Novel aspects of prions, their receptor molecules, and innovative approaches for TSE therapy

Cellular and Molecular Neurobiology

Volumn 27, Issue 1, 2007, Pages 107-128

  Vana, Karen ^a   Zuber, Chantal ^a   Nikles, Daphne ^a   Weiss, Stefan ^a  

^a UNIVERSITY OF MUNICH   (Germany)

Author keywords

37 kDa 67 kDa laminin receptor; Bovine spongiform encephalopathy; Creutzfeldt Jakob disease; Heparan sulfate; LRP LR; Prion; PrP therapy; Transmissible spongiform encephalopathy

Indexed keywords

AMPHOTERICIN B; CELL SURFACE RECEPTOR; CHLORPROMAZINE; CONGO RED; DEXTRAN SULFATE; FILIPIN; FLUPIRTINE; HEPARAN SULFATE; LAMININ RECEPTOR; MEPACRINE; MS 8209; PENTOSAN POLYSULFATE; PHTHALOCYANINE; POLYETHYLENEIMINE; PORPHYRIN DERIVATIVE; PRION PROTEIN; SIALOGLYCOPROTEIN; SURAMIN; TRASTUZUMAB;

ARTICLE; BETA SHEET; BOVINE SPONGIFORM ENCEPHALOPATHY; BREAST CANCER; CIRCULAR DICHROISM; CREUTZFELDT JAKOB DISEASE; HUMAN; INFRARED SPECTROSCOPY; KURU; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PATHOGENESIS; PRION DISEASE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; RNA INTERFERENCE; SIGNAL TRANSDUCTION; SKELETAL MUSCLE; VACCINATION;

ANIMALS; DNA REPLICATION; HEPARITIN SULFATE; HUMANS; MODELS, BIOLOGICAL; PRION DISEASES; PRIONS; RECEPTORS, LAMININ;

ANIMALIA; BOS; BOVINAE; CERVIDAE; OVIS ARIES;

EID: 33846476657     PISSN: 02724340     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10571-006-9121-1     Document Type: Article

References (181)

1. Achour, A. (2002). Phenothiazines and prion diseases: A potential mechanism of action towards oxidative stress. Int. J. Antimicrob. Agents 20:305-306.
2. Adjou, K. T., Demaimay, R., Lasmezas, C., Deslys, J. P., Seman, M., and Dormont, D. (1995). MS-8209, a new amphotericin B derivative, provides enhanced efficacy in delaying hamster scrapie. Antimicrob. Agents Chemother. 39(12):2810-2812.
3. Adjou, K. T., Simoneau, S., Sales, N., Lamoury, F., Dormont, D., Papy-Garcia, D., Barritault, D., Deslys, J. P., and Lasmezas, C. I. (2003). A novel generation of heparan sulfate mimetics for the treatment of prion diseases. J. Gen. Virol. 84(Pt. 9):2595-2603.
4. Akache, B., Grimm, D., Pandey, K., Yant, S. R., Xu, H., and Kay, M. A. (2006). The 37/67-kilodalton Laminin Receptor is a receptor for Adeno-associated-Virus Serotypes 8, 2, 3, and 9. J. Virol. 80(19):9831-9836.
5. Alper, T., Cramp, W. A., Haig, D. A., and Clarke, M. C. (1967). Does the agent of scrapie replicate without nucleic acid? Nature 214(90):764-766.
6. Ardini, E., Pesole, G., Tagliabue, E., Magnifico, A., Castronovo, V., Sobel, M. E., Colnaghi, M. I., and Menard, S. (1998). The 67-kDa laminin receptor originated from a ribosomal protein that acquired a dual function during evolution. Mol. Biol. Evol. 15(8):1017-1025.
7. Arnold, J. E., Tipler, C., Laszlo, L., Hope, J., Landon, M., and Mayer, R. J. (1995). The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain. J. Pathol. 176(4):403-411.
8. Auth, D., and Brawerman, G. (1992). A 33-kDa polypeptide with homology to the laminin receptor: Component of translation machinery. Proc. Natl. Acad. Sci. U. S. A. 89(10):4368-4372.
9. Bainbridge, J., and Walker, K. B. (2005). The normal cellular form of prion protein modulates T cell responses. Immunol. Lett. 96(1):147-150.
10. Ballerini, C., Gourdain, P., Bachy, V., Blanchard, N., Levavasseur, E., Gregoire, S., Fontes, P., Aucouturier, P., Hivroz, C., and Carnaud, C. (2006). Functional implication of cellular prion protein in antigen-driven interactions between T cells and dendritic cells. J. Immunol. 176(12):7254- 7262.
11. Baloui, H., von Boxberg, Y., Vinh, J., Weiss, S., Rossier, J., Nothias, F., and Stettler, O. (2004). Cellular prion protein/laminin receptor: Distribution in adult central nervous system and characterization of an isoform associated with a subtype of cortical neurons. Eur. J. Neurosci. 20(10):2605-2616.
12. Baron, G. S., and Caughey, B. (2003). Effect of glycosylphosphatidylinositol anchor-dependent and - independent prion protein association with model raft membranes on conversion to the protease-resistant isoform. J. Biol. Chem. 278(17):14883-14892.
13. Basler, K., Oesch, B., Scott, M., Westaway, D., Walchli, M., Groth, D. F., McKinley, M. P., Prusiner, S. B., and Weissmann, C. (1986). Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46(3):417-428.
14. Belichenko, P. V., Miklossy, J., Belser, B., Budka, H., and Celio, M. R. (1999). Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease. Neurobiol. Dis. 6(4):269-279.
