Evidence map›Paper›PMID 35383280›Full record

ArticleCommunications biology2022

Cell environment shapes TDP-43 function with implications in neuronal and muscle disease.

Urša Šušnjar, Neva Škrabar, Anna-Leigh Brown, Yasmine Abbassi, Hemali Phatnani, NYGC ALS Consortium, Andrea Cortese, Cristina Cereda, Enrico Bugiardini, Rosanna Cardani and 7 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
5.8field-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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.

  1. Proteome-wide Mendelian randomization identifies causal plasma proteins in frontotemporal dementia.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Pooled it
  2. Article
  3. Review
  4. Neuronal TDP-43 regulates myelin formation via neurexin 1 mRNA stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Aberrant Splicing Signatures Underpin Oligodendrocyte Damage in ALS and Neuron Loss in FTD.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. TDP-43 Cryptic RNAs in Perry Syndrome: Differences across Brain Regions and TDP-43 Proteinopathies.Movement disorders : official journal of the Movement Disorder Society · 2025
    Article
  16. Article
  17. TDP-43-mediated amyotrophic lateral sclerosis: new/hidden insights fromFrontiers in cell and developmental biology · 2025
    Article
  18. Review
  19. Review
  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

17 authors at 20 institutions in 7 countries.

Urša ŠušnjarMolecular Pathology Lab, International Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy.
Neva ŠkrabarTumour Virology Lab, International Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy.
Anna-Leigh BrownDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.
Yasmine AbbassiMolecular Pathology Lab, International Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy.
Hemali PhatnaniCenter for Genomics of Neurodegenerative Disease, New York Genome Center, New York, USA.
NYGC ALS Consortium
Andrea CorteseDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.
Cristina CeredaGenomic and post-Genomic Unit, IRCCS Mondino Foundation, Pavia, Italy.
Enrico BugiardiniDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.
Rosanna CardaniBioCor Biobank, UOC SMEL-1 of Clinical Pathology, IRCCS-Policlinico San Donato, San Donato Milanese, Italy.
Giovanni MeolaDepartment of Biomedical Sciences for Health, University of Milan, Milan, Italy.
Michela RipoloneNeuromuscular and Rare Diseases Unit, Department of Neuroscience, Fondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico, Milan, Italy.
Maurizio MoggioNeuromuscular and Rare Diseases Unit, Department of Neuroscience, Fondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico, Milan, Italy.
Maurizio RomanoDepartment of Life Sciences, University of Trieste, Trieste, Italy.ORCID http://orcid.org/0000-0002-4820-2897
Maria SecrierUCL Genetics Institute, Department of Genetics, Evolution and Environment, University College London, London, UK.ORCID http://orcid.org/0000-0003-2758-1741
Pietro FrattaDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.ORCID http://orcid.org/0000-0002-8762-8188
Emanuele BurattiMolecular Pathology Lab, International Centre for Genetic Engineering and Biotechnology (ICGEB), Trieste, Italy. buratti@icgeb.org.ORCID http://orcid.org/0000-0002-1356-9074
National Hospital for Neurology and Neurosurgery · GBHarvard University · USIcahn School of Medicine at Mount Sinai · USInternational Centre for Genetic Engineering and Biotechnology · ITPennsylvania State University · USUniversity of Pennsylvania · USCedars-Sinai Medical Center · USColumbia University · USFondazione IRCCS Ca' Granda Ospedale Maggiore Policlinico · ITMRC Centre for Regenerative Medicine · GBNew York Genome Center · USTemple University · USUniversity of California, San Francisco · USAllen Institute for Brain Science · USAmsterdam UMC Location University of Amsterdam · NLBarrow Neurological Institute · USBrigham and Women's Hospital · USBroad Institute · USChildren's Hospital of Philadelphia · USCold Spring Harbor Laboratory · US

Funding

Medical Research Council MC_PC_MR/S022708/1Medical Research Council MR/S006508/1Medical Research Council MR/T001712/1Medical Research Council MR/W005190/1Motor Neurone Disease Association MALASPINA/APR13/817-791
6 · The paper itself

Abstract

TDP-43 (TAR DNA-binding protein 43) aggregation and redistribution are recognised as a hallmark of amyotrophic lateral sclerosis and frontotemporal dementia. As TDP-43 inclusions have recently been described in the muscle of inclusion body myositis patients, this highlights the need to understand the role of TDP-43 beyond the central nervous system. Using RNA-seq, we directly compare TDP-43-mediated RNA processing in muscle (C2C12) and neuronal (NSC34) mouse cells. TDP-43 displays a cell-type-characteristic behaviour targeting unique transcripts in each cell-type, which is due to characteristic expression of RNA-binding proteins, that influence TDP-43's performance and define cell-type specific splicing. Among splicing events commonly dysregulated in both cell lines, we identify some that are TDP-43-dependent also in human cells. Inclusion levels of these alternative exons are altered in tissues of patients suffering from FTLD and IBM. We therefore propose that TDP-43 dysfunction contributes to disease development either in a common or a tissue-specific manner.

Indexed as

Amyotrophic Lateral SclerosisFrontotemporal DementiaAnimalsDNA-Binding ProteinsHumansMiceMusclesRNA SplicingDNA-Binding ProteinsTardbp protein, mouse

Identifiers

PMID35383280
PMCPMC8983780
OpenAlexW4225356316

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.