Evidence map›Paper›PMID 33051572›Full record

ReviewExperimental & molecular medicine2020

The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies.

Myungjin Jo, Shinrye Lee, Yu-Mi Jeon, Seyeon Kim, Younghwi Kwon, Hyung-Jun Kim

Open access · goldAbstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 238 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
238citing papers in PubMed, 3 pooled it
12.4field-weighted citation impact, top 1% 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

238 citing papers in PubMed, 3 syntheses or guidelines pooled it, 375 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Exploring dysregulated miRNAs in ALS: implications for disease pathogenesis and early diagnosis.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Pooled it
  4. Article
  5. Synaptic Proteostasis in Health and Disease.Journal of neurochemistry · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
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  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Nuclear dysfunction in aging and neurodegeneration.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
    Review
  18. Review
  19. Article
  20. Article

178 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

6 authors at 2 institutions in 1 country.

Myungjin Jo *Dementia Research Group, Korea Brain Research Institute (KBRI), Daegu, 41062, South Korea.
Shinrye Lee *Dementia Research Group, Korea Brain Research Institute (KBRI), Daegu, 41062, South Korea.
Yu-Mi JeonDementia Research Group, Korea Brain Research Institute (KBRI), Daegu, 41062, South Korea.
Seyeon KimDementia Research Group, Korea Brain Research Institute (KBRI), Daegu, 41062, South Korea.
Younghwi KwonDementia Research Group, Korea Brain Research Institute (KBRI), Daegu, 41062, South Korea.
Hyung-Jun KimDementia Research Group, Korea Brain Research Institute (KBRI), Daegu, 41062, South Korea. kijang1@kbri.re.kr.
Korea Brain Research Institute · KRDaegu Gyeongbuk Institute of Science and Technology · KR

Funding

Korea Health Industry Development Institute (KHIDI) H I14C1135National Research Foundation of Korea (NRF) 2020R1A2C4002366
6 · The paper itself

Abstract

TAR DNA-binding protein 43 (TDP-43) is a highly conserved nuclear RNA/DNA-binding protein involved in the regulation of RNA processing. The accumulation of TDP-43 aggregates in the central nervous system is a common feature of many neurodegenerative diseases, such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer's disease (AD), and limbic predominant age-related TDP-43 encephalopathy (LATE). Accumulating evidence suggests that prion-like spreading of aberrant protein aggregates composed of tau, amyloid-β, and α-synuclein is involved in the progression of neurodegenerative diseases such as AD and PD. Similar to those of prion-like proteins, pathological aggregates of TDP-43 can be transferred from cell-to-cell in a seed-dependent and self-templating manner. Here, we review clinical and experimental studies supporting the prion-like spreading of misfolded TDP-43 and discuss the molecular mechanisms underlying the propagation of these pathological aggregated proteins. The idea that misfolded TDP-43 spreads in a prion-like manner between cells may guide novel therapeutic strategies for TDP-43-associated neurodegenerative diseases.

Indexed as

Disease SusceptibilityAnimalsDNA-Binding ProteinsGene Expression RegulationHumansNeurodegenerative DiseasesProtein Aggregation, PathologicalProtein BindingStructure-Activity RelationshipDNA-Binding ProteinsTARDBP protein, human

Identifiers

PMID33051572
PMCPMC8080625
OpenAlexW3092252141

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.