2-phosphoglycerate has been researched along with d-tartronic semialdehyde phosphate in 2 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (50.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Laughlin, LT; Poyner, RR; Reed, GH; Sowa, GA | 1 |
Brewer, JM; Chai, G; Lebioda, L; Lovelace, LL; Qin, J | 1 |
2 other study(ies) available for 2-phosphoglycerate and d-tartronic semialdehyde phosphate
Article | Year |
---|---|
Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants.
Topics: Base Sequence; Binding Sites; Catalysis; Glyceric Acids; Hydrolysis; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphoenolpyruvate; Phosphopyruvate Hydratase; Recombinant Proteins; Substrate Specificity; Tartronates; Yeasts | 1996 |
Structures of asymmetric complexes of human neuron specific enolase with resolved substrate and product and an analogous complex with two inhibitors indicate subunit interaction and inhibitor cooperativity.
Topics: Binding, Competitive; Crystallography, X-Ray; Enzyme Inhibitors; Glyceric Acids; Humans; Kinetics; Models, Molecular; Molecular Structure; Phosphoenolpyruvate; Phosphopyruvate Hydratase; Protein Binding; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein Subunits; Recombinant Proteins; Substrate Specificity; Tartronates | 2012 |