lysine has been researched along with erythrosine isothiocyanate in 2 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (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 |
|---|---|
| Huang, S; Negash, S; Squier, TC | 1 |
| Huang, S; Squier, TC | 1 |
2 other study(ies) available for lysine and erythrosine isothiocyanate
| Article | Year |
|---|---|
Erythrosin isothiocyanate selectively labels lysine464 within an ATP-protectable binding site on the Ca-ATPase in skeletal sarcoplasmic reticulum membranes.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Calcium-Transporting ATPases; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Enzyme Activation; Enzyme Stability; Erythrosine; Intracellular Membranes; Isothiocyanates; Lysine; Mass Spectrometry; Molecular Sequence Data; Muscle Fibers, Fast-Twitch; Peptides; Phosphoproteins; Phosphorylation; Rabbits; Sarcoplasmic Reticulum; Solubility | 1998 |
Enhanced rotational dynamics of the phosphorylation domain of the Ca-ATPase upon calcium activation.
Topics: Animals; Calcium; Calcium-Transporting ATPases; Catalysis; Energy Transfer; Erythrosine; Fluorescence Polarization; Intracellular Membranes; Isothiocyanates; Luminescent Measurements; Lysine; Membrane Lipids; Peptide Fragments; Phosphorylation; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum; Time Factors; Viscosity | 1998 |