Skip to main content
SpringerLink
Log in

A Function for the Prion Protein?

  • Protocol
Molecular Pathology of the Prions

Part of the book series: Methods in Molecular Medicine™ ((MIMM,volume 59))

  • 532 Accesses

Abstract

Protein function is often observed directly following protein isolation, or is deduced by loss of function following gene knockout or by analogy with proteins of known function and similar amino acid sequence. None of these is true in the case of prion proteins because aside from the association with the pathogenesis of the spongiform encaphalopathies, no single obvious function has been described for these molecules until recently. The first two chapters in this volume (see refs. 1-3), concentrated on the characterization of the infectious agent, and led to the introduction of the term “prion” in 1982 (4). But it was not until the positive association of the infectious agent, PrPSc, with a normal host gene locus, prnp, that real opportunities to consider protein function in relation to the disease phenotype arose (5). The identification of the prion gene on chromosome 2 of the mouse (chromosome 20 in the human) (6), and the determination of its sequence (7), led to the translation of the encoded protein and speculation concerning its function.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 159.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 109.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Horwich, A. L. and Weissman, J. S. (1997) Deadly conformations-protein misfolding in prion disease. Cell 89, 499–510.

    Article  PubMed  CAS  Google Scholar 

  2. Liemann, S. and Glockshuber, R. (1998) Transmissible spongiform encephalopathies. Biochem. Biophys. Res. Commun. 250, 187–93.

    Article  PubMed  CAS  Google Scholar 

  3. Prusiner, S. B. (1997) Prion diseases and the BSE crisis. Science 278, 245–51.

    Article  PubMed  CAS  Google Scholar 

  4. Prusiner, S. B. (1982) Novel proteinaceous infectious particles cause scrapie. Science 216, 136–44.

    Article  PubMed  CAS  Google Scholar 

  5. Basler, K., Oesch, B., Scott, M., Westaway, D., Walchli, M., Groth, D. F., et al. (1986) Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46, 417–28.

    Article  PubMed  CAS  Google Scholar 

  6. Sparkes, R. S., Simon, M., Cohn, V. H., Fournier, R. E., Lem, J., Klisak, et al. (1986) Assignment of the human and mouse prion protein genes to homologous chromosomes. Proc. Natl. Acad. Sci. USA 83, 7358–7362.

    Article  PubMed  CAS  Google Scholar 

  7. Locht, C., Chesebro, B., Race, R., and Keith, J. M. (1986) Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Proc. Natl. Acad. Sci. USA 83, 6372–6376.

    Article  PubMed  CAS  Google Scholar 

  8. Sendo, F., Suzuki, K., Watanabe, T., Takeda, Y. and Araki, Y. (1998) Modulation of leukocyte transendothelial migration by integrin-associated glycosyl phosphatidyl inositol (GPI)-anchored proteins. Inflamm. Res. 47, S133–136.

    Article  PubMed  CAS  Google Scholar 

  9. Gabriel, J. M., Oesch, B., Kretzschmar, H., Scott, M. and Prusiner, S. B. (1992) Molecular cloning of a candidate chicken prion protein. Proc. Natl. Acad. Sci. USA 89, 9097–9101.

    Article  PubMed  CAS  Google Scholar 

  10. Simonic, T., Duga, S., Strumbo, B., Asselta, R., Ceciliani, F., and Ronchi, S. (2000) cDNA cloning of turtle prion protein. FEBS Lett. 469, 33–38.

    Article  PubMed  CAS  Google Scholar 

  11. Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E., et al. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis [see comments]. Nature 385, 787–793.

    Article  PubMed  CAS  Google Scholar 

  12. Moore, R. C., Lee, I. Y., Silverman, G. L., Harrison, P. M., Strome, R., Heinrich, C., et al. (1999) Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J. Mol. Biol. 292, 797–817.

    Article  PubMed  CAS  Google Scholar 

  13. Sakaguchi, S., Katamine, S., Nishida, N., Moriuchi, R., Shigematsu, K., Sugimoto, T., et al. (1996). Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene. Nature 380, 528–531.

    Article  PubMed  CAS  Google Scholar 

  14. Matthews, S., Barlow, P., Boyd, J., Barton, G., Russell, R., Mills, H., et al. (1994) Structural similarity between the p17 matrix protein of HIV-1 and interferon gamma. Nature 370, 666–668.

    Article  PubMed  CAS  Google Scholar 

  15. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R., and Wuthrich, K. (1996). NMR structure of the mouse prion protein domain PrP (121-321). Nature 382, 180–182.

