Evidence map›Paper›PMID 38326375›Full record

ArticleNature communications2024

Structural basis for the oligomerization-facilitated NLRP3 activation.

Xiaodi Yu, Rosalie E Matico, Robyn Miller, Dhruv Chauhan, Bertrand Van Schoubroeck, Karolien Grauwen, Javier Suarez, Beth Pietrak, Nandan Haloi, Yanting Yin and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
11.0field-weighted citation impact, top 1% of its field
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

45 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  4. Innate immunity: current understandings and future perspectives.Signal transduction and targeted therapy · 2026
    Review
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  9. Article
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  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Molecular mechanisms of NLRP3 inflammasome activation.Experimental & molecular medicine · 2026
    Review
  18. Review
  19. Diverse Scaffolds Facilitate NLRP3 Clustering and Inflammasome Formation in Response to Perturbations in Cell Homeostasis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  20. 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

17 authors at 3 institutions in 2 countries.

Xiaodi Yu *Johnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA. xyu6@its.jnj.com.ORCID 0000-0001-7520-0646
Rosalie E Matico *Johnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA.
Robyn MillerJohnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA.
Dhruv ChauhanJohnson & Johnson Innovation Medicine, J&J Interventional Oncology, Beerse, Belgium.
Bertrand Van SchoubroeckJohnson & Johnson Innovation Medicine, J&J Interventional Oncology, Beerse, Belgium.
Karolien GrauwenJohnson & Johnson Innovation Medicine, J&J Interventional Oncology, Beerse, Belgium.
Javier SuarezJohnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA.
Beth PietrakJohnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA.
Nandan HaloiDepartment of Applied Physics, Swedish e-Science Research Center, KTH Royal Institute of Technology, Stockholm, Sweden.ORCID 0000-0003-3542-333X
Yanting YinJohnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA.
Gary John TresadernJohnson & Johnson Innovation Medicine, Discovery Sciences, Beerse, Belgium.ORCID 0000-0002-4801-1644
Laura Perez-BenitoJohnson & Johnson Innovation Medicine, Discovery Sciences, Beerse, Belgium.
Erik LindahlDepartment of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Stockholm, Sweden.ORCID 0000-0002-2734-2794
Astrid BottelbergsJohnson & Johnson Innovation Medicine, Discovery Sciences, Beerse, Belgium.
Daniel OehlrichJohnson & Johnson Innovation Medicine, Discovery Sciences, Beerse, Belgium.
Nina Van OpdenboschJohnson & Johnson Innovation Medicine, J&J Interventional Oncology, Beerse, Belgium.
Sujata SharmaJohnson & Johnson Innovation Medicine, Spring House, PA, 19044, USA.ORCID 0000-0002-7588-2939
Johnson & Johnson (United States) · USKTH Royal Institute of Technology · SEStockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The NACHT-, leucine-rich-repeat-, and pyrin domain-containing protein 3 (NLRP3) is a critical intracellular inflammasome sensor and an important clinical target against inflammation-driven human diseases. Recent studies have elucidated its transition from a closed cage to an activated disk-like inflammasome, but the intermediate activation mechanism remains elusive. Here we report the cryo-electron microscopy structure of NLRP3, which forms an open octamer and undergoes a ~ 90° hinge rotation at the NACHT domain. Mutations on open octamer's interfaces reduce IL-1β signaling, highlighting its essential role in NLRP3 activation/inflammasome assembly. The centrosomal NIMA-related kinase 7 (NEK7) disrupts large NLRP3 oligomers and forms NEK7/NLRP3 monomers/dimers which is a critical step preceding the assembly of the disk-like inflammasome. These data demonstrate an oligomeric cooperative activation of NLRP3 and provide insight into its inflammasome assembly mechanism.

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinCryoelectron MicroscopyHumansNIMA-Related KinasesProteinsInflammasomesNIMA-Related KinasesNLR Family, Pyrin Domain-Containing 3 ProteinProteins

Identifiers

PMID38326375
PMCPMC10850481
OpenAlexW4391617570

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.