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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
A focused fragment library targeting the antibiotic resistance enzyme - Oxacillinase-48: Synthesis, structural evaluation and inhibitor design.
β-Lactam antibiotics are of utmost importance when treating bacterial infections in the medical community. However, currently their utility is threatened by the emergence and spread of β-lactamExpand
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
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
- 1-A focused fragment library targeting the antibiotic 1 resistance enzyme-oxacillinase-48 : synthesis , structural 2 evaluation and inhibitor design 3
Sundus Akhter,Bjarte Aarmo Lund, Aya Ismael, Manuel Langer, Johan Isaksson, Tony 4 Christopeit, Hanna-Kirsti S. Leiros, Annette Bayer 5 6 1 Department of Chemistry, Faculty of Science and Technology,Expand