tyrosine and cytidine triphosphate

tyrosine has been researched along with cytidine triphosphate in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19904 (50.00)18.7374
1990's2 (25.00)18.2507
2000's2 (25.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Evans, DR; Landfear, SM; Lipscomb, WN1
Hsuanyu, YC; Kantrowitz, ER; Middleton, SA; Wedler, FC1
Schachman, HK; Wacks, DB1
Browne, DT; Moore, AC1
Blinder, L; Chong, AS; Gong, H; Shen, J; Williams, JW; Xu, X1
Kemp, RG; Wang, X1
Chatterjee, DK; Eisenhauer, BM; Gotte, M; Hecht, SM; Klarmann, GJ; Le Grice, SF; Pata, JD; Zhang, Y1
Cornell, RB; Ding, Z; Johnson, J; Lee, J; Paetzel, M1

Other Studies

8 other study(ies) available for tyrosine and cytidine triphosphate

ArticleYear
Functional modifications of aspartate transcarbamylase induced by nitration with tetranitromethane.
    The Journal of biological chemistry, 1978, Jun-10, Volume: 253, Issue:11

    Topics: Aspartate Carbamoyltransferase; Cytidine Triphosphate; Escherichia coli; Kinetics; Methane; Tetranitromethane; Tyrosine

1978
Regulatory behavior of Escherichia coli aspartate transcarbamylase altered by site-specific mutation of Tyr240----Phe in the catalytic chain.
    The Journal of biological chemistry, 1989, Oct-15, Volume: 264, Issue:29

    Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Catalysis; Computer Simulation; Cytidine Triphosphate; Enzyme Activation; Escherichia coli; Kinetics; Mutation; Phenylalanine; Phosphates; Structure-Activity Relationship; Thermodynamics; Tyrosine

1989
19F nuclear magnetic resonance studies of fluorotyrosine-labeled aspartate transcarbamoylase. Properties of the enzyme and its catalytic and regulatory subunits.
    The Journal of biological chemistry, 1985, Sep-25, Volume: 260, Issue:21

    Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Cytidine Triphosphate; Magnetic Resonance Spectroscopy; Phosphonoacetic Acid; Tyrosine

1985
Binding of regulatory nucleotides to aspartate transcarbamylase: nuclear magnetic resonance studies of selectively enriched carbon-13 regulatory subunit.
    Biochemistry, 1980, Dec-09, Volume: 19, Issue:25

    Topics: Adenosine Triphosphate; Aspartate Carbamoyltransferase; Binding Sites; Cytidine Triphosphate; Cytosine Nucleotides; Enzyme Activation; Escherichia coli; Histidine; Macromolecular Substances; Magnetic Resonance Spectroscopy; Phenylalanine; Protein Binding; Tyrosine

1980
Control of lymphoproliferative and autoimmune disease in MRL-lpr/lpr mice by brequinar sodium: mechanisms of action.
    The Journal of pharmacology and experimental therapeutics, 1997, Volume: 283, Issue:2

    Topics: Animals; Autoantibodies; Autoimmune Diseases; Biphenyl Compounds; Cytidine Triphosphate; Female; Immunosuppressive Agents; Isoxazoles; Leflunomide; Lymphoproliferative Disorders; Mice; Mice, Inbred BALB C; Mice, Inbred MRL lpr; Phosphorylation; Tyrosine; Uridine; Uridine Triphosphate

1997
Identification of residues of Escherichia coli phosphofructokinase that contribute to nucleotide binding and specificity.
    Biochemistry, 1999, Apr-06, Volume: 38, Issue:14

    Topics: Adenine Nucleotides; Adenosine Triphosphate; Amino Acids; Arginine; Binding Sites; Cytidine Triphosphate; Escherichia coli; Guanosine Triphosphate; Inosine Triphosphate; Models, Molecular; Mutagenesis, Site-Directed; Phenylalanine; Phosphofructokinase-1; Substrate Specificity; Tyrosine; Uridine Triphosphate

1999
Investigating the "steric gate" of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase by targeted insertion of unnatural amino acids.
    Biochemistry, 2007, Feb-27, Volume: 46, Issue:8

    Topics: Amino Acid Substitution; Binding Sites; Cell-Free System; Cytidine Triphosphate; Deoxycytosine Nucleotides; Dideoxynucleotides; DNA; Escherichia coli; HIV Reverse Transcriptase; HIV-1; Hydrogen Bonding; Kinetics; Lamivudine; Models, Molecular; Protein Biosynthesis; Protein Engineering; Reverse Transcriptase Inhibitors; Transcription, Genetic; Tyrosine

2007
Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold.
    The Journal of biological chemistry, 2009, Nov-27, Volume: 284, Issue:48

    Topics: Animals; Catalysis; Catalytic Domain; Choline-Phosphate Cytidylyltransferase; Crystallization; Crystallography, X-Ray; Cytidine Triphosphate; Histidine; Kinetics; Models, Molecular; Mutation; Nucleotidyltransferases; Phosphorylcholine; Protein Binding; Protein Multimerization; Protein Structure, Tertiary; Rats; Recombinant Proteins; Structure-Activity Relationship; Substrate Specificity; Tyrosine

2009