D
Deborah A. Berthold
Researcher at University of Illinois at Urbana–Champaign
Publications - 27
Citations - 3980
Deborah A. Berthold is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Alternative oxidase & Solid-state nuclear magnetic resonance. The author has an hindex of 18, co-authored 27 publications receiving 3723 citations. Previous affiliations of Deborah A. Berthold include Duke University & Stockholm University.
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Journal ArticleDOI
A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes
TL;DR: The properties of oxygenevolving PS II preparations obtained by detergent resolution of chloroplast thylakoid membranes are reported.
Journal ArticleDOI
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
Marcus D. Tuttle,Marcus D. Tuttle,Gemma Comellas,Andrew J. Nieuwkoop,Andrew J. Nieuwkoop,Dustin J. Covell,Deborah A. Berthold,Kathryn D. Kloepper,Kathryn D. Kloepper,Joseph M. Courtney,Jae K Kim,Alexander M. Barclay,Amy Kendall,William Wan,William Wan,Gerald Stubbs,Charles D. Schwieters,Virginia M.-Y. Lee,Jimin George,Chad M. Rienstra +19 more
TL;DR: A high-resolution structure of an α-synuclein fibril, in a form that induces robust pathology in primary neuronal culture, determined by solid-state NMR spectroscopy and validated by EM and X-ray fiber diffraction is presented.
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New insight into the structure and function of the alternative oxidase.
TL;DR: The cloning of the Arabidopsis thaliana IMMUTANS (Im) gene, which encodes a plastid enzyme distantly related to the mitochondrial alternative oxidases, has now narrowed the range of possible ligands to the diiron center of the alternative oxidase, and the Im protein sequence suggests a minor modification to the recent model of the active site.
Journal ArticleDOI
Membrane-bound diiron carboxylate proteins.
Deborah A. Berthold,Pål Stenmark +1 more
TL;DR: Four proteins have been identified recently as diiron carboxylate proteins on the basis of conservation of six amino acids constituting an iron-binding motif, indicating that each is membrane bound, although homology modeling rules out a transmembrane mode of binding.
Journal ArticleDOI
A new member of the family of di-iron carboxylate proteins. Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis.
Pål Stenmark,Jacob Grünler,Jonas Mattsson,Pavel J. Sindelar,Pär Nordlund,Deborah A. Berthold +5 more
TL;DR: This work cloned COQ7 from Pseudomonas aeruginosa and Thiobacillus ferrooxidans and shows that indeed this gene complements an Escherichia coli mutant that lacks an unrelated 5-demethoxyubiquinone hydroxylase, and proposes a structural model for Coq7 as an interfacial integral membrane protein.