serine and mdl 105519

serine has been researched along with mdl 105519 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	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Ivanovic, A; Kuhse, J; Laube, B; Reiländer, H	1
Johnson, MS; Moretti, L; Pentikäinen, OT; Settimo, L	1

Other Studies

2 other study(ies) available for serine and mdl 105519

Article	Year
Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit. The Journal of biological chemistry, 1998, Aug-07, Volume: 273, Issue:32 Topics: Animals; Baculoviridae; Binding Sites; Binding, Competitive; Excitatory Amino Acid Antagonists; Glutamic Acid; Glycine; Indoles; Kynurenic Acid; Protein Binding; Protein Conformation; Receptors, N-Methyl-D-Aspartate; Recombinant Fusion Proteins; Serine; Spodoptera	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

Article

Year

Expression and initial characterization of a soluble glycine binding domain of the N-methyl-D-aspartate receptor NR1 subunit.

The Journal of biological chemistry, 1998, Aug-07, Volume: 273, Issue:32

Topics: Animals; Baculoviridae; Binding Sites; Binding, Competitive; Excitatory Amino Acid Antagonists; Glutamic Acid; Glycine; Indoles; Kynurenic Acid; Protein Binding; Protein Conformation; Receptors, N-Methyl-D-Aspartate; Recombinant Fusion Proteins; Serine; Spodoptera

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