Collinge, J. Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519–550 (2001).
Wickner, R. B. et al. Prion diseases of yeast: amyloid structure and biology. Semin. Cell Dev. Biol. 22, 469–475 (2011).
Jucker, M. & Walker, L. C. Self-propagation of pathogenic protein aggregates in neurodegenerative diseases. Nature 501, 45–51 (2013).
Bruce, M. E. Scrapie strain variation and mutation. Br. Med. Bull. 49, 822–838 (1993).
Collinge, J. Prion strain mutation and selection. Science 328, 1111–1112 (2010).
Li, J., Browning, S., Mahal, S. P., Oelschlegel, A. M. & Weissmann, C. Darwinian evolution of prions in cell culture. Science 327, 869–872 (2010).
An important study of prions in cell culture showing that biologically 'cloned' populations of prions gradually become heterogeneous by accumulating 'mutants', with selection pressure resulting in the emergence of different mutants in the evolving population.
Sandberg, M. K., Al Doujaily, H., Sharps, B., Clarke, A. R. & Collinge, J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 470, 540–542 (2011).
Refs 7 and 19 demonstrate that prion propagation and neurotoxicity occur in two distinct mechanistic phases in vivo; they also show that neurotoxicity relates to distinct species of PrP that are produced following a pathway switch that occurs when prion levels become saturated.
Hill, A. F. et al. Species barrier independent prion replication in apparently resistant species. Proc. Natl Acad. Sci. USA 97, 10248–10253 (2000).
Griffith, J. S. Self Replication and scrapie. Nature 215, 1043–1044 (1967).
Alper, T., Cramp, W. A., Haig, D. A. & Clarke, M. C. Does the agent of scrapie replicate without nucleic acid? Nature 214, 764–766 (1967).
Prusiner, S. B. Prions. Proc. Natl Acad. Sci. USA 95, 13363–13383 (1998).
Telling, G. C. et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 83, 79–90 (1995).
Bolton, D. C., McKinley, M. P. & Prusiner, S. B. Identification of a protein that purifies with the scrapie prion. Science 218, 1309–1311 (1982).
Meyer, R. K. et al. Separation and properties of cellular and scrapie prion proteins. Proc. Natl Acad. Sci. USA 83, 2310–2314 (1986).
Gajdusek, D. C. Transmissible and non-transmissible amyloidoses: autocatalytic post-translational conversion of host precursor proteins to β-pleated sheet configurations. J. Neuroimmunol. 20, 95–110 (1988).
Come, J. H., Fraser, P. E. & Lansbury, P. T. J. A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc. Natl Acad. Sci. USA 90, 5959–5963 (1993).
Safar, J. et al. Eight prion strains have PrPSc molecules with different conformations. Nature Med. 4, 1157–1165 (1998).
Cronier, S. et al. Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin. Biochem. J. 416, 297–305 (2008).
Sandberg, M. K. et al. Prion neuropathology follows the accumulation of alternate prion protein isoforms after infective titre has peaked. Nature Commun. 5, 4347 (2014).
Fraser, H. & Dickinson, A. G. Scrapie in mice: agent-strain differences in the distribution and intensity of grey matter vacuolation. J. Comp. Pathol. 83, 29–40 (1973).
Bessen, R. A. & Marsh, R. F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68, 7859–7868 (1994).
Collinge, J., Sidle, K. C., Meads, J., Ironside, J. & Hill, A. F. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383, 685–690 (1996).
Telling, G. C. et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274, 2079–2082 (1996).
Bessen, R. A. et al. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375, 698–700 (1995).
Bruce, M. et al. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Phil. Trans. R. Soc. Lond. B 343, 405–411 (1994).
Prusiner, S. B. et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63, 673–686 (1990).
Collinge, J. et al. Unaltered susceptibility to BSE in transgenic mice expressing human prion protein. Nature 378, 779–783 (1995).
Collinge, J. Variant Creutzfeldt–Jakob disease. Lancet 354, 317–323 (1999).
