Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases
The conversion of native peptides and proteins into amyloid aggregates is a hallmark of over
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …
50 human disorders, including Alzheimer's and Parkinson's diseases. Increasing evidence …
Passive Immunotherapies Targeting Amyloid-β in Alzheimer's Disease: A Quantitative Systems Pharmacology Perspective
M Marković, J Milošević, W Wang, Y Cao - Molecular Pharmacology, 2024 - ASPET
Alzheimer's disease (AD) is a neurodegenerative disorder characterized by amyloid-β (A β)
protein accumulation in the brain. Passive immunotherapies using monoclonal antibodies …
protein accumulation in the brain. Passive immunotherapies using monoclonal antibodies …
Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain
Protein misfolding can generate toxic intermediates, which underlies several devastating
diseases, such as Alzheimer's disease (AD). The surface of AD-associated amyloid-β …
diseases, such as Alzheimer's disease (AD). The surface of AD-associated amyloid-β …
The supersaturation perspective on the amyloid hypothesis
DP Barron, Z Guo - Chemical Science, 2024 - pubs.rsc.org
Development of therapeutic interventions for Alzheimer's over the past three decades has
been guided by the amyloid hypothesis, which puts Aβ deposition as the initiating event of a …
been guided by the amyloid hypothesis, which puts Aβ deposition as the initiating event of a …
Design of amyloidogenic peptide traps
Segments of proteins with high β-strand propensity can self-associate to form amyloid fibrils
implicated in many diseases. We describe a general approach to bind such segments in β …
implicated in many diseases. We describe a general approach to bind such segments in β …
Self-replication of Aβ42 aggregates occurs on small and isolated fibril sites
Self-replication of amyloid fibrils via secondary nucleation is an intriguing physicochemical
phenomenon in which existing fibrils catalyze the formation of their own copies. The …
phenomenon in which existing fibrils catalyze the formation of their own copies. The …
[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 …
Surface-functionalized SERS platform for deep learning-assisted diagnosis of Alzheimer's disease
M Kim, S Huh, HJ Park, SH Cho, MY Lee, S Jo… - Biosensors and …, 2024 - Elsevier
Early diagnosis of Alzheimer's disease is crucial to stall the deterioration of brain function,
but conventional diagnostic methods require complicated analytical procedures or inflict …
but conventional diagnostic methods require complicated analytical procedures or inflict …
The role of shear forces in primary and secondary nucleation of amyloid fibrils
E Axell, J Hu, M Lindberg, AJ Dear… - Proceedings of the …, 2024 - National Acad Sciences
Shear forces affect self-assembly processes ranging from crystallization to fiber formation.
Here, the effect of mild agitation on amyloid fibril formation was explored for four peptides …
Here, the effect of mild agitation on amyloid fibril formation was explored for four peptides …
Growth kinetics of amyloid-like fibrils: An integrated atomistic simulation and continuum theory approach
Amyloid fibrils have long been associated with many neurodegenerative diseases. The
conventional picture of the formation and proliferation of fibrils from unfolded proteins …
conventional picture of the formation and proliferation of fibrils from unfolded proteins …