Molecular structure of amyloid fibrils: insights from solid-state NMR.
about
Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solutionProtein-induced photophysical changes to the amyloid indicator dye thioflavin TDry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wiresStructural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrilsExpression and purification of 15N- and 13C-isotope labeled 40-residue human Alzheimer's β-amyloid peptide for NMR-based structural analysisAmyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structureAmyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structureNew Potential Pharmacological Functions of Chinese Herbal Medicines via Regulation of AutophagyAromatic Cross-Strand Ladders Control the Structure and Stability of β-Rich Peptide Self-Assembly MimicsMolecular structural basis for polymorphism in Alzheimer's -amyloid fibrilsAtomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopySupramolecular Protein Structure Determination by Site-Specific Long-Range Intermolecular Solid State NMR Spectroscopyβ2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkagesCrystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomersMy 65 years in protein chemistryAmyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosisComputational design of new Peptide inhibitors for amyloid Beta (aβ) aggregation in Alzheimer's disease: application of a novel methodologyStructural Characterization of Fibrils from Recombinant Human Islet Amyloid Polypeptide by Solid-State NMR: The Central FGAILS Segment Is Part of the β-Sheet CoreThe Japanese Mutant Aβ (ΔE22-Aβ1−39) Forms Fibrils Instantaneously, with Low-Thioflavin T Fluorescence: Seeding of Wild-Type Aβ1−40into Atypical Fibrils by ΔE22-Aβ1−39High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .The impact of protein disulfide bonds on the amyloid fibril morphology.Structural studies of proteins by paramagnetic solid-state NMR spectroscopyStructural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac SulfideSolid-state NMR studies of HIV-1 capsid protein assemblies.Prion amyloid structure explains templating: how proteins can be genes.Coarse-grained force field: general folding theory.Revealing protein structures in solid-phase peptide synthesis by 13C solid-state NMR: evidence of excessive misfolding for Alzheimer's β.Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFMConformational switching within individual amyloid fibrils.Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modelingMetal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.Biomolecular solid state NMR with magic-angle spinning at 25KMeasurement of amyloid fibril mass-per-length by tilted-beam transmission electron microscopy.Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils.The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesisSelection of peptide inhibitors of soluble Aβ(1-42) oligomer formation by phage display.Performance of RINEPT is amplified by dipolar couplings under ultrafast MAS conditions.Retinal conformation and dynamics in activation of rhodopsin illuminated by solid-state H NMR spectroscopy.
P2860
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P2860
Molecular structure of amyloid fibrils: insights from solid-state NMR.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@ast
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@en
type
label
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@ast
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@en
prefLabel
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@ast
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@en
P1476
Molecular structure of amyloid fibrils: insights from solid-state NMR.
@en
P356
10.1017/S0033583506004173
P50
P577
2006-02-01T00:00:00Z