On the nucleation of amyloid beta-protein monomer folding.
about
Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solutionA partially folded structure of amyloid-beta(1-40) in an aqueous environmentAmyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesThe Alzheimer's peptides Abeta40 and 42 adopt distinct conformations in water: a combined MD / NMR studyTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseDisrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsStructural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyChaperones of F1-ATPaseModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsInfluence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formationStructure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrilsInteraction between amyloid beta peptide and an aggregation blocker peptide mimicking islet amyloid polypeptideAmyloid-β protofibrils: size, morphology and synaptotoxicity of an engineered mimicDesign and Characterization of Chemically Stabilized Aβ42 OligomersStructural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity.Nano-assembly of amyloid β peptide: role of the hairpin fold.Efficient access to highly pure β-amyloid peptide by optimized solid-phase synthesis.Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).Structure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.Inhibition of beta-amyloid(1-40) Peptide Aggregation and Neurotoxicity by CitrateAssociation thermodynamics and conformational stability of beta-sheet amyloid beta(17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralizationStructure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersHigh-resolution conformation and backbone dynamics of a soluble aggregate of apomyoglobin119.Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity.Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragmentsDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Stabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineeringFibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsSolvent and mutation effects on the nucleation of amyloid beta-protein foldingAmyloid-β peptide structure in aqueous solution varies with fragment size.Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.A differential association of Apolipoprotein E isoforms with the amyloid-β oligomer in solution.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationA synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.
P2860
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P2860
On the nucleation of amyloid beta-protein monomer folding.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
On the nucleation of amyloid beta-protein monomer folding.
@en
On the nucleation of amyloid beta-protein monomer folding.
@nl
type
label
On the nucleation of amyloid beta-protein monomer folding.
@en
On the nucleation of amyloid beta-protein monomer folding.
@nl
prefLabel
On the nucleation of amyloid beta-protein monomer folding.
@en
On the nucleation of amyloid beta-protein monomer folding.
@nl
P2093
P2860
P356
P1433
P1476
On the nucleation of amyloid beta-protein monomer folding.
@en
P2093
Alan C Rigby
David B Teplow
Margaret C Condron
Marianne A Grant
P2860
P304
P356
10.1110/PS.041292205
P50
P577
2005-06-01T00:00:00Z