Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
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MAS (1)H NMR Probes Freezing Point Depression of Water and Liquid-Gel Phase Transitions in LiposomesCataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine coreFolding Landscape of Mutant Huntingtin Exon1: Diffusible Multimers, Oligomers and Fibrils, and No Detectable Monomer.Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Formation and Structure of Wild Type Huntingtin Exon-1 Fibrils.Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein.Emerging β-Sheet Rich Conformations in Supercompact Huntingtin Exon-1 Mutant Structures.Peptide-Directed Assembly of Single-Helical Gold Nanoparticle Superstructures Exhibiting Intense Chiroptical Activity.Inhibition of polyglutamine aggregation by SIMILAR huntingtin N-terminal sequences: Prospective molecules for preclinical evaluation in Huntington's disease.Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.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.Characterization of Protein-Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease.Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.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.Covalent Tethering and Residues with Bulky Hydrophobic Side Chains Enable Self-Assembly of Distinct Amyloid Structures.Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.The Aggregation Free Energy Landscapes of Polyglutamine Repeats.Sphingomyelin and GM1 Influence Huntingtin Binding to, Disruption of, and Aggregation on Lipid Membranes.Assembly of Huntingtin headpiece into α-helical bundles.Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.Magic angle spinning spheresNew applications of solid-state NMR in structural biology
P2860
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P2860
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@ast
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@en
type
label
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@ast
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@en
prefLabel
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@ast
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@en
P2093
P2860
P50
P356
P1476
Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine core
@en
P2093
Abhishek Mandal
Hsiang-Kai Lin
Jonathan M Lamley
Ronald Wetzel
P2860
P304
P356
10.1073/PNAS.1521933113
P407
P577
2016-02-01T00:00:00Z