Protein Kinase C Activation Modulates α-Calmodulin Kinase II Binding to NR2A Subunit of N-Methyl-D-Aspartate Receptor Complex

Journal of Biological Chemistry

Volumn 276, Issue 10, 2001, Pages 7609-7613

  Gardoni, Fabrizio ^a   Bellone, Camilla ^b   Cattabeni, Flaminio ^b   Di Luca, Monica ^b  

^a UNIVERSITY OF MILAN   (Italy)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ESTERS; MUTAGENESIS;

PHOSPHORYLATION;

ENZYMES;

1 AMINO 1,3 CYCLOPENTANEDICARBOXYLIC ACID; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR 2A; PHORBOL DIBUTYRATE; POSTSYNAPTIC DENSITY PROTEIN; PROTEIN KINASE (CALCIUM,CALMODULIN) II; PROTEIN KINASE C; RECEPTOR SUBUNIT; SERINE; UNCLASSIFIED DRUG; 1-AMINO-1,3-DICARBOXYCYCLOPENTANE; CALMODULIN DEPENDENT PROTEIN KINASE II; CALMODULIN-DEPENDENT PROTEIN KINASE II; CYCLOLEUCINE; DRUG DERIVATIVE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; NEUROPROTECTIVE AGENT; NR2A NMDA RECEPTOR; PROTEIN KINASE (CALCIUM,CALMODULIN);

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOSOL; DISSOCIATION; ENZYME ACTIVATION; ENZYME BINDING; HIPPOCAMPUS; IN VITRO STUDY; NONHUMAN; POSTSYNAPTIC MEMBRANE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; RAT; SITE DIRECTED MUTAGENESIS; ANIMAL; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR CLONING; PHOSPHORYLATION; PLASMID; POINT MUTATION; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SERODIAGNOSIS; SIGNAL TRANSDUCTION;

ANIMALIA;

ANIMALS; CA(2+)-CALMODULIN DEPENDENT PROTEIN KINASE; CLONING, MOLECULAR; CYCLOLEUCINE; CYTOSOL; ENZYME ACTIVATION; GLUTATHIONE TRANSFERASE; HIPPOCAMPUS; MUTAGENESIS, SITE-DIRECTED; NEUROPROTECTIVE AGENTS; PHOSPHORYLATION; PLASMIDS; POINT MUTATION; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN KINASE C; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, N-METHYL-D-ASPARTATE; RECOMBINANT FUSION PROTEINS; SIGNAL TRANSDUCTION;

EID: 0035831431     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M009922200     Document Type: Article

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