title: High pressure modulates amyloid formation.
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.
authors.affiliation: INSERM U710, CC 105, Université Montpellier 2, Place Eugène Bataillon, F-34095 Montpellier cédex 5, France.
authors.forename: Joan
authors.initials: J
authors.lastname: Torrent
authors.forename: Claude
authors.initials: C
authors.lastname: Balny
authors.forename: Reinhard
authors.initials: R
authors.lastname: Lange
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D006874:Hydrostatic Pressure / Q000009:adverse effects; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D000682:Amyloid