Evidence map›Paper›PMID 35532156›Full record

ArticleFEBS letters2022

Cadherins can dimerize via asymmetric interactions.

Andrew Vae Priest, Ramesh Koirala, Sanjeevi Sivasankar

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Engineering the Interactions of Classical Cadherin Cell-Cell Adhesion Proteins.Journal of immunology (Baltimore, Md. : 1950) · 2023
    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

3 authors at 1 institution in 1 country.

Andrew Vae PriestDepartment of Biomedical Engineering, University of California, Davis, CA, USA.
Ramesh KoiralaDepartment of Biomedical Engineering, University of California, Davis, CA, USA.
Sanjeevi SivasankarDepartment of Biomedical Engineering, University of California, Davis, CA, USA.ORCID 0000-0003-2593-0477
University of California, Davis · US

Funding

Microscope for ultrasensitive measurement of single-molecule interaction and conformationR01GM121885 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SIVASANKAR, SANJEEVI · 2017 to 2024
$2.5M
Mechanosensitive cadherin adhesion and its regulationR01GM133880 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI SIVASANKAR, SANJEEVI · 2021 to 2024
$1.5M
NIGMS NIH HHS R01 GM121885NIGMS NIH HHS R01 GM133880
6 · The paper itself

Abstract

Cadherins are essential cell-cell adhesion proteins that interact in two distinct conformations: X-dimers and strand-swap dimers. Both X-dimers and strand-swap dimers are thought to exclusively rely on symmetric sets of interactions between key amino acids on both cadherin binding partners. Here, we use single-molecule atomic force microscopy and computer simulations to show that symmetry in cadherin binding is dispensable and that cadherins can also interact in a novel conformation that asymmetrically incorporates key elements of both strand-swap dimers and X-dimers. Our results clarify the biophysical rules for cadherin binding and demonstrate that cadherins interact in a more diverse range of conformations than previously understood.

Indexed as

CadherinsCell AdhesionDimerizationProtein BindingProtein MultimerizationCadherinsAFM force measurementsclassical cadherinsmolecular dynamicsstrand-swap dimertrans interactionsX-dimer

Identifiers

PMID35532156
PMCPMC9829383
OpenAlexW4229445978

What OpenQuestion holds

Textmetadata
LicenceTDM
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.