ArticleStructure (London, England : 1993)2008
Regulation of neurexin 1beta tertiary structure and ligand binding through alternative splicing.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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.
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.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- The soluble neurexin-1β ectodomain causes calcium influx and augments dendritic outgrowth and synaptic transmission.Scientific reports · 2020Article
- Alternative splicing controls teneurin-latrophilin interaction and synapse specificity by a shape-shifting mechanism.Nature communications · 2020Article
- Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing.The EMBO journal · 2019Article
- Neurexins - versatile molecular platforms in the synaptic cleft.Current opinion in structural biology · 2019Review
- Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains.Frontiers in molecular biosciences · 2019Review
- Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer.Journal of molecular biology · 2018Article
- Structural insights into modulation and selectivity of transsynaptic neurexin-LRRTM interaction.Nature communications · 2018Article
- Dynamic Control of Synaptic Adhesion and Organizing Molecules in Synaptic Plasticity.Neural plasticity · 2017Review
- ChSeq: A database of chameleon sequences.Protein science : a publication of the Protein Society · 2015Review
- A neuroligin-1-derived peptide stimulates phosphorylation of the NMDA receptor NR1 subunit and rescues MK-801-induced decrease in long-term potentiation and memory impairment.Pharmacology research & perspectives · 2015Article
- Calsyntenin-3 molecular architecture and interaction with neurexin 1α.The Journal of biological chemistry · 2014Article
- The neuroligins and their ligands: from structure to function at the synapse.Journal of molecular neuroscience : MN · 2014Article
- A matter of balance: role of neurexin and neuroligin at the synapse.Neurochemical research · 2013Review
- Neurexins.Genome biology · 2013Review
- Proteomic analysis of Col11a1-associated protein complexes.Proteomics · 2011Article
- The crystal structure of the α-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function.Structure (London, England : 1993) · 2011Article
- The structure of neurexin 1α reveals features promoting a role as synaptic organizer.Structure (London, England : 1993) · 2011Article
- Neurexins, neuroligins and LRRTMs: synaptic adhesion getting fishy.Journal of neurochemistry · 2011Review
- Article
- The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition.Structure (London, England : 1993) · 2010Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Neurexins and neuroligins play an essential role in synapse function, and their alterations are linked to autistic spectrum disorder. Interactions between neurexins and neuroligins regulate inhibitory and excitatory synaptogenesis in vitro through a "splice-insert signaling code." In particular, neurexin 1beta carrying an alternative splice insert at site SS#4 interacts with neuroligin 2 (found predominantly at inhibitory synapses) but much less so with other neuroligins (those carrying an insert at site B and prevalent at excitatory synapses). The structure of neurexin 1beta+SS#4 reveals dramatic rearrangements to the "hypervariable surface," the binding site for neuroligins. The splice insert protrudes as a long helix into space, triggers conversion of loop beta10-beta11 into a helix rearranging the binding site for neuroligins, and rearranges the Ca(2+)-binding site required for ligand binding, increasing its affinity. Our structures reveal the mechanism by which neurexin 1beta isoforms acquire neuroligin splice isoform selectivity.
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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.