Blar i forfatter Artikler, rapporter og annet (kjemi) "Thomassen, Ane Molden"

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    • Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436 

      Lund, Bjarte Aarmo; Thomassen, Ane Molden; Carlsen, Trine Josefine Warg; Leiros, Hanna-Kirsti Schrøder (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-31)
      The crystal structure of the class D β-lactamase OXA-436 was solved to a resolution of 1.80 Å. Higher catalytic rates were found at higher temperatures for the clinically important antibiotic imipenem, indicating better adaptation of OXA-436 to its mesophilic host than OXA-48, which is believed to originate from an environmental source. Furthermore, based on the most populated conformations during ...

    • OXA-48-Mediated Ceftazidime-Avibactam Resistance Is Associated with Evolutionary Trade-Offs 

      Fröhlich, Christopher; Sørum, Vidar; Thomassen, Ane Molden; Johnsen, Pål Jarle; Samuelsen, Ørjan (Journal article; Tidsskriftartikkel; Peer reviewed, 2019-03-27)
      Infections due to carbapenemase-producing Gram-negative pathogens are associated with limited treatment options and consequently lead to increased mortality and morbidity. In response, combinations of existing β-lactams and novel β-lactamase inhibitors, such as ceftazidime-avibactam (CAZ-AVI), have been developed as alternative treatment options. To understand the development of resistance and ...

    • Structural insights into the enhanced carbapenemase efficiency of OXA-655 compared to OXA-10 

      Leiros, Hanna-Kirsti S.; Thomassen, Ane Molden; Samuelsen, Ørjan; Flach, Carl-Fredrik; Kotsakis, Stathis D.; Larsson, Joakim (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-07-19)
      Carbapenemases are the main cause of carbapenem resistance in Gram‐negative bacteria. How β‐lactamases with weak carbapenemase activity, such as the OXA‐10‐type class D β‐lactamases, contribute to anti‐bacterial drug resistance is unclear. OXA‐655 is a T26M and V117L OXA‐10 variant, recently identified from hospital wastewater. Despite exhibiting stronger carbapenemase activity towards ertapenem ...

    • Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis 

      Lund, Bjarte Aarmo; Thomassen, Ane Molden; Carlsen, Trine Josefine Olsen; Leiros, Hanna-Kirsti S. (Journal article; Tidsskriftartikkel; Peer reviewed, 2017)
      The first crystal structures of the class D β-lactamases OXA-181 and OXA-245 were determined to 2.05 and 2.20 Å resolution, respectively; in addition, the structure of a new crystal form of OXA-163 was resolved to 2.07 Å resolution. All of these enzymes are OXA-48-like and have been isolated from different clinical Klebsiella pneumoniae strains and also from other human pathogens such as Pseudomonas ...