Perspectives on prion biology, prion disease pathogenesis, and pharmacologic approaches to treatment

Clinics in Laboratory Medicine

Volumn 23, Issue 1, 2003, Pages 1-41

  DeArmond, Stephen J ^a   Prusiner, Stanley B ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORPROMAZINE; MEPACRINE; PHENOTHIAZINE; PRION PROTEIN;

BINDING SITE; NONHUMAN; PATHOGENESIS; PHENOTYPE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; REVIEW; TRANSGENIC MOUSE;

EID: 0037368005     PISSN: 02722712     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0272-2712(02)00041-0     Document Type: Review

References (136)

1. Prusiner SB, Scott MR, DeArmond SJ, Cohen FE. Prion protein biology. Cell 1998;93:337-48.
2. Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982;216:136-44.
3. Oesch B, Westaway D, Wälchli M, et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985;40:735-46.
4. Sparkes RS, Simon M, Cohn VH, Fournier REK, Lem J, Klisak I, et al. Assignment of the human and mouse prion protein genes to homologous chromosomes. Proc Natl Acad Sci USA 1986;83:7358-62.
5. Meyer RK, McKinley MP, Bowman KA, et al. Separation and properties of cellular and scrapie prion proteins. Proc Natl Acad Sci USA 1986;83:2310-4.
6. DeArmond SJ, Prusiner SB. Prion diseases. In: Graham DI, Lantos PL, editors. Greenfield's neuropathology, vol. 2. 6th edition. London: Arnold (Oxford University Press); 1997. p. 235-80.
7. Gambetti P, Petersen RB, Parchi P, et al. Inherited prion diseases. In: Prusiner SB, editor. Prion biology and diseases. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1999. p. 509-83.
8. Cohen FE, Pan K-M, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. Structural clues to prion replication. Science 1994;264:530-1.
9. Jendroska K, Heinzel FP, Torchia M, et al. Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity. Neurology 1991;41:1482-90.
10. 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;110:341-54.
11. Wickner RB. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994;264:566-9.
12. +] factor by in vitro-converted Sup35 protein. Science 2000;289:595-9.
13. Prusiner SB. Shattuck lecture - neurodegenerative diseases and prions. N Engl J Med 2001;344:1516-26.
14. DeArmond SJ, Kretzschmar HA, Prusiner SB. Prion diseases. In: Lantos PL, Graham DI, editors. Greenfield's neuropathology. 7th editioin. London: Arnold (Oxford University Press), 2002;2:273-323.
15. Telling GC, Parchi P, DeArmond SJ, et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 1996;274;2:2079-82.
16. Hadlow WJ. Scrapie and kuru. Lancet 1959;2:289-90.
17. Cuillé J, Chelle PL. Experimental transmission of trembling to the goat. C.R. Seances Acad Sci 1939;208:1058-60.
18. Klatzo I, Gajdusek DC, Zigas V. Pathology of kuru. Lab Invest 1959;8:799-847.
19. Gajdusek DC, Gibbs CJ Jr, Alpers M. Experimental transmission of a kuru-like syndrome to chimpanzees. Nature 1966;209:794-6.
20. Gibbs CJ Jr, Gajdusek DC, Asher DM, et al. Creutzfeldt-Jakob disease (spongiform encephalopathy): transmission to the chimpanzee. Science 1968;161:388-9.
21. Masters CL, Gajdusek DC, Gibbs CJ Jr. The familial occurrence of Creutzfeldt-Jakob disease and Alzheimer's disease. Brain 1981;104:535-58.
22. Medori R, Montagna P, Tritschler HJ, et al. Fatal familial insomnia: a second kindred with mutation of prion protein gene at codon 178. Neurology 1992;42:669-70.
23. Medori R, Tritschler H-J, LeBlanc A, et al. Fatal familial insomnia, a prion disease with a mutation at codon 178 of the prion protein gene. N Engl J Med 1992;326:444-9.
24. Tateishi J, Brown P, Kitamoto T, et al. First experimental transmission of fatal familial insomnia. Nature 1995;376:434-5.
25. Mastrianni JA, Nixon R, Layzer R, et al. Prion protein conformation in a patient with sporadic fatal insomnia. N Engl J Med 1999;340:1630-8.
26. Ghetti B, Piccardo P, Frangione B, et al. Prion protein amyloidosis. Brain Pathol 1996;6:127-45.
27. Hsiao K, Baker HF, Crow TJ, et al. Linkage of a prion protein missense variant to Gerstmann-Sträussler syndrome. Nature 1989;338:342-5.
