arginine has been researched along with phosphoribosyl pyrophosphate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (25.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Paulus, TJ; Switzer, RL | 1 |
| Focia, P; Kanaani, J; Maltby, D; Wang, CC | 1 |
| Kim, JH; Krahn, JM; Smith, JL; Tomchick, DR; Zalkin, H | 1 |
| Craig, SP; Fletterick, RJ; Focia, PJ | 1 |
4 other study(ies) available for arginine and phosphoribosyl pyrophosphate
| Article | Year |
|---|---|
Characterization of pyrimidine-repressible and arginine-repressible carbamyl phosphate synthetases from Bacillus subtilis.
Topics: Arginine; Bacillus subtilis; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing); Enzyme Repression; Guanine Nucleotides; Hot Temperature; Isoenzymes; Kinetics; Molecular Weight; Phosphoribosyl Pyrophosphate; Phosphotransferases; Uracil; Uracil Nucleotides | 1979 |
Identification of the active sites of human and schistosomal hypoxanthine-guanine phosphoribosyltransferases by GMP-2',3'-dialdehyde affinity labeling.
Topics: Affinity Labels; Amino Acid Sequence; Animals; Arginine; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Guanosine Monophosphate; Humans; Hypoxanthine Phosphoribosyltransferase; Iodoacetates; Iodoacetic Acid; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Phosphoribosyl Pyrophosphate; Schistosoma mansoni; Sequence Analysis; Trypsin | 1995 |
Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site.
Topics: Adenosine Monophosphate; Amidophosphoribosyltransferase; Arginine; Aspartate-Ammonia Ligase; Base Sequence; Binding Sites; DNA Primers; Enzyme Inhibitors; Glutamate Synthase; Glutamine; Guanosine Monophosphate; Hydrogen Bonding; Kinetics; Models, Molecular; Molecular Sequence Data; Phosphoribosyl Pyrophosphate; Protein Binding; Protein Structure, Tertiary; Structure-Activity Relationship; Tyrosine | 1996 |
Substitution of lysine for arginine at position 199 of a hypoxanthine phosphoribosyltransferase interferes with binding of the primary substrate to the active site.
Topics: Animals; Arginine; Binding Sites; Humans; Hypoxanthine Phosphoribosyltransferase; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Phosphoribosyl Pyrophosphate; Schistosoma | 1997 |