Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Different sites of alcohol action in the NMDA receptor GluN2A and GluN2B subunits.

Neuropharmacology - 1 Oct 2015

Zhao Yulin, Ren Hong, Dwyer Donard S, Peoples Robert W

Abstract excerpt

The NMDA receptor is a major target of alcohol action in the CNS, and recent behavioral and cellular studies have pointed to the importance of the GluN2B subunit in alcohol action. We and others have previously characterized four amino acid positions in the third and fourth membrane-associated (M) domains of the NMDA receptor GluN2A subunit that influence both ion channel gating and alcohol sensitivity. In this...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Central Nervous System Depressants
Share to Ethanol
Share to Glutamic Acid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HEK293 Cells

Share to Membrane Potentials

Share to Models, Molecular

Share to Patch-Clamp Techniques

Share to Receptors, N-Methyl-D-Aspartate

Source

Open in PubMed Open full text

Identifiers

PMID: 26051400
DOI: 10.1016/j.neuropharm.2015.05.018
PMCID: PMC4537375

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Different sites of alcohol action in the NMDA receptor GluN2A and GluN2B subunits.PMID 26051400Read ↗

A novel alcohol-sensitive position in the N-methyl-D-aspartate receptor GluN2A subunit M3 domain regulates agonist affinity and ion channel gating.Semantic proximity Read ↗

Mutations at F637 in the NMDA receptor NR2A subunit M3 domain influence agonist potency, ion channel gating and alcohol action.Semantic proximity Read ↗

A site of alcohol action in the fourth membrane-associated domain of the N-methyl-D-aspartate receptor.Semantic proximity Read ↗

Functional interactions of alcohol-sensitive sites in the N-methyl-D-aspartate receptor M3 and M4 domains.Semantic proximity Read ↗

Cysteine substitution of transmembrane domain amino acids alters the ethanol inhibition of GluN1/GluN2A N-methyl-D-aspartate receptors.Semantic proximity Read ↗

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

Two adjacent phenylalanines in the NMDA receptor GluN2A subunit M3 domain interactively regulate alcohol sensitivity and ion channel gating.Semantic proximity Read ↗

Specific pathogenic mutations in the M3 domain of the GluN1 subunit regulate the surface delivery and pharmacological sensitivity of NMDA receptors.Semantic proximity Read ↗

The pathogenic S688Y mutation in the ligand-binding domain of the GluN1 subunit regulates the properties of NMDA receptors.Semantic proximity Read ↗

Differential effects of TM4 tryptophan mutations on inhibition of N-methyl-d-aspartate receptors by ethanol and toluene.Semantic proximity Read ↗

Ethanol inhibition of constitutively open N-methyl-D-aspartate receptors.Semantic proximity Read ↗

Identification of novel allosteric modulator binding sites in NMDA receptors: A molecular modeling study.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.