cytidine triphosphate has been researched along with histidine in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (25.00) | 18.7374 |
| 1990's | 2 (25.00) | 18.2507 |
| 2000's | 3 (37.50) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 1 (12.50) | 2.80 |
| Authors | Studies |
|---|---|
| Schachman, HK; Wente, SR | 1 |
| Cole, SC; Yon, RJ | 1 |
| Browne, DT; Moore, AC | 1 |
| Cornell, RB; Gilham, D; Veitch, DP | 1 |
| Brieba, LG; Huang, J; Sousa, R | 1 |
| Cornell, RB; Dennis, MK; Ding, Z; Smith, JL; Taneva, S | 1 |
| Cornell, RB; Ding, Z; Johnson, J; Lee, J; Paetzel, M | 1 |
| Chakraborty, A; Chang, IY; Chang, YS; Chen, BC; Chien, KY; Hsieh, YJ; Huang, KJ; Huang, XR; Lee, YH; Lin, TY; Lin, WC; Lin, YT; Liu, JL; Ma, KT; Pai, LM; Sung, LY; Wang, CY; Wang, HI; Wang, PY; Yu, JS | 1 |
8 other study(ies) available for cytidine triphosphate and histidine
| Article | Year |
|---|---|
Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme.
Topics: Adenosine Triphosphate; Allosteric Regulation; Aspartate Carbamoyltransferase; Aspartic Acid; Binding Sites; Carbamyl Phosphate; Cytidine Triphosphate; DNA Mutational Analysis; Histidine; Lysine; Phosphonoacetic Acid; Structure-Activity Relationship | 1991 |
Comparison of aspartate transcarbamoylases from wheat germ and Escherichia coli: functionally identical histidines in nonhomologous local sequences.
Topics: Amino Acid Sequence; Aspartate Carbamoyltransferase; Binding Sites; Cytidine Triphosphate; Diethyl Pyrocarbonate; Escherichia coli; Histidine; Kinetics; Peptide Fragments; Plants; Species Specificity; Triticum; Uridine Monophosphate | 1986 |
Binding of regulatory nucleotides to aspartate transcarbamylase: nuclear magnetic resonance studies of selectively enriched carbon-13 regulatory subunit.
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 |
The role of histidine residues in the HXGH site of CTP:phosphocholine cytidylyltransferase in CTP binding and catalysis.
Topics: Animals; Binding Sites; Choline-Phosphate Cytidylyltransferase; COS Cells; Cytidine Triphosphate; Enzyme Stability; Histidine; Hydrogen Bonding; Kinetics; Liver; Mutagenesis, Site-Directed; Mutation; Protein Conformation; Protein Denaturation; Rats; Transfection | 1998 |
Misincorporation by wild-type and mutant T7 RNA polymerases: identification of interactions that reduce misincorporation rates by stabilizing the catalytically incompetent open conformation.
Topics: Alanine; Bacteriophage T7; Base Pair Mismatch; Catalysis; Cytidine Triphosphate; DNA-Directed RNA Polymerases; Enzyme Stability; Glycine; Histidine; Mutagenesis, Site-Directed; Phenylalanine; Point Mutation; Protein Conformation; Transcription, Genetic; Uridine Triphosphate | 2000 |
Contribution of each membrane binding domain of the CTP:phosphocholine cytidylyltransferase-alpha dimer to its activation, membrane binding, and membrane cross-bridging.
Topics: Amino Acid Motifs; Animals; Cell Membrane; Choline-Phosphate Cytidylyltransferase; Cross-Linking Reagents; Cytidine Triphosphate; Dimerization; Glutaral; Histidine; Kinetics; Models, Biological; Mutagenesis; Protein Binding; Protein Structure, Tertiary; Rats | 2008 |
Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold.
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 |
SNAP29 mediates the assembly of histidine-induced CTP synthase filaments in proximity to the cytokeratin network.
Topics: Animals; Carbon-Nitrogen Ligases; Cytidine Triphosphate; Histidine; Keratins | 2020 |