Free Access
Vet. Res.
Volume 39, Number 4, July-August 2008
Prion diseases in animals
Number of page(s) 17
Published online 05 June 2008
How to cite this article Vet. Res. (2008) 39:48
References of Vet. Res. 39 (2008) 481-17
  1. Aronoff-Spencer E., Burns C.S., Avdievich N.I., Gerfen G.J., Peisach J., Antholine W.E., et al., Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy, Biochemistry (2000) 39:13760–13771.
  2. Azzalin A., Ferrara V., Arias A., Cerri S., Avella D., Pisu M.B., et al., Interaction between the cellular prion (PrP$^{\rm C})$ and the 2P domain K+ channel TREK-1 protein, Biochem. Biophys. Res. Commun. (2006) 346:108–115.
  3. Baron G.S., Wehrly K., Dorward D.W., Chesebro B., Caughey B., Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrP $^{\rm Sc})$ into contiguous membranes, EMBO J. (2002) 21:1031–1040.
  4. Baskakov I.V., Legname G., Baldwin M.A., Prusiner S.B., Cohen F.E., Pathway complexity of prion protein assembly into amyloid, J. Biol. Chem. (2002) 277:21140–21148.
  5. Bate C., Salmona M., Diomede L., Williams A., Squalestatin cures prion-infected neurons and protects against prion neurotoxicity, J. Biol. Chem. (2004) 279:14983–14990.
  6. Baumann M.H., Kallijärvi J., Lankinen H., Soto C., Haltia M., Apolipoprotein E includes a binding site which is recognized by several amyloidogenic polypeptides, Biochem. J. (2000) 349:77–84.
  7. Beck K.E., Kay J.G., Braun J.E., Rdj2, a J protein family member, interacts with cellular prion PrP$^{\rm C}$, Biochem. Biophys. Res. Commun. (2006) 346:866–871.
  8. Bocharova O.V., Breydo L., Parfenov A.S., Salnikov V.V., Baskakov I.V., In vitro conversion of full-length Mammalian prion protein produces amyloid form with physical properties of PrP$^{\rm Sc}$, J. Mol. Biol. (2005) 346:645–659.
  9. Borchelt D.R., Scott M., Taraboulos A., Stahl N., Prusiner S.B., Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells, J. Cell Biol. (1990) 110:743–752.
  10. Bossers A., de Vries R., Smits M.A., Susceptibility of sheep for scrapie as assessed by in vitro conversion of nine naturally occurring variants of PrP, J. Virol. (2000) 74:1407–1414.
  11. Brown D.R., Schmidt B., Kretzschmar H.A., Prion protein fragment interacts with PrP-deficient cells, J. Neurosci. Res. (1998) 52:260–267.
  12. Campana V., Sarnataro D., Fasano C., Casanova P., Paladino S., Zurzolo C., Detergent-resistant membrane domains but not the proteasome are involved in the misfolding of a PrP mutant retained in the endoplasmic reticulum, J. Cell. Sci. (2006) 119:433–442.
  13. Castilla J., Saá P., Hetz C., Soto C., In vitro generation of infectious scrapie prions, Cell (2005) 121:195–206.
  14. Caughey B., Race R.E., Vogel M., Buchmeier M.J., Chesebro B., In vitro expression in eukaryotic cells of a prion protein gene cloned from scrapie-infected mouse brain, Proc. Natl. Acad. Sci. USA (1988) 85:4657–4661.
  15. Caughey B., Race R.E., Ernst D., Buchmeier M.J., Chesebro B., Prion protein biosynthesis in scrapie-infected and uninfected neuroblastoma cells, J. Virol. (1989) 63:175–181.
  16. Caughey B., Lansbury P.T., Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders, Annu. Rev. Neurosci. (2003) 26:267–298.
  17. Chabry J., Ratsimanohatra C., Sponne I., Elena P.P., Vincent J.P., Pillot T., In vivo and in vitro neurotoxicity of the human prion protein (PrP) fragment P118-135 independently of PrP expression, J. Neurosci. (2003) 23:462–469.
