Evidence map›Paper›PMID 34021258›Full record

ArticleCommunications biology2021

Super-resolution imaging reveals α-synuclein seeded aggregation in SH-SY5Y cells.

Jason C Sang, Eric Hidari, Georg Meisl, Rohan T Ranasinghe, Maria Grazia Spillantini, David Klenerman

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.7field-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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025
    Review
  7. Pathological α-Synuclein Perturbs Nuclear Integrity.bioRxiv : the preprint server for biology · 2025
    Article
  8. α-Synuclein Pathology Spreads in a Midbrain-Hindbrain Assembloid Model.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  9. Article
  10. Single molecule delivery into living cells.Nature communications · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Monitoring α-synuclein aggregation.Neurobiology of disease · 2023
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  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

6 authors at 1 institution in 1 country.

Jason C SangDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-8567-5415
Eric HidariDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-4777-5239
Georg MeislDepartment of Chemistry, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0002-6562-7715
Rohan T RanasingheDepartment of Chemistry, University of Cambridge, Cambridge, UK.
Maria Grazia SpillantiniDepartment of Clinical Neuroscience, University of Cambridge, Cambridge, UK.
David KlenermanDepartment of Chemistry, University of Cambridge, Cambridge, UK. dk10012@cam.ac.uk.ORCID http://orcid.org/0000-0001-7116-6954
University of Cambridge · GB

Funding

Medical Research CouncilParkinson's UK G-1703
6 · The paper itself

Abstract

Aggregation of α-synuclein (α-syn) is closely linked to Parkinson's disease (PD) and the related synucleinopathies. Aggregates spread through the brain during the progression of PD, but the mechanism by which this occurs is still not known. One possibility is a self-propagating, templated-seeding mechanism, but this cannot be established without quantitative information about the efficiencies and rates of the key steps in the cellular process. To address this issue, we imaged the uptake and seeding of unlabeled exogenous α-syn fibrils by SH-SY5Y cells and the resulting secreted aggregates, using super-resolution microscopy. Externally-applied fibrils very inefficiently induced self-assembly of endogenous α-syn in a process accelerated by the proteasome. Seeding resulted in the increased secretion of nanoscopic aggregates (mean 35 nm diameter), of both α-syn and Aβ. Our results suggest that cells respond to seed-induced disruption of protein homeostasis predominantly by secreting nanoscopic aggregates; this mechanism may therefore be an important protective response by cells to protein aggregation.

Indexed as

Protein Aggregatesalpha-SynucleinAmyloidHumansMolecular ImagingNeuroblastomaTumor Cells, Culturedalpha-SynucleinAmyloidProtein AggregatesSNCA protein, human

Identifiers

PMID34021258
PMCPMC8139990
OpenAlexW3163107759

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.