Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.
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MAS (1)H NMR Probes Freezing Point Depression of Water and Liquid-Gel Phase Transitions in LiposomesFree-Energy Landscape of the Amino-Terminal Fragment of Huntingtin in Aqueous SolutionFibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine coreNano-mole scale side-chain signal assignment by 1H-detected protein solid-state NMR by ultra-fast magic-angle spinning and stereo-array isotope labelingThe emerging role of the first 17 amino acids of huntingtin in Huntington's diseaseHuntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine coreSolid-State Nuclear Magnetic Resonance on the Static and Dynamic Domains of Huntingtin Exon-1 Fibrils.Identification and Structural Characterization of the N-terminal Amyloid Core of Orb2 isoform A.Investigating Mutations to Reduce Huntingtin Aggregation by Increasing Htt-N-Terminal Stability and Weakening Interactions with PolyQ Domain.Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils.Peptide-Directed Assembly of Single-Helical Gold Nanoparticle Superstructures Exhibiting Intense Chiroptical Activity.Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G.Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.A toxic mutant huntingtin species is resistant to selective autophagy.The 17-residue-long N terminus in huntingtin controls step-wise aggregation in solution and on membranes via different mechanisms.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.On the use of ultracentrifugal devices for routine sample preparation in biomolecular magic-angle-spinning NMR.Assembly of Huntingtin headpiece into α-helical bundles.Methionine oxidized apolipoprotein A-I at the crossroads of HDL biogenesis and amyloid formation.Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.
P2860
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P2860
Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@ast
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@en
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@nl
type
label
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@ast
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@en
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@nl
prefLabel
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@ast
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@en
Polyglutamine amyloid core bou ...... te nuclear magnetic resonance.
@nl
P2093
P2860
P50
P356
P1433
P1476
Polyglutamine amyloid core bou ...... ate nuclear magnetic resonance
@en
P2093
Hsiang-Kai Lin
Michelle A Poirier
Ronald Wetzel
Zhipeng Hou
P2860
P304
P356
10.1021/BI501010Q
P407
P577
2014-10-16T00:00:00Z