Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy
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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesHistorical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue TargetingParallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.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.Amyloid polymorphism: structural basis and neurobiological relevance.Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.A Structural Model for a Self-Assembled Nanotube Provides Insight into Its Exciton Dynamics.Enhanced sensitivity by nonuniform sampling enables multidimensional MAS NMR spectroscopy of protein assemblies.High resolution structural characterization of Aβ42 amyloid fibrils by magic angle spinning NMR.3D DUMAS: simultaneous acquisition of three-dimensional magic angle spinning solid-state NMR experiments of proteinsStructural 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.Amyloid fibrils from the N-terminal prion protein fragment are infectious.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Higher order amyloid fibril structure by MAS NMR and DNP spectroscopy.Burial of the polymorphic residue 129 in amyloid fibrils of prion stop mutantsDetermination of amyloid core structure using chemical shifts.Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.N-terminal Prion Protein Peptides (PrP(120-144)) Form Parallel In-register β-Sheets via Multiple Nucleation-dependent PathwaysPathogenic Mutations Induce Partial Structural Changes in the Native β-Sheet Structure of Transthyretin and Accelerate Aggregation.13C and 15N chemical shift assignments of mammalian Y145Stop prion protein amyloid fibrils.BetaSerpentine: a bioinformatics tool for reconstruction of amyloid structures.Comparing the Folds of Prions and Other Pathogenic Amyloids.New applications of solid-state NMR in structural biologyWhat Does Solid-State NMR Tell Us about Amyloid Structures?
P2860
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P2860
Intermolecular alignment in Y145Stop human prion protein amyloid fibrils probed by solid-state NMR spectroscopy
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@ast
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@en
type
label
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@ast
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@en
prefLabel
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@ast
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@en
P2093
P2860
P356
P1476
Intermolecular alignment in Y1 ...... y solid-state NMR spectroscopy
@en
P2093
Christopher P Jaroniec
Jonathan J Helmus
Krystyna Surewicz
Marcin I Apostol
Witold K Surewicz
P2860
P304
13934-13937
P356
10.1021/JA206469Q
P407
P577
2011-08-15T00:00:00Z