trifluoroethanol has been researched along with alpha-synuclein 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 | 2 (22.22) | 29.6817 |
| 2010's | 7 (77.78) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Du, HN; Hu, HY; Hu, J; Li, HT; Tang, L | 1 |
| Fink, AL; Munishkina, LA; Phelan, C; Uversky, VN | 1 |
| Anderson, VL; Eliezer, D; Ramlall, TF; Rospigliosi, CC; Webb, WW | 1 |
| Benetti, F; Doglia, SM; Grandori, R; Legname, G; Natalello, A | 1 |
| Giehm, L; Lorenzen, N; Otzen, DE | 1 |
| Anderson, VL; Eliezer, D; Webb, WW | 1 |
| Hao, Y; Li, D; Liu, YN; Wang, C; Zhou, B; Zhou, F | 1 |
| Buscarino, G; Di Carlo, MG; Foderà, V; Leone, M; Vestergaard, B; Vetri, V | 1 |
| Eliezer, D; Sung, YH | 1 |
1 review(s) available for trifluoroethanol and alpha-synuclein
| Article | Year |
|---|---|
Assays for α-synuclein aggregation.
Topics: alpha-Synuclein; Amyloid; Humans; Parkinson Disease; Reproducibility of Results; Research Design; Sodium Dodecyl Sulfate; Trifluoroethanol | 2011 |
8 other study(ies) available for trifluoroethanol and alpha-synuclein
| Article | Year |
|---|---|
Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation.
Topics: alpha-Synuclein; Biopolymers; Circular Dichroism; gamma-Synuclein; Humans; In Vitro Techniques; Macromolecular Substances; Nerve Tissue Proteins; Parkinson Disease; Peptide Fragments; Protein Structure, Secondary; Spectrometry, Fluorescence; Synucleins; Trifluoroethanol | 2002 |
Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes.
Topics: Alcohols; alpha-Synuclein; Benzothiazoles; Circular Dichroism; Ethanol; Fluorescent Dyes; Humans; Kinetics; Light; Models, Chemical; Nerve Tissue Proteins; Phospholipids; Propanols; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Scattering, Radiation; Solvents; Spectroscopy, Fourier Transform Infrared; Synucleins; Thiazoles; Trifluoroethanol | 2003 |
Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation.
Topics: alpha-Synuclein; Humans; Mutation; Parkinson Disease; Protein Structure, Secondary; Trifluoroethanol | 2010 |
Compact conformations of α-synuclein induced by alcohols and copper.
Topics: alpha-Synuclein; Copper Sulfate; Hydrogen-Ion Concentration; Methanol; Propanols; Protein Folding; Protein Structure, Tertiary; Spectrometry, Mass, Electrospray Ionization; Trifluoroethanol | 2011 |
Interplay between desolvation and secondary structure in mediating cosolvent and temperature induced alpha-synuclein aggregation.
Topics: alpha-Synuclein; Circular Dichroism; Microscopy, Electron, Transmission; Protein Structure, Secondary; Temperature; Trifluoroethanol | 2012 |
Conversion of natively unstructured α-synuclein to its α-helical conformation significantly attenuates production of reactive oxygen species.
Topics: alpha-Synuclein; Amino Acid Sequence; Copper; Humans; Hydrogen Peroxide; Hydroxides; Kinetics; Molecular Sequence Data; Protein Binding; Protein Stability; Protein Structure, Secondary; Reactive Oxygen Species; Solvents; Trifluoroethanol; Water | 2013 |
Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution.
Topics: alpha-Synuclein; Amyloid; Humans; Protein Aggregates; Protein Stability; Spectrum Analysis; Temperature; Trifluoroethanol | 2016 |
Structure and dynamics of the extended-helix state of alpha-synuclein: Intrinsic lability of the linker region.
Topics: Alcohols; alpha-Synuclein; Humans; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Parkinson Disease; Propanols; Protein Aggregates; Protein Structure, Secondary; Trifluoroethanol | 2018 |