Evidence map›Paper›PMID 20655837›Full record

ArticleBiophysical journal2010

Allosteric cross talk between cadherin extracellular domains.

Quanming Shi, Venkat Maruthamuthu, Fang Li, Deborah Leckband

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    Review
  4. Article
  5. Inside-out regulation of E-cadherin conformation and adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Metastasis review: from bench to bedside.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Review
  12. Tuning the kinetics of cadherin adhesion.The Journal of investigative dermatology · 2013
    Review
  13. Article
  14. Article
  15. Ideal, catch, and slip bonds in cadherin adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Cadherin recognition and adhesion.Current opinion in cell biology · 2012
    Review
  17. Article
  18. Review
  19. Modulation of E-cadherin function and dysfunction by N-glycosylation.Cellular and molecular life sciences : CMLS · 2011
    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

4 authors.

Quanming ShiDepartment of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Venkat Maruthamuthu
Fang Li
Deborah Leckband

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atomic force microscopy and surface force apparatus measurements determined the functional impact of the cadherin point mutation W2A and domain deletion mutations on C-cadherin binding signatures. Direct comparison of results obtained using both experimental approaches demonstrates that C-cadherin ectodomains form multiple independent bonds that require different structural regions. The results presented reveal significant interdomain cross talk. They further demonstrate that the mutation W2A not only abolishes adhesion between N-terminal domains, but allosterically modulates other binding states that require functional domains distal to the N-terminal binding site. Such allosteric effects may play a prominent role in modulating adhesion by Type I classic cadherins, cadherin oligomerization at junctional contacts, and propagation of binding information to the cytoplasmic region.

Indexed as

Allosteric RegulationAnimalsCadherinsCHO CellsCricetinaeCricetulusExtracellular SpaceHumansMicroscopy, Atomic ForceProtein Structure, TertiarySequence DeletionStructure-Activity RelationshipCadherins

Identifiers

PMID20655837
PMCPMC2895362

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.