Altered adenylyl cyclase responsiveness subsequent to point mutations of Asp 128 in the third transmembrane domain of the δ-opioid receptor

Neuroscience

Volumn 93, Issue 3, 1999, Pages 1025-1031

  Cavalli, A ^a   Babey, A M ^a   Loh, H H ^a  

^a UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

Opioid receptor; Adenylyl cyclase; Constitutive activity; Point mutations

Indexed keywords

ADENYLATE CYCLASE; DELTA OPIATE RECEPTOR; FORSKOLIN; NALOXONE; PERTUSSIS TOXIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; RECEPTOR AFFINITY; SIGNAL TRANSDUCTION; SITE DIRECTED MUTAGENESIS;

ADENYLATE CYCLASE; ADENYLATE CYCLASE TOXIN; AMINO ACID SUBSTITUTION; ANIMALS; ASPARTIC ACID; BINDING, COMPETITIVE; CERCOPITHECUS AETHIOPS; CODON; COS CELLS; CYCLIC AMP; DIPRENORPHINE; DNA, COMPLEMENTARY; ENKEPHALIN, D-PENICILLAMINE (2,5)-; ENKEPHALINS; FORSKOLIN; GTP-BINDING PROTEINS; LIGANDS; MICE; MUTAGENESIS, SITE-DIRECTED; NALOXONE; PERTUSSIS TOXIN; POINT MUTATION; PROTEIN BINDING; RECEPTORS, OPIOID, DELTA; RECOMBINANT FUSION PROTEINS; SECOND MESSENGER SYSTEMS; TRANSFECTION; VIRULENCE FACTORS, BORDETELLA;

EID: 0032812836     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-4522(99)00280-8     Document Type: Article

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