thioflavin t has been researched along with nile red in 5 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (20.00) | 29.6817 |
| 2010's | 4 (80.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Arvinte, T; Demeule, B; Gurny, R | 1 |
| Hammarström, P; Mishra, R; Sjölander, D | 1 |
| Azami-Movahed, M; Ebrahim-Habibi, A; Ghasemi, A; Nemat-Gorgani, M; Sabbaghian, M; Shariatizi, S | 1 |
| Basu, A; Bhattacharya, SC; Kumar, GS | 1 |
| Abou-Zied, OK; Akhtari, K; Aziz, FM; Falahati, M; Mustafa, TA; Salihi, A; Shahpasand, K; Tahaei Gilan, SS; Yahya Rayat, D | 1 |
5 other study(ies) available for thioflavin t and nile red
| Article | Year |
|---|---|
Detection and characterization of protein aggregates by fluorescence microscopy.
Topics: Antibodies; Benzothiazoles; Calcitonin; Congo Red; Microscopy, Fluorescence; Oxazines; Staining and Labeling; Thiazoles | 2007 |
Spectroscopic characterization of diverse amyloid fibrils in vitro by the fluorescent dye Nile red.
Topics: Amyloid; Benzothiazoles; Binding Sites; Fluorescence Resonance Energy Transfer; Humans; Hydrogen-Ion Concentration; Kinetics; Microscopy; Muramidase; Oxazines; Prealbumin; Protein Binding; Staining and Labeling; Thiazoles | 2011 |
Heme binding site in apomyoglobin may be effectively targeted with small molecules to control aggregation.
Topics: Amyloid; Animals; Apoproteins; Benzothiazoles; Binding Sites; Cell Survival; Flavonoids; Fluorescent Dyes; Heme; Horses; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Kinetics; Light; Molecular Docking Simulation; Myoglobin; Oxazines; Particle Size; PC12 Cells; Protein Binding; Protein Multimerization; Protein Structure, Quaternary; Rats; Scattering, Radiation; Thiazoles | 2013 |
Influence of the ionic liquid 1-butyl-3-methylimidazolium bromide on amyloid fibrillogenesis in lysozyme: Evidence from photophysical and imaging studies.
Topics: Amyloid; Anilino Naphthalenesulfonates; Animals; Benzothiazoles; Chickens; Circular Dichroism; Congo Red; Imaging, Three-Dimensional; Imidazoles; Ionic Liquids; Light; Microscopy, Atomic Force; Muramidase; Oxazines; Spectrometry, Fluorescence; Thiazoles | 2018 |
α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency.
Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Cell Death; Cell Line, Tumor; Congo Red; Humans; Iron; Kinetics; L-Lactate Dehydrogenase; Metal Nanoparticles; Molecular Docking Simulation; Molecular Dynamics Simulation; Oxazines; Protein Aggregates; Protein Structure, Secondary; Spectrometry, Fluorescence; Tyrosine | 2019 |