Single-domain antibodies as potent inhibitors of clinically relevant <i>β</i>-lactamases in multidrug-resistant bacteria. [PDF]
Osset-Trenor P +2 more
europepmc +1 more source
A β-lactamase inhibitory protein mutant displays high potency and a broad inhibition profile due to an altered binding mode with β-lactamases. [PDF]
Rivera P +5 more
europepmc +1 more source
Enzyme graphene oxide interaction: the case system of β-lactamases. [PDF]
Piccirilli A +7 more
europepmc +1 more source
SAND: a comprehensive annotation of class D β-lactamases using structural alignment-based numbering. [PDF]
Attana F +17 more
europepmc +1 more source
Diversity in the Common Fold: Structural Insights into Class D β-Lactamases from Gram-Negative Pathogens. [PDF]
Smith CA, Stasyuk A.
europepmc +1 more source
Deciphering curcumin's differential inhibition of KPC-3, L2, and CTX-M-15 β-lactamases through binding energetics and structural dynamics. [PDF]
Shirzadi R, Bayan AM, Mosawi SH.
europepmc +1 more source
Standardized Residue Numbering and Secondary Structure Nomenclature in the Class D β-Lactamases. [PDF]
Stasyuk A, Smith CA.
europepmc +1 more source
Plant Metabolites as Potential Agents That Potentiate or Block Resistance Mechanisms Involving β-Lactamases and Efflux Pumps. [PDF]
Zai MJ, Cock IE, Cheesman MJ.
europepmc +1 more source
Genomic Analysis and Virulence Features of Vibrio cholerae Non-O1/Non-O139 Harbouring CARB-Type β-Lactamases From Freshwater Bodies, Argentina. [PDF]
Guevara Núñez D +10 more
europepmc +1 more source

