Setting up for the block: the mechanism underlying lidocaine's use-dependent inhibition of sodium channels.
Cummins
Theodore R
TR
Department of Pharmacology and Toxicology, Stark Neurosciences Research Institute, Indiana University School of Medicine, 950 W. Walnut St, R2-Room 468, Indianapolis, IN 46202, USA . rcummin@iupui.edu
D000779:Anesthetics, Local / Q000494:pharmacology*; D000889:Anti-Arrhythmia Agents / Q000494:pharmacology*; D001120:Arginine / Q000737:chemistry; D001665:Binding Sites; D001710:Biotin / Q000031:analogs & derivatives / Q000737:chemistry; D002460:Cell Line; D003545:Cysteine / Q000737:chemistry; D006801:Humans; D015640:Ion Channel Gating / Q000187:drug effects*; D007700:Kinetics; D008012:Lidocaine / Q000494:pharmacology*; D008564:Membrane Potentials; D009124:Muscle Proteins / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009154:Mutation; D062554:NAV1.5 Voltage-Gated Sodium Channel; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D026941:Sodium Channel Blockers / Q000494:pharmacology*; D015222:Sodium Channels / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014162:Transfection
D000779:Anesthetics, Local; D000889:Anti-Arrhythmia Agents; D009124:Muscle Proteins; C419543:N-biotinylaminoethyl methanethiosulfonate; D062554:NAV1.5 Voltage-Gated Sodium Channel; C568320:SCN5A protein, human; D026941:Sodium Channel Blockers; D015222:Sodium Channels; D001710:Biotin; D001120:Arginine; D008012:Lidocaine; D003545:Cysteine