Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide.
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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesStability and structure of oligomers of the Alzheimer peptide Abeta16-22: from the dimer to the 32-merExperimental characterization of disordered and ordered aggregates populated during the process of amyloid fibril formation.Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentImpact on the replacement of Phe by Trp in a short fragment of Aβ amyloid peptide on the formation of fibrils.Metal and complementary molecular bioimaging in Alzheimer's disease.Fibrils and nanotubes assembled from a modified amyloid-β peptide fragment differ in the packing of the same β-sheet building blocks.Structural stability and dynamics of an amyloid-forming peptide GNNQQNY from the yeast prion sup-35.Tracking fiber formation in human islet amyloid polypeptide with automated 2D-IR spectroscopy.New insights into the mechanism of Alzheimer amyloid-beta fibrillogenesis inhibition by N-methylated peptides.Light-triggered disassembly of amyloid fibrils.Dissecting structure of prion amyloid fibrils by hydrogen-deuterium exchange ultraviolet Raman spectroscopy.FTIR spectroscopic imaging of protein aggregation in living cells.Computational simulations of the early steps of protein aggregation.Sequence and crowding effects in the aggregation of a 10-residue fragment derived from islet amyloid polypeptideConformational changes induced by the A21G Flemish mutation in the amyloid precursor protein lead to increased Aβ production.Self-assembly of amphipathic β-sheet peptides: insights and applications.Amyloid scaffolds as alternative chlorosomes.The interplay of aggregation, fibrillization and gelation of an unexpected low molecular weight gelator: glycylalanylglycine in ethanol/water.Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides.The (13)C amide I band is still sensitive to conformation change when the regular amide I band cannot be distinguished at the typical position in H2O.Molecular, Local, and Network-Level Basis for the Enhanced Stiffness of Hydrogel Networks Formed from Coassembled Racemic Peptides: Predictions from Pauling and Corey.Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide.Effect of dehydration on the aggregation kinetics of two amyloid peptides.Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrilsPyroglutamylated amyloid-β peptide reverses cross β-sheets by a prion-like mechanism.An infrared spectroscopic study of the conformational transition of elastin-like polypeptides.Beta-adrenoceptor antagonists affect amyloid nanostructure; amyloid hydrogels as drug delivery vehicles.Mapping ApoE/Aβ binding regions to guide inhibitor discovery.Carbon-deuterium vibrational probes of peptide conformation: alanine dipeptide and glycine dipeptide.Unmodified and pyroglutamylated amyloid β peptides form hypertoxic hetero-oligomers of unique secondary structure.Sensing site-specific structural characteristics and chirality using vibrational circular dichroism of isotope labeled peptides.Balancing hydrophobicity and sequence pattern to influence self-assembly of amphipathic peptides.Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide.Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core.Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation.Coarse-grained protein molecular dynamics simulationsStructural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulations
P2860
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P2860
Experimental evidence for the reorganization of beta-strands within aggregates of the Abeta(16-22) peptide.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Experimental evidence for the ...... within aggregates of the Abeta
@nl
Experimental evidence for the ...... s of the Abeta(16-22) peptide.
@en
type
label
Experimental evidence for the ...... within aggregates of the Abeta
@nl
Experimental evidence for the ...... s of the Abeta(16-22) peptide.
@en
prefLabel
Experimental evidence for the ...... within aggregates of the Abeta
@nl
Experimental evidence for the ...... s of the Abeta(16-22) peptide.
@en
P356
P1476
Experimental evidence for the ...... s of the Abeta(16-22) peptide.
@en
P2093
Sarah A Petty
Sean M Decatur
P304
13488-13489
P356
10.1021/JA054663Y
P407
P577
2005-10-01T00:00:00Z