Title : High pressure modulates amyloid formation - Torrent_2006_Protein.Pept.Lett_13_271 |
Author(s) : Torrent J , Balny C , Lange R |
Ref : Protein Pept Lett , 13 :271 , 2006 |
Abstract :
A common mechanism of conformational changes and pathological aggregation of proteins associated with amyloid diseases remains to be proven. High pressure is emerging as a new strategy for studying aspects of amyloid formation. Pressure provides a convenient means to populate and characterize partially folded states, which are thought to have a key role in assembly processes of proteins into amyloid fibrils. High pressure can also be used to dissociate aggregates and amyloid fibrils or on the opposite to generate such species. |
PubMedSearch : Torrent_2006_Protein.Pept.Lett_13_271 |
PubMedID: 16515455 |
Torrent J, Balny C, Lange R (2006)
High pressure modulates amyloid formation
Protein Pept Lett
13 :271
Torrent J, Balny C, Lange R (2006)
Protein Pept Lett
13 :271