28. Hsiao K, Scott M, Foster D, et al. Spontaneous neurodegeneration in transgenic mice with prion protein codon 101 proline→leucine substitution. Ann NY Acad Sci 1991;640:166-70.
29. Hegde RS, Mastrianni JA, Scott MR, et al. A transmembrane form of prion protein in neurodegenerative disease. Science 1998;279:827-34.
30. Hsiao KK, Scott M, Foster D, et al. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 1990;250:1587-90.
31. Hsiao KK, Groth D, Scott M, et al. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc Natl Acad Sci USA 1994;91:9126-30.
32. Will RG, Ironside JW, Zeidler M, et al. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 1996;347:921-5.
33. Scott MR, Will R, Ironside J, et al. Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. Proc Natl Acad Sci USA 1999;96:15137-42.
34. Brown P, Will RG, Bradley R, et al. Bovine spongiform encephalopathy and variant Creutzfeldt-Jakob disease: background, evolution, and current concerns. CDC (http://www/cdc.gov/ncidod/EID/vol7nol/brown.htm). 2001;7:1-13. Accessed 2002 April 4.
35. Balter M. Tracking the human fallout from "mad cow disease". Science 2000;289:1452-4.
36. Kaneko K, Zulianello L, Scott M, et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc Natl Acad Sci USA 1997;94:10069-74.
37. Telling GC, Scott M, Mastrianni J, et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell 1995;83:79-90.
38. James TL, Liu H, Ulyanov NB, et al. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc Natl Acad Sci USA 1997;94:10086-91.
39. Donne DG, Viles JH, Groth D, et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci USA 1997;94:13452-7.
40. Scott M, Groth D, Foster D, et al. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 1993;73:979-88.
41. Pan K-M, Baldwin M, Nguyen J, et al. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993;90:10962-6.
42. Yost CS, Lopez CD, Prusiner SB, et al. Non-hydrophobic extracytoplasmic determinant of stop transfer in the prion protein. Nature 1990;343:669-72.
43. Hay B, Barry RA, Lieberburg I, et al. Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein. Mol Cell Biol 1987;7:914-20.
44. Hay B, Prusiner SB, Lingappa VR. Evidence for a secretory form of the cellular prion protein. Biochemistry 1987;26:8110-5.
45. Hegde RS, Tremblay P, Groth D, et al. Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 1999;402:822-6.
46. Brown P, Cathala F, Raubertas RF, et al. The epidemiology of Creutzfeldt-Jakob disease: conclusion of 15-year investigation in France and review of the world literature. Neurology 1987;37:895-904.
47. Holman RC, Khan AS, Kent J, et al. Epidemiology of Creutzfeldt-Jakob disease in the United States, 1979-1990: analysis of national mortality data. Neuroepidemiology 1995;14:174-81.
48. Holman RC, Khan AS, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States, 1979-1994: using national mortality data to assess the possible occurrence of variant cases. Emerg Infect Dis 1996;2:333-7.
49. Büeler H, Fischer M, Lang Y, Bluethmann H, et al. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992;356:577-82.
50. Büeler H, Aguzzi A, Sailer A, et al. Mice devoid of PrP are resistant to scrapie. Cell 1993;73:1339-47.
51. Prusiner SB, Groth D, Serban A, et al. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc Natl Acad Sci USA 1993;90:10608-12.
52. Brandner S, Isenmann S, Raeber A, et al. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 1996:379:339-43.
53. Lledo P-M, Tremblay P, DeArmond SJ, et al. Mice deficient for prion protein exhibit normal neuronal excitability and synaptic transmission in the hippocampus. Proc Natl Acad Sci USA 1996;93:2403-7.
54. Tobler I, Gaus SE, Deboer T, et al. Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 1996;380:639-42.
55. Tremblay P, Meiner Z, Galou M, et al. Doxycylcline control of prion protein transgene expression modulates prion disease in mice. Proc Natl Acad Sci USA 1998;95:12580-5.
56. Manson JC, Clarke AR, Hooper ML, et al. 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 1994;8:121-7.
57. Sakaguchi S, Katamine S, Nishida N, et al. Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 1996;380:528-31.
58. Moore R. Gene targeting studies at the mouse prion protein locus. Edinburgh, Scotland: University of Edinburgh; 1997.
