xanthosine 5'-triphosphate has been researched along with nad in 15 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (20.00) | 18.7374 |
| 1990's | 5 (33.33) | 18.2507 |
| 2000's | 5 (33.33) | 29.6817 |
| 2010's | 2 (13.33) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Heyde, E; Morrison, JF; Nagabhushanam, A; Vonarx, M | 1 |
| Hedstrom, L; Wang, CC | 1 |
| Ikegami, T; Natsumeda, Y; Weber, G; Yamada, Y | 1 |
| Natsumeda, Y; Weber, G; Yamada, Y; Yamaji, Y | 1 |
| Antonino, LC; Wu, JC | 1 |
| Pugh, ME; Skibo, EB | 1 |
| Hedstrom, L; Wang, W | 1 |
| Cahoon, M; Hedstrom, L; McMillan, FM; Petsko, GA; Ringe, D; White, A | 1 |
| Caron, PR; DeCenzo, MT; Futer, O; Livingston, DJ; Nimmesgern, E; Raybuck, SA; Sintchak, MD | 1 |
| Luecke, H; Prosise, GL | 1 |
| Berg, A; Boitz, JM; Dobie, F; Jardim, A | 1 |
| Hedstrom, L; Josephine, HR; Riera, TV; Wang, W | 1 |
| Anderson, WF; Binkowski, TA; Gollapalli, DR; Gornicki, P; Hedstrom, L; Jedrzejczak, R; Joachimiak, A; Kim, Y; Kuhn, ML; Mack, JC; Makowska-Grzyska, M; Maltseva, N; Mulligan, R; Wang, XK; Wilton, R; Wu, R; Zhang, R | 1 |
| Anthony, S; Ji, Y; Peterson, JR | 1 |
| Simon, MI; Slepak, VZ; Yu, B | 1 |
15 other study(ies) available for xanthosine 5'-triphosphate and nad
| Article | Year |
|---|---|
Studies on inosine monophosphate dehydrogenase. Steady state kinetics.
Topics: Enterobacter; Guanine Nucleotides; IMP Dehydrogenase; Ketone Oxidoreductases; Kinetics; Lithium; NAD; Nicotinic Acids; Osmolar Concentration; Potassium; Protein Binding; Ribonucleotides; Xanthine; Xanthines | 1976 |
Mycophenolic acid and thiazole adenine dinucleotide inhibition of Tritrichomonas foetus inosine 5'-monophosphate dehydrogenase: implications on enzyme mechanism.
Topics: Adenine Nucleotides; Animals; Binding Sites; Binding, Competitive; IMP Dehydrogenase; Isomerism; Ketone Oxidoreductases; Kinetics; Mycophenolic Acid; NAD; Ribonucleotides; Tritrichomonas; Xanthine | 1990 |
Kinetic properties of IMP dehydrogenase purified from rat hepatoma 3924A.
Topics: Animals; Dose-Response Relationship, Drug; IMP Dehydrogenase; Inosine Monophosphate; Ketone Oxidoreductases; Kinetics; Liver Neoplasms, Experimental; NAD; Rats; Ribonucleotides; Tumor Cells, Cultured; Xanthine | 1989 |
Two distinct target sites on IMP dehydrogenase in chemotherapy.
Topics: Adenine Nucleotides; Animals; Antineoplastic Agents; Drug Synergism; Guanosine Monophosphate; IMP Dehydrogenase; Inosine Monophosphate; Ketone Oxidoreductases; Liver Neoplasms, Experimental; NAD; Nucleotides; Rats; Ribonucleotides; Temperature; Time Factors; Tumor Cells, Cultured; Xanthine | 1989 |
Human IMP dehydrogenase catalyzes the dehalogenation of 2-fluoro- and 2-chloroinosine 5'-monophosphate in the absence of NAD.
Topics: Adenosine Deaminase; Binding, Competitive; Catalysis; Chromatography, High Pressure Liquid; Humans; IMP Dehydrogenase; Inosine Monophosphate; Kinetics; Magnetic Resonance Spectroscopy; NAD; Ribonucleotides; Spectrophotometry, Ultraviolet; Xanthine | 1994 |
Inosine monophosphate dehydrogenase from porcine (Sus scrofa domestica) thymus: purification and properties.
