Rational Design of Benzobisheterocycle Metallo-β-Lactamase Inhibitors: A Tricyclic Scaffold Enhances Potency against Target Enzymes. [PDF]
Villamil V +13 more
europepmc +1 more source
Hydroxyhexylitaconic acids as potent IMP-type metallo-β-lactamase inhibitors for controlling carbapenem resistance in <i>Enterobacterales</i>. [PDF]
Wachino J-i +6 more
europepmc +1 more source
Antimicrobial and Diagnostic Stewardship of the Novel β-Lactam/β-Lactamase Inhibitors for Infections Due to Carbapenem-Resistant Enterobacterales Species and Pseudomonas aeruginosa. [PDF]
Ferous S +4 more
europepmc +1 more source
Assessment of the activity and mechanisms of resistance to cefiderocol and combinations of β-lactams and the novel β-lactamase inhibitors avibactam, taniborbactam, zidebactam, nacubactam, xeruborbactam, and ANT3310 in emerging double-carbapenemase-producing Enterobacterales. [PDF]
Blanco-Martín T +17 more
europepmc +1 more source
Development and Validation of a Capillary Zone Electrophoresis-Tandem Mass Spectrometry Method for Simultaneous Quantification of Eight β-Lactam Antibiotics and Two β-Lactamase Inhibitors in Plasma Samples. [PDF]
Cizmarova I +3 more
europepmc +1 more source
Comprehensive stability analysis of 13 β-lactams and β-lactamase inhibitors in <i>in vitro</i> media, and novel supplement dosing strategy to mitigate thermal drug degradation. [PDF]
Zhou J +17 more
europepmc +1 more source
BlaC, the single chromosomally-encoded β-lactamase of Mycobacterium tuberculosis, has been identified as a promising target for novel therapies that rely upon β-lactamase inhibition.
Saugata Hazra +2 more
exaly +2 more sources

