Evidence map›Paper›PMID 29969391›Full record

ArticleeLife2018

Cryo-EM structure of alpha-synuclein fibrils.

Ricardo Guerrero-Ferreira, Nicholas Mi Taylor, Daniel Mona, Philippe Ringler, Matthias E Lauer, Roland Riek, Markus Britschgi, Henning Stahlberg

Abstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 345 papers.

0numbers the graph read from it
0cells of the map it votes in
345citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

345 citing papers in PubMed.

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  8. Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026
    Article
  9. PET imaging of alpha-synuclein: from radiotracer design through in vitro and in vivo translation.European journal of nuclear medicine and molecular imaging · 2026
    Review
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  15. bioRxiv : the preprint server for biology · 2026
    Article
  16. Article
  17. Review
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  19. Review
  20. Article

285 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Ricardo Guerrero-FerreiraCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Basel, Switzerland.ORCID http://orcid.org/0000-0002-3664-8277
Nicholas Mi TaylorCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Basel, Switzerland.ORCID https://orcid.org/0000-0003-0761-4921
Daniel MonaRoche Pharma Research and Early Development, Neuroscience, Ophthalmology and Rare Diseases Discovery and Translational Area/Neuroscience Discovery, Roche Innovation Center Basel, Basel, Switzerland.
Philippe RinglerCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Basel, Switzerland.ORCID https://orcid.org/0000-0003-4346-5089
Matthias E LauerRoche Pharma Research and Early Development, Chemical Biology, Roche Innovation Center Basel, Basel, Switzerland.ORCID https://orcid.org/0000-0003-3252-8718
Roland RiekLaboratory of Physical Chemistry, ETH Zürich, Zürich, Switzerland.
Markus BritschgiRoche Pharma Research and Early Development, Neuroscience, Ophthalmology and Rare Diseases Discovery and Translational Area/Neuroscience Discovery, Roche Innovation Center Basel, Basel, Switzerland.ORCID http://orcid.org/0000-0001-6151-4257
Henning StahlbergCenter for Cellular Imaging and NanoAnalytics, Biozentrum, University of Basel, Basel, Switzerland.ORCID http://orcid.org/0000-0002-1185-4592

Funding

Swiss National Science Foundation CRSII3_154461Swiss National Science Foundation CRSII3_154461 and CRSII5_177195Swiss National Science Foundation CRSII5_177195
6 · The paper itself

Abstract

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.

Indexed as

Cryoelectron Microscopyalpha-SynucleinAmino Acid SequenceHumansHydrophobic and Hydrophilic InteractionsModels, MolecularMutationParkinson Diseasealpha-Synucleinalpha-synucleincryo-electron microscopyE. colifibrilhumanmolecular biophysicsneurodegenerationneuroscienceParkinson's diseasestructural biology

Identifiers

PMID29969391
PMCPMC6092118

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.