Enhanced electron flux and reduced calmodulin dissociation may explain 'calcium-independent' eNOS activation by phosphorylation

Journal of Biological Chemistry

Volumn 275, Issue 9, 2000, Pages 6123-6128

  McCabe, Timothy J ^a   Fulton, David ^a   Roman, Linda J ^b   Sessa, William C ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; CALCIUM ION; CALMODULIN; CYTOCHROME C OXIDASE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; SERINE;

ANIMAL CELL; ARTICLE; CALCIUM CELL LEVEL; CATTLE; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME MECHANISM; ENZYME PHOSPHORYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION;

ANIMALS; CALCIUM; CALMODULIN; CATTLE; DIMERIZATION; EGTAZIC ACID; ELECTRONS; ELECTROSTATICS; ENZYME ACTIVATION; KINETICS; MUTATION; NADH DEHYDROGENASE; NADP; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE TYPE III; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-AKT;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0034054493     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.9.6123     Document Type: Article

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