ArticleeLife2016
Antiparallel protocadherin homodimers use distinct affinity- and specificity-mediating regions in cadherin repeats 1-4.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 58 citations in OpenAlex.
- Structural Insights into Ordered Multicomponent Assemblies in Cell Junctions.Advances in experimental medicine and biology · 2026Review
- Surface delivery quantification reveals distinct trafficking efficiencies among clustered protocadherin isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Clustered protocadherinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Visualization ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- γ-Protocadherins control synapse formation and peripheral branching of touch sensory neurons.Neuron · 2023Article
- On the formation of ordered protein assemblies in cell-cell interfaces.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Collective mechanical responses of cadherin-based adhesive junctions as predicted by simulations.Biophysical journal · 2022Article
- Elastic versus brittle mechanical responses predicted for dimeric cadherin complexes.Biophysical journal · 2022Article
- How clustered protocadherin binding specificity is tuned for neuronal self-/nonself-recognition.eLife · 2022Article
- The Conserved Serine Transporter SdaC Moonlights To Enable Self Recognition.Journal of bacteriology · 2022Article
- Viscoelasticity, Like Forces, Plays a Role in Mechanotransduction.Frontiers in cell and developmental biology · 2022Review
- Heterophilic and homophilic cadherin interactions in intestinal intermicrovillar links are species dependent.PLoS biology · 2021Article
- Mechanism of dimerization and structural features of human LI-cadherin.The Journal of biological chemistry · 2021Article
- Crystal structure of the nonclassical cadherin-17 N-terminus and implications for its adhesive binding mechanism.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Wiring the Brain by Clustered Protocadherin Neural Codes.Neuroscience bulletin · 2021Review
- Chelicerata sDscam isoforms combine homophilic specificities to define unique cell recognition.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Expression of protocadherin-γC4 protein in the rat brain.The Journal of comparative neurology · 2020Article
- Family-wide Structural and Biophysical Analysis of Binding Interactions among Non-clustered δ-Protocadherins.Cell reports · 2020Article
- Protocadherins at the Crossroad of Signaling Pathways.Frontiers in molecular neuroscience · 2020Review
- Clustered Protocadherins Emerge as Novel Susceptibility Loci for Mental Disorders.Frontiers in neuroscience · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
Protocadherins (Pcdhs) are cell adhesion and signaling proteins used by neurons to develop and maintain neuronal networks, relying on trans homophilic interactions between their extracellular cadherin (EC) repeat domains. We present the structure of the antiparallel EC1-4 homodimer of human PcdhγB3, a member of the γ subfamily of clustered Pcdhs. Structure and sequence comparisons of α, β, and γ clustered Pcdh isoforms illustrate that subfamilies encode specificity in distinct ways through diversification of loop region structure and composition in EC2 and EC3, which contains isoform-specific conservation of primarily polar residues. In contrast, the EC1/EC4 interface comprises hydrophobic interactions that provide non-selective dimerization affinity. Using sequence coevolution analysis, we found evidence for a similar antiparallel EC1-4 interaction in non-clustered Pcdh families. We thus deduce that the EC1-4 antiparallel homodimer is a general interaction strategy that evolved before the divergence of these distinct protocadherin families.
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.