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Published: 4 June 2021

Last updated: 14 March 2023

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1

Hill, Andrew F., ed. Prion Protein Protocols. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-234-2.

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2

Zhang, Jiapu. Molecular Dynamics Analyses of Prion Protein Structures. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8815-5.

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3

Fatal flaws: How a misfolded protein baffled scientists and changed the way we look at the brain. New Haven: Yale University Press, 2013.

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4

Fatal flaws: How a misfolded protein baffled scientists and changed the way we look at the brain. Toronto, Ont: HarperCollins, 2012.

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5

Ridley, Rosalind M. Fatal protein: The story of CJD, BSE, and other prion diseases. Oxford: Oxford University Press, 1998.

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6

Silverman, Gregory Lindsay. Identification and characterization of proteins binding to the amino-terminus of the human prion protein. Ottawa: National Library of Canada, 1999.

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7

The pathological protein: Mad Cow, Chronic Wasting, and other deadly prion diseases. New York: Copernicus, 2003.

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8

Loftus, Brendan. Analysis of the prion protein (PrP) and PrP genes from Ovis aries and Oryctalagus cuniculus. Dublin: University College Dublin, 1996.

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9

Dr, Soto Claudio, ed. Prions: The new biology of proteins. Boca Raton, FL: CRC/Taylor & Francis, 2006.

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10

Tatzelt, Jörg, ed. Prion Proteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-24067-6.

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11

Winslow, Caughey Byron, ed. Prion proteins. San Diego: Academic Press, 2001.

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12

service), SpringerLink (Online, ed. Prion Proteins. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2011.

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13

Prion biology: Research and advances. Toronto: Apple Academic Press, 2013.

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14

Andrey, Kajava, Squire John 1945-, and Parry David A. D, eds. Fibrous proteins: Amyloids, prions and beta proteins. Amsterdam: Elsevier, 2006.

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15

Zhang, Jiapu. Molecular Structures and Structural Dynamics of Prion Proteins and Prions. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-017-7318-8.

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16

O, Chernoff Yury, ed. Protein-based inheritance. Austin: Landes Bioscience, 2007.

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17

Ronald, Wetzel, ed. Amyloid, prions, and other protein aggregates. San Diego, CA: Academic Press, 1999.

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18

Astrid, Sigel, Sigel Helmut, and Sigel Roland K. O, eds. Neurodegenerative diseases and metal ions. Chichester, West Sussex, England: Wiley, 2006.

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19

Chernoff, Yury O. Protein-based inheritance. Austin, Tex: Landes Bioscience, 2007.

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20

Zou, Wen-Quan, and Pierluigi Gambetti. Prions and diseases. New York: Springer, 2013.

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21

Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part B. Amsterdam: Elsevier/Academic, 2006.

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22

Indu, Kheterpal, and Wetzel Ronald, eds. Amyloid, prions, and other protein aggregates Part C. Amsterdam: Elsevier/Academic, 2006.

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23

Arthur, M. Sackler Colloquia of the National Academy of Sciences (2002 Washington D. C. ). Self-perpetuating structural states in biology, disease, and genetics. Washington, D.C: National Academy of Sciences, 2002.

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24

Gerbe, Suzanne. Un automne à la prison de Montluc. Paris: Harmattan, 2003.

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25

Legname, Giuseppe, and Silvia Vanni. Prion Protein. Elsevier Science & Technology Books, 2017.

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26

Prion Protein. Elsevier, 2017. http://dx.doi.org/10.1016/s1877-1173(17)x0007-0.

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27

Legname, Giuseppe, and Silvia Vanni. Prion Protein. Elsevier Science & Technology Books, 2017.

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28

F, Hill A., ed. Prion protein protocols. Totowa, N.J: Humana, 2008.

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29

The Prion Protein. Caister Academic Press, 2010. http://dx.doi.org/10.21775/9781912530076.

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30

Hill, Andrew F. Prion Protein Protocols. Humana Press, 2010.

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31

Caughey, Byron. Advances in Protein Chemistry, Volume 57: Prion Proteins (Advances in Protein Chemistry). Academic Press, 2001.

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32

Caughey, Byron. Advances in Protein Chemistry, Volume 57: Prion Proteins (Advances in Protein Chemistry). Academic Press, 2001.

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33

Yam, Philip. The Pathological Protein. Copernicus, 2013.

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34

Hope, James, and Mark P. Dagleish. Prion-protein-related diseases of animals and man. Oxford University Press, 2011. http://dx.doi.org/10.1093/med/9780198570028.003.0041.

