The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Structure–neurotoxicity relationships of amyloid β-protein oligomers
Open accessAbstract
Amyloid β-protein (Aβ) oligomers may be the proximate neurotoxins in Alzheimer's disease (AD). “Oligomer” is an ill-defined term because many kinds have been reported and they often exist in rapid equilibrium with monomers and higher-order assemblies. We report here results of studies in which specific oligomers have been stabilized structurally, fractionated in pure form, and then studied by using a combination of CD spectroscopy, Thioflavin T fluorescence, EM, atomic force microscopy (AFM), and neurotoxicity assays. Aβ monomers were largely unstructured, but oligomers exhibited order-dependent increases in β-sheet content. EM and AFM data suggest that dimerization and subsequent monomer addition are processes in which significant and asymmetric monomer conformational changes occur. Oligomer secondary structure and order correlated directly with fibril nucleation activity. Neurotoxic activity increased disproportionately (order dependence >1) with oligomer order. The structure–activity correlations reported here significantly extend our understanding of the conformational dynamics, structure, and relative toxicity of pure Aβ oligomers of specific order.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
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“We note that, apart from its minor amount, the fiber component would be of lesser importance since its toxicity is lower than that of oligomers (Klein et al., 2004; Ono et al., 2009).”
BackgroundResult
Metadata
- Authors
- Ono, K., Condron, M. M., & Teplow, D. B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-09
- Volume
- 106
- Issue
- 35
- Pages
- 14745-14750
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2015640782
- Cited by
- 770
- References
- 32
- FWCI
- 32.28
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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