Overexpression of the recombinant Enterobacter cloacae P99 AmpC β-lactamase and its mutants based on a ϕ105 prophage system in Bacillus subtilis
Author:
Publisher
Elsevier BV
Subject
Biotechnology
Reference39 articles.
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2. Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity;Fisher;Chem. Rev.,2005
3. β-Lactamase inhibitors: agents to overcome bacterial resistance;Maiti;Curr. Med. Chem.,1998
4. β-Lactamase epidemiology and the utility of established and novel β-lactamase inhibitors;Payne;Expert. Opin. Investig. Drugs,2000
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1. Comparative Phosphoproteomics Reveals the Role of AmpC β-lactamase Phosphorylation in the Clinical Imipenem-resistant Strain Acinetobacter baumannii SK17;Molecular & Cellular Proteomics;2016-01
2. Actividad inhibitoria de dihidroxifenilpropenona sobre β-lactamasa de Enterobacter cloacae: estudio preliminar en el desarrollo de fármacos para enfrentar la resistencia bacteriana;Biomédica;2013-11-25
3. Validation of the AmpC β-Lactamase Binding Site and Identification of Inhibitors with Novel Scaffolds;Journal of Chemical Information and Modeling;2012-05-04
4. Engineered Amp C β-Lactamase as a Fluorescent Screening Tool for Class C β-Lactamase Inhibitors;Analytical Chemistry;2011-02-21
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