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Distinct Functional and Pharmacological Properties of Triheteromeric GluN1/GluN2A/GluN2B NMDA Receptors

Neuron (Cambridge, Mass.), 2014-03, Vol.81 (5), p.1084-1096

2014

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Structure, function, and allosteric modulation of NMDA receptors

The Journal of general physiology, 2018-08, Vol.150 (8), p.1081-1105

2018

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Glutamate receptor ion channels: structure, regulation, and function

Pharmacological reviews, 2010-09, Vol.62 (3), p.405

2010

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Functional and pharmacological properties of triheteromeric GluN1/2B/2D NMDA receptors

The Journal of physiology, 2019-11, Vol.597 (22), p.5495-5514

2019

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NMDA Receptors in the Central Nervous System

Methods in molecular biology (Clifton, N.J.), 2017-01, Vol.1677, p.1

2017

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Structural Basis for Negative Allosteric Modulation of GluN2A-Containing NMDA Receptors

Neuron (Cambridge, Mass.), 2016-09, Vol.91 (6), p.1316-1329

2016

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Control of NMDA Receptor Function by the NR2 Subunit Amino-Terminal Domain

The Journal of neuroscience, 2009-09, Vol.29 (39), p.12045-12058

2009

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Control of assembly and function of glutamate receptors by the amino-terminal domain

Molecular pharmacology, 2010-10, Vol.78 (4), p.535-549

2010

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Structural and mechanistic determinants of a novel site for noncompetitive inhibition of GluN2D-containing NMDA receptors

The Journal of neuroscience, 2011-03, Vol.31 (10), p.3650-3661

2011

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Quinazolin-4-one Derivatives: A Novel Class of Noncompetitive NR2C/D Subunit-Selective N-Methyl-d-aspartate Receptor Antagonists

Journal of medicinal chemistry, 2010-08, Vol.53 (15), p.5476-5490

2010

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A subunit-selective potentiator of NR2C- and NR2D-containing NMDA receptors

Nature communications, 2010-10, Vol.1 (7), p.1-8, Article 90

2010

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Mechanism for noncompetitive inhibition by novel GluN2C/D N-methyl-D-aspartate receptor subunit-selective modulators

Molecular pharmacology, 2011-11, Vol.80 (5), p.782-795

2011

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Mutational Mapping and Modeling of the Binding Site for (S)-Citalopram in the Human Serotonin Transporter

The Journal of biological chemistry, 2010-01, Vol.285 (3), p.2051-2063

2010

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Ionotropic glutamate-like receptor δ2 binds D-serine and glycine

Proceedings of the National Academy of Sciences - PNAS, 2007-08, Vol.104 (35), p.14116-14121

2007

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Pharmacology and Structural Analysis of Ligand Binding to the Orthosteric Site of Glutamate-Like GluD2 Receptors

Molecular pharmacology, 2016-02, Vol.89 (2), p.253-262

2016

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Discovery of ( R )-2-amino-3-triazolpropanoic acid derivatives as NMDA receptor glycine site agonists with GluN2 subunit-specific activity

Frontiers in chemistry, 2022-11, Vol.10, p.1008233-1008233

2022

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Synaptic Dysfunction by Mutations in GRIN2B: Influence of Triheteromeric NMDA Receptors on Gain-of-Function and Loss-of-Function Mutant Classification

Brain sciences, 2022-06, Vol.12 (6), p.789

2022

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Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties

Neuron (Cambridge, Mass.), 2017-04, Vol.94 (1), p.58-64.e3

2017

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Subunit-Specific Agonist Activity at NR2A-, NR2B-, NR2C-, and NR2D-Containing N-Methyl-d-aspartate Glutamate Receptors

Molecular pharmacology, 2007-10, Vol.72 (4), p.907-920

2007

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How Glutamate Receptor Subunits Mix and Match: Details Uncovered

Neuron (Cambridge, Mass.), 2011-07, Vol.71 (2), p.198-200

2011

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Subunit-selective allosteric inhibition of glycine binding to NMDA receptors

