rivastigmine has been researched along with phenserine 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 | 3 (75.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brossi, A; Greig, NH; Holloway, HW; Whittaker, NF; Yu, QS; Zhu, X | 1 |
| Alley, GM; Brossi, A; Deschamps, JR; Greig, NH; Holloway, HW; Kulkarni, SS; Lahiri, DK; Luo, W; Parrish, D; Yu, QS; Zhan, M | 1 |
| Chaudhaery, SS; Nath, C; Nazir, A; Roy, KK; Sammi, SR; Saxena, AK; Saxena, G; Shakya, N | 1 |
| Barak, D; Greig, NH; Ordentlich, A; Shafferman, A; Stein, D; Yu, QS | 1 |
4 other study(ies) available for rivastigmine and phenserine
| Article | Year |
|---|---|
Anticholinesterase activity of compounds related to geneserine tautomers. N-Oxides and 1,2-oxazines.
Topics: Acetylcholinesterase; Alkaloids; Butyrylcholinesterase; Cholinesterase Inhibitors; Cyclic N-Oxides; Humans; Isomerism; Oxazines; Structure-Activity Relationship | 2002 |
Novel anticholinesterases based on the molecular skeletons of furobenzofuran and methanobenzodioxepine.
Topics: Acetylcholinesterase; Amyloid beta-Protein Precursor; Benzofurans; Butyrylcholinesterase; Carbamates; Cell Line; Cell Survival; Cholinesterase Inhibitors; Crystallography, X-Ray; Humans; Models, Molecular; Molecular Structure; Neurons; Oxepins; Structure-Activity Relationship | 2005 |
Novel carbamates as orally active acetylcholinesterase inhibitors found to improve scopolamine-induced cognition impairment: pharmacophore-based virtual screening, synthesis, and pharmacology.
Topics: Acetylcholinesterase; Administration, Oral; Animals; Avoidance Learning; Caenorhabditis elegans; Carbamates; Catalytic Domain; Cholinesterase Inhibitors; Databases, Factual; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Male; Mice; Models, Molecular; Nootropic Agents; Quantitative Structure-Activity Relationship; Scopolamine | 2010 |
Accommodation of physostigmine and its analogues by acetylcholinesterase is dominated by hydrophobic interactions.
Topics: Acetylcholinesterase; Binding Sites; Catalysis; Cholinesterase Inhibitors; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Models, Molecular; Molecular Structure; Mutation; Phenylcarbamates; Physostigmine; Protein Binding; Pyridostigmine Bromide; Rivastigmine; Structure-Activity Relationship | 2009 |