The C-terminal basic residues contribute to the chemical- and voltage-dependent activation of TRPA1

Biochemical Journal

Volumn 433, Issue 1, 2011, Pages 197-204

  Samad, Abdul ^a,b   Sura, Lucie ^a   Benedikt, Jan ^a   Ettrich, Rudiger ^b   Minofar, Babak ^b   Teisinger, Jan ^a   Vlachova, Viktorie ^a  

^a INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^b INSTITUTE OF MATHEMATICS   (Czech Republic)

Author keywords

C terminal domain; Pleckstrin homology (PH) domain; Structure function relationship; Transient receptor potential ankyrin (TRPA); Voltage dependent gating

Indexed keywords

ALLYL ISOTHIOCYANATE; AMINO ACID; ARGININE; LYSINE; TRANSIENT RECEPTOR POTENTIAL CHANNEL A1;

ALPHA HELIX; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE POTENTIAL; ELECTRIC CONDUCTIVITY; EMBRYO; GENE MUTATION; HUMAN; HUMAN CELL; MOLECULAR INTERACTION; MUTAGENESIS; PRIORITY JOURNAL; SENSITIVITY ANALYSIS; STEADY STATE;

AMINO ACID SUBSTITUTION; AMINO ACIDS, BASIC; ANKYRIN REPEAT; ANKYRINS; CALCIUM CHANNELS; HUMANS; IONS; MEMBRANE POTENTIALS; NERVE TISSUE PROTEINS; SENSORY RECEPTOR CELLS; STATIC ELECTRICITY; TRANSIENT RECEPTOR POTENTIAL CHANNELS;

CINNAMOMUM VERUM;

EID: 79551485942     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101256     Document Type: Article

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