Forced Homodimerization by Site-Directed Mutagenesis Alters Guanylyl Cyclase Activity of Natriuretic Peptide Receptor B

Hypertension

Volumn 43, Issue 2, 2004, Pages 460-465

  Langenickel, Thomas ^a   Buttgereit, Jens ^a   Pagel, Ines ^a   Dietz, Rainer ^a   Willenbrock, Roland ^a   Bader, Michael ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

Author keywords

Cyclic GMP; Natriuretic peptides; Receptors, natriuretic peptides; Signal transduction

Indexed keywords

BRAIN NATRIURETIC PEPTIDE; BRAIN NATRIURETIC PEPTIDE RECEPTOR; CYSTEINE; DISULFIDE; G PROTEIN COUPLED RECEPTOR; GUANYLATE CYCLASE; GUANYLYL CYCLASE COUPLED RECEPTOR; LIGAND; RECEPTOR PROTEIN; SERINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; CONFERENCE PAPER; CONTROLLED STUDY; COVALENT BOND; DELETION MUTANT; DIMERIZATION; DISULFIDE BOND; DOSE RESPONSE; ENZYME ACTIVITY; ENZYME ASSAY; EXTRACELLULAR SPACE; FORCED HOMODIMERIZATION; GENE DELETION; GENETIC TRANSFECTION; LIGAND BINDING; MEMBRANE BINDING; NATRIURESIS; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; RAT; RECEPTOR BINDING; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; DIMERIZATION; GUANYLATE CYCLASE; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RATS; RECEPTORS, ATRIAL NATRIURETIC FACTOR; RNA, MESSENGER;

EID: 0842289494     PISSN: 0194911X     EISSN: 15244563     Source Type: Journal    
DOI: 10.1161/01.HYP.0000110907.33263.0b     Document Type: Article

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