6 Article(s)Download |
PMID | Title | Pub. Year | #Total Relationships |
1 | 27372900 | Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution. | 2016 Sep | 1 |
2 | 24383916 | Probing conformational change of intrinsically disordered α-synuclein to helical structures by distinctive regional interactions with lipid membranes. | 2014 Feb 4 | 1 |
3 | 23123341 | Conversion of natively unstructured α-synuclein to its α-helical conformation significantly attenuates production of reactive oxygen species. | 2013 Jan | 2 |
4 | 20947801 | Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation. | 2010 Nov 2 | 1 |
5 | 12115139 | Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol: non-amyloid component sequence is essential and beta-sheet formation is prerequisite to aggregation. | 2002 Aug 5 | 2 |
6 | 9851705 | The N-terminal region of non-A beta component of Alzheimer's disease amyloid is responsible for its tendency to assume beta-sheet and aggregate to form fibrils. | 1998 Nov 15 | 3 |