ATP inhibition of K(ATP) channels: Control of nucleotide sensitivity by the N-terminal domain of the Kir6.2 subunit

Journal of Physiology

Volumn 515, Issue 1, 1999, Pages 19-30

  Koster, J C ^a   Sha, Q ^a   Shyng, S L ^a   Nichols, C G ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TETRAPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID; NUCLEOTIDE; POTASSIUM CHANNEL; PROTEIN SUBUNIT; SULFONYLUREA RECEPTOR; UNCLASSIFIED DRUG; ABC TRANSPORTER; ADENINE NUCLEOTIDE; ADENOSINE 5'-TETRAPHOSPHATE; DIAGNOSTIC AGENT; INWARDLY RECTIFYING POTASSIUM CHANNEL; MEMBRANE PROTEIN; POTASSIUM CHANNEL BLOCKING AGENT; REPRESSOR PROTEIN; RUBIDIUM; SACCHAROMYCES CEREVISIAE PROTEIN; SUR1 PROTEIN, S CEREVISIAE; UK ATP 1 POTASSIUM CHANNEL; UK-ATP-1 POTASSIUM CHANNEL; ADENOSINE DERIVATIVE; ADENOSINE TRIPHOSPHATE SENSITIVE POTASSIUM CHANNEL; INWARDLY RECTIFYING POTASSIUM CHANNEL SUBUNIT KIR6.2; SULFONYLUREA RECEPTOR 1;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOPLASM; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; ANIMAL; BIOSYNTHESIS; CELL LINE; CELL MEMBRANE POTENTIAL; CHANNEL GATING; DRUG ANTAGONISM; DRUG EFFECT; ENERGY METABOLISM; GENE DELETION; GENETICS; METABOLISM; PATCH CLAMP; PHYSIOLOGY; RAT; GENE MUTATION; MOLECULAR STABILITY; NUCLEOTIDE TRANSPORT; PROTEIN DOMAIN; PROTEIN FUNCTION; REGULATORY MECHANISM; SENSITIVITY ANALYSIS;

ADENINE NUCLEOTIDES; ADENOSINE DIPHOSPHATE; ADENOSINE MONOPHOSPHATE; ADENOSINE TRIPHOSPHATE; ANIMALS; ATP-BINDING CASSETTE TRANSPORTERS; CELL LINE; ENERGY METABOLISM; ION CHANNEL GATING; MEMBRANE POTENTIALS; MEMBRANE PROTEINS; PATCH-CLAMP TECHNIQUES; POTASSIUM CHANNEL BLOCKERS; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; RATS; REPRESSOR PROTEINS; RUBIDIUM; RUBIDIUM RADIOISOTOPES; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE DELETION;

EID: 0033558098     PISSN: 00223751     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1469-7793.1999.019ad.x     Document Type: Article

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