thioflavin t has been researched along with proline in 9 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 7 (77.78) | 29.6817 |
| 2010's | 2 (22.22) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Conway, KA; Harper, JD; Lansbury, PT | 1 |
| Damas, AM; Merlini, G; Saraiva, MJ; Sebastião, MP | 1 |
| Corboy, MJ; Cutler, TD; Hunt, JF; Lee, MG; Oldan, J; Rizo, J; Thibodeau, PH; Thomas, PJ; Wigley, WC | 1 |
| Aksenova, M; Butterfield, DA; Kanski, J; Schöneich, C | 1 |
| Baud, S; Keeley, FW; Miao, M; Pomès, R; Rauscher, S | 1 |
| Chang, HY; King, CY; Lee, HC; Lin, JY; Wang, HL | 1 |
| Chang, ES; Chen, RP; Fann, W; Liao, TY; Lim, TS | 1 |
| Keeley, FW; Muiznieks, LD | 1 |
| Chen, BP; Chen, W; Chern, Y; He, RY; Huang, JJ; Liu, GC; Sun, CS; Wang, CH; Wang, CY | 1 |
9 other study(ies) available for thioflavin t and proline
| Article | Year |
|---|---|
Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid.
Topics: Alanine; alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; Binding Sites; Brain; Circular Dichroism; Congo Red; Endopeptidases; Humans; Hydrolysis; Immunohistochemistry; Lewy Bodies; Microscopy, Atomic Force; Microscopy, Polarization; Molecular Sequence Data; Mutation, Missense; Nerve Tissue Proteins; Parkinson Disease; Postmortem Changes; Proline; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Synucleins; Thiazoles; Threonine | 2000 |
The molecular interaction of 4'-iodo-4'-deoxydoxorubicin with Leu-55Pro transthyretin 'amyloid-like' oligomer leading to disaggregation.
Topics: Amino Acid Substitution; Amyloidosis; Benzothiazoles; Crystallization; Doxorubicin; Humans; Iodine; Leucine; Models, Molecular; Prealbumin; Proline; Protein Binding; Protein Structure, Secondary; Thiazoles; X-Ray Diffraction | 2000 |
A protein sequence that can encode native structure by disfavoring alternate conformations.
Topics: Amino Acid Sequence; Benzothiazoles; Cell Line; Cell Membrane; Circular Dichroism; Computational Biology; Cystic Fibrosis Transmembrane Conductance Regulator; Genome; Humans; Liposomes; Micelles; Molecular Sequence Data; Mutation; Proline; Protein Folding; Protein Structure, Secondary; Recombinant Fusion Proteins; Spectroscopy, Fourier Transform Infrared; Structure-Activity Relationship; Thermodynamics; Thiazoles | 2002 |
Substitution of isoleucine-31 by helical-breaking proline abolishes oxidative stress and neurotoxic properties of Alzheimer's amyloid beta-peptide.
Topics: Amino Acid Substitution; Amyloid beta-Peptides; Animals; Benzothiazoles; Circular Dichroism; Copper; Isoleucine; Microscopy, Electron; Neurons; Oxidative Stress; Peptide Fragments; Proline; Rats; Thiazoles | 2002 |
Proline and glycine control protein self-organization into elastomeric or amyloid fibrils.
Topics: Alzheimer Disease; Amino Acid Sequence; Amyloid; Animals; Benzothiazoles; Chickens; Elastin; Entropy; Glycine; Humans; Insecta; Models, Molecular; Molecular Sequence Data; Peptides; Proline; Protein Conformation; Thiazoles; Triticum | 2006 |
Strain-specific sequences required for yeast [PSI+] prion propagation.
Topics: Amino Acid Sequence; Benzothiazoles; Glycine; Peptide Termination Factors; Prions; Proline; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thiazoles | 2008 |
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 |
Proline periodicity modulates the self-assembly properties of elastin-like polypeptides.
Topics: Amyloid; Benzothiazoles; Elastin; Proline; Protein Multimerization; Protein Structure, Secondary; Thiazoles | 2010 |
The influence of pathological mutations and proline substitutions in TDP-43 glycine-rich peptides on its amyloid properties and cellular toxicity.
Topics: Amino Acid Sequence; Amino Acid Substitution; Amyloid; Animals; Benzothiazoles; Cell Membrane; DNA-Binding Proteins; Glycine; Mice; Molecular Sequence Data; Mutant Proteins; Mutation; Peptides; Proline; Protein Aggregates; Protein Multimerization; Protein Structure, Secondary; Spectrum Analysis, Raman; Thiazoles; Time Factors | 2014 |