Protein-lipid interactions of human dihydroorotate dehydrogenase and three mutants associated with Miller syndrome
Author:
Affiliation:
1. Department of Biology & Lund Protein Production Platform, Lund University, Lund, Sweden
2. Department of Chemistry, Division of Physical Chemistry, Lund University, Lund, Sweden
3. European Spallation Source ERIC, Lund, Sweden
Funder
Royal Physiographic Society of Lund
Erik Philip-Sörensen Foundation
Jörgen Lindström Foundation
Publisher
Informa UK Limited
Subject
Genetics,Molecular Medicine,Biochemistry,General Medicine
Link
https://www.tandfonline.com/doi/pdf/10.1080/15257770.2022.2039393
Reference27 articles.
1. Preparation of human dihydroorotate dehydrogenase for interaction studies with lipid bilayers
2. The pathway to pyrimidines: The essential focus on dihydroorotate dehydrogenase, the mitochondrial enzyme coupled to the respiratory chain
3. Requirements for the mitochondrial import and localization of dihydroorotate dehydrogenase
4. Miller (Genee-Wiedemann) syndrome represents a clinically and biochemically distinct subgroup of postaxial acrofacial dysostosis associated with partial deficiency of DHODH
5. Protein instability and functional defects caused by mutations of dihydro-orotate dehydrogenase in Miller syndrome patients
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