Influence of the Active Site Flexibility on the Efficiency of Substrate Activation in the Active Sites of Bi-Zinc Metallo-β-Lactamases. [PDF]
Krivitskaya AV, Khrenova MG.
europepmc +1 more source
Global and regional prevalence of metallo-β-lactamases in carbapenem-resistant Acinetobacter baumannii: a systematic review and meta-analysis. [PDF]
Karakonstantis S +3 more
europepmc +1 more source
A Case of New Delhi Metallo-β-Lactamases (NDM) Citrobacter sedlakii Osteomyelitis Successfully Treated With Ceftazidime-Avibactam and Aztreonam. [PDF]
Rubnitz ZA +3 more
europepmc +1 more source
Inhibition of metallo-β-lactamases in carbapenem resistant Gram negative bacilli by omeprazole and pantoprazole. [PDF]
Omar EM +4 more
europepmc +1 more source
Aspergillomarasmine A inhibits metallo-β-lactamases by selectively sequestering Zn2. [PDF]
Sychantha D +4 more
europepmc +1 more source
Aeromonas spp, are increasingly being recognized as human pathogens. The presence of metallo-β-lactamases in these organisms represents a potential problem in antimicrobial therapy.
Quiroga, M. I. +6 more
core
Deciphering the evolution of metallo-β-lactamases: A journey from the test tube to the bacterial periplasm. [PDF]
López C +3 more
europepmc +1 more source
Active site loops of membrane-anchored metallo-β-lactamases from environmental bacteria determine cephalosporinase activity. [PDF]
Carnevale MC +8 more
europepmc +1 more source
Metallo-β-lactamases and a tug-of-war for the available zinc at the host-pathogen interface. [PDF]
Bahr G, González LJ, Vila AJ.
europepmc +1 more source
Comment On: Encoding Genes of Metallo‑β‑Lactamases (IMP, NDM, and VIM) in <i>Klebsiella pneumoniae</i> in Iran: A Systematic Review and Meta‑Analysis (Sadeghi et al., 2025). [PDF]
Kumari N, Kumari J, Khan MS.
europepmc +1 more source

