Evidence map›Paper›PMID 31455540›Full record

ArticleMethods in enzymology2019

Monitoring gasdermin pore formation in vitro.

Shiyu Xia, Jianbin Ruan, Hao Wu

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.2field-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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. De novo discovery of bicyclic cysteine-rich peptides targeting gasdermin D.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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 2 institutions in 1 country.

Shiyu XiaProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, United States; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, United States.
Jianbin RuanProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, United States; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, United States. Electronic address: jianbin.ruan@childrens.harvard.edu.
Hao WuProgram in Cellular and Molecular Medicine, Boston Children's Hospital, Boston, MA, United States; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, United States. Electronic address: 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
NIAID NIH HHS R01 AI124491NIAID NIH HHS R01 AI139914NICHD NIH HHS DP1 HD087988
6 · The paper itself

Abstract

The gasdermin (GSDM) family consists of gasdermin A (GSDMA), B (GSDMB), C (GSDMC), D (GSDMD), E or DNFA5 (GSDME), and DFNB59 in human. Expressed in the skin, gastrointestinal tract, and various immune cells, GSDMs mediate homeostasis and inflammation upon activation by caspases and unknown proteases. In particular, GSDMD is activated by inflammasome-activated caspases-1/-4/-5/-11 as well as a caspase-8-mediated pathway during Yersinia infection. These caspases cleave GSDMD to release its functional N-terminal fragment (GSDMD-NT) from its auto-inhibitory C-terminal fragment (GSDMD-CT). GSDMD-NTs bind to acid lipids in mammalian cell membranes and bacterial membranes, oligomerize, and insert into the membranes to form large transmembrane pores. Consequently, cellular contents including inflammatory cytokines are released and cells can undergo pyroptosis, a highly inflammatory form of cell death. In this chapter, we summarize recent research findings and present experimental procedures to obtain pure recombinant GSDMs for biochemical studies. We highlight a liposome-based assay that yields robust fluorescence signals for characterizing GSDM activities in vitro and may be applicable to other pore-forming proteins and ion channels in general.

Indexed as

AnimalsBiomarkers, TumorCaspasesDNA-Binding ProteinsGasderminsHumansInflammasomesInflammationIntracellular Signaling Peptides and ProteinsLiposomesNeoplasm ProteinsNerve Tissue ProteinsPhosphate-Binding ProteinsPyroptosisReceptors, EstrogenBiomarkers, TumorCaspasesDNA-Binding ProteinsGasderminsGSDMA protein, humanGSDMB protein, humanGSDMC protein, humanGSDMD protein, humanGSDME protein, humanInflammasomesIntracellular Signaling Peptides and ProteinsLiposomesNeoplasm ProteinsNerve Tissue ProteinsPhosphate-Binding ProteinsPJVK protein, humanReceptors, EstrogenCaspasesGasderminImmunityInflammationLiposomePore-forming proteinPyroptosis

Identifiers

PMID31455540
PMCPMC7533106
OpenAlexW2945865676

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.