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- W2023016718 abstract "Structural modification of naturally occurring β-lactams and β-lactones is a highly effective strategy for generating drugs for treating bacterial infections, cancer, obesity, and hyperlipidemia. These drugs acylate catalytic amino acids (serine, threonine, or cysteine) in enzyme targets such as penicillin-binding proteins (PBPs), β-lactamases, lipases, HMG-CoA reductase, fatty acid synthetase, and the 20S proteasome. Optimally performing drugs combine features of high target affinity, chemoselective reactivity, and high stability of the acylated target protein. This review provides a perspective on these two classes of acylating agents and summarizes recent advances in mechanism and structure-based design of acylating drugs." @default.
- W2023016718 created "2016-06-24" @default.
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- W2023016718 date "2010-06-01" @default.
- W2023016718 modified "2023-10-17" @default.
- W2023016718 title "Acylating drugs: redesigning natural covalent inhibitors" @default.
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- W2023016718 doi "https://doi.org/10.1016/j.cbpa.2010.03.035" @default.
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