Review: The prion and its potentiality

Biomedical Research

Volumn 21, Issue 2, 2010, Pages 111-125

  Pandeya, Dipendra Raj ^a   Acharya, Nimish K ^b   Hong, Seong Tshool ^a  

^a Chonbuk National University Medical School   (South Korea)

^b UNIVERSITY OF MEDICINE AND DENTISTRY OF NEW JERSEY   (United States)

Author keywords

Bovine spongiform encephalopathy; Neurodegeneration; Prion; Prion diseases

Indexed keywords

ACRIDINE DERIVATIVE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BASIC FIBROBLAST GROWTH FACTOR; CHLORPROMAZINE; CONGO RED; CURCUMIN; DEXTRAN DERIVATIVE; DEXTRAN SULFATE; DIMETHYL SULFOXIDE; GLYCAN DERIVATIVE; GLYCOSAMINOGLYCAN; GROWTH FACTOR; HEPARIN DERIVATIVE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; ISOPROTEIN; MEPACRINE; MEVINOLIN; OLIGONUCLEOTIDE; PENTOSAN POLYSULFATE; PHTHALOCYANINE DERIVATIVE; POLYENE ANTIBIOTIC AGENT; PORPHYRIN DERIVATIVE; PRION PROTEIN; PROTEIN DERIVATIVE; QUININE; QUINOLINE; SQUALESTATIN; TETRAPYRROLE DERIVATIVE; UNINDEXED DRUG;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; AMYOTROPHIC LATERAL SCLEROSIS; ANIMAL DISEASE; ANIMAL HEALTH; BINDING SITE; BOVINE SPONGIFORM ENCEPHALOPATHY; CENTRAL NERVOUS SYSTEM INFECTION; COGNITIVE DEFECT; CREUTZFELDT JAKOB DISEASE; DEGENERATIVE DISEASE; DISEASE ACTIVITY; DRUG MECHANISM; FRONTOTEMPORAL DEMENTIA; HUMAN; INFECTION SENSITIVITY; MOTOR DYSFUNCTION; NONHUMAN; NUCLEOTIDE SEQUENCE; PARKINSON DISEASE; PATHOGENESIS; PHYSICAL CHEMISTRY; PRION; PRION DISEASE; PROTEIN BINDING; PROTEIN DEFECT; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; REVIEW; SCRAPIE; VIRUS INFECTIVITY; VIRUS STRAIN;

ANIMALIA; BOVINAE; MAMMALIA;

EID: 77956242339     PISSN: 0970938X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (131)

