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• W2130037065 abstract "The ClpXP protease is a critical bacterial intracellular protease that regulates protein turnover in many bacterial species. Here we identified a pharmacological inhibitor of the ClpXP protease, F2, and evaluated its action in Bacillus anthracis and Staphylococcus aureus. We found that F2 exhibited synergistic antimicrobial activity with cathelicidin antimicrobial peptides and antibiotics that target the cell well and/or cell membrane, such as penicillin and daptomycin, in B. anthracis and drug-resistant strains of S. aureus. ClpXP inhibition represents a novel therapeutic strategy to simultaneously sensitize pathogenic bacteria to host defenses and pharmaceutical antibiotics." @default.
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• W2130037065 date "2012-04-01" @default.
• W2130037065 modified "2023-09-26" @default.
• W2130037065 title "Pharmacological Inhibition of the ClpXP Protease Increases Bacterial Susceptibility to Host Cathelicidin Antimicrobial Peptides and Cell Envelope-Active Antibiotics" @default.
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• W2130037065 doi "https://doi.org/10.1128/aac.05131-11" @default.
• W2130037065 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3318395" @default.
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