Results 11 to 20 of about 9,598 (127)

Metallo-Beta-Lactamases: NDM

open access: yesJournal of Education, Health and Sport, 2019
New Delhi, an enzyme belonging to the Metallo-beta-lactamases and Carbapenemases group, is most commonly found in Klebsiella pneumoniae and Escherichia coli. It determines these bacteria resistance to the majority of known antibiotics.
Kamil Leis   +13 more
doaj   +3 more sources

Successful Management of Urosepsis with Ceftriaxone+Sulbactam+EDTA: A Case Report of Penem Sparing Approach [PDF]

open access: yesJournal of Clinical and Diagnostic Research, 2017
Over the past decade, the Anti-Microbial Resistance (AMR) among members of Enterobacteriaceae family is on rise mainly due to rapid spread of strains producing Extended-Spectrum Beta-Lactamases (ESBLs) and Metallo Beta-Lactamases (MBLs).
Amit Bery, Candy Sodhi, Rishu Bhanot
doaj   +1 more source

A promiscuous ancestral enzyme´s structure unveils protein variable regions of the highly diverse metallo-β-lactamase family

open access: yesCommunications Biology, 2021
The structure of Igni18, ancient enzyme from the Crenarchaean species Ignicoccus hospitalis, is solved and characterized by Pérez-García, Chow and colleagues.
Pablo Perez-Garcia   +12 more
doaj   +1 more source

Detection of Beta-Lactamases (ESBL and MBL) Producing Gram-Negative Pathogens in National Public Health Laboratory of Nepal

open access: yesInternational Journal of Microbiology, 2022
Background. Bacterial resistance to antibiotics has increased in recent years. Resistance to β-lactams in Gram-negative bacteria has been reported to be associated with extended spectrum beta-lactamases and metallo-beta-lactamases.
Anjana Shrestha   +4 more
doaj   +1 more source

Analysis of Class 1 Integrons and Antibiotic Resistance Genes in Pseudomonas aeruginosa Strains from Benin City, Nigeria

open access: yesJournal of Applied Sciences and Environmental Management, 2020
The presence of integrons and antibiotic resistance genes in the genome of Pseudomonas aeruginosa pose a serious problem in the treatment and control of infections caused by this pathogen in hospitals.
B.O. Isichei-Ukah, O.I. Enabulele
doaj   +1 more source

Structural basis of metallo-β-lactamase, serine-β-lactamase and penicillin-binding protein inhibition by cyclic boronates

open access: yesNature Communications, 2016
Bacterial beta-lactamases are responsible for resistance to beta-lactams, the most important family of antibiotics. Here, the authors reveal cyclic boronate inhibitors that are active against both serine- and metallo-beta-lactamases and represent a ...
Jürgen Brem   +9 more
doaj   +1 more source

Ventilator-associated pneumonia in a tertiary care hospital in India: role of multi-drug resistant pathogens

open access: yesJournal of Infection in Developing Countries, 2010
Background: Ventilator-Associated Pneumonia (VAP) is the most frequent intensive-care-unit (ICU)-acquired infection. The aetiology of VAP varies with different patient populations and types of ICUs.
Noyal Mariya Joseph   +5 more
doaj   +1 more source

Antibacterial potential of neem (Azadirachta indica) against uropathogens producing beta-lactamase enzymes: A clue to future antibacterial agent?

open access: yesBiomedical and Biotechnology Research Journal, 2020
Background: Emergence of drug resistance in Gram-negative bacilli due to production of extended-spectrum beta-lactamases (ESBL), metallo-beta-lactamases (MBL), and AmpC beta-lactamase is very common nowadays; therefore, we are left with less choice for ...
Sameer Singh Faujdar   +2 more
doaj   +1 more source

Restoring Meropenem Activity Against VIM-1-Producing Klebsiella pneumoniae Through Zinc-Binding Ligands. [PDF]

open access: yesChembiochem
Approved zinc‐binding drugs and newly synthesized HisPyr ligands were evaluated as adjuvants to meropenem against metallo‐β‐lactamase‐producing Klebsiella pneumoniae. Chlorpropamide and D‐penicillamine restored meropenem activity against the VIM‐1‐producing strain, while computational analyses supported interactions with the enzyme's binuclear zinc ...
Ragusa C   +6 more
europepmc   +2 more sources

Evolution of metallo-beta-lactamases in focus of the antibiotic resistance problem

open access: yesВісник Харківського Національного Університету Імені В.Н. Каразіна: Серія Біологія
The article considers the place of metallo-beta-lactamases among the mechanisms of antibiotic resistance. These enzymes have important differences from serine beta-lactamases, which affect the mechanism of their catalytic activity, inhibition, rate of ...
V.B. Moskalov, I.V. Kadenko, A.M. Mukhin
doaj   +1 more source

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