1. Zigas V. Kuru in New Guinea: Discovery and Epide-miology. Am J Trop Med Hyg. 1970; 19:130-132.
2. Liberski PP, Gajdusek DC. Kuru: forty years later, a historical note. Brain Pathol.1997; 7: 555-560.
3. Williams ES, Youn S. Chronic wasting disease of cap-tive mule deer; a spongiform encephalopathy. J Wildl. Dis 1980; 16: 89-98.
4. Guiroy DC, Williams ES, Yanagihara R. Gajdusek, DC. Immunolocalization of scrapie amyloid (PrP27-30) in chronic wasting disease of Rocky Mountain elk and hybrids of captive mule deer and white-tailed deer. Neurosci Lett 1991; 27: 195-198.
5. Aguzzi A, Polymenidou M. Mammalian prion biology: one century of evolving concepts. Cell 2004; 116:313-327.
6. Ross ED, Minton A, Wickner RB. Prion domains: seq-uences, structures and interactions. Nat Cell Biol 2005b; 7: 1039-1044.
7. Shkundina IS, Ter-Avanesyan MD. Prions. Biochemis-try 2007; 72: 1519-1536.
8. Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Natl Rev 2005; 6: 435-450.
9. Sparrer HE, Santoso A, Szoka FC, Weissman Jr, Weissman JS. Evidence for the prion hypothesis: in-duction of the yeast [PSI+] factor by in vitro- converted Sup35 protein. Science 2000; 289: 595-599.
10. Inge-Vechtomov SG, Zhouravleva GA, Chernoff YO. Biological roles of prion domains. Prion 2007; 1: 228-235.
11. Wickner RB, Edskes HK, Shewmaker F, Nakayashiki T. Prions of fungi: inherited structures and biological roles. Nature Rev. Microbiol 2007; 5: 611-618.
12. Prusiner SB. Prion diseases and the BSE crisis. Science 1997; 278: 245-251.
13. Prusiner SB. Prion Biology and Diseases. Cold Spring Harbor Laboratory Press, New York Cold 2003; 6: pp. 1-800.
14. Prusiner SB, Scott MR, DeArmond SJ, Cohen FE. Pri-on protein biology. Cell 1998; 93: 337-348.
15. Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosc 2001; 24: 519-550.
16. Tanaka M, Chien P, Yonekura K, Weissman JS. Mech-anism of cross-species prion transmission: An infec-tious conformation compatible with two highly diver-gent yeast prion proteins. Cell 2005; 121: 49-62.
17. Medori R, Tritschler HJ, LeBlanc A, Villare F, Manetto V, Chen, HY. Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene. N Engl J Med 1992; 326: 444-449.
18. Deriziotis P, Tabrizi SJ. Prions and the proteasome Biochim Biophys Acta 2008; 1782: 713-722.
19. Aguzzi A, Weissmann C. Prion research: the next fron-tiers. Nature 1997; 389: 795-798.
20. Alper T, Cramp WA, Haig DA, Clarke, MC. Does the agent of scrapie replicate without nucleic acid? Nature 1967; 214: 764-766.
21. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216: 136-144.
22. Dickinson AG, Outram GW. The scrapie replication-site hypothesis and its implications for pathogenesis. Academic Press, NY. In Slow transmissible diseases of the central nervous system 1979; 2: 13-31.
23. Gibbs CJ Jr, Gajdusek DC, Latarjet R. Unusual resis-tance to ionizing radiation of the viruses of kuru, Creutzfeldt-Jakob disease. Proc. Natl. Acad. Sci. USA 1978; 75: 6268-6270.
24. Levine P. Scrapie: an infective polypeptide? Lancet 1972; 1: 748-749.
25. Anonymous. Scrapie: strategies, stalemates, and suc-cesses. Lancet 1982; 1: 1221-1223.
26. Kimberlin R. Scrapie agent: Prions or virinos? Nature 1982; 297: 107-108.
27. Somerville RA. The transmissible agent causing scra-pie must contain more than protein. Rev Med Virol 1991; 1: 131-139.
28. Kocisko DA, Come JH, Priola SA, Chesebro B, Ray-mond GJ, Lansbury PT, et al. Cell-free formation of protease-resistant prion protein. Nature 1994 370: 471-474.
29. Prusiner SB, Bolton DC, Groth DF, Bowman KA, Cochran P, McKinley MP. Further purification and characterization of scrapie prions. Biochemistry 1982; 21: 6942- 6950.
30. Prusiner SB. Prions. Proc. Natl Acad Sci USA 1998; 95: 13363-13383.
31. Borchelt DR, Scott M, Taraboulos A, Stahl N, Prusiner SB. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J Cell Biol 1990; 110: 743-752.
