Evidence map›Paper›PMID 30630951›Full record

ArticleThe Journal of biological chemistry2019

Aggregation of the nucleic acid-binding protein TDP-43 occurs via distinct routes that are coordinated with stress granule formation.

Youjun Chen, Todd J Cohen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.5field-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

67 citing papers in PubMed, 102 citations in OpenAlex.

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  5. TDP-43 Aggregation: The Healthy-Toxic Balance of the Prion-Like Domain.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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7 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 1 institution in 1 country.

Youjun ChenFrom the Department of Neurology, University of North Carolina Neuroscience Center, University of North Carolina, Chapel Hill, North Carolina 27599.
Todd J CohenFrom the Department of Neurology, University of North Carolina Neuroscience Center, University of North Carolina, Chapel Hill, North Carolina 27599 toddcohen@neurology.unc.edu.ORCID 0000-0002-4099-0278
University of North Carolina at Chapel Hill · US

Funding

UNC Neuroscience Center Research Cores: MicroscopyP30NS045892 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZYLKA, MARK J. · 2003 to 2022
$11.5M
Elucidating The Aberrant TDP-43 Species That Promote NeurodegenerationR01NS105981 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COHEN, TODD JONATHAN · 2018 to 2022
$1.7M
TDP-43 acetylation as a pathogenic modification in ALS & related proteinopathiesR00NS080985 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COHEN, TODD JONATHAN · 2014 to 2016
$731k
NINDS NIH HHS P30 NS045892NINDS NIH HHS R00 NS080985NINDS NIH HHS R01 NS105981
6 · The paper itself

Abstract

TAR DNA-binding protein 43 (TDP-43) is a nucleic acid-binding protein, and its aggregation represents the defining pathology in amyotrophic lateral sclerosis (ALS) and related proteinopathies. Recent studies implicate cytoplasmic stress granules (SGs) as hubs that may facilitate TDP-43 aggregation. Here, using cellular fractionation, biochemical analyses, and histological assays, we show that TDP-43 targeted to the cytoplasm has multiple fates. Whereas a TDP-43 subpopulation is indeed recruited to SGs, mature aggregated TDP-43, produced with aggregate-prone TDP-43 variants or exposure to oxidative stress, generates distinct TDP-43 inclusions that are surprisingly devoid of SGs. Consistent with this observation, we found that SG components are predominantly excluded from TDP-43 pathology in motor neurons from individuals with ALS. We generated

Indexed as

CytosolDNA-Binding ProteinsProtein AggregatesAmyotrophic Lateral SclerosisAnimalsCell LineFragile X Messenger Ribonucleoprotein 1HumansProtein ConformationProtein TransportSpinal CordDNA-Binding ProteinsFMR1 protein, humanFragile X Messenger Ribonucleoprotein 1Protein AggregatesTARDBP protein, humanamyloidamyotrophic lateral sclerosis (ALS) (Lou Gehrig disease)histone deacetylase 6 (HDAC6)motor neuron diseaseneurodegenerationoxidative stresspost-translational modification (PTM)protein aggregationstress granuleTAR DNA-binding protein 43 (TDP-43) (TARDBP)

Identifiers

PMID30630951
PMCPMC6416430
OpenAlexW2908605292

What OpenQuestion holds

Textmetadata
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.