ReviewTrends in cell biology2012
Thinking outside the cell: how cadherins drive adhesion.
Review in Trends in cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers.
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.
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.
Who cites it
177 citing papers in PubMed, 340 citations in OpenAlex.
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- RET receptor tyrosine kinase architecture, assemblies, and activation.Endocrine-related cancer · 2026Review
- Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026Review
- Reorganization of E-cadherin into apical spot junctions mediates interlineage adhesion between epithelial and germline cells.Frontiers in cell and developmental biology · 2026Article
- Antigens in membranous nephropathy: discovery and clinical implications.Nature reviews. Nephrology · 2025Review
- The dual role of PCDH9 in tumors, neurological and developmental diseases.Medical oncology (Northwood, London, England) · 2025Review
- Role of vinculin in the structural dynamics of cadherin-catenin complexes and its implications for F-actin binding.Protein science : a publication of the Protein Society · 2025Article
- Polyacrylic Acid-Coated LaBPharmaceutics · 2025Article
- IgStrand: A universal residue numbering scheme for the immunoglobulin-fold (Ig-fold) to study Ig-proteomes and Ig-interactomes.PLoS computational biology · 2025Review
- Nervous system-wide analysis of allScience advances · 2025Article
- Actin-dependent α-catenin oligomerization contributes to adherens junction assembly.Nature communications · 2025Article
- Identification of Amino Acid Residues Critical for the Interaction of Fibrin with N-Cadherin.Biochemistry · 2025Article
- Effect of heat stress on ileal epithelial barrier integrity in broilers divergently selected for high- and low-water efficiency.Frontiers in physiology · 2025Article
- Dsg2 ectodomain organization increases throughout desmosome assembly.Cell adhesion & migration · 2024Article
- Afadin mediates cadherin-catenin complex clustering on F-actin linked to cooperative binding and filament curvature.bioRxiv : the preprint server for biology · 2024Article
- Nanoscale dynamics of the cadherin-catenin complex bound to vinculin revealed by neutron spin echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Activity-dependent diffusion trapping of AMPA receptors as a key step for expression of early LTP.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Article
- Adherens junctions as molecular regulators of emergent tissue mechanics.Nature reviews. Molecular cell biology · 2024Review
- Characterization of early and late events of adherens junction assembly.bioRxiv : the preprint server for biology · 2024Article
117 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cadherins are a superfamily of cell surface glycoproteins whose ectodomains contain multiple repeats of β-sandwich extracellular cadherin (EC) domains that adopt a similar fold to immunoglobulin domains. The best characterized cadherins are the vertebrate 'classical' cadherins, which mediate adhesion via trans homodimerization between their membrane-distal EC1 domains that extend from apposed cells, and assemble intercellular adherens junctions through cis clustering. To form mature trans adhesive dimers, cadherin domains from apposed cells dimerize in a 'strand-swapped' conformation. This occurs in a two-step binding process involving a fast-binding intermediate called the 'X-dimer'. Trans dimers are less flexible than cadherin monomers, a factor that drives junction assembly following cell-cell contact by reducing the entropic cost associated with the formation of lateral cis oligomers. Cadherins outside the classical subfamily appear to have evolved distinct adhesive mechanisms that are only now beginning to be understood.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.