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• W2072684305 abstract "Helicobacter pylori colonizes the human gastric epithelium and causes diseases such as gastritis, peptic ulcers, and stomach cancer. Undecaprenyl pyrophosphate synthase (UPPS), which catalyzes consecutive condensation reactions of farnesyl pyrophosphate with eight isopentenyl pyrophosphate to form lipid carrier for bacterial peptidoglycan biosynthesis, represents a potential target for developing new antibiotics. In this study, we solved the crystal structure of H. pylori UPPS and performed virtual screening of inhibitors from a library of 58,635 compounds. Two hits were found to exhibit differential activities against Helicobacter pylori and Escherichia coli UPPS, giving the possibility of developing antibiotics specially targeting pathogenic H. pylori without killing the intestinal E. coli ." @default.
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• W2072684305 date "2008-01-01" @default.
• W2072684305 modified "2023-10-06" @default.
• W2072684305 title "Structure-Based Inhibitors Exhibit Differential Activities against<i>Helicobacter pylori</i>and<i>Escherichia coli</i>Undecaprenyl Pyrophosphate Synthases" @default.
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• W2072684305 doi "https://doi.org/10.1155/2008/841312" @default.
• W2072684305 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2276626" @default.
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