Evidence map›Paper›PMID 41756868›Full record

ArticlebioRxiv : the preprint server for biology2026

PXL: a Nucleic Acid-Binding Module of Promyelocytic Leukemia Protein.

Daniel Fairchild, Irina V Semenova, Dane Geddes-Buehre, Yunfeng Li, Renata Szczepaniak, Sandra K Weller, Bing Hao, Irina Bezsonova

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

8 authors.

Daniel FairchildDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.
Irina V SemenovaDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.
Dane Geddes-BuehreDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.ORCID 0000-0002-1861-0515
Yunfeng LiDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.
Renata SzczepaniakDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.
Sandra K WellerDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.ORCID 0000-0002-4519-6276
Bing HaoDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.ORCID 0000-0003-3029-5340
Irina BezsonovaDepartment of Molecular Biology and Biophysics, School of Medicine, University of Connecticut, 263 Farmington Avenue, Farmington, CT, 06030, United States.ORCID 0000-0002-8629-0349

Funding

UBIQUITIN-PROTEASOME PATHWAY in HUMAN DISEASER35GM156397 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI Irina Bezsonova · 2025 to 2026
$1000k
Molecular mechanisms of sensing nuclear stress and launching antiviral defense by PMLR21AI178136 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI BEZSONOVA, IRINA, WELLER, SANDRA K · 2024 to 2025
$458k
Oxidation is a trigger for PML multimerization and Nuclear Body formation in HSV infected cellsR21AI135451 · NIAID · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI BEZSONOVA, IRINA, WELLER, SANDRA K · 2018 to 2019
$433k
NIAID NIH HHS R21 AI135451NIAID NIH HHS R21 AI178136NIGMS NIH HHS R35 GM156397
6 · The paper itself

Abstract

The promyelocytic leukemia protein (PML) is a stress-response factor that assembles into PML nuclear bodies, dynamic subnuclear compartments involved in tumor suppression and antiviral defense. The most abundant isoform, PML-1, has been linked to transcriptional regulation, genome stability, and antiviral responses, yet the molecular basis of these functions remains unclear. Here, we report that PML-1 contains a unique nucleic acid-binding module, PXL, and determine its three-dimensional structure by X-ray crystallography. Further biochemical, mutational, and cellular analyses, including RNA-seq, demonstrate that this module selectively binds single-stranded G-rich RNA and DNA motifs and modulates the transcriptome. These findings reveal an unexpected molecular function of PML and provide a framework for understanding its roles in nuclear organization and gene regulation.

Indexed as

DNA bindingG-quadruplexPML-1PML isoformsPromyelocytic leukemia (PML)protein structurepseudo-nucleaseRNA bindingRNAseqtranscriptionX-ray crystallography

Identifiers

PMID41756868
PMCPMC12934764

What OpenQuestion holds

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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.