  18. Chernoff Y.O., Stress and prions: lessons from the yeast model, FEBS Lett. (2007) 581:3695–3701.
  19. Chesebro B., Trifilo M., Race R., Meade-White K., Teng C., LaCasse R., et al., Anchorless prion protein results in infectious amyloid disease without clinical scrapie, Science (2005) 308:1435–1439.
  20. Chich J.F., Schaeffer B., Bouin A.P., Mouthon F., Labas V., Larramendy C., et al., Prion infection-impaired functional blocks identified by proteomics enlighten the targets and the curing pathways of an anti-prion drug, Biochim. Biophys. Acta (2007) 1774:154–167.
  21. Chien P., Weissman J.S., DePace A.H., Emerging principles of conformation-based prion inheritance, Annu. Rev. Biochem. (2004) 73:617–656.
  22. Coitinho A.S., Lopes M.H., Hajj G.N., Rossato J.I., Freitas A.R., Castro C.C., et al., Short-term memory formation and long-term memory consolidation are enhanced by cellular prion association to stress-inducible protein 1, Neurobiol. Dis. (2007) 26:282–290.
  23. Collinge J., Clarke A.R., A general model of prion strains and their pathogenicity, Science (2007) 318:930–936.
  24. Critchley P., Kazlauskaite J., Eason R., Pinheiro T.J., Binding of prion proteins to lipid membranes, Biochem. Biophys. Res. Commun. (2004) 313:559–567.
  25. Cunningham C., Deacon R., Wells H., Boche D., Waters S., Diniz C.P., et al., Synaptic changes characterize early behavioural signs in the ME7 model of murine prion disease, Eur. J. Neurosci. (2003) 17:2147–2155.
  26. De Simone A., Dodson G.G., Fraternali F., Zagari A., Water molecules as structural determinants among prions of low sequence identity, FEBS Lett. (2006) 580:2488–2494.
  27. DebBurman S.K., Raymond G.J., Caughey B., Lindquist S., Chaperone-supervised conversion of prion protein to its protease-resistant form, Proc. Natl. Acad. Sci. USA (1997) 94:13938–13943.
  28. Dima R.I., Thirumalai D., Probing the instabilities in the dynamics of helical fragments from mouse PrP$^{\rm C}$, Proc. Natl. Acad. Sci. USA (2004) 101:15335–15340.
  29. Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E., 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) 94:13452–13457.
  30. Eberl H., Tittmann P., Glockshuber R., Characterization of recombinant, membrane-attached full-length prion protein, J. Biol. Chem. (2004) 279:25058–25065.
  31. Edenhofer F., Rieger R., Famulok M., Wendler W., Weiss S., Winnacker E.L., Prion protein PrP$^{\rm C}$ interacts with molecular chaperones of the Hsp60 family, J. Virol. (1996) 70:4724–4728.
  32. Eghiaian F., Grosclaude J., Lesceu S., Debey P., Doublet B., Tréguer E., et al., Insight into the PrP$^{\rm C}$ $\rightarrow$ PrP$^{\rm Sc}$ conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants, Proc. Natl. Acad. Sci. USA (2004) 101:10254–10259.
  33. Eghiaian F., Daubenfeld T., Quenet Y., van Audenhaege M., Bouin A.P., van der Rest G., et al., Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage, Proc. Natl. Acad. Sci. USA (2007) 104:7414–7419.
  34. 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) 98:9295–9299.
  35. Féraudet C., Morel N., Simon S., Volland H., Frobert Y., Créminon C., et al., Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells, J. Biol. Chem. (2005) 280:11247–11258.
  36. Fischer M., Rülicke T., Raeber A.J., Sailer A., Moser M., Oesch B., et al., Prion portein (PrP) with amino-proximal deletions restoring susceptibility of PrP konckout mice to scrapie, EMBO J. (1996) 15:1255–1264.
