Evidence map›Paper›PMID 34558120›Full record

ReviewGlia2022

Glial TDP-43 and TDP-43 induced glial pathology, focus on neurodegenerative proteinopathy syndromes.

Katherine E Prater, Caitlin S Latimer, Suman Jayadev

Open access · greenAbstract readReview
In one paragraph

Review in Glia, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
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  8. Loss of Nuclear TDP-43 Impairs Lipid Metabolism in Microglia-Like Cells.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
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  11. Review
  12. Review
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  16. CSF IL-6, GDF-15, GFAP and NfL levels in early Alzheimer disease: a pilot study.Therapeutic advances in neurological disorders · 2025
    Article
  17. Article
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  19. Review
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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

3 authors at 1 institution in 1 country.

Katherine E PraterDepartment of Neurology, University of Washington, Seattle, Washington, USA.ORCID 0000-0001-8615-207X
Caitlin S LatimerDivision of Neuropathology, Department of Laboratory Medicine and Pathology, University of Washington, Seattle, Washington, USA.ORCID 0000-0003-3727-4278
Suman JayadevDepartment of Neurology, University of Washington, Seattle, Washington, USA.ORCID 0000-0003-3164-9665
University of Washington · US

Funding

University of Washington Alzheimer's Disease Research CenterP30AG066509 · NIA · UNIVERSITY OF WASHINGTON · PI ALI SHOJAIE · 2020 to 2026
$29.0M
Understanding the functional impact of cumulative genetic risk in Alzheimer DiseaseRF1AG063540 · NIA · UNIVERSITY OF WASHINGTON · PI GARDEN, GWENN A, JAYADEV, SUMAN · 2019 to 2020
$4.6M
Molecular Regulation of Microglia BehaviorR01NS073848 · NINDS · UNIVERSITY OF WASHINGTON · PI GARDEN, GWENN A · 2011 to 2016
$1.7M
Molecular Mechanisms of Synergistic TDP-43 and Tau Proteotoxicity in Alzheimer's DiseaseK08AG065426 · NIA · UNIVERSITY OF WASHINGTON · PI LATIMER, CAITLIN SHANNON · 2020 to 2024
$705k
NIA NIH HHS K08 AG065426NIA NIH HHS P30 AG066509NIA NIH HHS RF1 AG063540NINDS NIH HHS R01 NS073848
6 · The paper itself

Abstract

Since its discovery in 2006, TAR DNA binding protein 43 (TDP-43) has driven rapidly evolving research in neurodegenerative diseases including amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration (FTLD), and limbic predominant age-related TDP-43 encephalopathy (LATE). TDP-43 mislocalization or aggregation is the hallmark of TDP-43 proteinopathy and is associated with cognitive impairment that can be mapped to its regional deposition. Studies in human tissue and model systems demonstrate that TDP-43 may potentiate other proteinopathies such as the amyloid or tau pathology seen in Alzheimer's Disease (AD) in the combination of AD+LATE. Despite this growing body of literature, there remain gaps in our understanding of whether there is heterogeneity in TDP-43 driven mechanisms across cell types. The growing observations of correlation between TDP-43 proteinopathy and glial pathology suggest a relationship between the two, including pathogenic glial cell-autonomous dysfunction and dysregulated glial immune responses to neuronal TDP-43. In this review, we discuss the available data on TDP-43 in glia within the context of the neurodegenerative diseases ALS and FTLD and highlight the current lack of information about glial TDP-43 interaction in AD+LATE. TDP-43 has proven to be a significant modulator of cognitive and neuropathological outcomes. A deeper understanding of its role in diverse cell types may provide relevant insights into neurodegenerative syndromes.

Indexed as

Amyotrophic Lateral SclerosisFrontotemporal Lobar DegenerationTDP-43 ProteinopathiesDNA-Binding ProteinsHumansNeurogliaSyndromeDNA-Binding ProteinsTARDBP protein, humanAlzheimer's diseaseamyotrophic lateral sclerosisastrocytefrontotemporal lobar degenerationgliamicrogliaoligodendrocyteTDP-43

Identifiers

PMID34558120
PMCPMC8722378
OpenAlexW3200339367

What OpenQuestion holds

Textmetadata
LicenceTDM
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.