xanthosine 5'-triphosphate and asparagine

xanthosine 5'-triphosphate has been researched along with asparagine 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
Munagala, NR; Wang, CC	1
Fromm, HJ; Honzatko, RB; Kang, C; Sun, N	1

Other Studies

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

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
Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphate. The Journal of biological chemistry, 1994, Sep-30, Volume: 269, Issue:39 Topics: Adenylosuccinate Synthase; Amino Acid Sequence; Asparagine; Aspartic Acid; Base Sequence; Circular Dichroism; DNA, Complementary; Escherichia coli; GTP-Binding Proteins; Guanosine Triphosphate; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Ribonucleotides; Substrate Specificity	1994

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

Replacement of Asp333 with Asn by site-directed mutagenesis changes the substrate specificity of Escherichia coli adenylosuccinate synthetase from guanosine 5'-triphosphate to xanthosine 5'-triphosphate.

The Journal of biological chemistry, 1994, Sep-30, Volume: 269, Issue:39

Topics: Adenylosuccinate Synthase; Amino Acid Sequence; Asparagine; Aspartic Acid; Base Sequence; Circular Dichroism; DNA, Complementary; Escherichia coli; GTP-Binding Proteins; Guanosine Triphosphate; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Ribonucleotides; Substrate Specificity

1994