phenylalanyl adenylate has been researched along with phenylalanine in 4 studies
| Studies (phenylalanyl adenylate) | Trials (phenylalanyl adenylate) | Recent Studies (post-2010) (phenylalanyl adenylate) | Studies (phenylalanine) | Trials (phenylalanine) | Recent Studies (post-2010) (phenylalanine) |
|---|---|---|---|---|---|
| 9 | 0 | 0 | 23,695 | 721 | 4,367 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (50.00) | 18.7374 |
| 1990's | 1 (25.00) | 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 |
|---|---|
| Baltzinger, M; Lin, SX; Remy, P | 1 |
| Ishigami, M; Kinjo, M; Nagano, K; Tonotsuka-Ohta, N | 1 |
| Lavrik, O; Moor, N; Reshetnikova, L; Vassylyev, DG | 1 |
| Favre, A; Lavrik, O; Moor, N; Safro, M | 1 |
4 other study(ies) available for phenylalanyl adenylate and phenylalanine
| Article | Year |
|---|---|
Yeast phenylalanyl-tRNA synthetase: symmetric behavior of the enzyme during activation of phenylalanine as shown by a rapid kinetic investigation.
Topics: Adenosine Monophosphate; Amino Acyl-tRNA Synthetases; Binding Sites; Enzyme Activation; Kinetics; Phenylalanine; Phenylalanine-tRNA Ligase; Saccharomyces cerevisiae; Spectrometry, Fluorescence | 1983 |
Effect of polynucleotides and a basic protein on the condensation of phenylalanyl adenylate.
Topics: Adenosine Monophosphate; Animals; Cattle; Chemistry, Organic; Histones; Kinetics; Organic Chemistry Phenomena; Phenylalanine; Poly U; Serum Albumin, Bovine; Thymus Gland | 1980 |
Crystal structures of phenylalanyl-tRNA synthetase complexed with phenylalanine and a phenylalanyl-adenylate analogue.
Topics: Adenosine Monophosphate; Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Macromolecular Substances; Metals; Models, Molecular; Molecular Sequence Data; Phenylalanine; Phenylalanine-tRNA Ligase; Protein Conformation; Sequence Homology, Amino Acid; Thermus thermophilus | 1999 |
Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end.
Topics: Adenosine Monophosphate; Adenosine Triphosphate; Affinity Labels; Amino Acid Sequence; Base Sequence; Conserved Sequence; Cross-Linking Reagents; Escherichia coli; Humans; Molecular Sequence Data; Nucleic Acid Conformation; Phenylalanine; Phenylalanine-tRNA Ligase; Photochemistry; Protein Binding; Protein Subunits; RNA, Transfer, Phe; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity; Thiouridine | 2003 |