Results 21 to 30 of about 52,332 (219)
Aspergillomarasmine A inhibits metallo-β-lactamases by selectively sequestering Zn2. [PDF]
J Biol Chem, 2021 Class B metallo-β-lactamases (MBLs) are Zn2+-dependent enzymes that catalyze the hydrolysis of β-lactam antibiotics to confer resistance in bacteria. Several problematic groups of MBLs belong to subclass B1, including the binuclear New Delhi MBL (NDM ...
Sychantha D +4 more
europepmc +2 more sources
Metallo-β-lactamases and a tug-of-war for the available zinc at the host-pathogen interface. [PDF]
Curr Opin Chem Biol, 2022 Metallo-β-lactamases (MBLs) are zinc-dependent hydrolases that inactivate virtually all β-lactam antibiotics. The expression of MBLs by Gram-negative bacteria severely limits the therapeutic options to treat infections. MBLs bind the essential metal ions
Bahr G, González LJ, Vila AJ.
europepmc +2 more sources
Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design. [PDF]
Chem Rev, 2021 Antimicrobial resistance is one of the major problems in current practical medicine. The spread of genes coding for resistance determinants among bacteria challenges the use of approved antibiotics, narrowing the options for treatment.
Bahr G, González LJ, Vila AJ.
europepmc +2 more sources
Relative inhibitory activities of the broad-spectrum β-lactamase inhibitor taniborbactam against metallo-β-lactamases. [PDF]
Antimicrob Agents Chemother, 2023 Taniborbactam (TAN) is a novel broad-spectrum β-lactamase inhibitor with significant activity against subclass B1 metallo-β-lactamases (MBLs). Here, we showed that TAN exhibited an overall excellent activity against B1 MBLs including most NDM- and VIM ...
Le Terrier C +4 more
europepmc +2 more sources
Scientific Reports, 2021 New Delhi metallo-β-lactamase variants and different types of metallo-β-lactamases have attracted enormous consideration for hydrolyzing almost all β-lactam antibiotics, which leads to multi drug resistance bacteria.
Azhar Salari-jazi +4 more
doaj +1 more source
Emerging Infectious Diseases, 2023 Controlling the spread of carbapenem-resistant Enterobacterales is a global priority. Using National Healthcare Safety Network data, we characterized the changing epidemiology of carbapenem-resistant Klebsiella pneumoniae (CRKP) in a large public health
Jennifer Lee +7 more
doaj +1 more source
Faropenem reacts with serine and metallo-β-lactamases to give multiple products. [PDF]
Eur J Med Chem, 2021 Penems have demonstrated potential as antibacterials and β-lactamase inhibitors; however, their clinical use has been limited, especially in comparison with the structurally related carbapenems.
Lucic A +12 more
europepmc +2 more sources
Could β-Lactam Antibiotics Block Humoral Immunity?
Frontiers in Immunology, 2021 It has been reported that treatment with β-lactam antibiotics induces leukopenia and candidemia, worsens the clinical response to anticancer immunotherapy and decreases immune response to vaccination.
Cléa Melenotte +13 more
doaj +1 more source
RUHS Journal of Health Sciences, 2023 Introduction: Infections are the major cause of morbidity and mortality in burn patients. The ESBL, MBL and AmpC are the major mediators of antimicrobial resistance in gram negative bacteria. Early detection of ESBL, MBL and AmpC β -lactamases is crucial
Kusum Lata Lodha, Seema Surana
doaj +1 more source
Specific Protein-Membrane Interactions Promote Packaging of Metallo-β-Lactamases into Outer Membrane Vesicles. [PDF]
Antimicrob Agents Chemother, 2021 Outer membrane vesicles (OMVs) act as carriers of bacterial products such as plasmids and resistance determinants, including metallo-β-lactamases. The lipidated, membrane-anchored metallo-β-lactamase NDM-1 can be detected in Gram-negative OMVs.
López C +6 more
europepmc +2 more sources