Evidence map›Paper›PMID 30761127›Full record

ArticleFrontiers in immunology2019

p31-43 Gliadin Peptide Forms Oligomers and Induces NLRP3 Inflammasome/Caspase 1- Dependent Mucosal Damage in Small Intestine.

María Florencia Gómez Castro, Emanuel Miculán, María Georgina Herrera, Carolina Ruera, Federico Perez, Eduardo Daniel Prieto, Exequiel Barrera, Sergio Pantano, Paula Carasi, Fernando Gabriel Chirdo

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Harnessing gut microbiome enzymes:Microbiology spectrum · 2026
    Article
  2. Frontiers in immunology · 2026
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  19. Dissecting the role of glutamine in seeding peptide aggregation.Computational and structural biotechnology journal · 2021
    Article
  20. Structural Perspective of Gliadin Peptides Active in Celiac Disease.International journal of molecular sciences · 2020
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

María Florencia Gómez CastroInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
Emanuel MiculánInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
María Georgina HerreraInstituto de Fisicoquímica y Químicas Biológicas, Dr. Alejandro Paladini (CONICET), Universidad de Buenos Aires, Buenos Aires, Argentina.
Carolina RueraInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
Federico PerezInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
Eduardo Daniel PrietoLaboratorio de Nanoscopía y Fisicoquímica de Superficies (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
Exequiel BarreraBiomolecular Simulations Group, Institut Pasteur de Montevideo, Montevideo, Uruguay.
Sergio PantanoBiomolecular Simulations Group, Institut Pasteur de Montevideo, Montevideo, Uruguay.
Paula CarasiInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
Fernando Gabriel ChirdoInstituto de Estudios Inmunológicos y Fisiopatológicos (CONICET), Universidad Nacional de La Plata, La Plata, Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversidad Nacional de La Plata · ARInstitut Pasteur de Montevideo · UYUniversity of Buenos Aires · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Celiac disease (CD) is a chronic enteropathy elicited by a Th1 response to gluten peptides in the small intestine of genetically susceptible individuals. However, it remains unclear what drives the induction of inflammatory responses of this kind against harmless antigens in food. In a recent work, we have shown that the p31-43 peptide (p31-43) from α-gliadin can induce an innate immune response in the intestine and that this may initiate pathological adaptive immunity. The receptors and mechanisms responsible for the induction of innate immunity by p31-43 are unknown and here we present evidence that this may reflect conformational changes in the peptide that allow it to activate the NLRP3 inflammasome. Administration of p31-43, but not scrambled or inverted peptides, to normal mice induced enteropathy in the proximal small intestine, associated with increased production of type I interferon and mature IL-1β. P31-43 showed a sequence-specific spontaneous ability to form structured oligomers and aggregates

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsApoptosisCaspase 1Celiac DiseaseDisease Models, AnimalDisease SusceptibilityGliadinInflammasomesIntestinal MucosaIntestine, SmallMaleMiceMice, TransgenicModels, MolecularCaspase 1Gliadingliadin p31-43InflammasomesNLR Family, Pyrin Domain-Containing 3 ProteinPeptide Fragmentscaspase-1celiac diseaseenteropathygliadin peptidesinflammasomeinnate immunityp31-43small intestine damage

Identifiers

PMID30761127
PMCPMC6363691
OpenAlexW2914047584

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.