Evidence map›Paper›PMID 34443678›Full record

ReviewMolecules (Basel, Switzerland)2021

Significance of Oligomeric and Fibrillar Species in Amyloidosis: Insights into Pathophysiology and Treatment.

Haruki Koike, Yohei Iguchi, Kentaro Sahashi, Masahisa Katsuno

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2021. 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
2.3field-weighted citation impact, top 11% 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, 33 citations in OpenAlex.

  1. Neurofilament Light Chains in Systemic Amyloidosis: A Systematic Review.International journal of molecular sciences · 2024
    Pooled it
  2. Article
  3. Mechanisms of damage and therapies for cardiac amyloidosis: a role for inflammation?Clinical research in cardiology : official journal of the German Cardiac Society · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Secondary Structure in Amyloids in Relation to Their Wild Type Forms.International journal of molecular sciences · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Redox signaling and metabolism in Alzheimer's disease.Frontiers in aging neuroscience · 2022
    Review
  19. Review
  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.

Haruki KoikeDepartment of Neurology, Graduate School of Medicine, Nagoya University, Nagoya 466-8550, Japan.ORCID 0000-0002-4612-3183
Yohei IguchiDepartment of Neurology, Graduate School of Medicine, Nagoya University, Nagoya 466-8550, Japan.
Kentaro SahashiDepartment of Neurology, Graduate School of Medicine, Nagoya University, Nagoya 466-8550, Japan.
Masahisa KatsunoDepartment of Neurology, Graduate School of Medicine, Nagoya University, Nagoya 466-8550, Japan.ORCID 0000-0001-9453-9311
Nagoya University · JP

Funding

The Ministry of Health, Labor and Welfare of Japan 20FC1022
6 · The paper itself

Abstract

Amyloidosis is a term referring to a group of various protein-misfolding diseases wherein normally soluble proteins form aggregates as insoluble amyloid fibrils. How, or whether, amyloid fibrils contribute to tissue damage in amyloidosis has been the topic of debate. In vitro studies have demonstrated the appearance of small globular oligomeric species during the incubation of amyloid beta peptide (Aβ). Nerve biopsy specimens from patients with systemic amyloidosis have suggested that globular structures similar to Aβ oligomers were generated from amorphous electron-dense materials and later developed into mature amyloid fibrils. Schwann cells adjacent to amyloid fibrils become atrophic and degenerative, suggesting that the direct tissue damage induced by amyloid fibrils plays an important role in systemic amyloidosis. In contrast, there is increasing evidence that oligomers, rather than amyloid fibrils, are responsible for cell death in neurodegenerative diseases, particularly Alzheimer's disease. Disease-modifying therapies based on the pathophysiology of amyloidosis have now become available. Aducanumab, a human monoclonal antibody against the aggregated form of Aβ, was recently approved for Alzheimer's disease, and other monoclonal antibodies, including gantenerumab, solanezumab, and lecanemab, could also be up for approval. As many other agents for amyloidosis will be developed in the future, studies to develop sensitive clinical scales for identifying improvement and markers that can act as surrogates for clinical scales should be conducted.

Indexed as

AmyloidAmyloidosisAnimalsHumansOrgan SpecificityProtein AggregatesSchwann CellsAmyloidProtein AggregatesAA amyloidosisAL amyloidosisAlzheimer’s diseaseamyotrophic lateral sclerosisATTR amyloidosisdementiaParkinson’s diseasepathologypriontransthyretin

Identifiers

PMID34443678
PMCPMC8401015
OpenAlexW3195304920

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.