High pressure modulates amyloid formation.


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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@article{Torrent2006HighPM, title={High pressure modulates amyloid formation.}, author={Joan Torrent and Claude Balny and Reinhard Lange}, journal={Protein and peptide letters}, year={2006}, volume={13 3}, pages={271-7} }