15. Benito-Leon, J. (2004). Combined quinacrine and chlorpromazine therapy in fatal familial insomnia. Clin. Neuropharmacol. 27(4):201-203.
16. Bertsch, U., Winklhofer, K. F., Hirschberger, T., Bieschke, J., Weber, P., Hartl, F. U., Tavan, P., Tatzelt, J., Kretzschmar, H. A., and Giese, A. (2005). Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets. J. Virol. 79(12):7785-7791.
17. Bolton, D. C., McKinley, M. P., and Prusiner, S. B. (1982). Identification of a protein that purifies with the scrapie prion. Science 218(4579):1309-1311.
18. Bosque, P. J., Ryou, C., Telling, G., Peretz, D., Legname, G., DeArmond, S. J., and Prusiner, S. B. (2002). Prions in skeletal muscle. Proc. Natl. Acad. Sci. U. S. A. 99(6):3812-3817.
19. Botto, L., Masserini, M., Cassetti, A., and Palestini, P. (2004). Immunoseparation of prion protein-enriched domains from other detergent-resistant membrane fractions, isolated from neuronal cells. FEBS Lett. 557(1-3):143-147.
20. Bounhar, Y., Zhang, Y., Goodyer, C. G., and LeBlanc, A. (2001). Prion protein protects human neurons against Bax-mediated apoptosis. J. Biol. Chem. 276(42):39145-39149.
21. Bragason, B. T., and Palsdottir, A. (2005). Interaction of PrP with NRAGE, a protein involved in neuronal apoptosis. Mol. Cell. Neurosci. 29(2):232-244.
22. Brown, D. R., Qin, K., Herms, J. W., Madlung, A., Manson, J., Strome, R., Fraser, P. E., Kruck, T., von Bohlen, A., Schulz-Schaeffer, W., Giese, A., Westaway, D., and Kretzschmar, H. (1997). The cellular prion protein binds copper in vivo. Nature 390(6661):684-687.
23. Brown, D. R., Schmidt, B., Groschup, M. H., and Kretzschmar, H. A. (1998). Prion protein expression in muscle cells and toxicity of a prion protein fragment. Eur. J. Cell Biol. 75(1):29-37.
24. Brown, D. R., Wong, B. S., Hafiz, F., Clive, C., Haswell, S. J., and Jones, I. M. (1999). Normal prion protein has an activity like that of superoxide dismutase. Biochem. J. 344(Pt. 1):1-5.
25. Brown, H. R., Goller, N. L., Rudelli, R. D., Merz, G. S., Wolfe, G. C., Wisniewski, H. N., and Robakis, N. K. (1990). The mRNA encoding the scrapie agent protein is present in a variety of non-neuronal cells. Acta Neuropathol. (Berl.) 80(1):1-6.
26. Buchholz, C. J., Bach, P., Nikles, D., and Kalinke, U. (2006). Prion protein-specific antibodies for therapeutic intervention of transmissible spongiform encephalopathies. Expert Opin. Biol. Ther. 6:293-300.
27. 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(7):1339-1347.
28. Bueler, H., Fischer, M., Lang, Y., Bluethmann, H., Lipp, H. P., DeArmond, S. J., Prusiner, S. B., Aguet, M., and Weissmann, C. (1992). Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356(6370):577-582.
29. Burger, D., and Hartsough, G. R. (1965). Encephalopathy of mink. II. Experimental and natural transmission. J. Infect. Dis. 115(4):393-399.
30. Buto, S., Tagliabue, E., Ardini, E., Magnifico, A., Ghirelli, C., Van Den Brule, F., Castronovo, V., Colnaghi, M. I., Sobel, M. E., and Menard, S. (1998). Formation of the 67-kDa laminin receptor by acylation of the precursor. J. Cell. Biochem. 69(3):244-251.
31. Cashman, N. R., Loertscher, R., Nalbantoglu, J., Shaw, I., Kascsak, R. J., Bolton, D. C., and Bendheim, P. E. (1990). Cellular isoform of the scrapie agent protein participates in lymphocyte activation. Cell 61(1):185-192.
32. Castilla, J., Saa, P., Hetz, C., and Soto, C. (2005). In vitro generation of infectious scrapie prions. Cell 121(2):195-206.
33. Castronovo, V., Taraboletti, G., and Sobel, M. E. (1991). Functional domains of the 67-kDa laminin receptor precursor. J. Biol. Chem. 266(30):20440-20446.
34. Caughey, B., Kocisko, D. A., Raymond, G. J., and Lansbury, P. T. Jr. (1995). Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2(12):807-817.
35. Caughey, B., and Race, R. E. (1992). Potent inhibition of scrapie-associated PrP accumulation by Congo red. J. Neurochem. 59(2):768-771.
36. Caughey, B., and Raymond, G. J. (1993). Sulfated polyanion inhibition of scrapie-associated PrP accumulation in cultured cells. J. Virol. 67(2):643-650.
37. Caughey, W. S., Raymond, L. D., Horiuchi, M., and Caughey, B. (1998). Inhibition of protease-resistant prion protein formation by porphyrins and phthalocyanines. Proc. Natl. Acad. Sci. U. S. A. 95(21):12117- 12122.
38. Chesebro, B., Trifilo, M., Race, R., Meade-White, K., Teng, C., LaCasse, R., Raymond, L., Favara, C., Baron, G., Priola, S., Caughey, B., Masliah, E., and Oldstone, M. (2005). Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308(5727):1435-1439.
39. Cohen, F. E., Pan, K. M., Huang, Z., Baldwin, M., Fletterick, R. J., and Prusiner, S. B. (1994). Structural clues to prion replication. Science 264(5158):530-531.
