Pegan, Scott <br/><br/>
Cytoplasmic domain structures of Kir2.1 and Kir3.1 show sites for modulating gating and rectification.  [electronic resource] 

 -  Nature neuroscience  Mar 2005 
 - 279-87 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>1097-6256 
<br/><br/><label>Standard No.: </label>10.1038/nn1411  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Analysis of Variance<br/>Animals<br/>Cloning, Molecular--methods<br/>Crystallography--methods<br/>Dose-Response Relationship, Drug<br/>Electric Conductivity<br/>G Protein-Coupled Inwardly-Rectifying Potassium Channels<br/>GTP-Binding Protein beta Subunits--genetics<br/>Ion Channel Gating--drug effects<br/>Macromolecular Substances<br/>Membrane Potentials--drug effects<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed--physiology<br/>Patch-Clamp Techniques--methods<br/>Phosphatidylinositol 4,5-Diphosphate--metabolism<br/>Potassium--pharmacology<br/>Potassium Channels, Inwardly Rectifying--chemistry<br/>Protein Conformation<br/>Protein Structure, Tertiary--physiology<br/>Recombinant Fusion Proteins--chemistry<br/>Xenopus laevis