  37. Fischer M.B., Roeckl C., Parizek P., Schwarz H.P., Aguzzi A., Binding of disease-associated prion protein to plasminogen, Nature (2000) 408:479–483.
  38. Gabizon R., Meiner Z., Halimi M., Ben-Sasson S.A., Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate, J. Cell. Physiol. (1993) 157:319–325.
  39. Gajdusek D.C., Transmissible and non-transmissible amyloidoses: autocatalytic post-translational conversion of host precursor proteins to $\beta$-pleated sheet configurations, J. Neuroimmunol. (1988) 20:95–110.
  40. Giese A., Groschup M.H., Hess B., Kretzschmar H.A., Neuronal cell death in scrapie-infected mice is due to apoptosis, Brain Pathol. (1995) 5:213–221.
  41. Gossert A.D., Bonjour S., Lysek D.A., Fiorito F., Wüthrich K., Prion protein NMR structures of elk and of mouse/elk hybrids, Proc. Natl. Acad. Sci. USA (2005) 102:646–650.
  42. Graner E., Mercadante A.F., Zanata S.M., Forlenza O.V., Cabral A.L., Veiga S.S., et al., Cellular prion protein binds laminin and mediates neuritogenesis, Brain Res. Mol. Brain Res. (2000) 76:85–92.
  43. Haire L.F., Whyte S.M., Vasisht N., Gill A.C., Verma C., Dodson E.J., et al., The crystal structure of the globular domain of sheep prion protein, J. Mol. Biol. (2004) 336:1175–1183.
  44. Hajj G.N., Lopes M.H., Mercadante A.F., Veiga S.S., da Silveira R.B., Santos T.G., et al., Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins, J. Cell Sci. (2007) 120:1915–1926.
  45. Heppner F.L., Musahl C., Arrighi I., Klein M.A., Rülicke T., Oesch B., et al., Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies, Science (2001) 294:178–182.
  46. Hornemann S., Schorn C., Wüthrich K., NMR structure of the bovine prion protein isolated from healthy calf brains, EMBO Rep. (2004) 5:1159–1164.
  47. Hornshaw M.P., McDermott J.R., Candy J.M., Lakey J.H., Copper binding to the N-terminal tandem repeat region of mammalian and avian prion protein: structural studies using synthetic peptides, Biochem. Biophys. Res. Commun. (1995) 214:993–999.
  48. Hundt C., Peyrin J.M., Haïk S., Gauczynski S., Leucht C., Rieger R., et al., Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor, EMBO J. (2001) 20:5876–5886.
  49. Hunter N., Goldmann W., Benson G., Foster J.D., Hope J., Swaledale sheep affected by natural scrapie differ significantly in PrP genotype frequencies from healthy sheep and those selected for reduced incidence of scrapie, J. Gen. Virol. (1993) 74:1025–1031.
  50. Jansen K., Schäfer O., Birkmann E., Post K., Serban H., Prusiner S.B., et al., Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form, Biol. Chem. (2001) 382:683–691.
  51. Jarrett J.T., Lansbury P.T. Jr., Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?, Cell (1993) 73:1055–1058.
  52. Jeffrey M., Halliday W.G., Bell J., Johnston A.R., MacLeod N.K., Ingham C., et al., Synapse loss associated with abnormal PrP precedes neuronal degeneration in the scrapie-infected murine hippocampus, Neuropathol. Appl. Neurobiol. (2000) 26:41–54.
  53. Jones E.M., Surewicz W.K., Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids, Cell (2005) 121:63–72.
  54. Kaneko K., Zulianello L., Scott M., Cooper C.M., Wallace A.C., James T.L., 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) 94:10069–10074.
  55. Kazlauskaite J., Sanghera N., Sylvester I., Vénien-Bryan C., Pinheiro T.J., Structural changes of the prion protein in lipid membranes leading to aggregation and fibrillization, Biochemistry (2003) 42:3295–3304.
