Topographical amino acid substitution in position 10 of glucagon leads to antagonists/partial agonists with greater binding differences

Journal of Medicinal Chemistry

Volumn 39, Issue 13, 1996, Pages 2449-2455

  Azizeh, Bassem Y ^a   Shenderovich, Mark D ^a   Trivedi, Dev ^a   Li, Guigen ^a   Sturm, Noel S ^a   Hruby, Victor J ^a  

^a University of Arizona ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; AMINO ACID; GLUCAGON; GLUCAGON DERIVATIVE; GLUCAGON RECEPTOR;

AGONIST; AMINO ACID SUBSTITUTION; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING COMPETITION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG ANTAGONISM; DRUG RECEPTOR BINDING; DRUG STRUCTURE; ENZYME ACTIVATION; ISOMER; LIVER MEMBRANE; NONHUMAN; RAT; TOPOGRAPHY;

ADENYLATE CYCLASE; AMINO ACID SEQUENCE; AMINOBUTYRIC ACIDS; ANIMALS; CELL MEMBRANE; GLUCAGON; LIVER; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; RATS; RATS, SPRAGUE-DAWLEY; RECEPTORS, GLUCAGON; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0029993270     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm960130b     Document Type: Article

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