m-(n,n,n-trimethylammonio)trifluoroacetophenone has been researched along with propidium in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (33.33) | 18.2507 |
| 2000's | 2 (66.67) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Mallender, WD; Rosenberry, TL; Szegletes, T | 1 |
| De Ferrari, GV; Inestrosa, NC; Mallender, WD; Rosenberry, TL | 1 |
| Cusack, B; Davies, MP; Fauq, A; Johnson, JL; Rosenberry, TL | 1 |
3 other study(ies) available for m-(n,n,n-trimethylammonio)trifluoroacetophenone and propidium
| Article | Year |
|---|---|
Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands.
Topics: Acetophenones; Acetylcholinesterase; Acylation; Alkaloids; Binding Sites; Binding, Competitive; Cholinesterase Inhibitors; Enzyme Activation; Humans; Hydrolysis; Ligands; Models, Chemical; Propidium; Sesquiterpenes | 1998 |
Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites.
Topics: Acetophenones; Acetylcholinesterase; Acylation; Benzothiazoles; Binding Sites; Cholinesterase Inhibitors; Coloring Agents; Dose-Response Relationship, Drug; Edrophonium; Fluorescent Dyes; Humans; Propidium; Protein Conformation; Thiazoles | 2001 |
Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate.
Topics: Acetanilides; Acetophenones; Acetylcholinesterase; Acetylthiocholine; Acylation; Benzothiazoles; Binding Sites; Catalysis; Cholinesterase Inhibitors; Drug Interactions; Fluorescent Dyes; Humans; Hydrolysis; Ligands; Models, Chemical; Mutagenesis, Site-Directed; Propidium; Protein Conformation; Recombinant Proteins; Stereoisomerism; Substrate Specificity; Thiazoles | 2003 |