SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Bester LA) "

Search: WFRF:(Bester LA)

  • Result 1-9 of 9
Sort/group result
   
EnumerationReferenceCoverFind
1.
  •  
2.
  •  
3.
  •  
4.
  •  
5.
  • El-taliawy, H., et al. (author)
  • Ozonation efficiency in removing organic micro pollutants from wastewater with respect to hydraulic loading rates and different wastewaters
  • 2017
  • In: Chemical Engineering Journal. - : Elsevier BV. - 1385-8947. ; 325, s. 310-321
  • Journal article (peer-reviewed)abstract
    • Organic micro pollutants can be removed from water by ozonation. In this article we studied the performance of ozonation under real life conditions and compared results of the same ozonation pilot plant installed at different wastewater treatment plants (WWTPs) thus operating with different waters. The comparability of the removal and reaction rate constants from one waste water treatment plant were low in respect to reaction rate, removal as well as to response to the specific ozone dose. Neither pH-value nor residual nitrite concentrations were the driving force considering these differences. Further tests with different loadings were conducted at the same WWTP under different weather conditions. For the different hydraulic loading of the biological plant, the ozonation was running with rather similar removal rates concerning the same specific (TOC normalized) ozone dose. The compounds that were removed quantitatively under dry weather were still removed well with three times dry weather flow. Using a dataset from one WWTP to optimize operation in another one is thus questionable.
  •  
6.
  •  
7.
  • Reddy, N, et al. (author)
  • Neutralizing Carbapenem Resistance by Co-Administering Meropenem with Novel β-Lactam-Metallo-β-Lactamase Inhibitors
  • 2023
  • In: Antibiotics (Basel, Switzerland). - : MDPI AG. - 2079-6382. ; 12:4
  • Journal article (peer-reviewed)abstract
    • 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 resistance. Currently, serine β-lactamase inhibitors (SBLIs) are in therapeutic use. However, an urgent global need for clinical metallo-β-lactamase inhibitors (MBLIs) has become dire. To address this problem, this study evaluated BP2, a novel beta-lactam-derived β-lactamase inhibitor, co-administered with meropenem. According to the antimicrobial susceptibility results, BP2 potentiates the synergistic activity of meropenem to a minimum inhibitory concentration (MIC) of ≤1 mg/L. In addition, BP2 is bactericidal over 24 h and safe to administer at the selected concentrations. Enzyme inhibition kinetics showed that BP2 had an apparent inhibitory constant (Kiapp) of 35.3 µM and 30.9 µM against New Delhi Metallo-β-lactamase (NDM-1) and Verona Integron-encoded Metallo-β-lactamase (VIM-2), respectively. BP2 did not interact with glyoxylase II enzyme up to 500 µM, indicating specific (MBL) binding. In a murine infection model, BP2 co-administered with meropenem was efficacious, observed by the >3 log10 reduction in K. pneumoniae NDM cfu/thigh. Given the promising pre-clinical results, BP2 is a suitable candidate for further research and development as an (MBLI).
  •  
8.
  • Reddy, N, et al. (author)
  • Neutralizing Carbapenem Resistance by Co-Administering Meropenem with Novel β-Lactam-Metallo-β-Lactamase Inhibitors
  • 2023
  • In: Antibiotics (Basel, Switzerland). - : MDPI AG. - 2079-6382. ; 12:4
  • Journal article (peer-reviewed)abstract
    • 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 resistance. Currently, serine β-lactamase inhibitors (SBLIs) are in therapeutic use. However, an urgent global need for clinical metallo-β-lactamase inhibitors (MBLIs) has become dire. To address this problem, this study evaluated BP2, a novel beta-lactam-derived β-lactamase inhibitor, co-administered with meropenem. According to the antimicrobial susceptibility results, BP2 potentiates the synergistic activity of meropenem to a minimum inhibitory concentration (MIC) of ≤1 mg/L. In addition, BP2 is bactericidal over 24 h and safe to administer at the selected concentrations. Enzyme inhibition kinetics showed that BP2 had an apparent inhibitory constant (Kiapp) of 35.3 µM and 30.9 µM against New Delhi Metallo-β-lactamase (NDM-1) and Verona Integron-encoded Metallo-β-lactamase (VIM-2), respectively. BP2 did not interact with glyoxylase II enzyme up to 500 µM, indicating specific (MBL) binding. In a murine infection model, BP2 co-administered with meropenem was efficacious, observed by the >3 log10 reduction in K. pneumoniae NDM cfu/thigh. Given the promising pre-clinical results, BP2 is a suitable candidate for further research and development as an (MBLI).
  •  
9.
  • Somboro, AM, et al. (author)
  • NOTA: a potent metallo-β-lactamase inhibitor
  • 2015
  • In: The Journal of antimicrobial chemotherapy. - : Oxford University Press (OUP). - 1460-2091 .- 0305-7453. ; 70:5, s. 1594-1596
  • Journal article (other academic/artistic)
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-9 of 9

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view