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dihydroergotamine and 1-(1-naphthyl)piperazine

dihydroergotamine has been researched along with 1-(1-naphthyl)piperazine in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (100.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hamblin, MW; Monsma, FJ; Shen, Y; Sibley, DR; Ward, RP1
Adham, N; Bard, JA; Branchek, TA; Vaysse, P; Weinshank, RL; Zgombick, J1
Izzarelli, DG; Lewis-Higgins, L; Palmer, D; Parker, EM; Shapiro, RA1

Other Studies

3 other study(ies) available for dihydroergotamine and 1-(1-naphthyl)piperazine

ArticleYear
Cloning and expression of a novel serotonin receptor with high affinity for tricyclic psychotropic drugs.
    Molecular pharmacology, 1993, Volume: 43, Issue:3

    Topics: Amino Acid Sequence; Animals; Base Sequence; Binding, Competitive; Blotting, Northern; Brain Chemistry; Cell Line; Cloning, Molecular; DNA; GTP-Binding Proteins; Lysergic Acid Diethylamide; Molecular Sequence Data; Polymerase Chain Reaction; Psychotropic Drugs; Rats; Receptors, Serotonin; RNA; Serotonin; Serotonin Antagonists; Serotonin Receptor Agonists; Transfection

1993
Cloning of a novel human serotonin receptor (5-HT7) positively linked to adenylate cyclase.
    The Journal of biological chemistry, 1993, Nov-05, Volume: 268, Issue:31

    Topics: Adenylyl Cyclases; Base Sequence; Cloning, Molecular; DNA Primers; Humans; Molecular Sequence Data; Receptors, Serotonin; Sequence Alignment; Sequence Homology, Amino Acid; Serotonin Antagonists; Serotonin Receptor Agonists; Signal Transduction

1993
Two amino acid differences in the sixth transmembrane domain are partially responsible for the pharmacological differences between the 5-HT1D beta and 5-HT1E 5-hydroxytryptamine receptors.
    Journal of neurochemistry, 1996, Volume: 67, Issue:5

    Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Binding, Competitive; Chlorocebus aethiops; Cloning, Molecular; COS Cells; DNA Primers; Ergolines; Glutamic Acid; Humans; Isoleucine; Kinetics; Ligands; Lysine; Models, Structural; Molecular Sequence Data; Point Mutation; Polymerase Chain Reaction; Protein Structure, Secondary; Receptor, Serotonin, 5-HT1B; Receptors, Serotonin; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Serine; Serotonin; Transfection

1996