Evidence map›Paper›PMID 31594228›Full record

ReviewJournal of Alzheimer's disease : JAD2019

Cofilin, a Master Node Regulating Cytoskeletal Pathogenesis in Alzheimer's Disease.

David E Kang, Jung A Woo

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of Alzheimer's disease : JAD, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
5.7field-weighted citation impact, top 3% 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

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

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Amyloid Beta Oligomers as Early Triggers of Neuronal Cytoskeleton Dysfunction in Alzheimer's Disease.Pathophysiology : the official journal of the International Society for Pathophysiology · 2026
    Review
  7. Article
  8. Review
  9. Review
  10. Cofilin(s) and Mitochondria: Function Beyond Actin Dynamics.International journal of molecular sciences · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Key Proteins in Rat Cerebral Cortex: Application ofMolecules (Basel, Switzerland) · 2024
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

David E KangByrd Institute and Alzheimer's Center, USF Health Morsani College of Medicine, Tampa, FL, USA.
Jung A WooByrd Institute and Alzheimer's Center, USF Health Morsani College of Medicine, Tampa, FL, USA.
University of South Florida · US

Funding

Role of the Slingshot-1 pathway in APP and Tau pathogenesisRF1AG053060 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI KANG, DAVID E · 2017 to 2017
$1.9M
BLRD VA I01 BX002478NIA NIH HHS RF1 AG053060
6 · The paper itself

Abstract

The defining pathological hallmarks of Alzheimer's disease (AD) are proteinopathies marked by the amyloid-β (Aβ) peptide and hyperphosphorylated tau. In addition, Hirano bodies and cofilin-actin rods are extensively found in AD brains, both of which are associated with the actin cytoskeleton. The actin-binding protein cofilin known for its actin filament severing, depolymerizing, nucleating, and bundling activities has emerged as a significant player in AD pathogenesis. In this review, we discuss the regulation of cofilin by multiple signaling events impinging on LIM kinase-1 (LIMK1) and/or Slingshot homolog-1 (SSH1) downstream of Aβ. Such pathophysiological signaling pathways impact actin dynamics to regulate synaptic integrity, mitochondrial translocation of cofilin to promote neurotoxicity, and formation of cofilin-actin pathology. Other intracellular signaling proteins, such as β-arrestin, RanBP9, Chronophin, PLD1, and 14-3-3 also impinge on the regulation of cofilin downstream of Aβ. Finally, we discuss the role of activated cofilin as a bridge between actin and microtubule dynamics by displacing tau from microtubules, thereby destabilizing tau-induced microtubule assembly, missorting tau, and promoting tauopathy.

Indexed as

Alzheimer DiseaseAnimalsBrainCofilin 1CytoskeletonHumansLim KinasesPhosphoprotein PhosphatasesTauopathiesCofilin 1LIMK1 protein, humanLim KinasesPhosphoprotein PhosphatasesSSH1 protein, humanAlzheimer’s diseaseamyloidchronophincofilincytoskeletonF-actinLIMK1microtubulemitochondriaPLD1slingshotSSH1tauβ-arrestin

Identifiers

PMID31594228
PMCPMC6971827
OpenAlexW2975806923

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.