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Article

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

The Journal of pharmacology and experimental therapeutics - 1 Aug 2007

Smothers C Thetford, Woodward John J

Abstract excerpt

N-Methyl-D-aspartate (NMDA) receptors are important targets for drugs of abuse such as ethanol, toluene, and ketamine. Ligand-gated ion channels assembled from the NR1 and NR3 subunits have functional and pharmacological properties that are distinct from those of conventional NMDA receptors containing NR2 subunits. In the present study we used voltage-clamp electrophysiology to characterize excitatory...

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Source

Identifiers

PMID: 17502428
DOI: 10.1124/jpet.107.123836

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Pharmacological characterization of glycine-activated currents in HEK 293 cells expressing N-methyl-D-aspartate NR1 and NR3 subunits.PMID 17502428Read ↗

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

Activation of N-methyl-D-aspartate receptors by glycine: role of an aspartate residue in the M3-M4 loop of the NR1 subunit.Semantic proximity Read ↗

Ethanol sensitivity of heteromeric NMDA receptors: effects of subunit assembly, glycine and NMDAR1 Mg(2+)-insensitive mutants.Semantic proximity Read ↗

Supralinear potentiation of NR1/NR3A excitatory glycine receptors by Zn2+ and NR1 antagonist.Semantic proximity Read ↗

Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly.Semantic proximity Read ↗

Site within N-Methyl-D-aspartate receptor pore modulates channel gating.Semantic proximity Read ↗

Characterisation of the human NMDA receptor subunit NR3A glycine binding site.Semantic proximity Read ↗

Effects of anesthetics on mutant N-methyl-D-aspartate receptors expressed in Xenopus oocytes.Semantic proximity Read ↗

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Identification of amino acids in the N-methyl-D-aspartate receptor NR1 subunit that contribute to the glycine binding site.Semantic proximity Read ↗

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