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Volumn 16, Issue 3, 2002, Pages 390-400
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Disease-associated mutations in KCNE potassium channel subunits (MiRPs) reveal promiscuous disruption of multiple currents and conservation of mechanism
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Author keywords
Cardiac arrhythmia; HERG; KCNQ1; Kv3.4; MinK; MiRP1; MiRP2; Periodic paralysis
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Indexed keywords
ARGININE;
ASPARAGINE;
ASPARTIC ACID;
GENE PRODUCT;
HISTIDINE;
POTASSIUM CHANNEL;
PROTEIN MINK;
PROTEIN MIRP1;
PROTEIN MIRP2;
PROTEIN SUBUNIT;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
ANIMAL CELL;
ARTICLE;
CONTROLLED STUDY;
GENE ACTIVITY;
GENE FUNCTION;
GENE MUTATION;
HEART ARRHYTHMIA;
MOLECULAR INTERACTION;
NONHUMAN;
PARALYSIS;
POINT MUTATION;
POTASSIUM CURRENT;
PRIORITY JOURNAL;
REGULATORY MECHANISM;
AMINO ACID SEQUENCE;
ANIMALS;
ARRHYTHMIA;
CATION TRANSPORT PROTEINS;
CELLS, CULTURED;
CONSERVED SEQUENCE;
COS CELLS;
DNA-BINDING PROTEINS;
ELECTRIC CONDUCTIVITY;
ETHER-A-GO-GO POTASSIUM CHANNELS;
KCNQ POTASSIUM CHANNELS;
KCNQ1 POTASSIUM CHANNEL;
MOLECULAR SEQUENCE DATA;
PATCH-CLAMP TECHNIQUES;
POINT MUTATION;
POTASSIUM CHANNELS;
POTASSIUM CHANNELS, VOLTAGE-GATED;
PROTEIN SUBUNITS;
SEQUENCE ALIGNMENT;
SHAW POTASSIUM CHANNELS;
TRANS-ACTIVATORS;
UP-REGULATION;
ANIMALIA;
MUSTELA VISON;
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EID: 0036190347
PISSN: 08926638
EISSN: None
Source Type: Journal
DOI: 10.1096/fj.01-0520hyp Document Type: Article |
Times cited : (76)
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References (36)
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