Blar i forfatter "Courtade, Gaston"

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    • 1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10A from Jonesia denitrificans 

      Christensen, Idd Andrea; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-11-19)
      The lytic polysaccharide monooxygenase <i>Jd</i>LPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated <i>Jd</i>LPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 kDa. <i>Jd</i>LPMO10A is a copper-dependent oxidative enzyme that depolymerizes chitin by hydroxylating the C1 carbon in the glycosidic ...

    • Class IV lasso peptides synergistically induce proliferation of cancer cells and sensitize them to doxorubicin 

      Felipe Guerrero-Garzón, Jaime; Madland, Eva; Zehl, Martin; Singh, Madhurendra; Rezaei, Shiva; Aachmann, Finn Lillelund; Courtade, Gaston; Urban, Ernst; Rückert, Christian; Busche, Tobias; Kalinowski, Jörn; Cao, Yan-Ru; Jiang, Yi; Jiang, Cheng-lin; Selivanova, Galina; Zotchev, Sergey (Journal article; Tidsskriftartikkel; Peer reviewed, 2020-11-10)
      Heterologous expression of a biosynthesis gene cluster from <i>Amycolatopsis</i> sp. resulted in the discovery of two unique class IV lasso peptides, felipeptins A1 and A2. A mixture of felipeptins stimulated proliferation of cancer cells, while having no such effect on the normal cells. Detailed investigation revealed, that pre-treatment of cancer cells with a mixture of felipeptins resulted in ...

    • Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus 

      Madland, Eva; Forsberg, Zarah; Wang, Yong; Lindorff-Larsen, Kresten; Niebisch, Axel; Modregger, Jan; Eijsink, Vincent; Aachmann, Finn Lillelund; Courtade, Gaston (Journal article; Tidsskriftartikkel; Peer reviewed, 2021-08-17)
      Among the extensive repertoire of carbohydrate-active enzymes, lytic polysaccharide monooxygenases (LPMOs) have a key role in recalcitrant biomass degradation. LPMOs are copper-dependent enzymes that catalyze oxidative cleavage of glycosidic bonds in polysaccharides such as cellulose and chitin. Several LPMOs contain carbohydrate-binding modules (CBMs) that are known to promote LPMO efficiency. ...