Page last updated: 2024-09-02

3,5-dihydroxyphenylglycine and sib 1757

3,5-dihydroxyphenylglycine has been researched along with sib 1757 in 3 studies

Compound Research Comparison

Studies (3,5-dihydroxyphenylglycine)	Trials (3,5-dihydroxyphenylglycine)	Recent Studies (post-2010) (3,5-dihydroxyphenylglycine)	Studies (sib 1757)	Trials (sib 1757)	Recent Studies (post-2010) (sib 1757)
22	0	10	29	0	9

Protein Interaction Comparison

Protein	Taxonomy	3,5-dihydroxyphenylglycine (IC50)	sib 1757 (IC50)
Luciferin 4-monooxygenase	Photinus pyralis (common eastern firefly)		2.212
Metabotropic glutamate receptor 5	Homo sapiens (human)		0.37

Research

Studies (3)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (33.33)	18.2507
2000's	2 (66.67)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Costantino, G; Macchiarulo, A; Pellicciari, R	1
Bräuner-Osborne, H; Egebjerg, J; Krogsgaard-Larsen, P; Madsen, U; Nielsen, EO	1
Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J	1

Reviews

1 review(s) available for 3,5-dihydroxyphenylglycine and sib 1757

Article	Year
Ligands for glutamate receptors: design and therapeutic prospects. Journal of medicinal chemistry, 2000, Jul-13, Volume: 43, Issue:14 Topics: Animals; Drug Design; Excitatory Amino Acid Agonists; Excitatory Amino Acid Antagonists; Humans; Ligands; N-Methylaspartate; Receptors, AMPA; Receptors, Glutamate; Receptors, Kainic Acid; Receptors, Metabotropic Glutamate; Synapses	2000

Other Studies

2 other study(ies) available for 3,5-dihydroxyphenylglycine and sib 1757

Article	Year
Modeling of amino-terminal domains of group I metabotropic glutamate receptors: structural motifs affecting ligand selectivity. Journal of medicinal chemistry, 1999, Dec-30, Volume: 42, Issue:26 Topics: Amino Acid Sequence; Binding Sites; Excitatory Amino Acid Agonists; Excitatory Amino Acid Antagonists; Ligands; Models, Molecular; Molecular Sequence Data; Protein Conformation; Receptors, Metabotropic Glutamate; Sequence Homology, Amino Acid	1999
Chemical genetics reveals a complex functional ground state of neural stem cells. Nature chemical biology, 2007, Volume: 3, Issue:5 Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells	2007

Article

Year

Modeling of amino-terminal domains of group I metabotropic glutamate receptors: structural motifs affecting ligand selectivity.

Journal of medicinal chemistry, 1999, Dec-30, Volume: 42, Issue:26

Topics: Amino Acid Sequence; Binding Sites; Excitatory Amino Acid Agonists; Excitatory Amino Acid Antagonists; Ligands; Models, Molecular; Molecular Sequence Data; Protein Conformation; Receptors, Metabotropic Glutamate; Sequence Homology, Amino Acid

1999

Chemical genetics reveals a complex functional ground state of neural stem cells.

Nature chemical biology, 2007, Volume: 3, Issue:5

Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells

2007