Collinge, J. & Clarke, A. A general model of prion strains and their pathogenicity. Science 318, 930–936 (2007).
Wadsworth, J. D. et al. Human prion protein with valine 129 prevents expression of variant CJD phenotype. Science 306, 1793–1796 (2004).
Hill, A. F. et al. The same prion strain causes vCJD and BSE. Nature 389, 448–450 (1997).
Bruce, M. E. & Dickinson, A. G. Biological evidence that scrapie agent has an independent genome. J. Gen. Virol. 68, 79–89 (1987).
Kimberlin, R. H. & Walker, C. A. Evidence that the transmission of one source of scrapie agent to hamsters involves separation of agent strains from a mixture. J. Gen. Virol. 39, 487–496 (1978).
Polymenidou, M. et al. Coexistence of multiple PrPSc types in individuals with Creutzfeldt–Jakob disease. Lancet Neurol. 4, 805–814 (2005).
Yull, H. M. et al. Detection of type 1 prion protein in variant Creutzfeldt–Jakob disease. Am. J. Pathol. 168, 151–157 (2006).
Taylor, D. M., Fernie, K., McConnell, I. & Steele, P. J. Observations on thermostable subpopulations of the unconventional agents that cause transmissible degenerative encephalopathies. Vet. Microbiol. 64, 33–38 (1998).
Oelschlegel, A. M. & Weissmann, C. Acquisition of drug resistance and dependence by prions. PLoS Pathog. 9, e1003158 (2013).
Refs 37 and 91 demonstrate that prion populations or quasispecies can develop drug resistance rapidly through the selection of resistant conformers.
Solforosi, L. et al. Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 303, 1514–1516 (2004).
Hegde, R. S. et al. A transmembrane from of the prion protein in neurodegenerative disease. Science 279, 827–834 (1998).
Ma, J., Wollmann, R. & Lindquist, S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298, 1781–1785 (2002).
Chesebro, B. et al. Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308, 1435–1439 (2005).
Sonati, T. et al. The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein. Nature 501, 102–106 (2013).
Büeler, H. et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356, 577–582 (1992).
Mallucci, G. R. et al. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 21, 202–210 (2002).
Büeler, H. et al. Mice devoid of PrP are resistant to scrapie. Cell 73, 1339–1347 (1993).
Manson, J. C., Clarke, A., McBride, P. A., McConnell, I. & Hope, J. PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 3, 331–340 (1994).
Brandner, S. et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 379, 339–343 (1996).
Mallucci, G. et al. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 302, 871–874 (2003).
Collinge, J. et al. Kuru in the 21st century—an acquired human prion disease with very long incubation periods. Lancet 367, 2068–2074 (2006).
Race, R., Raines, A., Raymond, G. J., Caughey, B. & Chesebro, B. Long-term subclinical carrier state precedes scrapie replication and adaptation in a resistant species: analogies to bovine spongiform encephalopathy and variant Creutzfeldt–Jakob disease in humans. J. Virol. 75, 10106–10112 (2001).
Hill, A. F. & Collinge, J. Subclinical prion infection. Trends Microbiol. 11, 578–584 (2003).
Thackray, A. M., Klein, M. A., Aguzzi, A. & Bujdoso, R. Chronic subclinical prion disease induced by low-dose inoculum. J. Virol. 76, 2510–2517 (2002).
Thackray, A. M., Klein, M. A. & Bujdoso, R. Subclinical prion disease induced by oral inoculation. J. Virol. 77, 7991–7998 (2003).
Goedert, M. Alzheimer's and Parkinson's diseases: the prion concept in relation to assembled Aβ, tau, and α-synuclein. Science 349, 1255555 (2015).
Walsh, D. M. & Selkoe, D. J. A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration. Nature Rev. Neurosci. 17, 251–260 (2016).
A counterview to the extensive literature on prion-like mechanisms in neurodegeneration, which questions the role of propagating protein assemblies in pathogenesis and emphasises the role of selective neuronal vulnerability.
