ArticleNature communications2023
Two gates mediate NMDA receptor activity and are under subunit-specific regulation.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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
14 citing papers in PubMed, 15 citations in OpenAlex.
- Subconductance states in NMDA receptor variants are CaResearch square · 2026Article
- Molecular mechanism of calcium permeability and magnesium block in NMDA receptors.Nature neuroscience · 2026Article
- NMDA Receptor Mediated Mechanisms in the Post-Stroke Brain: From Physiology to Pathology.Biomolecules · 2026Review
- Neuroplasticity-Driven Mechanisms and Therapeutic Targets in the Anterior Cingulate Cortex in Neuropathic Pain.Brain and behavior · 2026Review
- Article
- Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements.Science advances · 2025Article
- GluK2 kainate receptor subunit-selective, potentiating RNA aptamer.Scientific reports · 2025Article
- Membrane Association of Intrinsically Disordered Proteins.Annual review of biophysics · 2025Review
- Article
- EAR-20 peptide, a novel NMDA receptor positive allosteric modulator.Frontiers in pharmacology · 2025Article
- Temperature Sensitive Glutamate Gating of AMPA-subtype iGluRs.bioRxiv : the preprint server for biology · 2024Article
- Article
- The open gate of the AMPA receptor forms a CaNature structural & molecular biology · 2024Article
- Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Kinetics of NMDA receptor (NMDAR) ion channel opening and closing contribute to their unique role in synaptic signaling. Agonist binding generates free energy to open a canonical gate at the M3 helix bundle crossing. Single channel activity is characterized by clusters, or periods of rapid opening and closing, that are separated by long silent periods. A conserved glycine in the outer most transmembrane helices, the M4 helices, regulates NMDAR function. Here we find that the GluN1 glycine mainly regulates single channel events within a cluster, whereas the GluN2 glycine mainly regulates entry and exit from clusters. Molecular dynamics simulations suggest that, whereas the GluN2 M4 (along with GluN2 pre-M1) regulates the gate at the M3 helix bundle crossing, the GluN1 glycine regulates a 'gate' at the M2 loop. Subsequent functional experiments support this interpretation. Thus, the distinct kinetics of NMDARs are mediated by two gates that are under subunit-specific regulation.
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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.