xanthosine 5'-triphosphate and tyrosine

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

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Munagala, NR; Wang, CC	1
Guillén Schlippe, YV; Hedstrom, L; Riera, TV; Seyedsayamdost, MR	1

Other Studies

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

Article	Year
Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein. Biochemistry, 1998, Nov-24, Volume: 37, Issue:47 Topics: Adenine Phosphoribosyltransferase; Amino Acid Substitution; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Enzyme Activation; Glutamic Acid; Guanine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Isoleucine; Lysine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Purines; Ribonucleotides; Serine; Structure-Activity Relationship; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine	1998
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

Altering the purine specificity of hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus by structure-based point mutations in the enzyme protein.

Biochemistry, 1998, Nov-24, Volume: 37, Issue:47

Topics: Adenine Phosphoribosyltransferase; Amino Acid Substitution; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Enzyme Activation; Glutamic Acid; Guanine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Isoleucine; Lysine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Purines; Ribonucleotides; Serine; Structure-Activity Relationship; Substrate Specificity; Tritrichomonas foetus; Tyrosine; Xanthine

1998

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