Constitutive activation and uncoupling of the atrial natriuretic peptide receptor by mutations at the dimer interface: Role of the dimer structure in signaling

Journal of Biological Chemistry

Volumn 279, Issue 7, 2004, Pages 6115-6123

  Qiu, Yue ^a   Ogawa, Haruo ^a   Miyagi, Masaru ^a,b   Misono, Kunio S ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

^b Dept of Biochem and Molec Biology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION REACTIONS; BIOLOGICAL MEMBRANES; CELLS; CHEMICAL ACTIVATION; CRYSTAL STRUCTURE; DIMERS; HORMONES; INTERFACES (MATERIALS); MUTAGENESIS; PHYSIOLOGY; ROTATION;

ATRIAL NATRIURETIC PEPTIDE (ANP); MUTATIONS;

BIOCHEMISTRY;

ACID ANHYDRIDE; ARGININE; ATRIAL NATRIURETIC FACTOR; ATRIAL NATRIURETIC FACTOR RECEPTOR; DIMER; GUANYLATE CYCLASE; HISTIDINE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL STRAIN COS1; CRYSTAL STRUCTURE; ENZYME ACTIVATION; HORMONE BINDING; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; RECEPTOR UPREGULATION; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS;

ANIMALS; ARGININE; COS CELLS; CRYSTALLOGRAPHY, X-RAY; CYCLIC GMP; DIETHYL PYROCARBONATE; DIMERIZATION; DNA, COMPLEMENTARY; HISTIDINE; HYDROGEN BONDING; KINETICS; MASS SPECTROMETRY; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDES; PROTEIN CONFORMATION; RECEPTORS, ATRIAL NATRIURETIC FACTOR; SIGNAL TRANSDUCTION; TIME FACTORS; TRANSFECTION; TRYPSIN; TRYPTOPHAN;

ANIMALIA;

EID: 1242316955     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M310225200     Document Type: Article

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