serine and 4-iodo-2,5-dimethoxyphenylisopropylamine

serine has been researched along with 4-iodo-2,5-dimethoxyphenylisopropylamine 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	0 (0.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Baez, M; Johnson, MP; Lucaites, VL; Nelson, DL; Wainscott, DB	1
Becamel, C; Bockaert, J; Karaki, S; Mannoury la Cour, C; Marin, P; Millan, MJ; Murat, S; Prézeau, L; Vandermoere, F	1

Other Studies

2 other study(ies) available for serine and 4-iodo-2,5-dimethoxyphenylisopropylamine

Article	Year
Mutations of transmembrane IV and V serines indicate that all tryptamines do not bind to the rat 5-HT2A receptor in the same manner. Brain research. Molecular brain research, 1997, Oct-03, Volume: 49, Issue:1-2 Topics: Amino Acid Sequence; Amino Acid Substitution; Amphetamines; Animals; Binding Sites; Binding, Competitive; Cell Membrane; Ergolines; Ketanserin; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Rats; Receptor, Serotonin, 5-HT2A; Receptors, Serotonin; Recombinant Proteins; Serine; Serotonin; Serotonin Antagonists; Tryptamines	1997
Quantitative phosphoproteomics unravels biased phosphorylation of serotonin 2A receptor at Ser280 by hallucinogenic versus nonhallucinogenic agonists. Molecular & cellular proteomics : MCP, 2014, Volume: 13, Issue:5 Topics: Amphetamines; Animals; Cells, Cultured; Gene Expression Regulation; Hallucinogens; HEK293 Cells; Humans; Lisuride; Mice; Neurons; Phosphorylation; Prefrontal Cortex; Proteomics; Receptor, Serotonin, 5-HT2A; Serine; Serotonin 5-HT2 Receptor Agonists; Signal Transduction	2014

Article

Year

Mutations of transmembrane IV and V serines indicate that all tryptamines do not bind to the rat 5-HT2A receptor in the same manner.

Brain research. Molecular brain research, 1997, Oct-03, Volume: 49, Issue:1-2

Topics: Amino Acid Sequence; Amino Acid Substitution; Amphetamines; Animals; Binding Sites; Binding, Competitive; Cell Membrane; Ergolines; Ketanserin; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Structure, Secondary; Rats; Receptor, Serotonin, 5-HT2A; Receptors, Serotonin; Recombinant Proteins; Serine; Serotonin; Serotonin Antagonists; Tryptamines

1997

Quantitative phosphoproteomics unravels biased phosphorylation of serotonin 2A receptor at Ser280 by hallucinogenic versus nonhallucinogenic agonists.

Molecular & cellular proteomics : MCP, 2014, Volume: 13, Issue:5

Topics: Amphetamines; Animals; Cells, Cultured; Gene Expression Regulation; Hallucinogens; HEK293 Cells; Humans; Lisuride; Mice; Neurons; Phosphorylation; Prefrontal Cortex; Proteomics; Receptor, Serotonin, 5-HT2A; Serine; Serotonin 5-HT2 Receptor Agonists; Signal Transduction

2014