thioflavin t has been researched along with Dementias, Transmissible in 16 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (6.25) | 18.2507 |
| 2000's | 7 (43.75) | 29.6817 |
| 2010's | 8 (50.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Brindisi, M; Brogi, S; Butini, S; Campiani, G; Chemi, G; Gemma, S; Legname, G; Zaccagnini, L | 1 |
| Anson, KJ; Campbell, KJ; Caughey, B; Groveman, BR; Hughson, AG; Kraus, A; Manca, M; Orrù, CD; Raymond, GJ; Raymond, LD | 1 |
| Abskharon, R; Castilla, J; Dang, J; Elfarash, A; Fujioka, H; Hassan, S; Mulaj, M; Shen, P; Steyaert, J; Surewicz, WK; Wang, F; Wang, Z; Wohlkonig, A; Zou, LS; Zou, WQ | 1 |
| Bannach, O; Birkmann, E; Luers, L; Nagel-Steger, L; Riesner, D; Stöhr, J; Willbold, D; Wolff, M; Wördehoff, MM | 1 |
| Chen, J; Liang, Y; Pan, K; Yi, CW | 1 |
| Collins, SJ; Haigh, CL | 1 |
| Bawumia, S; Bayley, PM; Bronstein, I; Dear, D; Dodson, G; Hirst, E; Martin, S; Nash, A; Polyakova, O; Stern, I | 1 |
| Artamonova, TO; Artemov, AV; Khodorkovskiĭ, MA; Mikhaĭlova, EV; Nevzgliadova, OV; Snigirevskaia, ES; Soĭdla, TR | 1 |
| Cortez, LM; Kumar, J; Renault, L; Sim, VL; Young, HS | 1 |
| Surewicz, KA; Surewicz, WK; Vanik, DL | 1 |
| Doh-ura, K | 1 |
| Bryszewska, M; Cladera, J; Cortijo-Arellano, M; Klajnert, B | 1 |
| Jones, EM; Surewicz, K; Surewicz, WK | 1 |
| Caughey, B; James, W; Sim, VL; Tahiri-Alaoui, A | 1 |
| Nandi, PK | 1 |
| Bose, S; Gu, Y; Kalepu, S; Mishra, RS; Singh, N; Verghese, S | 1 |
1 review(s) available for thioflavin t and Dementias, Transmissible
| Article | Year |
|---|---|
[Therapeutics for prion diseases].
Topics: Amyloid; Animals; Benzothiazoles; Clinical Trials as Topic; Drug Design; Humans; Pentosan Sulfuric Polyester; Prion Diseases; Prions; Protein Binding; Quinacrine; Thiazoles | 2003 |
15 other study(ies) available for thioflavin t and Dementias, Transmissible
| Article | Year |
|---|---|
Identification of novel fluorescent probes preventing PrP
Topics: Cell Line, Tumor; Cell Survival; Fluorescent Dyes; Humans; Molecular Docking Simulation; Prion Diseases; Protein Aggregates; Protein Conformation; PrPSc Proteins; Quantitative Structure-Activity Relationship | 2017 |
RT-QuIC Assays for Prion Disease Detection and Diagnostics.
Topics: Amyloid; Animals; Benzothiazoles; Biological Assay; Brain; Brain Chemistry; Fluorescent Dyes; Gene Expression; Humans; Nasal Cavity; Prion Diseases; Protein Conformation, beta-Strand; Protein Folding; PrPC Proteins; PrPSc Proteins; Recombinant Proteins; Sensitivity and Specificity; Thiazoles | 2017 |
Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors.
Topics: Animals; Arvicolinae; Benzothiazoles; Circular Dichroism; Escherichia coli; Humans; Mice; Mice, Transgenic; Microscopy, Electron; Oxidoreductases; Polymorphism, Genetic; Prion Diseases; Prion Proteins; Prions; Protein Aggregates; PrPC Proteins; Surface Plasmon Resonance; Thiazoles | 2017 |
Seeded fibrillation as molecular basis of the species barrier in human prion diseases.
Topics: Amyloid; Animals; Benzothiazoles; Cattle; Circular Dichroism; Deer; Humans; Kinetics; Prion Diseases; PrPSc Proteins; Sheep; Species Specificity; Thiazoles; Ultracentrifugation | 2013 |
Zinc significantly changes the aggregation pathway and the conformation of aggregates of human prion protein.
Topics: Benzothiazoles; Humans; Prion Diseases; Prions; Protein Aggregates; Protein Conformation; Thiazoles; Zinc | 2015 |
Simplified Murine 3D Neuronal Cultures for Investigating Neuronal Activity and Neurodegeneration.
