Duan, Jingjing <br/><br/>
Cryo-EM structure of TRPC5 at 2.8-Å resolution reveals unique and conserved structural elements essential for channel function.  [electronic resource] 

 -  Science advances  07 2019 
 - eaaw7935 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>2375-2548 
<br/><br/><label>Standard No.: </label>10.1126/sciadv.aaw7935  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Binding Sites<br/>Cations<br/>Conserved Sequence<br/>Cryoelectron Microscopy<br/>Gadolinium--pharmacology<br/>HEK293 Cells<br/>Humans<br/>Ion Channel Gating--drug effects<br/>Kinetics<br/>Lanthanum--pharmacology<br/>Lipids--chemistry<br/>Mice<br/>Mutation--genetics<br/>Structure-Activity Relationship<br/>TRPC Cation Channels--chemistry