ArticleNeuron2007
Structures of neuroligin-1 and the neuroligin-1/neurexin-1 beta complex reveal specific protein-protein and protein-Ca2+ interactions.
Article in Neuron, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 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
128 citing papers in PubMed.
- Transcriptomics and machine learning predict diagnosis and severity of growth hormone deficiency.JCI insight · 2018Trial
- Neuroligin-3-CSPG4 interaction maintains oligodendrocyte precursor cell progenitor state and promotes glioma proliferation through mechanotransduction.Nature neuroscience · 2026Article
- Neuroligins and Neuropathic Pain: Insights into Synaptic Plasticity and Pain Transmission.Biology · 2026Review
- Nematode extracellular protein interactome expands connections between signaling pathways.Cell genomics · 2026Article
- Weaker neuroligin 2-neurexin β1 interaction tethers membranes and recruits gephyrin at membrane junctions through clustering.Science advances · 2026Article
- Roles of NRXN1 in neuropsychiatric disorders: from genetic lesion to molecular mechanism.Frontiers in neuroscience · 2026Review
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Structural basis for regulation of CELSR1 by a compact module in its extracellular region.Nature communications · 2025Article
- Uncovering synaptic and cellular nanoarchitecture of brain tissue via seamlessbioRxiv : the preprint server for biology · 2025Article
- Article
- Perturbed synaptic adhesion molecules signaling in neurodevelopmental disorders: The impact of metal neurotoxicity.Ibrain · 2025Review
- Monitoring Synapses via Trans-synaptic GFP Complementation.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Chronic stress induces depression through MDGA1-Neuroligin2 mediated suppression of inhibitory synapses in the lateral habenula.Theranostics · 2025Article
- A Systematic Structure-Function Characterization of a Human Mutation in Neurexin-3α Reveals an Extracellular Modulatory Sequence That Stabilizes Neuroligin-1 Binding to Enhance the Postsynaptic Properties of Excitatory Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Nematode Extracellular Protein Interactome Expands Connections between Signaling Pathways.bioRxiv : the preprint server for biology · 2024Article
- Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition.Nature communications · 2024Article
- Female GluA3-KO mice show early onset hearing loss and afferent swellings in ambient sound levels.bioRxiv : the preprint server for biology · 2024Article
- Real-time visualization of structural dynamics of synapses in live cells in vivo.Nature methods · 2024Article
- Neuroligin-1 dependent phosphotyrosine signaling in excitatory synapse differentiation.Frontiers in molecular neuroscience · 2024Article
- Engineered adhesion molecules drive synapse organization.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
68 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Commented on by
Authors and funding
7 authors.
Funding
Abstract
Neurexins and neuroligins provide trans-synaptic connectivity by the Ca2+-dependent interaction of their alternatively spliced extracellular domains. Neuroligins specify synapses in an activity-dependent manner, presumably by binding to neurexins. Here, we present the crystal structures of neuroligin-1 in isolation and in complex with neurexin-1 beta. Neuroligin-1 forms a constitutive dimer, and two neurexin-1 beta monomers bind to two identical surfaces on the opposite faces of the neuroligin-1 dimer to form a heterotetramer. The neuroligin-1/neurexin-1 beta complex exhibits a nanomolar affinity and includes a large binding interface that contains bound Ca2+. Alternatively spliced sites in neurexin-1 beta and in neuroligin-1 are positioned nearby the binding interface, explaining how they regulate the interaction. Structure-based mutations of neuroligin-1 at the interface disrupt binding to neurexin-1 beta, but not the folding of neuroligin-1 and confirm the validity of the binding interface of the neuroligin-1/neurexin-1 beta complex. Our results provide molecular insights for understanding the role of cell-adhesion proteins in synapse function.
Indexed as
Identifiers
18093522What 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.