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Scrapie, bovine spongiform encephalopathy (BSE), Creutzfeldt–Jakob disease (CJD), and related diseases of mink (transmissible mink encephalopathy), mule deer and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE). These diseases can be transmitted by prions from affected to healthy animals by inoculation or by feeding diseased tissues. Prions are cellular proteins that can transfer metabolic and pathological phenotypes vertically from parent to progeny or horizontally between cells and animals. TSEs are characterised by the accumulation of the prion form of the mammalian prion protein (PrPC) in the central nervous system or peripheral tissues of animals and humans. Mutations of the human PrP gene are linked to rare, familial forms of disease and prion-protein gene polymorphisms in humans and other species are linked to survival time and disease characteristics in affected individuals. Iatrogenic transmission of CJD in man has occurred, and a variant form of CJD (vCJD) is due to cross-species transmission of BSE from cattle to humans. Atypical forms of scrapie and BSE have been identified during large-scale monitoring for TSEs worldwide. This chapter outlines our current understanding of scrapie, BSE, CJD and other TSEs and highlights recent progress in defining the role in disease of the prion protein, PrP.

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35

Ingram, Jay, and Lin Tang. Fatal Flaws: How a Misfolded Protein Baffled Scientists and Changed the Way We Look at the Brain. Yale University Press, 2013.

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36

Safar, Jiri G. Prion Paradigm of Human Neurodegenerative Diseases Caused by Protein Misfolding. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0005.

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Data accumulated from different laboratories argue that a growing number of proteins causing neurodegeneration share certain characteristics with prions. Prion-like particles were produced from synthetic amyloid beta (Aβ‎) peptides of Alzheimer’s disease (AD), from recombinant α‎-synuclein linked to Parkinson’s disease (PD), and from recombinant tau associated with frontotemporal dementias (FTD). Evidence from human prions reveals that variable disease phenotypes, rates of propagation, and targeting of different brain structures are determined by distinct conformers (strains) of pathogenic prion protein. Recent progress in the development of advanced biophysical tools identified the structural characteristics of Aβ‎ in the brain cortex of phenotypically diverse AD patients and thus allowed an investigation of the prion paradigm of AD. The findings of distinctly structured strains of human brain Aβ‎, forming a unique spectrum of oligomeric particles in the cortex of rapidly progressive cases, implicates these structures in variable rates of propagation in the brain.

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37

Mastrianni, James A., and Joshuae G. Gallardo. Prion Diseases. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0166.

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Prion diseases are transmissible fatal neurodegenerative disorders resulting from the accumulation of misfolded prion protein. Although primarily sporadic diseases, 5% to 10% result from a mutation of the prion protein gene (PRNP), and less than 1% occur from exposure to prions. The current family of prion diseases includes Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker disease (GSS), fatal insomnia (FI), variant CJD (vCJD), and variably protease-sensitive prionopathy (VPSPr). Kuru is a disease of historical interest that was transmitted through cannibalistic rituals. Iatrogenic CJD (iCJD) is the result of secondary transmission of prion disease from contaminated biologicals.

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38

Mouillet-Richard, Sophie, and Jean-Luc Vilotte, eds. Promiscuous Functions of the Prion Protein Gene Family. Frontiers Media SA, 2015. http://dx.doi.org/10.3389/978-2-88919-605-0.

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39

Ingram, Jay. Fatal Flaws: How a Misfolded Protein Baffled Scientists and Changed the Way We Look at the Brain. Yale University Press, 2013.

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40

Zhang, Jiapu. Molecular Dynamics Analyses of Prion Protein Structures: The Resistance to Prion Diseases Down Under. Springer, 2018.

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41

Zhang, Jiapu. Molecular Dynamics Analyses of Prion Protein Structures: The Resistance to Prion Diseases Down Under. Springer, 2018.

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42

(Editor), Johannes Buchner, and Thomas Kiefhaber (Editor), eds. Protein Folding Handbook 5-volume set. Wiley-VCH, 2005.

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43

Knight, Richard. Prion disease. Edited by Patrick Davey and David Sprigings. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199568741.003.0319.

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Prion diseases (also known as transmissible spongiform encephalopathies (TSEs)) affect animals and humans, although only the human diseases will be discussed in this chapter. Despite TSEs having somewhat disparate causes and effects, there are unifying features: TSEs are brain diseases with neurodegenerative pathology, which is typically associated with spongiform change, and, most characteristically, there is tissue deposition of an abnormal structural form of the prion protein. Some of the TSEs are naturally acquired infections and, while others are not, they are potentially transmissible in certain circumstances.

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44

Cellular Prion Protein - at the Crossroads of Prion Diseases and Other Amyloid Neurodegenerative Diseases [Working Title]. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.77814.

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45

Ridley, Rosalind M., and Harry F. Baker. Fatal Protein: The Story of Cjd, Bse and Other Prion Diseases. Oxford University Press, 1997.

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46

Yam, Philip. Pathological Protein: Mad Cow, Chronic Wasting, and Other Deadly Prion Diseases. Springer, 2007.

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47

Yam, Philip. The Pathological Protein: Mad Cow, Chronic Wasting, and Other Deadly Prion Diseases. Springer, 2003.

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48

Soto, Claudio. Prions: The New Biology of Proteins. Taylor & Francis Group, 2005.

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49

Soto, Claudio. Prions: The New Biology of Proteins. Taylor & Francis Group, 2005.

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50

Soto, Claudio. Prions: The New Biology of Proteins. Taylor & Francis Group, 2006.

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