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- W1513723427 endingPage "253" @default.
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- W1513723427 abstract "With antibiotic resistance mechanisms increasing in diversity and spreading among bacterial pathogens, the development of new classes of antibacterial agents against judiciously chosen targets is a high-priority task. The biochemical pathway for peptidoglycan biosynthesis is one of the best sources of antibacterial targets. Within this pathway are the Mur ligases, described in this review as highly suitable targets for the development of new classes of antibacterial agents. The amide ligases MurC, MurD, MurE and MurF function with the same catalytic mechanism and share conserved amino acid regions and structural features that can conceivably be exploited for the design of inhibitors that simultaneously target more than one enzyme. This would provide multi-target antibacterial weapons with minimized likelihood of target-mediated resistance development." @default.
- W1513723427 created "2016-06-24" @default.
- W1513723427 creator A5006593204 @default.
- W1513723427 creator A5058001103 @default.
- W1513723427 creator A5069650075 @default.
- W1513723427 date "2014-09-05" @default.
- W1513723427 modified "2023-10-14" @default.
- W1513723427 title "The biology of <scp>Mur</scp> ligases as an antibacterial target" @default.
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- W1513723427 doi "https://doi.org/10.1111/mmi.12758" @default.
- W1513723427 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25130693" @default.