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Metallo-β-lactamase inhibitors by bioisosteric replacement: Preparation, activity and binding.
Bacterial resistance is compromising the use of β-lactam antibiotics including carbapenems. The main resistance mechanism against β-lactams is hydrolysis of the β-lactam ring mediated by serine- orExpand
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His224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo-β-Lactamase VIM-7
ABSTRACT Metallo-β-lactamases (MBLs) are the causative mechanism for resistance to β-lactams, including carbapenems, in many Gram-negative pathogenic bacteria. One important family of MBLs is theExpand
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Role of Residues W228 and Y233 in the Structure and Activity of Metallo-β-Lactamase GIM-1
ABSTRACT Metallo-β-lactamases (MBLs) hydrolyze virtually all β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems. The worldwide emergence of antibiotic-resistant bacteriaExpand
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ZN148 Is a Modular Synthetic Metallo-β-Lactamase Inhibitor That Reverses Carbapenem Resistance in Gram-Negative Pathogens In Vivo
Carbapenem-resistant Gram-negative pathogens are a critical public health threat and there is an urgent need for new treatments. Carbapenemases (β-lactamases able to inactivate carbapenems) have beenExpand
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Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding
ABSTRACT Metallo-β-lactamases (MBLs) threaten the effectiveness of β-lactam antibiotics, including carbapenems, and are a concern for global public health. β-Lactam/β-lactamase inhibitor combinationsExpand
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Structural studies of triazole inhibitors with promising inhibitor effects against antibiotic resistance metallo-β-lactamases.
Metallo-β-lactamases (MBLs) are an emerging cause of bacterial antibiotic resistance by hydrolysing all classes of β-lactams except monobactams, and the MBLs are not inhibited by clinically availableExpand
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Site-directed mutagenesis of the metallo-β-lactamase VIM-7 from the opportunistic human pathogenic bacteria Pseudomonas aeruginosa KJE-3900
The metallo-β-lactamases (MBLs) are enzymes with the ability to hydrolyse the βlactam antibiotics. The worldwide emergence of the antibiotic resistant MBLs poses an increasing clinical threat. TheExpand
Site-directed mutagenesis of the metallo-β-lactamase VIM-7 from the opportunistic human pathogenic bacteria Pseudomonas aeruginosa
The metallo-β-lactamases (MBLs) are enzymes with the ability to hydrolyse the βlactam antibiotics. The worldwide emergence of the antibiotic resistant MBLs poses an increasing clinical threat. TheExpand
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