serine and mdl 100907

serine has been researched along with mdl 100907 in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Backstrom, JR; Fentress, HM; Grinde, E; Herrick-Davis, K; Mazurkiewicz, JE; Sanders-Bush, E	1
Grinde, E; Harrigan, TJ; Herrick-Davis, K; Mazurkiewicz, JE	1

Other Studies

2 other study(ies) available for serine and mdl 100907

Article	Year
Pharmacological properties of the Cys23Ser single nucleotide polymorphism in human 5-HT2C receptor isoforms. The pharmacogenomics journal, 2005, Volume: 5, Issue:4 Topics: Animals; Binding, Competitive; Cell Line; Chlorocebus aethiops; Cysteine; Dose-Response Relationship, Drug; Humans; Ligands; Mice; Mutagenesis, Site-Directed; Polymorphism, Single Nucleotide; Protein Isoforms; Receptor, Serotonin, 5-HT2C; Serine; Serotonin 5-HT2 Receptor Agonists; Serotonin 5-HT2 Receptor Antagonists; Serotonin Antagonists; Serotonin Receptor Agonists; Transfection	2005
Inhibition of serotonin 5-hydroxytryptamine2c receptor function through heterodimerization: receptor dimers bind two molecules of ligand and one G-protein. The Journal of biological chemistry, 2005, Dec-02, Volume: 280, Issue:48 Topics: Arginine; Bacterial Proteins; Blotting, Western; Cell Line; Cell Membrane; Dimerization; DNA, Complementary; Endocytosis; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; GTP-Binding Proteins; Humans; Immunoprecipitation; Ligands; Luminescent Proteins; Microscopy, Confocal; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Protein Binding; Receptor, Serotonin, 5-HT2C; Serine; Serotonin 5-HT2 Receptor Antagonists; Signal Transduction; Time Factors; Transfection	2005

Article

Year

Pharmacological properties of the Cys23Ser single nucleotide polymorphism in human 5-HT2C receptor isoforms.

The pharmacogenomics journal, 2005, Volume: 5, Issue:4

Topics: Animals; Binding, Competitive; Cell Line; Chlorocebus aethiops; Cysteine; Dose-Response Relationship, Drug; Humans; Ligands; Mice; Mutagenesis, Site-Directed; Polymorphism, Single Nucleotide; Protein Isoforms; Receptor, Serotonin, 5-HT2C; Serine; Serotonin 5-HT2 Receptor Agonists; Serotonin 5-HT2 Receptor Antagonists; Serotonin Antagonists; Serotonin Receptor Agonists; Transfection

2005

Inhibition of serotonin 5-hydroxytryptamine2c receptor function through heterodimerization: receptor dimers bind two molecules of ligand and one G-protein.

The Journal of biological chemistry, 2005, Dec-02, Volume: 280, Issue:48

Topics: Arginine; Bacterial Proteins; Blotting, Western; Cell Line; Cell Membrane; Dimerization; DNA, Complementary; Endocytosis; Fluorescence Resonance Energy Transfer; Green Fluorescent Proteins; GTP-Binding Proteins; Humans; Immunoprecipitation; Ligands; Luminescent Proteins; Microscopy, Confocal; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Protein Binding; Receptor, Serotonin, 5-HT2C; Serine; Serotonin 5-HT2 Receptor Antagonists; Signal Transduction; Time Factors; Transfection

2005