Evidence map›Paper›PMID 31690840›Full record

ReviewNature reviews. Immunology2020

The gasdermins, a protein family executing cell death and inflammation.

Petr Broz, Pablo Pelegrín, Feng Shao

2 registry-linked trialsOpen access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Immunology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to 2 registered trials, which are not on this map. Cited by 961 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
961citing papers in PubMed, 2 pooled it
52.7field-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.

NCT05475951 nacompletednot on this mapstarted 2021, after this paper: background citation

Investigation of Gasdermin-D and Pannexin-1 in Fat and Placental Tissues in Pregnant Women With Obesity

TypeinterventionalSponsorHaseki Training and Research HospitalRan2021 to 2022Enrolled79ConditionsPregnancy Complications, Maternal ObesityArmsBiomarker measurement of pannexin-1 and gasdermin-D
NCT06584643 unknown statusnot on this mapstarted 2024, after this paper: background citation

Evaluation of Serum Gasdermin D Level As a Potential Biomarker of Disease Activity in Vitiligo Patients

TypeobservationalSponsorAssiut UniversityRan2024 to 2025Enrolled84ConditionsSerum Gasdermin D in VitiligoArmsgasdermin d
3 · Its place in the literature

Who cites it

961 citing papers in PubMed, 2 syntheses or guidelines pooled it, 1,563 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Article
  5. Article
  6. The gasdermin family: from pyroptosis mechanisms to therapeutic targets.Signal transduction and targeted therapy · 2026
    Review
  7. Article
  8. Article
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  10. Review
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  12. Observational
  13. Associations ofBiomolecules · 2026
    Article
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  15. Review
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  20. 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

901 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

3 authors at 3 institutions in 3 countries.

Petr BrozDepartment of Biochemistry, University of Lausanne, Epalinges, Switzerland. petr.broz@unil.ch.ORCID http://orcid.org/0000-0002-2334-7790
Pablo PelegrínBiomedical Research Institute of Murcia (IMIB-Arrixaca), University Clinical Hospital 'Virgen de la Arrixaca', Murcia, Spain. pablo.pelegrin@imib.es.ORCID http://orcid.org/0000-0002-9688-1804
Feng ShaoNational Institute of Biological Sciences, Beijing, China. shaofeng@nibs.ac.cn.ORCID http://orcid.org/0000-0002-9562-7791
Instituto Murciano de Investigación Biosanitaria · ESNational Institute of Biological Sciences, Beijing · CNUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gasdermins are a family of recently identified pore-forming effector proteins that cause membrane permeabilization and pyroptosis, a lytic pro-inflammatory type of cell death. Gasdermins contain a cytotoxic N-terminal domain and a C-terminal repressor domain connected by a flexible linker. Proteolytic cleavage between these two domains releases the intramolecular inhibition on the cytotoxic domain, allowing it to insert into cell membranes and form large oligomeric pores, which disrupts ion homeostasis and induces cell death. Gasdermin-induced pyroptosis plays a prominent role in many hereditary diseases and (auto)inflammatory disorders as well as in cancer. In this Review, we discuss recent developments in gasdermin research with a focus on mechanisms that control gasdermin activation, pore formation and functional consequences of gasdermin-induced membrane permeabilization.

Indexed as

Cell DeathCell MembraneCell Membrane PermeabilityHumansInflammationNeoplasm ProteinsPyroptosisNeoplasm Proteins

Identifiers

PMID31690840
OpenAlexW2983652778

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.