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Inhibition by Avibactam and Clavulanate of the β-Lactamases KPC-2 and CTX-M-15 Harboring the Substitution N(132)G in the Conserved SDN Motif

The substitution N(132)G in the SDN motif of class A β-lactamases from rapidly growing mycobacteria was previously shown to impair their inhibition by avibactam but to improve the stability of acyl-enzymes formed with clavulanate. The same substitution was introduced in KPC-2 and CTX-M-15 to assess...

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Detalhes bibliográficos
Publicado no:Antimicrob Agents Chemother
Main Authors: Ourghanlian, Clément, Soroka, Daria, Arthur, Michel
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Microbiology 2017
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC5328567/
https://ncbi.nlm.nih.gov/pubmed/28069651
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AAC.02510-16
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