Evidence map›Paper›PMID 29396541›Full record

ArticleScientific reports2018

TDP-43 self-interaction is modulated by redox-active compounds Auranofin, Chelerythrine and Riluzole.

Moritz Oberstadt, Jens Stieler, David Larbi Simpong, Ute Römuß, Nicole Urban, Michael Schaefer, Thomas Arendt, Max Holzer

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Discovery of TDP-43 aggregation inhibitorsbioRxiv : the preprint server for biology · 2026
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  5. Review
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  10. Multiple roles for the cytoskeleton in ALS.Experimental neurology · 2022
    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

8 authors at 2 institutions in 1 country.

Moritz OberstadtDepartment of Neurology, University of Leipzig, Liebigstraße 20, 04103, Leipzig, Germany. moritz.oberstadt@medizin.uni-leipzig.de.
Jens StielerDepartment for Molecular and Cellular Mechanisms of Neurodegeneration, Paul Flechsig Institute for Brain Research, University of Leipzig, Liebigstraße 19, 04103, Leipzig, Germany.
David Larbi SimpongDepartment for Molecular and Cellular Mechanisms of Neurodegeneration, Paul Flechsig Institute for Brain Research, University of Leipzig, Liebigstraße 19, 04103, Leipzig, Germany.
Ute RömußDepartment of Neurology, University of Leipzig, Liebigstraße 20, 04103, Leipzig, Germany.
Nicole UrbanRudolf-Boehm-Institute of Pharmacology and Toxicology, University of Leipzig, Härtelstraße 16-18, 04107, Leipzig, Germany.
Michael SchaeferRudolf-Boehm-Institute of Pharmacology and Toxicology, University of Leipzig, Härtelstraße 16-18, 04107, Leipzig, Germany.
Thomas ArendtDepartment for Molecular and Cellular Mechanisms of Neurodegeneration, Paul Flechsig Institute for Brain Research, University of Leipzig, Liebigstraße 19, 04103, Leipzig, Germany.
Max HolzerDepartment for Molecular and Cellular Mechanisms of Neurodegeneration, Paul Flechsig Institute for Brain Research, University of Leipzig, Liebigstraße 19, 04103, Leipzig, Germany.ORCID http://orcid.org/0000-0003-1754-9932
Leipzig University · DELeipzig University of Applied Sciences · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) represents a fatal neurodegenerative disease, which is characterized by a rapid loss of lower and upper motor neurons. As a major neuropathological hallmark, protein aggregates containing the Transactivating Response Region (TAR) DNA Binding Protein (TDP-43) are detectable in about 95% of sporadic ALS patients. TDP-43 interacts with itself physiologically to form liquid droplets, which may progress to pathological aggregates. In this study, we established the NanoBit luciferase complementation assay to measure TDP-43 self-interaction and found the fusion of the split luciferase subunits to the N-terminus of the protein as the strongest interacting partners. A screen of pharmacologically active compounds from the LOPAC

Indexed as

Amyotrophic Lateral SclerosisAnimalsAuranofinBenzophenanthridinesCell Line, TumorDNA-Binding ProteinsGlutathioneMiceMotor NeuronsOxidation-ReductionProtein AggregatesProtein Aggregation, PathologicalRiluzoleThioredoxin-Disulfide ReductaseAuranofinBenzophenanthridineschelerythrineDNA-Binding ProteinsGlutathioneProtein AggregatesRiluzoleTardbp protein, mouseThioredoxin-Disulfide Reductase

Identifiers

PMID29396541
PMCPMC5797228
OpenAlexW2799516388

What OpenQuestion holds

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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.