Evidence map›Paper›PMID 33328890›Full record

ArticleFrontiers in cellular neuroscience2020

Amyotrophic Lateral Sclerosis: Proteins, Proteostasis, Prions, and Promises.

Luke McAlary, Yee Lian Chew, Jeremy Stephen Lum, Nicholas John Geraghty, Justin John Yerbury, Neil R Cashman

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cellular neuroscience, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 43 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Structural insights into the role of reduced cysteine residues in SOD1 amyloid filament formation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Review
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  11. Review
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  15. Repetitive Mild Closed Head Injury in Adolescent Mice Is Associated with Impaired Proteostasis, Neuroinflammation, and Tauopathy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  16. Article
  17. Review
  18. Review
  19. Protein conformation and biomolecular condensates.Current research in structural biology · 2022
    Review
  20. Metals in ALS TDP-43 Pathology.International journal of molecular sciences · 2021
    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

6 authors at 3 institutions in 2 countries.

Luke McAlaryIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, Australia.
Yee Lian ChewIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, Australia.
Jeremy Stephen LumIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, Australia.
Nicholas John GeraghtyIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, Australia.
Justin John YerburyIllawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW, Australia.
Neil R CashmanDjavad Mowafaghian Centre for Brain Health, University of British Columbia, Vancouver, BC, Canada.
Illawarra Health and Medical Research Institute · AUUniversity of British Columbia · CAUniversity of Wollongong · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is characterized by the progressive degeneration of the motor neurons that innervate muscle, resulting in gradual paralysis and culminating in the inability to breathe or swallow. This neuronal degeneration occurs in a spatiotemporal manner from a point of onset in the central nervous system (CNS), suggesting that there is a molecule that spreads from cell-to-cell. There is strong evidence that the onset and progression of ALS pathology is a consequence of protein misfolding and aggregation. In line with this, a hallmark pathology of ALS is protein deposition and inclusion formation within motor neurons and surrounding glia of the proteins TAR DNA-binding protein 43, superoxide dismutase-1, or fused in sarcoma. Collectively, the observed protein aggregation, in conjunction with the spatiotemporal spread of symptoms, strongly suggests a prion-like propagation of protein aggregation occurs in ALS. In this review, we discuss the role of protein aggregation in ALS concerning protein homeostasis (proteostasis) mechanisms and prion-like propagation. Furthermore, we examine the experimental models used to investigate these processes, including

Indexed as

amyotrophic lateral scelerosisinvertebrate modelsin vitro modelsmouse modelsprion-likeprotein aggregationproteostasistherapeutics

Identifiers

PMID33328890
PMCPMC7671971
OpenAlexW3095446841

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.