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Non-histone protein acetylation modulation refers to the dynamic regulation of acetylation (primarily lysine acetylation) on proteins other than histones, mediated by acetyltransferases and deacetylases. This post-translational modification can regulate protein stability, enzymatic activity, protein-protein interactions, subcellular localization, and cross-talk with other modifications. Non-histone protein acetylation is involved in a broad range of cellular processes, including gene transcription, DNA repair, cell division, metabolism, and cell signaling, and dysregulation is implicated in diseases such as cancer and neurodegeneration. Instead of designating a single molecular target, this term encompasses a set of regulatory enzymes (like lysine acetyltransferases and deacetylases) and their non-histone substrates. Drugs that influence non-histone acetylation, such as HDAC inhibitors, have therapeutic relevance but act on the modifying enzymes rather than on a single substrate.
Inhibition of deacetylase activity (increases acetylation levels); Inhibition of acetyltransferase activity (decreases acetylation levels)
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