ArticleJournal of Alzheimer's disease : JAD2014
Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.
Article in Journal of Alzheimer's disease : JAD, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Insights into proton transfer dynamics in histidine tautomers of amyloid-β (1-40).Communications chemistry · 2025Article
- Nucleation dynamics in amyloid-beta dimerization revealed by single-molecule fingerprinting.Cell reports. Physical science · 2025Article
- Production of Distinct Fibrillar, Oligomeric, and Other Aggregation States from Network Models of Multibody Interaction.Journal of chemical theory and computation · 2024Article
- Small Molecule Decoys of Aggregation for Elimination of Aβ-Peptide Toxicity.ACS chemical neuroscience · 2023Article
- Perphenazine-Macrocycle Conjugates Rapidly Sequester the Aβ42 Monomer and Prevent Formation of Toxic Oligomers and Amyloid.ACS chemical neuroscience · 2023Article
- A genome-wide association study in human lymphoblastoid cells supports safety of mitochondrial complex I inhibitor.Mitochondrion · 2021Article
- Differential effect of amyloid beta peptides on mitochondrial axonal trafficking depends on their state of aggregation and binding to the plasma membrane.Neurobiology of disease · 2018Article
- Initial Structural Models of the Aβ42 Dimer from Replica Exchange Molecular Dynamics Simulations.ACS omega · 2017Article
- Article
- Small molecule NPT-440-1 inhibits ionic flux through AβNanomedicine : nanotechnology, biology, and medicine · 2016Article
- Differential protein structural disturbances and suppression of assembly partners produced by nonsense GABRG2 epilepsy mutations: implications for disease phenotypic heterogeneity.Scientific reports · 2016Article
- Reducing Endogenous α-Synuclein Mitigates the Degeneration of Selective Neuronal Populations in an Alzheimer's Disease Transgenic Mouse Model.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2016Article
- Systemic Central Nervous System (CNS)-targeted Delivery of Neuropeptide Y (NPY) Reduces Neurodegeneration and Increases Neural Precursor Cell Proliferation in a Mouse Model of Alzheimer Disease.The Journal of biological chemistry · 2016Article
- The Binding Receptors of Aβ: an Alternative Therapeutic Target for Alzheimer's Disease.Molecular neurobiology · 2016Review
- Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions.ACS chemical neuroscience · 2015Article
- Amyloid β oligomers in Alzheimer's disease pathogenesis, treatment, and diagnosis.Acta neuropathologica · 2015Review
- Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's disease.Frontiers in cellular neuroscience · 2015Review
- Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease.Biochemical pharmacology · 2014Review
- Toxic oligomer species of amyloid-β in Alzheimer's disease, a timing issue.Swiss medical weekly · 2014Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Alzheimer's disease (AD) is associated with the formation of toxic amyloid-β (Aβ)42 oligomers, and recent evidence supports a role for Aβ dimers as building blocks for oligomers. Molecular dynamics simulation studies have identified clans for the dominant conformations of Aβ42 forming dimers; however, it is unclear if a larger spectrum of dimers is involved and which set(s) of dimers might evolve to oligomers verse fibrils. Therefore, for this study we generated multiple structural conformations of Aβ42, using explicit all-atom molecular dynamics, and then clustering the different structures based on key conformational similarities. Those matching a selection threshold were then used to model a process of oligomerization. Remarkably, we showed a greater diversity in Aβ dimers than previously described. Depending on the clan family, different types of Aβ dimers were obtained. While some had the tendency to evolve into oligomeric rings, others formed fibrils of diverse characteristics. Then we selected the dimers that would evolve to membranephilic annular oligomers. Nearly one third of the 28 evaluated annular oligomers had the dimer interfaces between the neighboring Aβ42 monomers with possible salt bridges between the residue K28 from one side and either residue E22 or D23 on the other. Based on these results, key amino acids were identified for point mutations that either enhanced or suppressed the formation and toxicity of oligomer rings. Our studies suggest a greater diversity of Aβ dimers. Understanding the structure of Aβ dimers might be important for the rationale design of small molecules that block formation of toxic oligomers.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.