Position of aromatic residues in the S6 domain, not inactivation, dictates cisapride sensitivity of HERG and eag potassium channels

Proceedings of the National Academy of Sciences of the United States of America

Volumn 99, Issue 19, 2002, Pages 12461-12466

  Chen, Jun ^a   Seebohm, Guiscard ^a,b   Sanguinetti, Michael C ^a,b  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF UTAH   (United States)

Author keywords

Delayed rectifier; Voltage clamp; Xenopus oocyte

Indexed keywords

1' (6 CYANO 1,2,3,4 TETRAHYDRO 2 NAPHTHYL) 3,4 DIHYDRO 6 METHANESULFONAMIDOSPIRO[2H 1 BENZOPYRAN 2,4' PIPERIDIN] 4 OL; CISAPRIDE; PHENYLALANINE; POTASSIUM CHANNEL; TYROSINE;

ARTICLE; DRUG SENSITIVITY; GENE; GENE MUTATION; HEART ARRHYTHMIA; HERG GENE; HUMAN; LONG QT SYNDROME; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACIDS, AROMATIC; ANIMALS; BINDING SITES; CATION TRANSPORT PROTEINS; CISAPRIDE; DNA-BINDING PROTEINS; DROSOPHILA PROTEINS; ETHER-A-GO-GO POTASSIUM CHANNELS; FEMALE; HUMANS; LONG QT SYNDROME; MEMBRANE POTENTIALS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OOCYTES; POTASSIUM CHANNEL BLOCKERS; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TRANS-ACTIVATORS; XENOPUS LAEVIS;

EID: 0037126062     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.192367299     Document Type: Article

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