Sofie Nørager
University of Copenhagen
8 Papers
22 Citations
Sofie Nørager is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Dihydroorotate dehydrogenase & Lactococcus lactis. The author has an hindex of 6, co-authored 7 publications.
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Papers
Structure of Dihydroorotate Dehydrogenase B: Electron Transfer between Two Flavin Groups Bridged by an Iron-Sulphur Cluster
TL;DR: In this paper, the crystal structures of the dihydroorotate dehydrogenase (DHOD) and its product complex have been determined for DHODB and its products.
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A walk in the PARC: developing and implementing 21st century chemical risk assessment in Europe
Philip Marx-Stoelting,G. Rivière,Mirjam Luijten,K. Aiello-Holden,N. Bandow,K. Baken,Ana Cañas,Argelia Castaño,Sã©bastien Denys,Clémence Fillol,Matthias Herzler,Ivo Iavicoli,Spyros Karakitsios,Jana Klánová,Marike Kolossa-Gehring,Aglaia Koutsodimou,Joana Lobo Vicente,I. Lynch,Sónia Namorado,Sofie Nørager,A. Pittman,Stefanie Rotter,Denis Sarigiannis,M. J. Silva,Jan Theunis,Tewes Tralau,Monica Uhl,Jacob D. van Klaveren,Lina Wendt-Rasch,Emma Westerholm,Christophe Rousselle,P. Sanders +31 more
TL;DR: The European Partnership for the Assessment of Risks from Chemicals (PARC) as mentioned in this paper has been designed to address various challenges associated with innovating chemical risk assessment and its overall goal is to consolidate and strengthen the European research and innovation capacity for chemical risk assess to protect human health and the environment.
Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
Sofie Nørager,Susan Arent,Olof Björnberg,M. Ottosen,Leila Lo Leggio,Kaj Frank Jensen,Sine Larsen +6 more
TL;DR: Based on the DHODA structure, seven residues that are highly conserved between both main classes of DHODs as well as three residues representing surface charges close to the active site for site-directed mutagenesis are selected.
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The dimeric dihydroorotate dehydrogenase A from Lactococcus lactis dissociates reversibly into inactive monomers
TL;DR: Wild‐type dihydroorotate dehydrogenase A was similarly found to dissociate into inactive monomers, but with a KD for dissociation equal to 0.12 μM, implying that the dimeric state is necessary for activity of the enzyme.
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Crystallization and preliminary X-ray studies of membrane-associated Escherichia coli dihydroorotate dehydrogenase.
TL;DR: Two major families of DHODs have now been identified based on their amino-acid sequence similarities, and structures are only known of enzymes belonging to family 1 and family 2.
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