phenylalanyl adenylate has been researched along with adenosine monophosphate in 8 studies
*Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position. [MeSH]
*Adenosine Monophosphate: Adenine nucleotide containing one phosphate group esterified to the sugar moiety in the 2'-, 3'-, or 5'-position. [MeSH]
| Studies (phenylalanyl adenylate) | Trials (phenylalanyl adenylate) | Recent Studies (post-2010) (phenylalanyl adenylate) | Studies (adenosine monophosphate) | Trials (adenosine monophosphate) | Recent Studies (post-2010) (adenosine monophosphate) |
|---|---|---|---|---|---|
| 9 | 0 | 0 | 11,432 | 257 | 2,798 |
| Protein | Taxonomy | phenylalanyl adenylate (IC50) | adenosine monophosphate (IC50) |
|---|---|---|---|
| Fructose-1,6-bisphosphatase 1 | Sus scrofa (pig) | 1.3 | |
| Fructose-1,6-bisphosphatase 1 | Homo sapiens (human) | 2.6436 | |
| Cytochrome P450 2C9 | Homo sapiens (human) | 2.6 | |
| Proto-oncogene tyrosine-protein kinase Src | Homo sapiens (human) | 0.1 | |
| Amine oxidase [flavin-containing] B | Rattus norvegicus (Norway rat) | 0.44 | |
| Histamine H3 receptor | Rattus norvegicus (Norway rat) | 0.8 |
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 3 (37.50) | 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 | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Baltzinger, M; Lin, SX; Remy, P | 1 |
| Ishigami, M; Kinjo, M; Yamamoto, N | 1 |
| Ishigami, M; Kinjo, M; Nagano, K; Tonotsuka-Ohta, N | 1 |
| Fersht, AR; Hennecke, H; Ibba, M; Johnson, CM | 1 |
| Lavrik, O; Moor, N; Reshetnikova, L; Vassylyev, DG | 1 |
| Ankilova, V; Fishman, R; Moor, N; Safro, M | 1 |
| Favre, A; Lavrik, O; Moor, N; Safro, M | 1 |
| Kotik-Kogan, O; Moor, N; Safro, M; Sukhanova, M; Tworowski, D | 1 |
8 other study(ies) available for phenylalanyl adenylate and adenosine monophosphate
| 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 |
Catalytic mechanism of histone in peptide formation from phenylalanyl adenylate.
Topics: Adenosine Monophosphate; Animals; Cattle; Histones; Kinetics; Peptides; Thymus Gland | 1982 |
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 |
Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase.
Topics: Adenosine Monophosphate; Kinetics; Phenylalanine-tRNA Ligase; RNA, Transfer | 1995 |
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 |
Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese.
Topics: Acylation; Adenosine Monophosphate; Crystallization; Crystallography, X-Ray; Dimerization; DNA; Manganese; Models, Molecular; Phenylalanine-tRNA Ligase; Protein Conformation; Protein Structure, Tertiary; Sulfates; Thermus thermophilus | 2001 |
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 |
The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end.
Topics: Adenosine Monophosphate; Binding Sites; Crystallization; Models, Molecular; Phenylalanine-tRNA Ligase; Protein Structure, Tertiary; RNA, Transfer, Phe; Structure-Activity Relationship; Substrate Specificity; Thermus thermophilus | 2006 |