arginine and 2'-deoxyuridylic acid

arginine has been researched along with 2'-deoxyuridylic acid in 7 studies

Research

Studies (7)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (42.86)18.2507
2000's4 (57.14)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cisneros, RJ; Deng, WL; Dunlap, RB; Johnson, LF; Zhang, HC1
Fauman, EB; Finer-Moore, JS; Morse, RJ; Santi, DV; Stroud, RM1
Changchien, L; Maley, F; Montfort, WR; Strop, P1
Finer-Moore, J; Kawase, S; Morse, RJ; Santi, DV; Stroud, RM1
Lee, TT; Liu, Y; Santi, DV; Stroud, RM; Variath, P1
Cieśla, J; Gołos, B; Jagielska, E; Płucienniczak, A; Rode, W; Wałajtys-Rode, E1
Changchien, L; Maley, F; Montfort, WR; Sotelo-Mundo, RR1

Other Studies

7 other study(ies) available for arginine and 2'-deoxyuridylic acid

ArticleYear
Site-directed mutagenesis of mouse thymidylate synthase: alteration of Arg44 to Val44 in a conserved loop guarding the active site has striking effects on catalysis and nucleotide binding.
    Biochemical and biophysical research communications, 1990, Mar-30, Volume: 167, Issue:3

    Topics: Amino Acid Sequence; Animals; Arginine; Base Sequence; Binding Sites; Catalysis; Deoxyuracil Nucleotides; Fluorodeoxyuridylate; Hydrogen Bonding; Kinetics; Mice; Molecular Sequence Data; Mutation; Oligonucleotide Probes; Plasmids; Protein Conformation; Thymidylate Synthase; Valine

1990
Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
    Protein engineering, 1996, Volume: 9, Issue:1

    Topics: Arginine; Binding Sites; Catalysis; Crystallography, X-Ray; Deoxyuracil Nucleotides; Escherichia coli; Glutamic Acid; Hydrogen Bonding; Kinetics; Lacticaseibacillus casei; Models, Molecular; Molecular Structure; Mutagenesis; Phosphates; Protein Binding; Protein Conformation; Protein Engineering; Recombinant Proteins; Thymidylate Synthase

1996
Crystal structures of a marginally active thymidylate synthase mutant, Arg 126-->Glu.
    Protein science : a publication of the Protein Society, 1997, Volume: 6, Issue:12

    Topics: Antineoplastic Agents; Arginine; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Deoxyuracil Nucleotides; Dimerization; Folic Acid; Folic Acid Antagonists; Glutamic Acid; Hydrogen Bonding; Kinetics; Models, Molecular; Molecular Structure; Mutation; Phosphates; Quinazolines; Thymidylate Synthase

1997
Energetic contributions of four arginines to phosphate-binding in thymidylate synthase are more than additive and depend on optimization of "effective charge balance".
    Biochemistry, 2000, Feb-08, Volume: 39, Issue:5

    Topics: Arginine; Binding Sites; Crystallography, X-Ray; Deoxyuracil Nucleotides; Hydrogen Bonding; Kinetics; Lacticaseibacillus casei; Mutagenesis, Site-Directed; Phosphates; Static Electricity; Structure-Activity Relationship; Thermodynamics; Threonine; Thymidylate Synthase

2000
Effects of subunit occupancy on partitioning of an intermediate in thymidylate synthase mutants.
    Biochemistry, 2000, Mar-14, Volume: 39, Issue:10

    Topics: Alanine; Arginine; Catalysis; Deoxyuracil Nucleotides; Escherichia coli; Glycine; Kinetics; Lacticaseibacillus casei; Models, Chemical; Mutagenesis, Site-Directed; Peptide Fragments; Tetrahydrofolates; Thymidine Monophosphate; Thymidylate Synthase; Valine

2000
The effect of Arg209 to Lys mutation in mouse thymidylate synthase.
    Acta biochimica Polonica, 2002, Volume: 49, Issue:3

    Topics: Amino Acid Substitution; Animals; Arginine; Catalysis; Deoxyuracil Nucleotides; Enzyme Induction; Escherichia coli; Kinetics; Lacticaseibacillus casei; Leukemia L1210; Lysine; Mice; Recombinant Proteins; Solubility; Thymidylate Synthase; Tumor Cells, Cultured

2002
Crystal structures of thymidylate synthase mutant R166Q: structural basis for the nearly complete loss of catalytic activity.
    Journal of biochemical and molecular toxicology, 2006, Volume: 20, Issue:2

    Topics: Amino Acid Substitution; Arginine; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Deoxyuracil Nucleotides; Dimerization; Escherichia coli; Folic Acid; Folic Acid Antagonists; Hydrogen Bonding; Kinetics; Ligands; Models, Molecular; Molecular Structure; Protein Binding; Protein Conformation; Recombinant Proteins; Thymidine Monophosphate; Thymidylate Synthase

2006