40. Cohen, F. E., and Prusiner, S. B. (1998). Pathologic conformations of prion proteins. Annu. Rev. Biochem. 67:793-819.
41. Collinge, J., and Palmer, M. S. (1994). Molecular genetics of human prion diseases. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 343(1306):371-378.
42. 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(6487):295-297.
43. Creutzfeldt, H. G. (1920). Über eine eigenartige Erkrankung des Zentralnervensystems. Vorläufige Mitteilung. Z. f. d. ges. Neurol. und Psych., 1-18.
44. Daude, N., Marella, M., and Chabry, J. (2003). Specific inhibition of pathological prion protein accumulation by small interfering RNAs. J. Cell Sci. 116(Pt. 13):2775-2779.
45. Della-Bianca, V., Rossi, F., Armato, U., Dal-Pra, I., Costantini, C., Perini, G., Politi, V., and Della Valle, G. (2001). Neurotrophin p75 receptor is involved in neuronal damage by prion peptide-(106-126). J. Biol. Chem. 276(42):38929-38933.
46. De Lorenzo, C., Tedesco, A., Terrazzano, G., Cozzolino, R., Laccetti, P., Piccoli, R., and D'Alessio, G. (2004). A human, compact, fully functional anti-ErbB2 antibody as a novel antitumour agent. Br. J. Cancer 91:1200-1204.
47. Demaimay, R., Adjou, K. T., Beringue, V., Demart, S., Lasmezas, C. I., Deslys, J. P., Seman, M., and Dormont, D. (1997). Late treatment with polyene antibiotics can prolong the survival time of scrapie-infected animals. J. Virol. 71(12):9685-9689.
48. Diarra-Mehrpour, M., Arrabal, S., Jalil, A., Pinson, X., Gaudin, C., Pietu, G., Pitaval, A., Ripoche, H., Eloit, M., Dormont, D., and Chouaib, S. (2004). Prion protein prevents human breast carcinoma cell line from tumor necrosis factor alpha-induced cell death. Cancer Res. 64(2):719-727.
49. Diringer, H., and Ehlers, B. (1991). Chemoprophylaxis of scrapie in mice. J. Gen. Virol. 72(Pt. 2):457-460.
50. Donne, D. G., Viles, J. H., Groth, D., Mehlhorn, I., James, T. L., Cohen, F. E., Prusiner, S. B., Wright, P. E., and Dyson, H. J. (1997). Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl. Acad. Sci. U. S. A. 94(25):13452- 13457.
51. Donofrio, G., Heppner, F. L., Polymenidou, M., Musahl, C., and Aguzzi, A. (2005). Paracrine inhibition of prion propagation by anti-PrP single-chain Fv miniantibodies. J. Virol. 79(13):8330-8338.
52. Duffy, P., Wolf, J., Collins, G., DeVoe, A. G., Streeten, B., and Cowen, D. (1974). Letter: Possible person-to-person transmission of Creutzfeldt-Jakob disease. N. Engl. J. Med. 290(12):692-693.
53. Edenhofer, F., Rieger, R., Famulok, M., Wendler, W., Weiss, S., and Winnacker, E. L. (1996). Prion protein PrPc interacts with molecular chaperones of the Hsp60 family. J. Virol. 70(7):4724-4728.
54. Enari, M., Flechsig, E., and Weissmann, C. (2001). Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc. Natl. Acad. Sci. U. S. A. 98(16):9295-9299.
55. Farquhar, C. F., Dickinson, A., and Bruce, M. (1999). Prophylactic potential of pentosan polysulphate in spongiform transmissible encephalopathies. Lancet 353:117.
56. Farquhar, C. F., and Dickinson, A. G. (1986). Prolongation of scrapie incubation period by an injection of dextran sulphate 500 within the month before or after infection. J. Gen. Virol. 67(Pt. 3):463-473.
57. Feng, X., Eide, F. F., Jiang, H., and Reder, A. T. (2004). Adeno-associated viral vector-mediated ApoE expression in Alzheimer's disease mice: low CNS immune response, long-term expression, and astrocyte specificity. Front. Biosci. 9:1540-1546.
58. Gabizon, R., Meiner, Z., Halimi, M., and Ben-Sasson, S. A. (1993). Heparin-like molecules bind differentially to prion-proteins and change their intracellular metabolic fate. J. Cell. Physiol. 157:319-325.
59. Gajdusek, D. C., and Zigas, V. (1957). Degenerative disease of the central nervous system in New Guinea; the endemic occurrence of Kuru in the native population. N. Engl. J. Med. 257(20):974-978.
60. Gauczynski, S., Nikles, D., El-Gogo, S., Papy-Garcia, D., Rey, C., Alban, S., Barritault, D., Lasmezas, C. I., and Weiss, S. (2006). The 37-kDa/67-kDa laminin receptor acts as a receptor for infectious prions and is inhibited by polysulfated glycanes. J. Infect. Dis. 194(5):702-709.
61. Gauczynski, S., Peyrin, J. M., Haik, S., Leucht, C., Hundt, C., Rieger, R., Krasemann, S., Deslys, J. P., Dormont, D., Lasmezas, C. I., and Weiss, S. (2001). The 37-kDa/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein. EMBO J. 20(21):5863-5875.
62. Gerstmann, J., Straussler, E., and Scheinker, I. (1936). Über eine eigenartige hereditär-familiäre Erkrankung des Zentralnervensystems. Zugleich ein Beitrag zur Frage des vorzeitigen lokalen Alterns. Zeitschrift für die gesamte Neurologie und Psychiatrie 154:736-762.