    Article  PubMed  CAS  Google Scholar 

  16. James, T. L., Liu, H., Ulyanov, N. B., Farr-Jones, S., Zhang, H., Donne, D. G., et al. (1997) Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94, 10,086–10,091.

    Article  PubMed  CAS  Google Scholar 

  17. Wildegger, G., Liemann, S., and Glockshuber, R. (1999) Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nat. Struct. Biol. 6, 550–553.

    Article  PubMed  CAS  Google Scholar 

  18. Hornshaw, M. P., McDermott, J. R. and Candy, J. M. (1995) Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem. Biophys. Res. Commun. 207, 621–629.

    Article  PubMed  CAS  Google Scholar 

  19. Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., et al. (1997) The cellular prion protein binds copper in vivo. Nature 390, 684–687.

    Article  PubMed  CAS  Google Scholar 

  20. Stockel, J., Safar, J., Wallace, A. C., Cohen, F. E., and Prusiner, S. B. (1998). Prion protein selectively binds copper(II) ions. Biochemistry 37, 7185–7193.

    Article  PubMed  CAS  Google Scholar 

  21. Brown, D. R., Wong, B. S., Hafiz, F., Clive, C., Haswell, S., and Jones, I. M. (1999) Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344, 1–5.

    Article  PubMed  CAS  Google Scholar 

  22. Marcotte, E. M. and Eisenberg, D. (1999) Chicken prion tandem repeats form a stable, protease-resistant domain. Biochemistry 38, 667–676.

    Article  PubMed  CAS  Google Scholar 

  23. Viles, J. H., Cohen, F. E., Prusiner, S. B., Goodin, D. B., Wright, P. E., and Dyson, H. J. (1999). Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. USA 96, 2042–2047.

    Article  PubMed  CAS  Google Scholar 

  24. Miura, T., Hori-i, A., Mototani, H., and Takeuchi, H. (1999) Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence. Biochemistry 38, 11560–11569.

    Article  PubMed  CAS  Google Scholar 

  25. Ruiz, F. H., Silva, E. and Inestrosa, N. C. (2000) The N-Terminal tandem repeat region of human prion protein reduces copper: role of tryptophan Residues. Biochem. Biophys. Res. Commun. 269, 491–495.

    Article  PubMed  CAS  Google Scholar 

  26. Shiraishi, N., Ohta, Y., and Nishikimi, M. (2000) The octapeptide repeat region of prion protein binds Cu(II) in the redox-inactive state. Biochem. Biophys. Res. Commun. 267, 398–402.

    Article  PubMed  CAS  Google Scholar 

  27. Wong, B. S., Wang, H., Brown, D. R., and Jones, I. M. (1999) Selective oxidation of methionine residues in prion proteins. Biochem. Biophys. Res. Commun. 259, 352–355.

    Article  PubMed  CAS  Google Scholar 

  28. Zhou, B. and Gitschier, J. (1997) hCTR1: a human gene for copper uptake identified by complementation in yeast. Proc. Natl. Acad. Sci. USA 94, 7481–7486.

    Article  PubMed  CAS  Google Scholar 

  29. Brown, D. R., Herms, J., and Kretzschmar, H. A. (1994) Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. Neuroreport 5, 2057–2060.

    Article  PubMed  CAS  Google Scholar 

  30. Giese, A., Brown, D. R., Groschup, M. H., Feldmann, C., Haist, I., and Kretzschmar, H. A. (1998) Role of microglia in neuronal cell death in prion disease. Brain Pathol. 8, 449–457.

    Article  PubMed  CAS  Google Scholar 

  31. Brandner, S., Isenmann, S., Raeber, A., Fischer, M., Sailer, A., Kobayashi, Y., et al. (1996). Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature 379, 339–343.

    Article  PubMed  CAS  Google Scholar 

  32. Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1996) Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380, 345–347.

    Article  PubMed  CAS  Google Scholar 

  33. Brown, D. R., Schulz-Schaeffer, W. J., Schmidt, B., and Kretzschmar, H. A. (1997) Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146, 104–112.

    Article  PubMed  CAS  Google Scholar 

  34. Bueler, H., Aguzzi, A., Sailer, A., Greiner, R. A., Autenried, P., Aguet, M., and Weissmann, C. (1993) Mice devoid of PrP are resistant to scrapie. Cell 73, 1339–1347.

    Article  PubMed  CAS  Google Scholar 

  35. Kuwahara, C., Takeuchi, A. M., Nishimura, T., Haraguchi, K., Kubosaki, A., Matsumoto, Y. et al. (1999) Prions prevent neuronal cell line death. Nature 400, 225–226.