Topics: Animals; Benzothiazoles; Calcium Signaling; Cell Culture Techniques; Cell Differentiation; Cell Survival; Cells, Cultured; Mice; Microscopy, Confocal; Models, Neurological; Nerve Tissue Proteins; Neural Stem Cells; Neurons; Prion Diseases; Spheroids, Cellular; Thiazoles | 2017 |
Proteolysis of prion protein by cathepsin S generates a soluble beta-structured intermediate oligomeric form, with potential implications for neurotoxic mechanisms.
Topics: Animals; Benzothiazoles; Cathepsins; Circular Dichroism; Hydrolysis; Neurotoxins; Peptide Fragments; Prion Diseases; Prions; Protein Conformation; Protein Folding; Protein Multimerization; Sequence Deletion; Sheep; Thiazoles | 2009 |
[The effect of red pigment of Saccharomyces cerevisiae on insulin fibril formation in vitro].
Topics: Amyloid; Animals; Benzothiazoles; Biomimetic Materials; Fluorescence; Fluorescent Dyes; Humans; Hydrogen-Ion Concentration; Hydrolysis; Insulin; Microscopy, Electron; Microscopy, Electron, Transmission; Pigments, Biological; Prion Diseases; Saccharomyces cerevisiae; Solutions; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thiazoles | 2011 |
Mouse prion protein polymorphism Phe-108/Val-189 affects the kinetics of fibril formation and the response to seeding: evidence for a two-step nucleation polymerization mechanism.
Topics: Alleles; Animals; Benzothiazoles; Circular Dichroism; Dose-Response Relationship, Drug; Kinetics; Mice; Microscopy, Electron; Phenylalanine; Polymers; Polymorphism, Genetic; Prion Diseases; Prions; Protein Conformation; Recombinant Proteins; Thiazoles; Time Factors; Valine | 2013 |
Molecular basis of barriers for interspecies transmissibility of mammalian prions.
Topics: Amino Acid Sequence; Amino Acid Substitution; Amyloid; Animals; Animals, Genetically Modified; Benzothiazoles; Cattle; Disease Transmission, Infectious; Fluorescent Dyes; Humans; Molecular Sequence Data; Prion Diseases; Prions; Protein Conformation; Recombinant Proteins; Sequence Alignment; Species Specificity; Thiazoles | 2004 |
Influence of heparin and dendrimers on the aggregation of two amyloid peptides related to Alzheimer's and prion diseases.
Topics: Alzheimer Disease; Amyloid; Benzothiazoles; Dendrimers; Heparin; Kinetics; Molecular Structure; Peptide Fragments; Prion Diseases; Spectrometry, Fluorescence; Thiazoles | 2006 |
Role of N-terminal familial mutations in prion protein fibrillization and prion amyloid propagation in vitro.
Topics: Amyloid; Benzothiazoles; Escherichia coli; Genetic Predisposition to Disease; Humans; In Vitro Techniques; Kinetics; Methionine; Microscopy, Atomic Force; Molecular Conformation; Mutation; Plasmids; Polymorphism, Genetic; Prion Diseases; Prions; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Spectroscopy, Fourier Transform Infrared; Thiazoles; Time Factors; Valine | 2006 |
Molecular heterosis of prion protein beta-oligomers. A potential mechanism of human resistance to disease.
Topics: Alleles; Amyloid; Benzothiazoles; Circular Dichroism; Heterozygote; Homozygote; Humans; Hybrid Vigor; Kinetics; Methionine; Prion Diseases; Prions; Thiazoles; Valine | 2006 |
Polymerization of human prion peptide HuPrP 106-126 to amyloid in nucleic acid solution.
Topics: Amino Acid Sequence; Amyloid; Anilino Naphthalenesulfonates; Animals; Benzothiazoles; DNA; Fluorescent Dyes; Humans; Hydrogen-Ion Concentration; In Vitro Techniques; Macromolecular Substances; Molecular Sequence Data; Peptide Fragments; Polymers; Prion Diseases; Prions; Protein Binding; Solutions; Thiazoles | 1998 |
Prion peptide 106-126 as a model for prion replication and neurotoxicity.
Topics: Benzothiazoles; Cell Line; Detergents; Fluorescent Dyes; Humans; Membrane Proteins; Microscopy, Fluorescence; Models, Biological; Mutation; Neurons; Peptide Fragments; Prion Diseases; Prions; Protein Transport; PrPC Proteins; Solubility; Thiazoles; Tumor Cells, Cultured | 2002 |