63. Gibbs, C. J. Jr., and Bolis, C. L. (1997). Normal isoform of amyloid protein (PrP) in brains of spawning salmon. Mol. Psychiatry 2(2):146-147.
64. Gilch, S., Winklhofer, K. F., Groschup, M. H., Nunziante, M., Lucassen, R., Spielhaupter, C., Muranyi, W., Riesner, D., Tatzelt, J., and Schatzl, H. M. (2001). Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease. EMBO J. 20(15):3957- 3966.
65. Goni, F., Knudsen, E., Schreiber, F., Scholtzova, H., Pankiewicz, J., Carp, R., Meeker, H. C., Rubenstein, R., Brown, D. R., Sy, M. S., Chabalgoity, J. A., Sigurdsson, E. M., and Wisniewski, T. (2005). Mucosal vaccination delays or prevents prion infection via an oral route. Neuroscience 133(2):413-421.
66. Graner, E., Mercadante, A. F., Zanata, S. M., Forlenza, O. V., Cabral, A. L., Veiga, S. S., Juliano, M. A., Roesler, R., Walz, R., Minetti, A., Izquierdo, I., Martins, V. R., and Brentani, R. R. (2000). Cellular prion protein binds laminin and mediates neuritogenesis. Brain Res. Mol. Brain Res. 76(1):85-92.
67. Griffith, J. S. (1967). Self-replication and scrapie. Nature 215(105):1043-1044.
68. Hara, H., Monsonego, A., Yuasa, K., Adachi, K., Xiao, X., Takeda, S., Takahashi, K., Weiner, H. L., and Tabira, T. (2004). Development of a safe oral Abeta vaccine using recombinant adeno-associated virus vector for Alzheimer's disease. J. Alzheimers Dis. 6:483-488.
69. Harris, D. A., Lele, P., and Snider, W. D. (1993). Localization of the mRNA for a chicken prion protein by in situ hybridization. Proc. Natl. Acad. Sci. U. S. A. 90(9):4309-4313.
70. Hijazi, N., Kariv-Inbal, Z., Gasset, M., and Gabizon, R. (2005). PrPSc incorporation to cells requires endogenous glycosaminoglycan expression. J. Biol. Chem. 280:17057-17061.
71. Hope, J., Morton, L. J., Farquhar, C. F., Multhaup, G., Beyreuther, K., and Kimberlin, R. H. (1986). The major polypeptide of scrapie-associated fibrils (SAF) has the same size, charge distribution and N-terminal protein sequence as predicted for the normal brain protein (PrP). EMBO J. 5(10):2591-2597.
72. 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(2):621-629.
73. Horonchik, L., Tzaban, S., Ben-Zaken, O., Yedidia, Y., Rouvinski, A., Papy-Garcia, D., Barritault, D., Vlodavsky, I., and Taraboulos, A. (2005). Heparan sulfate is a cellular receptor for purified infectious prions. J. Biol. Chem. 280:17062-17067.
74. Hundt, C., Peyrin, J. M., Haik, S., Gauczynski, S., Leucht, C., Rieger, R., Riley, M. L., Deslys, J. P., Dormont, D., Lasmezas, C. I., and Weiss, S. (2001). Identification of interaction domains of the prion protein with its 37-kDa/67-kDa laminin receptor. EMBO J. 20(21):5876-5886.
75. Ingrosso, L., Ladogana, A., and Pocchiari, M. (1995). Congo red prolongs the incubation period in scrapie-infected hamsters. J. Virol. 69(1):506-508.
76. Jackers, P., Clausse, N., Fernandez, M., Berti, A., Princen, F., Wewer, U., Sobel, M. E., and Castronovo, V. (1996). Seventeen copies of the human 37 kDa laminin receptor precursor/p40 ribosome-associated protein gene are processed pseudogenes arisen from retropositional events. Biochim. Biophys. Acta 1305(1-2):98-104.
77. Jakob, A. (1921). Über eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswerten anatomischen Befunden (spastische Pseudosklerose-Encephalomyelopathie mit dissemierten Degenerationsherden). Vorläufige Mitteilung. Z. Ges. Neurol. Psychiatr 64:147-228.
78. Jeffrey, M., and Wells, G. A. (1988). Spongiform encephalopathy in a nyala (Tragelaphus angasi). Vet. Pathol. 25(5):398-399.
79. Kinoshita, K., Kaneda, Y., Sato, M., Saeki, Y., Wataya-Kaneda, M., and Hoffmann, A. (1998). LBP-p40 binds DNA tightly through associations with histones H2A, H2B, and H4. Biochem. Biophys. Res. Commun. 253:277-282.
80. Kirkwood, J. K., Wells, G. A., Wilesmith, J. W., Cunningham, A. A., and Jackson, S. I. (1990). Spongiform encephalopathy in an arabian oryx (Oryx leucoryx) and a greater kudu (Tragelaphus strepsiceros). Vet. Rec. 127(17):418-420.
81. Kirschbaum, W. (1924). Zwei eigenartige Erkrankungen des Zentralnervensystems nach Art der spastischen Pseudosklerose (Jakob). Zeitschrift für die gesamte Neurologie und Psychiatrie 92:175-220.
82. Klamt, F., Dal-Pizzol, F., Conte da Frota, Ml Jr, Walz, R., Andrades, M. E., da Silva, E. G., Brentani, R. R., Izquierdo, I., and Fonseca Moreira, J. C. (2001). Imbalance of antioxidant defense in mice lacking cellular prion protein. Free Radic. Biol. Med. 30(10):1137-1144.
83. Koch, C. A., Anderson, D., Moran, M. F., Ellis, C., and Pawson, T. (1991). SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins. Science 252(5006):668-674.
