The N terminus of the cardiac L-type Ca2+ channel α(1C) subunit. The initial segment is ubiquitous and crucial for protein kinase C modulation, but is not directly phosphorylated

Journal of Biological Chemistry

Volumn 274, Issue 44, 1999, Pages 31145-31149

  Shistik, Elena ^a   Keren Raifman, Tal ^a   Idelson, Gregory H ^b   Blumenstein, Yakov ^a   Dascal, Nathan ^a   Ivanina, Tatiana ^a  

^a TEL AVIV UNIVERSITY   (Israel)

^b Alomone Labs Ltd   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CALCIUM CHANNEL; POLYCLONAL ANTIBODY; PROTEIN KINASE C;

AMINO ACID ANALYSIS; ANIMAL TISSUE; ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PHOSPHORYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN INTERACTION; RAT;

AMINO ACID SEQUENCE; ANIMALS; BRAIN CHEMISTRY; CALCIUM CHANNELS, L-TYPE; ENZYME ACTIVATION; ION CHANNEL GATING; MOLECULAR SEQUENCE DATA; MYOCARDIUM; PATCH-CLAMP TECHNIQUES; PEPTIDE FRAGMENTS; PHOSPHORYLATION; PROTEIN ISOFORMS; PROTEIN KINASE C; RABBITS; RATS; RATS, WISTAR; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0033615701     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.44.31145     Document Type: Article

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