thioflavin t has been researched along with phenylalanine 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 | 6 (85.71) | 29.6817 |
| 2010's | 1 (14.29) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Gordon, DJ; Meredith, SC | 1 |
| Almeida, FC; Ferrão-Gonzales, AD; Ferreira, A; Foguel, D; Juliano, L; Moreau, VH; Robbs, BK; Silva, JL; Valente, AP | 1 |
| Keasling, JD; Muller, SJ; Wang, K | 1 |
| Bemporad, F; Chiti, F; Stefani, M; Taddei, N | 1 |
| Gupta, R; Marek, P; Raleigh, DP | 1 |
| Meredith, SC; Orgel, JP; Sciarretta, KL; Tycko, R | 1 |
| Cortez, LM; Kumar, J; Renault, L; Sim, VL; Young, HS | 1 |
7 other study(ies) available for thioflavin t and phenylalanine
| Article | Year |
|---|---|
Probing the role of backbone hydrogen bonding in beta-amyloid fibrils with inhibitor peptides containing ester bonds at alternate positions.
Topics: Amino Acid Sequence; Amyloid beta-Peptides; Benzothiazoles; Congo Red; Cross-Linking Reagents; Diphenylhexatriene; Esters; Fluorescent Dyes; Humans; Hydrogen Bonding; Molecular Sequence Data; Peptide Fragments; Phenylalanine; Protein Binding; Protein Conformation; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Thiazoles; Ultracentrifugation | 2003 |
Controlling {beta}-amyloid oligomerization by the use of naphthalene sulfonates: trapping low molecular weight oligomeric species.
Topics: Amyloid; Amyloid beta-Peptides; Anilino Naphthalenesulfonates; Animals; Anions; Benzothiazoles; Biochemistry; Cell Line; Chromatography; Congo Red; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Fluorescent Dyes; Hydrogen-Ion Concentration; Kinetics; Light; Lysine; Magnetic Resonance Spectroscopy; Mice; Micelles; Models, Chemical; Models, Molecular; Molecular Conformation; Molecular Weight; Naphthalenesulfonates; Peptide Fragments; Peptides; Phenylalanine; Prions; Protein Structure, Secondary; Scattering, Radiation; Sodium Dodecyl Sulfate; Spectrophotometry; Static Electricity; Sulfonic Acids; Temperature; Tetrazolium Salts; Thiazoles; Time Factors | 2005 |
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 |
Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.
Topics: Acid Anhydride Hydrolases; Acylphosphatase; Amino Acid Substitution; Amyloid; Benzothiazoles; Birefringence; Circular Dichroism; Congo Red; Data Interpretation, Statistical; Humans; Hydrophobic and Hydrophilic Interactions; Muscles; Phase Transition; Phenylalanine; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Thiazoles; Trifluoroethanol; Tyrosine | 2006 |
The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation.
Topics: Alanine; Amino Acid Sequence; Amyloid; Benzothiazoles; Diabetes Mellitus, Type 2; Fluorescence; Fluorescent Dyes; Humans; Islet Amyloid Polypeptide; Kinetics; Molecular Sequence Data; Nitriles; Phenylalanine; Point Mutation; Protein Binding; Thiazoles; Time Factors | 2008 |
Evidence for novel beta-sheet structures in Iowa mutant beta-amyloid fibrils.
Topics: Amyloid; Amyloid beta-Peptides; Amyloid Neuropathies, Familial; Aspartic Acid; Benzothiazoles; Glutamic Acid; Humans; Kinetics; Leucine; Lysine; Microscopy, Electron, Transmission; Models, Molecular; Mutation, Missense; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Phenylalanine; Protein Structure, Secondary; Spectrometry, Fluorescence; Thiazoles; X-Ray Diffraction | 2009 |
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 |