ArticleThe Journal of biological chemistry2014
Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Convergence of neuroinflammation across major neurotropic viral exposomes in AD and ADRD.Journal of neuroinflammation · 2026Review
- The role of probiotics, prebiotics, and postbiotics: cellular and molecular pathways activated on glial cells in Alzheimer's disease.Frontiers in neuroscience · 2025Review
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- EPR Studies of Aβ42 Oligomers Indicate a Parallel In-Register β-Sheet Structure.ACS chemical neuroscience · 2024Article
- Sugar distributions on gangliosides guide the formation and stability of amyloid-β oligomers.Biophysical chemistry · 2023Article
- Article
- Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides.Biochemistry · 2022Article
- Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils.The Journal of chemical physics · 2021Article
- Amyloid Prefibrillar Oligomers: The Surprising Commonalities in Their Structure and Activity.International journal of molecular sciences · 2021Review
- Segmental structural dynamics in Aβ42 globulomers.Biochemical and biophysical research communications · 2021Article
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- Inhibition of Amyloid β-Induced Lipid Membrane Permeation and Amyloid β Aggregation by K162.ACS chemical neuroscience · 2021Article
- Characterization of Homogeneous and Heterogeneous Amyloid-β42 Oligomer Preparations with Biochemical Methods and Infrared Spectroscopy Reveals a Correlation between Infrared Spectrum and Oligomer Size.ACS chemical neuroscience · 2021Article
- Biophysical characteristics of lipid-induced Aβ oligomers correlate to distinctive phenotypes in transgenic mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Distinguishing the Effect on the Rate and Yield of Aβ42 Aggregation by Green Tea Polyphenol EGCG.ACS omega · 2020Article
- High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease.Chemical communications (Cambridge, England) · 2020Review
- NMR-based site-resolved profiling of β-amyloid misfolding reveals structural transitions from pathologically relevant spherical oligomer to fibril.The Journal of biological chemistry · 2020Article
- Molecular interactions between monoclonal oligomer-specific antibody 5E3 and its amyloid beta cognates.PloS one · 2020Article
- Aβ42 fibril formation from predominantly oligomeric samples suggests a link between oligomer heterogeneity and fibril polymorphism.Royal Society open science · 2019Article
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Authors and funding
6 authors.
Funding
Abstract
Aβ42 oligomers play key roles in the pathogenesis of Alzheimer disease, but their structures remain elusive partly due to their transient nature. Here, we show that Aβ42 in a fusion construct can be trapped in a stable oligomer state, which recapitulates characteristics of prefibrillar Aβ42 oligomers and enables us to establish their detailed structures. Site-directed spin labeling and electron paramagnetic resonance studies provide structural restraints in terms of side chain mobility and intermolecular distances at all 42 residue positions. Using these restraints and other biophysical data, we present a novel atomic-level oligomer model. In our model, each Aβ42 protein forms a single β-sheet with three β-strands in an antiparallel arrangement. Each β-sheet consists of four Aβ42 molecules in a head-to-tail arrangement. Four β-sheets are packed together in a face-to-back fashion. The stacking of identical segments between different β-sheets within an oligomer suggests that prefibrillar oligomers may interconvert with fibrils via strand rotation, wherein β-strands undergo an ∼90° rotation along the strand direction. This work provides insights into rational design of therapeutics targeting the process of interconversion between toxic oligomers and non-toxic fibrils.
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