Evidence map›Paper›PMID 29531885›Full record

ReviewChemistryOpen2018

Translational Chemistry Meets Gluten-Related Disorders.

Karen M Lammers, Maria G Herrera, Veronica I Dodero

Open access · goldAbstract readReview
In one paragraph

Review in ChemistryOpen, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. A short update on new approaches to celiac disease.Acta bio-medica : Atenei Parmensis · 2022
    Review
  5. Thin-Plate Superstructures of the Immunogenic 33-mer Gliadin Peptide.Chembiochem : a European journal of chemical biology · 2022
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Review
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.

Karen M LammersLaboratory Immunogenetics, Department of Medical Microbiology and Infection Control VU University Medical Center 1081 Amsterdam Netherlands.
Maria G HerreraFaculty of Pharmacy and Biochemistry Institute of biological chemistry and Physicochemical CONICET-University of Buenos Aires Junín 956 C1113AAD Buenos Aires Argentina.
Veronica I DoderoDepartment of Chemistry, Organic Chemistry III Bielefeld University Universitätsstraße 25 33615 Bielefeld Germany.ORCID 0000-0001-7937-1880
Amsterdam UMC Location Vrije Universiteit Amsterdam · NLBielefeld University · DEConsejo Nacional de Investigaciones Científicas y Técnicas · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gluten-related disorders are a complex group of diseases that involve the activation of the immune system triggered by the ingestion of gluten. Among these, celiac disease, with a prevalence of 1 %, is the most investigated, but recently, a new pathology, named nonceliac gluten sensitivity, was reported with a general prevalence of 7 %. Finally, there other less-prevalent gluten-related diseases such as wheat allergy, gluten ataxia, and dermatitis herpetiformis (with an overall prevalence of less than 0.1 %). As mentioned, the common molecular trigger is gluten, a complex mixture of storage proteins present in wheat, barley, and a variety of oats that are not fully degraded by humans. The most-studied protein related to disease is gliadin, present in wheat, which possesses in its sequence many pathological fragments. Despite a lot of effort to treat these disorders, the only effective method is a long-life gluten-free diet. This Review summarizes the actual knowledge of gluten-related disorders from a translational chemistry point of view. We discuss what is currently known from the literature about the interaction of gluten with the gut and the critical host responses it evokes and, finally, connect them to our current and novel molecular understanding of the supramolecular organization of gliadin and the 33-mer gliadin peptide fragment under physiological conditions.

Indexed as

gluten-related disordersimmunologyoligomerizationpeptidesprotein structures

Identifiers

PMID29531885
PMCPMC5838388
OpenAlexW2793100952

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.