Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutants.
Lukasz Skora,Luis Fonseca-Ornelas,Romina V. Hofele,Dietmar Riedel,Karin Giller,Jens O. Watzlawik,Walter J. Schulz-Schaeffer,Henning Urlaub,Henning Urlaub,Stefan Becker,Markus Zweckstetter,Markus Zweckstetter +11 more
TLDR
It is demonstrated that stop mutants of the human prion protein have a conserved amyloid core and the 129 residue is deeply buried in the amyloids core structure, and its mutation strongly impacts aggregation.About:
This article is published in Journal of Biological Chemistry.The article was published on 2013-02-01 and is currently open access. It has received 16 citations till now.read more
Citations
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Applications of hydrogen/deuterium exchange MS from 2012 to 2014.
TL;DR: This Review catalogs applications of HDX MS that have appeared in the literature during the 30 months from January 2012 to June 2014 as penetration of the method into nonacademic sectors where confidentiality is necessary is also at an all-time high.
Journal ArticleDOI
Analysis of protein aggregation in neurodegenerative disease.
TL;DR: Analytical methods for studying protein aggregation in neurodegenerative diseases are important for mapping pathophysiological events and ultimately for the development of new therapies and better diagnostic tools.
Journal ArticleDOI
N-terminal Prion Protein Peptides (PrP(120–144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent Pathways
TL;DR: Light is shed on the amyloid core structures underlying prion strains and how I138M, I139M, and S143N affect prion protein aggregation kinetics.
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Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy.
Darryl Aucoin,Yongjie Xia,Theint Theint,Philippe S. Nadaud,Krystyna Surewicz,Witold K. Surewicz,Christopher P. Jaroniec +6 more
TL;DR: The protein-solvent interfaces in human PrP23-144 amyloid fibrils generated from recombinant 13C,15N-enriched protein and incubated in aqueous solution containing paramagnetic Cu(II)-EDTA are determined by measuring residue-specific 15N longitudinal paramagnetic relaxation enhancements using two-dimensional magic-angle spinning solid-state NMR spectroscopy.
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Cryo-EM structures of prion protein filaments from Gerstmann–Sträussler–Scheinker disease
Grace I. Hallinan,Kadir A. Ozcan,Md. Rejaul Hoq,Laura Cracco,Frank S. Vago,Sakshibeedu R. Bharath,Daoyi Li,Max H. Jacobsen,Emma Doud,Amber L. Mosley,Anllely Fernandez,Holly J. Garringer,Wen Jiang,Bernardino Ghetti,R. Vidal +14 more
TL;DR: In this paper , the structure of PrP amyloid filaments was determined using cryogenic electron microscopy (cryo-EM) from the brain of two symptomatic prion protein F198S mutation carriers, where the filaments are composed of dimeric, trimeric and tetrameric left-handed protofilaments with their protomers sharing a common protein fold.
References
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