High Pressure Modulates Amyloid Formation

Joan      Torrent; Claude      Balny; Reinhard      Lange

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.

Keywords: Amyloid, high pressure, fibrils, protein aggregation, protein folding, protein conformation, prion

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Protein & Peptide Letters

Title: High Pressure Modulates Amyloid Formation

Volume: 13 Issue: 3

Author(s): Joan Torrent, Claude Balny and Reinhard Lange

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Keywords: Amyloid, high pressure, fibrils, protein aggregation, protein folding, protein conformation, prion

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.

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Torrent Joan, Balny Claude and Lange Reinhard, High Pressure Modulates Amyloid Formation, Protein & Peptide Letters 2006; 13 (3) . https://dx.doi.org/10.2174/092986606775338371