lysine has been researched along with uridine triphosphate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Fukui, T; Kazuta, Y; Nakano, K; Omura, Y; Tagaya, M | 1 |
| Kantrowitz, ER; Zhang, Y | 1 |
| Fukui, T; Konishi, Y; Muroya, S; Tanizawa, K | 1 |
| Davidson, JN; Haubner, A; Ream, A; Simmons, AJ; Simmons, CQ | 1 |
4 other study(ies) available for lysine and uridine triphosphate
| Article | Year |
|---|---|
Identification of lysyl residues located at the substrate-binding site in UDP-glucose pyrophosphorylase from potato tuber: affinity labeling with uridine di- and triphosphopyridoxals.
Topics: Affinity Labels; Amino Acid Sequence; Binding Sites; Enzyme Activation; Lysine; Molecular Sequence Data; Pyridoxal Phosphate; Solanum tuberosum; Substrate Specificity; Uridine Diphosphate; Uridine Triphosphate; UTP-Glucose-1-Phosphate Uridylyltransferase | 1991 |
Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATP.
Topics: Adenosine Triphosphate; Alanine; Aspartate Carbamoyltransferase; Binding Sites; Binding, Competitive; Chemical Phenomena; Chemistry; Cytidine Triphosphate; Cytosine Nucleotides; Escherichia coli; Hydrogen-Ion Concentration; Lysine; Mutation; Protein Conformation; Uridine Triphosphate | 1989 |
Molecular cloning, nucleotide sequencing, and affinity labeling of bovine liver UDP-glucose pyrophosphorylase.
Topics: Affinity Labels; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cattle; Chromatography, High Pressure Liquid; Cloning, Molecular; Dictyostelium; Liver; Lysine; Molecular Sequence Data; Oligonucleotide Probes; Pyridoxal Phosphate; Restriction Mapping; Sequence Homology, Amino Acid; Solanum tuberosum; Uridine Triphosphate; UTP-Glucose-1-Phosphate Uridylyltransferase | 1993 |
Substitutions in hamster CAD carbamoyl-phosphate synthetase alter allosteric response to 5-phosphoribosyl-alpha-pyrophosphate (PRPP) and UTP.
Topics: Allosteric Regulation; Amino Acid Sequence; Amino Acid Substitution; Animals; Aspartate Carbamoyltransferase; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Cricetinae; Dihydroorotase; Escherichia coli; Lysine; Molecular Sequence Data; Multienzyme Complexes; Mutagenesis, Site-Directed; Phosphoribosyl Pyrophosphate; Sequence Homology, Amino Acid; Serine; Tryptophan; Uridine Triphosphate | 2004 |