Evidence map›Paper›PMID 27760104›Full record

ReviewNature immunology2016

Epithelial glycosylation in gut homeostasis and inflammation.

Yoshiyuki Goto, Satoshi Uematsu, Hiroshi Kiyono

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed
7.3field-weighted citation impact, top 2% 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

107 citing papers in PubMed, 216 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
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  6. Review
  7. Article
  8. FUT2-Mediated Fucosylation of OLFM4 Promotes Colon Cancer Cell Differentiation.Canadian journal of gastroenterology & hepatology · 2026
    Article
  9. Emerging Mechanistic Links Between Fucosylation and Senescence in Lung Diseases.Journal of respiratory biology and translational medicine · 2026
    Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Host-pathobiont interactions in Crohn's disease.Nature reviews. Gastroenterology & hepatology · 2025
    Review
  16. Journal of diabetes and metabolic disorders · 2025
    Review
  17. Article
  18. St3gal5-mediated sialylation of glyco-CD177 on neutrophils restricts neuroinflammation following CNS injury.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. OralFrontiers in cellular and infection microbiology · 2025
    Review

47 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 2 institutions in 1 country.

Yoshiyuki GotoDivision of Molecular Immunology, Medical Mycology Research Center, Chiba University, Chiba, Japan.
Satoshi UematsuInternational Research and Development Center for Mucosal Vaccines, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
Hiroshi KiyonoInternational Research and Development Center for Mucosal Vaccines, The Institute of Medical Science, The University of Tokyo, Tokyo, Japan.
The University of Tokyo · JPChiba University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intestinal epithelial cells apically express glycans, especially α1,2-fucosyl linkages, which work as a biological interface for the host-microbe interaction. Emerging studies have shown that epithelial α1,2-fucosylation is regulated by microbes and by group 3 innate lymphoid cells (ILC3s). Dysregulation of the gene (FUT2) encoding fucosyltransferase 2, an enzyme governing epithelial α1,2-fucosylation, is associated with various human disorders, including infection and chronic inflammatory diseases. This suggests a critical role for an interaction between microbes, epithelial cells and ILC3s mediated via glycan residues. In this Review, using α1,2-fucose and Fut2 gene expression as an example, we describe how epithelial glycosylation is controlled by immune cells and luminal microbes. We also address the pathophysiological contribution of epithelial α1,2-fucosylation to pathogenic and commensal microbes as well as the potential of α1,2-fucose and its regulatory pathway as previously unexploited targets in the development of new therapeutic approaches for human diseases.

Indexed as

HomeostasisAnimalsCarbohydrate MetabolismCarbohydratesFucoseFucosyltransferasesGalactoside 2-alpha-L-fucosyltransferaseGastroenteritisGenetic Predisposition to DiseaseGlycosylationHost-Pathogen InteractionsHumansImmunity, InnateImmunity, MucosalIntestinal MucosaLymphocytesCarbohydratesFucoseFucosyltransferasesGalactoside 2-alpha-L-fucosyltransferase

Identifiers

PMID27760104
OpenAlexW2536381222

What OpenQuestion holds

Textmetadata
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.