Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibitio...
Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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β-Lactamases enable resistance to almost all β-lactam antibiotics. Pioneering work revealed that acyclic boronic acids can act as ‘transition state analogue’ inhibitors of nucleophilic serine enzymes, including serine-β-lactamases. Here we report biochemical and biophysical analyses revealing that cyclic boronates potently inhibit both nucleophilic...
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Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates
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TN_cdi_doaj_primary_oai_doaj_org_article_bb894e352b404c67a6c95bd78e1a12a8
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bb894e352b404c67a6c95bd78e1a12a8
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/ncomms12406
