Evidence map›Paper›PMID 41571747›Full record

ArticleCommunications biology2026

NLRP10 engages oxidized DNA through a Schiff-base mechanism and dissociates from NLRP3 upon inflammasome activation.

Julia Elise Cabral, Angela Lackner, Wenjin Jiang, Sophia Lin, Haitian Zhou, Anna Wu, Courtney Demos, Minh Anh Pham, Reginald McNulty

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2026. 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. Article
  2. 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

9 authors.

Julia Elise CabralLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.ORCID http://orcid.org/0000-0001-6072-6362
Angela LacknerLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Wenjin JiangLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Sophia LinLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Haitian ZhouLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Anna WuLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Courtney DemosLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Minh Anh PhamLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA.
Reginald McNultyLaboratory of Macromolecular Structure, Department of Molecular Biology & Biochemistry, University of California, Irvine, CA, USA. rmcnulty@uci.edu.ORCID http://orcid.org/0000-0003-2101-1377

Funding

Immunology Research Training GrantT32AI177324 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI Eric Pearlman · 2023 to 2026
$735k
Macromolecular assemblies of transcription factors initiated by pathogen infectionK22AI139444 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI MCNULTY, REGINALD · 2019 to 2021
$297k
NIAID NIH HHS K22 AI139444NIAID NIH HHS T32 AI177324U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) K22AI139444U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) T32AI177324
6 · The paper itself

Abstract

Mitochondrial DNA release into the cytosol is a critical event in innate immune activation, often acting as a damage-associated molecular pattern (DAMP) that triggers inflammasome assembly. Here, we demonstrate that NLRP3 is involved in the release of D-loop mtDNA into the cytosol. We further show that NLRP3 interacts with NLRP10. NLRP10-mediated oxidized DNA cleavage involves a Schiff base intermediate and is inhibited by small molecules known to inhibit glycosylases. These findings support a model where NLRP10 interaction with oxidized DNA may contribute to long-term senescence secretory phenotype and modulate inflammasome activation. Our study highlights a novel mechanism by which NLRP10 can respond to mitochondrial stress signals to influence innate immunity and suggests therapeutic potential for targeting these interactions in inflammatory diseases.

Indexed as

DNA, MitochondrialInflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinAnimalsHumansImmunity, InnateNLR ProteinsOxidation-ReductionSchiff BasesDNA, MitochondrialInflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinNLRP3 protein, humanNLR ProteinsSchiff Bases

Identifiers

PMID41571747
PMCPMC12827243

What OpenQuestion holds

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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.