    Article  PubMed  CAS  Google Scholar 

  36. Brown, D. R., Schmidt, B. and Kretzschmar, H. A. (1997). Expression of prion protein in PC12 is enhanced by exposure to oxidative stress. Int. J. Dev. Neurosci 15, 961–972.

    Article  PubMed  CAS  Google Scholar 

  37. Brown, D. R. and Besinger, A. (1998) Prion protein expression and superoxide dismutase activity. Biochem. J. 334, 423–429.

    PubMed  CAS  Google Scholar 

  38. White, A. R., Collins, S. J., Maher, F., Jobling, M. F., Stewart, L. R., Thyer, J. M., et al. (1999) Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity. Am. J. Pathol. 155, 1723–1730.

    Article  PubMed  CAS  Google Scholar 

  39. Perovic, S., Schroder, H. C., Pergande, G., Ushijima, H., and Muller, W. E. (1997) Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126). Exp. Neurol. 147, 518–524.

    Article  PubMed  CAS  Google Scholar 

  40. Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1997) Effects of oxidative stress on prion protein expression in PC12 cells. Int. J. Dev. Neurosci. 15, 961–972.

    Article  PubMed  CAS  Google Scholar 

  41. Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1998) Effects of copper on survival of prion protein knockout neurons and glia. J. Neurochem. 70, 1686–1693.

    Article  PubMed  CAS  Google Scholar 

  42. Hornshaw, M. P., McDermott, J. R., Candy, J. M., and Lakey, J. H. (1995) Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem. Biophys. Res. Commun. 214, 993–999.

    Article  PubMed  CAS  Google Scholar 

  43. Miura, T., Hori-i, A., and Takeuchi, H. (1996) Metal-dependent alpha-helix formation promoted by the glycine-rich octapeptide region of prion protein. FEBS Lett. 396, 248–252.

    Article  PubMed  CAS  Google Scholar 

  44. Steinebach, O. M. and Wolterbeek, H. T. (1994) Role of cytosolic copper, metallothionein and glutathione in copper toxicity in rat hepatoma tissue culture cells. Toxicology 92, 75–90.

    Article  PubMed  CAS  Google Scholar 

  45. Stahl, N., Borchelt, D. R., and Prusiner, S. B. (1990) Differential release of cellular and scrapie prion proteins from cellular membranes by phosphatidylinositolspecific phospholipase C. Biochemistry 29, 5405–5412.

    Article  PubMed  CAS  Google Scholar 

  46. Sales, N., Rodolfo, K., Hassig, R., Faucheux, B., Di Giamberardino, L., and Moya, K. L. (1998). Cellular prion protein localization in rodent and primate brain. Eur. J. Neurosci. 10, 2464–2471.

    Article  PubMed  CAS  Google Scholar 

  47. Vulpe, C. D. and Packman, S. (1995) Cellular copper transport. Annu. Rev. Nutr. 15, 293–322.

    Article  PubMed  CAS  Google Scholar 

  48. Di Donato, M. and Sarkar, B. (1997) Copper transport and its alterations in Menkes and Wilson diseases. Biochim. Biophys. Acta. 1360, 3–16.

    Google Scholar 

  49. Waggoner, D. J., Bartnikas, T. B., and Gitlin, J. D. (1999) The role of copper in neurodegenerative disease. Neurobiol. Dis. 6, 221–2230.

    Article  PubMed  CAS  Google Scholar 

  50. Horn, N., Tonnesen, T., and Tümer, Z. (1992) Menkes disease: an x-linked neurological disorder of the copper metabolism. Brain Pathol. 2, 351–362.

    Article  PubMed  CAS  Google Scholar 

  51. Hartmann, H. A. and Evenson, M. A. (1992) Deficiency of copper can cause neuronal degeneration. Med. Hypotheses 38, 75–85.

    Article  PubMed  CAS  Google Scholar 

  52. Tanzi, R. E., Petrukhin, K., Chernov, I., Pellequer, J. L., Wasco, W., Ross, B., et al. (1993) The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene. Nature Genet. 5, 344–350.

    Article  PubMed  CAS  Google Scholar 

  53. Cuthbert, J. A. (1995) Wilson’s disease: a new gene and an animal model for an old disease. J. Investig. Med. 43, 323–336.

    PubMed  CAS  Google Scholar 

  54. Dijkstra, M., Vonk, R. J., and Kuipers, F. (1996) How does copper get into bile? New insights into the mechanism(s) of hepatobiliary copper transport. J. Hepatol. 24, 109–120.