  56. Kazlauskaite J., Young A., Gardner C.E., Macpherson J.V., Vénien-Bryan C., Pinheiro T.J., An unusual soluble $\beta$-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells, Biochem. Biophys. Res. Commun. (2005) 328:292–305.
  57. Kourie J.I., Culverson A., Prion peptide fragment PrP(106-126) forms distinct cation channel types, J. Neurosci. Res. (2000) 62:120–133.
  58. Kurschner C., Morgan J.I., The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system, Brain Res. Mol. Brain Res. (1995) 30:165–168.
  59. Lee K.S., Caughey B., A simplified recipe for prions, Proc. Natl. Acad. Sci. USA (2007) 104:9551–9552.
  60. Legname G., Baskakov I.V., Nguyen H.O., Riesner D., Cohen F.E., DeArmond S.J., et al., Synthetic mammalian prions, Science (2004) 305:673–676.
  61. Lopes M.H., Hajj G.N., Muras A.G., Mancini G.L., Castro R.M., Ribeiro K.C., et al., Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways, J. Neurosci. (2005) 25:11330–11339.
  62. López Garcia F., Zahn R., Riek R., Wüthrich K., NMR structure of the bovine prion protein, Proc. Natl. Acad. Sci. USA (2000) 97:8334–8339.
  63. Lu X., Wintrode P.L., Surewicz W.K., $\beta$-sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange, Proc. Natl. Acad. Sci. USA (2007) 104:1510–1515.
  64. Lysek D.A., Schorn C., Nivon L.G., Esteve-Moya V., Christen B., Calzolai L., et al., Prion protein NMR structures of cats, dogs, pigs, and sheep, Proc. Natl. Acad. Sci. USA (2005) 102:640–645.
  65. Ma J., Lindquist S., Conversion of PrP to a self-perpetuating PrP$^{\rm Sc}$-like conformation in the cytosol, Science (2002) 298:1785–1788.
  66. Ma J., Wollmann R., Lindquist S., Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol, Science (2002) 298:1781–1785.
  67. Maissen M., Roeckl C., Glatzel M., Goldmann W., Aguzzi A., Plasminogen binds to disease-associated prion protein of multiple species, Lancet (2001) 357:2026–2028.
  68. Makarava N., Baskakov I.V., The same primary structure of the prion protein yields two distinct self-propagating states, J. Biol. Chem. (2008) 283:15988–15996.
  69. Martins S.M., Chapeaurouge A., Ferreira S.T., Folding intermediates of the prion protein stabilized by hydrostatic pressure and low temperature, J. Biol. Chem. (2003) 278:50449–50455.
  70. Martins V.R., Graner E., Garcia-Abreu J., de Souza S.J., Mercadante A.F., Veiga S.S., et al., Complementary hydropathy identifies a cellular prion protein receptor, Nat. Med. (1997) 3:1376–1382.
  71. Martins V.R., A receptor for infectious and cellular prion protein, Braz. J. Med. Biol. Res. (1999) 32:853–859.
  72. Mattei V., Garofalo T., Misasi R., Gizzi C., Mascellino M.T., Dolo V., et al., Association of cellular prion protein with gangliosides in plasma membrane microdomains of neural and lymphocytic cells, Neurochem. Res. (2002) 27:743–749.
  73. May B.C., Govaerts C., Prusiner S.B., Cohen F.E., Prions: so many fibers, so little infectivity, Trends Biochem. Sci. (2004) 29:162–165.
  74. Moore R.A., Vorberg I., Priola S.A., Species barriers in prion diseases – brief review, Arch. Virol. Suppl. (2005) 187–202.
  75. Morillas M., Swietnicki W., Gambetti P., Surewicz W.K., Membrane environment alters the conformational structure of the recombinant human prion protein, J. Biol. Chem. (1999) 274:36859–36865.
