Evidence map›Paper›PMID 37188797›Full record

ArticleCommunications biology2023

α-Synuclein fibril and synaptic vesicle interactions lead to vesicle destruction and increased lipid-associated fibril uptake into iPSC-derived neurons.

Amberley D Stephens, Ana Fernandez Villegas, Chyi Wei Chung, Oliver Vanderpoorten, Dorothea Pinotsi, Ioanna Mela, Edward Ward, Thomas M McCoy, Robert Cubitt, Alexander F Routh and 2 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Global kinetic model of lipid-inducedProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Residues 2 to 7 of α-synuclein regulate amyloid formation via lipid-dependent and lipid-independent pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Review
  9. Frontiers in molecular neuroscience · 2024
    Review
  10. Article
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

12 authors at 3 institutions in 4 countries.

Amberley D StephensDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK. asd.stephens@gmail.com.ORCID 0000-0002-7303-6392
Ana Fernandez VillegasDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.ORCID 0000-0002-9766-8722
Chyi Wei ChungDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.ORCID 0000-0003-1780-3486
Oliver VanderpoortenDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.
Dorothea PinotsiScientific Center for Optical and Electron Microscopy, ETH Zürich, Zürich, Switzerland.
Ioanna MelaDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.
Edward WardDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.ORCID 0000-0002-9078-9716
Thomas M McCoyDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.
Robert CubittInstitut Laue-Langevin, Grenoble, France.
Alexander F RouthDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.
Clemens F KaminskiDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK.ORCID 0000-0002-5194-0962
Gabriele S Kaminski SchierleDepartment of Chemical Engineering and Biotechnology, University of Cambridge, Cambridge, UK. gsk20@cam.ac.uk.ORCID 0000-0002-1843-2202
University of Cambridge · GBETH Zurich · CHInstitut Laue-Langevin · FR

Funding

Medical Research Council G0902243Medical Research Council MR/K02292X/1Wellcome TrustWellcome Trust 065807/Z/01/ZWellcome Trust 203249/Z/16/Z
6 · The paper itself

Abstract

Monomeric alpha-synuclein (aSyn) is a well characterised protein that importantly binds to lipids. aSyn monomers assemble into amyloid fibrils which are localised to lipids and organelles in insoluble structures found in Parkinson's disease patient's brains. Previous work to address pathological aSyn-lipid interactions has focused on using synthetic lipid membranes, which lack the complexity of physiological lipid membranes. Here, we use physiological membranes in the form of synaptic vesicles (SV) isolated from rodent brain to demonstrate that lipid-associated aSyn fibrils are more easily taken up into iPSC-derived cortical i

Indexed as

alpha-SynucleinInduced Pluripotent Stem CellsAnimalsLipidsNeuronsRodentiaSynaptic Vesiclesalpha-SynucleinLipids

Identifiers

PMID37188797
PMCPMC10185682
OpenAlexW4376642954

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.