fluorescein-5-isothiocyanate has been researched along with acetyl phosphate 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 | 1 (25.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Beaugé, L; Berberián, G | 1 |
Daiho, T; Kanazawa, T; Yamagata, K | 1 |
Hayashi, Y; Kaya, S; Taniguchi, K; Tsuda, T; Yokoyama, T | 1 |
Champeil, P; Henao, F; Lacapere, JJ; McIntosh, DB | 1 |
4 other study(ies) available for fluorescein-5-isothiocyanate and acetyl phosphate
Article | Year |
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Phosphorylation of Na,K-ATPase by acetyl phosphate and inorganic phosphate. Sidedness of Na+, K+ and nucleotide interactions and related enzyme conformations.
Topics: Animals; Cell Membrane; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescence; Fluorescent Dyes; Kidney; Liposomes; Organophosphates; Phosphates; Phosphorylation; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Swine; Thiocyanates | 1991 |
Labeling of lysine 492 with pyridoxal 5'-phosphate in the sarcoplasmic reticulum Ca(2+)-ATPase. Lysine 492 residue is located outside the fluorescein 5-isothiocyanate-binding region in or near the ATP binding site.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Animals; Binding Sites; Calcium-Transporting ATPases; Chromatography, High Pressure Liquid; Fluorescein-5-isothiocyanate; Hydrolysis; Lysine; Molecular Sequence Data; Organophosphates; Peptide Mapping; Pyridoxal Phosphate; Rabbits; Sarcoplasmic Reticulum | 1993 |
ATP and acetyl phosphate induces molecular events near the ATP binding site and the membrane domain of Na+,K+-ATPase. The tetrameric nature of the enzyme.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Affinity Labels; Animals; Cell Membrane; Dogs; Fluorescein-5-isothiocyanate; Kidney; Kinetics; Macromolecular Substances; Magnesium; Models, Structural; Organophosphates; Pyridoxal Phosphate; Sodium; Sodium-Potassium-Exchanging ATPase; Spectrometry, Fluorescence; Swine; Time Factors | 1998 |
A remarkably stable phosphorylated form of Ca2+-ATPase prepared from Ca2+-loaded and fluorescein isothiocyanate-labeled sarcoplasmic reticulum vesicles.
Topics: Biological Transport, Active; Calcium; Calcium-Transporting ATPases; Cell Polarity; Cytosol; Enzyme Stability; Fluorescein-5-isothiocyanate; Fluorescence; Models, Chemical; Organophosphates; Phosphates; Phosphoproteins; Sarcoplasmic Reticulum; Spectrophotometry | 2001 |