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m-(n,n,n-trimethylammonio)trifluoroacetophenone and thioflavin t

m-(n,n,n-trimethylammonio)trifluoroacetophenone has been researched along with thioflavin t in 2 studies

Research

Studies (2)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
De Ferrari, GV; Inestrosa, NC; Mallender, WD; Rosenberry, TL1
Cusack, B; Davies, MP; Fauq, A; Johnson, JL; Rosenberry, TL1

Other Studies

2 other study(ies) available for m-(n,n,n-trimethylammonio)trifluoroacetophenone and thioflavin t

ArticleYear
Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites.
    The Journal of biological chemistry, 2001, Jun-29, Volume: 276, Issue:26

    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.
    Biochemistry, 2003, May-13, Volume: 42, Issue:18

    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