5'-adenylyl (beta,gamma-methylene)diphosphonate has been researched along with fluorescein-5-isothiocyanate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (50.00) | 18.7374 |
| 1990's | 2 (50.00) | 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 |
|---|---|
| Entman, ML; Fisher, DJ; Tate, CA | 1 |
| Briggs, FN; Cable, MB; Feher, JJ | 1 |
| McIntosh, DB; Ross, DC | 1 |
| Askari, A; Huang, WH; Periyasamy, SM; Zolotarjova, N | 1 |
4 other study(ies) available for 5'-adenylyl (beta,gamma-methylene)diphosphonate and fluorescein-5-isothiocyanate
| Article | Year |
|---|---|
Inhibition of dicarboxylic anion transport by fluorescein isothiocyanate in skeletal sarcoplasmic reticulum.
Topics: Adenosine Triphosphate; Animals; Anions; Biological Transport, Active; Calcium; Calcium-Transporting ATPases; Dicarboxylic Acids; Fluorescein-5-isothiocyanate; Fluoresceins; In Vitro Techniques; Ion Channels; Oxalates; Oxalic Acid; Rabbits; Sarcoplasmic Reticulum; Thiocyanates | 1991 |
Mechanism of allosteric regulation of the Ca,Mg-ATPase of sarcoplasmic reticulum: studies with 5'-adenylyl methylenediphosphate.
Topics: Adenosine Triphosphate; Allosteric Regulation; Animals; Ca(2+) Mg(2+)-ATPase; Calcium-Transporting ATPases; Fluorescein-5-isothiocyanate; Fluoresceins; Fluorescent Dyes; Kinetics; Mathematics; Mice; Muscles; Protein Binding; Sarcoplasmic Reticulum; Thiocyanates | 1985 |
Intramolecular cross-linking of domains at the active site links A1 and B subfragments of the Ca2+-ATPase of sarcoplasmic reticulum.
Topics: Adenosine Triphosphate; Animals; Binding Sites; Calcium-Transporting ATPases; Electrophoresis, Polyacrylamide Gel; Fluorescein-5-isothiocyanate; Fluoresceins; Glutaral; Lysine; Macromolecular Substances; Mannose; Molecular Weight; Nitrophenols; Organophosphorus Compounds; Peptide Fragments; Phosphorylation; Rabbits; Sarcoplasmic Reticulum; Thiocyanates; Trypsin; Vanadates; Vanadium | 1987 |
Functional coupling of phosphorylation and nucleotide binding sites in the proteolytic fragments of Na+/K(+)-ATPase.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Amino Acid Sequence; Animals; Binding Sites; Biological Transport; Dogs; Fluorescein-5-isothiocyanate; Hydrolysis; Kidney Medulla; Molecular Sequence Data; Peptide Fragments; Phosphorylation; Sodium-Potassium-Exchanging ATPase | 1995 |