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

Xu, Minfu; Smothers, C Thetford; Woodward, John J

Xu, Minfu; Smothers, C Thetford; Woodward, John J.

Affiliation

Xu M; Department of Neuroscience, Medical University of South Carolina, Charleston, South Carolina.
Smothers CT; Department of Neuroscience, Medical University of South Carolina, Charleston, South Carolina.
Woodward JJ; Department of Neuroscience, Medical University of South Carolina, Charleston, South Carolina woodward@musc.edu.

J Pharmacol Exp Ther ; 353(1): 91-101, 2015 Apr.

Article in En | MEDLINE | ID: mdl-25635140

Subject(s)

Ethanol/pharmacology; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors; Amino Acid Substitution; Cysteine/genetics; HEK293 Cells; Humans; Models, Molecular; Mutation; Patch-Clamp Techniques; Protein Structure, Tertiary; Receptors, N-Methyl-D-Aspartate/genetics; Receptors, N-Methyl-D-Aspartate/metabolism

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Full text: 1 Database: MEDLINE Main subject: Receptors, N-Methyl-D-Aspartate / Ethanol Limits: Humans Language: En Year: 2015 Type: Article

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Full text: 1 Database: MEDLINE Main subject: Receptors, N-Methyl-D-Aspartate / Ethanol Limits: Humans Language: En Year: 2015 Type: Article