Evidence map›Paper›PMID 37596282›Full record

ArticleNature communications2023

Reactivated endogenous retroviruses promote protein aggregate spreading.

Shu Liu, Stefanie-Elisabeth Heumüller, André Hossinger, Stephan A Müller, Oleksandra Buravlova, Stefan F Lichtenthaler, Philip Denner, Ina M Vorberg

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Review
  7. ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  8. Review
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  10. Article
  11. Article
  12. Review
  13. Article
  14. Widespread transposable element dysregulation in human aging brains with Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024
    Article
  15. Article
  16. Microorganisms · 2024
    Review
  17. Review
  18. Review
  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

8 authors at 3 institutions in 1 country.

Shu Liu *German Center for Neurodegenerative Diseases Bonn (DZNE), Venusberg Campus 1/ 99, 53127, Bonn, Germany.
Stefanie-Elisabeth Heumüller *German Center for Neurodegenerative Diseases Bonn (DZNE), Venusberg Campus 1/ 99, 53127, Bonn, Germany.
André HossingerGerman Center for Neurodegenerative Diseases Bonn (DZNE), Venusberg Campus 1/ 99, 53127, Bonn, Germany.
Stephan A MüllerGerman Center for Neurodegenerative Diseases (DZNE), Munich, Germany.ORCID http://orcid.org/0000-0003-3414-307X
Oleksandra BuravlovaGerman Center for Neurodegenerative Diseases Bonn (DZNE), Venusberg Campus 1/ 99, 53127, Bonn, Germany.
Stefan F LichtenthalerGerman Center for Neurodegenerative Diseases (DZNE), Munich, Germany.ORCID http://orcid.org/0000-0003-2211-2575
Philip DennerGerman Center for Neurodegenerative Diseases Bonn (DZNE), Venusberg Campus 1/ 99, 53127, Bonn, Germany.
Ina M VorbergGerman Center for Neurodegenerative Diseases Bonn (DZNE), Venusberg Campus 1/ 99, 53127, Bonn, Germany. ina.vorberg@dzne.de.ORCID http://orcid.org/0000-0003-0583-4015
German Center for Neurodegenerative Diseases · DEFederal Institute for Risk Assessment · DEUniversity of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prion-like spreading of protein misfolding is a characteristic of neurodegenerative diseases, but the exact mechanisms of intercellular protein aggregate dissemination remain unresolved. Evidence accumulates that endogenous retroviruses, remnants of viral germline infections that are normally epigenetically silenced, become upregulated in neurodegenerative diseases such as amyotrophic lateral sclerosis and tauopathies. Here we uncover that activation of endogenous retroviruses affects prion-like spreading of proteopathic seeds. We show that upregulation of endogenous retroviruses drastically increases the dissemination of protein aggregates between cells in culture, a process that can be inhibited by targeting the viral envelope protein or viral protein processing. Human endogenous retrovirus envelopes of four different clades also elevate intercellular spreading of proteopathic seeds, including pathological Tau. Our data support a role of endogenous retroviruses in protein misfolding diseases and suggest that antiviral drugs could represent promising candidates for inhibiting protein aggregate spreading.

Indexed as

Amyotrophic Lateral SclerosisEndogenous RetrovirusesPrionsAntiviral AgentsHumansProtein AggregatesAntiviral AgentsPrionsProtein Aggregates

Identifiers

PMID37596282
PMCPMC10439213
OpenAlexW4385971153

What Socratic 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 Socratic graph.