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Updated: Jul 17, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Pharmacological targeting of lysine acetyltransferases in human disease: a progress report
David M Heery1, Peter M Fischer
1Centre for Biomolecular Sciences and School of Pharmacy, University of Nottingham, University Park, Nottingham, NG7 2RD, UK.
Abstract:
Lysine acetyltransferases (LATs) are a structurally disparate group of enzymes involved in regulating transcription by participating as cofactors in transcriptional regulatory complexes, and by acetylation of lysine residues in histones and other proteins. Aberrant LAT function probably plays an important part in the pathogenesis of certain cancers, especially leukaemias and endocrine tumours. However, LAT activity might also be an important drug target in a range of other indications, including inflammatory lung diseases, viral infections and metabolic disorders. At present, comparatively few LAT inhibitors are known, but progress regarding the understanding of their structural and functional biology is now beginning to reveal LATs as promising new epigenetic drug targets.
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