Evidence map›Paper›PMID 31790267›Full record

ArticleThe journal of physical chemistry letters2019

Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils.

Céline Galvagnion, Daniel Topgaard, Katarzyna Makasewicz, Alexander K Buell, Sara Linse, Emma Sparr, Christopher M Dobson

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Research Priorities on the Role of α-Synuclein in Parkinson's Disease Pathogenesis.Movement disorders : official journal of the Movement Disorder Society · 2024
    Review
  6. 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
  7. Article
  8. Review
  9. Article
  10. Review
  11. Lipid-induced polymorphic amyloid fibril formation by α-synuclein.Protein science : a publication of the Protein Society · 2023
    Article
  12. Article
  13. Morphology-Dependent Interactions between α-Synuclein Monomers and Fibrils.International journal of molecular sciences · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. 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

7 authors at 3 institutions in 4 countries.

Céline GalvagnionCentre for Misfolding Diseases, Department of Chemistry , University of Cambridge , Lensfield Road , Cambridge CB2 1EW , United Kingdom.ORCID http://orcid.org/0000-0001-9753-3310
Daniel TopgaardDivision of Physical Chemistry, Center for Chemistry and Chemical Engineering , Lund University , P.O. Box 124, SE-22100 Lund , Sweden.
Katarzyna MakasewiczDivision of Physical Chemistry, Center for Chemistry and Chemical Engineering , Lund University , P.O. Box 124, SE-22100 Lund , Sweden.
Alexander K BuellDepartment of Biotechnology and Biomedicine, DTU Bioengineering , Technical University of Denmark , Soltofts Plads 227 , DK-2800 Kgs. Lyngby , Denmark.ORCID http://orcid.org/0000-0003-1161-3622
Sara LinseDepartment of Biochemistry and Structural Biology , Lund University , SE-22100 Lund , Sweden.ORCID http://orcid.org/0000-0001-9629-7109
Emma SparrDivision of Physical Chemistry, Center for Chemistry and Chemical Engineering , Lund University , P.O. Box 124, SE-22100 Lund , Sweden.
Christopher M DobsonCentre for Misfolding Diseases, Department of Chemistry , University of Cambridge , Lensfield Road , Cambridge CB2 1EW , United Kingdom.
Lund University · SEUniversity of Cambridge · GBTechnical University of Denmark · DK

Funding

Wellcome Trust
6 · The paper itself

Abstract

The deposition of coassemblies made of the small presynaptic protein, α-synuclein, and lipids in the brains of patients is the hallmark of Parkinson's disease. In this study, we used natural abundance

Indexed as

alpha-SynucleinAmyloidKineticsLipid BilayersMolecular StructurePhase TransitionProtein BindingSerineStructure-Activity RelationshipThermodynamicsTransition Temperaturealpha-SynucleinAmyloidLipid BilayersSerine

Identifiers

PMID31790267
PMCPMC6937551
OpenAlexW2993040260

What OpenQuestion holds

Textmetadata
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.