32. Caughey B, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS. Secondary structure analysis of the scra-pie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991; 30: 7672-7680.
33. Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993; 90: 10962-10966.
34. Stahl N, Baldwin MA, Teplow DB, Hood L, Gibson GW, Burlingame AL, et al. Structural studies of the scrapie prion protein using mass spectrometry and ami-no acid sequencing. Biochemistry 1993; 32: 1991-2002.
35. Safar J, Roller PP, Gajdusek DC, Gibbs CJ. Conforma-tional transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J Biol Chem 1993; 268: 202-76-20284.
36. Prusiner SB. Shattuck Lecture: Neurodegenerative dis-eases and prions. N Engl J Med 2001; 344: 1516-1526.
37. Donne DG, Viles JH, Groth D, Mehlhorn I, James TL, Cohen FE, et al. Structure of the recombinant full-length hamster prion protein PrP (29-231): the N termi-nus is highly flexible. Proc Natl Acad Sci USA 1997; 94: 13452-13457.
38. Riek R, Hornemann S, Wider G, Billeter M, Glock-shuber R, Wuthrich K. NMR structure of the mouse prion protein domain PrP (121-231). Nature 1996; 382: 180-182.
39. Moser M, Colello RJ, Pott U, Oesch B. Developmental expression of the prion protein gene in glial cells. Neu-ron 1995, 14: 509-517.
40. Caughey B, Race RE, Chesebro, B. Detection of prion protein mRNA in normal and scrapie-infected tissues and cell lines. J Gen Virol 1988; 69: 711-716.
41. Dodelet VC, Cashman NR. Prion protein expression in human leukocyte differentiation. Blood 1998; 91: 1556-1561.
42. Ford MJ, Burton LJ, Li H, Graham CH, Frobert Y, Grassi J, et al. A marked disparity between the expres-sion of prion protein and its message by neurones of the CNS. Neuroscience 2002; 111: 533-551.
43. C. Br. Med. Bull 2003; 66: 61-70.
44. Manson J, West JD, Thomson V, McBride P, Kaufman MH, Hope J. The prion protein gene: a role in mouse embryogenesis? Development 1992; 115: 117-122.
45. Aguzzi A, Baumann F, Bremer J. The prion's elusive reason for being. Annu Rev Neurosci 2008; 31: 439-477.
46. Collinge J, Whittington MA, Sidle KC, Smith CJ, Palmer MS, Clarke AR, et al. Prion protein is necessary for normal synaptic function. Nature 1994; 370: 295- 297.
47. Herms J, Tings T, Gall S, Madlung A, Giese A, Siebert H, et al. Evidence of presynaptic location and function of the prion protein. J Neurosci 1999; 19: 8866-8875.
48. Moore RC, Lee IY, Silverman GL, Harrison PM, Strome R, Heinrich C, et al. Ataxia in prion protein de-ficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Bio 1999; 292: 797-817.
49. Brown DR, Besinger A. Prion protein and superoxide dismutase activity. Biochemical Journal 1998; 334: 423-429.
50. Aronoff-Spencer E, Burns CS, Avdievich, NI, Gerfen, GJ, Peisach J, Antholine WE, et al. Identification of the Cu21 binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy. Biochem-istry 2000; 39: 13760-13771.
51. Jackson GS, Murray I, Hosszu LL, Gibbs N, Waltho JP, Clarke AR, et al. Location and properties of metal-binding sites on the human prion protein. Proc Natl Acad Sci USA 2001; 98: 8531-8535.
52. Pauly PC, Harris DA. Copper stimulates endocytosis of the prion protein. J Biol Chem 1998; 273: 33107-33110.
53. Perera WS, Hooper NM. Ablation of the metal ion in-duced endocytosis of the prion protein by disease-associated mutation of the octarepeat region. Curr Biol 2001; 11: 519-523.
54. Brown DR. Normal protein and the synapse. Trends Neurosci 2001; 24: 85-90.
55. McLennan NF, Brennan PM, McNeill A, Davies I, Fotheringham A, Rennison KA, et al. Prion protein ac-cumulation and neuroprotection in hypoxic brain dam-age. Am J Pathol 2004; 165: 227-235.
56. Spudich A, Frigg R, Kilic E, Kilic U, Oesch B, Raeber A, et al. Aggravation of ischemic brain injury by prion protein deficiency: role of ERK-1/-2 and STAT-1. Neu-robiol Dis 2005; 20: 442-449.
57. Chiarini LB, Freitas AR, Zanata SM, Brentani RR, Martins VR, Linden R. Cellular prion protein transdu-ces neuroprotective signals. EMBO J 2002; 21: 3317 -3326.
