Evidence map›Paper›PMID 32976566›Full record

ReviewJournal of molecular cell biology2021

Role and therapeutic potential of liquid-liquid phase separation in amyotrophic lateral sclerosis.

Donya Pakravan, Gabriele Orlando, Valérie Bercier, Ludo Van Den Bosch

Open access · goldAbstract readReview
In one paragraph

Review in Journal of molecular cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.2field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 47 citations in OpenAlex.

  1. Classical and Nonclassical Nucleation Mechanisms of Biomolecules.Advances in biochemical engineering/biotechnology · 2026
    Review
  2. Article
  3. TDP-43: unveiling the hidden key to cellular fate decisions.Cell communication and signaling : CCS · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Neurological Diseases can be Regulated by Phase Separation.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  12. Review
  13. Maturation and Conformational Switching of aJournal of the American Chemical Society · 2024
    Article
  14. Review
  15. Article
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  17. Article
  18. Article
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  20. Review
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

4 authors at 1 institution in 1 country.

Donya PakravanDepartment of Neurosciences, Experimental Neurology and Leuven Brain Institute (LBI), KU Leuven-University of Leuven, 3000 Leuven, Belgium.
Gabriele OrlandoSwitch Laboratory, VIB-KU Leuven Center for Brain & Disease Research, 3000 Leuven, Belgium.
Valérie BercierDepartment of Neurosciences, Experimental Neurology and Leuven Brain Institute (LBI), KU Leuven-University of Leuven, 3000 Leuven, Belgium.
Ludo Van Den BoschDepartment of Neurosciences, Experimental Neurology and Leuven Brain Institute (LBI), KU Leuven-University of Leuven, 3000 Leuven, Belgium.
VIB-KU Leuven Center for Brain & Disease Research · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is a late-onset neurodegenerative disease selectively affecting motor neurons, leading to progressive paralysis. Although most cases are sporadic, ∼10% are familial. Similar proteins are found in aggregates in sporadic and familial ALS, and over the last decade, research has been focused on the underlying nature of this common pathology. Notably, TDP-43 inclusions are found in almost all ALS patients, while FUS inclusions have been reported in some familial ALS patients. Both TDP-43 and FUS possess 'low-complexity domains' (LCDs) and are considered as 'intrinsically disordered proteins', which form liquid droplets in vitro due to the weak interactions caused by the LCDs. Dysfunctional 'liquid-liquid phase separation' (LLPS) emerged as a new mechanism linking ALS-related proteins to pathogenesis. Here, we review the current state of knowledge on ALS-related gene products associated with a proteinopathy and discuss their status as LLPS proteins. In addition, we highlight the therapeutic potential of targeting LLPS for treating ALS.

Indexed as

Amyotrophic Lateral SclerosisAutophagyDNA-Binding ProteinsHumansIntrinsically Disordered ProteinsMolecular ChaperonesMutationOligonucleotides, AntisenseProtein Aggregation, PathologicalProtein FoldingRNA-Binding Protein FUSDNA-Binding ProteinsFUS protein, humanIntrinsically Disordered ProteinsMolecular ChaperonesOligonucleotides, AntisenseRNA-Binding Protein FUSTARDBP protein, humanALS therapymotor neuronphase separationstress granule

Identifiers

PMID32976566
PMCPMC8036000
OpenAlexW3088498893

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.