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High pressure modulates amyloid formation.

Joan Torrent·Claude Balny·Reinhard Lange
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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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AmyloidHydrostatic PressureProtein ConformationProtein FoldingJournal ArticleResearch Support, Non-U.S. Gov'tReview

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Joan Torrent, Claude Balny, Reinhard Lange. 2006. High pressure modulates amyloid formation.. https://doi.org/10.2174/092986606775338371

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