Torrent_2006_Protein.Pept.Lett_13_271

Reference

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

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Citations formats

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