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

thioflavin t and edrophonium

thioflavin t has been researched along with edrophonium in 4 studies

Research

Studies (4)

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

Authors

AuthorsStudies
De Ferrari, GV; Inestrosa, NC; Mallender, WD; Rosenberry, TL1
Cheung, J; Martin, PK; Nix, AJ; Rosenberry, TL; Snyder, SA; Tan, RX; Wildman, SA1
Darvesh, S; Macdonald, IR; Martin, E; Rosenberry, TL1
Al-Rashid, ZF; Beri, V; Cheung, J; Rosenberry, TL; Shiomi, K; Wildman, SA1

Other Studies

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

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
Hopeahainol A binds reversibly at the acetylcholinesterase (AChE) peripheral site and inhibits enzyme activity with a novel higher order concentration dependence.
    Chemico-biological interactions, 2016, Nov-25, Volume: 259, Issue:Pt B

    Topics: Acetylcholinesterase; Benzothiazoles; Binding Sites; Catalytic Domain; Cholinesterase Inhibitors; Dipterocarpaceae; Edrophonium; Heterocyclic Compounds, 4 or More Rings; Kinetics; Molecular Docking Simulation; Plant Bark; Substrate Specificity; Thermodynamics; Thiazoles

2016
Probing the peripheral site of human butyrylcholinesterase.
    Biochemistry, 2012, Sep-11, Volume: 51, Issue:36

    Topics: Binding, Competitive; Butyrylcholinesterase; Catalytic Domain; Cholinesterase Inhibitors; Humans; Models, Molecular; Mutation

2012
The natural product dihydrotanshinone I provides a prototype for uncharged inhibitors that bind specifically to the acetylcholinesterase peripheral site with nanomolar affinity.
    Biochemistry, 2013, Oct-22, Volume: 52, Issue:42

    Topics: Acetylcholine; Acetylcholinesterase; Aflatoxin B1; Binding Sites; Binding, Competitive; Catalysis; Catalytic Domain; Cholinesterase Inhibitors; Crystallography, X-Ray; Furans; Humans; Hydrolysis; Kinetics; Models, Chemical; Phenanthrenes; Pyrans; Quinones; Recombinant Proteins; Structure-Activity Relationship; Substrate Specificity

2013