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- W4220979841 abstract "Lysine acylation plays pivotal roles in cell physiology, including DNA transcription and repair, signal transduction, immune defense, metabolism, and many other key cellular processes. Molecular mechanisms of dysregulated lysine acylation are closely involved in the pathophysiological progress of many human diseases, most notably cancers. In recent years, chemical biology tools have become instrumental in studying the function of post-translational modifications (PTMs), identifying new “writers”, “erasers” and “readers”, and in targeted therapies. Here, we describe key developments in chemical biology approaches that have advanced the study of lysine acylation and its regulatory proteins (2016–2021). We further discuss the discovery of ligands (inhibitors and PROTACs) that are capable of targeting regulators of lysine acylation. Next, we discuss some current challenges of these chemical biology probes and suggest how chemists and biologists can utilize chemical probes with more discriminating capacity. Finally, we suggest some critical considerations in future studies of PTMs from our perspective." @default.
- W4220979841 created "2022-04-03" @default.
- W4220979841 creator A5013676597 @default.
- W4220979841 creator A5017138858 @default.
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- W4220979841 creator A5021379796 @default.
- W4220979841 creator A5021926450 @default.
- W4220979841 creator A5034789862 @default.
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- W4220979841 creator A5058457237 @default.
- W4220979841 creator A5060604363 @default.
- W4220979841 creator A5083269293 @default.
- W4220979841 date "2022-04-05" @default.
- W4220979841 modified "2023-10-17" @default.
- W4220979841 title "Chemical Biology Tools for Protein Lysine Acylation" @default.
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