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. 2020 Nov 25;39:261. doi: 10.1186/s13046-020-01773-x

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© The Author(s) 2020

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Bromodomain inhibition with JQ1 alters relative histone peptide modification states in DIPG, in vitro. a Unsupervised hierarchical clustering of DIPG cell line SF8628 histone tail modification profiles reveals clustering by treatment condition. b-e Relative abundance of H3.1/3.3 K27, H3.3K36, and H4K20 peptide modification states in SF8628 cells are distinct after JQ1 treatment. f-g Relative abundance of H3K79me2 and H3K18ac peptides in SF8628 cell lines are distinct after JQ1 treatment. * p < 0.05 compared to DMSO group (independent-sample t test, two-tailed)