Ethanol inhibition of NMDA receptors in calcium-dependent and –independent modes
Author:
Funder
Russian Science Foundation
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference24 articles.
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2. Interactions among positions in the third and fourth membrane-associated domains at the intersubunit interface of the N-Methyl-D-aspartate receptor forming sites of alcohol action;Ren;J. Biol. Chem.,2012
3. A novel alcohol-sensitive position in the N-methyl-D-aspartate receptor GluN2A subunit M3 domain regulates agonist affinity and ion channel gating;Ren;Mol. Pharmacol.,2013
4. Two adjacent phenylalanines in the NMDA receptor GluN2A subunit M3 domain interactively regulate alcohol sensitivity and ion channel gating;Ren;Neuropharmacology,2017
5. Intersubunit interactions at putative sites of ethanol action in the M3 and M4 domains of the NMDA receptor GluN1 and GluN2B subunits;Zhao;Br. J. Pharmacol.,2016
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