The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.
Cryo-EM structure of alpha-synuclein fibrils
Open accessAbstract
Parkinson’s disease is a progressive neuropathological disorder that belongs to the class of synucleinopathies, in which the protein alpha-synuclein is found at abnormally high concentrations in affected neurons. Its hallmark are intracellular inclusions called Lewy bodies and Lewy neurites. We here report the structure of cytotoxic alpha-synuclein fibrils (residues 1–121), determined by cryo-electron microscopy at a resolution of 3.4 Å. Two protofilaments form a polar fibril composed of staggered β-strands. The backbone of residues 38 to 95, including the fibril core and the non-amyloid component region, are well resolved in the EM map. Residues 50–57, containing three of the mutation sites associated with familial synucleinopathies, form the interface between the two protofilaments and contribute to fibril stability. A hydrophobic cleft at one end of the fibril may have implications for fibril elongation, and invites for the design of molecules for diagnosis and treatment of synucleinopathies.
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Cites
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Structures of α-synuclein filaments from multiple system atrophy
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Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules
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Metadata
- Authors
- Guerrero-Ferreira, R., Taylor, N. M., Mona, D., Ringler, P., Lauer, M. E., Riek, R., Britschgi, M., & Stahlberg, H.
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2018-07-03
- Volume
- 7
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W2793431243
- Cited by
- 600
- References
- 84
- FWCI
- 38.83
- Type
- journal article
- Language
- en
- Open access
- gold
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- Guerrero-Ferreira, R., Taylor, N. M., Mona, D., Ringler, P., Lauer, M. E., Riek, R., Britschgi, M., & Stahlberg, H. (2018). Cryo-EM structure of alpha-synuclein fibrils. eLife. https://doi.org/10.7554/elife.36402
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