Evidence map›Paper›PMID 41491828›Full record

ArticleScientific reports2026

Intrinsically disordered regions in the yeast transcriptional regulator Ixr1 support prion-like behavior.

Aida Barreiro-Alonso, Cora Rey-Souto, Mónica Lamas-Maceiras, José Manuel Pérez-Martínez, Anahir Franco-Gacio, Esther Rodríguez-Belmonte, M Esperanza Cerdán, Ángel Vizoso-Vázquez

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In one paragraph

Article in Scientific reports, 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

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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

8 authors.

Aida Barreiro-Alonso *Centro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain.
Cora Rey-Souto *Centro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain.
Mónica Lamas-Maceiras *Centro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain.
José Manuel Pérez-MartínezCentro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain.
Anahir Franco-GacioCentro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain.
Esther Rodríguez-BelmonteInstituto de Investigación Biomédica de A Coruña (INIBIC), As Xubias de Arriba 84, 15006, A Coruña, Spain.
M Esperanza CerdánCentro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain.
Ángel Vizoso-VázquezCentro Interdisciplinar de Química e Bioloxía (CICA), Universidade da Coruña, Campus de Elviña, As Carballeiras, s/n, 15071, A Coruña, Spain. a.vizoso@udc.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ixr1 is a yeast transcriptional regulator previously identified as a player in the response to stress conditions, such as oxidative stress, hypoxia, iron limitation or DNA damage. Little is known about the structure of the Ixr1 protein apart from their HMG-boxes, which conform two well-known folded DNA binding domains. Intrinsically disordered regions (IDRs) are predicted in Ixr1 by algorithms and analytical methods. Ixr1 protein is non-globular and prone to aggregation, sustaining a concentration-dependent equilibrium between monomeric and dimeric forms. Treatment with 150 µM glutaraldehyde, to stabilize and fix weak protein-protein interactions, induces Ixr1 to form large oligomers. Indeed, Ixr1 forms amyloids as demonstrated both by in vitro and in vivo approaches. Chimeras constructed between Ixr1 and the C-terminal domain of Sup35, which provides the translation termination function to the yeast prion [PSI

Indexed as

Intrinsically Disordered ProteinsPrionsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsPeptide Termination FactorsProtein BindingIntrinsically Disordered ProteinsPeptide Termination FactorsPrionsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeTranscription Factors

Identifiers

PMID41491828
PMCPMC12852091

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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.