Direct measurement of lipid membrane disruption connects kinetics and toxicity of Aβ42 aggregation
The formation of amyloid deposits in human tissues is a defining feature of more than 50
medical disorders, including Alzheimer's disease. Strong genetic and histological evidence …
medical disorders, including Alzheimer's disease. Strong genetic and histological evidence …
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
S De, DC Wirthensohn, P Flagmeier, C Hughes… - Nature …, 2019 - nature.com
Protein aggregation is a complex process resulting in the formation of heterogeneous
mixtures of aggregate populations that are closely linked to neurodegenerative conditions …
mixtures of aggregate populations that are closely linked to neurodegenerative conditions …
Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism
SIA Cohen, S Linse, LM Luheshi… - Proceedings of the …, 2013 - National Acad Sciences
The generation of toxic oligomers during the aggregation of the amyloid-β (Aβ) peptide Aβ42
into amyloid fibrils and plaques has emerged as a central feature of the onset and …
into amyloid fibrils and plaques has emerged as a central feature of the onset and …
Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide
Oligomeric species populated during the aggregation of the Aβ42 peptide have been
identified as potent cytotoxins linked to Alzheimer's disease, but the fundamental molecular …
identified as potent cytotoxins linked to Alzheimer's disease, but the fundamental molecular …
Cholesterol in membranes facilitates aggregation of amyloid β protein at physiologically relevant concentrations
The formation of amyloid β (1-42)(Aβ42) oligomers is considered to be a critical step in the
development of Alzheimer's disease (AD). However, the mechanism underlying this process …
development of Alzheimer's disease (AD). However, the mechanism underlying this process …
Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes
Alzheimer's disease is a neurodegenerative disorder associated with the aberrant
aggregation of the amyloid-β peptide. Although increasing evidence implicates cholesterol …
aggregation of the amyloid-β peptide. Although increasing evidence implicates cholesterol …
[HTML][HTML] Impact of Membrane Phospholipids and Exosomes on the Kinetics of Amyloid-β Fibril Assembly
A Khursheed, JH Viles - Journal of Molecular Biology, 2024 - Elsevier
Alzheimer's disease (AD) is linked with the self-association of the amyloid-β peptide (Aβ)
into oligomers and fibrils. The brain is a lipid rich environment for Aβ to assemble, while the …
into oligomers and fibrils. The brain is a lipid rich environment for Aβ to assemble, while the …
A Kinetic Map of the Influence of Biomimetic Lipid Model Membranes on Aβ42 Aggregation
KN Baumann, G Šneiderienė… - ACS Chemical …, 2022 - ACS Publications
The aggregation of the amyloid β (Aβ) peptide is one of the molecular hallmarks of
Alzheimer's disease (AD). Although Aβ deposits have mostly been observed extracellularly …
Alzheimer's disease (AD). Although Aβ deposits have mostly been observed extracellularly …
Complexity in Lipid Membrane Composition Induces Resilience to Aβ42 Aggregation
M Sanguanini, KN Baumann, S Preet… - ACS chemical …, 2020 - ACS Publications
The molecular origins of Alzheimer's disease are associated with the aggregation of the
amyloid-β peptide (Aβ). This process is controlled by a complex cellular homeostasis …
amyloid-β peptide (Aβ). This process is controlled by a complex cellular homeostasis …
Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation
KL Stewart, SE Radford - Biophysical reviews, 2017 - Springer
Aggregation of the amyloid-β (Aβ) peptide is strongly correlated with Alzheimer's disease
(AD). Recent research has improved our understanding of the kinetics of amyloid fibril …
(AD). Recent research has improved our understanding of the kinetics of amyloid fibril …