trifluoroethanol has been researched along with Parkinson Disease in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 3 (75.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Eliezer, D; Sung, YH | 1 |
| Anderson, VL; Eliezer, D; Ramlall, TF; Rospigliosi, CC; Webb, WW | 1 |
| Giehm, L; Lorenzen, N; Otzen, DE | 1 |
| Du, HN; Hu, HY; Hu, J; Li, HT; Tang, L | 1 |
1 review(s) available for trifluoroethanol and Parkinson Disease
| Article | Year |
|---|---|
Assays for α-synuclein aggregation.
Topics: alpha-Synuclein; Amyloid; Humans; Parkinson Disease; Reproducibility of Results; Research Design; Sodium Dodecyl Sulfate; Trifluoroethanol | 2011 |
3 other study(ies) available for trifluoroethanol and Parkinson Disease
| Article | Year |
|---|---|
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 |
Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation.
Topics: alpha-Synuclein; Humans; Mutation; Parkinson Disease; Protein Structure, Secondary; Trifluoroethanol | 2010 |
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 |