ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
NMDA receptor NR2 subunit dependence of the slow component of magnesium unblock.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 90 citations in OpenAlex.
- Single-cell multiomic human brain atlas reveals regulatory drivers of cortical regionality.Nature communications · 2026Article
- Heterosynaptic NMDA receptor plasticity in hippocampal dentate granule cells.Frontiers in synaptic neuroscience · 2026Article
- Activation of GluN2D-containing NMDA receptors promotes development of axons and axon-carrying dendrites of cortical interneurons.Cerebral cortex (New York, N.Y. : 1991) · 2025Article
- GluN2A or GluN2B subunits of the NMDA receptor contribute to changes in neuronal excitability and impairments in LTP in the hippocampus of aging mice but do not mediate detrimental effects of oligomeric Aβ (1-42).Frontiers in aging neuroscience · 2024Article
- Therapeutic potential of N-methyl-D-aspartate receptor modulators in psychiatry.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2024Review
- An integrated approach to evaluate the functional effects of disease-associated NMDA receptor variants.Neuropharmacology · 2023Article
- Potential Roles for the GluN2D NMDA Receptor Subunit in Schizophrenia.International journal of molecular sciences · 2023Review
- Article
- Synapse-specific diversity of distinct postsynaptic GluN2 subtypes defines transmission strength in spinal lamina I.Frontiers in synaptic neuroscience · 2023Article
- Recent advances in the study of anesthesia-and analgesia-related mechanisms of S-ketamine.Frontiers in pharmacology · 2023Review
- GluN2A-Selective NMDA Receptor Antagonists: Mimicking the U-Shaped Bioactive Conformation of TCN-201 by a [2.2]Paracyclophane System.ChemMedChem · 2022Article
- [2.2]Paracyclophane-Based TCN-201 Analogs as GluN2A-Selective NMDA Receptor Antagonists.ChemMedChem · 2021Article
- Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels.Pharmacological reviews · 2021Review
- The glutamatergic synapse: a complex machinery for information processing.Cognitive neurodynamics · 2021Review
- Synaptic communication mediates the assembly of a self-organizing circuit that controls reproduction.Science advances · 2021Article
- Interplay between Gating and Block of Ligand-Gated Ion Channels.Brain sciences · 2020Review
- Hippocampal Synaptic Plasticity, Spatial Memory, and Neurotransmitter Receptor Expression Are Profoundly Altered by Gradual Loss of Hearing Ability.Cerebral cortex (New York, N.Y. : 1991) · 2020Article
- A calcium-influx-dependent plasticity model exhibiting multiple STDP curves.Journal of computational neuroscience · 2020Article
- GRIN2D/GluN2D NMDA receptor: Unique features and its contribution to pediatric developmental and epileptic encephalopathy.European journal of paediatric neurology : EJPN : official journal of the European Paediatric Neurology Society · 2020Review
- Structure, function, and allosteric modulation of NMDA receptors.The Journal of general physiology · 2018Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
NMDA receptor activity is important for many physiological functions, including synapse formation and alterations in synaptic strength. NMDA receptors are composed most commonly of NR1 and NR2 subunits. There are four NR2 subunits (NR2A-NR2D). NR2 subunit expression varies across both brain regions and developmental stages. The identity of the NR2 subunit within a functional NMDA receptor helps to determine many pharmacological and biophysical receptor properties, including strength of block by external Mg2+ (Mg(o)2+). Mg(o)2+ block confers strong voltage dependence to NMDA receptor-mediated responses and is critically important for many of the functions that the NMDA receptor plays within the CNS. Here we describe the NR2 subunit dependence of the kinetics of Mg(o)2+ unblock after rapid depolarizations. We find that Mg(o)2+ unblocks from NR1/2A and NR1/2B receptors with a prominent slow component similar to that previously described in native hippocampal and cortical NMDA receptors. Strikingly, this slow component of Mg(o)2+ unblock is completely absent from NR1/2C and NR1/2D receptors. Thus currents from NR1/2C and NR1/2D receptors respond more rapidly to fast depolarizations than currents from NR1/2A and NR1/2B receptors. In addition, the slow component of Mg(o)2+ unblock from NR1/2B receptors is consistently slower than from NR1/2A receptors. This makes rapid depolarizations, such as action potential waveforms, more efficacious at stimulating Mg(o)2+ unblock from NR1/2A than from NR1/2B receptors. These NR2 subunit differences in the kinetics of Mg(o)2+ unblock are likely to help determine the contribution of each NMDA receptor subtype to current flow during synaptic activity.
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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.