eosine yellowish-(ys) has been researched along with 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate in 1 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Amler, E; Ettrich, R; Hofbauerová, K; Krumscheid, R; Lánský, Z; Linnertz, H; Schoner, W; Sovová, Z; Susánková, K; Teisinger, J | 1 |
1 other study(ies) available for eosine yellowish-(ys) and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
| Article | Year |
|---|---|
The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site.
Topics: 4-Nitrophenylphosphatase; Adenosine Triphosphate; Amino Acid Sequence; Animals; Binding Sites; Cytoplasm; Enzyme Stability; Eosine Yellowish-(YS); Fluorescent Dyes; Glutathione Transferase; Kidney; Mice; Molecular Sequence Data; Mutation; Phosphorylation; Protein Binding; Protein Structure, Tertiary; Protein Tyrosine Phosphatases; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Sodium-Potassium-Exchanging ATPase; Structure-Activity Relationship; Substrate Specificity; Swine | 2004 |