A familial mutation renders atrial natriuretic peptide resistant to proteolytic degradation

Journal of Biological Chemistry

Volumn 284, Issue 29, 2009, Pages 19196-19202

  Dickey, Deborah M ^a   Yoder, Andrea R ^a   Potter, Lincoln R ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATRIAL FIBRILLATION; ATRIAL NATRIURETIC PEPTIDES; C TERMINUS; FRAME-SHIFT MUTATION; FRAMESHIFT; MOLECULAR BASIS; NATRIURETIC; NATRIURETIC PEPTIDES; PEPTIDE RECEPTOR; PROTEOLYTIC DEGRADATION; PROTEOLYTIC SUSCEPTIBILITY; WILD TYPES;

AMINO ACIDS; ORGANIC ACIDS;

AMINES;

ATRIAL NATRIURETIC FACTOR; CYCLIC GMP; MEMBRANE METALLOENDOPEPTIDASE; NATRIURETIC PEPTIDE RECEPTOR A; NATRIURETIC PEPTIDE RECEPTOR B; NATRIURETIC PEPTIDE RECEPTOR C;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; FAMILIAL DISEASE; FRAMESHIFT MUTATION; HEART ATRIUM FIBRILLATION; HUMAN; HUMAN CELL; HUMAN TISSUE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT; RECEPTOR BINDING;

AMINO ACID SEQUENCE; ANIMALS; ATRIAL NATRIURETIC FACTOR; BINDING, COMPETITIVE; CELL LINE; CYCLIC GMP; FAMILY HEALTH; HUMANS; HYDROLYSIS; MOLECULAR SEQUENCE DATA; MUTANT PROTEINS; MUTATION; NEPRILYSIN; PROTEIN BINDING; RATS; RECEPTORS, ATRIAL NATRIURETIC FACTOR; SERINE ENDOPEPTIDASES;

EID: 67749099838     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.010777     Document Type: Article

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