84. Korth, C., May, B. C., Cohen, F. E., and Prusiner, S. B. (2001). Acridine and phenothiazine derivatives as pharmacotherapeutics for prion disease. Proc. Natl. Acad. Sci. U. S. A. 98(17):9836-9841.
85. Kretzschmar, H. A., Prusiner, S. B., Stowring, L. E., and DeArmond, S. J. (1986). Scrapie prion proteins are synthesized in neurons. Am. J. Pathol. 122(1):1-5.
86. Kretzschmar, H. A., Tings, T., Madlung, A., Giese, A., and Herms, J. (2000). Function of PrP(C) as a copper-binding protein at the synapse. Arch. Virol. 16(Suppl.):239-249.
87. Kurschner, C., and Morgan, J. I. (1995). The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system. Brain Res. Mol. Brain Res. 30(1):165-168.
88. Landowski, T. H., Dratz, E. A., and Starkey, J. R. (1995). Studies of the structure of the metastasis-associated 67 kDa laminin binding protein: Fatty acid acylation and evidence supporting dimerization of the 32 kDa gene product to form the mature protein. Biochemistry 34(35):11276-11287.
89. Lansbury, P. T. Jr., and Caughey, B. (1995). The chemistry of scrapie infection: Implications of the "ice 9" metaphor. Chem. Biol. 2(1):1-5.
90. Legname, G., Baskakov, I. V., Nguyen, H. O., Riesner, D., Cohen, F. E., DeArmond, S. J., and Prusiner, S. B. (2004). Synthetic mammalian prions. Science 305(5684):673-676.
91. Leliveld, S. R., Dame, R. T., Wuite, G. J., Stitz, L., and Korth, C. (2006). The expanded octarepeat domain selectively binds prions and disrupts homomeric prion protein interactions. J. Biol. Chem. 281:3268- 3275.
92. Leucht, C., Simoneau, S., Rey, C., Vana, K., Rieger, R., Lasmezas, C. I., and Weiss, S. (2003). The 37 kDa/67 kDa laminin receptor is required for PrP(Sc) propagation in scrapie-infected neuronal cells. EMBO Rep. 4(3):290-295.
93. Liang, J., Pan, Y. L., Ning, X. X., Sun, L. J., Lan, M., Hong, L., Du, J. P., Liu, N., Liu, C. J., Qiao, T. D., and Fan, D. M. (2006). Overexpression of PrP and its antiapoptosis function in gastric cancer. Tumor Biol. 27:84-91.
94. Liao, Y. C., Lebo, R. V., Clawson, G. A., and Smuckler, E. A. (1986). Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications. Science 233(4761):364-367.
95. Liu, T., Li, R., Wong, B. S., Liu, D., Pan, T., Petersen, R. B., Gambetti, P., and Sy, M. S. (2001). Normal cellular prion protein is preferentially expressed on subpopulations of murine hemopoietic cells. J. Immunol. 166(6):3733-3742.
96. Ludwig, G. V., Kondig, J. P., and Smith, J. F. (1996). A putative receptor for Venezuelan equine encephalitis virus from mosquito cells. J. Virol. 70(8):5592-5599.
97. Lugaresi, E., Medori, R., Montagna, P., Baruzzi, A., Cortelli, P., Lugaresi, A., Tinuper, P., Zucconi, M., and Gambetti, P. (1986). Fatal familial insomnia and dysautonomia with selective degeneration of thalamic nuclei. N. Engl. J. Med. 315(16):997-1003.
98. Makrides, S., Chitpatima, S. T., Bandyopadhyay, R., and Brawerman, G. (1988). Nucleotide sequence for a major messenger RNA for a 40 kilodalton polypeptide that is under translational control in mouse tumor cells. Nucleic Acids Res. 16(5):2349.
99. Marella, M., Lehmann, S., Grassi, J., and Chabry, J. (2002). Filipin prevents pathological prion protein accumulation by reducing endocytosis and inducing cellular PrP release. J. Biol. Chem. 277(28):25457-25464.
100. Martins, V. R., Graner, E., Garcia-Abreu, J., de Souza, S. J., Mercadante, A. F., Veiga, S. S., Zanata, S. M., Neto, V. M., and Brentani, R. R. (1997). Complementary hydropathy identifies a cellular prion protein receptor. Nat. Med. 3(12):1376-1382.
101. Mastrianni, J. A., Nixon, R., Layzer, R., Telling, G. C., Han, D., DeArmond, S. J., and Prusiner, S. B. (1999). Prion protein conformation in a patient with sporadic fatal insomnia. N. Engl. J. Med. 340(21):1630-1638.
102. Mattei, V., Garofalo, T., Misasi, R., Circella, A., Manganelli, V., Lucania, G., Pavan, A., and Sorice, M. (2004). Prion protein is a component of the multimolecular signaling complex involved in T cell activation. FEBS Lett. 560:14-18.
103. Mayer, R. J., Landon, M., Laszlo, L., Lennox, G., and Lowe, J. (1992). Protein processing in lysosomes: The new therapeutic target in neurodegenerative disease. Lancet 340(8812):156-159.
104. Mazzoni, I. E., Ledebur, H. C. Jr., Paramithiotis, E., and Cashman, N. (2005). Lymphoid signal transduction mechanisms linked to cellular prion protein. Biochem. Cell Biol. 83(5):644-653.
105. McGowan, J. P. (1922). Scrapie in sheep. Scott. J. Agric. 5:365-375.
106. McKinley, M. P., Meyer, R. K., Kenaga, L., Rahbar, F., Cotter, R., Serban, A., and Prusiner, S. B. (1991). Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65(3):1340-1351.
