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

Effects of ethanol on phosphorylation site mutants of recombinant N-methyl-D-aspartate receptors.

Alcohol (Fayetteville, N.Y.) - 1 Jun 2011

Xu Minfu, Smothers Corigan Thetford, Woodward John J

Abstract excerpt

N-methyl-D-aspartate (NMDA) receptors are ligand-gated ion channels activated by the neurotransmitter glutamate. These channels are highly expressed by brain neurons and are critically involved in excitatory synaptic transmission. Results from previous studies show that both native and recombinant NMDA receptors are inhibited by ethanol at concentrations associated with signs of behavioral impairment and...

Read the complete abstract on PubMed

Topics

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

Share to Cyclic AMP-Dependent Protein Kinases
Share to Ethanol
Share to HEK293 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Patch-Clamp Techniques

Share to Protein Kinase C

Share to Receptors, N-Methyl-D-Aspartate

Share to Recombinant Proteins

Share to Serine

Source

Open in PubMed Open full text

Identifiers

PMID: 21163614
DOI: 10.1016/j.alcohol.2010.08.015
PMCID: PMC3095724

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of ethanol on phosphorylation site mutants of recombinant N-methyl-D-aspartate receptors.PMID 21163614Read ↗

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

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

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

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

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

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 ↗

Altered effects of ethanol in NR2A(DeltaC/DeltaC) mice expressing C-terminally truncated NR2A subunit of NMDA receptor.Semantic proximity Read ↗

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

Alcohols inhibit N-methyl-D-aspartate receptors via a site exposed to the extracellular environment.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 sensitivity of heteromeric NMDA receptors: effects of subunit assembly, glycine and NMDAR1 Mg(2+)-insensitive mutants.Semantic proximity Read ↗

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