Differential activation of nitric-oxide synthase isozymes by calmodulin-troponin C chimeras

Journal of Biological Chemistry

Volumn 279, Issue 32, 2004, Pages 33547-33557

  Newman, Elena ^a   Spratt, Donald E ^a   Mosher, Jennifer ^a   Cheyne, Bo ^a   Montgomery, Heather J ^a   Wilson, Denney L ^b   Weinberg, J Brice ^b   Smith, Susan M E ^c   Salerno, John C ^c   Ghosh, Dipak K ^b   Guillemette, J Guy ^a  

^a UNIVERSITY OF WATERLOO   (Canada)

^b DURHAM VA MEDICAL CENTER   (United States)

^c Research Rensselaer Polytechnic Institute   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; ASSAYS; ENZYMES; OXIDATION;

MUTANTS; NITRIC OXIDE SYNTHASE;

BIOCHEMISTRY;

CALCIUM; CALMODULIN; CALMODULIN TROPONIN C; CHIMERIC PROTEIN; CONSTITUTIVE NITRIC OXIDE SYNTHASE; CYTOCHROME C; ENDOTHELIAL NITRIC OXIDE SYNTHASE; FLAVINE MONONUCLEOTIDE; HEME; INDUCIBLE NITRIC OXIDE SYNTHASE; ISOENZYME; MUTANT PROTEIN; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; OXYGENASE; OXYHEMOGLOBIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TROPONIN C; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BINDING SITE; BIOASSAY; CALCIUM DEPLETION; CATTLE; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME MECHANISM; ESCHERICHIA COLI; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN PURIFICATION; RAT; REDUCTION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALMODULIN; CATTLE; CYTOCHROMES C; ENZYME ACTIVATION; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE TYPE I; NITRIC OXIDE SYNTHASE TYPE II; NITRIC OXIDE SYNTHASE TYPE III; RATS; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; TROPONIN C;

ANIMALIA; BOS TAURUS; ESCHERICHIA COLI;

EID: 4043170593     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M403892200     Document Type: Article

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