Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes

Journal of Physiology

Volumn 514, Issue 3, 1999, Pages 667-675

  Sanguinetti, M C ^a   Xu, Q P ^a  

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

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; LYSINE; POTASSIUM CHANNEL; ALANINE; POTASSIUM CHANNEL HERG;

ANIMAL CELL; ARTICLE; CHANNEL GATING; FEMALE; GENE MUTATION; HYPERPOLARIZATION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; XENOPUS; ACTION POTENTIAL AMPLITUDE; ACTIVATION TIME CONSTANT; ADULT; AMINO ACID SUBSTITUTION; ANIMAL EXPERIMENT; CELL MEMBRANE DEPOLARIZATION; CONTROLLED STUDY; DEACTIVATION TIME CONSTANT; DECAY TIME CONSTANT; HERG GENE; INACTIVATION TIME CONSTANT; MEMBRANE POTENTIAL; POTASSIUM CURRENT; PROTEIN DOMAIN; PROTEIN EXPRESSION; S4 S5 LINKER; WILD TYPE;

ANIMALS; BIOTRANSFORMATION; CATION TRANSPORT PROTEINS; CYTOPLASM; DNA-BINDING PROTEINS; ELECTRIC STIMULATION; ELECTROPHYSIOLOGY; ETHER-A-GO-GO POTASSIUM CHANNELS; HUMANS; ION CHANNEL GATING; KINETICS; MEMBRANE POTENTIALS; MUTAGENESIS, INSERTIONAL; MUTATION; OOCYTES; PATCH-CLAMP TECHNIQUES; POTASSIUM CHANNELS; POTASSIUM CHANNELS, VOLTAGE-GATED; TRANS-ACTIVATORS; XENOPUS LAEVIS;

EID: 0033082093     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1469-7793.1999.667ad.x     Document Type: Article

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