ArticleStructure (London, England : 1993)2010
The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 33 citations in OpenAlex.
- In vivo dissection of human NRXN1 isoforms reveals gain-of-function pathogenicity of schizophrenia-associated 3' deletions.Human molecular genetics · 2026Article
- Synthetic host defense peptide inhibits SARS-CoV-2 replicationAntimicrobial agents and chemotherapy · 2025Article
- Alpha-neurexins in health and disease.Frontiers in molecular neuroscience · 2025Review
- Dissecting the epigenomic differences between smoking and nicotine dependence in a veteran cohort.Addiction biology · 2023Article
- Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023Review
- Neurexins: molecular codes for shaping neuronal synapses.Nature reviews. Neuroscience · 2021Review
- Addiction associated N40D mu-opioid receptor variant modulates synaptic function in human neurons.Molecular psychiatry · 2020Article
- Neurexins - versatile molecular platforms in the synaptic cleft.Current opinion in structural biology · 2019Review
- Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer.Journal of molecular biology · 2018Article
- Conformational Plasticity in the Transsynaptic Neurexin-Cerebellin-Glutamate Receptor Adhesion Complex.Structure (London, England : 1993) · 2016Article
- Molecular Architecture of Contactin-associated Protein-like 2 (CNTNAP2) and Its Interaction with Contactin 2 (CNTN2).The Journal of biological chemistry · 2016Article
- Structural Characterization of the Extracellular Domain of CASPR2 and Insights into Its Association with the Novel Ligand Contactin1.The Journal of biological chemistry · 2016Article
- Article
- Extracellular regulation of type IIa receptor protein tyrosine phosphatases: mechanistic insights from structural analyses.Seminars in cell & developmental biology · 2015Review
- Structural basis for extracellular cis and trans RPTPσ signal competition in synaptogenesis.Nature communications · 2014Article
- Dystroglycan binding to α-neurexin competes with neurexophilin-1 and neuroligin in the brain.The Journal of biological chemistry · 2014Article
- Reelin induces Erk1/2 signaling in cortical neurons through a non-canonical pathway.The Journal of biological chemistry · 2014Article
- The neuroligins and their ligands: from structure to function at the synapse.Journal of molecular neuroscience : MN · 2014Article
- Mutation screening of the neurexin 1 gene in thai patients with intellectual disability and autism spectrum disorder.Genetic testing and molecular biomarkers · 2014Article
- Neurexins.Genome biology · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Neurexins are multidomain synaptic cell-adhesion proteins that associate with multiple partnering proteins. Genetic evidence indicates that neurexins may contribute to autism, schizophrenia, and nicotine dependence. Using analytical ultracentrifugation, single-particle electron microscopy, and solution X-ray scattering, we obtained a three-dimensional structural model of the entire extracellular domain of neurexin-1alpha. This protein adopts a dimensionally asymmetric conformation that is monomeric in solution, with a maximum dimension of approximately 170 A. The extracellular domain of alpha-neurexin maintains a characteristic "Y" shape, whereby LNS domains 1-4 form an extended base of the "Y" and LNS5-6 the shorter arms. Moreover, two major regions of flexibility are present: one between EGF1 and LNS2, corresponding to splice site 1, another between LNS5 and 6. We thus provide the first structural insights into the architecture of the extracellular region of neurexin-1alpha, show how the protein may fit in the synaptic cleft, and how partnering proteins could bind simultaneously.
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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.