adenosine monophosphate has been researched along with salicylates in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 6 (75.00) | 18.7374 |
| 1990's | 1 (12.50) | 18.2507 |
| 2000's | 1 (12.50) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Avramovic-Zikic, O; Brooks, D; Busby, SJ; Griffiths, JR; Radda, GK | 1 |
| Marcus, F | 1 |
| Beliaeva, NF; Nikulin, IR | 1 |
| Brooks, DJ; Busby, SJ; Radda, GK | 1 |
| Belfield, A; Ellis, G; Goldberg, DM | 1 |
| Davidson, ED; Killenberg, PG; Webster, LT | 1 |
| François, J; Hers, HG; Van Schaftingen, E | 1 |
| Gomez-Fernández, JC; Guerrero, JR; Teruel, JA; Velasco-Guillén, I | 1 |
8 other study(ies) available for adenosine monophosphate and salicylates
| Article | Year |
|---|---|
The interaction of ligands with chemically modified phosphorylase b.
Topics: Adenosine Monophosphate; Animals; Azoles; Binding Sites; Electron Spin Resonance Spectroscopy; Glycogen; Iodoacetamide; Iodoacetates; Ligands; Light; Muscles; Phosphorylases; Protein Binding; Protein Conformation; Rabbits; Salicylates; Scattering, Radiation; Spectrometry, Fluorescence; Spin Labels; Tetrazoles | 1976 |
Interaction of salicylate at the AMP site of fructose 1,6-bisphosphatase.
Topics: Adenosine Monophosphate; Allosteric Site; Animals; Binding Sites; Fructose-Bisphosphatase; Kidney; Kinetics; Protein Binding; Pyridoxal Phosphate; Salicylates; Swine | 1976 |
[The allosteric nature of substrate inhibition of rabbit skeletal muscle fructose-1,6-diphosphatase].
Topics: Adenosine Monophosphate; Allosteric Regulation; Animals; Catalysis; Dithionitrobenzoic Acid; Edetic Acid; Fructose-Bisphosphatase; Kinetics; Magnesium; Muscles; Pyridoxal Phosphate; Rabbits; Salicylates | 1990 |
Studies on ligand binding during the conversion of phosphorylase b to phosphorylase a.
Topics: Adenosine Monophosphate; Enzyme Activation; Glucosephosphates; Iodoacetates; Ligands; Macromolecular Substances; Phosphorylase Kinase; Phosphorylases; Protein Binding; Salicylates; Spectrometry, Fluorescence | 1974 |
Human prostatic acid phosphatase. Studies on the mechanism of catalysis and on the nature of inhibition by purines and pyrimidines.
Topics: Acid Phosphatase; Adenosine Monophosphate; Benzoates; Cold Temperature; Colorimetry; Humans; Hydrolysis; Kinetics; Male; Methods; Nitrophenols; Phosphoric Acids; Prostate; Purines; Pyrimidines; Salicylates; Time Factors | 1972 |
Evidence for a medium-chain fatty acid: coenzyme A ligase (adenosine monophosphate) that activates salicylate.
Topics: Adenosine Monophosphate; Aminosalicylic Acids; Animals; Benzoates; Caproates; Carbon Isotopes; Catalysis; Cattle; Chemical Precipitation; Chromatography, Gel; Coenzyme A; Dialysis; Electrophoresis, Disc; Fatty Acids; Ligases; Methods; Mitochondria, Liver; ortho-Aminobenzoates; Quaternary Ammonium Compounds; Salicylates; Sulfates | 1971 |
On the mechanism of inhibition of neutral liver fructose 1,6-bisphosphatase by fructose 2,6-bisphosphate.
Topics: Adenosine Monophosphate; Animals; Benzenesulfonates; Binding Sites; Fructose-Bisphosphatase; Fructosediphosphates; Hexosediphosphates; Hydrogen-Ion Concentration; Lithium; Liver; Magnesium; Rats; Salicylates; Temperature | 1983 |
Labeling the Ca2+-ATPase of skeletal muscle sarcoplasmic reticulum with maleimidylsalicylic acid.
Topics: Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphatases; Adenosine Triphosphate; Animals; Aspartic Acid; Binding Sites; Calcium-Transporting ATPases; Catalysis; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Enzyme Inhibitors; Ethylmaleimide; Fluorescein-5-isothiocyanate; Fluorescent Dyes; Kinetics; Maleimides; Muscle, Skeletal; Phosphorylation; Protein Binding; Salicylates; Sarcoplasmic Reticulum; Spectrometry, Fluorescence; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Time Factors; Trypsin | 2000 |