A network of control mediated by of regulator of calcium/calmodulin- dependent signaling

Science

Volumn 306, Issue 5696, 2004, Pages 698-701

  Rakhilin, S V ^a   Olson, P A ^b   Nishi, A ^a,c   Starkova, N N ^a   Fienberg, A A ^a,d   Nairn, A C ^a,e   Surmeier, D J ^b   Greengard, P ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

^b NORTHWESTERN UNIVERSITY   (United States)

^c KURUME UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^d Intra Cellular Therapies Inc   (United States)

^e YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CHEMICAL ACTIVATION; ENZYME INHIBITION; ENZYMES; GENETIC ENGINEERING;

CALMODULIN (CAM); NEURONS; PHOSPHORYLATION; REGULATOR OF CALMODULIN SIGNALING (RCS);

CALCIUM;

CALCINEURIN; CALCIUM; CALCIUM CHANNEL L TYPE; CALMODULIN; CALMODULIN BINDING PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; G PROTEIN COUPLED RECEPTOR;

BIOLOGY;

ANIMAL CELL; ARTICLE; CALCIUM CURRENT; CELL TYPE; COMPETITIVE INHIBITION; CORPUS STRIATUM; ENZYME ACTIVATION; ENZYME INHIBITION; GENE AMPLIFICATION; GENE DELETION; MOLECULAR MECHANICS; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

ANIMALS; CALCINEURIN; CALCIUM; CALCIUM CHANNELS, L-TYPE; CALCIUM SIGNALING; CALMODULIN; CYCLIC AMP-DEPENDENT PROTEIN KINASES; DOPAMINE AND CAMP-REGULATED PHOSPHOPROTEIN 32; MICE; MICE, INBRED C57BL; MICE, KNOCKOUT; NEOSTRIATUM; NERVE TISSUE PROTEINS; NEURONS; PHOSPHOPROTEINS; PHOSPHORYLATION; RECEPTOR, MUSCARINIC M1; RECEPTORS, DOPAMINE D1; SIGNAL TRANSDUCTION;

ANIMALIA;

EID: 7444239120     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1099961     Document Type: Article

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26. We thank P. Ingrassia, A. Horiuchi, F. Liu, and E. Griggs for technical support. Work described in this paper was supported by U.S. Public Health Service grants MH40899 and DA10044 (A.C.N. and P.C.) and NS34696 and DA12958 (D.J.S.), the Picower Foundation, the Peter Jay Sharp Foundation, and the Simons Foundation (P.C.), and a Grant-in-Aid for Scientific Research from the Japan Society for the Promotion of Science (A.N.). Molecular interaction data have been deposited in the Biomolecular Interaction Network Database with accession codes 169429 to 169431.