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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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Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels

Pharmacological reviews, 2021-10, Vol.73 (4), p.298-1658

2021

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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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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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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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4-Hydroxy-1,2,5-oxadiazol-3-yl Moiety as Bioisoster of the Carboxy Function. Synthesis, Ionization Constants, and Molecular Pharmacological Characterization at Ionotropic Glutamate Receptors of Compounds Related to Glutamate and Its Homologues

Journal of medicinal chemistry, 2010-05, Vol.53 (10), p.4110-4118

2010

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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

Structure, Function, and Pharmacology of Glutamate Receptor Ion Channels

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

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

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

4-Hydroxy-1,2,5-oxadiazol-3-yl Moiety as Bioisoster of the Carboxy Function. Synthesis, Ionization Constants, and Molecular Pharmacological Characterization at Ionotropic Glutamate Receptors of Compounds Related to Glutamate and Its Homologues

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