    Article  PubMed  CAS  Google Scholar 

  55. Colburn, R. W. and Maas, J. W. (1965) Adenosine triphosphate—metal—norepinephrine ternary complexes and catecholamine binding. Nature 208, 37–41.

    Article  PubMed  CAS  Google Scholar 

  56. Rajan, K. S., Colburn, R. W., and Davis, J. M. (1976) Distribution of metal ions in the subcellular fractions of several rat brain areas. Life Sci. 18, 423–431.

    Article  PubMed  CAS  Google Scholar 

  57. Kardos, J., Kovacs, I., Hajos, F., Kalman, M., and Simonyi, M. (1989) Nerve endings from rat brain tissue release copper upon depolarization. A possible role in regulating neuronal excitability. Neurosci. Lett. 103, 139–144.

    Article  PubMed  CAS  Google Scholar 

  58. Barnea, A., Hartter, D. E., and Cho, G. (1989) High-affinity uptake of 67Cu into a veratridine-releasable pool in brain tissue. Am. J. Physiol. 257, C315–322.

    PubMed  CAS  Google Scholar 

  59. Gabrielsson, B., Robson, T., Norris, D., and Chung, S. H}. (1986) Effects of divalent metal ions on the uptake of glutamate and GABA from synaptosomal fractions. Brain Res. 384, 218–223.

    Article  PubMed  CAS  Google Scholar 

  60. Ma, J. Y. and Narahashi, T. (1993) Differential modulation of gaba-areceptorchannel complex by polyvalent cations in rat dorsal root ganglion neurons. Brain Res. 607, 222–232.

    Article  PubMed  CAS  Google Scholar 

  61. Velez-Pardo, C., Jimenez del Rio, M., Ebinger, G. and Vauquelin, G. (1995) Manganese and copper promote the binding of dopamine to " serotonin binding proteins" in bovine frontal cortex. Neurochem. Int. 26, 615–622.

    Article  PubMed  CAS  Google Scholar 

  62. Farrar, J. R. and Hoss, W. (1984) Effects of copper on the binding of agonists and antagonists to muscarinic receptors in rat brain. Biochem. Pharmacol. 33, 2849–2856.

    Article  PubMed  CAS  Google Scholar 

  63. Farrar, J. R., Hoss, W., Herndon, R. M., and Kuzmiak, M. (1985) Characterization of muscarinic cholinergic receptors in the brains of copper-deficient rats. J. Neurosci. 5, 1083–1089.

    PubMed  CAS  Google Scholar 

  64. Geiger, J. D., Seth, P. K., Klevay, L. M., and Parmar, S. S. (1984) Receptorbinding changes in copper-deficient rats. Pharmacology 28, 196–202.

    Article  PubMed  CAS  Google Scholar 

  65. Vlachova, V., Zemkova, H. and Vyklicky, L., Jr. (1996). Copper modulation of NMDA responses in mouse and rat cultured hippocampal neurons. Eur. J. Neurosci. 8, 2257–2264.

    Article  PubMed  CAS  Google Scholar 

  66. Collinge, J., Whittington, M. A., Sidle, K. C., Smith, C. J., Palmer, M. S., Clarke, A. R., and Jefferys, J. G. (1994) Prion protein is necessary for normal synaptic function. Nature 370, 295–297.

    Article  PubMed  CAS  Google Scholar 

  67. FraÚsto de Silva, J. J. R. and Williams, R. J. P. (1991), in The Biological Chemistry of Elements. Clarendon, Oxford.

    Google Scholar 

  68. Linder, M. C. (1991) Biochemistry of copper. New York: Plenum Press.

    Google Scholar 

  69. Hartter, D. E. and Barnea, A.} (1988) Brain tissue accumulates 67copper by two liganddependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process. J. Biol. Chem. 263, 799–805.

    PubMed  CAS  Google Scholar 

  70. Brown, D. R. (1999) Prion protein expression aids cellular uptake and veratridine-induced release of copper. J. Neurosci. Res. 58, 717–725.

    Article  PubMed  CAS  Google Scholar 

  71. Hornemann, S., Korth, C., Oesch, B., Riek, R., Wider, G., Wuthrich, K. and Glockshuber, R. (1997) Recombinant full-length murine prion protein, mPrP (23-231): purification and spectroscopic characterization. FEBS Lett. 413, 277–281.

