ArticleNature communications2018
Unmasking GluN1/GluN3A excitatory glycine NMDA receptors.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
66 citing papers in PubMed, 98 citations in OpenAlex.
- Chronic Alcohol Exposure Alters Expression of GluN3A-NMDA Receptors in Adult VTA DA Neurons.bioRxiv : the preprint server for biology · 2026Article
- Structural and mechanistic insights into gating and allosteric modulation of GluN1-GluN3A NMDA receptors.Nature structural & molecular biology · 2026Article
- Non-classical NMDAR subunit GluN3A in a specialized hippocampal region regulates stress-coping strategies in male mice.Communications biology · 2026Article
- N-Methyl-D-aspartate receptors: structure, signaling and roles in atherosclerosis.Journal of translational medicine · 2026Review
- NMDA and glycine receptors provide dual presynaptic regulation on climbing fibre inputs to cerebellar Purkinje cells.The Journal of physiology · 2026Article
- The Role of Disulfide Bonds in the GluN1 Subunit in the Early Trafficking and Functional Properties of GluN1/GluN2 and GluN1/GluN3 NMDA Receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Article
- Glutamatergic Neurotransmission Disruption as a Pathomechanism of Brain Damage in Disorders of Amino Acid and Organic Acid Metabolism: Insights from Animal and Cellular Studies.Neurochemical research · 2026Review
- UCM-A86 is a selective positive allosteric modulator of GluN1/GluN3 NMDA receptors.Molecular pharmacology · 2026Article
- Emerging Roles of GluN3B NMDA Receptor Subunit in the Central Nervous System.Neuroscience bulletin · 2026Review
- Modulation of glycine transporters as a novel therapeutic strategy in neuropsychiatry.Psychopharmacology · 2026Review
- Identification of small-molecule inhibitors for GluN1/GluN3A NMDA receptors via a multiscale CNN-based prediction model.Acta pharmacologica Sinica · 2026Article
- AI-enhanced virtual screening approach to hit identification for GluN1/GluN3A NMDA receptor.Acta pharmacologica Sinica · 2026Article
- New advances in small molecule drugs targeting NMDA receptors.Acta pharmacologica Sinica · 2026Review
- The GluN3-containing NMDA receptors.Channels (Austin, Tex.) · 2025Review
- UCM-A86 is a selective positive allosteric modulator of GluN1/GluN3 NMDA receptors.bioRxiv : the preprint server for biology · 2025Article
- Contrastive learning-based drug screening model for GluN1/GluN3A inhibitors.Acta pharmacologica Sinica · 2025Article
- An efficient deep learning-based strategy to screen inhibitors for GluN1/GluN3A receptor.Acta pharmacologica Sinica · 2025Article
- Discovery of novel GluN1/GluN3A NMDA receptor inhibitors using a deep learning-based method.Acta pharmacologica Sinica · 2025Article
- Discrete interneuron subsets participate in GluN1/GluN3A excitatory glycine receptor (eGlyR)-mediated regulation of hippocampal network activity throughout development and evolution.Research square · 2025Article
- Discrete interneuron subsets participate in GluN1/GluN3A excitatory glycine receptor (eGlyR)-mediated regulation of hippocampal network activity throughout development and evolution.bioRxiv : the preprint server for biology · 2025Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
GluN3A and GluN3B are glycine-binding subunits belonging to the NMDA receptor (NMDAR) family that can assemble with the GluN1 subunit to form unconventional receptors activated by glycine alone. Functional characterization of GluN1/GluN3 NMDARs has been difficult. Here, we uncover two modalities that have transformative properties on GluN1/GluN3A receptors. First, we identify a compound, CGP-78608, which greatly enhances GluN1/GluN3A responses, converting small and rapidly desensitizing currents into large and stable responses. Second, we show that an endogenous GluN3A disulfide bond endows GluN1/GluN3A receptors with distinct redox modulation, profoundly affecting agonist sensitivity and gating kinetics. Under reducing conditions, ambient glycine is sufficient to generate tonic receptor activation. Finally, using CGP-78608 on P8-P12 mouse hippocampal slices, we demonstrate that excitatory glycine GluN1/GluN3A NMDARs are functionally expressed in native neurons, at least in the juvenile brain. Our work opens new perspectives on the exploration of excitatory glycine receptors in brain function and development.
Indexed as
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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.