A protein kinase C site highly conserved in P2X subunits controls the desensitization kinetics of P2X2 ATP-gated channels

Journal of Biological Chemistry

Volumn 275, Issue 14, 2000, Pages 10190-10195

  Boué Grabot, Éric ^a   Archambault, Vincent ^a   Séguéla, Philippe ^a  

^a MCGILL UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CATION CHANNEL; CHELERYTHRINE; COMPLEMENTARY DNA; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; PURINE P2X RECEPTOR; PURINE RECEPTOR; STAUROSPORINE;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; GENE MUTATION; MEMBRANE ELECTROPHYSIOLOGY; NONHUMAN; OOCYTE; PRIORITY JOURNAL; RECEPTOR DOWN REGULATION; VOLTAGE CLAMP; XENOPUS;

ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CELL LINE; CONSENSUS SEQUENCE; CONSERVED SEQUENCE; HUMANS; ION CHANNEL GATING; KINETICS; MEMBRANE POTENTIALS; MOLECULAR SEQUENCE DATA; PATCH-CLAMP TECHNIQUES; PROTEIN KINASE C; RATS; RECEPTORS, PURINERGIC P2; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TRANSFECTION;

ANIMALIA; MAMMALIA;

EID: 0040609340     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.14.10190     Document Type: Article

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