Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.
about
Familial Alzheimer's disease Osaka mutant (ΔE22) β-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment.Biophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Alzheimer's disease: which type of amyloid-preventing drug agents to employ?Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Single nucleotide variations: biological impact and theoretical interpretation.Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions.Point mutations in Aβ induce polymorphic aggregates at liquid/solid interfaces.Atomic force microscopy of model lipid membranes.The modulating effect of mechanical changes in lipid bilayers caused by apoE-containing lipoproteins on Aβ induced membrane disruptionAmyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.Investigation of temperature induced mechanical changes in supported bilayers by variants of tapping mode atomic force microscopy.Structural origin of polymorphism of Alzheimer's amyloid β-fibrils.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Arctic mutant Aβ40 aggregates on α7 nicotinic acetylcholine receptors and inhibits their functions.
P2860
Q30153519-E0221C3B-B858-4AB9-928C-380FDC1960EDQ30427825-C2374233-F2BC-411E-AC42-EC0A74747D6BQ34330351-DEBAA00B-7610-4069-B4F3-DB4297659F87Q34434154-6B3B022F-55D1-4644-80FE-50B2E185F4BEQ34621290-354042B8-D0DB-4CE0-8810-57513B3E8FD5Q35691850-12624EF9-D9E7-4E22-9545-453D87203727Q36015441-CC8A4B94-56C1-4A19-880D-22C27BF2FB9CQ38042569-69800119-7E73-46FA-B12A-9EA316708144Q39369410-A6C2914C-09A6-4E8B-A9AA-6DD1AAAE8713Q41142736-23477596-6F12-4AC3-BB2D-1A65D663DA08Q41970717-1374728B-2DCD-4C0D-8D83-02A47A6B05ABQ45005211-38D42324-6C3F-42AF-AEE2-A66C71526C32Q45989310-EB469A4B-BBD9-41F0-827C-636013F61741Q48175839-8FF0A3B0-C948-480A-88CF-924730B77967Q51747523-3A54C8EA-FB39-4348-9AB9-ACE00133A695
P2860
Point mutations in Aβ result in the formation of distinct polymorphic aggregates in the presence of lipid bilayers.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@ast
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@en
type
label
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@ast
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@en
prefLabel
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@ast
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@en
P2860
P1433
P1476
Point mutations in Aβ result i ...... he presence of lipid bilayers.
@en
P2093
Justin Legleiter
Phillip M Pifer
P2860
P304
P356
10.1371/JOURNAL.PONE.0016248
P407
P577
2011-01-18T00:00:00Z