Page last updated: 2024-08-16

ribavirin and xanthosine 5'-triphosphate

ribavirin has been researched along with xanthosine 5'-triphosphate in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Luecke, H; Prosise, GL	1
Guillén Schlippe, YV; Hedstrom, L; Riera, TV; Seyedsayamdost, MR	1

Other Studies

2 other study(ies) available for ribavirin and xanthosine 5'-triphosphate

Article	Year
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. Journal of molecular biology, 2003, Feb-14, Volume: 326, Issue:2 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
Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase reaction. Biochemistry, 2004, Apr-20, Volume: 43, Issue:15 Topics: Adenosine Diphosphate; Alanine; Amino Acid Substitution; Animals; Arginine; Binding Sites; Cattle; Conserved Sequence; Deuterium Exchange Measurement; Enzyme Inhibitors; Hydrolysis; IMP Dehydrogenase; Kinetics; Mutagenesis, Site-Directed; Mycophenolic Acid; Phenylalanine; Point Mutation; Protein Binding; Ribavirin; Ribonucleosides; Ribonucleotides; Solvents; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine	2004

Article

Year

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.

Journal of molecular biology, 2003, Feb-14, Volume: 326, Issue:2

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

Substitution of the conserved Arg-Tyr dyad selectively disrupts the hydrolysis phase of the IMP dehydrogenase reaction.

Biochemistry, 2004, Apr-20, Volume: 43, Issue:15

Topics: Adenosine Diphosphate; Alanine; Amino Acid Substitution; Animals; Arginine; Binding Sites; Cattle; Conserved Sequence; Deuterium Exchange Measurement; Enzyme Inhibitors; Hydrolysis; IMP Dehydrogenase; Kinetics; Mutagenesis, Site-Directed; Mycophenolic Acid; Phenylalanine; Point Mutation; Protein Binding; Ribavirin; Ribonucleosides; Ribonucleotides; Solvents; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine

2004