Primary structure and function of the catecholamine release inhibitory peptide catestatin (chromogranin A344-364): Identification of amino acid residues crucial for activity

Molecular Endocrinology

Volumn 14, Issue 10, 2000, Pages 1525-1535

  Mahata, S K ^a   Mahata, M ^a   Wakade, A R ^a   O'Connor, D T ^a  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ARGININE; ARGINYLSERYLMETHIONYLARGINYLLEUCYLSERYLPHENYLALANYLARGINYLALANYLARGINYLGLYC YLTYROSYLGLYCYLPHENYLALANYLARGINYLGLYCYLPROLYLGLYCYLLEUCYLGLUTAMINYLLEUCINE; CATECHOLAMINE; CATESTATIN; CHROMOGRANIN A; CHROMOGRANIN A[344-364]; GLYCINE; LEUCINE; METHIONINE; NICOTINE; NICOTINIC RECEPTOR; NICOTINIC RECEPTOR BLOCKING AGENT; PEPTIDE FRAGMENT; PHENYLALANINE; SERINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATECHOLAMINE RELEASE; CONTROLLED STUDY; DESENSITIZATION; IC 50; MUTAGENESIS; NONHUMAN; PHARMACOPHORE; PHEOCHROMOCYTOMA CELL; PRIORITY JOURNAL; PROTEIN DOMAIN; RAT; SIGNAL TRANSDUCTION;

ANIMALIA; BOVINAE;

EID: 0033768870     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/mend.14.10.0531     Document Type: Article

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