Compounds > phosphonoacetic acid

phosphonoacetic acid and tyrosine

phosphonoacetic acid has been researched along with tyrosine in 6 studies

Research

Studies (6)

TimeframeStudies, this research(%)All Research%
pre-19903 (50.00)18.7374
1990's2 (33.33)18.2507
2000's1 (16.67)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Coen, DM; Hwang, CB; Ruffner, KL1
Hoover, TA; Wales, ME; Wild, JR1
Schachman, HK; Wacks, DB2
Gao, L; Hwang, CB; Hwang, YT; Smith, JF1
Brochon, JC; Cunin, R; Fetler, L; Hervé, G; Tauc, P1

Other Studies

6 other study(ies) available for phosphonoacetic acid and tyrosine

ArticleYear
A point mutation within a distinct conserved region of the herpes simplex virus DNA polymerase gene confers drug resistance.
    Journal of virology, 1992, Volume: 66, Issue:3

    Topics: Acyclovir; Amino Acid Sequence; DNA-Directed DNA Polymerase; Drug Resistance, Microbial; Foscarnet; Genes, Viral; Molecular Sequence Data; Mutation; Phosphonoacetic Acid; Sequence Alignment; Simplexvirus; Tyrosine; Viral Structural Proteins

1992
Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme.
    The Journal of biological chemistry, 1988, May-05, Volume: 263, Issue:13

    Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Escherichia coli; Hydroxymercuribenzoates; Kinetics; Mutation; Phosphonoacetic Acid; Structure-Activity Relationship; Tyrosine; X-Ray Diffraction

1988
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
19F nuclear magnetic resonance studies of communication between catalytic and regulatory subunits in aspartate transcarbamoylase.
    The Journal of biological chemistry, 1985, Sep-25, Volume: 260, Issue:21

    Topics: Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Kinetics; Magnetic Resonance Spectroscopy; Phosphonoacetic Acid; Protein Conformation; Tyrosine

1985
Mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene can confer altered drug sensitivities.
    Virology, 1998, Jul-05, Volume: 246, Issue:2

    Topics: Amino Acid Sequence; Animals; Antiviral Agents; Aphidicolin; Binding Sites; Chlorocebus aethiops; DNA-Directed DNA Polymerase; DNA, Viral; Drug Resistance, Microbial; Enzyme Inhibitors; Exodeoxyribonuclease V; Exodeoxyribonucleases; Genes, pol; Genes, Viral; Herpesvirus 1, Human; Histidine; Humans; Molecular Sequence Data; Mutation; Nucleosides; Open Reading Frames; Phosphonoacetic Acid; Protein Structure, Secondary; Recombination, Genetic; Tyrosine; Vero Cells; Viral Proteins

1998
Tryptophan residues at subunit interfaces used as fluorescence probes to investigate homotropic and heterotropic regulation of aspartate transcarbamylase.
    Biochemistry, 2001, Jul-31, Volume: 40, Issue:30

    Topics: Allosteric Regulation; Asparagine; Aspartate Carbamoyltransferase; Aspartic Acid; Escherichia coli; Fluorescent Dyes; Kinetics; Peptide Fragments; Phenylalanine; Phosphonoacetic Acid; Spectrometry, Fluorescence; Substrate Specificity; Titrimetry; Tryptophan; Tyrosine

2001