Location and Conformation of Amyloid β (25–35) Peptide and its Sequence‐Shuffled Peptides within Membranes: Implications for Aggregation and Toxicity in PC12 …
Extracellular deposits of amyloid β (Aβ) aggregates in the brain is the hallmark of
Alzheimer's disease. We present the configurations (location and conformation) and the …
Alzheimer's disease. We present the configurations (location and conformation) and the …
Aggregation of Alzheimer's amyloid β-peptide in biological membranes: A molecular dynamics study
Numerous studies have concluded that the interaction of the amyloid β-peptide (Aβ) and
cellular membranes contributes to the toxicity and cell death observed in the progression of …
cellular membranes contributes to the toxicity and cell death observed in the progression of …
Folding and membrane insertion of amyloid‐beta (25–35) peptide and its mutants: Implications for aggregation and neurotoxicity
HHG Tsai, JB Lee, SS Tseng, XA Pan… - Proteins: Structure …, 2010 - Wiley Online Library
The mechanisms of interfacial folding and membrane insertion of the Alzheimer's amyloid‐β
fragment Aβ (25–35) and its less toxic mutant, N27A‐Aβ (25–35) and more toxic mutant …
fragment Aβ (25–35) and its less toxic mutant, N27A‐Aβ (25–35) and more toxic mutant …
[HTML][HTML] Molecular dynamics simulations of amyloid β-peptide (1-42): tetramer formation and membrane interactions
The aggregation cascade and peptide-membrane interactions of the amyloid β-peptide (Aβ)
have been implicated as toxic events in the development and progression of Alzheimer's …
have been implicated as toxic events in the development and progression of Alzheimer's …
Biophysical insights into the membrane interaction of the core amyloid-forming Aβ 40 fragment K16–K28 and its role in the pathogenesis of Alzheimer's disease
The aggregation of amyloid-β (Aβ) on neuronal membranes is implicated in both neuronal
toxicity and the progression of Alzheimer's disease. Unfortunately, the heterogeneous …
toxicity and the progression of Alzheimer's disease. Unfortunately, the heterogeneous …
Linking folding with aggregation in Alzheimer's β-amyloid peptides
J Khandogin, CL Brooks III - Proceedings of the National …, 2007 - National Acad Sciences
Growing evidence suggests that the β-amyloid (Aβ) peptides of Alzheimer's disease are
generated in early endosomes and that small oligomers are the principal toxic species. We …
generated in early endosomes and that small oligomers are the principal toxic species. We …
Putative structures of membrane-embedded amyloid β oligomers
A Sepehri, T Lazaridis - ACS Chemical Neuroscience, 2022 - ACS Publications
Perturbation of cell membranes by amyloid β (Ab) peptide oligomers is one possible
mechanism of cytotoxicity in Alzheimer's disease, but the structure of such Ab–membrane …
mechanism of cytotoxicity in Alzheimer's disease, but the structure of such Ab–membrane …
Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation
Amyloid-β (Aβ) peptides are thought to be involved in neurodegenerative diseases such as
Alzheimer's disease and Down's syndrome. They form a large number of polymorphic …
Alzheimer's disease and Down's syndrome. They form a large number of polymorphic …
Stability of Aβ11–40 trimers with parallel and antiparallel β-sheet organizations in a membrane-mimicking environment by replica exchange molecular dynamics …
ST Ngo, PH Nguyen, P Derreumaux - The Journal of Physical …, 2020 - ACS Publications
The aggregation of the amyloid (Aβ) peptide of 39–43 amino acids into plaques is observed
in the brain of Alzheimer's disease (AD) patients, but the mechanisms underlying the …
in the brain of Alzheimer's disease (AD) patients, but the mechanisms underlying the …
[HTML][HTML] De novo aggregation of Alzheimer's Aβ25-35 peptides in a lipid bilayer
AK Smith, DK Klimov - Scientific Reports, 2019 - nature.com
A potential mechanism of cytotoxicity attributed to Alzheimer's A β peptides postulates that
their aggregation disrupts membrane structure causing uncontrollable permeation of Ca2+ …
their aggregation disrupts membrane structure causing uncontrollable permeation of Ca2+ …
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