Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
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A comparative analysis of the aggregation behavior of amyloid-β peptide variantsStabilization of neurotoxic soluble beta-sheet-rich conformations of the Alzheimer's disease amyloid-beta peptideX-ray Crystallographic Structures of Trimers and Higher-Order Oligomeric Assemblies of a Peptide Derived from Aβ 17–36An intranasally delivered peptide drug ameliorates cognitive decline in Alzheimer transgenic mice.Multifaceted Roles of Metzincins in CNS Physiology and Pathology: From Synaptic Plasticity and Cognition to Neurodegenerative DisordersAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Structural determination of Abeta25-35 micelles by molecular dynamics simulations.A peptide that binds specifically to the β-amyloid of Alzheimer's disease: selection and assessment of anti-β-amyloid neurotoxic effects.Peptides for therapy and diagnosis of Alzheimer's disease.Physicochemical characteristics of soluble oligomeric Abeta and their pathologic role in Alzheimer's disease.Curcumin Binding to Beta Amyloid: A Computational Study.Effect of alanine replacement of l17 and f19 on the aggregation and neurotoxicity of arctic-type aβ40Effects of solvent on the structure of the Alzheimer amyloid-beta(25-35) peptide.Effect of C-terminal residues of Aβ on copper binding affinity, structural conversion and aggregation.Allosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.Nanotools for megaproblems: probing protein misfolding diseases using nanomedicine modus operandiInfluence of the physiochemical properties of superparamagnetic iron oxide nanoparticles on amyloid β protein fibrillation in solution.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.AFM for analysis of structure and dynamics of DNA and protein-DNA complexesAβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approachA covalently reactive group-modified peptide that specifically reacts with lysine16 in amyloid β.Impact of a discordant helix on β-amyloid structure, aggregation ability and toxicity.Assembly of Peptides Derived from β-Sheet Regions of β-Amyloid.Coassembly of Peptides Derived from β-Sheet Regions of β-AmyloidMembrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets.Design of 11-residue peptides with unusual biophysical properties: induced secondary structure in the absence of water.Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α,α-disubstitution results in altered aggregate size and morphologyCytokine-mediated inhibition of fibrillar amyloid-beta peptide degradation by human mononuclear phagocytes.Interaction of the amyloid β peptide with sodium dodecyl sulfate as a membrane-mimicking detergent.In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process.Reversal of temperature-induced conformational changes in the amyloid-beta peptide, Abeta40, by the beta-sheet breaker peptides 16-23 and 17-24.Calorimetric investigation of copper(II) binding to Aβ peptides: thermodynamics of coordination plasticity.Characterization of the internal dynamics and conformational space of zinc-bound amyloid β peptides by replica-exchange molecular dynamics simulations.Synthesis and evaluation of antineurotoxicity properties of an amyloid-β peptide targeting ligand containing a triamino acid.Assemblies of amyloid-β30-36 hexamer and its G33V/L34T mutants by replica-exchange molecular dynamics simulation.A peptide probe for detection of various beta-amyloid oligomers.Understanding the roles of mutations in the amyloid precursor protein in Alzheimer disease.Delineation of the core aggregation sequences of TDP-43 C-terminal fragment.Graphene quantum dots for the inhibition of β amyloid aggregation.Engineering of a peptide probe for β-amyloid aggregates.
P2860
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P2860
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@ast
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@en
type
label
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@ast
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@en
prefLabel
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@ast
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@en
P2093
P356
P1476
Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.
@en
P2093
Chad McAllister
Michael R Sierks
Ruitian Liu
Yuri Lyubchenko
P304
P356
10.1002/JNR.10859
P577
2004-01-01T00:00:00Z