Drug binding to HERG channels: evidence for a 'non-aromatic' binding site for fluvoxamine.
Mitcheson
John S
JS
Department of Cell Physiology and Pharmacology, University of Leicester, Maurice Shock Medical Sciences Building, University Road, Leicester LEI 9HN. jm109@le.ac.uk
D000818:Animals; D001665:Binding Sites / Q000187:drug effects / Q000502:physiology; D027682:Cation Transport Proteins; D004268:DNA-Binding Proteins; D000072237:ERG1 Potassium Channel; D051638:Ether-A-Go-Go Potassium Channels; D016666:Fluvoxamine / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D015221:Potassium Channels / Q000737:chemistry / Q000378:metabolism*; D024642:Potassium Channels, Voltage-Gated; D011955:Receptors, Drug / Q000378:metabolism*; D015534:Trans-Activators; D000071230:Transcriptional Regulator ERG
D027682:Cation Transport Proteins; D004268:DNA-Binding Proteins; C072312:ERG protein, human; D000072237:ERG1 Potassium Channel; D051638:Ether-A-Go-Go Potassium Channels; C000606913:KCNH2 protein, human; C092509:KCNH6 protein, human; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D011955:Receptors, Drug; D015534:Trans-Activators; D000071230:Transcriptional Regulator ERG; D016666:Fluvoxamine