Page last updated: 2024-08-21

bufotenin and serine

bufotenin has been researched along with serine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Almaula, N; Ebersole, BJ; Sealfon, SC; Weinstein, H; Zhang, D	1
Ebersole, BJ; Sealfon, SC; Visiers, I; Weinstein, H	1

Other Studies

2 other study(ies) available for bufotenin and serine

Article	Year
Mapping the binding site pocket of the serotonin 5-Hydroxytryptamine2A receptor. Ser3.36(159) provides a second interaction site for the protonated amine of serotonin but not of lysergic acid diethylamide or bufotenin. The Journal of biological chemistry, 1996, Jun-21, Volume: 271, Issue:25 Topics: Amino Acid Sequence; Animals; Binding Sites; Bufotenin; Cell Line; Chlorocebus aethiops; Cloning, Molecular; Computer Simulation; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphatidylinositols; Protein Structure, Secondary; Receptor, Serotonin, 5-HT2A; Receptors, Serotonin; Recombinant Proteins; Serine; Serotonin; Transfection	1996
Molecular basis of partial agonism: orientation of indoleamine ligands in the binding pocket of the human serotonin 5-HT2A receptor determines relative efficacy. Molecular pharmacology, 2003, Volume: 63, Issue:1 Topics: Alanine; Amino Acid Substitution; Animals; Binding Sites; Bufotenin; Chlorocebus aethiops; COS Cells; Models, Molecular; Mutation; Receptor, Serotonin, 5-HT2A; Receptors, Serotonin; Serine; Serotonin; Structure-Activity Relationship	2003

Article

Year

Mapping the binding site pocket of the serotonin 5-Hydroxytryptamine2A receptor. Ser3.36(159) provides a second interaction site for the protonated amine of serotonin but not of lysergic acid diethylamide or bufotenin.

The Journal of biological chemistry, 1996, Jun-21, Volume: 271, Issue:25

Topics: Amino Acid Sequence; Animals; Binding Sites; Bufotenin; Cell Line; Chlorocebus aethiops; Cloning, Molecular; Computer Simulation; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphatidylinositols; Protein Structure, Secondary; Receptor, Serotonin, 5-HT2A; Receptors, Serotonin; Recombinant Proteins; Serine; Serotonin; Transfection

1996

Molecular basis of partial agonism: orientation of indoleamine ligands in the binding pocket of the human serotonin 5-HT2A receptor determines relative efficacy.

Molecular pharmacology, 2003, Volume: 63, Issue:1

Topics: Alanine; Amino Acid Substitution; Animals; Binding Sites; Bufotenin; Chlorocebus aethiops; COS Cells; Models, Molecular; Mutation; Receptor, Serotonin, 5-HT2A; Receptors, Serotonin; Serine; Serotonin; Structure-Activity Relationship

2003