Evidence map›Paper›PMID 31097008›Full record

ReviewMolecular neurodegeneration2019

The role of neurofilament aggregation in neurodegeneration: lessons from rare inherited neurological disorders.

Alessandro Didonna, Puneet Opal

Open access · goldAbstract readReview
In one paragraph

Review in Molecular neurodegeneration, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 1 pooled it
8.0field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Junctions in Jeopardy: the neuromuscular junction is a selective pathological target in Charcot-Marie-Tooth disease.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Review
  6. Review
  7. Article
  8. Review
  9. [Advances in the Structure and Function of Neurofilament Protein and Its Application in Early Diagnosis of Amyotrophic Lateral Sclerosis].Sichuan da xue xue bao. Yi xue ban = Journal of Sichuan University. Medical science edition · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Dissecting neurofilament tail sequence-phosphorylation-structure relationships with multicomponent reconstituted protein brushes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Review
  18. Article
  19. Article
  20. Article

15 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

2 authors at 2 institutions in 1 country.

Alessandro DidonnaDepartment of Neurology and Weill Institute for Neurosciences, University of California at San Francisco, San Francisco, CA, 94158, USA.
Puneet OpalDavee Department of Neurology, Northwestern University Feinberg School of Medicine, Chicago, IL, 60611, USA. p-opal@northwestern.edu.
Northwestern University · USUniversity of California, San Francisco · US

Funding

Understanding the Cellular Basis of Movement DisordersR01NS082351 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Puneet Opal · 2013 to 2026
$6.2M
Cellular pathways underlying polyglutamine degenerationR01NS062051 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI OPAL, PUNEET · 2010 to 2014
$1.7M
Understanding pathophysiological mechanisms underlying neurodegenerationR56NS108639 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI OPAL, PUNEET · 2019 to 2019
$510k
NINDS NIH HHS R01 NS062051NINDS NIH HHS R01 NS082351NINDS NIH HHS R56 NS108639
6 · The paper itself

Abstract

Many neurodegenerative disorders, including Parkinson's, Alzheimer's, and amyotrophic lateral sclerosis, are well known to involve the accumulation of disease-specific proteins. Less well known are the accumulations of another set of proteins, neuronal intermediate filaments (NFs), which have been observed in these diseases for decades. NFs belong to the family of cytoskeletal intermediate filament proteins (IFs) that give cells their shape; they determine axonal caliber, which controls signal conduction; and they regulate the transport of synaptic vesicles and modulate synaptic plasticity by binding to neurotransmitter receptors. In the last two decades, a number of rare disorders caused by mutations in genes that encode NFs or regulate their metabolism have been discovered. These less prevalent disorders are providing novel insights into the role of NF aggregation in the more common neurological disorders.

Indexed as

Amyotrophic Lateral SclerosisAnimalsCytoskeletal ProteinsCytoskeletonHumansIntermediate FilamentsMutationNeurodegenerative DiseasesCytoskeletal ProteinsCharcot-Marie-tooth (CMT) diseaseGiant axonal neuropathy (GAN)NeurodegenerationNeurofilamentsProtein aggregationProtein degradation

Identifiers

PMID31097008
PMCPMC6524292
OpenAlexW2947448690

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.