β-hairpin-mediated nucleation of polyglutamine amyloid formation.
about
An improved capping unit for stabilizing the ends of associated β-strands.Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.Biophysical underpinnings of the repeat length dependence of polyglutamine amyloid formationFibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine corePolyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state nuclear magnetic resonance.An Analysis of Biomolecular Force Fields for Simulations of Polyglutamine in SolutionIts preferential interactions with biopolymers account for diverse observed effects of trehaloseHuntingtin N-Terminal Monomeric and Multimeric Structures Destabilized by Covalent Modification of Heteroatomic Residues.Huntingtin exon 1 fibrils feature an interdigitated β-hairpin-based polyglutamine coreAggregation formation in the polyglutamine diseases: protection at a cost?Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.Structural motif of polyglutamine amyloid fibrils discerned with mixed-isotope infrared spectroscopy.A serendipitous survey of prediction algorithms for amyloidogenicity.An overview of peptide and peptoid foldamers in medicinal chemistry.Emerging β-Sheet Rich Conformations in Supercompact Huntingtin Exon-1 Mutant Structures.Structural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.Backbone Engineering within a Latent β-Hairpin Structure to Design Inhibitors of Polyglutamine Amyloid Formation.Versatile members of the DNAJ family show Hsp70 dependent anti-aggregation activity on RING1 mutant parkin C289G.Tuning self-assembly in elastin-derived peptides.Amyloid nanospheres from polyglutamine rich peptides: assemblage through an intermolecular salt bridge interaction.Aggregation behavior of chemically synthesized, full-length huntingtin exon1.Architecture of polyglutamine-containing fibrils from time-resolved fluorescence decay.How to Get Insight into Amyloid Structure and Formation from Infrared Spectroscopy.Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease.Structure and Dynamics of DNA and RNA Double Helices of CAG and GAC Trinucleotide Repeats.Lysine residues in the N-terminal huntingtin amphipathic α-helix play a key role in peptide aggregation.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.The Aggregation Free Energy Landscapes of Polyglutamine Repeats.Assembly of Huntingtin headpiece into α-helical bundles.Hidden motions and motion-induced invisibility: Dynamics-based spectral editing in solid-state NMR.
P2860
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P2860
β-hairpin-mediated nucleation of polyglutamine amyloid formation.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
β-hairpin-mediated nucleation of polyglutamine amyloid formation.
@en
type
label
β-hairpin-mediated nucleation of polyglutamine amyloid formation.
@en
prefLabel
β-hairpin-mediated nucleation of polyglutamine amyloid formation.
@en
P2093
P2860
P50
P1476
β-hairpin-mediated nucleation of polyglutamine amyloid formation
@en
P2093
Irene Arduini
Kenneth W Drombosky
Ravindra Kodali
Ronald Wetzel
W Seth Horne
P2860
P304
P356
10.1016/J.JMB.2013.01.016
P407
P577
2013-01-23T00:00:00Z