A single point mutation increases the affinity of serotonin 5-HT1Dα, 5-HT1Dβ, 5-HT1E and 5-HT1F receptors for β-adrenergic antagonists
- 1 March 1994
- journal article
- Published by Elsevier in Neuropharmacology
- Vol. 33 (3-4) , 387-391
- https://doi.org/10.1016/0028-3908(94)90068-x
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- A Single Amino Acid Difference Accounts for the Pharmacological Distinctions Between the Rat and Human 5‐Hydroxytryptamine1B ReceptorsJournal of Neurochemistry, 1993
- Conversion of the human 5-HT1Dβ serotonin receptor to the rat 5-HT1b ligand-binding phenotype by Thr355 ASN site directed mutagenesisBiochemical Pharmacology, 1992
- A single amino-acid difference confers major pharmacological variation between human and rodent 5-HT1B receptorsNature, 1992
- Molecular cloning of a human serotonin receptor (S12) with a pharmacological profile resembling that of the 5-HT1D subtype.Journal of Biological Chemistry, 1992
- Molecular cloning and functional characterization of a human 5-HT1B serotonin receptor: A homologue of the rat 5-HT1B receptor with 5-HT1D-like pharmacological specificityBiochemical and Biophysical Research Communications, 1992
- Characterization of the human 5-hydroxytryptamine1B receptor.Journal of Biological Chemistry, 1992
- Species differences in the pharmacology of terminal 5-HT autoreceptors in mammalian brainTrends in Pharmacological Sciences, 1989
- Chimeric α 2 -,β 2 -Adrenergic Receptors: Delineation of Domains Involved in Effector Coupling and Ligand Binding SpecificityScience, 1988
- [71] Use of eukaryotic expression technology in the functional analysis of cloned genesPublished by Elsevier ,1987
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976