Evidence map›Paper›PMID 37603556›Full record

ArticlePloS one2023

Tau protein aggregation associated with SARS-CoV-2 main protease.

Raphael Josef Eberle, Mônika Aparecida Coronado, Ian Gering, Simon Sommerhage, Karolina Korostov, Anja Stefanski, Kai Stühler, Victoria Kraemer-Schulien, Lara Blömeke, Oliver Bannach and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 16 citations in OpenAlex.

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  9. Reemerging Infectious Diseases and Neuroimmunologic Complications.Neurology(R) neuroimmunology & neuroinflammation · 2025
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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

11 authors at 2 institutions in 1 country.

Raphael Josef EberleInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-8763-3884
Mônika Aparecida CoronadoInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-6518-6497
Ian GeringInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0003-0965-3908
Simon SommerhageInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Karolina KorostovInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Anja StefanskiMolecular Proteomics Laboratory (MPL), BMFZ, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0001-8532-954X
Kai StühlerMolecular Proteomics Laboratory (MPL), BMFZ, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.ORCID 0000-0002-3111-9368
Victoria Kraemer-SchulienInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-7413-7646
Lara BlömekeInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-8861-9224
Oliver BannachInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-7438-3791
Dieter WillboldInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.ORCID 0000-0002-0065-7366
Forschungszentrum Jülich · DEHeinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The primary function of virus proteases is the proteolytic processing of the viral polyprotein. These enzymes can also cleave host cell proteins, which is important for viral pathogenicity, modulation of cellular processes, viral replication, the defeat of antiviral responses and modulation of the immune response. It is known that COVID-19 can influence multiple tissues or organs and that infection can damage the functionality of the brain in multiple ways. After COVID-19 infections, amyloid-β, neurogranin, tau and phosphorylated tau were detected extracellularly, implicating possible neurodegenerative processes. The present study describes the possible induction of tau aggregation by the SARS-CoV-2 3CL protease (3CLpro) possibly relevant in neuropathology. Further investigations demonstrated that tau was proteolytically cleaved by the viral protease 3CL and, consequently, generated aggregates. However, more evidence is needed to confirm that COVID-19 is able to trigger neurodegenerative diseases.

Indexed as

Coronavirus 3C ProteasesCOVID-19Protein Aggregatestau ProteinsEndopeptidasesHumansPeptide HydrolasesSARS-CoV-23C-like proteinase, SARS-CoV-2Coronavirus 3C ProteasesEndopeptidasesPeptide HydrolasesProtein Aggregatestau Proteins

Identifiers

PMID37603556
PMCPMC10441795
OpenAlexW4386022837

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.