Evidence map›Paper›PMID 12770907›Full record

ArticleBiophysical journal2003

Functional analysis of the structural basis of homophilic cadherin adhesion.

B Zhu, S Chappuis-Flament, E Wong, I E Jensen, B M Gumbiner, D Leckband

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 102 citations in OpenAlex.

  1. Review
  2. Mechanics of cell-cell junctions.Biophysical journal · 2023
    Article
  3. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  4. Article
  5. Cadherin cis and trans interactions are mutually cooperative.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
  8. Cadherin Extracellular Domain Clustering in the Absence ofThe journal of physical chemistry letters · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Tuning the kinetics of cadherin adhesion.The Journal of investigative dermatology · 2013
    Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

6 authors at 3 institutions in 1 country.

B ZhuDepartment of Chemical and Biomolecular Engineering, University of Illinois, Urbana, Illinois 61801, USA.
S Chappuis-Flament
E Wong
I E Jensen
B M Gumbiner
D Leckband
University of Illinois Urbana-Champaign · USRockefeller University · USUniversity of Virginia · US

Funding

BIOCHEMISTRY AND REGULATION OF CADHERIN ACTIVITYR01GM052717 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI GUMBINER, BARRY M. · 1996 to 2011
$4.2M
The Molecular Basis of Cadherin AdhesionR01GM051338 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI LECKBAND, DEBORAH E · 1999 to 2006
$1.6M
NIGMS NIH HHS R01 GM051338NIGMS NIH HHS R01 GM052717NIGMS NIH HHS R01 GM51338NIGMS NIH HHS R01 GM52717
6 · The paper itself

Abstract

The structures of many cell surface adhesion proteins comprise multiple tandem repeats of structurally similar domains. In many cases, the functional significance of this architecture is unknown, and there are several cases in which evidence for individual domain involvement in adhesion has been contradictory. In particular, the extracellular region of the adhesion glycoprotein cadherin consists of five tandemly arranged domains. One proposed mechanism postulated that adhesion involves only trans interactions between the outermost domains. However, subsequent investigations have generated several competing models. Here we describe direct measurements of the distance-dependent interaction potentials between cadherin mutants lacking different domains. By quantifying both the absolute distances at which opposed cadherin fragments bind and the quantized changes in the interaction potentials that result from deletions of individual domains, we demonstrate that two domains participate in homophilic cadherin binding. This finding contrasts with the current view that cadherins bind via a single, unique site on the protein surface. The potentials that result from interactions involving multiple domains generate a novel, modular binding mechanism in which opposed cadherin ectodomains can adhere in any of three antiparallel alignments.

Indexed as

Protein BindingStructure-Activity RelationshipBinding SitesCadherinsCell AdhesionDimerizationElasticityEnergy TransferMacromolecular SubstancesMutationProtein ConformationProtein Structure, TertiaryStress, MechanicalSurface PropertiesCadherinsMacromolecular Substances

Identifiers

PMID12770907
PMCPMC1302983
OpenAlexW2075574902

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.