  76. Morillas M., Vanik D.L., Surewicz W.K., On the mechanism of $\alpha$-helix to $\beta$-sheet transition in the recombinant prion protein, Biochemistry (2001) 40:6982–6987.
  77. Morot-Gaudry-Talarmain Y., Rezaei H., Guermonprez L., Treguer E., Grosclaude J., Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin, J. Neurochem. (2003) 87:1456–1470.
  78. Morrissey M.P., Shakhnovich E.I., Evidence for the role of PrP$^{\rm C}$ helix 1 in the hydrophilic seeding of prion aggregates, Proc. Natl. Acad. Sci. USA (1999) 96:11293–11298.
  79. Mouillet-Richard S., Ermonval M., Chebassier C., Laplanche J.L., Lehmann S., Launay J.M., Kellermann O., Signal transduction through prion protein, Science (2000) 289:1925–1928.
  80. Nandi P.K., Interaction of prion peptide HuPrP106-126 with nucleic acid, Arch. Virol. (1997) 142:2537–2545.
  81. Nandi P.K., Sizaret P.Y., Murine recombinant prion protein induces ordered aggregation of linear nucleic acids to condensed globular structures, Arch. Virol. (2001) 146:327–345.
  82. Naslavsky N., Shmeeda H., Friedlander G., Yanai A., Futerman A.H., Barenholz Y., et al., Sphingolipid depletion increases formation of the scrapie prion protein in neuroblastoma cells infected with prions, J. Biol. Chem. (1999) 274:20763–20771.
  83. Novitskaya V., Bocharova O.V., Bronstein I., Baskakov I.V., Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons, J. Biol. Chem. (2006) 281:13828–13836.
  84. Novitskaya V., Makarava N., Sylvester I., Bronstein I.B., Baskakov I.V., Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2-derived terminally differentiated neurons, J. Neurochem. (2007) 102:398–407.
  85. Oboznaya M.B., Gilch S., Titova M.A., Koroev D.O., Volkova T.D., Volpina O.M., et al., Antibodies to a nonconjugated prion protein peptide 95-123 interfere with PrP$^{\rm Sc}$ propagation in prion-infected cells, Cell. Mol. Neurobiol. (2007) 27:271–284.
  86. Oesch B., Westaway D., Wälchli M., McKinley M.P., Kent S.B., Aebersold R., et al., A cellular gene encodes scrapie PrP 27-30 protein, Cell (1985) 40:735–746.
  87. Oesch B., Teplow D.B., Stahl N., Serban D., Hood L.E., Prusiner S.B., Identification of cellular proteins binding to the scrapie prion protein, Biochemistry (1990) 29:5848–5855.
  88. Oosawa F., Asakura S., Thermodynamics of the polymerization of protein, Academic Press, New York, USA, 1975, p. 223.
  89. Owen J.P., Rees H.C., Maddison B.C., Terry L.A., Thorne L., Jackman R., et al., Molecular profiling of ovine prion diseases by using thermolysin-resistant PrP$^{\rm Sc}$ and endogenous C2 PrP fragments, J. Virol. (2007) 81:10532–10539.
  90. Pan K.M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., et al., Conversion of $\alpha$-helices into $\beta$-sheets features in the formation of the scrapie prion proteins, Proc. Natl. Acad. Sci. USA (1993) 90:10962–10966.
  91. Parizek P., Roeckl C., Weber J., Flechsig E., Aguzzi A., Raeber A.J., Similar turnover and shedding of the cellular prion protein in primary lymphoid and neuronal cells, J. Biol. Chem. (2001) 276:44627–44632.
  92. Peretz D., Williamson R.A., Kaneko K., Vergara J., Leclerc E., Schmitt-Ulms G., et al., Antibodies inhibit prion propagation and clear cell cultures of prion infectivity, Nature (2001) 412:739–743.
