alpha,beta-methyleneadenosine 5'-triphosphate has been researched along with lysine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| McIntosh, DB; Ross, DC | 1 |
| Harris, TK; Massiah, MA; Mildvan, AS; Wu, G | 1 |
| Brick, P; Desogus, G; Onesti, S; Todone, F | 1 |
| Fischer, W; Franke, H; Gröger-Arndt, H; Illes, P; Kullnick, Y; Mager, PP; Wirkner, K; Zadori, Z | 1 |
4 other study(ies) available for alpha,beta-methyleneadenosine 5'-triphosphate and lysine
| Article | Year |
|---|---|
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 |
Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase.
Topics: Adenosine Triphosphate; Aspartic Acid; Bacterial Proteins; Binding, Competitive; Catalysis; Chlorides; Conserved Sequence; DNA Mutational Analysis; Escherichia coli Proteins; Glutamic Acid; Glutamine; Kinetics; Lysine; Magnesium; Magnesium Chloride; Manganese; Manganese Compounds; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Phosphoric Monoester Hydrolases; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Protons; Pyrophosphatases; Recombinant Proteins; Solvents | 2000 |
Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Amino Acyl-tRNA Synthetases; Catalytic Domain; Crystallography, X-Ray; Escherichia coli; Ligands; Lysine; Lysine-tRNA Ligase; Models, Molecular; Molecular Sequence Data; Protein Conformation; Recombinant Proteins; Sequence Homology, Amino Acid; Static Electricity | 2000 |
Conserved lysin and arginin residues in the extracellular loop of P2X(3) receptors are involved in agonist binding.
Topics: Adenosine Triphosphate; Arginine; Binding Sites; Calcium; Cell Line; Cell Membrane; Computational Biology; Humans; Lysine; Models, Molecular; Mutation; Protein Structure, Tertiary; Purinergic P2 Receptor Agonists; Purinergic P2 Receptor Antagonists; Receptors, Purinergic P2; Receptors, Purinergic P2X3; Transfection | 2007 |