Alper, T., Cramp, W. A., Haig, D. A., and Clarke, M. C. (1967). Does the Agent of Scrapie Replicate without Nucleic Acid? Nature 214, 764-766.

Ananthan, J., Goldberg, A. R., and Voellmy, R. (1986). Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heatshock genes. Science 232, 252-58.

Basler, K., Oesch, B., Scott, M., Westaway, D., WE4lchli, M., Groth, D. F., McKinley, M. P., Prusiner, S. B., and Weismann, C. (1986) Scrapie and Cellular PrP Isoforms Are Encoded by the Same Chromosomal Gene. Cell 46, 417-428.

Borchelt, D. R., Scott, M. Taraboulos A., Stahl, N., and Prusiner, S. B. (1990). Scrapie and Cellular Prion Proteins Differ in Their Kinetics of Synthesis and Topology in Cultured Cells. J. Cell Biol. 110, 743-752.

Borchelt, D. R., Taraboulos, A., and Prusiner, S. A. (1992). Evidence for Synthesis of Scrapie Prion Proteins in the Endocytic Pathway. J. Biol. Chem. 267(23), 16188-16199.

Braig, H. R., and Diringer, H. (1985). Scrapie: concept of a virus-induced amyloidosis of the brain. EMBO J. 4(9), 2309-2312.

Brown, C. R., Martin, R. L., Hansen, W. J., Beckmann, R. P., and Welch, W. J. (1993). The Constitutive and Stress Inducible Forms of hsp70 Exhibit Functional Similarities and Interact with One Another in an ATP-dependent Fashion. J. Cell Biol. 120(5), 1101-12.

Bruce, M. E., and Dickinson, A. G. (1987) Biological Evidence that Scrapie has an Independent Genome. J. gen. Virol. 68, 79-89.

Bueler, H., Aguzzi, A., Sailer, A., Greiner, R.-A., Autenried, P., et al. (1993). Mice devoid of PrP are resistant to scrapie. Cell 73, 1339-47.

Bueler, H., Fischer, M., Lang, Y., Bluthmann, H., Lipp, H.-L., et al. (1992). The neuronal cell surface protein PrP is not essential for normal development and behavior of the mouse. Nature 356, 577-582.

Butler D. A., Michael, R. D., Bockman, J. M., Borchelt, Taraboulos, A., Hsiao, K. K., Kingsbury, D. T., and Prusiner, S. B. (1988). Scrapie-Infected Murine Neuroblastoma Cells Produce Protease-Resistant Prion Proteins. J. Virol. 62(5), 1558-1564.

Caughey, B., Neary, K., Buller, R., Ernst, D., Perry, L. L., Chesebro, B., Race, R. E. (1990). Normal and Scrapie-Associated Forms of Prion Protein Differ in Their Sensitivities to Phospholipase and Proteases in Intact Neuroblastoma Cells. J. Virol. 64(3), 1093-1101.

Caughey, B., and Raymond, G. J. (1991). The scrapie-associated form of PrP is made from a cell surface precursor that is both protease and phospholipase sensitive. J. Biol. Chem. 266, 18217-18223.

Chavrier, P., Parton, R. G., Hauri, H. P., Simons K., and Zerial, M. (1990). Localization of Low Molecular Weight GTP Binding Proteins to Exocytic and Endocytic Compartments. Cell 62, 317-329.

Cheng, M. Y., Hartl, F.-U., and Horwich, A. L. (1990). The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348, 455-58.

Chernoff, Y. O., Lindquist, S. L., Ono, B.-i. Inge-Vechtomov, S. G., and Liebman, S. W. (1995). Role of the Chaperone Protein Hsp104 in Propagation of the Yeast Prion-Like Factor [psi+]. Science 268, 880-884.

Cho, H. J. (1976) Is the scrapie agent a virus? Nature 262, 412-413.

Clarke, C. F., Cheng, K., Frey, A. B., Stein, R., Hinds, P. W., Levine, A. J. (1988). Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and dnaK from murine p53 by ATP. Mol. Cell. Biol. 8(3), 1206-15.

Come, J. H., Fraser, P. E., and Lansbury, P. T., Jr. (1993). Proc. Natl. Acad. Sci. USA 90, 5959-5963.

DeArmond, S. J., McKinley, M. P., Barry, R. A., Braunfeld, M. B., McColloch, J. R., and Prusiner, S. B. (1985). Identification of Prion Amyloid Filaments in Scrapie-Infected Brain. Cell 41, 221-235.

Doms, R. W., Russ, G., Yewdell, J. W. (1989). Brefeldin A redistributes resident and itinerant Golgi proteins to the endoplasmic reticulum. J. Cell Biol. 109(1), 61-72.

