Results 1 to 10 of about 17,127 (173)

Morin combined with meropenem is a potent inhibitor of NDM-1 against NDM-1-producing E. coli [PDF]

open access: yesScientific Reports
Some β-lactam antibiotics are hydrolyzed by the enzyme New Delhi metallo-β-lactamase 1 (NDM-1), increasing antibiotic resistance and posing a significant threat to public health. Thus, there is an urgent need to develop and use potent inhibitors of NDM-1
Qinghai Ren   +8 more
doaj   +3 more sources

The directed evolution of NDM-1. [PDF]

open access: yesAntimicrob Agents Chemother, 2023
ABSTRACT β-Lactam antibiotics are among the most frequently prescribed therapeutic agents. A common mechanism of resistance toward β-lactam antibiotics is the production of β-lactamases. These enzymes are capable of hydrolyzing the β-lactam bond, rendering the drug inactive.
Thomas CA   +8 more
europepmc   +3 more sources

NDM-1 plasmid clustering reflects clonal transmission of Klebsiella pneumoniae ST147 in four hospitals in Berlin, Germany [PDF]

open access: yesAntimicrobial Resistance and Infection Control
Background In recent years, the detection of Klebsiella pneumoniae (KLPN) producing New Delhi metallo-β-lactamase (NDM), particularly NDM-1, has increased in Germany.
Anna Weber   +4 more
doaj   +2 more sources

The transferability and evolution of NDM-1 and KPC-2 co-producing Klebsiella pneumoniae from clinical settings

open access: yesEBioMedicine, 2020
Background: Emergence of KPC-2 and NDM-1-coproducing carbapenem-resistant Klebsiella pneumoniae (KPC-2-NDM-1-CRKP) has escalated threat of CRKP to healthcare. Currently, only 4 isolates had been reported sporadically.
Hua Gao, Yudong Liu, Longyang Jin
exaly   +3 more sources

Production of plasmid-encoding NDM-1 in clinical Raoultella ornithinolytica and Leclercia adecarboxylata from China

open access: yesFrontiers in Microbiology, 2015
Raoultella ornithinolytica YNKP001 and Leclercia adecarboxylata P10164, harboring conjugative plasmids pYNKP001-NDM and pP10164-NDM with determination of complete nucleotide sequences, respectively, were isolated from two different Chinese patients ...
Fengjun Sun, Peiyuan Xia, Dongsheng Zhou
exaly   +3 more sources

In Silico Evaluation of Potential NDM-1 Inhibitors: An Integrated Docking and Molecular Dynamics Approach [PDF]

open access: yesPharmaceuticals
Background/Objectives: Non-fermenting Gram-negative bacteria are resistant to most antibiotics, due to the production of enzymes such as NDM-1. Faced with this challenge, computational methods have become essential for the design of NDM-1 carbapenemase ...
Eduvan Valencia   +4 more
doaj   +2 more sources

Cefiderocol-Based Regimen for Acinetobacter NDM-1 Outbreak. [PDF]

open access: yesAntibiotics (Basel)
Variable outcomes have been reported with cefiderocol in infections due to carbapenem-resistant Acinetobacter baumannii (CRAB). Nonetheless, it may be the only option for metallo-beta-lactamase-producing strains. We describe an outbreak of NDM-CRAB infections treated with cefiderocol. Thirty-eight patients were colonized and/or infected.
Travi G   +10 more
europepmc   +4 more sources

Embelin Restores Carbapenem Efficacy against NDM-1-Positive Pathogens [PDF]

open access: yesFrontiers in Microbiology, 2018
The emergence and spread of carbapenemase in Gram-negative pathogens poses an enormous threat to global public health. New Delhi metallo-β-lactamase-1 (NDM-1) inactivates nearly every class of β-lactam antibiotics, including carbapenem; however, there is
Nian-Zhi Ning   +11 more
doaj   +3 more sources

Genetic basis of transmission of bla NDM-1 among foodborne Vibrio parahaemolyticus strains in China [PDF]

open access: yesApplied Microbiology and Biotechnology
Carbapenem-resistant Vibrio parahaemolyticus has emerged and spread extensively in China, posing a substantial threat to food safety and human health. This study investigated the prevalence of carbapenem resistance in V.
Dan Chen   +8 more
doaj   +2 more sources

The antimicrobial peptide thanatin disrupts the bacterial outer membrane and inactivates the NDM-1 metallo-β-lactamase

open access: yesNature Communications, 2019
The NDM-1 metallo-β-lactamase confers resistance to β-lactam antibiotics. Here, the authors show that the antimicrobial peptide thanatin is active against NDM-1-producing bacteria through a dual mechanism of action consisting of disruption of outer ...
Bo Ma, Chao Fang, Xiao-yan Xue
exaly   +2 more sources

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