arginine and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
arginine has been researched along with 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate in 6 studies
Research
Studies (6)
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 6 (100.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors
Authors | Studies |
---|---|
Hua, S; Inesi, G; Lewis, D; Ma, H; Toyoshima, C | 1 |
Andersson, KE; Pandita, RK | 1 |
Dong, K; Hebert, SC; MacGregor, GG; Tang, L | 1 |
Amler, E; Ettrich, R; Kubala, M; Kutý, M; Lánský, Z; Plásek, J; Schoner, W; Teisinger, J | 1 |
Fischer, W; Franke, H; Gröger-Arndt, H; Illes, P; Kullnick, Y; Mager, PP; Wirkner, K; Zadori, Z | 1 |
Lushington, GH; Mou, TC; Pinto, C; Richter, M; Seifert, R; Suryanarayana, S | 1 |
Other Studies
6 other study(ies) available for arginine and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate
Article | Year |
---|---|
Functional role of "N" (nucleotide) and "P" (phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase.
Topics: 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Adenosine Monophosphate; Adenosine Triphosphate; Alanine; Amino Acid Substitution; Animals; Arginine; Binding Sites; Calcium-Transporting ATPases; COS Cells; Cross-Linking Reagents; Endopeptidase K; Hydrolysis; Lysine; Phosphorylation; Photosensitizing Agents; Protein Structure, Tertiary; Rabbits; Sarcoplasmic Reticulum; Sarcoplasmic Reticulum Calcium-Transporting ATPases; Vanadates | 2002 |
Intravesical adenosine triphosphate stimulates the micturition reflex in awake, freely moving rats.
Topics: Adenosine Triphosphate; Administration, Intravesical; Amides; Animals; Arginine; Benzamides; Benzophenones; Female; Hexamethonium; Nerve Fibers; Neurons, Afferent; Piperidines; Purinergic Antagonists; Rats; Rats, Sprague-Dawley; Receptors, Neurokinin-2; Reflex; Urinary Bladder; Urination; Urodynamics | 2002 |
Localization of the ATP/phosphatidylinositol 4,5 diphosphate-binding site to a 39-amino acid region of the carboxyl terminus of the ATP-regulated K+ channel Kir1.1.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Arginine; Binding Sites; Binding, Competitive; Carrier Proteins; Cytosol; DNA; Dose-Response Relationship, Drug; Gene Deletion; Kinetics; Light; Maltose-Binding Proteins; Models, Chemical; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Phosphatidylinositol 4,5-Diphosphate; Potassium Channels; Potassium Channels, Inwardly Rectifying; Protein Binding; Protein Structure, Tertiary; Rats; Recombinant Fusion Proteins; Scattering, Radiation; Sequence Homology, Amino Acid | 2002 |
The hydrogen bonds between Arg423 and Glu472 and other key residues, Asp443, Ser477, and Pro489, are responsible for the formation and a different positioning of TNP-ATP and ATP within the nucleotide-binding site of Na(+)/K(+)-ATPase.
Topics: Adenosine; Adenosine Triphosphate; Amino Acid Sequence; Amino Acids; Animals; Arginine; Aspartic Acid; Binding Sites; Crystallography, X-Ray; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescent Dyes; Genetic Vectors; Glutamic Acid; Glutathione Transferase; Hydrogen; Hydrogen Bonding; Hydrolysis; Kinetics; Ligands; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular Sequence Data; Mutation; Nucleotides; Point Mutation; Proline; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins; Sequence Homology, Amino Acid; Serine; Sodium-Potassium-Exchanging ATPase; Software; Spectrophotometry; Temperature | 2004 |
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 |
The C1 homodimer of adenylyl cyclase binds nucleotides with high affinity but possesses exceedingly low catalytic activity.
Topics: Adenosine Triphosphate; Adenylyl Cyclase Inhibitors; Adenylyl Cyclases; Arginine; Enzyme Inhibitors; Fluorescence; Fluorescence Resonance Energy Transfer; Guanosine Triphosphate; Histidine; Manganese; Models, Chemical; Models, Molecular; Nucleotides; Protein Multimerization | 2009 |