Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation.

Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation.

Item
http://www.wikidata.org/entity/Q35207585
Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresDisordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Mechanisms for the Insertion of Toxic, Fibril-like β-Amyloid Oligomers into the Membrane.Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Interactions between Aβ and mutated Tau lead to polymorphism and induce aggregation of Aβ-mutated tau oligomeric complexesAtomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology.Molecular interactions of Alzheimer amyloid-β oligomers with neutral and negatively charged lipid bilayers.Membrane permeation induced by aggregates of human islet amyloid polypeptidesThe interplay between carbon nanomaterials and amyloid fibrils in bio-nanotechnology.Stability of transmembrane amyloid β-peptide and membrane integrity tested by molecular modeling of site-specific Aβ42 mutations.Small molecule NPT-440-1 inhibits ionic flux through Aβ1-42 pores: Implications for Alzheimer's disease therapeutics.Sonication-induced coiled fibrous architectures of Boc-L-Phe-L-Lys(Z)-OMe.Amyloid β Ion Channels in a Membrane Comprising Brain Total Lipid Extracts.The diphenylpyrazole compound anle138b blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology.Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO 2 surface.Reduced Lipid Bilayer Thickness Regulates the Aggregation and Cytotoxicity of Amyloid-β.A novel form of β-strand assembly observed in Aβ33–42adsorbed onto graphene
P2860

Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation.

Item
http://www.wikidata.org/entity/Q35207585
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին 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
Polymorphism of amyloid β pept ...... insertion and pore formation.
@ast
Polymorphism of amyloid β pept ...... insertion and pore formation.
@en
type
label
Polymorphism of amyloid β pept ...... insertion and pore formation.
@ast
Polymorphism of amyloid β pept ...... insertion and pore formation.
@en
prefLabel
Polymorphism of amyloid β pept ...... insertion and pore formation.
@ast
Polymorphism of amyloid β pept ...... insertion and pore formation.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P698
P932
P356
P1433
P1476
Polymorphism of amyloid β pept ...... insertion and pore formation.
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P698
P932