Cysteine residues 87 and 320 in the amino terminal domain of NMDA receptor GluN2A govern its homodimerization but do not influence GluN2A/GluN1 heteromeric assembly

Neuroscience Bulletin

Volumn 29, Issue 6, 2013, Pages 671-684

  Zhang, Xiao Min ^a   Lv, Xin You ^a   Tang, Yang ^a   Zhu, Li Jun ^a   Luo, Jian Hong ^a  

^a ZHEJIANG UNIVERSITY SCHOOL OF MEDICINE   (China)

Author keywords

amino terminal domain; heteromeric assembly; homodimerization; N methyl D aspartate receptor

Indexed keywords

AMINO ACID; CYSTEINE; GLUTAMATE RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; RECEPTOR SUBUNIT;

AMINO TERMINAL DOMAIN; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BRAIN ELECTROPHYSIOLOGY; CELL STRAIN COS7; CELL STRAIN HEK293; CENTRAL NERVOUS SYSTEM; DIMERIZATION; HUMAN; HUMAN CELL; NEUROTRANSMISSION; NONHUMAN; PLASMID; PROTEIN DOMAIN; PROTEIN LOCALIZATION; SITE DIRECTED MUTAGENESIS; WESTERN BLOTTING;

AMINO ACID MOTIFS; ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; CYSTEINE; HEK293 CELLS; HUMANS; NEURONS; PROTEIN MULTIMERIZATION; RATS; RECEPTORS, N-METHYL-D-ASPARTATE;

EID: 84890791611     PISSN: 16737067     EISSN: 19958218     Source Type: Journal    
DOI: 10.1007/s12264-013-1335-x     Document Type: Article

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