107. Meggio, F., Negro, A., Sarno, S., Ruzzene, M., Bertoli, A., Sorgato, M. C., and Pinna, L. A. (2000). Bovine prion protein as a modulator of protein kinase CK2. Biochem. J. 352(Pt. 1):191-196.
108. Morel, E., Andrieu, T., Casagrande, F., Gauczynski, S., Weiss, S., Grassi, J., Rousset, M., Dormont, D., and Chambaz, J. (2005). Bovine Prion Is Endocytosed by Human Enterocytes via the 37 kDa/67 kDa Laminin Receptor. Am. J. Pathol. 167(4):1033-1042.
109. Morel, E., Fouquet, S., Chateau, D., Yvernault, L., Frobert, Y., Pincon-Raymond, M., Chambaz, J., Pillot, T., and Rousset, M. (2004). The cellular prion protein PrPc is expressed in human enterocytes in cell-cell junctional domains. J. Biol. Chem. 279(2):1499-1505.
110. Moudjou, M., Frobert, Y., Grassi, J., and La Bonnardiere, C. (2001). Cellular prion protein status in sheep: tissue-specific biochemical signatures. J. Gen. Virol. 82(Pt. 8):2017-2024.
111. Mouillet-Richard, S., Ermonval, M., Chebassier, C., Laplanche, J. L., Lehmann, S., Launay, J. M., and Kellermann, O. (2000). Signal transduction through prion protein. Science 289(5486):1925-1928.
112. Mouillet-Richard, S., Pietri, M., Schneider, B., Vidal, C., Mutel, V., Launay, J. M., and Kellermann, O. (2005). Modulation of serotonergic receptor signaling and cross-talk by prion protein. J. Biol. Chem. 280:4592-4601.
113. Nieznanski, K., Nieznanska, H., Skowronek, K. J., Osiecka, K. M., and Stepkowski, D. (2005). Direct interaction between prion protein and tubulin. Biochem. Biophys. Res. Commun. 334:403-411.
114. Nikles, D., Bach, P., Boller, K., Merten, C. A., Montrasio, F., Heppner, F. L., Aguzzi, A., Cichutek, K., Kalinke, U., and Buchholz, C. J. (2005). Circumventing tolerance to the prion protein (PrP): Vaccination with PrP-displaying retrovirus particles induces humoral immune responses against the native form of cellular PrP. J. Virol. 79(7):4033-4042.
115. Oishi, T., Hagiwara, K., Kinumi, T., Yamakawa, Y., Nishijima, M., Nakamura, K., and Arimoto, H. (2003). Effects of beta-sheet breaker peptide polymers on scrapie-infected mouse neuroblastoma cells and their affinities to prion protein fragment PrP(81-145). Org. Biomol. Chem. 1:2626-2629.
116. Otto, M., Cepek, L., Ratzka, P., Doehlinger, S., Boekhoff, I., Wiltfang, J., Irle, E., Pergande, G., Ellers-Lenz, B., Windl, O., Kretzschmar, H. A., Poser, S., and Prange, H. (2004). Efficacy of flupirtine on cognitive function in patients with CJD: A double-blind study. Neurology 62(5):714-718.
117. Paitel, E., Alves da Costa, C., Vilette, D., Grassi, J., and Checler, F. (2002). Overexpression of PrPc triggers caspase 3 activation: Potentiation by proteasome inhibitors and blockade by anti-PrP antibodies. J. Neurochem. 83(5):1208-1214.
118. Paitel, E., Fahraeus, R., and Checler, F. (2003). Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53-dependent caspase 3-like activation. J. Biol. Chem. 278(12):10061-10066.
119. Paitel, E., Sunyach, C., Alves da Costa, C., Bourdon, J. C., Vincent, B., and Checler, F. (2004). Primary cultured neurons devoid of cellular prion display lower responsiveness to staurosporine through the control of p53 at both transcriptional and post-transcriptional levels. J. Biol. Chem. 279(1):612-618.
120. Paltrinieri, S., Comazzi, S., Spagnolo, V., Rondena, M., Ponti, W., and Ceciliani, F. (2004). Bovine Doppel (Dpl) and prion protein (PrP) expression on lymphoid tissue and circulating leukocytes. J. Histochem. Cytochem. 52(12):1639-1645.
121. Pan, K. M., Baldwin, M., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R. J., Cohen, F. E., et al. (1993). Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. U. S. A. 90(23):10962-10966.
122. Pan, T., Wong, B. S., Liu, T., Li, R., Petersen, R. B., and Sy, M. S. (2002). Cell-surface prion protein interacts with glycosaminoglycans. Biochem. J. 368(Pt. 1):81-90.
123. Pankiewicz, J., Prelli, F., Sy, M. S., Kascsak, R. J., Kascsak, R. B., Spinner, D. S., Carp, R. I., Meeker, H. C., Sadowski, M., and Wisniewski, T. (2006). Clearance and prevention of prion infection in cell culture by anti-PrP antibodies. Eur. J. Neurosci. 23(10):2635-2647.
124. Parchi, P., Capellari, S., Chin, S., Schwarz, H. B., Schecter, N. P., Butts, J. D., Hudkins, P., Burns, D. K., Powers, J. M., and Gambetti, P. (1999). A subtype of sporadic prion disease mimicking fatal familial insomnia. Neurology 52:1757-1763.
125. Pocchiari, M., Schmittinger, S., and Masullo, C. (1987). Amphotericin B delays the incubation period of scrapie in intracerebrally inoculated hamsters. J. Gen. Virol. 68(Pt. 1):219-223.
