Evidence map›Paper›PMID 32152117›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Disruption of cellular proteostasis by H1N1 influenza A virus causes α-synuclein aggregation.

Rita Marreiros, Andreas Müller-Schiffmann, Svenja V Trossbach, Ingrid Prikulis, Sebastian Hänsch, Stefanie Weidtkamp-Peters, Ana Raquel Moreira, Shriya Sahu, Irina Soloviev, Suganya Selvarajah and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
10.9field-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

90 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Review
  3. Neurodegenerative and Cognitive Consequences of Long COVID.International journal of molecular sciences · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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  14. Social Reward Learning Deficits and Concordant Brain Alterations in Rats Overexpressing Disrupted-in-Schizophrenia 1 (DISC1).The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Autophagy-Mediated Suppression of Tumor Growth by Food-Grade Lipid Nanoparticles in Mice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  19. Review
  20. Review

30 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

12 authors at 1 institution in 1 country.

Rita MarreirosDepartment Neuropathology, Heinrich Heine University Düsseldorf Medical School, 40225 Düsseldorf, Germany.
Andreas Müller-SchiffmannDepartment Neuropathology, Heinrich Heine University Düsseldorf Medical School, 40225 Düsseldorf, Germany.
Svenja V TrossbachDepartment Neuropathology, Heinrich Heine University Düsseldorf Medical School, 40225 Düsseldorf, Germany.
Ingrid PrikulisDepartment Neuropathology, Heinrich Heine University Düsseldorf Medical School, 40225 Düsseldorf, Germany.ORCID 0000-0003-4330-7187
Sebastian HänschCenter for Advanced Imaging, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Stefanie Weidtkamp-PetersCenter for Advanced Imaging, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.
Ana Raquel MoreiraProsetta Biosciences, San Francisco, CA 94107.
Shriya SahuProsetta Biosciences, San Francisco, CA 94107.
Irina SolovievProsetta Biosciences, San Francisco, CA 94107.
Suganya SelvarajahProsetta Biosciences, San Francisco, CA 94107.
Vishwanath R LingappaProsetta Biosciences, San Francisco, CA 94107.
Carsten KorthDepartment Neuropathology, Heinrich Heine University Düsseldorf Medical School, 40225 Düsseldorf, Germany; ckorth@hhu.de.
Heinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurodegenerative diseases feature specific misfolded or misassembled proteins associated with neurotoxicity. The precise mechanisms by which protein aggregates first arise in the majority of sporadic cases have remained unclear. Likely, a first critical mass of misfolded proteins starts a vicious cycle of a prion-like expansion. We hypothesize that viruses, having evolved to hijack the host cellular machinery for catalyzing their replication, lead to profound disturbances of cellular proteostasis, resulting in such a critical mass of protein aggregates. Here, we investigated the effect of influenza virus (H1N1) strains on proteostasis of proteins associated with neurodegenerative diseases in Lund human mesencephalic dopaminergic cells in vitro and infection of

Indexed as

Proteostasisalpha-SynucleinAnimalsDopaminergic NeuronsFemaleHomeodomain ProteinsHumansInfluenza A Virus, H1N1 SubtypeInfluenza, HumanMiceMice, KnockoutNerve Tissue ProteinsOrthomyxoviridae InfectionsProtein MultimerizationSynucleinopathiesalpha-SynucleinDisc1 protein, mouseHomeodomain ProteinsNerve Tissue ProteinsRAG-1 proteinDISC1influenzaParkinson’s diseaseprotein misfoldingα-synuclein

Identifiers

PMID32152117
PMCPMC7104400
OpenAlexW3012397026

What Socratic 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 Socratic graph.