Evidence map›Paper›PMID 35545613›Full record

ArticleNature communications2022

Gasdermin-A3 pore formation propagates along variable pathways.

Stefania A Mari, Kristyna Pluhackova, Joka Pipercevic, Matthew Leipner, Sebastian Hiller, Andreas Engel, Daniel J Müller

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.8field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. The gasdermin family: from pyroptosis mechanisms to therapeutic targets.Signal transduction and targeted therapy · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Mechanistic insights into gasdermin-mediated pyroptosis.Nature reviews. Molecular cell biology · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. The gasdermin family: emerging therapeutic targets in diseases.Signal transduction and targeted therapy · 2024
    Review
  16. Article
  17. Article
  18. Structure and assembly of a bacterial gasdermin pore.bioRxiv : the preprint server for biology · 2023
    Article
  19. Review
  20. Unbreaking Assemblies in Molecular Simulations with Periodic Boundaries.Journal of chemical information and modeling · 2023
    Article
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

7 authors at 2 institutions in 1 country.

Stefania A Mari *Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, 4058, Basel, Switzerland.ORCID 0000-0002-6420-8578
Kristyna Pluhackova *Department of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, 4058, Basel, Switzerland. kristyna.pluhackova@bsse.ethz.ch.ORCID 0000-0002-7498-6584
Joka PipercevicBiozentrum, University of Basel, 4056, Basel, Switzerland.
Matthew LeipnerDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, 4058, Basel, Switzerland.ORCID 0000-0002-0079-140X
Sebastian HillerBiozentrum, University of Basel, 4056, Basel, Switzerland.ORCID 0000-0002-6709-4684
Andreas EngelDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, 4058, Basel, Switzerland.ORCID 0000-0002-0118-8733
Daniel J MüllerDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zurich, 4058, Basel, Switzerland. daniel.mueller@bsse.ethz.ch.ORCID 0000-0003-3075-0665
Board of the Swiss Federal Institutes of Technology · CHUniversity of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gasdermins are main effectors of pyroptosis, an inflammatory form of cell death. Released by proteolysis, the N-terminal gasdermin domain assembles large oligomers to punch lytic pores into the cell membrane. While the endpoint of this reaction, the fully formed pore, has been well characterized, the assembly and pore-forming mechanisms remain largely unknown. To resolve these mechanisms, we characterize mouse gasdermin-A3 by high-resolution time-lapse atomic force microscopy. We find that gasdermin-A3 oligomers assemble on the membrane surface where they remain attached and mobile. Once inserted into the membrane gasdermin-A3 grows variable oligomeric stoichiometries and shapes, each able to open transmembrane pores. Molecular dynamics simulations resolve how the membrane-inserted amphiphilic β-hairpins and the structurally adapting hydrophilic head domains stabilize variable oligomeric conformations and open the pore. The results show that without a vertical collapse gasdermin pore formation propagates along a set of multiple parallel but connected reaction pathways to ensure a robust cellular response.

Indexed as

PyroptosisAnimalsCell DeathCell MembraneGasderminsMiceMicroscopy, Atomic ForcePhosphate-Binding ProteinsPore Forming Cytotoxic ProteinsGasderminsGsdma3 protein, mousePhosphate-Binding ProteinsPore Forming Cytotoxic Proteins

Identifiers

PMID35545613
PMCPMC9095878
OpenAlexW4280525434

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.