trifluoroethanol has been researched along with congo red in 8 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 5 (62.50) | 29.6817 |
| 2010's | 3 (37.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bucciantini, M; Capanni, C; Chiti, F; Dobson, CM; Stefani, M; Taddei, N | 1 |
| Avilés, FX; Pallarès, I; Vendrell, J; Ventura, S | 1 |
| Bemporad, F; Calamai, M; Chiti, F; Dobson, CM; Plakoutsi, G; Taddei, N | 1 |
| Bemporad, F; Chiti, F; Stefani, M; Taddei, N | 1 |
| Karimi, SA; Khodarahmi, R; Soori, H | 1 |
| Ahmad, B; Chiti, F; Tiribilli, B; Winkelmann, J | 1 |
| Iram, A; Naeem, A | 1 |
| Bhat, SA; Iram, A; Naeem, A | 1 |
8 other study(ies) available for trifluoroethanol and congo red
| Article | Year |
|---|---|
Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain.
Topics: Amyloid; Amyloid beta-Peptides; Bacterial Proteins; Benzothiazoles; Circular Dichroism; Cloning, Molecular; Coloring Agents; Congo Red; Escherichia coli; Fluorescent Dyes; Hot Temperature; Hydrogen-Ion Concentration; Microscopy, Electron; Protein Structure, Tertiary; Thiazoles; Time Factors; Trifluoroethanol; Urea | 2001 |
Amyloid fibril formation by a partially structured intermediate state of alpha-chymotrypsin.
Topics: Amyloid; Benzothiazoles; Chymotrypsin; Circular Dichroism; Congo Red; Fluorescent Dyes; Protein Structure, Secondary; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Thiazoles; Trifluoroethanol | 2004 |
Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates.
Topics: Acid Anhydride Hydrolases; Acylphosphatase; Amyloid; Anilino Naphthalenesulfonates; Archaeal Proteins; Circular Dichroism; Congo Red; Kinetics; Microscopy, Electron; Models, Molecular; Multiprotein Complexes; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Sulfolobus solfataricus; Trifluoroethanol; Troponin T | 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 |
Chaperone-like activity of heme group against amyloid-like fibril formation by hen egg ovalbumin: possible mechanism of action.
Topics: Amyloid; Animals; Chickens; Circular Dichroism; Congo Red; Dimethyl Sulfoxide; Electrophoresis, Polyacrylamide Gel; Female; Fluorescence; Heme; Hot Temperature; Molecular Chaperones; Ovalbumin; Oxidation-Reduction; Protein Denaturation; Trifluoroethanol | 2009 |
Searching for conditions to form stable protein oligomers with amyloid-like characteristics: The unexplored basic pH.
Topics: Amyloid; Benzothiazoles; Carboxyl and Carbamoyl Transferases; Circular Dichroism; Congo Red; Escherichia coli Proteins; Hydrogen-Ion Concentration; Microscopy, Atomic Force; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Protein Multimerization; Protein Structure, Quaternary; Spectrometry, Fluorescence; Thiazoles; Trifluoroethanol; Tryptophan | 2010 |
Trifluoroethanol and acetonitrile induced formation of the molten globule states and aggregates of cellulase.
Topics: Acetonitriles; Aspergillus niger; Benzothiazoles; Biomimetics; Cellulase; Circular Dichroism; Congo Red; Protein Conformation; Protein Multimerization; Spectroscopy, Fourier Transform Infrared; Thiazoles; Trifluoroethanol | 2012 |
Anesthetic 2,2,2-trifluoroethanol induces amyloidogenesis and cytotoxicity in human serum albumin.
Topics: Anesthetics; Benzothiazoles; Comet Assay; Congo Red; Fluorescent Dyes; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Lymphocytes; Nucleic Acid Denaturation; Primary Cell Culture; Protein Aggregates; Protein Binding; Protein Folding; Protein Structure, Secondary; Serum Albumin; Solutions; Thiazoles; Trifluoroethanol | 2015 |