Evidence map›Paper›PMID 33912014›Full record

ArticleFrontiers in cellular neuroscience2021

Nucleolin Rescues TDP-43 Toxicity in Yeast and Human Cell Models.

Caterina Peggion, Maria Lina Massimino, Roberto Stella, Raissa Bortolotto, Jessica Agostini, Arianna Maldi, Geppo Sartori, Fiorella Tonello, Alessandro Bertoli, Raffaele Lopreiato

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cellular neuroscience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Sequestration of TDP-43ACS chemical neuroscience · 2022
    Article
  10. Nucleolin: a cell portal for viruses, bacteria, and toxins.Cellular and molecular life sciences : CMLS · 2022
    Review
  11. Review
  12. Review
  13. Secreted Phospholipases AInternational journal of biological sciences · 2022
    Review
  14. Regulation of Endoplasmic Reticulum-Mitochondria Tethering and CaInternational journal of molecular sciences · 2021
    Article
  15. 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

10 authors at 3 institutions in 1 country.

Caterina PeggionDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Maria Lina MassiminoCNR - Neuroscience Institute, Padova, Italy.
Roberto StellaFood Safety Division, Department of Chemistry, Istituto Zooprofilattico Sperimentale delle Venezie, Legnaro, Italy.
Raissa BortolottoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Jessica AgostiniDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Arianna MaldiDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Geppo SartoriDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Fiorella TonelloCNR - Neuroscience Institute, Padova, Italy.
Alessandro BertoliDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Raffaele LopreiatoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
University of Padua · ITNeuroscience Institute · ITIstituto Zooprofilattico Sperimentale delle Venezie · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TDP-43 is a nuclear protein involved in pivotal processes, extensively studied for its implication in neurodegenerative disorders. TDP-43 cytosolic inclusions are a common neuropathologic hallmark in amyotrophic lateral sclerosis (ALS) and related diseases, and it is now established that TDP-43 misfolding and aggregation play a key role in their etiopathology. TDP-43 neurotoxic mechanisms are not yet clarified, but the identification of proteins able to modulate TDP-43-mediated damage may be promising therapeutic targets for TDP-43 proteinopathies. Here we show by the use of refined yeast models that the nucleolar protein nucleolin (NCL) acts as a potent suppressor of TDP-43 toxicity, restoring cell viability. We provide evidence that NCL co-expression is able to alleviate TDP-43-induced damage also in human cells, further supporting its beneficial effects in a more consistent pathophysiological context. Presented data suggest that NCL could promote TDP-43 nuclear retention, reducing the formation of toxic cytosolic TDP-43 inclusions.

Indexed as

ALSFTDmisfolded proteinsneurodegenerative disordersnucleo-cytoplasmic transportnucleolinTDP-43 proteinopathies

Identifiers

PMID33912014
PMCPMC8072491
OpenAlexW3114675965

What OpenQuestion holds

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LicenceCC BY
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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.