Evidence map›Paper›PMID 34860005›Full record

ArticleACS chemical neuroscience2022

Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation.

Slav A Semerdzhiev, Mohammad A A Fakhree, Ine Segers-Nolten, Christian Blum, Mireille M A E Claessens

Open access · greenAbstract read
In one paragraph

Article in ACS chemical neuroscience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed, 1 pooled it
11.8field-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

92 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Cellular and systemic modifiers of alpha-synuclein proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
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  11. Article
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  13. Article
  14. Modulation of AβJournal of chemical information and modeling · 2025
    Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. iPSC-derived human cortical organoids display profound alterations of cellular homeostasis following SARS-CoV-2 infection and Spike protein exposure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article

32 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

5 authors at 1 institution in 1 country.

Slav A SemerdzhievNanobiophysics, MESA+ Institute for Nanotechnology, Faculty of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.ORCID 0000-0002-7594-0641
Mohammad A A FakhreeNanobiophysics, MESA+ Institute for Nanotechnology, Faculty of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.ORCID 0000-0002-8559-1377
Ine Segers-NoltenNanobiophysics, MESA+ Institute for Nanotechnology, Faculty of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.
Christian BlumNanobiophysics, MESA+ Institute for Nanotechnology, Faculty of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.ORCID 0000-0002-6524-2495
Mireille M A E ClaessensNanobiophysics, MESA+ Institute for Nanotechnology, Faculty of Science and Technology, University of Twente, P.O. Box 217, 7500 AE Enschede, The Netherlands.ORCID 0000-0002-2206-4422
University of Twente · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

First cases that point at a correlation between SARS-CoV-2 infections and the development of Parkinson's disease (PD) have been reported. Currently, it is unclear if there is also a direct causal link between these diseases. To obtain first insights into a possible molecular relation between viral infections and the aggregation of α-synuclein protein into amyloid fibrils characteristic for PD, we investigated the effect of the presence of SARS-CoV-2 proteins on α-synuclein aggregation. We show, in test tube experiments, that SARS-CoV-2 spike protein (S-protein) has no effect on α-synuclein aggregation, while SARS-CoV-2 nucleocapsid protein (N-protein) considerably speeds up the aggregation process. We observe the formation of multiprotein complexes and eventually amyloid fibrils. Microinjection of N-protein in SH-SY5Y cells disturbed the α-synuclein proteostasis and increased cell death. Our results point toward direct interactions between the N-protein of SARS-CoV-2 and α-synuclein as molecular basis for the observed correlation between SARS-CoV-2 infections and Parkinsonism.

Indexed as

alpha-SynucleinAmyloidCoronavirus Nucleocapsid ProteinsCOVID-19HumansPhosphoproteinsSARS-CoV-2Spike Glycoprotein, Coronavirusalpha-SynucleinAmyloidCoronavirus Nucleocapsid Proteinsnucleocapsid phosphoprotein, SARS-CoV-2PhosphoproteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2amyloidsCovid-19neurodegenerationParkinson’s diseaseprotein aggregationSARS-CoV-2

Identifiers

PMID34860005
PMCPMC8739828
OpenAlexW3215083090

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.