Single-channel analysis of a point mutation of a conserved serine residue in the S2 ligand-binding domain of the NR2A NMDA receptor subunit

Journal of Physiology

Volumn 574, Issue 2, 2006, Pages 477-489

  Wyllie, David J A ^a   Johnston, Alexander R ^a   Lipscombe, Diane ^b   Chen, Philip E ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b BROWN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; GLYCINE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 1; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; SERINE;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CORRELATION ANALYSIS; GENE EXPRESSION; HYPOTHESIS; LIGAND BINDING; MEMBRANE CURRENT; MUTANT; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROBABILITY; PROTEIN DOMAIN; VOLTAGE CLAMP; WILD TYPE; XENOPUS LAEVIS; ANIMAL CELL; ENZYME ACTIVATION; OOCYTE; PROTEIN EXPRESSION; SINGLE CHANNEL PATCH CLAMP;

ANIMALS; CELLS, CULTURED; FEMALE; GENE EXPRESSION REGULATION; GLUTAMIC ACID; ION CHANNEL GATING; MEMBRANE POTENTIALS; OOCYTES; PATCH-CLAMP TECHNIQUES; POINT MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, N-METHYL-D-ASPARTATE; SERINE; XENOPUS LAEVIS;

EID: 33745741431     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2006.112193     Document Type: Article

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