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The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variantsStructure of the cross-beta spine of amyloid-like fibrilsA method to assess compositional bias in biological sequences and its application to prion-like glutamine/asparagine-rich domains in eukaryotic proteomesMolecular origin of polyglutamine aggregation in neurodegenerative diseases.Fibrillogenesis of huntingtin and other glutamine containing proteinsDeciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopyA helical structural nucleus is the primary elongating unit of insulin amyloid fibrilsHigh-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopyThe structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice modelMolecular structural basis for polymorphism in Alzheimer's -amyloid fibrilsMolecular Mechanism of Thioflavin-T Binding to the Surface of β-Rich Peptide Self-AssembliesSecondary Structure of Huntingtin Amino-Terminal RegionBeta conformation of polyglutamine track revealed by a crystal structure of Huntingtin N-terminal region with insertion of three histidine residuesDisease-Associated Polyglutamine Stretches in Monomeric Huntingtin Adopt a Compact StructureLinear and extended: a common polyglutamine conformation recognized by the three antibodies MW1, 1C2 and 3B5H10Site-specific identification of non-beta-strand conformations in Alzheimer's beta-amyloid fibrils by solid-state NMRA structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMRExperimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrilsSolid-state NMR as a probe of amyloid structureBinding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current statusGel formation in protein amyloid aggregation: a physical mechanism for cytotoxicityStructural Polymorphism of Alzheimer's β-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR StudyStructural basis for rodlet assembly in fungal hydrophobinsAmyloid-like fibrils of ribonuclease A with three-dimensional domain-swapped and native-like structure.Asparagine and glutamine differ in their propensities to form specific side chain-backbone hydrogen bonded motifs in proteins.Polyglutamine aggregate structure in vitro and in vivo; new avenues for coherent anti-Stokes Raman scattering microscopyElongation kinetics of polyglutamine peptide fibrils: a quartz crystal microbalance with dissipation study.Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide.Nanomaterials design and tests for neural tissue engineering.Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrilsParallel beta-sheets and polar zippers in amyloid fibrils formed by residues 10-39 of the yeast prion protein Ure2p.BETASCAN: probable beta-amyloids identified by pairwise probabilistic analysis.Hydration profiles of amyloidogenic molecular structures.Stable polyglutamine dimers can contain β-hairpins with interdigitated side chains-but not α-helices, β-nanotubes, β-pseudohelices, or steric zippers.Conformational switching in PolyGln amyloid fibrils resulting from a single amino acid insertion.Monomeric, oligomeric and polymeric proteins in huntington disease and other diseases of polyglutamine expansionPolyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences.Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: significant role of Asn ladder.A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation.Investigating the structural impact of the glutamine repeat in huntingtin assembly.
P2860
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P2860
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Amyloid fibers are water-filled nanotubes.
@ast
Amyloid fibers are water-filled nanotubes.
@en
type
label
Amyloid fibers are water-filled nanotubes.
@ast
Amyloid fibers are water-filled nanotubes.
@en
prefLabel
Amyloid fibers are water-filled nanotubes.
@ast
Amyloid fibers are water-filled nanotubes.
@en
P2093
P2860
P356
P1476
Amyloid fibers are water-filled nanotubes.
@en
P2093
P2860
P304
P356
10.1073/PNAS.042681399
P407
P577
2002-04-01T00:00:00Z