oleanolic acid has been researched along with tryptophan in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 4 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Chen, S; Chen, Y; Hu, X; Li, Q; Li, Z; Wang, Z; Xie, W; Zhai, J; Zhang, H; Zhang, L; Zhao, Y; Zheng, X | 1 |
Hou, J; Li, Q; Shao, S; Wang, Z; Yue, Y | 1 |
Brodelius, PE; Guo, M; Lu, X; Wang, Y | 1 |
Aiba, Y; Hoshino, T; Nakano, C; Terasawa, Y; Watanabe, T | 1 |
4 other study(ies) available for oleanolic acid and tryptophan
Article | Year |
---|---|
Inhibitor selectivity between aldo-keto reductase superfamily members AKR1B10 and AKR1B1: role of Trp112 (Trp111).
Topics: Aldehyde Reductase; Aldo-Keto Reductases; Benzothiazoles; Catalytic Domain; Crystallography, X-Ray; Enzyme Inhibitors; Flufenamic Acid; Hydrogen Bonding; Imidazolidines; Models, Molecular; Naphthalenes; Oleanolic Acid; Phthalazines; Protein Binding; Protein Structure, Secondary; Rhodanine; Structural Homology, Protein; Thiazolidines; Tryptophan | 2013 |
Spectroscopic analysis on structure-affinity relationship in the interactions of different oleanane-type triterpenoids with bovine serum albumin.
Topics: Binding Sites; Fluorescence Resonance Energy Transfer; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Oleanolic Acid; Serum Albumin, Bovine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Thermodynamics; Triterpenes; Tryptophan | 2015 |
Comparison of the interaction between lactoferrin and isomeric drugs.
Topics: Animals; Binding Sites; Cattle; Energy Transfer; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Isomerism; Lactoferrin; Metals; Models, Molecular; Molecular Docking Simulation; Oleanolic Acid; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Triterpenes; Tryptophan; Ursolic Acid | 2017 |
Strictly Conserved Residues in Euphorbia tirucalli β-Amyrin Cyclase: Trp612 Stabilizes Transient Cation through Cation-π Interaction and CH-π Interaction of Tyr736 with Leu734 Confers Robust Local Protein Architecture.
Topics: Biosynthetic Pathways; Cations; Cyclization; Enzyme Stability; Euphorbia; Intramolecular Transferases; Models, Molecular; Mutagenesis; Oleanolic Acid; Point Mutation; Protein Conformation; Tryptophan | 2018 |