Fraser, H. & Dickinson, A. G. Targeting of scrapie lesions and spread of agent via the retino-tectal projection. Brain Res. 346, 32–41 (1985).
Vickery, C. M., Beck, K. E., Simmons, M. M., Hawkins, S. A. & Spiropoulos, J. Disease characteristics of bovine spongiform encephalopathy following inoculation into mice via three different routes. Int. J. Exp. Pathol. 94, 320–328 (2013).
Bruce, M. E., Fraser, H., McBride, P. A., Scott, J. R. & Dickinson, A. G. in Prion Diseases of Humans and Animals (eds Prusiner, S. B., Collinge, J., Powell, J. & Anderton, B.) Ch. 40 (Ellis Horwood, 1992).
Schmidt, C. et al. A systematic investigation of production of synthetic prions from recombinant prion protein. Open Biol. 5, 150165 (2015).
Salvadores, N., Shahnawaz, M., Scarpini, E., Tagliavini, F. & Soto, C. Detection of misfolded Aβ oligomers for sensitive biochemical diagnosis of Alzheimer's disease. Cell Rep. 7, 261–268 (2014).
A proof-of-principle adaptation of the protein misfolding cyclic amplification method to prions to amplify amyloid-β oligomers, which suggests the possibility of quantitative in vitro analysis of amyloid-β seeding activity.
Herva, M. E. et al. Anti-amyloid compounds inhibit α-synuclein aggregation induced by protein misfolding cyclic amplification (PMCA). J. Biol. Chem. 289, 11897–11905 (2014).
Diaz-Espinoza, R. & Soto, C. High-resolution structure of infectious prion protein: the final frontier. Nature Struct. Mol. Biol. 19, 370–377 (2012).
Requena, J. R. & Wille, H. The structure of the infectious prion protein: experimental data and molecular models. Prion 8, 60–66 (2014).
Jackson, G. S. et al. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science 283, 1935–1937 (1999).
Hornemann, S. & Glockshuber, R. A scrapie-like unfolding intermediate of the prion protein domain PrP(121–231) induced by acidic pH. Proc. Natl Acad. Sci. USA 95, 6010–6014 (1998).
Daude, N., Lehmann, S. & Harris, D. A. Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J. Biol. Chem. 272, 11604–11612 (1997).
Morillas, M., Vanik, D. L. & Surewicz, W. K. On the mechanism of α-helix to β-sheet transition in the recombinant prion protein. Biochemistry 40, 6982–6987 (2001).
Torrent, J. et al. High pressure induces scrapie-like prion protein misfolding and amyloid fibril formation. Biochemistry 43, 7162–7170 (2004).
Tattum, M. H. et al. Elongated oligomers assemble into mammalian PrP amyloid fibrils. J. Mol. Biol. 357, 975–985 (2006).
Collinge, J. et al. Transmission of fatal familial insomnia to laboratory animals. Lancet 346, 569–570 (1995).
Lasmézas, C. I. et al. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science 275, 402–405 (1997).
Legname, G. et al. Synthetic mammalian prions. Science 305, 673–676 (2004).
Deleault, N. R., Harris, B. T., Rees, J. R. & Supattapone, S. Formation of native prions from minimal components in vitro. Proc. Natl Acad. Sci. USA 104, 9741–9746 (2007).
Makarava, N. et al. Recombinant prion protein induces a new transmissible prion disease in wild-type animals. Acta Neuropathol. 119, 177 (2010).
Kim, J. I. et al. Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J. Biol. Chem. 285, 14083–14087 (2010).
Wang, F., Wang, X., Yuan, C. G. & Ma, J. Generating a prion with bacterially expressed recombinant prion protein. Science 327, 1132–1135 (2010).
Edgeworth, J. A. et al. Spontaneous generation of mammalian prions. Proc. Natl Acad. Sci. USA 107, 14402–14406 (2010).
Prusiner, S. B. et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349–358 (1983).
