The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
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Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Doxycycline hinders phenylalanine fibril assemblies revealing a potential novel therapeutic approach in phenylketonuriaAlzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.Amylin-Aβ oligomers at atomic resolution using molecular dynamics simulations: a link between Type 2 diabetes and Alzheimer's diseaseAllosteric stabilization of the amyloid-β peptide hairpin by the fluctuating N-terminal.Tackling amyloidogenesis in Alzheimer's disease with A2V variants of Amyloid-β.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.Amyloid-β peptides in interaction with raft-mime model membranes: a neutron reflectivity insight.Alternative Selection of β-Site APP-Cleaving Enzyme 1 (BACE1) Cleavage Sites in Amyloid β-Protein Precursor (APP) Harboring Protective and Pathogenic Mutations within the Aβ Sequence.High-Resolution Structures of the Amyloid-β 1-42 Dimers from the Comparison of Four Atomistic Force Fields.HIV-1 matrix protein p17 misfolding forms toxic amyloidogenic assemblies that induce neurocognitive disorders.Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide.The A2V mutation as a new tool for hindering Aβ aggregation: A neutron and x-ray diffraction studyBeta-amyloid 1-42 monomers, but not oligomers, produce PHF-like conformation of Tau protein.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.The Tat-Aβ1-6A2V(D) peptide against AD synaptopathy.Translational Research in Alzheimer's and Prion Diseases.The Pathogenic A2V Mutant Exhibits Distinct Aggregation Kinetics, Metal Site Structure, and Metal Exchange of the Cu2+ -Aβ Complex.A2T and A2V Aβ peptides exhibit different aggregation kinetics, primary nucleation, morphology, structure, and LTP inhibition.Elucidating the Inhibitory Potential of Designed Peptides Against Amyloid Fibrillation and Amyloid Associated Cytotoxicity
P2860
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P2860
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
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2014 nî lūn-bûn
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2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
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name
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@ast
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@en
type
label
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@ast
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@en
prefLabel
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@ast
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@en
P2093
P2860
P50
P356
P1476
The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assembly
@en
P2093
Alessandro Rossi
Laura Cantù
Laura Colombo
Massimo Messa
Tatiana Stoilova
P2860
P304
24143-24152
P356
10.1074/JBC.M114.576256
P407
P577
2014-07-18T00:00:00Z