The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: Evidence from solid state NMR
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Summary
Measurements of solid state nuclear magnetic measurements on amyloid fibrils formed by the full-length prion protein PrP indicate that β-sheets in these fibrils have an in-register parallel structure, as previously observed in amyloid fibrils associated with Alzheimer’s disease and type 2 diabetes and in yeast prion fibrils.
- Type
- article
- Published
- 2010-11-09
- Cited by
- 126
- References
- 0
- Access
- Open access
- OpenAlex
- https://openalex.org/W1964944526
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:206839035
Keywords
Solid-state nuclear magnetic resonance, Crystallography, Fibril, Chemistry, Nuclear magnetic resonance spectroscopy
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Cited by
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- Solid-state NMR techniques for the structural determination of amyloid fibrils.
- Amyloid Polymorphism: Structural Basis and Neurobiological Relevance
- Critical Significance of the Region between Helix 1 and 2 for Efficient Dominant-Negative Inhibition by Conversion-Incompetent Prion Protein
- A general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymers
- The role of RNA in mammalian prion protein conversion
- Synthetic prions and other human neurodegenerative proteinopathies.
- PrP assemblies
- Interactions between non-identical prion proteins.
- Decrypting Prion Protein Conversion into a β-Rich Conformer by Molecular Dynamics
- Perturbations in inter-domain associations may trigger the onset of pathogenic transformations in PrP(C): insights from atomistic simulations.
- Structural Polymorphism in Amyloids
- Structural Insights into Functional and Pathological Amyloid*
- Depletion of Water Molecules Near the End Stage of Steric Zipper Formation
- Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
- Helium-cooling and -spinning dynamic nuclear polarization for sensitivity-enhanced solid-state NMR at 14 T and 30 K.
- Parallel β-sheet vibrational couplings revealed by 2D IR spectroscopy of an isotopically labeled macrocycle: Quantitative benchmark for the interpretation of amyloid and protein infrared spectra
- Structural Conversion Rate Changes of Recombinant Bovine Prion by Designed Synthetic Peptides
- Helices 2 and 3 are the initiation sites in the PrPC → PrPSC transition
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