Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity.
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A comparative analysis of the aggregation behavior of amyloid-β peptide variantsStructural basis of β-amyloid-dependent synaptic dysfunctions.High-speed atomic force microscopy reveals structural dynamics of amyloid β1-42 aggregates.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Cross-seeding effects of amyloid β-protein and α-synuclein.The Alzheimer disease protective mutation A2T modulates kinetic and thermodynamic properties of amyloid-β (Aβ) aggregation.Interplay of histidine residues of the Alzheimer's disease Aβ peptide governs its Zn-induced oligomerization.Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Specific antibody binding to the APP672-699 region shifts APP processing from α- to β-cleavagePhenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding.Amyloid precursor protein mutation E682K at the alternative β-secretase cleavage β'-site increases Aβ generation.Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.The domestic cat as a natural animal model of Alzheimer's disease.Familial Alzheimer's disease mutations differentially alter amyloid β-protein oligomerizationAllosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.Amyloid β-protein oligomers and Alzheimer's disease.Low-n oligomers as therapeutic targets of Alzheimer's disease.Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease.Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Modulation in the conformational and stability attributes of the Alzheimer's disease associated amyloid-beta mutants and their favorable stabilization by curcumin: molecular dynamics simulation analysis.DENN/MADD/IG20 alternative splicing changes and cell death in Alzheimer's disease.Divalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms.Potent amyloidogenicity and pathogenicity of Aβ43.Phosphorylation Interferes with Maturation of Amyloid-β Fibrillar Structure in the N Terminus.C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42.Phosphorylation modifies the molecular stability of β-amyloid deposits.Zinc-induced heterodimer formation between metal-binding domains of intact and naturally modified amyloid-beta species: implication to amyloid seeding in Alzheimer's disease?Role of Species-Specific Primary Structure Differences in Aβ42 Assembly and NeurotoxicityModeling the Aggregation Propensity and Toxicity of Amyloid-β Variants.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Kinetics of the Interactions between Copper and Amyloid-β with FAD Mutations and Phosphorylation at the N terminus.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity.Role of the N-terminus for the stability of an amyloid-β fibril with three-fold symmetry.Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42Effect of the Tottori familial disease mutation (D7N) on the monomers and dimers of Aβ40 and Aβ42.Familial Alzheimer's Disease Mutations within the Amyloid Precursor Protein Alter the Aggregation and Conformation of the Amyloid-β Peptide.APP/Aβ structural diversity and Alzheimer's disease pathogenesis.Unmodified and pyroglutamylated amyloid β peptides form hypertoxic hetero-oligomers of unique secondary structure.
P2860
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P2860
Effects of the English (H6R) and Tottori (D7N) familial Alzheimer disease mutations on amyloid beta-protein assembly and toxicity.
description
2010 nî lūn-bûn
@nan
2010 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Effects of the English (H6R) a ...... protein assembly and toxicity.
@ast
Effects of the English (H6R) a ...... protein assembly and toxicity.
@en
Effects of the English
@nl
type
label
Effects of the English (H6R) a ...... protein assembly and toxicity.
@ast
Effects of the English (H6R) a ...... protein assembly and toxicity.
@en
Effects of the English
@nl
prefLabel
Effects of the English (H6R) a ...... protein assembly and toxicity.
@ast
Effects of the English (H6R) a ...... protein assembly and toxicity.
@en
Effects of the English
@nl
P2093
P2860
P356
P1476
Effects of the English (H6R) a ...... protein assembly and toxicity.
@en
P2093
David B Teplow
Kenjiro Ono
Margaret M Condron
P2860
P304
23186-23197
P356
10.1074/JBC.M109.086496
P407
P577
2010-05-07T00:00:00Z