ArticleScientific reports2016
Structure of ring-shaped Aβ₄₂ oligomers determined by conformational selection.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Targeting Iron Responsive Elements (IREs) of APP mRNA into Novel Therapeutics to Control the Translation of Amyloid-β Precursor Protein in Alzheimer's Disease.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer's Disease, Parkinson's Disease and Prionopathies.International journal of molecular sciences · 2024Review
- Survey of the Aβ-peptide structural diversity: molecular dynamics approaches.Biophysical reviews · 2024Review
- Hairpin trimer transition state of amyloid fibril.Nature communications · 2024Article
- Amyloid beta 42 alters cardiac metabolism and impairs cardiac function in male mice with obesity.Nature communications · 2024Article
- The Effect of Ethanol on Disassembly of Amyloid-βInternational journal of molecular sciences · 2022Article
- The Different Faces of the TDP-43 Low-Complexity Domain: The Formation of Liquid Droplets and Amyloid Fibrils.International journal of molecular sciences · 2021Review
- β-amyloid redirects norepinephrine signaling to activate the pathogenic GSK3β/tau cascade.Science translational medicine · 2020Article
- Modulation of Amyloid-β42 Conformation by Small Molecules Through Nonspecific Binding.Journal of chemical theory and computation · 2019Article
- Atomistic investigation of an Iowa Amyloid-β trimer in aqueous solution.RSC advances · 2018Article
- Residue-Specific Dynamics and Local Environmental Changes in Aβ40 Oligomer and Fibril Formation.Angewandte Chemie (International ed. in English) · 2018Article
- Initial Structural Models of the Aβ42 Dimer from Replica Exchange Molecular Dynamics Simulations.ACS omega · 2017Article
- Amyloid beta: structure, biology and structure-based therapeutic development.Acta pharmacologica Sinica · 2017Review
- Fluorescence correlation spectroscopy reveals a cooperative unfolding of monomeric amyloid-β 42 with a low Gibbs free energy.Scientific reports · 2017Article
- Article
- Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer's Disease Immunotherapy.Drugs & aging · 2016Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The oligomerization of amyloid beta (Aβ) peptides into soluble non-fibrillar species plays a critical role in the pathogenesis of Alzheimer's disease. However, it has been challenging to characterize the tertiary and quaternary structures of Aβ peptides due to their disordered nature and high aggregation propensity. In this work, replica exchange molecular dynamics simulations were used to explore the conformational space of Aβ42 monomer. Among the most populated transient states, we identified a particular conformation which was able to generate ring-shaped pentamers and hexamers, when docked onto itself. The structures of these aggregates were stable during microsecond all-atom MD simulations in explicit solvent. In addition to high resolution models of these oligomers, this study provides support for the conformational selection mechanism of Aβ peptide self-assembly.
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