Results 11 to 20 of about 14,756 (172)

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

Outer membrane permeability of β-lactamase inhibitors inPseudomonas aeruginosa [PDF]

open access: yesFEMS Microbiology Letters, 1995
Evaluation of four beta-lactamase inhibitors in terms of their outer membrane permeability in Pseudomonas aeruginosa revealed that sulbactam and tazobactam diffused most efficiently and equally well. That of BRL42715 appeared to be a factor of ten lower than that of the above two, but it showed the strongest beta-lactamase inhibitory activity.
S, Satake, T, Nakae
openaire   +2 more sources

Penetration of β-lactamase inhibitors into the periplasm of Gram-negative bacteria [PDF]

open access: yesFEMS Microbiology Letters, 1999
The effectiveness of a beta-lactamase inhibitor/beta-lactam combination against Gram-negative pathogens depends on many interplaying factors, one of which is the penetration of the inhibitor across the outer membrane. In this work we have measured the relative penetrations of clavulanic acid, sulbactam, tazobactam and BRL 42715 into two strains of ...
Farmer TH, Degnan BA, Payne DJ
openaire   +3 more sources

Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]

open access: yesFEMS Microbiology Letters, 2005
IMP-1 metallo-beta-lactamase is a zinc metalloenzyme that confers antibiotic resistance to bacteria through the hydrolysis of beta-lactam antibiotics. Pathogens that express the enzyme show reduced susceptibility to carbapenems, such as meropenem and imipenem.
Joseph G, Moloughney   +2 more
openaire   +2 more sources

Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors [PDF]

open access: yesFEMS Microbiology Letters, 1994
The clinical isolate Escherichia coli PEY was highly resistant to amoxycillin, ticarcillin and piperacillin associated to beta-lactamase inhibitors such as clavulanic acid, sulbactam, tazobactam and brobactam but susceptible to cephalosporins, aztreonam and imipenem.
T, Brun   +6 more
openaire   +2 more sources

Substitution of Met-69 by Ala or Gly in TEM-1 β-lactamase confer an increased susceptibility to clavulanic acid and other inhibitors [PDF]

open access: yesFEMS Microbiology Letters, 2002
In some inhibitor-resistant TEM-derived beta-lactamases, Met-69 is substituted by Leu, Ile or Val. Residue 69 is located in a region of strong structural constraints, at the beginning of H2 alpha-helix, and in the vicinity of B3 and B4 beta-strands.
Stéphanie, Madec   +6 more
openaire   +2 more sources

Fluoroquinolones versus β-Lactam/β-Lactamase Inhibitors in Outpatients with Chronic Obstructive Pulmonary Disease and Pneumonia: A Nationwide Population-Based Study. [PDF]

open access: yesPLoS ONE, 2015
Studies on the association between antibiotic treatment and outcomes in outpatients with chronic obstructive pulmonary disease (COPD) and pneumonia are scarce.
Kuan-Yin Lin   +4 more
doaj   +1 more source

In Vitro Susceptibility of Aztreonam-Vaborbactam, Aztreonam-Relebactam and Aztreonam-Avibactam Associations against Metallo-β-Lactamase-Producing Gram-Negative Bacteria

open access: yesAntibiotics, 2023
Background: Despite the availability of new options (ceftazidime-avibactam, imipenem-relebactam, meropenem-vaborbactam and cefiderocol), it is still very difficult to treat infections caused by metallo-β-lactamase (MBLs)-producers resistant to aztreonam.
Cécile Emeraud   +2 more
doaj   +1 more source

Substitution of Arg-244 by Cys or Ser in SHV-1 and SHV-5 β-lactamases confers resistance to mechanism-based inhibitors and reduces catalytic efficiency of the enzymes [PDF]

open access: yesFEMS Microbiology Letters, 1998
The conserved residue Arg-244 was substituted by the smaller uncharged amino acids Cys and Ser in SHV-1 and SHV-5 beta-lactamases by a PCR-based site-specific mutagenesis procedure. The mutant beta-lactamases displayed decreased susceptibility to clavulanate and, to a lesser extent, to tazobactam and sulbactam.
Giakkoupi, P   +3 more
openaire   +3 more sources

Discovery of beta-lactamase CMY-10 inhibitors for combination therapy against multi-drug resistant Enterobacteriaceae.

open access: yesPLoS ONE, 2021
β-lactam antibiotics are the most widely used antimicrobial agents since the discovery of benzylpenicillin in the 1920s. Unfortunately, these life-saving antibiotics are vulnerable to inactivation by continuously evolving β-lactamase enzymes that are ...
Nousheen Parvaiz   +4 more
doaj   +1 more source

Home - About - Disclaimer - Privacy