59. Nishida N, Tremblay P, Sugimoto T, et al. A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeration and demyelination. Lab Invest 1999;79:689-97.
60. Lee IY, Westaway D, Smit AFA, et al. Complete genomic sequence and analysis of the prion protein region from three mammalian species. Genome Res 1998;8:1022-37.
61. Westaway D, Mirenda CA, Foster D, et al. Paradoxical shortening of scrapie incubation times by expression of prion protein transgenes derived from long incubation period mice. Neuron 1991;7:59-68.
62. Moore RC, Lee IY, Silverman GL, et al. Ataxia in prion protein (PrP) deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol 1999;292:797-817.
63. Mo H, Moore RC, Cohen FE, et al. Two different neurodegenerative diseases caused by proteins with similar structures. Proc Natl Acad Sci USA 2001;27:2352-7.
64. Kretzschmar HA, Prusiner SB, Stowring LE, DeArmond SJ. Scrapie prion proteins are synthesized in neurons. Am J Pathol 1986;122:1-5.
65. Moore RC, Mastrangelo P, Bouzamondo E, et al. Doppel-induced cerebellar degeneration in transgenic mice. Proc Natl Acad Sci USA 2001;98:15288-93.
66. Prusiner SB, Scott M, Foster D, et al. Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 1990;63:673-86.
67. Scott M, Foster D, Mirenda C, et al. Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 1989;59:847-57.
68. Gibbs CJ Jr, Gajdusek DC, Amyx H. Strain variation in the viruses of Creutzfeldt-Jakob disease and kuru. In: Prusiner SB, Hadlow WJ, editors. Slow transmissible diseases of the nervous system, vol. 2. New York: Academic Press: 1979. p. 87-110.
69. Telling GC, Scott M, Hsiao KK, et al. Transmission of Creutzfeldt-Jakob disease from humans to transgenic mice expressing chimeric human-mouse prion protein. Proc Natl Acad Sci USA 1994;91:9936-40.
70. Westaway D, Zuliani V, Cooper CM, et al. Homozygosity for prion protein alleles encoding glutamine-171 renders sheep susceptible to natural scrapie. Genes Dev 1994;8:959-69.
71. Kitamoto T, Tateishi J. Human prion diseases with variant prion protein. Philos Trans R Soc Lond B Biol Sci 1994;343:391-8.
72. Shibuya S, Higuchi J, Shin R-W, et al. Codon 219 Lys allele of PRNP is not found in sporadic Creutzfeldt-Jakob disease. Ann Neurol 1998;63:1212-22.
73. Prusiner SB, Groth DF, Bolton DC, et al. Purification and structural studies of a major scrapie prion protein. Cell 1984;38:127-34.
74. Fischer M, Rülicke T, Raeber A, et al. Prion protein (PrP) with amino-proximal deletions restoring suceptibility of PrP knockout mice to scrapie. EMBO J 1996;15:1255-64.
75. Supattapone S, Bosque P, Muramoto T, et al. Prion protein of 106 residues creates an artificial transmission barrier for prion replication in transgenic mice. Cell 1999;96:869-78.
76. Muramoto T, DeArmond SJ, Scott M, et al. Heritable disorder resembling neuronal storage disease in mice expressing prion protein with deletion of an α-helix. Nat Med 1997;3:750-5.
77. Supattapone S, Bouzamondo E, Ball HL, et al. A protease-resistant 61-residue prion peptide causes neurodegeneration in transgenic mice. Mol Cell Biol 2001;21:2608-16.
78. Dickinson AG, Meikle VMH. Host-genotype and agent effects in scrapie incubation: change in allelic interaction with different strains of agent. Mol Gen Genet 1971;112:73-9.
79. Dickinson AG, Fraser H, Meikle VMH, Outram GW. Competition between different scrapie agents in mice. Nat New Biol 1972;237:244-5.
80. Fraser H, Dickinson AG. The sequential development of the brain lesions of scrapie in three strains of mice. J Comp Pathol 1968;78:301-11.
81. Fraser H, Bruce ME. Argyrophilic plaques in mice inoculated with scrapie from particular sources. Lancet 1973;1:617-8.
82. Fraser H, Dickinson AG. Scrapie in mice. Agent-strain differences in the distribution and intensity of grey matter vacuolation. J Comp Pathol 1973;83:29-40.
83. Bruce ME, McBride PA, Farquhar CF. Precise targeting of the pathology of the sialoglycoprotein, PrP, and vacuolar degeneration in mouse scrapie. Neurosci Lett 1989;102:1-6.