Endo, T., Groth, D., Prusiner, S. B., and Kobata, A. (1989). Diversity of Oligosaccharide Structures Linked to Asparagines of the Scrapie Prion Protein. Biochemistry 28, 8380-8388.

Gajdusek, D. C. (1988). Mt. Sinai J. Med. 55, 3-5.

Goodloe-Holland, C. M., and Luna, E. J. (1987). Purification and Characterization of Dictyostelium discoideum Plasma Membranes. Methods in Cell Biology, ed Spudich, J. A. (Academic, New York), Vol. 28, pp.103-128.

Griffiths, G., Hoflack, B., Simons, K., Mellman, I., and Kornfeld, S. (1988). The Mannose 6-Phosphate Receptor and the Biogenesis of Lysosomes. Cell 52, 329-341

Hadlow, W. J., Race, R. E., Kennedy, R. C., and Eklund, C. M. (1979). Natural infection of sheep with scrapie virus. In Slow Transmissible Diseases of the Nervous System, 2, S. B. Prusiner and W. J. Hadlow, eds. (New York: Academic Press), pp. 3-12.

Hamos, J. E., Oblas, B., Pulaski-Salo, D., Welch, W. J., Bole, D. G., and Drachman, D. A. (1991). Expression of heat shock proteins in Alzheiner's disease. Neurology 41(3), 345-50.

Hopkins, C. R., and Trowbridge, I. S. (1983). Internalization and processing of transferrin and the transferrin receptor in human carcinoma A431 cells. J. Cell Biol. 97, 508-21.

Jarrett, J. T., and Lansbury, P. T., Jr. (1993) Cell 73, 1055-1058.

Kimberlin, R. H., and Hunter, G. D. (1967). J. Gen. Virol. 1, 115.

Kocisko, D. A., Come, J. H., Priola, S. A., Chesebro, B., Raymond, G. J., Lansbury, P. T., and Caughey, B. (1994). Cell-free formation of protease- resistant prion protein. Nature 370, 471-474.

McKinley, M. P., Taraboulos, A., Kenaga, L., Serban, D., Steiber, A., DeArmond, S. J., Prusiner, S. B., and Gonatas, N. (1991). Ultrastructural Localization of Scrapie Prion Proteins in Cytoplasmic Vesicles of Infected Cultured Cells. Lab. Invest. 65(6), 622-30.

Meyer, R. K., McKinley, M. P., Bowman, K. A., Braunfeld, M. B., Barry, R. A., and Prusiner, S. B. (1986). Separation and properties of cellular and scrapie prion proteins. Proc. Natl. Acad. Sci. USA 83, 2310-2314.

Milner, J., and Medcalf, E. A. (1991). Cotranslation of Activated Mutant p53 with Wild Type Drives the Wild-Type p53 Protein into the Mutant Conformation. Cell 65, 765-74.

Mu, F-.T., Callaghan, J. M., Steele-Mortimer, Stenmark, H., Parton, R. G., Campbell, P. L., McCluskey, J., Yeo, J-.P., Tock, E. P. C., and Toh, B-.H. (1995). EEA1, an Early Endosome- Associated Protein. J. Biol. Chem. 270(22), 13503-13511.

Oesch, B., Westaway, D., Walchli, M., McKinley, M. P., Kent, S. B. H., Aebersold, R., Barry, R. A., Tempst, P., Teplow, D. B., Hood, L. E., Prusiner, S. B., and Weissmann, C. (1985). A Cellular Gene Encodes Scrapie PrP 27-30 Protein. Cell 40, 735-746.

Pan, K.-M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Melhorn, I., Huang, Z., Fletterick, R. J., Cohen, F. E., and Prusiner, S. B. (1993). Conversion of a-helices into b-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90, 10962- 10966.

Papini, E., de Bernard, M., Milia, E., Bugnoli, M., Zerial, M., Rappuoli, R., Montecucco, C. (1994). Cellular vacuoles induced by Helicobacter pylori originate from late endosomal compartments. Proc. Natl. Acad. Sci. USA 91(21), 9720-9724.

Parsell, D. A., Sanchez, Y., Stitzel, J. D., Lindquist, S. (1991). Hsp104 as a highly conserved protein with two essential nucleotide-binding sites. Nature 353, 270-273.

Perez, N., Sugar, J., Charya, S., Johnson, G., Merril, C., Bierer, L., Perl, D., Haroutunian, V., and Wallace, W. (1991). Increased synthesis and accumulation of heat shock 70 proteins in Alzheimer's disease. Brain Research. Mol. Brain Res. 11(3-4), 249-54.

