Results 11 to 20 of about 1,471,936 (197)

Neutralizing Carbapenem Resistance by Co-Administering Meropenem with Novel β-Lactam-Metallo-β-Lactamase Inhibitors

Antibiotics, 2023
Virulent Enterobacterale strains expressing serine and metallo-β-lactamases (MBL) genes have emerged responsible for conferring resistance to hard-to-treat infectious diseases. One strategy that exists is to develop β-lactamase inhibitors to counter this
Nakita Reddy, Letisha Girdhari, Mbongeni Shungube, Arnoldus C. Gouws, Byron K. Peters, Kamal K. Rajbongshi, Sooraj Baijnath, Sipho Mdanda, Thandokuhle Ntombela, Thilona Arumugam, Linda A. Bester, Sanil D. Singh, Anil Chuturgoon, Per I. Arvidsson, Glenn E. M Maguire, Hendrik G. Kruger, Thavendran Govender, Tricia Naicker   +17 more
doaj   +2 more sources

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   +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

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

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

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

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

Antibiotics, 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, Sandrine Bernabeu, Laurent Dortet   +2 more
doaj   +1 more source

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

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

PLoS 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, Chi-Chuan Wang, Chia-Hui Lin, Wang-Huei Sheng, Shan-Chwen Chang   +4 more
doaj   +1 more source