84. Hecker R, Taraboulos A, Scott M, et al. Replication of distinct prion isolates is region specific in brains of transgenic mice and hamsters. Genes Dev 1992;6:1213-28.
85. DeArmond SJ, Yang S-L, Lee A, et al. Three scrapie prion isolates exhibit different accumulation patterns of the prion protein scrapie isoform. Proc Natl Acad Sci USA 1993;90:6449-53.
86. DeArmond SJ, Prusiner SB. Prion diseases. In: Markesbery WR, editor. Neuropathology of dementing disorders. London: Arnold; 1998. p. 340-76.
87. DeArmond SJ. Prion diseases: the spectrum of etiologic and pathogenic mechanisms. In: Folstein MF, editor. Neurobiology of primary dementia. Washington, DC: American Psychiatric Press Inc.; 1998. p. 83-118.
88. DeArmond SJ, Ironside JW. Neuropathology of prion diseases. In: Prusiner SB, editor. Prion biology and diseases. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1999. p. 585-652.
89. DeArmond SJ. Cerebral amyloidosis in prion diseases. Amyloid 2000;7:3-6.
90. Bendheim PE, Barry RA, DeArmond SJ, et al. Antibodies to a scrapie prion protein. Nature 1984;310:418-21.
91. DeArmond SJ, McKinley MP, Barry RA, et al. Identification of prion amyloid filaments in scrapie-infected brain. Cell 1985;41:221-35.
92. Kitamoto T, Tateishi J, Tashima I, et al. Amyloid plaques in Creutzfeldt-Jakob disease stain with prion protein antibodies. Ann Neurol 1986;20:204-8.
93. Snow AD, Kisilevsky R, Willmer J, et al. Sulfated glycosaminoglycans in amyloid plaques of prion diseases. Acta Neuropathol (Berl) 1989;77:337-42.
94. DeArmond SJ, Prusiner SB. Etiology and pathogenesis of prion diseases. Am J Pathol 1995;146:785-811.
95. DeArmond SJ, Mobley WC, DeMott DL, et al. Changes in the localization of brain prion proteins during scrapie infection. Neurology 1987;37:1271-80.
96. DeArmond SJ, Prusiner SB, The neurochemistry of prion diseases. J Neurochem 1993;61:1589-601.
97. Vey M, Pilkuhn S, Wille H, et al. Subcellular colocalization of cellular and scrapie prion proteins in caveolae-like membranous domains. Proc Natl Acad Sci USA 1996;93:14945-9.
98. Kristensson K, Feuerstein B, Taraboulos A, et al. Scrapie prions alter receptor-mediated calcium responses in cultured cells. Neurology 1993;43:2335-41.
99. Wong K, Qiu Y, Hyun W, et al. Decreased receptor-mediated calcium response in prion-infected cells correlates with decreased membrane fluidity and IP3 release. Neurology 1996;47:741-50.
100. Diez M, Koistinaho J, DeArmond SJ, et al. Marked decrease of neuropeptide Y Y2 receptor binding sites in the hippocampus in murine prion disease. Proc Natl Acad Sci USA 1997;94:13267-72.
101. Diez M, DeArmond SJ, Groth D, et al. Decreased MK-801 binding in discrete hippocampal regions of prion-infected mice. Neurobiol Dis 2001;8:692-699.
102. DeArmond SJ, Sanchez H, Qiu Y, et al. Selective neuronal targeting in prion diseases. Neuron 1997;19:1337-48.
103. C glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. J Neuropathol Exp Neurol 1999;58:1000-9.
104. Carlson GA, Kingsbury DT, Goodman PA, et al. Linkage of prion protein and scrapie incubation time genes. Cell 1986;46:503-11.
105. Westaway D, Goodman PA, Mirenda CA, et al. Distinct prion proteins in short and long scrapie incubation period mice. Cell 1987;51:651-62.
106. Carlson GA, Ebeling C, Yang S-L, et al. Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice. Proc Natl Acad Sci USA 1994;91:5690-4.
107. Fraser H, Bruce ME. Experimental control of cerebral amyloid in scrapie in mice. In: Behan PO, ter Meulen V, Rose FC, editors. Immunology of nervous system infections, progress in brain research, vol. 59. Amsterdam: Elsevier Science Publishers; 1983. p. 281-90.
