Mutation of a conserved serine in TM4 of opioid receptors confers full agonistic properties to classical antagonists

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 12, 1996, Pages 5715-5719

  Claude, P A ^a   Wotta, D R ^a   Zhang, X H ^a   Prather, P L ^a   McGinn, T M ^a   Erickson, L J ^a   Loh, H H ^a   Law, P Y ^a  

^a UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; FORSKOLIN; GUANINE NUCLEOTIDE BINDING PROTEIN; MU OPIATE RECEPTOR; NALOXONE; NALTREXONE; NALTRIBEN; OPIATE RECEPTOR; POTASSIUM CHANNEL; SERINE; SIGMA OPIATE RECEPTOR;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CHO CELL; GENE MUTATION; NONHUMAN; OOCYTE; PRIORITY JOURNAL; RECEPTOR BINDING; RECEPTOR DENSITY; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; XENOPUS LAEVIS;

ANIMALS; BASE SEQUENCE; CONSERVED SEQUENCE; G PROTEIN-COUPLED INWARDLY-RECTIFYING POTASSIUM CHANNELS; LEUCINE; MOLECULAR SEQUENCE DATA; MUTATION; NARCOTIC ANTAGONISTS; OLIGODEOXYRIBONUCLEOTIDES; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; RECEPTORS, OPIOID; RECOMBINANT FUSION PROTEINS; SERINE; XENOPUS LAEVIS;

EID: 0029942187     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.12.5715     Document Type: Article

References (0)