58. Zhang CC, Steele AD, Lindquist S, Lodish HF. Prion protein is expressed on long-term repopulating hemato-poietic stem cells and is important for their self renewal. Proc Natl Acad Sci USA 2006; 103: 2184-2189.
59. Masel J, Jansen V AA, Nowak MA. Quantifying the kinetic parameters of prion replication. Biophys Chem 1999; 77: 139-152.
60. Hill AF, Zeidler M, Ironside J, Collinge J. Diagnosis of new variant Creutzfeldt-Jakob disease by tonsil biopsy. Lancet 1997; 349: 99-100.
61. Kitamoto T, Muramoto T, Mohri S, Dohura K, Tateishi J. Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeld-Jakob disease. J Virol 1991; 65: 6292-6295.
62. Mabbott NA, MacPherson GG. Prions and their lethal journey to the brain. Nat Rev Microbiol 2006; 4: 201-211.
63. Gerdes HH. Prions tunnel between cells. Nature cell biology 2009; 11: 235-236.
64. Gousset K, Schiff E, Langevin C, Marijanovic Z, Ca-puto A, Browman DT, et al. Prions hijack tunnelling nanotubes for intercellular spread. Nature Cell Biology 2009; 11: 328-336.
65. Radebold K, Chernyak M, Martin D, Manuelidis L. Blood-borne transit of CJD from brain to gut at early stages of infection. BMC Infect Dis 2001; 1: 20.
66. Bons N, Lehmann S, Mestre-Frances N, Dormont D, Brown P. Brain and buffy coat transmission of bovine spongiform encephalopathy to the primate Microcebus murinus. Transfusion 2002; 42: 513-516.
67. Holada K, Simak J, Vostal JG. Transmission of BSE by blood transfusion. Lancet 2000; 356: 999-1000.
68. Klein MA, Kaeser PS, Schwarz P, Weyd H, Xenarios I, Zinkernagel RM, et al. Compliment facilitates early prion pathogenesis. Nat Med 2001; 7: 488-492.
69. Gregori L, McCombie N, Palmer D, Birch P, Sowemi-mo-Coker SO, Giulivi A, et al. Effectiveness of leu-coreduction for removal of infectivity of transmissible spongiform encephalopathies from blood. Lancet 2004; 264: 529-531.
70. Sigurdsson B. Rida a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics. Br Vet J 1954; 110: 341-354.
71. Chandler RL. Encephalopathy in mice produced by inoculation with scrapie brain material. Lancet 1961; 1: 1378-1379.
72. Gordon WS. Advances in veterinary research. Vet Rec 1946; 58: 516-520.
73. Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science 1982; 218: 1309-1311.
74. Prusiner SB, McKinley MP, Groth DF, Bowman KA, Mock NI, Cochran SP, et al. Scrapie agent contains a hydrophobic protein. Proc Natl Acad Sci USA 1981; 78: 6675-6679.
75. Prusiner SB, Bolton DC, Groth DF, Bowman KA, Cochran P, McKinley MP. Further purification and characterization of scrapie prions. Biochemistry 1982; 21: 6942-6950.
76. Ratte S, Prescott SA, Collinge J, Jefferys JG. Hippo-campal bursts caused by changes in NMDA receptor-dependent excitation in a mouse model of variant CJD. Neurobiol Dis 2008; 32: 96-104.
77. LaCasse RA, Striebel JF, Favara C, Kercher L, Chese-bro B. Role of Erk1/2 activation in prion disease patho-genesis: Absence of CCR1 leads to increased Erk1/2 activation and accelerated disease progression. J. Neu-roimmunol 2008; 196: 16-26.
78. Bruce ME. TSE strain variation. Br. Med. Bull 2003; 66: 99-108.
79. Dickinson A, Fraser H, Outram G. Scrapie incubation time can exceed natural lifespan. Nature 1976; 256: 732-733.
80. Scott M, Groth D, Foster D, Torchia M, Shu-Lian Y, DeArmond SJ, et al. Propagation of prions with artifi-cial properties in transgenic mice expressing chimeric PrP genes. Cell 1993; 73: 979-988.
81. Telling GC, Scott M, Mastrianni J, Gabizon R, Torchia M, Cohen FE, et al. Prion propagation in mice express-ing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995; 83: 79-90.
82. Manson JC, Jamieson E, Baybutt H, Tuzi NL, Barron R, McConnell I, et al. A single amino acid alteration (101) introduced into murine PrP dramatically alters incuba-tion time of transmissible spongiform encephalopathy. EMBO J 1999; 18: 6855-6864.
83. Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev. Neurosc 2001; 24: 519-550.
