Evidence map›Paper›PMID 36127465›Full record

ReviewCellular & molecular immunology2022

How location and cellular signaling combine to activate the NLRP3 inflammasome.

Anil Akbal, Alesja Dernst, Marta Lovotti, Matthew S J Mangan, Róisín M McManus, Eicke Latz

Open access · hybridAbstract readReview
In one paragraph

Review in Cellular & molecular immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed, 1 pooled it
17.2field-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

139 citing papers in PubMed, 1 synthesis or guideline pooled it, 222 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Altered cholesterol immunometabolism activates the macrophage NLRP3-inflammasome in lung fibrosis.American journal of respiratory cell and molecular biology · 2026
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Inflammasomes in Sjögren's Disease: Exploring the Therapeutic Value.International journal of molecular sciences · 2026
    Review
  12. Review
  13. Review
  14. Review
  15. The Mechanism of NLRP3 Inflammasome Activation and Its Roles in Chronic Rhinosinusitis.World journal of otorhinolaryngology - head and neck surgery · 2026
    Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. ROS breaks the cofilin lock on NLRP3.Nature immunology · 2026
    Article

79 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 3 countries.

Anil Akbal *Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 53127, Bonn, Germany.
Alesja Dernst *Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 53127, Bonn, Germany.
Marta Lovotti *Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 53127, Bonn, Germany.ORCID http://orcid.org/0000-0003-3379-2190
Matthew S J Mangan *Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 53127, Bonn, Germany.
Róisín M McManus *Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 53127, Bonn, Germany.
Eicke Latz *Institute of Innate Immunity, University Hospital Bonn, University of Bonn, 53127, Bonn, Germany. Eicke.latz@uni-bonn.de.ORCID http://orcid.org/0000-0003-1488-5666
University of Bonn · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NOD-, LRR-, and pyrin domain-containing 3 (NLRP3) is a cytosolic innate immune sensor of cellular stress signals, triggered by infection and sterile inflammation. Upon detection of an activating stimulus, NLRP3 transitions from an inactive homo-oligomeric multimer into an active multimeric inflammasome, which promotes the helical oligomeric assembly of the adaptor molecule ASC. ASC oligomers provide a platform for caspase-1 activation, leading to the proteolytic cleavage and activation of proinflammatory cytokines in the IL-1 family and gasdermin D, which can induce a lytic form of cell death. Recent studies investigating both the cellular requirement for NLRP3 activation and the structure of NLRP3 have revealed the complex regulation of NLRP3 and the multiple steps involved in its activation. This review presents a perspective on the biochemical and cellular processes controlling the assembly of the NLRP3 inflammasome with particular emphasis on structural regulation and the role of organelles. We also highlight the latest research on metabolic control of this inflammatory pathway and discuss promising clinical targets for intervention.

Indexed as

InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinCytokinesHumansInflammationInterleukin-1betaCytokinesInflammasomesInterleukin-1betaNLR Family, Pyrin Domain-Containing 3 ProteinInflammasomeLocalizationMechanismNLRP3RegulationStructure

Identifiers

PMID36127465
PMCPMC9622870
OpenAlexW4296773470

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.