    Article  PubMed  CAS  Google Scholar 

  72. Fridovich, I. (1974) Superoxide dismutases. Ann. Rev. Biochem. 44, 147–159.

    Article  Google Scholar 

  73. Chowdhury, S. K., Eshraghi, J., Wolfe, H., Forde, D., Hlavac, A. G., and Johnston, D. (1995) Mass spectrometric identification of amino acid transformations during oxidation of peptides and proteins: modifications of methionine and tyrosine. Anal. Chem. 67, 390–398.

    Article  PubMed  CAS  Google Scholar 

  74. Fridovich, I. (1997) Superoxide anion radical (O2-.), superoxide dismutases, and related matters. J. Biol. Chem. 272, 18515–18517.

    Article  PubMed  CAS  Google Scholar 

  75. Marklund, S. L. (1982) Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. USA 79, 7634–7638.

    Article  PubMed  CAS  Google Scholar 

  76. Ookawara, T., Imazeki, N., Matsubara, O., Kizaki, T., Oh-Ishi, S., Nakao, C., Sato, Y., and Ohno, H. (1998) Tissue distribution of immunoreactive mouse extracellular superoxide dismutase. Am. J. Physiol. 275, C840–847.

    PubMed  CAS  Google Scholar 

  77. Gohel, C., Grigoriev, V., Escaig-Haye, F., Lasmezas, C. I., Deslys, J. P., Langeveld, J., et al. (1999) Ultrastructural localization of cellular prion protein (PrPc) at the neuromuscular junction. J. Neurosci. Res. 55, 261–267.

    Article  PubMed  CAS  Google Scholar 

  78. Rodolfo, K., Hassig, R., Moya, K. L., Frobert, Y., Grassi, J., and Di Giamberardino, L. (1999). A Novel cellular prion protein isoform present in rapid anterograde axonal transport. Neuroreport 10, 3639–3644.

    Article  PubMed  CAS  Google Scholar 

  79. Brown, D. R. (1999) Prion protein peptide neurotoxicity can be mediated by astrocytes. J. Neurochem. 73, 1105–1113.

    Article  PubMed  CAS  Google Scholar 

  80. Moser, M., Colello, R. J., Pott, U., and Oesch, B. (1995) Developmental expression of the prion protein gene in glial cells. Neuron 14, 509–517.

    Article  PubMed  CAS  Google Scholar 

  81. Brown, D. R., Besinger, A., Herms, J. W., and Kretzschmar, H. A. (1998) Microglial expression of the prion protein. Neuroreport 9, 1425–1429.

    Article  PubMed  CAS  Google Scholar 

  82. Diomede, L., Sozzani, S., Luini, W., Algeri, M., De Gioia, L., Chiesa, R., et al. (1996) Activation effects of a prion protein fragment [PrP-(106-126)] on human leucocytes. Biochem. J. 320, 563–570.

    PubMed  CAS  Google Scholar 

  83. Bendheim, P. E., Brown, H. R., Rudelli, R. D., Scala, L. J., Goller, N. L., Wen, G. Y., et al. (1992) Nearly ubiquitous tissue distribution of the scrapie agent precursor protein. Neurology 42, 149–156.

    PubMed  CAS  Google Scholar 

  84. Brown, H. R., Goller, N. L., Rudelli, R. D., Merz, G. S., Wolfe, G. C., Wisniewski, H. M., and Robakis, N. K. (1990) The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells. Acta Neuropathol. 80, 1–6.

    Article  PubMed  CAS  Google Scholar 

  85. Brown, D. R., Schmidt, B., and Kretzschmar, H. A. (1998) Prion protein fragment primes type 1 astrocytes to proliferation signals from microglia. Neurobiol. Dis. 4, 410–422.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry, University of Cambridge, Cambridge, UK

    David R. Brown

  2. School of Animal and Microbial Sciences, University of Reading, Reading, UK

    Ian M. Jones

Authors
  1. David R. Brown
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ian M. Jones
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. Department of Experimental Psychology, MRC Comparative Cognition Team, School of Clinical Veterinary Medicine, Cambridge, UK

    Harry F. Baker

Rights and permissions

Reprints and permissions

Copyright information

© 2001 Humana Press Inc.

About this protocol

Cite this protocol

Brown, D.R., Jones, I.M. (2001). A Function for the Prion Protein?. In: Baker, H.F. (eds) Molecular Pathology of the Prions. Methods in Molecular Medicine™, vol 59. Humana Press. https://doi.org/10.1385/1-59259-134-5:31

Download citation

  • DOI: https://doi.org/10.1385/1-59259-134-5:31

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-924-7

  • Online ISBN: 978-1-59259-134-3

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics

Search

Navigation