Safar, J. G. et al. Search for a prion-specific nucleic acid. J. Virol. 79, 10796–10806 (2005).
Silveira, J. R. et al. The most infectious prion protein particles. Nature 437, 257–261 (2005).
Caughey, B. & Lansbury, P. T., Jr. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267–298 (2003).
Kraus, A., Groveman, B. R. & Caughey, B. Prions and the potential transmissibility of protein misfolding diseases. Annu. Rev. Microbiol. 67, 543–564 (2013).
McKinley, M. P. et al. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65, 1340–1351 (1991).
Wenborn, A. et al. A novel and rapid method for obtaining high titre intact prion strains from mammalian brain. Sci. Rep. 5, 10062 (2015).
Terry, C. et al. Ex vivo mammalian prions are formed of paired double helical prion protein fibrils. Open Biol. 6, 160035 (2016).
Precise cell-culture-based prion infectivity assays were used to define the physical relationship between PrP rods and prion infectivity, and electron tomography was used to define their architecture.
Khalili-Shirazi, A. et al. PrP glycoforms are associated in a strain-specific ratio in native PrPSc. J. Gen. Virol. 86, 2635–2644 (2005).
Manson, J. C. et al. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol. Neurobiol. 8, 121–127 (1994).
Mallucci, G. R. et al. Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron 53, 325–335 (2007).
Hosszu, L. L. P. et al. Structural mobility of the human prion protein probed by backbone hydrogen exchange. Nature Struct. Biol. 6, 740–743 (1999).
Nicoll, A. J. et al. Pharmacological chaperone for the structured domain of human prion protein. Proc. Natl Acad. Sci. USA 107, 17610–17615 (2010).
Berry, D. B. et al. Drug resistance confounding prion therapeutics. Proc. Natl Acad. Sci. USA 110, E4160–E4169 (2013).
Enari, M., Flechsig, E. & Weissmann, C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc. Natl Acad. Sci. USA 98, 9295–9299 (2001).
Peretz, D. et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412, 739–743 (2001).
Antonyuk, S. V. et al. Crystal structure of human prion protein bound to a therapeutic antibody. Proc. Natl Acad. Sci. USA 106, 2554–2558 (2009).
White, A. R. et al. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422, 80–83 (2003).
Song, C. H. et al. Effect of intraventricular infusion of anti-prion protein monoclonal antibodies on disease progression in prion-infected mice. J. Gen. Virol. 89, 1533–1544 (2008).
Ohsawa, N. et al. Therapeutic effect of peripheral administration of an anti-prion protein antibody on mice infected with prions. Microbiol. Immunol. 57, 288–297 (2013).
Klyubin, I. et al. Peripheral administration of a humanized anti-PrP antibody blocks Alzheimer's disease Aβ synaptotoxicity. J. Neurosci. 34, 6140–6145 (2014).
Gajdusek, D. C., Gibbs, C. J. Jr & Alpers M. P. Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 209, 794–796 (1966).
Gibbs, C. J. Jr. et al. Creutzfeldt–Jakob disease (spongiform encephalopathy): transmission to the chimpanzee. Science 161, 388–389 (1968).
Brown, P. et al. Human spongiform encephalopathy: the National Institutes of Health series of 300 cases of experimentally transmitted disease. Ann. Neurol. 35, 513–529 (1994).
Baker, H. F., Ridley, R. M., Duchen, L. W., Crow, T. J. & Bruton, C. J. Induction of β(A4)-amyloid in primates by injection of Alzheimer's disease brain homogenate: comparison with transmission of spongiform encephalopathy. Mol. Neurobiol. 8, 25–39 (1994).
Refs 102 and 103 are important studies that demonstrate the seeding of amyloid-β pathology in the primate brain by intracerebral inoculation with tissue affected by AD.
Ridley, R. M., Baker, H. F., Windle, C. P., & Cummings, R. M. Very long term studies of the seeding of β-amyloidosis in primates. J. Neural Transm. 113, 1243–1251 (2006).
