Evidence map›Paper›PMID 37046025›Full record

ArticleScientific reports2023

ALS-linked TDP-43 mutations interfere with the recruitment of RNA recognition motifs to G-quadruplex RNA.

Akira Ishiguro, Akira Ishihama

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
  5. Article
  6. G-Quadruplexes Abet Neuronal Burnout in ALS and FTD.Antioxidants (Basel, Switzerland) · 2025
    Review
  7. TDP-43 controls RNA structure through high affinity lattice interactions.bioRxiv : the preprint server for biology · 2025
    Article
  8. Article
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  11. Review
  12. Article
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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

2 authors at 1 institution in 1 country.

Akira IshiguroResearch Center for Micro-Nano Technology, Hosei University, Midori-cho 3-11-15, Koganei, Tokyo, 184-0003, Japan. akira.ishiguro.iu@hosei.ac.jp.
Akira IshihamaResearch Center for Micro-Nano Technology, Hosei University, Midori-cho 3-11-15, Koganei, Tokyo, 184-0003, Japan.
Hosei University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TDP-43 is a major pathological protein in sporadic and familial amyotrophic lateral sclerosis (ALS) and mediates mRNA fate. TDP-43 dysfunction leads to causes progressive degeneration of motor neurons, the details of which remain elusive. Elucidation of the molecular mechanisms of RNA binding could enhance our understanding of this devastating disease. We observed the involvement of the glycine-rich (GR) region of TDP-43 in the initial recognition and binding of G-quadruplex (G4)-RNA in conjunction with its RNA recognition motifs (RRM). We performed a molecular dissection of these intramolecular RNA-binding modules in this study. We confirmed that the ALS-linked mutations in the GR region lead to alteration in the G4 structure. In contrast, amino acid substitutions in the GR region alter the protein structure but do not void the interaction with G4-RNA. Based on these observations, we concluded that the structural distortion of G4 caused by these mutations interferes with RRM recruitment and leads to TDP-43 dysfunction. This intramolecular organization between RRM and GR regions modulates the overall G4-binding properties.

Indexed as

Amyotrophic Lateral SclerosisDNA-Binding ProteinsHumansMutationRNARNA Recognition MotifDNA-Binding ProteinsRNATARDBP protein, human

Identifiers

PMID37046025
PMCPMC10097714
OpenAlexW4365150646

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Registered trials

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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.