tryptophan has been researched along with tryptophyl adenylate in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 4 (80.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (20.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Andrews, D; Graves, PV; Labouesse, B; Merle, M; Muench, KH; Trezeguet, V | 1 |
Graves, PV; Labouesse, B; Labouesse, J; Merault, G | 1 |
Drutsa, VL; Favorova, OO; Madoyan, IA | 1 |
Gandar, JC; Graves, PV; Labouesse, B; Mazat, JP; Merault, G; Merle, M | 1 |
Buckner, FS; Fan, E; Hol, WG; Kim, JE; Koh, CY; Napoli, AJ; Van Voorhis, WC; Verlinde, CL | 1 |
5 other study(ies) available for tryptophan and tryptophyl adenylate
Article | Year |
---|---|
Tryptophanyl adenylate formation by tryptophanyl-tRNA synthetase from Escherichia coli.
Topics: Adenosine Monophosphate; Amino Acyl-tRNA Synthetases; Chromatography, Gel; Escherichia coli; Kinetics; Protein Binding; Spectrometry, Fluorescence; Tryptophan; Tryptophan-tRNA Ligase | 1986 |
Kinetics of formation of tryptophanyl-adenylate by tryptophanyl-tRNA synthetase from beef pancreas.
Topics: Adenosine Monophosphate; Adenosine Triphosphate; Amino Acyl-tRNA Synthetases; Animals; Cattle; Inorganic Pyrophosphatase; Kinetics; Macromolecular Substances; Pancreas; Pyrophosphatases; Tryptophan; Tryptophan-tRNA Ligase | 1981 |
"Half-site" affinity modification of tryptophanyl-tRNA synthetase leads to "freezing" of the free subunit.
Topics: Adenosine Monophosphate; Adenosine Triphosphate; Affinity Labels; Amino Acyl-tRNA Synthetases; Animals; Binding Sites; Cattle; Diphosphates; Kinetics; Macromolecular Substances; Pancreas; Tryptophan; Tryptophan-tRNA Ligase | 1981 |
Kinetic anticooperativity in pre-steady-state formation of tryptophanyl adenylate by tryptophanyl-tRNA synthetase from beef pancreas. A consequence of the tryptophan anticooperative binding.
Topics: Adenosine Monophosphate; Amino Acyl-tRNA Synthetases; Animals; Cattle; Kinetics; Mathematics; Pancreas; Protein Binding; Tryptophan; Tryptophan-tRNA Ligase | 1982 |
Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Antimalarials; Crystallography, X-Ray; Drug Design; Models, Molecular; Molecular Sequence Data; Plasmodium falciparum; Protein Binding; Protein Conformation; Sequence Alignment; Tryptophan; Tryptophan-tRNA Ligase | 2013 |