A disulfide-bridged mutant of natriuretic peptide receptor-A displays constitutive activity: Role of receptor dimerization in signal transduction

Journal of Biological Chemistry

Volumn 274, Issue 14, 1999, Pages 9752-9759

  Labrecque, Jean ^a   Mc Nicoll, Normand ^a   Marquis, Martin ^a   De Léan, André ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ATRIAL NATRIURETIC FACTOR; BRAIN NATRIURETIC PEPTIDE; CYCLIC GMP; CYSTEINE; DISULFIDE; GUANYLATE CYCLASE; MUTANT PROTEIN; NATRIURETIC PEPTIDE TYPE A; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; DIMERIZATION; ENZYME ACTIVATION; ENZYME INHIBITION; GENE MUTATION; HUMAN; HUMAN CELL; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; RECEPTOR BINDING; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING, COMPETITIVE; CYSTEINE; DIMERIZATION; DISULFIDES; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GUANYLATE CYCLASE; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RATS; RECEPTORS, ATRIAL NATRIURETIC FACTOR; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0040736351     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.14.9752     Document Type: Article

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