Pharmacological characterization of glycine-activated currents in HEK 293 cells expressing N-methyl-D-aspartate NR1 and NR3 subunits (Q24305588)

GOA release 2020-03-11

response to ethanol

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Journal of Pharmacology and Experimental Therapeutics

GOA release 2020-03-11

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C Thetford Smothers

1

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John J Woodward

series ordinal

2

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language of work or name

English

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publication date

August 2007

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published in

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volume

322

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issue

2

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page(s)

739-48

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3H5,7-Dichlorokynurenic acid, a novel radioligand labels NMDA receptor-associated glycine binding sites

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Principal role of NR3 subunits in NR1/NR3 excitatory glycine receptor function.

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Volatile organic compounds inhibit human and rat neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes

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Effect of the NR3 subunit on ethanol inhibition of recombinant NMDA receptors

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Identification of a long variant of mRNA encoding the NR3 subunit of the NMDA receptor: its regional distribution and developmental expression in the rat brain

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The anti-craving compound acamprosate acts as a weak NMDA-receptor antagonist, but modulates NMDA-receptor subunit expression similar to memantine and MK-801.

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Cloning and characterization of a novel NMDA receptor subunit NR3B: a dominant subunit that reduces calcium permeability.

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The effects and consequences of selected club drugs

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Inhalant abuse by adolescents.

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Increased NMDA current and spine density in mice lacking the NMDA receptor subunit NR3A

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Excitatory glycine receptors containing the NR3 family of NMDA receptor subunits

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Ethanol inhibition of N-methyl-D-aspartate-activated current in mouse hippocampal neurones: whole-cell patch-clamp analysis

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Effects of volatile solvents on recombinant N-methyl-D-aspartate receptors expressed in Xenopus oocytes

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Block of N-methyl-D-aspartate-activated current by the anticonvulsant MK-801: selective binding to open channels

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Functional expression of a recombinant unitary glutamate receptor from Xenopus, which contains N-methyl-D-aspartate (NMDA) and non-NMDA receptor subunits.

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Ethanol inhibition of N-methyl-D-aspartate receptors is reduced by site-directed mutagenesis of a transmembrane domain phenylalanine residue

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Multiple mechanisms of ketamine blockade of N-methyl-D-aspartate receptors

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Glycine receptors: recent insights into their structural organization and functional diversity

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Effects of amino acid substitutions in transmembrane domains of the NR1 subunit on the ethanol inhibition of recombinant N-methyl-D-aspartate receptors

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Effects of 8 different NR1 splice variants on the ethanol inhibition of recombinant NMDA receptors

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Mechanism of memantine block of NMDA-activated channels in rat retinal ganglion cells: uncompetitive antagonism

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Effects of anesthetics on mutant N-methyl-D-aspartate receptors expressed in Xenopus oocytes

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Subunit-specific roles of glycine-binding domains in activation of NR1/NR3 N-methyl-D-aspartate receptors

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Ethanol inhibits NMDA-activated ion current in hippocampal neurons

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Kinetics of AP5 dissociation from NMDA receptors: evidence for two identical cooperative binding sites

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The NR3B subunit does not alter the anesthetic sensitivities of recombinant N-methyl-D-aspartate receptors

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Characterization of a soluble ligand binding domain of the NMDA receptor regulatory subunit NR3A.

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Cloning and characterization of chi-1: a developmentally regulated member of a novel class of the ionotropic glutamate receptor family

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Motoneuron-specific expression of NR3B, a novel NMDA-type glutamate receptor subunit that works in a dominant-negative manner

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Specific assembly with the NMDA receptor 3B subunit controls surface expression and calcium permeability of NMDA receptors

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NR3A modulates the outer vestibule of the "NMDA" receptor channel

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