Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology.
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A hIAPP-derived all-D-amino-acid inhibits hIAPP fibrillation efficiently at membrane surface by targeting α-helical oligomeric intermediatesThe toxicity of amyloid β oligomersAmyloid beta: multiple mechanisms of toxicity and only some protective effects?Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domainFactors That Drive Peptide Assembly from Native to Amyloid Structures: Experimental and Theoretical Analysis of [Leu-5]-Enkephalin MutantsThe alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seedingInhibition of the mitochondrial enzyme ABAD restores the amyloid-β-mediated deregulation of estradiolPotential role of atomic force microscopy in systems biologySynaptotoxicity of Alzheimer beta amyloid can be explained by its membrane perforating propertyAβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.All-d-Enantiomer of β-Amyloid Peptide Forms Ion Channels in Lipid Bilayers.Effects of surface interactions on peptide aggregate morphology.Models of membrane-bound Alzheimer's Abeta peptide assembliesConversion of a porin-like peptide channel into a gramicidin-like channel by glycine to D-alanine substitutions.Aggregation of Aß(25-35) on DOPC and DOPC/DHA bilayers: an atomic force microscopy studyBiophysical insights into how surfaces, including lipid membranes, modulate protein aggregation related to neurodegeneration.Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFMComparison of the amyloid pore forming properties of rat and human Alzheimer's beta-amyloid peptide 1-42: Calcium imaging dataFilamentous-actins in human hepatocarcinoma cells with CLSM.Models of beta-amyloid ion channels in the membrane suggest that channel formation in the bilayer is a dynamic process.Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavitiesAutoinsertion of soluble oligomers of Alzheimer's Abeta(1-42) peptide into cholesterol-containing membranes is accompanied by relocation of the sterol towards the bilayer surface.A novel role for connexin hemichannel in oxidative stress and smoking-induced cell injury.α-helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes.Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases.Effect of metals on kinetic pathways of amyloid-β aggregationStructure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersTruncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndromeCalcium signaling and amyloid toxicity in Alzheimer disease.Amyloid-beta-induced ion flux in artificial lipid bilayers and neuronal cells: resolving a controversyMolecular mechanisms of neurodegeneration in Alzheimer's disease.Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studiesAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Activity and architecture of pyroglutamate-modified amyloid-β (AβpE3-42) poresAmyloid ion channels: a common structural link for protein-misfolding diseaseThe influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.Structural convergence among diverse, toxic beta-sheet ion channels.Late-onset Alzheimer's disease, heating up and foxed by several proteins: pathomolecular effects of the aging process.Effect of surfaces on amyloid fibril formation.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.
P2860
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P2860
Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology.
description
2001 nî lūn-bûn
@nan
2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@ast
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@en
type
label
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@ast
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@en
prefLabel
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@ast
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@en
P2093
P356
P1433
P1476
Amyloid beta protein forms ion ...... mer's disease pathophysiology.
@en
P2093
P304
P356
10.1096/FJ.01-0377COM
P407
P577
2001-11-01T00:00:00Z