The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Structural and functional characterization of two alpha-synuclein strains
Open accessAbstract
α-synuclein aggregation is implicated in a variety of diseases including Parkinson’s disease, dementia with Lewy bodies, pure autonomic failure and multiple system atrophy. The association of protein aggregates made of a single protein with a variety of clinical phenotypes has been explained for prion diseases by the existence of different strains that propagate through the infection pathway. Here we structurally and functionally characterize two polymorphs of α-synuclein. We present evidence that the two forms indeed fulfil the molecular criteria to be identified as two strains of α-synuclein. Specifically, we show that the two strains have different structures, levels of toxicity, and in vitro and in vivo seeding and propagation properties. Such strain differences may account for differences in disease progression in different individuals/cell types and/or types of synucleinopathies. α-synuclein is implicated in neurodegenerative diseases. Bousset et al. generate two α-synuclein polymorphs and find differences in aggregation, function and toxicity, suggesting that these altered properties may be the cause for differences in disease progression.
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Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
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α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
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Self-citationDistinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
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A new era for understanding amyloid structures and disease
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Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
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Metadata
- Authors
- Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Olieric, V., Böckmann, A., Meier, B. H., & Melki, R.
- Venue
- Nature Communications
- Published
- 2013-10-10
- Volume
- 4
- Issue
- 1
- Pages
- 2575-2575
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2158089391
- Cited by
- 909
- References
- 50
- FWCI
- 32.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Bousset, L., Pieri, L., Ruiz-Arlandis, G., Gath, J., Jensen, P. H., Habenstein, B., Madiona, K., Olieric, V., Böckmann, A., Meier, B. H., & Melki, R. (2013). Structural and functional characterization of two alpha-synuclein strains. Nature Communications. https://doi.org/10.1038/ncomms3575
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