Evidence map›Paper›PMID 39583578›Full record

ArticlemicroPublication biology2024

Conserved region of human TDP-43 is structurally similar to membrane binding protein FARP1 and protein chaperons BAG6 and CYP33.

Ljiljana Sjekloća, Emanuele Buratti

Abstract read
In one paragraph

Article in microPublication biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. TDP-43 Aggregation: The Healthy-Toxic Balance of the Prion-Like Domain.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  2. TDP-43: unveiling the hidden key to cellular fate decisions.Cell communication and signaling : CCS · 2025
    Review
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.

Ljiljana SjekloćaMolecular Pathology, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Emanuele BurattiMolecular Pathology, International Centre for Genetic Engineering and Biotechnology, Trieste, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transactive response DNA-binding protein of 43 KDa (TDP-43) is important for RNA metabolism in all animals and in humans is involved in neuromuscular diseases. Full-length TDP-43 is prone to oligomerization and misfolding what renders difficult its characterization. We report that TDP-43 domains are structurally similar to lipid binding protein FARP1 and protein chaperons BAG6 and CYP33. Sequence analysis suggests putative lipid binding sites throughout TDP-43 and in vitro thioflavin T fluorescence assays show that cholesterol and phosphatidylcholine affect fibrillation of recombinant TDP-43 fragments. Our findings suggest that TDP-43 can bind lipids directly and it may contribute to its own chaperoning.

Identifiers

PMID39583578
PMCPMC11582883

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.