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Updated: Aug 11, 2026

A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
Published on: May 22, 2018
High pressure modulates amyloid formation
Joan Torrent1, Claude Balny, Reinhard Lange
1INSERM U710, CC 105, Université Montpellier 2, Place Eugène Bataillon, F-34095 Montpellier cédex 5, France.
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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