arginine and mizoribine

arginine has been researched along with mizoribine 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
Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J	1
Guillén Schlippe, YV; Hedstrom, L; Riera, TV; Seyedsayamdost, MR	1

Other Studies

2 other study(ies) available for arginine and mizoribine

Article	Year
Chemical genetics reveals a complex functional ground state of neural stem cells. Nature chemical biology, 2007, Volume: 3, Issue:5 Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells	2007
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

Chemical genetics reveals a complex functional ground state of neural stem cells.

Nature chemical biology, 2007, Volume: 3, Issue:5

Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells

2007

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