ArticleCell2013
An extracellular interactome of immunoglobulin and LRR proteins reveals receptor-ligand networks.
Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.
What it found
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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.
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Who cites it
152 citing papers in PubMed, 252 citations in OpenAlex.
- The teneurin TEN-1 and its ligand LRON-11 support microbiota-induced neuroprotection and mechanosensory function in C. elegans.Current biology : CB · 2026Article
- Mapping and engineering the human cell-cell interactome.Nature biotechnology · 2026Review
- Beat- and Side-family cell-surface molecules are expressed combinatorially in the partner neurons of the olfactory circuit in Drosophila.PLoS biology · 2026Article
- Structure of the Beat-Side complex reveals their interaction is required for neuromuscular system wiring.Cell reports · 2026Article
- Beyond Hemostasis: Platelets' Multifaceted Functions in Immune Responses.Life (Basel, Switzerland) · 2026Review
- Nematode extracellular protein interactome expands connections between signaling pathways.Cell genomics · 2026Article
- A dating app for extracellular adhesion proteins.Cell genomics · 2026Article
- Selective regulation of transsynaptic alignment and postsynaptic assembly by a novel NCAM family synaptic adhesion molecule.bioRxiv : the preprint server for biology · 2026Article
- Beat II and Side IV keep migrating longitudinal visceral muscle precursor cells on their substratum in Drosophila.Journal of cell science · 2026Article
- A trans-synaptic IgLON adhesion molecular complex directly contacts and clusters a nicotinic receptor.Nature communications · 2026Article
- Article
- Approaches to deorphanize secretome: Classical, computational, and next generation strategies to reveal ligand-receptor networks.EXO : beyond the cell · 2026Article
- A critical affinity window for IgSF proteins DIP-α and Dpr10 is required for proper motor neuron arborization.Genes & development · 2025Article
- Formation of sensory maps: New tools reveal novel insights into neural development.Current opinion in neurobiology · 2025Review
- A gene expression atlas of a juvenile nervous system.bioRxiv : the preprint server for biology · 2025Article
- Hippo signaling regulates cuticle pigmentation and dopamine metabolism inbioRxiv : the preprint server for biology · 2025Article
- FETCH enables fluorescent labeling of membrane proteins in vivo with spatiotemporal control inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis and functional roles for Toll-like receptor binding to Latrophilin in C. elegans development.Nature structural & molecular biology · 2025Article
- Article
- Repulsive interactions instruct synaptic partner matching in an olfactory circuit.bioRxiv : the preprint server for biology · 2025Article
92 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Extracellular domains of cell surface receptors and ligands mediate cell-cell communication, adhesion, and initiation of signaling events, but most existing protein-protein "interactome" data sets lack information for extracellular interactions. We probed interactions between receptor extracellular domains, focusing on a set of 202 proteins composed of the Drosophila melanogaster immunoglobulin superfamily (IgSF), fibronectin type III (FnIII), and leucine-rich repeat (LRR) families, which are known to be important in neuronal and developmental functions. Out of 20,503 candidate protein pairs tested, we observed 106 interactions, 83 of which were previously unknown. We "deorphanized" the 20 member subfamily of defective-in-proboscis-response IgSF proteins, showing that they selectively interact with an 11 member subfamily of previously uncharacterized IgSF proteins. Both subfamilies interact with a single common "orphan" LRR protein. We also observed interactions between Hedgehog and EGFR pathway components. Several of these interactions could be visualized in live-dissected embryos, demonstrating that this approach can identify physiologically relevant receptor-ligand pairs.
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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.