  93. Peretz D., Williamson R.A., Legname G., Matsunaga Y., Vergara J., Burton D.R., et al., A change in the conformation of prions accompanies the emergence of a new prion strain, Neuron (2002) 34:921–932.
  94. Pillot T., Drouet B., Pinçon-Raymond M., Vandekerckhove J., Rosseneu M., Chambaz J., A nonfibrillar form of the fusogenic prion protein fragment (118-135) induces apoptotic cell death in rat cortical neurons, J. Neurochem. (2000) 75:2298–2308.
  95. Prusiner S.B., Novel proteinaceous infectious particles cause scrapie, Science (1982) 216:136–144.
  96. Prusiner S.B., Prions, Proc. Natl. Acad. Sci. USA (1998) 95:13363–13383.
  97. Rambold A.S., Miesbauer M., Rapaport D., Bartke T., Baier M., Winklhofer K.F., et al., Association of Bcl-2 with misfolded prion protein is linked to the toxic potential of cytosolic PrP, Mol. Biol. Cell (2006) 17:3356–3368.
  98. Rezaei H., Choiset Y., Eghiaian F., Treguer E., Mentre P., Debey P., et al., Amyloidogenic unfolding intermediates differentiate sheep prion protein variants, J. Mol. Biol. (2002) 322:799–814.
  99. Rezaei H., Eghiaian F., Perez J., Doublet B., Choiset Y., Haertle T., et al., Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities, J. Mol. Biol. (2005) 347:665–679.
  100. Rieger R., Edenhofer F., Lasmézas C.I., Weiss S., The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells, Nat. Med. (1997) 3:1383–1388.
  101. Riek R., Hornemann S., Wider G., Billeter M., Glockshuber R., Wüthrich K., NMR structure of the mouse prion protein domain PrP (121-321), Nature (1996) 382:180–182.
  102. Rogers M., Yehiely F., Scott M., Prusiner S.B., Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells, Proc. Natl. Acad. Sci. USA (1993) 90:3182–3186.
  103. Rudd P.M., Endo T., Colominas C., Groth D., Wheeler S.F., Harvey D.J., et al., Glycosylation differences between the normal and pathogenic prion protein isoforms, Proc. Natl. Acad. Sci. USA (1999) 96:13044–13049.
  104. Rybner C., Finel-Szermanski S., Felin M., Sahraoui T., Rousseau C., Fournier J.G., et al., The cellular prion protein: a new partner of the lectin CBP70 in the nucleus of NB4 human promyelocytic leukemia cells, J. Cell. Biochem. (2002) 84:408–419.
  105. Ryou C., Prusiner S.B., Legname G., Cooperative binding of dominant-negative prion protein to kringle domains, J. Mol. Biol. (2003) 329:323–333.
  106. Safar J., Ceroni M., Gajdusek D.C., Gibbs C.J. Jr., Differences in the membrane interaction of scrapie amyloid precursor proteins in normal and scrapie- or Creutzfeldt-Jakob disease-infected brains, J. Infect. Dis. (1991) 163:488–494.
  107. Sanghera N., Pinheiro T.J., Binding of prion protein to lipid membranes and implications for prion conversion, J. Mol. Biol. (2002) 315:1241–1256.
  108. Schirmer E.C., Lindquist S., Interactions of the chaperone Hsp104 with yeast Sup35 and mammalian PrP, Proc. Natl. Acad. Sci. USA (1997) 94:13932–13937.
  109. Schmitt-Ulms G., Legname G., Baldwin M.A., Ball H.L., Bradon N., Bosque P.J., et al., Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein, J. Mol. Biol. (2001) 314:1209–1225.
  110. Shmerling D., Hegyi I., Fischer M., Blättler T., Brandner S., Götz J., et al., Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions, Cell (1998) 93:203–214.
  111. Shyng S.L., Lehmann S., Moulder K.L., Harris D.A., Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrP$^{\rm C}$, in cultured cells, J. Biol. Chem. (1995) 270:30221–30229.
