Evidence map›Paper›PMID 32404934›Full record

ArticleNature communications2020

Trefoil factors share a lectin activity that defines their role in mucus.

Michael A Järvå, James P Lingford, Alan John, Niccolay Madiedo Soler, Nichollas E Scott, Ethan D Goddard-Borger

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.5field-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

30 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
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  10. Goblet cell differentiation subgroups in colorectal cancer.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. A novel cysteine-rich adaptor protein is required for mucin packaging and secretory granule stability in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. Review
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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

6 authors at 1 institution in 1 country.

Michael A JärvåThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.ORCID http://orcid.org/0000-0002-8519-5622
James P LingfordThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.
Alan JohnThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.
Niccolay Madiedo SolerThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia.
Nichollas E ScottDepartment of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Parkville, VIC, 3010, Australia.ORCID http://orcid.org/0000-0003-2556-8316
Ethan D Goddard-BorgerThe Walter and Eliza Hall Institute of Medical Research, Parkville, VIC, 3052, Australia. goddard-borger.e@wehi.edu.au.ORCID http://orcid.org/0000-0002-8181-9733
The University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mucosal epithelium secretes a host of protective disulfide-rich peptides, including the trefoil factors (TFFs). The TFFs increase the viscoelasticity of the mucosa and promote cell migration, though the molecular mechanisms underlying these functions have remained poorly defined. Here, we demonstrate that all TFFs are divalent lectins that recognise the GlcNAc-α-1,4-Gal disaccharide, which terminates some mucin-like O-glycans. Degradation of this disaccharide by a glycoside hydrolase abrogates TFF binding to mucins. Structural, mutagenic and biophysical data provide insights into how the TFFs recognise this disaccharide and rationalise their ability to modulate the physical properties of mucus across different pH ranges. These data reveal that TFF activity is dependent on the glycosylation state of mucosal glycoproteins and alludes to a lectin function for trefoil domains in other human proteins.

Indexed as

Crystallography, X-RayDisaccharidesGlycoside HydrolasesHumansHydrogen BondingHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsLectinsLigandsMass SpectrometryMucinsMucusPhylogenyPolysaccharidesTrefoil Factor-1Trefoil Factor-3DisaccharidesGlycoside HydrolasesLectinsLigandsMucinsPolysaccharidesTrefoil Factor-1Trefoil Factor-3

Identifiers

PMID32404934
PMCPMC7221086
OpenAlexW3024833905

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.