xanthosine 5'-triphosphate and lysine

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

Research

Studies (2)

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

Authors

Authors	Studies
Chin, MS; Munagala, NR; Wang, CC	1
Munagala, NR; Wang, CC	1

Other Studies

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

Article	Year
Steady-state kinetics of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus: the role of threonine-47. Biochemistry, 1998, Mar-24, Volume: 37, Issue:12 Topics: Amino Acid Substitution; Animals; Binding, Competitive; Guanosine Monophosphate; Hypoxanthine Phosphoribosyltransferase; Inosine Monophosphate; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Ribonucleotides; Threonine; Tritrichomonas foetus; Xanthine	1998
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

Article

Year

Steady-state kinetics of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from Tritrichomonas foetus: the role of threonine-47.

Biochemistry, 1998, Mar-24, Volume: 37, Issue:12

Topics: Amino Acid Substitution; Animals; Binding, Competitive; Guanosine Monophosphate; Hypoxanthine Phosphoribosyltransferase; Inosine Monophosphate; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Ribonucleotides; Threonine; Tritrichomonas foetus; Xanthine

1998

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