Topics: Adenosine Monophosphate; Amino Acids; Animals; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Guanosine Monophosphate; Hydrogen-Ion Concentration; IMP Dehydrogenase; Inosine Monophosphate; Molecular Weight; NAD; Ribonucleotides; Swine; Thymus Gland; Xanthine | 1993 |
Kinetic mechanism of human inosine 5'-monophosphate dehydrogenase type II: random addition of substrates and ordered release of products.
Topics: Humans; Hydrolysis; IMP Dehydrogenase; Inosine Monophosphate; Kinetics; Molecular Structure; NAD; Oxidation-Reduction; Ribonucleotides; Spectrometry, Fluorescence; Substrate Specificity; Xanthine | 1997 |
Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5'-monophosphate dehydrogenase: evidence of a substrate-induced hinged-lid motion by loop 6.
Topics: Amino Acid Sequence; Animals; Binding Sites; Borrelia burgdorferi Group; Catalytic Domain; Crystallography, X-Ray; Cysteine; Drug Design; Humans; IMP Dehydrogenase; Inosine Monophosphate; Models, Molecular; Molecular Sequence Data; Motion; NAD; Pliability; Protein Conformation; Ribonucleotides; Sequence Alignment; Solvents; Static Electricity; Structure-Activity Relationship; Sulfates; Xanthine | 2000 |
A mutational analysis of the active site of human type II inosine 5'-monophosphate dehydrogenase.
Topics: Binding Sites; Catalysis; Hydrolysis; IMP Dehydrogenase; Inosine Monophosphate; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; NAD; Ribonucleotides; Xanthine | 2002 |
Crystal structures of Tritrichomonasfoetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs: a structural basis for the random-in ordered-out kinetic mechanism.
Topics: Animals; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Enzyme Inhibitors; Humans; IMP Dehydrogenase; Inosine Monophosphate; Kinetics; Models, Molecular; Mycophenolic Acid; NAD; Protein Conformation; Ribavirin; Ribonucleotides; Tritrichomonas foetus; Xanthine | 2003 |
Kinetic characterization of inosine monophosphate dehydrogenase of Leishmania donovani.
Topics: Amino Acid Sequence; Animals; Enzyme Inhibitors; Escherichia coli; Guanosine Monophosphate; Inosine Monophosphate; Leishmania donovani; Microbodies; Microscopy, Confocal; Mycophenolic Acid; NAD; Peroxisome-Targeting Signal 1 Receptor; Phylogeny; Protein Binding; Protozoan Proteins; Receptors, Cytoplasmic and Nuclear; Recombinant Proteins; Ribonucleotides; Sequence Alignment; Subcellular Fractions; Substrate Specificity; Xanthine | 2007 |
A kinetic alignment of orthologous inosine-5'-monophosphate dehydrogenases.
Topics: Amino Acid Sequence; Animals; Binding Sites; Cryptosporidium parvum; Guanosine Monophosphate; IMP Dehydrogenase; Inosine Monophosphate; Kinetics; Models, Molecular; Molecular Conformation; Molecular Sequence Data; NAD; Protein Binding; Ribonucleotides; Xanthine | 2008 |
Bacillus anthracis inosine 5'-monophosphate dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate-, and product-bound complexes.
Topics: Amino Acid Sequence; Apoenzymes; Bacillus anthracis; Benzimidazoles; Catalytic Domain; Enzyme Inhibitors; IMP Dehydrogenase; Inosine Monophosphate; Models, Molecular; Molecular Sequence Data; Mycophenolic Acid; NAD; Protein Binding; Ribonucleotides; Triazoles; Xanthine | 2012 |
Use of Inosine Monophosphate Dehydrogenase Activity Assay to Determine the Specificity of PARP-1 Inhibitors.
Topics: Animals; Biological Assay; Humans; IMP Dehydrogenase; Inosine Monophosphate; NAD; Oxidation-Reduction; Poly (ADP-Ribose) Polymerase-1; Poly(ADP-ribose) Polymerase Inhibitors; Ribonucleotides; Xanthine | 2017 |
Characterization of a Goalpha mutant that binds xanthine nucleotides.
Topics: Amino Acid Sequence; Animals; Base Sequence; Binding Sites; COS Cells; GTP-Binding Proteins; Guanine Nucleotides; Kinetics; Macromolecular Substances; Mice; Mutagenesis, Site-Directed; NAD; Oligodeoxyribonucleotides; Point Mutation; Recombinant Proteins; Ribonucleotides; Substrate Specificity; Transfection; Virulence Factors, Bordetella | 1997 |