Results 11 to 20 of about 58,396 (229)

Structure, Genetics and Worldwide Spread of New Delhi Metallo-β-lactamase (NDM): a threat to public health [PDF]

open access: yesBMC Microbiology, 2017
BackgroundThe emergence of carbapenemase producing bacteria, especially New Delhi metallo-β-lactamase (NDM-1) and its variants, worldwide, has raised amajor public health concern.
Asad U. Khan, Lubna Maryam, R. Zarrilli
semanticscholar   +3 more sources

In vitro antimicrobial effects of aztreonam, colistin, and the 3-drug combination of aztreonam, ceftazidime and amikacin on metallo-β-lactamase-producing Pseudomonas aeruginosa [PDF]

open access: yesBMC Infectious Diseases, 2009
Background There are limited choice of antimicrobial agents to treat infection with metallo-β-lactamase-producing Pseudomonas aeruginosa. We evaluate the antimicrobial effects of aztreonam alone, colistin alone and the 3-drug combination of aztreonam ...
Oie Shigeharu   +4 more
doaj   +2 more sources

Membrane-anchoring stabilizes and favors secretion of New Delhi Metallo-β-lactamase [PDF]

open access: yesNature Chemical Biology, 2016
Carbapenems, “last resort” β-lactam antibiotics, are inactivated by zinc-dependent metallo-β-lactamases (MBLs). The host innate immune response withholds nutrient metal ions from microbial pathogens by releasing metal-chelating proteins such as ...
L. González   +5 more
semanticscholar   +5 more sources

Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution [PDF]

open access: yesAntibiotics, 2014
The production of β-lactamase enzymes is one of the most distributed resistance mechanisms towards β-lactam antibiotics. Metallo-β-lactamases constitute a worrisome group of these kinds of enzymes, since they present a broad spectrum profile, being able
María-Rocío Meini   +2 more
doaj   +5 more sources

Metallo-β-lactamase-mediated antimicrobial resistance and progress in inhibitor discovery.

open access: yesTrends in Microbiology, 2023
Resistance to β-lactam antibiotics is rapidly growing, substantially due to the spread of serine-β-lactamases (SBLs) and metallo-β-lactamases (MBLs), which efficiently catalyse β-lactam hydrolysis.
Yongqiang Yang   +5 more
semanticscholar   +1 more source

Taxifolin as a Metallo-β-Lactamase Inhibitor in Combination with Augmentin against Verona Imipenemase 2 Expressing Pseudomonas aeruginosa

open access: yesMicroorganisms, 2023
Among the various mechanisms that bacteria use to develop antibiotic resistance, the multiple expression of β-lactamases is particularly problematic, threatening public health and increasing patient mortality rates. Even if a combination therapy—in which
Bogdan M. Benin   +7 more
doaj   +1 more source

Therapeutic Options for Metallo-β-Lactamase-Producing Enterobacterales

open access: yesInfection and Drug Resistance, 2021
The spread of metallo-β-lactamase (MBL)-producing Enterobacterales worldwide without the simultaneous increase in active antibiotics makes these organisms an urgent public health threat.
X. Tan   +8 more
semanticscholar   +1 more source

Novel metallo β-lactamase mediated by aShigella flexneriplasmid [PDF]

open access: yesFEMS Microbiology Letters, 1998
Novel carbapenem-hydrolyzing beta-lactamase (newly named MET-1) encoded on a transferable plasmid pMS390 from Shigella flexneri JS19622 was purified. The molecular weight was 28,000 by SDS-PAGE and the isoelectric point was higher than 9.3. This beta-lactamase favorably hydrolyzed classical cephalosporins and oxyimino-cephalosporins rather than ...
K, O'Hara   +4 more
openaire   +2 more sources

Identification, Speciation and Antibiogram along with Detection of Metallo Beta-lactamase Production in Acinetobacter Isolated from Clinical Samples in a Tertiary Care Hospital

open access: yesJournal of Pure and Applied Microbiology, 2021
Acinetobacter species are gram negative non fermenters, which are important nosocomial pathogens involved in various outbreaks in hospitals due to widespread resistance to majority antibiotics.
N Ashwin Chitrabanu, Shrikara Mallya
doaj   +1 more source

Structural basis of metallo-β-lactamase resistance to taniborbactam

open access: yesAntimicrobial Agents and Chemotherapy, 2023
The design of inhibitors against metallo-β-lactamases (MBLs), the largest family of carbapenemases, has been a strategic goal in designing novel antimicrobial therapies.
Salvador I. Drusin   +5 more
semanticscholar   +1 more source

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