Blar i forfatter Artikler, rapporter og annet (kjemi) "Frøhlich, Christopher"

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    • Evolution of β-lactamase-mediated cefiderocol resistance 

      Frøhlich, Christopher; Sørum, Vidar; Tokuriki, Nobuhiko; Johnsen, Pål Jarle; Samuelsen, Ørjan (Journal article; Tidsskriftartikkel; Peer reviewed, 2022-07-11)
      Background: Cefiderocol is a novel siderophore β-lactam with improved hydrolytic stability toward β-lactamases, including carbapenemases, achieved by combining structural moieties of two clinically efficient cephalosporins, ceftazidime and cefepime. Consequently, cefiderocol represents a treatment alternative for infections caused by MDR Gram-negatives.<p> <p>Objectives: To study the role of ...

    • Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1 

      Frøhlich, Christopher; Sørum, Vidar; Huber, Sandra; Samuelsen, Ørjan; Berglund, Fanny; Kristiansson, Erik; Kotsakis, Stathis D.; Marathe, Nachiket P.; Larsson, Joakim; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-28)
      <i>Background</i> - MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure–activity ...

    • Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1 

      Frøhlich, Christopher; Sørum, Vidar; Huber, Sandra; Samuelsen, Ørjan; Berglund, Fanny; Kristiansson, Erik; Kotsakis, Stathis D.; Marathe, Nachiket; Larsson, DG Joakim; Leiros, Hanna-Kirsti Schrøder (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-05-28)
      Background: MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to b-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure–activity relationships ...

    • Structural studies of triazole inhibitors with promising inhibitor effects against antibiotic resistance metallo-β-lactamases 

      Muhammad, Zeeshan; Skagseth, Susann; Boomgaren, Marc; Akhter, Sundus; Frøhlich, Christopher; Ismael, Aya; Christopeit, Tony; Bayer, Annette; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-06-18)
      Metallo-β-lactamases (MBLs) are an emerging cause of bacterial antibiotic resistance by hydrolysing all classes of β-lactams except monobactams, and the MBLs are not inhibited by clinically available serine-β-lactamase inhibitors. Two of the most commonly encountered MBLs in clinical isolates worldwide – the New Delhi metallo-β-lactamase (NDM-1) and the Verona integron-encoded metallo-β-lactamase ...