Petrecca, K <br/><br/>
N-linked glycosylation sites determine HERG channel surface membrane expression.  [electronic resource] 

 -  The Journal of physiology  Feb 1999 
 - 41-8 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-3751 
<br/><br/><label>Standard No.: </label>10.1111/j.1469-7793.1999.041ad.x  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Anti-Bacterial Agents--pharmacology<br/>Blotting, Western<br/>Cation Transport Proteins<br/>Cell Line<br/>DNA-Binding Proteins<br/>ERG1 Potassium Channel<br/>Ether-A-Go-Go Potassium Channels<br/>Glycosylation--drug effects<br/>Green Fluorescent Proteins<br/>Humans<br/>Intracellular Membranes--physiology<br/>Ion Channel Gating--genetics<br/>Kidney--metabolism<br/>Luminescent Proteins--metabolism<br/>Membrane Potentials--physiology<br/>Microscopy, Confocal<br/>Mutation--physiology<br/>Patch-Clamp Techniques<br/>Potassium Channels--genetics<br/>Potassium Channels, Voltage-Gated<br/>Trans-Activators<br/>Transcriptional Regulator ERG<br/>Transfection--drug effects<br/>Tunicamycin--pharmacology