cAMP- and Ca2+-independent activation of cystic fibrosis transmembrane conductance regulator channels by phenylimidazothiazole drugs

Journal of Biological Chemistry

Volumn 271, Issue 27, 1996, Pages 16171-16179

  Becq, Frédéric ^a,b,d   Verrier, Bernard ^b   Chang, Xiu Bao ^c   Riordan, John R ^c   Hanrahan, John W ^a  

^a MCGILL UNIVERSITY   (Canada)

^b INSERM   (France)

^c MAYO CLINIC   (United States)

^d CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; CALCIUM ION; CYCLIC AMP DEPENDENT PROTEIN KINASE; ENZYME INHIBITOR; FORSKOLIN; LEVAMISOLE; PROTEIN KINASE INHIBITOR; 4 BROMOTETRAMISOLE; 4-BROMOTETRAMISOLE; ADENOSINE TRIPHOSPHATE; CALCIMYCIN; CALCIUM; CFTR PROTEIN, HUMAN; CYCLIC AMP; DRUG DERIVATIVE; IMIDAZOLE DERIVATIVE; ISOQUINOLINE DERIVATIVE; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; RECOMBINANT PROTEIN; SULFONAMIDE; TETRAMISOLE; THIAZOLE DERIVATIVE; TRANSMEMBRANE CONDUCTANCE REGULATOR;

ANIMAL CELL; ARTICLE; CALCIUM CELL LEVEL; CHO CELL; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYSTIC FIBROSIS; DRUG MECHANISM; ENZYME ACTIVITY; MEMBRANE BINDING; MEMBRANE CONDUCTANCE; NONHUMAN; PATCH CLAMP; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; ANIMAL; BINDING SITE; CELL MEMBRANE POTENTIAL; DRUG ANTAGONISM; DRUG EFFECT; GENETIC TRANSFECTION; HAMSTER; HUMAN; KINETICS; METABOLISM; PHYSIOLOGY; POINT MUTATION; SITE DIRECTED MUTAGENESIS;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CALCIMYCIN; CALCIUM; CHO CELLS; CRICETINAE; CYCLIC AMP; CYCLIC AMP-DEPENDENT PROTEIN KINASES; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; ENZYME INHIBITORS; FORSKOLIN; HUMANS; IMIDAZOLES; ISOQUINOLINES; KINETICS; LEVAMISOLE; MEMBRANE POTENTIALS; MUTAGENESIS, SITE-DIRECTED; PATCH-CLAMP TECHNIQUES; POINT MUTATION; RECOMBINANT PROTEINS; SULFONAMIDES; TETRAMISOLE; THIAZOLES; TRANSFECTION;

EID: 0029666280     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.27.16171     Document Type: Article

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