Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy
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Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicityStructural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR StudyFibrils of Truncated Pyroglutamyl-Modified Aβ Peptide Exhibit a Similar Structure as Wildtype Mature Aβ FibrilsStudying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to BiomoleculesA general Monte Carlo/simulated annealing algorithm for resonance assignment in NMR of uniformly labeled biopolymersSelectively dispersed isotope labeling for protein structure determination by magic angle spinning NMR.Progress towards structural understanding of infectious sheep PrP-amyloid.β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases.Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Characterization of prion-like conformational changes of the neuronal isoform of Aplysia CPEBA Monte Carlo/simulated annealing algorithm for sequential resonance assignment in solid state NMR of uniformly labeled proteins with magic-angle spinning.The nuclear magnetic resonance relaxation data analysis in solids: general R1/R1(ρ) equations and the model-free approach.Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.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 nuclear magnetic resonance.Physical and structural basis for polymorphism in amyloid fibrilsNmrglue: an open source Python package for the analysis of multidimensional NMR data.Cyclin-dependent kinase 5 phosphorylation of familial prion protein mutants exacerbates conversion into amyloid structure.Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites.Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopyStructural studies of truncated forms of the prion protein PrP.Solid-state NMR studies of amyloid fibril structureSegmental polymorphism in a functional amyloid.Amyloid polymorphism: structural basis and neurobiological relevance.Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studiesStructural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kineticsResolving nitrogen-15 and proton chemical shifts for mobile segments of elastin with two-dimensional NMR spectroscopy.High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopyQuantifying conformational dynamics using solid-state R₁ρ experiments.Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Amplitudes and time scales of picosecond-to-microsecond motion in proteins studied by solid-state NMR: a critical evaluation of experimental approaches and application to crystalline ubiquitin.Small-molecule theranostic probes: a promising future in neurodegenerative diseases.Histone H3 and H4 N-terminal tails in nucleosome arrays at cellular concentrations probed by magic angle spinning NMR spectroscopyAmyloid fibrils from the N-terminal prion protein fragment are infectious.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Secondary structure in the core of amyloid fibrils formed from human β₂m and its truncated variant ΔN6.
P2860
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P2860
Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Conformational flexibility of ...... agnetic resonance spectroscopy
@ast
Conformational flexibility of ...... agnetic resonance spectroscopy
@en
type
label
Conformational flexibility of ...... agnetic resonance spectroscopy
@ast
Conformational flexibility of ...... agnetic resonance spectroscopy
@en
prefLabel
Conformational flexibility of ...... agnetic resonance spectroscopy
@ast
Conformational flexibility of ...... agnetic resonance spectroscopy
@en
P2093
P2860
P356
P1476
Conformational flexibility of ...... agnetic resonance spectroscopy
@en
P2093
Jonathan J Helmus
Krystyna Surewicz
Witold K Surewicz
P2860
P304
P356
10.1021/JA909827V
P407
P577
2010-02-01T00:00:00Z