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- W2897032009 abstract "Condensins play a unique role in orchestrating the global folding of the chromosome, an essential cellular process, and contribute to human disease and bacterial pathogenicity. As such, they represent an attractive and as yet untapped target for diverse therapeutic interventions. We describe here the discovery of small molecule inhibitors of the Escherichia coli condensin MukBEF. Pilot screening of a small diversity set revealed five compounds that inhibit the MukBEF pathway, two of which, Michellamine B and NSC260594, affected MukB directly. Computer-assisted docking suggested plausible binding sites for the two compounds in the hinge and head domains of MukB, and both binding sites were experimentally validated using mutational analysis and inspection of NSC260594 analogs. These results outline a strategy for the discovery of condensin inhibitors, identify druggable binding sites on the protein, and describe two small molecule inhibitors of condensins." @default.
- W2897032009 created "2018-10-26" @default.
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- W2897032009 date "2018-10-11" @default.
- W2897032009 modified "2023-10-14" @default.
- W2897032009 title "Small Molecule Condensin Inhibitors" @default.
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- W2897032009 doi "https://doi.org/10.1021/acsinfecdis.8b00222" @default.
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