T. R. Jahn and S. E. Radford, Folding versus aggregation: Polypeptide conformations on competing pathways, Arch. Biochem. Biophys, vol.469, pp.100-117, 2008.

J. W. Kelly, Towards an understanding of amyloidogenesis, Nat. Struct. Biol, vol.9, pp.323-325, 2002.

C. Soto and S. Pritzkow, Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases, Nat. Neurosci, vol.21, pp.1332-1340, 2018.

K. Annamalai, K. H. Guhrs, R. Koehler, M. Schmidt, H. Michel et al., Polymorphism of Amyloid Fibrils In Vivo, Angew. Chem. Int. Ed. Engl, vol.55, pp.4822-4825, 2016.

G. Legname, H. O. Nguyen, D. Peretz, F. E. Cohen, S. J. Dearmond et al., Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes, Proc. Natl. Acad. Sci, vol.103, 2006.

J. Safar, H. Wille, V. Itri, D. Groth, H. Serban et al., Eight prion strains have PrP(Sc) molecules with different conformations, Nat. Med, vol.4, pp.1157-1165, 1998.

G. C. Telling, P. Parchi, S. J. Dearmond, P. Cortelli, P. Montagna et al., Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity, Science, vol.274, pp.2079-2082, 1996.

M. Jucker and L. C. Walker, Self-propagation of pathogenic protein aggregates in neurodegenerative diseases, Nature, vol.501, pp.45-51, 2013.

E. Gazit and . The, Correctly Folded" state of proteins: Is it a metastable state, Angew. Chem. Int. Ed. Engl, vol.41, pp.257-259, 2002.

W. Close, M. Neumann, A. Schmidt, M. Hora, K. Annamalai et al., Physical basis of amyloid fibril polymorphism, Nat. Commun, vol.9, p.699, 2018.

A. Igel-egalon, M. Moudjou, D. Martin, A. Busley, T. Knapple et al., Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick, PLoS Pathog, vol.13, 2017.

C. Balny, P. Masson, and K. Heremans, High pressure effects on biological macromolecules: From structural changes to alteration of cellular processes, Biochim. Biophys. Acta, vol.1595, pp.3-10, 2002.

K. Heremans, High pressure effects on proteins and other biomolecules, Annu. Rev. Biophys. Bioeng, vol.11, pp.1-21, 1982.

V. V. Mozhaev, K. Heremans, J. Frank, P. Masson, and C. Balny, High pressure effects on protein structure and function, Proteins, vol.24, pp.81-91, 1996.

T. W. Randolph, M. Seefeldt, and J. F. Carpenter, High hydrostatic pressure as a tool to study protein aggregation and amyloidosis, Biochim. Biophys. Acta, vol.1595, pp.224-234, 2002.

J. L. Silva, D. Foguel, and C. A. Royer, Pressure provides new insights into protein folding, dynamics and structure, Trends Biochem. Sci, vol.26, pp.612-618, 2001.

R. Winter and W. Dzwolak, Exploring the temperature-pressure configurational landscape of biomolecules: From lipid membranes to proteins, Philos. Trans. A Math. Phys. Eng. Sci, vol.363, p.202, 2005.

J. Roche, J. A. Caro, D. R. Norberto, P. Barthe, C. Roumestand et al., Cavities determine the pressure unfolding of proteins, Proc. Natl. Acad. Sci, vol.109, pp.6945-6950, 2012.

G. A. De-oliveira, M. A. Marques, C. Cruzeiro-silva, Y. Cordeiro, C. Schuabb et al., Structural basis for the dissociation of alpha-synuclein fibrils triggered by pressure perturbation of the hydrophobic core

D. El-moustaine, V. Perrier, I. Acquatella-tran-van-ba, F. Meersman, V. G. Ostapchenko et al., Amyloid features and neuronal toxicity of mature prion fibrils are highly sensitive to high pressure, J. Biol. Chem, vol.286, pp.13448-13459, 2011.

A. D. Ferrao-gonzales, L. Palmieri, M. Valory, J. L. Silva, H. Lashuel et al., Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease, J. Mol. Biol, vol.328, pp.963-974, 2003.

D. Foguel, M. C. Suarez, A. D. Ferrao-gonzales, T. C. Porto, L. Palmieri et al., Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities, Proc. Natl. Acad. Sci, vol.100, pp.9831-9836, 2003.

N. Rezaei-ghaleh, M. Amininasab, S. Kumar, J. Walter, and M. Zweckstetter, Phosphorylation modifies the molecular stability of beta-amyloid deposits, Nat. Commun, 2016.

J. Torrent, R. Lange, and H. Rezaei, The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation, J. Biol. Chem, vol.290, pp.20417-20426, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01837415

J. Torrent, M. T. Alvarez-martinez, F. Heitz, J. P. Liautard, C. Balny et al., Alternative prion structural changes revealed by high pressure, Biochemistry, vol.42, pp.1318-1325, 2003.

N. Makarava, R. Savtchenko, and I. V. Baskakov, Purification and Fibrillation of Full-Length Recombinant PrP, Methods Mol. Biol, vol.1658, pp.3-22, 2017.

F. Eghiaian, T. Daubenfeld, Y. Quenet, M. Van-audenhaege, A. P. Bouin et al., Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage, Proc. Natl. Acad. Sci, vol.104, pp.7414-7419, 2007.
URL : https://hal.archives-ouvertes.fr/inserm-00172995

A. Armiento, P. Moireau, D. Martin, N. Lepejova, M. Doumic et al., The mechanism of monomer transfer between two structurally distinct PrP oligomers, PLoS ONE, vol.12, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01574346

E. M. Jones and W. K. Surewicz, Fibril conformation as the basis of species-and strain-dependent seeding specificity of mammalian prion amyloids, Cell, vol.121, pp.63-72, 2005.

P. Tixador, L. Herzog, F. Reine, E. Jaumain, J. Chapuis et al., The physical relationship between infectivity and prion protein aggregates is strain-dependent, PLoS Pathog, vol.6, 2010.

F. Laferriere, P. Tixador, M. Moudjou, J. Chapuis, P. Sibille et al., Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics, PLoS Pathog, vol.9, 2013.

J. Li, S. P. Mahal, C. A. Demczyk, and C. Weissmann, Mutability of prions, EMBO Rep, vol.12, pp.1243-1250, 2011.

J. Rasmussen, J. Mahler, N. Beschorner, S. A. Kaeser, L. M. Hasler et al., Amyloid polymorphisms constitute distinct clouds of conformational variants in different etiological subtypes of Alzheimer's disease, Proc. Natl. Acad. Sci, vol.114, pp.13018-13023, 2017.

L. Breydo, N. Makarava, and I. V. Baskakov, Methods for conversion of prion protein into amyloid fibrils, Methods Mol. Biol, vol.459, pp.105-115, 2008.

J. Torrent, J. Font, H. Herberhold, S. Marchal, M. Ribo et al., The use of pressure-jump relaxation kinetics to study protein folding landscapes, Biochim. Biophys. Acta, vol.1764, pp.489-496, 2006.