tryptophan has been researched along with 3-phosphoglycerate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brochon, JC; Desmadril, M; Mouawad, L; Perahia, D; Yon, JM | 1 |
| Brindle, KM; Fulton, AM; Williams, SP | 1 |
| Cheung, CW; Mas, MT | 1 |
| Ballicora, MA; Falaschetti, CA; Figueroa, CM; Iglesias, AA; Kuhn, ML; Olsen, KW; Solamen, L | 1 |
4 other study(ies) available for tryptophan and 3-phosphoglycerate
| Article | Year |
|---|---|
The effects of ligands on the conformation of phosphoglycerate kinase: fluorescence anisotropy decay and theoretical interpretation.
Topics: Adenosine Diphosphate; Animals; Birefringence; Fluorescence Polarization; Glyceric Acids; Glycolysis; Horses; Isomerism; Kinetics; Ligands; Macromolecular Substances; Phosphoglycerate Kinase; Protein Conformation; Spectrophotometry, Ultraviolet; Temperature; Tryptophan | 1990 |
Estimation of the intracellular free ADP concentration by 19F NMR studies of fluorine-labeled yeast phosphoglycerate kinase in vivo.
Topics: Adenine Nucleotides; Adenosine Diphosphate; Cytosol; Diphosphoglyceric Acids; Enzyme Induction; Fluorine Radioisotopes; Glyceric Acids; Histocytochemistry; Hydrogen-Ion Concentration; Ligands; Magnetic Resonance Spectroscopy; Phosphoglycerate Kinase; Recombinant Proteins; Saccharomyces cerevisiae; Transformation, Genetic; Tryptophan | 1993 |
Substrate-induced conformational changes in yeast 3-phosphoglycerate kinase monitored by fluorescence of single tryptophan probes.
Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Binding Sites; Catalysis; Diphosphoglyceric Acids; Fluorescence; Fluorescent Dyes; Glyceric Acids; Magnesium; Mutagenesis; Phosphoglycerate Kinase; Point Mutation; Protein Conformation; Protein Structure, Tertiary; Saccharomyces cerevisiae; Spectrometry, Fluorescence; Titrimetry; Tryptophan | 1996 |
Unraveling the activation mechanism of the potato tuber ADP-glucose pyrophosphorylase.
Topics: Amino Acid Sequence; Enzyme Activation; Glucose-1-Phosphate Adenylyltransferase; Glyceric Acids; Kinetics; Molecular Dynamics Simulation; Molecular Sequence Data; Mutant Proteins; Mutation; Plant Tubers; Protein Subunits; Solanum tuberosum; Structure-Activity Relationship; Substrate Specificity; Tryptophan | 2013 |