Evidence map›Paper›PMID 29030601›Full record

ArticleScientific reports2017

Interfering with the high-affinity interaction between wheat amylase trypsin inhibitor CM3 and toll-like receptor 4: in silico and biosensor-based studies.

Massimiliano Cuccioloni, Matteo Mozzicafreddo, Laura Bonfili, Valentina Cecarini, Mara Giangrossi, Maurizio Falconi, Shin-Ichiroh Saitoh, Anna Maria Eleuteri, Mauro Angeletti

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
2.8field-weighted citation impact, top 9% 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, 39 citations in OpenAlex.

  1. Article
  2. Lower Diversity of Amylase-Trypsin Inhibitors andJournal of agricultural and food chemistry · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Genetic architecture underlying the expression of eight α-amylase trypsin inhibitors.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Wheat ATI CM3, CM16 and 0.28 Allergens Produced inPlants (Basel, Switzerland) · 2018
    Article
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

9 authors at 2 institutions in 2 countries.

Massimiliano CuccioloniSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy. massimiliano.cuccioloni@unicam.it.ORCID 0000-0002-6025-1990
Matteo MozzicafreddoSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.ORCID 0000-0001-9835-8446
Laura BonfiliSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.ORCID 0000-0002-9542-4310
Valentina CecariniSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.
Mara GiangrossiSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.
Maurizio FalconiSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.
Shin-Ichiroh SaitohDivision of Innate Immunity, Department of Microbiology and Immunology, The University of Tokyo, 4-6-1 Shirokanedai, Minatoku, Tokyo, 108 8639, Japan.
Anna Maria EleuteriSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.
Mauro AngelettiSchool of Biosciences and Biotechnology, University of Camerino, 62032, Camerino, Italy.
Università di Camerino · ITThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Wheat amylase/trypsin bi-functional inhibitors (ATIs) are protein stimulators of innate immune response, with a recently established role in promoting both gastrointestinal and extra-gastrointestinal inflammatory syndromes. These proteins have been reported to trigger downstream intestinal inflammation upon activation of TLR4, a member of the Toll-like family of proteins that activates signalling pathways and induces the expression of immune and pro-inflammatory genes. In this study, we demonstrated the ability of ATI to directly interact with TLR4 with nanomolar affinity, and we kinetically and structurally characterized the interaction between these macromolecules by means of a concerted approach based on surface plasmon resonance binding analyses and computational studies. On the strength of these results, we designed an oligopeptide capable of preventing the formation of the complex between ATI and the receptor.

Indexed as

Biosensing TechniquesPlant ProteinsProtein BindingSurface Plasmon ResonanceToll-Like Receptor 4TriticumTrypsin InhibitorsPlant ProteinsToll-Like Receptor 4Trypsin Inhibitors

Identifiers

PMID29030601
PMCPMC5640651
OpenAlexW2763840905

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.