Compounds > thioflavin t
Page last updated: 2024-08-22

thioflavin t and acetylthiocholine

thioflavin t has been researched along with acetylthiocholine in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's3 (75.00)29.6817
2010's1 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Cusack, B; Davies, MP; Fauq, A; Johnson, JL; Rosenberry, TL1
Cusack, B; Dekat, SE; Johnson, JL; Rosenberry, TL; Sonoda, LK2
Auletta, JT; Johnson, JL; Rosenberry, TL1

Other Studies

4 other study(ies) available for thioflavin t and acetylthiocholine

ArticleYear
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
Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis.
    Chemico-biological interactions, 2008, Sep-25, Volume: 175, Issue:1-3

    Topics: Acetylcholinesterase; Acetylthiocholine; Benzothiazoles; Carbachol; Humans; Hydrolysis; Recombinant Proteins; Spectrometry, Fluorescence; Thiazoles

2008
Analysis of the reaction of carbachol with acetylcholinesterase using thioflavin T as a coupled fluorescence reporter.
    Biochemistry, 2008, Dec-09, Volume: 47, Issue:49

    Topics: Acetylcholinesterase; Acetylthiocholine; Acylation; Benzothiazoles; Binding Sites; Carbachol; Catalysis; Fluorescent Dyes; Hydrolysis; Kinetics; Ligands; Spectrometry, Fluorescence; Substrate Specificity; Thermodynamics; Thiazoles

2008
Molecular basis of inhibition of substrate hydrolysis by a ligand bound to the peripheral site of acetylcholinesterase.
    Chemico-biological interactions, 2010, Sep-06, Volume: 187, Issue:1-3

    Topics: Acetylcholinesterase; Acetylthiocholine; Animals; Benzothiazoles; Binding, Competitive; Carbachol; Catalytic Domain; Cell Line; Cholinesterase Inhibitors; Crystallography, X-Ray; Humans; Hydrolysis; Kinetics; Ligands; Quaternary Ammonium Compounds; Substrate Specificity; Thiazoles

2010