Evidence map›Paper›PMID 42871744›Full record

ArticleMicrobial cell (Graz, Austria)2026

Scp160 deletion suppresses TDP-43 aggregation and toxicity in

Joan Castells-Ballester, Natalia Shcherbik

Abstract read
In one paragraph

Article in Microbial cell (Graz, Austria), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Joan Castells-BallesterDepartment of Cell and Molecular Biology, Rowan-Virtua University, School of Osteopathic Medicine, 2 Medical Center Drive, Stratford, NJ 08084, USA.
Natalia ShcherbikDepartment of Cell and Molecular Biology, Rowan-Virtua University, School of Osteopathic Medicine, 2 Medical Center Drive, Stratford, NJ 08084, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding and aberrant protein aggregation are central features of neurodegenerative disorders, including amyotrophic lateral sclerosis, where the RNA-binding protein TDP-43 accumulates in abnormal intracellular assemblies. Although yeast models have identified multiple modifiers of TDP-43 toxicity, the cellular factors that determine how aggregation-prone proteins are organized remain incompletely understood. Here, we investigated whether the ribosome- and mRNP-associated proteins Scp160 and Bfr1 influence TDP-43 proteotoxicity and aggregate formation. We report that deletion of

Indexed as

Bfr1endoplasmic reticulumprotein aggregationproteostasisproteotoxicitySaccharomyces cerevisiaeScp160/VigilinTDP-43

Identifiers

PMID42871744
PMCPMC13659451

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.