The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Cell-to-cell transmission of non-prion protein aggregates
Open accessAbstract
Neurodegenerative disorders such as Alzheimer disease, Parkinson disease, frontotemporal dementia, Huntington disease and Creutzfeldt–Jakob disease (CJD) are characterized by progressive accumulation of protein aggregates in selected brain regions. Protein misfolding and templated assembly into aggregates might result from an imbalance between protein synthesis, aggregation and clearance. Although protein misfolding and aggregation occur in most neurodegenerative disorders, the concept of spreading and infectivity of aggregates in the CNS has, until now, been confined to prion diseases such as CJD and bovine spongiform encephalopathy. Emerging evidence, however, suggests that prion-like spreading, involving secreted proteins such as amyloid-β and cytosolic proteins such as tau, huntingtin and α-synuclein, can occur in other neurodegenerative disorders. The underlying molecular mechanisms and the therapeutic implications of the new data are discussed in this article.
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Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
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Cited by
The amyloid state and its association with protein misfolding diseases.
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Self-citationα-Synuclein strains cause distinct synucleinopathies after local and systemic administration
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Metadata
- Authors
- Lee, S.-J., Desplats, P., Sigurdson, C., Tsigelny, I., & Masliah, E.
- Venue
- Nature Reviews Neurology
- Published
- 2010-10-12
- Volume
- 6
- Issue
- 12
- Pages
- 702-706
- ISSN
- 1759-4758 (ISSN-L)
- 1759-4766
- OpenAlex
- W2029978572
- Cited by
- 309
- References
- 18
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- green
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