Evidence map›Paper›PMID 30938443›Full record

ReviewBrain : a journal of neurology2019

The debated toxic role of aggregated TDP-43 in amyotrophic lateral sclerosis: a resolution in sight?

Rudolf C Hergesheimer, Anna A Chami, Denis Reis de Assis, Patrick Vourc'h, Christian R Andres, Philippe Corcia, Débora Lanznaster, Hélène Blasco

Abstract readReview
In one paragraph

Review in Brain : a journal of neurology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
17.7field-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

110 citing papers in PubMed, 201 citations in OpenAlex.

  1. Review
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  3. Review
  4. RNArchitects: how hnRNPs shape neuronal landscapes.Brain : a journal of neurology · 2026
    Review
  5. Article
  6. Article
  7. Review
  8. Antibody targeting TDP-43 mitigates pathogenic pathways induced by the cerebrospinal fluid of ALS.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Article
  9. A single dose of a vectorized mAb targeting TDP-43 potently inhibits the neuropathology in a model of ALS/FTD.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
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  19. Review
  20. Article

50 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

8 authors at 1 institution in 1 country.

Rudolf C HergesheimerUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Anna A ChamiUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Denis Reis de AssisUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Patrick Vourc'hUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Christian R AndresUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Philippe CorciaUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Débora LanznasterUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Hélène BlascoUMR 1253, iBRAIN, Université de Tours, INSERM, Tours, France.
Université de Tours · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transactive response DNA-binding protein-43 (TDP-43) is an RNA/DNA binding protein that forms phosphorylated and ubiquitinated aggregates in the cytoplasm of motor neurons in amyotrophic lateral sclerosis, which is a hallmark of this disease. Amyotrophic lateral sclerosis is a neurodegenerative condition affecting the upper and lower motor neurons. Even though the aggregative property of TDP-43 is considered a cornerstone of amyotrophic lateral sclerosis, there has been major controversy regarding the functional link between TDP-43 aggregates and cell death. In this review, we attempt to reconcile the current literature surrounding this debate by discussing the results and limitations of the published data relating TDP-43 aggregates to cytotoxicity, as well as therapeutic perspectives of TDP-43 aggregate clearance. We point out key data suggesting that the formation of TDP-43 aggregates and the capacity to self-template and propagate among cells as a 'prion-like' protein, another pathological property of TDP-43 aggregates, are a significant cause of motor neuronal death. We discuss the disparities among the various studies, particularly with respect to the type of models and the different forms of TDP-43 used to evaluate cellular toxicity. We also examine how these disparities can interfere with the interpretation of the results pertaining to a direct toxic effect of TDP-43 aggregates. Furthermore, we present perspectives for improving models in order to better uncover the toxic role of aggregated TDP-43. Finally, we review the recent studies on the enhancement of the cellular clearance mechanisms of autophagy, the ubiquitin proteasome system, and endocytosis in an attempt to counteract TDP-43 aggregation-induced toxicity. Altogether, the data available so far encourage us to suggest that the cytoplasmic aggregation of TDP-43 is key for the neurodegeneration observed in motor neurons in patients with amyotrophic lateral sclerosis. The corresponding findings provide novel avenues toward early therapeutic interventions and clinical outcomes for amyotrophic lateral sclerosis management.

Indexed as

Amyotrophic Lateral SclerosisAnimalsAutophagyCell DeathCytoplasmDNA-Binding ProteinsHumansProtein AggregatesDNA-Binding ProteinsProtein AggregatesTARDBP protein, humanaggregationALSneurodegenerationTDP-43therapeutics

Identifiers

PMID30938443
PMCPMC6487324
OpenAlexW2928985673

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.