Evidence map›Paper›PMID 38324572›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

Modulation of α-synuclein in vitro aggregation kinetics by its alternative splice isoforms.

Alexander Röntgen, Zenon Toprakcioglu, James E Tomkins, Michele Vendruscolo

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
7.4field-weighted citation impact, top 2% 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

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. Protein rheostasis: quality control in metastable proteomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Amyloid-β modulates the phase separation and aggregation of α-synuclein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Amyloid formation of alternatively spliced variants of α-synuclein.Protein science : a publication of the Protein Society · 2025
    Article
  16. Article
  17. Liquid-liquid phase separation and conformational strains ofFrontiers in molecular neuroscience · 2024
    Review
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

4 authors at 1 institution in 2 countries.

Alexander RöntgenCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Zenon ToprakciogluCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
James E TomkinsCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0003-3010-6634
Michele VendruscoloCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-3616-1610
University of Cambridge · GB

Funding

EC | ERC | HORIZON EUROPE European Research Council (ERC) 956977UK Research and Innovation (UKRI) 10059436UK Research and Innovation (UKRI) 10061100University of Cambridge | Pembroke College, University of Cambridge (Pembroke) Ron Thomson Research Fellowship
6 · The paper itself

Abstract

The misfolding and aggregation of α-synuclein is linked to a family of neurodegenerative disorders known as synucleinopathies, the most prominent of which is Parkinson's disease (PD). Understanding the aggregation process of α-synuclein from a mechanistic point of view is thus of key importance.

Indexed as

Parkinson DiseaseSynucleinopathiesalpha-SynucleinHumansKineticsProtein Isoformsalpha-SynucleinProtein Isoformsalpha-synucleinproteoformssplice isoforms

Identifiers

PMID38324572
PMCPMC10873642
OpenAlexW4391594219

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.