84. Scott MR, Safar J, Telling G, Nguyen O, Groth D, Tor-chia M, et al. Identification of a prion protein epitope modulating transmission of bovine spongiform en-cephalopathy prions to transgenic mice. Proc Natl Acad Sci USA 1997; 94: 14279-14284.
85. Bruce M, Chree A, McConnell I, Foster J, Pearson G, Fraser H. Transmission of bovine spongiform encepha-lopathy and scrapie to mice: strain variation and the species barrier. Phil Trans R Soc Lon 1994; 343: 405-411.
86. Pattison IH, Millson GC. Experimental transmission of scrapie to goats and sheep by the oral route. J Comp Pathol 1961; 71: 171-176.
87. Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. Structural clues to prion replication. Science 1994; 264: 530-531.
88. Bartz JC, Bessen RA, McKenzie D, Marsh RF, Aiken JM. Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathy. J Virol 2000; 74: 5542-5547.
89. c replication in vitro generates unique infectious prions.Cell 2008; 134: 757-768.
90. Morales R, Abid K, Soto C. The prion strain phenome-non: Molecular basis and unprecedented features. Bio-chim. Biophys Acta 2007; 1772: 681-691.
91. Oesch B, Teplow DB, Stahl N, Serban D, Hood LE, Prusiner SB. Identification of cellular proteins binding to the scrapie prion protein. Biochemistry 1990; 29: 5848-5855.
92. ccauses nerve cell death and stimulates astrocyte proliferation: a paradox. Prog Brain Res 1992; 94: 437-446.
93. Yehiely F, Bamborough P, Da Costa M, Perry BJ, Thi-nakaran G, Cohen FE, et al. Identification of candidate proteins binding to prion protein. Neurobiol Dis 1997; 3: 339-355.
94. Kurschner C, Morgan JI. Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and cellular prion protein. Brain Res. Mol Brain Res 1996; 37: 249-258.
95. Edenhofer F, Rieger R, Famulok M, Wendler W, Weiss S, Winnacker EL. Prion protein PrPc interacts with molecular chaperones of the Hsp60 family. J Virol 1996; 70: 4724-4728.
96. Rieger R, Edenhofer F, Lasmézas CI, Weiss S. The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat Med 1997; 3: 1383-1388.
97. c directly interacts with proteins involved in signaling pathways. J Biol.Chem 2001; 276: 44604-44612.
98. Shyu WC, Harn HJ, Saeki K, Kubosaki A, Matsumoto Y, Onodera T, et al. Molecular modulation of expres-sion of prion protein by heat shock. Mol. Neurobiol 2002; 26: 1-12.
99. Graner E, Mercadante AF, Zanata SM, Forlenza OV, Cabral AL, Veiga SS, et al. Cellular prion protein binds laminin and mediates neuritogenesis. Brain res. Mol Brain Res 2000; 76: 85-92.
100. Schmitt-Ulms G, Legname G, Baldwin MA, Ball HL, Bradon N, Bosque PJ, et al. Binding of neural cell ad-hesion molecules (N-CAMs) to the cellular prion pro-tein. J Mol Biol 2001; 314: 1209-1225.
101. Gauczynski S, Peyrin JM, Haik S, Leucht C, Hundt C, Rieger R, et al. The 37KDa/67KDa Laminin receptor acts as the cell surface receptor for the cellular prion protein. EMBO J 2001; 20: 5863-5875.
102. Priola SA, Caughey B. Inhibition of scrapie-associated PrP accumulation - probing the role of glycosami-noglycans in amyloidogenesis. Mol Neurobiol 1994; 8: 113-120.
103. Zanta SM, Lopes MH, Mercadante AF, Hajj GN, Chi-arini LB, Nomizo R, et al. Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neu-roprotection. EMBO J 2002; 21: 3307-3316.
104. Caughey B, Baron GS. Prions and their partners in crime. Nature 2006; 443: 803-810.
105. Toni M, Spisni E, Griffoni C, Santi S, Riccio M, Lenaz P, et al. Cellular Prion Protein and Caveolin-1 Interac-tion in a Neuronal Cell Line Precedes Fyn/Erk 1/2 Sig-nal Transduction. J Biomed Biotechnol 2006; 2006: 1-13.
106. Maissen M, Roecki C, Glatzel M, Goldmann W, Aguz-zi A. Plasminogen binds to disease associated prion protein of multiple species. Lancet; 2001; 357: 2026-2028.
107. DeArmond SJ. Alzheimer's disease and CJD: overlap of pathogenic mechanisms. Curr Opin Neurol 1993; 6: 872-881.
108. Caughey B, Gerald S, Chesebro BB, Jeffrey M. Getting a Grip on Prions: Oligomers, myloids, and Pathological Membrane Interactions. Annu. Rev Biochem 2009; 78: 177-204.
109. Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Stritt-matter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Na-ture 2009; 457: 1128-1132.
110. Vincent B, Cisse MA, Sunyach C, Guillot-Sestier MV, Checler F. Regulation of betaAPP and PrPc cleavage by alpha-secretase: mechanistic and therapeutic per-spectives. Curr. Alzheimer Res 2008; 5: 202-211.
111. Aguzzi A, Haass C. Games played by rogue proteins in prion disorders and Alzheimer's disease. Science 2003; 302: 814-818.
112. Shankar GM, Li S, Mehta TH, Garcia-Munoz A, Sheepardson NE, Smith I, et al. Amyloid-beta protein dimmers isolated directly from Alzheimer's brains im-pair synaptic plasticity and memory. Nature Med 2008; 14: 837-842.
113. Cheng IH, Scearce-Levie K, Legleiter J, Palop JJ, Ger-stein H, Bien-Ly N, et al. Accelerating amyloid-beta fi-brillization reduces oligomer levels and functional defi-cits in Alzheimer disease mouse models J Biol Chem 2007; 282: 23818-23828.
114. Lesné S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, et al. A specific amyloid-beta protein assem-bly in the brain impairs memory. Nature 2006; 440: 352-357.
115. Caughey G, Race RE. Potent inhibition of scrapie asso-ciated PrP accumulation by Congo red. J Neurochem 1992; 59: 768-771.
116. Fraser JR, Brown J, Bruce ME, Jeffrey M. Scrapie-induced neuronal loss is reduced by treatment with ba-sic fibroblast growth factor. Neuroreport 1997; 8: 2405-2409.
117. Korth C, May BC, Cohen FE, Prusiner SB. Acridine and phenothiavine derivatives as pharmacotherapeutics for prion disease. Proc Natl Acad Sci. USA 2001; 98: 9836-9841.
118. Murakami-Kubo I, Dohura K, Ishikawa K, Kawatake S, Sasaki K, Kira J, et al. Quinoline Derivatives Are Ther-apeutic Candidates for Transmissible Spongiform En-cephalopathies. J Virol 2004; 78: 1281-1288.
119. Perrier V, Kaneko K, Safar J, Vergara J, Tremblay P, DeArmond SJ, et al. Dominant-negative inhibition of prion replication in transgenic mice. Proc Natl Acad Sci USA 2002; 99: 13079-13084.
120. Supattapone S, Bosque P, Muramoto T, Wille H, Aa-gaard C, Peretz D, et al. Prion protein of 106 residues creates an artificial transmission barrier for prion repli-cation in transgenic mice. Cell 1999; 96: 869-878.
121. Tagliavini FR, McArthur A, Canciani B, Giaccone G, Porro M, Bugiani PM, et al. Effectiveness of anthracy-cline against experimental prion disease in Syrian ham-sters. Science 1997; 276: 1119-1122.
122. Xi YG, Ingrosso L, Ladogana A, Masullo C, Pocchiari M. Amphotericin B treatment dissociates in vivo repli-cation of the scrapie agent from PrP accumulation. Na-ture 1992; 356: 598-601.
123. Trevitt CR, Collinge J. A systematic review of prion therapeutics in experimental models. Brain 2006; 129: 2241-2265.
124. Doh-Ura K, Iwaki T, Caughey B. Lysosomotropic age-nts and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J Virol 2000; 74: 4894-4897.
125. Caughey B. Prion protein conversions: insight into mechanisms, TSE transmission barriers and strains. British Medical Bulletin 2003; 66: 109-120.
126. Tatzelt J, Prusiner SB, Welch WJ. Chemical chaper-ones interfere with the formation of scrapie prion pro-tein. EMBO J 1996; 15: 6363-6373.
127. Shaked GM, Fridlander G, Meiner Z, Taraboulos A, Gabizon R. Proteaseresistant and detergent-insoluble prion protein is not necessarily associated with prion infectivity. J Biol Chem 1999; 274: 17981-17986.
128. Ingrosso L, Ladogana A, Pocchiari M. Congo red pro-longs the incubation period in scrapie infected hamsters. J Virol 1995; 69: 506-508.
129. Priola SA, Raines A, Caughey WS. Porphyrin and phthalocyanine anti-scrapie compounds. Science 2000; 287: 1503-1506.
130. Lindquist S. Mad cows meet psi-chotic yeast, the ex-pansion of the prion hypothesis. Cell 1997; 89: 495-498.
131. Wickner RB, Taylor KL, Edskes HK, Maddelein ML, Moriyama H, Roberts BT. Prions of yeast as heritable amyloidoses. J Struct Biol 2000; 130: 310-322.