Results 11 to 20 of about 31,219 (256)

Old and New Beta-Lactamase Inhibitors: Molecular Structure, Mechanism of Action, and Clinical Use

Antibiotics, 2021
The β-lactams have a central place in the antibacterial armamentarium, but the increasing resistance to these drugs, especially among Gram-negative bacteria, is becoming one of the major threats to public health worldwide.
Davide Carcione, Claudia Siracusa, Adela Sulejmani, Valerio Leoni, Jari Intra   +4 more
doaj   +3 more sources

Use of Novel Antibiograms to Determine the Need for Earlier Susceptibility Testing and Administration for New β-Lactam/β-Lactamase Inhibitors in the United States [PDF]

Antibiotics, 2022
Antimicrobial resistance is a global public health threat, and gram-negative bacteria, such as Enterobacterales and Pseudomonas aeruginosa, are particularly problematic with difficult-to-treat resistance phenotypes.
Kenneth P. Klinker, Levita K. Hidayat, Eric Wenzler, Joan-Miquel Balada-Llasat, Mary Motyl, C. Andrew DeRyke, Karri A. Bauer   +6 more
doaj   +2 more sources

P50 Bismuth-based β-lactamase inhibitors to combat antibiotic resistance [PDF]

JAC Antimicrob Resist
A. E. Ajiboye, Jody Winter, Sophie L. Benjamin   +2 more
europepmc   +3 more sources

Molecular Docking Approach of Viscosin as Antibacterial for Methicillin-resistant Staphylococcus Aureus Via β-Lactamase Inhibitor Mechanism

Clinical and Research Journal in Internal Medicine, 2021
Background: β-lactamase is an enzyme that plays a role in the occurrence of antibiotic resistance against Methicillin-resistant Staphylococcus aureus (MRSA) bacteria. Viscosin is a lipopeptide biosurfactant produced by the Pseudomonas group bacteria.
Mokhamad Fahmi Rizki Syaban, Nabila Erina Erwan, Muhammad Rafif Raihan Syamsuddin, Fatimah Az Zahra, Faradilah Lukmana Sabila   +4 more
openaire   +1 more source

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

Microorganisms, 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, Trae Hillyer, Aylin S. Crugnale, Andrew Fulk, Caitlyn A. Thomas, Michael W. Crowder, Matthew A. Smith, Woo Shik Shin   +7 more
doaj   +1 more source

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

FEMS 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]

FEMS 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]

FEMS 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, Janice, D Thomas, Jeffrey H, Toney   +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]

FEMS 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, J, Péduzzi, M M, Caniça, G, Paul, P, Névot, M, Barthélémy, R, Labia   +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]

FEMS 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, Claudine, Blin, Rajagopal, Krishnamoorthy, Bertrand, Picard, El Bachir, Chaibi, Martine, Fouchereau-Péron, Roger, Labia   +6 more
openaire   +2 more sources