5,7-dichlorokynurenic acid and mdl 105519

5,7-dichlorokynurenic acid has been researched along with mdl 105519 in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's1 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Baron, BM; Gross, RS; Harrison, BL; Hawes, C; Siegel, BW; Towers, P1
Becker, J; Li, Z; Noe, CR1
Reynolds, IJ; Sharma, TA1
Johnson, MS; Moretti, L; Pentikäinen, OT; Settimo, L1

Other Studies

4 other study(ies) available for 5,7-dichlorokynurenic acid and mdl 105519

ArticleYear
[3H]MDL 105,519, a high-affinity radioligand for the N-methyl-D-aspartate receptor-associated glycine recognition site.
    The Journal of pharmacology and experimental therapeutics, 1996, Volume: 279, Issue:1

    Topics: Animals; Binding Sites; Glycine; Hydrogen-Ion Concentration; Indoles; Kynurenic Acid; Ligands; Rats; Receptors, N-Methyl-D-Aspartate; Structure-Activity Relationship

1996
Molecular and pharmacological characterization of recombinant rat/mice N-methyl-D-aspartate receptor subtypes in the yeast Saccharomyces cerevisiae.
    European journal of biochemistry, 1998, Sep-01, Volume: 256, Issue:2

    Topics: Animals; Carbodiimides; Cell Membrane; Cloning, Molecular; Cycloleucine; Excitatory Amino Acid Antagonists; Fluorescent Antibody Technique; Gene Expression; Glutamic Acid; Indoles; Kynurenic Acid; Mice; Microscopy, Fluorescence; Protein Binding; Rats; Receptors, N-Methyl-D-Aspartate; Recombinant Fusion Proteins; Recombinant Proteins; RNA, Messenger; Saccharomyces cerevisiae; Transformation, Genetic

1998
Complex polyamine effects on [3H]MDL 105,519 binding to the NMDA receptor glycine site.
    Neurochemistry international, 1998, Volume: 33, Issue:2

    Topics: Aminoquinolines; Animals; Binding Sites; Binding, Competitive; Brain; Cell Membrane; Dizocilpine Maleate; Excitatory Amino Acid Antagonists; Glycine; Indoles; Kynurenic Acid; Polyamines; Rats; Receptors, N-Methyl-D-Aspartate; Spermidine; Spermine; Tritium

1998
Model structures of the N-methyl-D-aspartate receptor subunit NR1 explain the molecular recognition of agonist and antagonist ligands.
    Journal of structural biology, 2004, Volume: 145, Issue:3

    Topics: Alanine; Amino Acid Sequence; Animals; Bacterial Proteins; Binding Sites; Crystallography, X-Ray; Cycloserine; Databases as Topic; Escherichia coli; Excitatory Amino Acid Antagonists; Glycine; Humans; Hydrogen Bonding; Indoles; Kynurenic Acid; Ligands; Mice; Models, Chemical; Models, Molecular; Molecular Sequence Data; Potassium Channels; Proline; Protein Binding; Protein Conformation; Protein Isoforms; Protein Structure, Tertiary; Rats; Receptors, AMPA; Receptors, Glutamate; Receptors, N-Methyl-D-Aspartate; Sequence Homology, Amino Acid; Serine; Threonine; Tryptophan; Water

2004