126. Poli, G., Martino, P. A., Villa, S., Carcassola, G., Giannino, M. L., Dall'Ara, P., Pollera, C., Iussich, S., Tranquillo, V. M., Bareggi, S., Mantegazza, P., and Ponti, W. (2004). Evaluation of anti-prion activity of congo red and its derivatives in experimentally infected hamsters. Arzneimittelforschung 54:406-415.
127. Priola, S. A., Raines, A., and Caughey, W. S. (2000). Porphyrin and phthalocyanine antiscrapie compounds. Science 287(5457):1503-1506.
128. Proske, D., Gilch, S., Wopfner, F., Schätzl, H. M., Winnacker, E. L., and Famulok, M. (2002). Prion-protein-specific aptamer reduces PrPSc formation. Chembiochem 3:717-725.
129. Prusiner, S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science 216(4542):136-144.
130. Prusiner, S B. (1991). Molecular biology of prion diseases. Science 252(5012):1515-1522.
131. Prusiner, S. B. (1994). Molecular biology and genetics of prion diseases. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 343(1306):447-463.
132. Prusiner, S. B., Groth, D., Serban, A., Stahl, N., and Gabizon, R. (1993). Attempts to restore scrapie prion infectivity after exposure to protein denaturants. Proc. Natl. Acad. Sci. U. S. A. 90(7):2793-2797.
133. Ralph, G. S., Radcliffe, P. A., Day, D. M., Carthy, J. M., Leroux, M. A., Lee, D. C., Wong, L. F., Bilsland, L. G., Greensmith, L., Kingsman, S. M., Mitrophanous, K. A., Mazarakis, N. D., and Azzouz, M. (2005). Silencing mutant SOD1 using RNAi protects against neurodegeneration and extends survival in an ALS model. Nat. Med. 11:429-433.
134. Rambold, A. S., Miesbauer, M., Rapaport, D., Bartke, T., Baier, M., Winklhofer, K. F., and Tatzelt, J. (2006). Association of Bcl-2 with misfolded prion protein is linked to the toxic potential of cytosolic PrP. Mol. Biol. Cell
135. Rao, N. C., Barsky, S. H., Terranova, V. P., and Liotta, L. A. (1983). Isolation of a tumor cell laminin receptor. Biochem. Biophys. Res. Commun. 111(3):804-808.
136. Raoul, C., Abbas-Terki, T., Bensadoun, J. C., Guillot, S., Haase, G., Szulc, J., Henderson, C. E., and Aebischer, P. (2005). Lentiviral-mediated silencing of SOD1 through RNA interference retards disease onset and progression in a mouse model of ALS. Nat. Med. 11:423-428.
137. Reilly, C. E. (2000). Beta-sheet breaker peptides reverse conformation of pathogenic prion proteins. J. Neurol. 247:319-320.
138. Rieger, R., Edenhofer, F., Lasmezas, C. I., and Weiss, S. (1997). The human 37-kDa laminin receptor precursor interacts with the prion protein in eukaryotic cells. Nat. Med. 3(12):1383-1388.
139. 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(6587):180-182.
140. Robakis, N. K., Devine-Gage, E. A., Jenkins, E. C., Kascsak, R. J., Brown, W. T., Krawczun, M. S., and Silverman, W. P. (1986). Localization of a human gene homologous to the PrP gene on the p arm of chromosome 20 and detection of PrP-related antigens in normal human brain. Biochem. Biophys. Res. Commun. 140(2):758-765.
141. Romanov, V., Sobel, M. E., pinto da Silva, P., Menard, S., and Castronovo, V. (1994). Cell localization and redistribution of the 67 kD laminin receptor and alpha 6 beta 1 integrin subunits in response to laminin stimulation: an immunogold electronmicroscopy study. Cell Adhes. Commun. 2(3):201-209.
142. Sakudo, A., Lee, D. C., Saeki, K., Matsumoto, Y., Itohara, S., and Onodera, T. (2003). Tumor necrosis factor attenuates prion protein-deficient neuronal cell death by increases in anti-apoptotic Bcl-2 family proteins. Biochem. Biophys. Res. Commun. 310:725-729.
143. Sanftner, L. M., Sommer, J. M., Suzuki, B. M., Smith, P. H., Vijay, S., Vargas, J. A., Forsayeth, J. R., Cunningham, J., Bankiewicz, K. S., Kao, H., Bernal, J., Pierce, G. F., and Johnson, K. W. (2005). AAV2-mediated gene delivery to monkey putamen: evaluation of an infusion device and delivery parameters. Exp. Neurol. 194:476-483.
144. Sato, M., Kinoshita, K., Kaneda, Y., Saeki, Y., Iwamatsu, A., and Tanaka, K. (1996). Analysis of nuclear localization of laminin binding protein precursor p40 (LBP/p40). Biochem. Biophys. Res. Commun. 229(3):896-901.
145. Schätzl, H. M., Da Costa, M., Taylor, L., Cohen, F. E., and Prusiner, S. B. (1995). Prion protein gene variation among primates. J. Mol. Biol. 245(4):362-374.
146. Schmitt-Ulms, G., Legname, G., Baldwin, M. A., Ball, H. L., Bradon, N., Bosque, P. J., Crossin, K. L., Edelman, G. M., DeArmond, S. J., Cohen, F. E., and Prusiner, S. B. (2001). Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein. J. Mol. Biol. 314(5):1209-1225.
147. Sekiya, S., Noda, K., Nishikawa, F., Yokoyama, T., Kumar, P. K., and Nishikawa, S. (2006). Characterization and Application of a Novel RNA Aptamer against the Mouse Prion Protein. J. Biochem. (Tokyo) 139:383-390.
148. 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.
149. 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.
