thioflavin t has been researched along with valine in 7 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 5 (71.43) | 29.6817 |
| 2010's | 2 (28.57) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Du, HN; Hu, HY; Hu, J; Li, HT; Luo, XY; Tang, L; Zhou, JW | 1 |
| Keasling, JD; Muller, SJ; Wang, K | 1 |
| Jones, EM; Surewicz, K; Surewicz, WK | 1 |
| Caughey, B; James, W; Sim, VL; Tahiri-Alaoui, A | 1 |
| Chang, ES; Chen, RP; Fann, W; Liao, TY; Lim, TS | 1 |
| Ciaccio, NA; Laurence, JS; Middaugh, CR; Reynolds, TS | 1 |
| Cortez, LM; Kumar, J; Renault, L; Sim, VL; Young, HS | 1 |
7 other study(ies) available for thioflavin t and valine
| Article | Year |
|---|---|
A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein.
Topics: Alanine; alpha-Synuclein; Amino Acid Motifs; Benzothiazoles; Circular Dichroism; Escherichia coli; Glycine; Humans; Microscopy, Atomic Force; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Peptides; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Synucleins; Thiazoles; Time Factors; Valine | 2003 |
Effects of the sequence and size of non-polar residues on self-assembly of amphiphilic peptides.
Topics: Alanine; Amino Acid Motifs; Amyloid; Benzothiazoles; Circular Dichroism; Congo Red; Gene Library; Glycine; Hydrogel, Polyethylene Glycol Dimethacrylate; Isoleucine; Leucine; Macromolecular Substances; Microscopy, Electron, Scanning; Microscopy, Electron, Transmission; Models, Molecular; Peptides; Phenylalanine; Protein Binding; Protein Conformation; Protein Folding; Protein Structure, Secondary; Temperature; Thiazoles; Ultraviolet Rays; Valine; X-Ray Diffraction | 2005 |
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 |
A new amyloid-like beta-aggregate with amyloid characteristics, except fibril morphology.
Topics: Amino Acid Substitution; Amyloid beta-Peptides; Animals; Benzothiazoles; Cell Death; Cell Line, Tumor; Congo Red; Mice; Models, Biological; Mutant Proteins; Mutation; Peptides; Proline; Protein Structure, Quaternary; Protein Structure, Secondary; Thiazoles; Time Factors; Valine | 2009 |
Influence of the valine zipper region on the structure and aggregation of the basic leucine zipper (bZIP) domain of activating transcription factor 5 (ATF5).
Topics: Activating Transcription Factors; Benzothiazoles; Circular Dichroism; Fluorescence; Humans; Leucine Zippers; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary; Spectroscopy, Fourier Transform Infrared; Thiazoles; Valine | 2012 |
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 |