Pfeifer, K., Bachmann, M., Schroder, H. C., Forrest, J., and MFCller, W. E. G. (1993). Kinetics of Expression of Prion Protein in Uninfected and Scrapie-infected N2a Mouse Neuroblastoma Cells. Cell. Biochem. Func. 11, 1-11.

Priola, S. A., Caughey, B., Wehrly, K., and Chesebro, B. (1995). A 60-kDa Prion Protein (PrP) with properties of Both the Normal and Scrapie-associated Forms of PrP. J. Biol. Chem. 270(7), 3299- 3305.

Prusiner, S. B., Groth, D., Serban, A., Koehler, R., Foster, D., et al. (1993). Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. USA 90, 10608-12.

Prusiner, S. B. (1992). Chemistry and Biology of Prions. Biochemistry 31(49), 12277-87.

Prusiner, S. B. (1991). Novel Properties and Biology of Scrapie Prions. Curr. Topics Microbiol. Immun. 172, 233-257

Prusiner, S. B., Bolton, D. C., Groth, D. F., Bowman, K. A., Cochran, S. P., and McKinley, M. P. (1982). Further Purification and Characterization of Scrapie Prions. Biochemistry 21(26), 6942- 50.

Prusiner, S. B. (1982). Novel Proteinaceous Infectious Particles Cause Scrapie. Science 216,136-144.

Raeber, A. J., Borchelt, D. R., Scott, M., and Prusiner, S. B. (1992). Attempts To Convert the Cellular Prion Protein into the Scrapie Isoform in Cell-Free Systems. J. Virol. 66(10), 6155-6163.

Rexach, M. F., Latterich, M., and Schekman, R. W. (1994). Characteristics of Endoplasmic Reticulum- derived Transport Vesicles. J. Cell Biol. 126(5), 1133-1148.

Rogers, M., Yehiely, F., Scott, M., and Prusiner, S. B. (1993). Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl. Acad. Sci. USA 90, 3182-86.

Sandoval I. V., and Bakke O. (1994). Targeting of membrane proteins to endosomes and lysosomes. Trends Cell Bio. 4, 292-297.

Schmid, S. L., Fuchs, R., Male, P., and Mellman, I. (1988). Two Distinct Subpopulations of Endosomes Involved in Membrane Recycling and Transport to Lysosomes. Cell 52, 73-83.

Scott, M. R., Kohler, R., Foster, D., and Prusiner, S. B. (1992). Chimeric prion protein expression in cultured cells and transgenic mice. Prot. Sci. 1, 986-997.

Shyng, S-.L., Huber, M. T., and Harris, D. A. (1993). A Prion Protein Cycles between the Cell Surface and an Endocytic Compartment in Cultured Neuroblastoma Cells. J. Biol. Chem. 268(21), 15922-15928.

Shyng, S.-L., Heuser, J. E., and Harris, D. A. (1994). A Glycolipid-anchored Prion Protein Is Endocytosed via Clathrin-coated Pits. J. Cell Biol. 125(6), 1239-1250.

Stahl, N., and Prusiner, S. B. (1991). Prions and prion proteins. FASEB J. 5, 2799-2807.

Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987). Scrapie Prion Protein Contains a Phosphatidylinositol Glycolipid. Cell 51, 229-240.

Taraboulos, A., Raeber, A., Borchelt, D., McKinley, M. P., and Prusiner, S. B. (1991). FASEB J. 5, A1177.

Taraboulos, A., Rogers, M., Borchelt, D. R., McKinley, M. P., Scott, M., Serban, D., and Prusiner, S. B. (1990) Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation. Proc. Natl. Acad. Sci. USA 87, 8262-66.

Taraboulos, A., Serban, D., and Prusiner, S. B. (1990). Scrapie Prion Proteins Accumulate in the Cytoplasm of Persistently Infected Cultured Cells. J. Cell Biol. 110, 2117- 32.

Tatzelt, J., Zuo, J., Voellmy, R., Scott, M., Hartl, U., Prusiner, S. B., Welch, W. J. (1995). Scrapie prions selectively modify the stress response in neuroblastoma cells. Proc. Natl. Acad. Sci. USA 92(7), 2944-8.

Tokuko H., Fisher, S., Olofsson, S., Endo, T., Groth, D., Tarentino, A., Borchelt, D. R., Teplow, D., Hood, L., Burlingame, A., Lycke, E., Kobata, A., and Prusiner, S. B. (1989). Asparagine-Linked Glycosylation of the Scrapie and Cellular Prion Proteins. Arch. Biochem. Biophys. 274(1), 1-13.

Weissmann, C. (1994). The Prion Connection: Now in Yeast? Science 264, 528-30.

This reference list includes references that are part of a section on proposed experiments, that has not been included in the Notes on Scrapie link.