A structural motif in the C-terminal tail of slo1 confers carbon monoxide sensitivity to human BKCa channels

Pflugers Archiv European Journal of Physiology

Volumn 456, Issue 3, 2008, Pages 561-572

  Williams, Sandile E ^a   Brazier, Stephen P ^a   Baban, Nian ^a   Telezhkin, Vsevolod ^a   Müller, Carsten T ^a   Riccardi, Daniela ^a   Kemp, Paul J ^a  

^a CARDIFF UNIVERSITY   (United Kingdom)

Author keywords

Carbon monoxide; Gas transmitter; Heme; Hemeoxygenase; Potassium channel

Indexed keywords

CARBON MONOXIDE; HISTIDINE; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL ALPHA SUBUNIT; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL ALPHA1 SUBUNIT; PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELL STRAIN HEK293; CHANNEL GATING; CONTROLLED STUDY; EMBRYO; GENE EXPRESSION; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PHYSIOLOGY; POTASSIUM CONDUCTANCE; PRIORITY JOURNAL; PROTEIN MOTIF;

AMINO ACID MOTIFS; BINDING SITES; CALCIUM; CARBON MONOXIDE; CELL LINE; HUMANS; ION CHANNEL GATING; KINETICS; LARGE-CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA SUBUNITS; MEMBRANE POTENTIALS; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PATCH-CLAMP TECHNIQUES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; TRANSFECTION;

EID: 43149105180     PISSN: 00316768     EISSN: 14322013     Source Type: Journal    
DOI: 10.1007/s00424-007-0439-4     Document Type: Article

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