Formation of NR1/NR2 and NR1/NR3 heterodimers constitutes the initial step in N-methyl-D-aspartate receptor assembly

Journal of Biological Chemistry

Volumn 283, Issue 1, 2008, Pages 37-46

  Schüler, Thomas ^a,b   Mesic, Ivana ^a,b   Madry, Christian ^a   Bartholoma, Ingo ^a   Laube, Bodo ^a,b  

^a MAX PLANCK INSTITUTE FOR BRAIN RESEARCH   (Germany)

^b DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; POLYACRYLATES; PROTEINS;

HETERODIMERS; METABOLIC LABELING; RECONSTITUTE CHANNELS;

DIMERS;

GLUTAMIC ACID; GLYCINE; HOMODIMER; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; RECEPTOR SUBUNIT;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; DIMERIZATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HUMAN CELL; OLIGOMERIZATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN PURIFICATION; PROTEIN STABILITY; RECEPTOR INTRINSIC ACTIVITY; STOICHIOMETRY;

ANIMALS; CELL LINE; DIMERIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ELECTROPHYSIOLOGY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMANS; MICE; MODELS, BIOLOGICAL; MUTATION; OOCYTES; PROTEIN SUBUNITS; RATS; RECEPTORS, N-METHYL-D-ASPARTATE; RECOMBINANT PROTEINS; TRANSFECTION; XENOPUS LAEVIS;

EID: 38049134598     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M703539200     Document Type: Article

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