ArticleNeuron2016
Structural Basis of Diverse Homophilic Recognition by Clustered α- and β-Protocadherins.
Article in Neuron, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed.
- Protocadherin γC4 regulates neuronal survival and dendritic self-avoidance.Communications biology · 2026Article
- Reduced Neuronal Self-Avoidance in Mouse Starburst Amacrine Cells With Only One Pcdhg Isoform.Developmental neurobiology · 2026Article
- 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
- Astrocyte morphogenesis requires self-recognition.Nature · 2025Article
- Diversity of clustered protocadherin-α genes in neuronal identity and its role in short-term specific associative memory formation.Scientific reports · 2025Article
- Reduced neuronal self-avoidance in mouse starburst amacrine cells with only onebioRxiv : the preprint server for biology · 2025Article
- Structural basis for regulation of CELSR1 by a compact module in its extracellular region.Nature communications · 2025Article
- Structural insights into the in situ assembly of clustered protocadherin γB4.Nature communications · 2025Article
- Clustered protocadherinProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mapping combinatorial expression of non-clustered protocadherins in the developing brain identifies novel PCDH19-mediated cell adhesion properties.Open biology · 2024Article
- PCDHA9 as a candidate gene for amyotrophic lateral sclerosis.Nature communications · 2024Article
- Visualization ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Visualization ofiScience · 2023Article
- γ-Protocadherins control synapse formation and peripheral branching of touch sensory neurons.Neuron · 2023Article
- The structure of fly Teneurin-m reveals an asymmetric self-assembly that allows expansion into zippers.EMBO reports · 2023Article
- Structure of the planar cell polarity cadherins Fat4 and Dachsous1.Nature communications · 2023Article
- A Unique Role for Protocadherin γC3 in Promoting Dendrite Arborization through an Axin1-Dependent Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Ubiquitination of the protocadherin-γA3 variable cytoplasmic domain modulates cell-cell interaction.Frontiers in cell and developmental biology · 2023Article
- Protocadherin gamma C3: a new player in regulating vascular barrier function.Neural regeneration research · 2023Review
- 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
5 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
10 authors.
Funding
Abstract
Clustered protocadherin proteins (α-, β-, and γ-Pcdhs) provide a high level of cell-surface diversity to individual vertebrate neurons, engaging in highly specific homophilic interactions to mediate important roles in mammalian neural circuit development. How Pcdhs bind homophilically through their extracellular cadherin (EC) domains among dozens of highly similar isoforms has not been determined. Here, we report crystal structures for extracellular regions from four mouse Pcdh isoforms (α4, α7, β6, and β8), revealing a canonical head-to-tail interaction mode for homophilic trans dimers comprising primary intermolecular EC1:EC4 and EC2:EC3 interactions. A subset of trans interface residues exhibit isoform-specific conservation, suggesting roles in recognition specificity. Mutation of these residues, along with trans-interacting partner residues, altered the specificities of Pcdh interactions. Together, these data show how sequence variation among Pcdh isoforms encodes their diverse strict homophilic recognition specificities, which are required for their key roles in neural circuit assembly.
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.