Evidence map›Paper›PMID 29695864›Full record

ArticleNature2018

Cryo-EM structure of the gasdermin A3 membrane pore.

Jianbin Ruan, Shiyu Xia, Xing Liu, Judy Lieberman, Hao Wu

Open access · greenAbstract read
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 257 papers.

0numbers the graph read from it
0cells of the map it votes in
257citing papers in PubMed
16.6field-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

257 citing papers in PubMed, 388 citations in OpenAlex.

  1. The gasdermin family: from pyroptosis mechanisms to therapeutic targets.Signal transduction and targeted therapy · 2026
    Review
  2. Review
  3. Review
  4. Structural basis of GSDME pore formation and its regulation by S-palmitoylation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Review
  7. Structural and molecular principles of DAMP biology.Nature structural & molecular biology · 2026
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Pyroptosis: Turning Up the Heat on Cancer.Annual review of immunology · 2026
    Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Teleost GSDMEc regulates GSDMEa-mediated pyroptosis.Journal of advanced research · 2026
    Article

197 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

5 authors at 2 institutions in 1 country.

Jianbin RuanProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Shiyu XiaProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Xing LiuProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Judy LiebermanProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA.
Hao WuProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, USA. wu@crystal.harvard.edu.
Boston Children's Hospital · USHarvard University · US

Funding

NLRP1 and CARD8 Inflammasomes: Assembly, Regulation and Stress SensingR01AI124491 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI WU, HAO · 2016 to 2025
$5.1M
SMOCs: Novel Signal Transduction Complexes as New Targets for Drug DiscoveryDP1HD087988 · NICHD · BOSTON CHILDREN'S HOSPITAL · PI WU, HAO · 2015 to 2019
$4.4M
Elucidating the structural mechanism of pore formation by the (GSDM) Gasdermin familyR01AI139914 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI WU, HAO · 2018 to 2022
$2.6M
Granulysin, Granzymes and Perforin in Bacterial Immune DefenseR01AI123265 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI LIEBERMAN, JUDY · 2016 to 2020
$2.2M
NIAID NIH HHS R01 AI123265NIAID NIH HHS R01 AI124491NIAID NIH HHS R01 AI139914NICHD NIH HHS DP1 HD087988
6 · The paper itself

Abstract

Gasdermins mediate inflammatory cell death after cleavage by caspases or other, unknown enzymes. The cleaved N-terminal fragments bind to acidic membrane lipids to form pores, but the mechanism of pore formation remains unresolved. Here we present the cryo-electron microscopy structures of the 27-fold and 28-fold single-ring pores formed by the N-terminal fragment of mouse GSDMA3 (GSDMA3-NT) at 3.8 and 4.2 Å resolutions, and of a double-ring pore at 4.6 Å resolution. In the 27-fold pore, a 108-stranded anti-parallel β-barrel is formed by two β-hairpins from each subunit capped by a globular domain. We identify a positively charged helix that interacts with the acidic lipid cardiolipin. GSDMA3-NT undergoes radical conformational changes upon membrane insertion to form long, membrane-spanning β-strands. We also observe an unexpected additional symmetric ring of GSDMA3-NT subunits that does not insert into the membrane in the double-ring pore, which may represent a pre-pore state of GSDMA3-NT. These structures provide a basis that explains the activities of several mutant gasdermins, including defective mutants that are associated with cancer.

Indexed as

Cryoelectron MicroscopyAnimalsCell MembraneGasderminsHumansIntracellular Signaling Peptides and ProteinsMembrane LipidsMiceModels, MolecularMutant ProteinsMutationNeoplasm ProteinsNeoplasmsPerforinPhosphate-Binding ProteinsProtein ConformationGasderminsGsdma3 protein, mouseGSDMD protein, humanIntracellular Signaling Peptides and ProteinsMembrane LipidsMutant ProteinsNeoplasm ProteinsPerforinPhosphate-Binding ProteinsProteinsProtein Subunits

Identifiers

PMID29695864
PMCPMC6007975
OpenAlexW2802099741

What OpenQuestion holds

Textmetadata
LicenceTDM
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.