Aβ42 oligomers, but not fibrils, simultaneously bind to and cause damage to ganglioside-containing lipid membranes.
about
Transient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseAmyloid β precursor protein as a molecular target for amyloid β--induced neuronal degeneration in Alzheimer's diseaseβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHRole of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's diseaseTwo-step mechanism of membrane disruption by Aβ through membrane fragmentation and pore formationEuropium as an inhibitor of Amyloid-β(1-42) induced membrane permeationAmino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.The Alzheimer's-related amyloid beta peptide is internalised by R28 neuroretinal cells and disrupts the microtubule associated protein 2 (MAP-2).Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer's disease.Increased Release of Apolipoprotein E in Extracellular Vesicles Following Amyloid-β Protofibril Exposure of Neuroglial Co-Cultures.Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease.Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates.Visualization of co-localization in Aβ42-administered neuroblastoma cells reveals lysosome damage and autophagosome accumulation related to cell death.Preferential interaction of the Alzheimer peptide Aβ-(1-42) with Omega-3-containing lipid bilayers: structure and interaction studies.GM1 Ganglioside Inhibits β-Amyloid Oligomerization Induced by Sphingomyelin.Global transition of human serum albumin to prefibrillar aggregates induced by temsirolimus: Insight into implications of anti-renal cancer drug.Unmodified and pyroglutamylated amyloid β peptides form hypertoxic hetero-oligomers of unique secondary structure.Probing oligomerization of amyloid beta peptide in silico.d-Amino Acid Pseudopeptides as Potential Amyloid-Beta Aggregation InhibitorsGM1 -Gangliosid hemmt die β-Amyloid-Oligomerisation, während Sphingomyelin diese initiiert
P2860
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P2860
Aβ42 oligomers, but not fibrils, simultaneously bind to and cause damage to ganglioside-containing lipid membranes.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh-hant
name
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@en
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@nl
type
label
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@en
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@nl
prefLabel
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@en
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@nl
P2093
P2860
P50
P356
P1433
P1476
Aβ42 oligomers, but not fibril ...... de-containing lipid membranes.
@en
P2093
A Toby A Jenkins
Benjamin R G Johnson
Simon D A Connell
P2860
P356
10.1042/BJ20110750
P407
P577
2011-10-01T00:00:00Z