ArticleNature communications2021
GluN2A and GluN2B NMDA receptors use distinct allosteric routes.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- How muscle talks to brain: apelin protein mediates exercise-induced antidepressant effects.Molecular psychiatry · 2026Article
- Chronic Alcohol Exposure Alters Expression of GluN3A-NMDA Receptors in Adult VTA DA Neurons.bioRxiv : the preprint server for biology · 2026Article
- NMDA Receptor Mediated Mechanisms in the Post-Stroke Brain: From Physiology to Pathology.Biomolecules · 2026Review
- Structures of partially occupied hetero-tetramers provide insight into kainate receptor activation and desensitization.Nature communications · 2026Article
- GluN2B-specific NMDAR positive allosteric modulation reverses cognitive and behavioral abnormalities inScience advances · 2026Article
- Novel binding mode for negative allosteric NMDA receptor modulators.The Journal of general physiology · 2026Article
- Regulation of NMDA receptor interactions with the actin cytoskeleton in dendritic spine development.Frontiers in cellular neuroscience · 2026Review
- Cryo-EM snapshots of NMDA receptor activation illuminate sequential rearrangements.Science advances · 2025Article
- Targeting HINT1 to improve synaptic plasticity: toward loganin as a new antidepressant strategy.Molecular psychiatry · 2025Article
- Optochemical profiling of NMDAR molecular diversity at synaptic and extrasynaptic sites.The EMBO journal · 2025Article
- Experimentally Constrained Mechanistic and Data-Driven Models for Simulating NMDA Receptor Dynamics.Biomedicines · 2025Article
- Regulation of NMDAR activation efficiency by environmental factors and subunit composition.The Journal of general physiology · 2025Article
- Possible antidepressant mechanism of acupuncture: targeting neuroplasticity.Frontiers in neuroscience · 2025Review
- Dose-Dependent Modulation of NMDA Receptors: Neuroprotective Mechanisms against Oxidative Stress in Hippocampal Neurons.International journal of molecular and cellular medicine · 2025Article
- Advancements in the application of brain-computer interfaces based on different paradigms in amyotrophic lateral sclerosis.Frontiers in neuroscience · 2025Review
- Research Progress on NMDA Receptor Enhancement Drugs for the Treatment of Depressive Disorder.CNS drugs · 2024Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- Reversible Control of Native GluN2B-Containing NMDA Receptors with Visible Light.ACS chemical neuroscience · 2024Article
- Subtype-specific conformational landscape of NMDA receptor gating.Cell reports · 2024Article
- Discovery of novel positive allosteric modulators targeting GluN1/2A NMDARs as anti-stroke therapeutic agents.RSC medicinal chemistry · 2024Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Allostery represents a fundamental mechanism of biological regulation that involves long-range communication between distant protein sites. It also provides a powerful framework for novel therapeutics. NMDA receptors (NMDARs), glutamate-gated ionotropic receptors that play central roles in synapse maturation and plasticity, are prototypical allosteric machines harboring large extracellular N-terminal domains (NTDs) that provide allosteric control of key receptor properties with impact on cognition and behavior. It is commonly thought that GluN2A and GluN2B receptors, the two predominant NMDAR subtypes in the adult brain, share similar allosteric transitions. Here, combining functional and structural interrogation, we reveal that GluN2A and GluN2B receptors utilize different long-distance allosteric mechanisms involving distinct subunit-subunit interfaces and molecular rearrangements. NMDARs have thus evolved multiple levels of subunit-specific allosteric control over their transmembrane ion channel pore. Our results uncover an unsuspected diversity in NMDAR molecular mechanisms with important implications for receptor physiology and precision drug development.
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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.