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Volumn 272, Issue 2, 1997, Pages 705-708
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The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression
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Author keywords
[No Author keywords available]
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Indexed keywords
MEMBRANE PROTEIN;
OLIGOMER;
POTASSIUM;
POTASSIUM CHANNEL;
PROTEIN SUBUNIT;
CATION TRANSPORT PROTEIN;
DNA BINDING PROTEIN;
ERG PROTEIN, HUMAN;
ERG1 POTASSIUM CHANNEL;
KCNH2 PROTEIN, HUMAN;
KCNH6 PROTEIN, HUMAN;
POTASSIUM CHANNEL HERG;
TRANSACTIVATOR PROTEIN;
VOLTAGE GATED POTASSIUM CHANNEL;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CHROMOSOME 7;
CROSS LINKING;
FRAMESHIFT MUTATION;
GENE MUTATION;
GENETIC TRANSFECTION;
HUMAN;
HUMAN CELL;
HYDROPHILICITY;
LONG QT SYNDROME;
PHENOTYPE;
PRIORITY JOURNAL;
PROTEIN ASSEMBLY;
PROTEIN LOCALIZATION;
PROTEIN PROTEIN INTERACTION;
SUDDEN DEATH;
VOLTAGE CLAMP;
GENETICS;
MUTAGENESIS;
POLYACRYLAMIDE GEL ELECTROPHORESIS;
PROTEIN CONFORMATION;
CATION TRANSPORT PROTEINS;
DNA-BINDING PROTEINS;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
ETHER-A-GO-GO POTASSIUM CHANNELS;
HUMANS;
LONG QT SYNDROME;
MUTAGENESIS;
POTASSIUM CHANNELS;
POTASSIUM CHANNELS, VOLTAGE-GATED;
PROTEIN CONFORMATION;
TRANS-ACTIVATORS;
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EID: 0030614462
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.272.2.705 Document Type: Article |
Times cited : (87)
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References (25)
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