Two serine residues on GluN2A C-terminal tails control NMDA receptor current decay times

Channels

Volumn 7, Issue 2, 2013, Pages 126-132

  Maki, Bruce A ^a   Cole, Ross ^a   Popescu, Gabriela K ^a  

^a UNIVERSITY AT BUFFALO   (United States)

Author keywords

Ionotropic glutamate receptors; NMDA receptors; Protein phosphorylation; Reaction mechanism; Single channel kinetics

Indexed keywords

AMINO ACID; CALCINEURIN; CALCIUM; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; SERINE; N-METHYL D-ASPARTATE RECEPTOR SUBTYPE 2A;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BRAIN DEVELOPMENT; CARBOXY TERMINAL SEQUENCE; CHANNEL GATING; DEPHOSPHORYLATION; DESENSITIZATION; ION CURRENT; MUTATION; NONHUMAN; PHOSPHORYLATION; PROTEIN SUBUNIT; RAT; CHEMISTRY; GENETICS; HEK293 CELL LINE; HUMAN; KINETICS; METABOLISM; MISSENSE MUTATION; PROTEIN TERTIARY STRUCTURE;

HEK293 CELLS; HUMANS; ION CHANNEL GATING; KINETICS; MUTATION, MISSENSE; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, N-METHYL-D-ASPARTATE; SERINE;

EID: 84876920736     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.23968     Document Type: Article

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