Position of aromatic residues in the S6 domain, not inactivation, dictates cisapride sensitivity of HERG and eag potassium channels. [electronic resource]
Producer: 20021028Description: 12461-6 p. digitalISSN:- 0027-8424
- Amino Acid Sequence
- Amino Acids, Aromatic -- chemistry
- Animals
- Binding Sites -- genetics
- Cation Transport Proteins
- Cisapride -- pharmacology
- DNA-Binding Proteins
- Drosophila Proteins -- antagonists & inhibitors
- ERG1 Potassium Channel
- Ether-A-Go-Go Potassium Channels
- Female
- Humans
- In Vitro Techniques
- Long QT Syndrome -- chemically induced
- Membrane Potentials
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Oocytes -- metabolism
- Potassium Channel Blockers
- Potassium Channels -- chemistry
- Potassium Channels, Voltage-Gated
- Protein Structure, Tertiary
- Recombinant Proteins -- antagonists & inhibitors
- Sequence Homology, Amino Acid
- Trans-Activators
- Transcriptional Regulator ERG
- Xenopus laevis
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Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
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