Optimization of 1, 2, 4-triazole-3-thiones toward broad-spectrum metallo-β-lactamase inhibitors showing potent synergistic activity on VIM-and NDM-1-producing …
A Legru, F Verdirosa, Y Vo-Hoang… - Journal of Medicinal …, 2022 - ACS Publications
Metallo-β-lactamases (MBLs) contribute to the resistance of Gram-negative bacteria to
carbapenems, last-resort antibiotics at hospital, and MBL inhibitors are urgently needed to …
carbapenems, last-resort antibiotics at hospital, and MBL inhibitors are urgently needed to …
Discovery of 2-aminothiazole-4-carboxylic acids as broad-spectrum metallo-β-lactamase inhibitors by mimicking carbapenem hydrolysate binding
YH Yan, TT Zhang, R Li, SY Wang, LL Wei… - Journal of Medicinal …, 2023 - ACS Publications
Metallo-β-lactamases (MBLs) are zinc-dependent enzymes capable of hydrolyzing all
bicyclic β-lactam antibiotics, posing a great threat to public health. However, there are …
bicyclic β-lactam antibiotics, posing a great threat to public health. However, there are …
Interactions of hydrolyzed β-lactams with the L1 metallo-β-lactamase: Crystallography supports stereoselective binding of cephem/carbapenem products
L1 is a dizinc subclass B3 metallo-β-lactamase (MBL) that hydrolyzes most β-lactam
antibiotics and is a key resistance determinant in the Gram-negative pathogen …
antibiotics and is a key resistance determinant in the Gram-negative pathogen …
Are the newer carbapenems of any value against tuberculosis
X Gonzalo, F Drobniewski - Antibiotics, 2022 - mdpi.com
Our aim was to assess whether newer carbapenems with a better administration profile than
meropenem (ertapenem, faropenem and tebipenem) were more effective against …
meropenem (ertapenem, faropenem and tebipenem) were more effective against …
Time-resolved β-lactam cleavage by L1 metallo-β-lactamase
Serial x-ray crystallography can uncover binding events, and subsequent chemical
conversions occurring during enzymatic reaction. Here, we reveal the structure, binding and …
conversions occurring during enzymatic reaction. Here, we reveal the structure, binding and …
Interplay between the Enamine and Imine Forms of the Hydrolyzed Imipenem in the Active Sites of Metallo-β-lactamases and in Water Solution
AV Krivitskaya, MG Khrenova - Journal of Chemical Information …, 2022 - ACS Publications
Deactivation of the β-lactam antibiotics in the active sites of the β-lactamases is among the
main mechanisms of bacterial antibiotic resistance. As drugs of last resort, carbapenems are …
main mechanisms of bacterial antibiotic resistance. As drugs of last resort, carbapenems are …
Small-molecule inhibitors of bacterial-producing metallo-β-lactamases: insights into their resistance mechanisms and biochemical analyses of their activities
Antibiotic resistance (AR) remains one of the major threats to the global healthcare system,
which is associated with alarming morbidity and mortality rates. The defence mechanisms of …
which is associated with alarming morbidity and mortality rates. The defence mechanisms of …
The crystal structure of the H116Q mutant of NDM-1: An enzyme devoid of zinc ions
WP Kong, YW Chen, KY Wong - Journal of Structural Biology, 2022 - Elsevier
New Delhi metallo-β-lactamase 1 (NDM-1) is an important causative factor of antimicrobial
resistance due to its efficient hydrolysis of a broad range of β-lactam compounds. The two …
resistance due to its efficient hydrolysis of a broad range of β-lactam compounds. The two …
Phenotypic versus molecular assays for detecting carbapenemase-producing Enterobacterales from urinary tract infections
AM Nour El Deen, YS Naga… - Microbes and …, 2024 - journals.ekb.eg
Background: Carbapenem-resistant Enterobacterales (CRE) have been identified as a
public health problem. Treatment options for CRE are limited as they are mostly resistant to …
public health problem. Treatment options for CRE are limited as they are mostly resistant to …
[PDF][PDF] Time-Resolved β-lactam Cleavage by L1 Metallo-β-Lactamase
Time-Resolved β-lactam Cleavage by L1 Metallo-β- Lactamase Page 1 Time-Resolved β-lactam
Cleavage by L1 Metallo-βLactamase Andrzej Joachimiak ( andrzejj@anl.gov ) University …
Cleavage by L1 Metallo-βLactamase Andrzej Joachimiak ( andrzejj@anl.gov ) University …