Page last updated: 2024-09-02

3,5-dihydroxyphenylglycine and 4-methylglutamic acid, threo-(l)-isomer

3,5-dihydroxyphenylglycine has been researched along with 4-methylglutamic acid, threo-(l)-isomer in 2 studies

Compound Research Comparison

Studies
(3,5-dihydroxyphenylglycine)
Trials
(3,5-dihydroxyphenylglycine)
Recent Studies (post-2010)
(3,5-dihydroxyphenylglycine)
Studies
(4-methylglutamic acid, threo-(l)-isomer)
Trials
(4-methylglutamic acid, threo-(l)-isomer)
Recent Studies (post-2010) (4-methylglutamic acid, threo-(l)-isomer)
22010502

Protein Interaction Comparison

ProteinTaxonomy3,5-dihydroxyphenylglycine (IC50)4-methylglutamic acid, threo-(l)-isomer (IC50)
Glutamate receptor ionotropic, kainate 1Rattus norvegicus (Norway rat)0.31
Glutamate receptor ionotropic, kainate 2Rattus norvegicus (Norway rat)0.31
Glutamate receptor ionotropic, kainate 3Rattus norvegicus (Norway rat)0.31
Glutamate receptor ionotropic, kainate 4Rattus norvegicus (Norway rat)0.31
Glutamate receptor ionotropic, kainate 5Rattus norvegicus (Norway rat)0.31

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (50.00)18.2507
2000's1 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Acher, FC; Brabet, I; Jullian, N; Pin, JP1
Bräuner-Osborne, H; Egebjerg, J; Krogsgaard-Larsen, P; Madsen, U; Nielsen, EO1

Reviews

1 review(s) available for 3,5-dihydroxyphenylglycine and 4-methylglutamic acid, threo-(l)-isomer

ArticleYear
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

1 other study(ies) available for 3,5-dihydroxyphenylglycine and 4-methylglutamic acid, threo-(l)-isomer

ArticleYear
Agonist selectivity of mGluR1 and mGluR2 metabotropic receptors: a different environment but similar recognition of an extended glutamate conformation.
    Journal of medicinal chemistry, 1999, May-06, Volume: 42, Issue:9

    Topics: Animals; Binding Sites; Cell Line; CHO Cells; Cricetinae; Glutamates; Ligands; Models, Molecular; Molecular Conformation; Receptors, Metabotropic Glutamate; Structure-Activity Relationship

1999