aspartic acid has been researched along with farnesyl pyrophosphate in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (25.00) | 18.2507 |
| 2000's | 3 (75.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cane, DE; Fitzsimons, BC; Xue, Q | 1 |
| Croteau, RB; Little, DB | 1 |
| Bowers, KE; Fierke, CA; Pickett, JS | 1 |
| Chen, AP; Guo, RT; Ko, TP; Kuo, CJ; Liang, PH; Wang, AH | 1 |
4 other study(ies) available for aspartic acid and farnesyl pyrophosphate
| Article | Year |
|---|---|
Trichodiene synthase. Probing the role of the highly conserved aspartate-rich region by site-directed mutagenesis.
Topics: Aspartic Acid; Binding Sites; Carbon-Carbon Lyases; Catalysis; Conserved Sequence; Cyclohexenes; Escherichia coli; Fusarium; Kinetics; Lyases; Magnesium; Manganese; Mutagenesis, Site-Directed; Polyisoprenyl Phosphates; Recombinant Proteins; Sesquiterpenes | 1996 |
Alteration of product formation by directed mutagenesis and truncation of the multiple-product sesquiterpene synthases delta-selinene synthase and gamma-humulene synthase.
Topics: Alkyl and Aryl Transferases; Arginine; Aspartic Acid; Gas Chromatography-Mass Spectrometry; Hemiterpenes; Isomerism; Kinetics; Models, Chemical; Models, Molecular; Mutagenesis, Site-Directed; Organophosphorus Compounds; Polyisoprenyl Phosphates; Recombinant Proteins; Sesquiterpenes; Trees | 2002 |
Mutagenesis studies of protein farnesyltransferase implicate aspartate beta 352 as a magnesium ligand.
Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Aspartic Acid; Binding Sites; Catalysis; Humans; Kinetics; Ligands; Magnesium; Mutagenesis, Site-Directed; Polyisoprenyl Phosphates; Sesquiterpenes | 2003 |
Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis.
Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Aspartic Acid; Binding Sites; Catalysis; Cell Wall; Conserved Sequence; Crystallization; Crystallography, X-Ray; Escherichia coli; Hemiterpenes; Hydrogen Bonding; Kinetics; Magnesium; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Organophosphorus Compounds; Peptidoglycan; Polyisoprenyl Phosphates; Protein Folding; Sequence Alignment; Sesquiterpenes; Structure-Activity Relationship | 2005 |