Gandy, S. Lifelong management of amyloid-β metabolism to prevent Alzheimer's disease. N. Engl. J. Med. 367, 864–866 (2012).
Benilova, I., Karran, E. & De Strooper, B. The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nature Neurosci. 15, 349–357 (2012).
Walsh, D. M. & Teplow, D. B. Alzheimer's disease and the amyloid β-protein. Prog. Mol. Biol. Transl. Sci. 107, 101–124 (2012).
Jan, A., Hartley, D. M. & Lashuel, H. A. Preparation and characterization of toxic Aβ aggregates for structural and functional studies in Alzheimer's disease research. Nature Protoc. 5, 1186–1209 (2010).
Kane, M. D. et al. Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice. J. Neurosci. 20, 3606–3611 (2000).
Meyer-Luehmann, M. et al. Exogenous induction of cerebral β-amyloidogenesis is governed by agent and host. Science 313, 1781–1784 (2006).
Stöhr, J. et al. Purified and synthetic Alzheimer's amyloid beta (Aβ) prions. Proc. Natl Acad. Sci. USA 109, 11025–11030 (2012).
Morales, R., Duran-Aniotz, C., Castilla, J., Estrada, L. D. & Soto, C. De novo induction of amyloid-β deposition in vivo. Mol. Psychiatry 17, 1347 (2012).
Eisele, Y. S. et al. Peripherally applied Aβ-containing inoculates induce cerebral β-amyloidosis. Science 330, 980–982 (2010).
Provides evidence to show that amyloid-β seeds can be transported from the abdomen to induce amyloid-β deposition in the CNS in a mouse model.
Clavaguera, F. et al. Peripheral administration of tau aggregates triggers intracerebral tauopathy in transgenic mice. Acta Neuropathol. 127, 299–301 (2014).
Prusiner, S. B. et al. Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism. Proc. Natl Acad. Sci. USA 112, E5308–E5317 (2015).
Ward, H. J. et al. Sporadic Creutzfeldt–Jakob disease and surgery: a case-control study using community controls. Neurology 59, 543–548 (2002).
Mahillo-Fernandez, I. et al. Surgery and risk of sporadic Creutzfeldt–Jakob disease in Denmark and Sweden: registry-based case-control studies. Neuroepidemiology 31, 229–240 (2008).
Jaunmuktane, Z. et al. Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy. Nature 525, 247–250 (2015).
A report of the possible iatrogenic transmission of amyloid-β pathology and CAA many years after treatment with pituitary extracts derived from cadavers.
Irwin, D. J. et al. Evaluation of potential infectivity of Alzheimer and Parkinson disease proteins in recipients of cadaver-derived human growth hormone. JAMA Neurol. 70, 462–468 (2013).
Frontzek, K., Lutz, M. I., Aguzzi, A., Kovacs, G. G. & Budka, H. Amyloid-β pathology and cerebral amyloid angiopathy are frequent in iatrogenic Creutzfeldt–Jakob disease after dural grafting. Swiss Med. Wkly. 146, w14287 (2016).
Refs 119 and 120 provide evidence that amyloid-β pathology and CAA might also be iatrogenically transmitted to humans through neurosurgical procedures involving dura mater grafts.
Kovacs, G. G. et al. Dura mater is a potential source of Aβ seeds. Acta Neuropathol. 131, 911–23 (2016).
Brandner, S. et al. Central and peripheral pathology of kuru: pathological analysis of a recent case and comparison with other forms of human prion disease. Phil. Trans. R. Soc. B 363, 3755–3763 (2008).
Wadsworth, J. D. et al. Tissue distribution of protease resistant prion protein in variant CJD using a highly sensitive immuno-blotting assay. Lancet 358, 171–180 (2001).
Urwin, P. J., Mackenzie, J. M., Llewelyn, C. A., Will, R. G. & Hewitt, P. E. Creutzfeldt–Jakob disease and blood transfusion: updated results of the UK Transfusion Medicine Epidemiology Review Study. Vox Sang. 110, 310–116 (2016).
