The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
Abstract
Recent findings indicate that soluble amyloid oligomers may represent the primary pathologic species in degenerative diseases. These amyloid oligomers share common structural features and the ability to permeabilize membranes, suggesting that they also share a common primary mechanism of pathogenesis. Membrane permeabilization by amyloid oligomers may initiate a common group of downstream pathologic processes, including intracellular calcium dyshomeostasis, production of reactive oxygen species, altered signaling pathways, and mitochondrial dysfunction that represent key effectors of cellular dysfunction and cell death in amyloid-associated degenerative disease, such as sporadic inclusion-body myositis.
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Cites
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
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Self-citationTargeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?
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Molecular pathways to neurodegeneration
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Cited by
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
The Amyloid State of Proteins in Human Diseases
Eisenberg, D., & Jucker, M. (2012) · Cell · doi:10.1016/j.cell.2012.02.022 · Cited by 1,744
A new era for understanding amyloid structures and disease
Iadanza, M. G., Jackson, M. P., Hewitt, E. W., Ranson, N. A., & Radford, S. E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0060-8 · Cited by 980
Reddy, P. H., & Beal, M. F. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.12.002 · Cited by 975
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Metadata
- Authors
- Glabe, C. G., & Kayed, R.
- Venue
- Neurology
- Published
- 2006-01-24
- Volume
- 66
- Issue
- 1_suppl_1
- Pages
- S74-8
- ISSN
- 0028-3878 (ISSN-L)
- 1526-632X
- OpenAlex
- W2138023380
- Cited by
- 367
- References
- 9
- FWCI
- 20.39
- Type
- journal article
- Language
- en
- Open access
- closed
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- Glabe, C. G., & Kayed, R. (2006). Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology. https://doi.org/10.1212/01.wnl.0000192103.24796.42
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
