Evidence map›Paper›PMID 11853539›Full record

ArticleThe Biochemical journal2002

Molecular interactions between desmosomal cadherins.

Shabih-e-Hassnain Syed, Brian Trinnaman, Stephen Martin, Sarah Major, Jon Hutchinson, Anthony I Magee

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.6field-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

48 citing papers in PubMed, 106 citations in OpenAlex.

  1. Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026
    Review
  2. Comprehensive analysis of desmosomal protein remodelling identifies desmocollin-2 as potential biomarker for arrhythmogenic cardiomyopathy.Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology · 2025
    Article
  3. Review
  4. Article
  5. Immunobiology of Atherosclerosis: A Complex Net of Interactions.International journal of molecular sciences · 2019
    Review
  6. Article
  7. Review
  8. Article
  9. EnteropathogenicCellular and molecular gastroenterology and hepatology · 2018
    Article
  10. Mechanisms of foam cell formation in atherosclerosis.Journal of molecular medicine (Berlin, Germany) · 2017
    Review
  11. Article
  12. Structural basis of adhesive binding by desmocollins and desmogleins.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Mechanistic basis of desmosome-targeted diseases.Journal of molecular biology · 2013
    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

6 authors at 2 institutions in 2 countries.

Shabih-e-Hassnain SyedDivision of Membrane Biology, The National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
Brian Trinnaman
Stephen Martin
Sarah Major
Jon Hutchinson
Anthony I Magee
National Institute for Medical Research · TZRoyal National Institute of Blind · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Desmocollins (Dscs) and desmogleins (Dsgs) are cell-adhesion molecules involved in the formation of desmosome cell-cell junctions and share structural similarities to classical cadherins such as E-cadherin. In order to identify and provide quantitative information on the types of protein-protein interactions displayed by the type 2 isoforms and investigate the role of Ca(2+) in this process, we have developed an Escherichia coli expression system to generate recombinant proteins containing the first two extracellular domains, namely Dsg2(1-2) and Dsc2(1-2). Analytical ultracentrifugation, chemical cross-linking, CD, fluorescence and BIAcore have been used to provide the first direct evidence of Ca(2+) binding to desmosomal cadherins. These studies suggest that Dsc2(1-2) not only exhibits homophilic interactions in solution, but can also form heterophilic interactions with Dsg2(1-2). The latter, on the other hand, shows much weaker homophilic association. Our results further demonstrate that heterophilic interactions are Ca(2+)-dependent, whereas the Ca(2+)-dependence of homophilic association is less clear. Our data indicate that the functional properties of Dsc2(1-2) are more similar to those of classical cadherins, consistent with the observation that Dsc shares a higher level of sequence homology with classical cadherins than does Dsg. In addition to corroborating the conclusions of previously reported transfection studies which suggest the formation of lateral heterodimers and homodimers, our results also provide direct quantitative information on the strength of these interactions which are essential for understanding the adhesion mechanism.

Indexed as

Binding SitesCadherinsCalciumCell Adhesion MoleculesCircular DichroismCloning, MolecularCross-Linking ReagentsCytoskeletal ProteinsDesmocollinsDesmoglein 2DesmogleinsDesmoplakinsDesmosomesDNA PrimersHumansPeptide FragmentsCadherinsCalciumCell Adhesion MoleculesCross-Linking ReagentsCytoskeletal ProteinsDesmocollinsDesmoglein 2DesmogleinsDesmoplakinsDNA PrimersDSG2 protein, humanPeptide FragmentsProtein SubunitsRecombinant Proteins

Identifiers

PMID11853539
PMCPMC1222391
OpenAlexW1997468335

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.