Compounds > phosphonoacetic acid

phosphonoacetic acid and glutamine

phosphonoacetic acid has been researched along with glutamine in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (60.00)18.2507
2000's2 (40.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Bellows, DS; Clarke, ID; Diamandis, P; Dirks, PB; Graham, J; Jamieson, LG; Ling, EK; Sacher, AG; Tyers, M; Ward, RJ; Wildenhain, J1
Burman, DL; Peterson, CB; Schachman, HK1
Kantrowitz, ER; Middleton, SA; Tauc, P; Vachette, P1
Kantrowitz, ER; Stebbins, JW; Zhang, Y1
Kantrowitz, ER; Pastra-Landis, SC; Stieglitz, KA; Tsuruta, H; Xia, J1

Other Studies

5 other study(ies) available for phosphonoacetic acid and glutamine

ArticleYear
Chemical genetics reveals a complex functional ground state of neural stem cells.
    Nature chemical biology, 2007, Volume: 3, Issue:5

    Topics: Animals; Cell Survival; Cells, Cultured; Mice; Molecular Structure; Neoplasms; Neurons; Pharmaceutical Preparations; Sensitivity and Specificity; Stem Cells

2007
Effects of replacement of active site residue glutamine 231 on activity and allosteric properties of aspartate transcarbamoylase.
    Biochemistry, 1992, Sep-15, Volume: 31, Issue:36

    Topics: Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Enzyme Activation; Escherichia coli; Glutamine; Kinetics; Ligands; Mutagenesis, Site-Directed; Phosphonoacetic Acid; Structure-Activity Relationship; Substrate Specificity

1992
Structural consequences of the replacement of Glu239 by Gln in the catalytic chain of Escherichia coli aspartate transcarbamylase.
    Journal of molecular biology, 1990, Jul-05, Volume: 214, Issue:1

    Topics: Adenosine Triphosphate; Amino Acid Sequence; Aspartate Carbamoyltransferase; Aspartic Acid; Carbamyl Phosphate; Cytidine Triphosphate; Escherichia coli; Glutamates; Glutamic Acid; Glutamine; Phosphonoacetic Acid; Protein Engineering; Structure-Activity Relationship; X-Ray Diffraction

1990
Importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamoylase.
    Biochemistry, 1990, Apr-24, Volume: 29, Issue:16

    Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Catalysis; Cytidine Triphosphate; Escherichia coli; Glutamine; Kinetics; Mutation; Phosphonoacetic Acid; Protein Conformation

1990
A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.
    Journal of molecular biology, 2005, Jun-03, Volume: 349, Issue:2

    Topics: Allosteric Regulation; Amino Acid Substitution; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Crystallography, X-Ray; Escherichia coli; Glutamine; Models, Molecular; Phosphonoacetic Acid; Protein Structure, Quaternary; Protein Subunits; Static Electricity; Structure-Activity Relationship

2005