Haley, N. J. & Hoover, E. A. Chronic wasting disease of cervids: current knowledge and future perspectives. Annu. Rev. Anim. Biosci. 3, 305–325 (2014).
Petkova, A. T. et al. Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils. Science 307, 262–265 (2005).
Clavaguera, F. et al. Brain homogenates from human tauopathies induce tau inclusions in mouse brain. Proc. Natl Acad. Sci. USA 110, 9535 (2013).
Guo, J. L. et al. Distinct α-synuclein strains differentially promote tau inclusions in neurons. Cell 154, 103–117 (2013).
Bousset, L. et al. Structural and functional characterization of two α-synuclein strains. Nature Commun. 4, 2575 (2013).
Heilbronner, G. et al. Seeded strain-like transmission of β-amyloid morphotypes in APP transgenic mice. EMBO Rep. 14, 1017–1022 (2013).
Lu, J. X. et al. Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell 154, 1257–1268 (2013).
A molecular structural model for amyloid-β40 fibrils seeded from the brains of two people with AD, which suggests that fibrils in the brain might spread from a single site of nucleation and that structural variations in fibrils might correlate with variations in AD phenotype.
Cohen, M. L. et al. Rapidly progressive Alzheimer's disease features distinct structures of amyloid-β. Brain 138, 1009–1022 (2015).
Watts, J. C. et al. Serial propagation of distinct strains of Aβ prions from Alzheimer's disease patients. Proc. Natl Acad. Sci. USA 111, 10323–10328 (2014).
Wadsworth, J. D., Asante, E. A. & Collinge, J. Contribution of transgenic models to understanding human prion disease. Neuropathol. Appl. Neurobiol. 36, 576–597 (2010).
Asante, E. A. et al. Transmission properties of human PrP 102L prions challenge the relevance of mouse models of GSS. PLoS Pathog. 11, e1004953 (2015).
Scheltens, P. et al. Alzheimer's disease. Lancet 388, 10–6736 505–517 (2016).
Hatami, A., Albay, R. III, Monjazeb, S., Milton, S. & Glabe, C. Monoclonal antibodies against Aβ42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain. J. Biol. Chem. 289, 32131–32143 (2014).
Labbadia, J. & Morimoto, R. I. The biology of proteostasis in aging and disease. Annu. Rev. Biochem. 84, 435–464 (2015).
Tjernberg, L. O., Rising, A., Johansson, J., Jaudzems, K. & Westermark, P. Transmissible amyloid. J. Intern. Med. 280, 153–163 (2016).
Mead, S. et al. Clinical trial simulations based on genetic stratification and the natural history of a functional outcome measure in Creutzfeldt–Jakob disease. JAMA Neurol. 73, 447–455 (2016).
Edgeworth, J. A. et al. Detection of prion infection in variant Creutzfeldt–Jakob disease: a blood-based assay. Lancet 377, 487–493 (2011).
Sawyer, E. B., Edgeworth, J. A., Thomas, C., Collinge, J. & Jackson, G. S. Preclinical detection of infectivity and disease-specific PrP in blood throughout the incubation period of prion disease. Sci Rep. 5, 17742 (2015).
Gill, O. N. et al. Prevalent abnormal prion protein in human appendixes after bovine spongiform encephalopathy epizootic: large scale survey. Br. Med. J. 347, f5675 (2013).
A study of more than 30,000 archived surgical appendix samples that searched for evidence of vCJD prion infection; it suggested that about 1 in 2,000 of the UK population might be infected.
Eisele, Y. S. et al. Induction of cerebral β-amyloidosis: intracerebral versus systemic Aβ inoculation. Proc. Natl Acad. Sci. USA 106, 12926–12931 (2009).
House of Commons Science and Technology Committee. After the storm? UK blood safety and the risk of variant Creutzfeldt–Jakob disease http://www.publications.parliament.uk/pa/cm201415/cmselect/cmsctech/327/327.pdf (House of Commons Science and Technology Committee, 2014).