N-linked glycosylation sites determine HERG channel surface membrane expression. [electronic resource]
Producer: 19990507Description: 41-8 p. digitalISSN:- 0022-3751
- Anti-Bacterial Agents -- pharmacology
- Blotting, Western
- Cation Transport Proteins
- Cell Line
- DNA-Binding Proteins
- ERG1 Potassium Channel
- Ether-A-Go-Go Potassium Channels
- Glycosylation -- drug effects
- Green Fluorescent Proteins
- Humans
- Intracellular Membranes -- physiology
- Ion Channel Gating -- genetics
- Kidney -- metabolism
- Luminescent Proteins -- metabolism
- Membrane Potentials -- physiology
- Microscopy, Confocal
- Mutation -- physiology
- Patch-Clamp Techniques
- Potassium Channels -- genetics
- Potassium Channels, Voltage-Gated
- Trans-Activators
- Transcriptional Regulator ERG
- Transfection -- drug effects
- Tunicamycin -- pharmacology
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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