previous publications. License: https://creativecommons.org/licenses/by/4.0/. Details: http://jnm.snmjournals.org/site/misc/permission.xhtml.

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FIGURE 1. — Cellular responses to TAT with ²²⁵Ac-PP-F11N. (A) A431/CCKBR cells were treated with ²⁵⁵Ac-PP-F11N, and the generated tryptic peptides and phosphopeptide-enriched samples were subjected to proteomics and phosphoproteomics analysis, respectively. Volcano plots display phosphopeptide (phosphoproteomics) and protein (proteomics) abundance shown as log2-transformed fold change. Red and blue dots indicate significantly altered abundance of phosphopeptides or proteins. Q-value < 0.05. (B) Interaction networks of proteins with altered phosphorylation or expression in response to ²²⁵Ac-PP-F11N treatment. (C) Western blot analysis for phosphorylation of HDAC9, HDAC4, and HDAC5 at S246, S259, and S220, respectively; p53BP1 at S1778; p53 at S15; and total p53BP1 and GAPDH in protein lysates isolated from ²²⁵Ac-PP-F11N–treated and untreated (control) cells.