The Journal of neuroscience, 2012-05, Vol.32 (18), p.6197-6208

2012

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Properties of Triheteromeric N -Methyl-d-Aspartate Receptors Containing Two Distinct GluN1 Isoforms

Molecular pharmacology, 2018-05, Vol.93 (5), p.453-467

2018

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Triheteromeric GluN1/GluN2A/GluN2C NMDARs with Unique Single-Channel Properties Are the Dominant Receptor Population in Cerebellar Granule Cells

Neuron (Cambridge, Mass.), 2018-07, Vol.99 (2), p.315-328.e5

2018

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Derivatives of (R)‑3-(5-Furanyl)carboxamido-2-aminopropanoic Acid as Potent NMDA Receptor Glycine Site Agonists with GluN2 Subunit-Specific Activity

Journal of medicinal chemistry, 2022-01, Vol.65 (1), p.734-746

2022

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Structural basis of subunit selectivity for competitive NMDA receptor antagonists with preference for GluN2A over GluN2B subunits

Proceedings of the National Academy of Sciences - PNAS, 2017-08, Vol.114 (33), p.E6942-E6951

2017

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Distinct Functional and Pharmacological Properties of Triheteromeric GluN1/GluN2A/GluN2B NMDA Receptors

Structure, function, and allosteric modulation of NMDA receptors

Glutamate receptor ion channels: structure, regulation, and function

Functional and pharmacological properties of triheteromeric GluN1/2B/2D NMDA receptors

NMDA Receptors in the Central Nervous System

Structural Basis for Negative Allosteric Modulation of GluN2A-Containing NMDA Receptors

Control of NMDA Receptor Function by the NR2 Subunit Amino-Terminal Domain

Control of assembly and function of glutamate receptors by the amino-terminal domain

Structural and mechanistic determinants of a novel site for noncompetitive inhibition of GluN2D-containing NMDA receptors

Quinazolin-4-one Derivatives: A Novel Class of Noncompetitive NR2C/D Subunit-Selective N-Methyl-d-aspartate Receptor Antagonists

A subunit-selective potentiator of NR2C- and NR2D-containing NMDA receptors

Mechanism for noncompetitive inhibition by novel GluN2C/D N-methyl-D-aspartate receptor subunit-selective modulators

Mutational Mapping and Modeling of the Binding Site for (S)-Citalopram in the Human Serotonin Transporter

Ionotropic glutamate-like receptor δ2 binds D-serine and glycine

Pharmacology and Structural Analysis of Ligand Binding to the Orthosteric Site of Glutamate-Like GluD2 Receptors

Discovery of ( R )-2-amino-3-triazolpropanoic acid derivatives as NMDA receptor glycine site agonists with GluN2 subunit-specific activity

Synaptic Dysfunction by Mutations in GRIN2B: Influence of Triheteromeric NMDA Receptors on Gain-of-Function and Loss-of-Function Mutant Classification

Allosteric Interactions between NMDA Receptor Subunits Shape the Developmental Shift in Channel Properties

Subunit-Specific Agonist Activity at NR2A-, NR2B-, NR2C-, and NR2D-Containing N-Methyl-d-aspartate Glutamate Receptors

How Glutamate Receptor Subunits Mix and Match: Details Uncovered

Subunit-selective allosteric inhibition of glycine binding to NMDA receptors

Properties of Triheteromeric N -Methyl-d-Aspartate Receptors Containing Two Distinct GluN1 Isoforms

Triheteromeric GluN1/GluN2A/GluN2C NMDARs with Unique Single-Channel Properties Are the Dominant Receptor Population in Cerebellar Granule Cells

Derivatives of (R)‑3-(5-Furanyl)carboxamido-2-aminopropanoic Acid as Potent NMDA Receptor Glycine Site Agonists with GluN2 Subunit-Specific Activity

Structural basis of subunit selectivity for competitive NMDA receptor antagonists with preference for GluN2A over GluN2B subunits

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