Evidence map›Paper›PMID 24871041›Full record

ArticleNature communications2014

Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.

Giuliana Fusco, Alfonso De Simone, Tata Gopinath, Vitaly Vostrikov, Michele Vendruscolo, Christopher M Dobson, Gianluigi Veglia

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 268 papers.

0numbers the graph read from it
0cells of the map it votes in
268citing papers in PubMed
17.8field-weighted citation impact, top 1% of its field
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

268 citing papers in PubMed, 466 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. bioRxiv : the preprint server for biology · 2026
    Article
  18. Article
  19. In situ NMR and integrative proteomics reveal the interaction signature of serum α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  20. Article

208 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

7 authors at 3 institutions in 2 countries.

Giuliana FuscoDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Alfonso De SimoneDepartment of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, UK.
Tata GopinathDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 6-155 Jackson Hall 321 Church street SE, Minneapolis, Minnesota 55455, USA.
Vitaly VostrikovDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 6-155 Jackson Hall 321 Church street SE, Minneapolis, Minnesota 55455, USA.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Gianluigi Veglia1] Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, 6-155 Jackson Hall 321 Church street SE, Minneapolis, Minnesota 55455, USA [2] Department of Chemistry, University of Minnesota, 6-155 Jackson Hall 321 Church street SE, Minneapolis, Minnesota 55455, USA.
University of Cambridge · GBUniversity of Minnesota · USImperial College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H003843/1Medical Research Council G1002272Parkinson's UK H-1103Wellcome Trust 094425
6 · The paper itself

Abstract

α-synuclein (αS) is a protein involved in neurotransmitter release in presynaptic terminals, and whose aberrant aggregation is associated with Parkinson's disease. In dopaminergic neurons, αS exists in a tightly regulated equilibrium between water-soluble and membrane-associated forms. Here we use a combination of solid-state and solution NMR spectroscopy to characterize the conformations of αS bound to lipid membranes mimicking the composition and physical properties of synaptic vesicles. The study shows three αS regions possessing distinct structural and dynamical properties, including an N-terminal helical segment having a role of membrane anchor, an unstructured C-terminal region that is weakly associated with the membrane and a central region acting as a sensor of the lipid properties and determining the affinity of αS membrane binding. Taken together, our data define the nature of the interactions of αS with biological membranes and provide insights into their roles in the function of this protein and in the molecular processes leading to its aggregation.

Indexed as

alpha-SynucleinCell MembraneLipid BilayersLipidsMagnetic Resonance SpectroscopyModels, BiologicalProtein BindingProtein Structure, SecondaryUnilamellar Liposomesalpha-SynucleinLipid BilayersLipidsUnilamellar Liposomes

Identifiers

PMID24871041
PMCPMC4046108
OpenAlexW2121937669

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.