Evidence map›Paper›PMID 32132902›Full record

ArticleFrontiers in molecular neuroscience2020

Chaperone Mediated Autophagy Degrades TDP-43 Protein and Is Affected by TDP-43 Aggregation.

Fernando Ormeño, Juan Hormazabal, José Moreno, Felipe Riquelme, Javiera Rios, Alfredo Criollo, Amelina Albornoz, Iván E Alfaro, Mauricio Budini

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.5field-weighted citation impact, top 5% 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

50 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Article
  3. TMEM106B is a selective modulator of TDP-43 pathology in Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. RNArchitects: how hnRNPs shape neuronal landscapes.Brain : a journal of neurology · 2026
    Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Molecular Visualization of Neuronal TDP43 PathologybioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Article
  17. 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

9 authors at 3 institutions in 1 country.

Fernando OrmeñoDentistry Faculty, Molecular and Cellular Pathology Laboratory, Institute in Dentistry Sciences, University of Chile, Santiago, Chile.
Juan HormazabalLysosome Biology Research Laboratory, Fundación Ciencia y Vida, Santiago, Chile.
José MorenoDentistry Faculty, Molecular and Cellular Pathology Laboratory, Institute in Dentistry Sciences, University of Chile, Santiago, Chile.
Felipe RiquelmeDentistry Faculty, Molecular and Cellular Pathology Laboratory, Institute in Dentistry Sciences, University of Chile, Santiago, Chile.
Javiera RiosDentistry Faculty, Molecular and Cellular Pathology Laboratory, Institute in Dentistry Sciences, University of Chile, Santiago, Chile.
Alfredo CriolloCellular Biology Laboratory, Dentistry Faculty, Institute in Dentistry Sciences, University of Chile, Santiago, Chile.
Amelina AlbornozFundación Ciencia y Vida, Santiago, Chile.
Iván E AlfaroLysosome Biology Research Laboratory, Fundación Ciencia y Vida, Santiago, Chile.
Mauricio BudiniDentistry Faculty, Molecular and Cellular Pathology Laboratory, Institute in Dentistry Sciences, University of Chile, Santiago, Chile.
University of Chile · CLFundación Ciencia and Vida · CLUniversidad del Desarrollo · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TAR DNA binding protein 43 kDa (TDP-43) is a ribonuclear protein regulating many aspects of RNA metabolism. Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Lobar Degeneration (FTLD) are fatal neurodegenerative diseases with the presence of TDP-43 aggregates in neuronal cells. Chaperone Mediated Autophagy (CMA) is a lysosomal degradation pathway participating in the proteostasis of several cytosolic proteins including neurodegenerative associated proteins. In addition, protein oligomers or aggregates can affect the status of CMA. In this work, we studied the relationship between CMA and the physiological and pathological forms of TDP-43. First, we found that recombinant TDP-43 was specifically degraded by rat liver's CMA+ lysosomes and that endogenous TDP-43 is localized in rat brain's CMA+ lysosomes, indicating that TDP-43 can be a CMA substrate

Indexed as

amyotrophic lateral sclerosiscellular modelchaperone mediated autophagylysosomal damageprotein aggregationTARDBP

Identifiers

PMID32132902
PMCPMC7040037
OpenAlexW3006458381

What OpenQuestion holds

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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.