ArticleStructure (London, England : 1993)2011
The structure of neurexin 1α reveals features promoting a role as synaptic organizer.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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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
49 citing papers in PubMed, 72 citations in OpenAlex.
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Chronic hypoxia induces alternative splicing of transcripts in the goldfish brain.Fish physiology and biochemistry · 2025Article
- Structural basis for regulation of CELSR1 by a compact module in its extracellular region.Nature communications · 2025Article
- Neurexin-3 is Elevated and Associated with Cognition Status and 4-Hydroxynonenal in Bipolar Disorder.Annals of neurosciences · 2025Article
- Alpha-neurexins in health and disease.Frontiers in molecular neuroscience · 2025Review
- 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
- New perspective on sustained antidepressant effect: focus on neurexins regulating synaptic plasticity.Cell death discovery · 2024Review
- Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Review
- Is NRXN1 Gene Expression an Important Marker of Treatment of Depressive Disorders? A Pilot Study.Journal of personalized medicine · 2021Article
- Interplay between hevin, SPARC, and MDGAs: Modulators of neurexin-neuroligin transsynaptic bridges.Structure (London, England : 1993) · 2021Article
- Neurexins: molecular codes for shaping neuronal synapses.Nature reviews. Neuroscience · 2021Review
- The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1.The Journal of biological chemistry · 2020Article
- Functional characterization of rare NRXN1 variants identified in autism spectrum disorders and schizophrenia.Journal of neurodevelopmental disorders · 2020Article
- Inhibitor discovery for the E. coli meningitis virulence factor IbeA from homology modeling and virtual screening.Journal of computer-aided molecular design · 2020Article
- Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing.The EMBO journal · 2019Article
- An integrative analysis of non-coding regulatory DNA variations associated with autism spectrum disorder.Molecular psychiatry · 2019Article
- Pathogenic effects of agrin V1727F mutation are isoform specific and decrease its expression and affinity for HSPGs and LRP4.Human molecular genetics · 2019Article
- Candidate CSPG4 mutations and induced pluripotent stem cell modeling implicate oligodendrocyte progenitor cell dysfunction in familial schizophrenia.Molecular psychiatry · 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
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4 authors at 1 institution in 1 country.
Funding
Abstract
α-neurexins are essential synaptic adhesion molecules implicated in autism spectrum disorder and schizophrenia. The α-neurexin extracellular domain consists of six LNS domains interspersed by three EGF-like repeats and interacts with many different proteins in the synaptic cleft. To understand how α-neurexins might function as synaptic organizers, we solved the structure of the neurexin 1α extracellular domain (n1α) to 2.65 Å. The L-shaped molecule can be divided into a flexible repeat I (LNS1-EGF-A-LNS2), a rigid horseshoe-shaped repeat II (LNS3-EGF-B-LNS4) with structural similarity to so-called reelin repeats, and an extended repeat III (LNS5-EGF-B-LNS6) with controlled flexibility. A 2.95 Å structure of n1α carrying splice insert SS#3 in LNS4 reveals that SS#3 protrudes as a loop and does not alter the rigid arrangement of repeat II. The global architecture imposed by conserved structural features enables α-neurexins to recruit and organize proteins in distinct and variable ways, influenced by splicing, thereby promoting synaptic function.
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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.