  112. Shyu W.C., Harn H.J., Saeki K., Kubosaki A., Matsumoto Y., Onodera T., et al., Molecular modulation of expression of prion protein by heat shock, Mol. Neurobiol. (2002) 26:1–12.
  113. Silveira J.R., Raymond G.J., Hughson A.G., Race R.E., Sim V.L., Hayes S.F., et al., The most infectious prion protein particles, Nature (2005) 437:257–261.
  114. Simoneau S., Rezaei H., Salès N., Kaiser-Schulz G., Lefebvre-Roque M., Vidal C., et al., In vitro and in vivo neurotoxicity of prion protein oligomers, PLoS Pathog. (2007) 3:e125.
  115. Spielhaupter C., Schätzl H.M., PrP$^{\rm C}$ directly interacts with proteins involved in signaling pathways, J. Biol. Chem. (2001) 276:44604–44612.
  116. Stahl N., Borchelt D.R., Hsiao K., Prusiner S.B., Scrapie prion protein contains a phosphatidylinositol glycolipid, Cell (1987) 51:229–240.
  117. Stahl N., Borchelt D.R., Prusiner S.B., Differential release of cellular and scrapie prion proteins from cellular membranes by phosphatidylinositol-specific phospholipase C, Biochemistry (1990) 29:5405–5412.
  118. Stahl N., Prusiner S.B., Prions and prion proteins, FASEB J. (1991) 5:2799–2807.
  119. Stöckel J., Safar J., Wallace A.C., Cohen F.E., Prusiner S.B., Prion protein selectively binds copper(II) ions, Biochemistry (1998) 37:7185–7193.
  120. Sun Y., Makarava N., Lee C.I., Laksanalamai P., Robb F.T., Baskakov I.V., Conformational stability of PrP amyloid fibrils controls their smallest possible fragment size, J. Mol. Biol. (2008) 376:1155–1167.
  121. Sunyach C., Jen A., Deng J., Fitzgerald K.T., Frobert Y., Grassi J., et al., The mechanism of internalization of glycosylphosphatidylinositol-anchored prion protein, EMBO J. (2003) 22:3591–3601.
  122. Swietnicki W., Morillas M., Chen S.G., Gambetti P., Surewicz W.K., Aggregation and fibrillization of the recombinant human prion protein huPrP90-231, Biochemistry (2000) 39:424–431.
  123. Taraboulos A., Scott M., Semenov A., Avrahami D., Laszlo L., Prusiner S.B., Cholesterol depletion and modification of COOH-terminal targeting sequence of the prion protein inhibit formation of the scrapie isoform, J. Cell Biol. (1995) 129:121–132.
  124. Tatzelt J., Zuo J., Voellmy R., Scott M., Hartl U., Prusiner S.B., et al., Scrapie prions selectively modify the stress response in neuroblastoma cells, Proc. Natl. Acad. Sci. USA (1995) 92:2944–2948.
  125. Telling G.C., Scott M., Mastriannni J., Gabizon R., Torchia M., Cohen F.E., 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.
  126. Telling G.C., Parchi P., DeArmond S.J., Cortelli P., Montagna P., Gabizon R., et al., Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity, Science (1996) 274:2079–2082.
  127. Toni M., Spisni E., Griffoni C., Santi S., Riccio M., Lenaz P., et al., Cellular prion protein and caveolin-1 interaction in a neuronal cell line precedes fyn/erk 1/2 signal transduction, J. Biomed. Biotechnol. (2006) 2006:69469.
  128. Weiss S., Proske D., Neumann M., Groschup M.H., Kretzschmar H.A., Famulok M., et al., RNA aptamers specifically interact with the prion protein PrP, J. Virol. (1997) 71:8790–8797.
  129. Yehiely F., Bamborough P., Da Costa M., Perry B.J., Thinakaran G., Cohen F.E., et al., Identification of candidate proteins binding to prion protein, Neurobiol. Dis. (1997) 3:339–355.