108. Bruce ME, Dickinson AG, Fraser H. Cerebral amyloidosis in scrapie in the mouse: effect of agent strain and mouse genotype. Neuropathol Appl Neurobiol 1976;2:471-8.
109. Ghetti B, Piccardo P, Spillantini MG, et al. Vascular variant of prion protein cerebral amyloidosis with τ-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP. Proc Natl Acad Sci USA 1996;93:744-8.
110. Lowenstein DH, Butler DA, Westaway D, et al. Three hamster species with different scrapie incubation times and neuropathological features encode distinct prion proteins. Mol Cell Biol 1990;10:1153-63.
111. Monari L, Chen SG, Brown P, et al. Fatal familial insomnia and familial Creutzfeldt-Jakob disease: different prion proteins determined by a DNA polymorphism. Proc Natl Acad Sci USA 1994;91:2839-42.
112. Parchi P, Castellani R, Capellari S, et al. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann Neurol 1996;39:767-78.
113. Gambetti P, Parchi P, Petersen RB, et al. Fatal familial insomnia and familial Creutzfeldt-Jakob disease: clinical, pathological and molecular features. Brain Pathol 1995;5:43-51.
114. Goldfarb LG, Petersen RB, Tabaton M, et al. Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism. Science 1992;258:806-8.
115. DeArmond SJ. Differential targeting of neurons by prion strains. In: Baker HF, editor. Methods in molecular medicine, vol. 59: molecular pathology of the prions. Totowa NJ: Humana Press, Inc.; 2001. p. 85-110.
116. Rademacher TW, Parekh RB, Dwek RA. Glycobiology. Annu Rev Biochem 1988;57:785-838.
117. Kaneko K, Ball HL, Wille H, et al. A synthetic peptide initiates Gerstmann-Sträussler-Scheinker (GSS) disease in transgenic mice. J Mol Biol 2000;295:997-1007.
118. Parchi P, Giese A, Capellari S, et al. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol 1999;46:224-33.
119. Alonso DW, DeArmond SJ, Cohen FE, Daggett V. Mapping the early steps in the pH-induced conformational conversion of the prion protein. Proc Natl Acad Sci USA 2001;98:2985-9.
120. Parchi P, Zou W, Wang W, et al. Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci USA 2000;97:10168-72.
121. Cohen FE, Prusiner SB. Structural studies of prion proteins. In: Prusiner SB, editor. Prion biology and diseases. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1999. p. 191-228.
122. Wells GAH, Scott AC, Johnson CT, et al. A novel progressive spongiform encephalopathy in cattle. Vet Rec 1987;121:419-20.
123. Bruce M, Chree A, McConnell I, et al. Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos Trans R Soc Lond B 1994;343:405-11.
124. Hill AF, Desbruslais M, Joiner S, et al. The same prion strain causes vCJD and BSE. Nature 1997;389:448-50.
125. Will RG, Alpers MP, Dormont D, et al. Infectious and sporadic prion diseases. In: Prusiner SB, editor. Prion biology and diseases. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press; 1999. p. 465-507.
126. Houston F, Foster JD, Chong A, et al. Transmission of BSE by blood transfusion in sheep. Lancet 2000;356:999-1000.
127. 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 2001;98:9295-9.
128. Peretz D, Williamson RA, Kaneko K, et al. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 2001;412:739-43.
129. Perrier V, Wallace AC, Kaneko K, et al. Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc Natl Acad Sci USA 2000;97:6073-8.
130. Korth K, May BCH, Cohen FE, Prusiner SB. Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc Natl Acad Sci USA 2001;98:9836-41.
131. Brown DR, Qin K, Herms JW, et al. The cellular prion protein binds copper in vivo. Nature 1997;390:684-7.
132. Stockel J, Safar J, Wallace AC, et al. Prion protein selectively binds copper (II) ions. Biochemistry 1998;37:7185-93.
133. Endo T, Groth D, Prusiner SB, Kobata A. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 1989;28:8380-8.
134. Tatzelt J, Groth DF, Torchia M, et al. Kinetics of prion protein accumulation in the CNS of mice with experimental scrapie. J Neuropathol Exp Neurol 1999;58:1244-9.
135. Fraser H. Neuronal spread of scrapie agent and targeting of lesions within the retinotectal pathway. Nature 1982;295:149-50.
136. Riek R, Hornemann S, Wider G, et al. NMR structure of the mouse prion protein domain PrP(121-321). Nature 1996;382:180-2.