Ethanol Inhibition of N-Methyl-D-aspartate Receptors Is Reduced by Site-directed Mutagenesis of a Transmembrane Domain Phenylalanine Residue

Journal of Biological Chemistry

Volumn 276, Issue 48, 2001, Pages 44729-44735

  Ronald, Kimberly M ^a   Mirshahi, Tooraj ^b   Woodward, John J ^c  

^a VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

^b MOUNT SINAI SCHOOL OF MEDICINE   (United States)

^c MEDICAL UNIVERSITY OF SOUTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELLS; MUTAGENESIS;

HETEROMERIC RECEPTORS;

ETHANOL;

3 AMINO 1 HYDROXY 2 PYRROLIDINONE; 5,7 DICHLOROKYNURENIC ACID; ALANINE; ALCOHOL; AMINO ACID; GLUTAMIC ACID; GLYCINE RECEPTOR ANTAGONIST; IONOTROPIC RECEPTOR; MEMBRANE PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHENYLALANINE; TRYPTOPHAN; 2 PYRROLIDONE DERIVATIVE; 5,7-DICHLOROKYNURENIC ACID; AMINO ACID RECEPTOR BLOCKING AGENT; DRUG DERIVATIVE; GLYCINE; KYNURENIC ACID; RECEPTORS, N METHYL D ASPARTATE;

ANIMAL CELL; ARTICLE; CHANNEL GATING; DRUG EFFICACY; HUMAN; HUMAN CELL; MUTAGENESIS; MUTATION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; RAT; SENSITIVITY ANALYSIS; SITE DIRECTED MUTAGENESIS; AMINO ACID SEQUENCE; ANIMAL; BINDING COMPETITION; CELL LINE; CHEMISTRY; DOSE RESPONSE; GENETIC TRANSFECTION; GENETICS; METABOLISM; MOLECULAR GENETICS; PATCH CLAMP; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; XENOPUS LAEVIS;

ANIMALIA;

AMINO ACID SEQUENCE; ANIMAL; BINDING, COMPETITIVE; CELL LINE; DOSE-RESPONSE RELATIONSHIP, DRUG; ETHANOL; EXCITATORY AMINO ACID ANTAGONISTS; GLUTAMIC ACID; GLYCINE; HUMAN; KYNURENIC ACID; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PATCH-CLAMP TECHNIQUES; PHENYLALANINE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PYRROLIDINONES; RECEPTORS, N-METHYL-D-ASPARTATE; SEQUENCE HOMOLOGY, AMINO ACID; SUPPORT, U.S. GOV'T, P.H.S.; TRANSFECTION; XENOPUS LAEVIS;

EID: 0035976931     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102800200     Document Type: Article

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