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)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's6 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Hua, S; Inesi, G; Lewis, D; Ma, H; Toyoshima, C1
Andersson, KE; Pandita, RK1
Dong, K; Hebert, SC; MacGregor, GG; Tang, L1
Amler, E; Ettrich, R; Kubala, M; Kutý, M; Lánský, Z; Plásek, J; Schoner, W; Teisinger, J1
Fischer, W; Franke, H; Gröger-Arndt, H; Illes, P; Kullnick, Y; Mager, PP; Wirkner, K; Zadori, Z1
Lushington, GH; Mou, TC; Pinto, C; Richter, M; Seifert, R; Suryanarayana, S1

Other Studies

6 other study(ies) available for arginine and 2',3'-o-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate

ArticleYear
Functional role of "N" (nucleotide) and "P" (phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase.
    Biochemistry, 2002, Feb-19, Volume: 41, Issue:7

    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.
    The Journal of urology, 2002, Volume: 168, Issue:3

    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.
    The Journal of biological chemistry, 2002, Dec-20, Volume: 277, Issue:51

    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.
    Biochemistry, 2004, Jul-06, Volume: 43, Issue:26

    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.
    European journal of pharmacology, 2007, Dec-08, Volume: 576, Issue:1-3

    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.
    Neuroscience letters, 2009, Dec-18, Volume: 467, Issue:1

    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
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