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Profiling histone post-translational modifications to identify signatures of epigenetic drug response in T-cell acute

Laura Corveleyn1,2, Lien Provez2,3, Osman Satilmis4,5

  • 1Laboratory of Pharmaceutical Biotechnology, ProGenTomics, Ghent University, Ghent, Belgium.

Scientific Reports
|March 26, 2026
PubMed
Abstract

No abstract available in PubMed .

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Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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