Syntaxin 1A modulates the voltage-gated L-type calcium channel (Cavl.2) in a cooperative manner

Journal of Biological Chemistry

Volumn 278, Issue 31, 2003, Pages 29231-29239

  Arien, Hadar ^a   Wiser, Ofer ^a   Arkin, Isaiah T ^a   Leonov, Hadas ^a   Atlas, Daphne ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CALCIUM; DIMERIZATION; MONOMERS; PROTEINS;

TRANSMEMBRANE DOMAIN;

BIOCHEMISTRY;

AMINO ACID; ARSENOSOBENZENE; CALCIUM CHANNEL L TYPE; CALCIUM ION; CYSTEINE; DIMER; DIMERCAPROL; MONOMER; REAGENT; SYNTAXIN; SYNTAXIN 1A; THIOL; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CALCIUM TRANSPORT; CELL MEMBRANE DEPOLARIZATION; CHANNEL GATING; CONFORMATIONAL TRANSITION; DIMERIZATION; DISULFIDE BOND; EXOCYTOSIS; MOLECULAR DYNAMICS; NEUROTRANSMITTER RELEASE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; SIGNAL TRANSDUCTION;

ANIMALS; ANTIGENS, SURFACE; ARSENICALS; CALCIUM; CALCIUM CHANNELS, L-TYPE; CELL MEMBRANE; CHELATING AGENTS; CYSTEINE; DIMERCAPROL; DIMERIZATION; DISULFIDES; ELECTRIC CONDUCTIVITY; FEMALE; GENE EXPRESSION; MEMBRANE POTENTIALS; MUTATION; NERVE TISSUE PROTEINS; OOCYTES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RABBITS; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; SULFHYDRYL COMPOUNDS; SYNTAXIN 1; TRANSFECTION; XENOPUS LAEVIS;

ANIMALIA;

EID: 0043208745     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M301401200     Document Type: Article

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