o-phosphohomoserine has been researched along with pyridoxal phosphate in 3 studies
| Studies (o-phosphohomoserine) | Trials (o-phosphohomoserine) | Recent Studies (post-2010) (o-phosphohomoserine) | Studies (pyridoxal phosphate) | Trials (pyridoxal phosphate) | Recent Studies (post-2010) (pyridoxal phosphate) |
|---|---|---|---|---|---|
| 19 | 0 | 3 | 6,511 | 140 | 860 |
| Protein | Taxonomy | o-phosphohomoserine (IC50) | pyridoxal phosphate (IC50) |
|---|---|---|---|
| P2X purinoceptor 1 | Homo sapiens (human) | 10 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (100.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Douce, R; Droux, M; Ravanel, S | 1 |
| Douce, R; Gakière, B; Job, D; Ravanel, S | 1 |
| Clausen, T; Huber, R; Laber, B; Messerschmidt, A; Steegborn, C; Streber, W | 1 |
3 other study(ies) available for o-phosphohomoserine and pyridoxal phosphate
| Article | Year |
|---|---|
Methionine biosynthesis in higher plants. I. Purification and characterization of cystathionine gamma-synthase from spinach chloroplasts.
Topics: Alkynes; Carbon-Oxygen Lyases; Carbon-Sulfur Lyases; Cell Compartmentation; Chloroplasts; Cystathionine; Glycine; Homocysteine; Homoserine; Kinetics; Lyases; Methionine; Molecular Weight; Pargyline; Plant Leaves; Protein Conformation; Pyridoxal Phosphate; Spectrophotometry; Spinacia oleracea | 1995 |
Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli.
Topics: Alkynes; Amino Acid Sequence; Arabidopsis; Binding Sites; Carbon-Oxygen Lyases; Cloning, Molecular; DNA, Complementary; Enzyme Inhibitors; Escherichia coli; Gene Expression; Glycine; Homoserine; Kinetics; Lysine; Macromolecular Substances; Methionine; Molecular Sequence Data; Pyridoxal Phosphate; Recombinant Proteins | 1998 |
The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity.
Topics: Amino Acid Sequence; Binding Sites; Carbon-Oxygen Lyases; Catalysis; Crystallization; Crystallography, X-Ray; Cysteine; Escherichia coli; Homoserine; Hydrogen Bonding; Hydrogen-Ion Concentration; Lyases; Models, Molecular; Molecular Sequence Data; Nicotiana; Plants, Toxic; Protein Structure, Secondary; Pyridoxal Phosphate; Substrate Specificity | 1999 |