Nitric-oxide synthase (NOS) reductase domain models suggest a new control element in endothelial NOS that attenuates calmodulin-dependent activity

Journal of Biological Chemistry

Volumn 278, Issue 34, 2003, Pages 31814-31824

  Knudsen, Giselle M ^a   Nishida, Clinton R ^a   Mooney, Sean D ^b   Ortiz de Montellano, Paul R ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b STANFORD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; ELECTROSTATICS; NITROGEN OXIDES;

ELECTRON TRANSFERS;

BIOCHEMISTRY;

CALCIUM ION; CALMODULIN; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE REDUCTASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; ATTENUATION; CALCIUM TRANSPORT; CARBOXY TERMINAL SEQUENCE; ELECTRICITY; ELECTRON TRANSPORT; ENDOTHELIUM CELL; ENZYME ACTIVITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; INHIBITION KINETICS; NONHUMAN; PREDICTION; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CALMODULIN; DNA PRIMERS; ELECTRON TRANSPORT; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE TYPE III; OXIDOREDUCTASES; SEQUENCE HOMOLOGY, AMINO ACID;

ANIMALIA;

EID: 0042357128     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M303267200     Document Type: Article

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