thioflavin t has been researched along with baicalein 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 | 2 (50.00) | 29.6817 |
2010's | 2 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Fink, AL; Han, S; Kaylor, J; Rajamani, S; Zhou, F; Zhu, M | 1 |
Danzer, KM; Duan, W; Finger, S; Garidel, P; Giese, A; Glabe, CG; Habeck, M; Heinzelmann, U; Högen, T; Kostka, M; Kretzschmar, H; Levin, J; Ross, CA; Wagner, R; Wirth, A | 1 |
Bae, SY; Hwang, H; Kim, HK; Kim, JH; Kim, S; Kim, TD; Lee, S; Yoon, HC | 1 |
Rochet, JC; Stanciu, LA; Zhang, H | 1 |
4 other study(ies) available for thioflavin t and baicalein
Article | Year |
---|---|
The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils.
Topics: alpha-Synuclein; Anaerobiosis; Benzothiazoles; Circular Dichroism; Escherichia coli; Flavanones; Flavonoids; Humans; Light; Lysine; Microscopy, Atomic Force; Molecular Weight; Nerve Tissue Proteins; Oxidation-Reduction; Protein Conformation; Quinones; Scattering, Radiation; Solubility; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Synucleins; Thiazoles; Tyrosine | 2004 |
Single particle characterization of iron-induced pore-forming alpha-synuclein oligomers.
Topics: alpha-Synuclein; Benzothiazoles; Electrophysiology; Flavanones; Fluorescent Dyes; Gene Expression Regulation; Humans; Iron; Lipid Bilayers; Microscopy, Atomic Force; Microscopy, Confocal; Models, Biological; Parkinson Disease; Protein Binding; Solvents; Thiazoles | 2008 |
Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR).
Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Catechin; Flavanones; Humans; Imidazoles; Imides; Ionic Liquids; Microscopy, Electron, Transmission; Parkinson Disease; Sulfonamides; Tandem Repeat Sequences; Thiazoles | 2010 |
Cu(II) promotes amyloid pore formation.
Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Cations, Divalent; Copper; Flavanones; Humans; Kinetics; Microscopy, Electron, Transmission; Oxidation-Reduction; Protein Aggregates; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Thiazoles | 2015 |