Carson, M R <br/><br/>
The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity.  [electronic resource] 

 -  The Journal of biological chemistry  Jan 1995 
 - 1711-7 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.270.4.1711  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>3T3 Cells<br/>Adenosine Triphosphate--analogs & derivatives<br/>Adenylyl Imidodiphosphate--pharmacology<br/>Amino Acid Sequence<br/>Animals<br/>Azides--metabolism<br/>Binding Sites<br/>Chloride Channels--chemistry<br/>Conserved Sequence<br/>Cyclic AMP-Dependent Protein Kinases--metabolism<br/>Cystic Fibrosis Transmembrane Conductance Regulator<br/>Genetic Variation<br/>HeLa Cells<br/>Humans<br/>Ion Channel Gating<br/>Lysine<br/>Membrane Potentials<br/>Membrane Proteins--chemistry<br/>Mice<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Patch-Clamp Techniques<br/>Phosphorylation<br/>Point Mutation<br/>Recombinant Proteins--chemistry<br/>Transfection