150. Sigurdsson, B. (1954). Rida-a chronic encephalitis of sheep-with general remarks on infections which develop slowly and some of their special characteristics. Br. Vet. J. 110:341-354.
151. Simoneau, S., Haik, S., Leucht, C., Dormont, D., Deslys, J. P., Weiss, S., and Lasmezas, C. (2003). Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP. Biol. Chem. 384(2):243-246.
152. Solforosi, L., Criado, J. R., McGavern, D. B., Wirz, S., Sanchez-Alavez, M., Sugama, S., DeGiorgio, L. A., Volpe, B. T., Wiseman, E., Abalos, G., Masliah, E., Gilden, D., Oldstone, M. B., Conti, B., and Williamson, R. A. (2004). Cross-linking cellular prion protein triggers neuronal apoptosis in vivo. Science 303(5663):1514-1516.
153. Sparkes, R. S., Simon, M., Cohn, V. H., Fournier, R. E., Lem, J., Klisak, I., Heinzmann, C., Blatt, C., Lucero, M., Mohandas, T., and et al. (1986). Assignment of the human and mouse prion protein genes to homologous chromosomes. Proc. Natl. Acad. Sci. U. S. A. 83(19):7358-7362.
154. Spielhaupter, C., and Schätzl, H. M. (2001). PrPC directly interacts with proteins involved in signaling pathways. J. Biol. Chem. 276(48):44604-44612.
155. Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L., and Prusiner, S. B. (1993). Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32(8):1991-2002.
156. Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51(2):229-240.
157. Stahl, N., and Prusiner, S. B. (1991). Prions and prion proteins. FASEB J. 5(13):2799-2807.
158. Supattapone, S., Wille, H., Uyechi, L., Safar, J., Tremblay, P., Szoka, F. C., Cohen, F. E., Prusiner, S. B., and Scott, M. R. (2001). Branched polyamines cure prion-infected neuroblastoma cells. J. Virol. 75(7):3453-3461.
159. Tagliavini, F., McArthur, R. A., Canciani, B., Giaccone, G., Porro, M., Bugiani, M., Lievens, P. M., Bugiani, O., Peri, E., Dall'Ara, P., Rocchi, M., Poli, G., Forloni, G., Bandiera, T., Varasi, M., Suarato, A., Cassutti, P., Cervini, M. A., Lansen, J., Salmona, M., and Post, C. (1997). Effectiveness of anthracycline against experimental prion disease in Syrian hamsters. Science 276(5315):1119-1122.
160. Tanji, K., Saeki, K., Matsumoto, Y., Takeda, M., Hirasawa, K., Doi, K., and Onodera, T. (1995). Analysis of PrPc mRNA by in situ hybridization in brain, placenta, uterus and testis of rats. Intervirology 38(6):309-315.
161. Thormar, H. (1971). Slow infections of the central nervous system II. Z. Neurol. 199(3):151-166.
162. Tio, P. H., Jong, W. W., and Cardosa, M. J. (2005). Two dimensional VOPBA reveals laminin receptor (LAMR1) interaction with dengue virus serotypes 1, 2 and 3. Virol. J. 2(1):25.
163. Tobler, I., Gaus, S. E., Deboer, T., Achermann, P., Fischer, M., Rulicke, T., Moser, M., Oesch, B., McBride, P. A., and Manson, J. C. (1996). Altered circadian activity rhythms and sleep in mice devoid of prion protein. Nature 380(6575):639-642.
164. Vana, K., and Weiss, S. (2006). A trans-dominant negative 37 kDa/67 kDa laminin receptor mutant impairs PrPSc propagation in scrapie-infected neuronal cells. J. Mol. Biol. 358(1):57-66.
165. Vassallo, N., and Herms, J. (2003). Cellular prion protein function in copper homeostasis and redox signalling at the synapse. J. Neurochem. 86(3):538-344.
166. Wang, K. S., Kuhn, R. J., Strauss, E. G., Ou, S., and Strauss, J. H. (1992). High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J. Virol. 66(8):4992-5001.
167. Weiss, S., Proske, D., Neumann, M., Groschup, M. H., Kretzschmar, H. A., Famulok, M., and Winnacker, E. L. (1997). RNA aptamers specifically interact with the prion protein PrP. J. Virol. 71:8790-8797.
168. Weissmann, C., and Flechsig, E. (2003). PrP knock-out and PrP transgenic mice in prion research. Br. Med. Bull. 66:43-60.
169. Wells, G. A., Scott, A. C., Johnson, C. T., Gunning, R. F., Hancock, R. D., Jeffrey, M., Dawson, M., and Bradley, R. (1987). A novel progressive spongiform encephalopathy in cattle. Vet. Rec. 121(18):419-420.
170. White, A. R., Enever, P., Tayebi, M., Mushens, R., Linehan, J., Brandner, S., Anstee, D., Collinge, J., and Hawke, S. (2003). Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422(6927):80-83.
171. Whittal, R. M., Ball, H. L., Cohen, F. E., Burlingame, A. L., Prusiner, S. B., and Baldwin, M. A. (2000). Copper binding to octarepeat peptides of the prion proteinmonitored bymass spectrometry. Protein Sci. 9:332-343.
172. Will, R. G., Ironside, J. W., Zeidler, M., Cousens, S. N., Estibeiro, K., Alperovitch, A., Poser, S., Pocchiari, M., Hofman, A., and Smith, P. G. (1996). A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347(9006):921-925.
173. Williams, E. S., and Young, S. (1980). Chronic wasting disease of captive mule deer: a spongiform encephalopathy. J. Wildl. Dis. 16(1):89-98.
174. Windl, O., Dempster, M., Estibeiro, P., and Lathe, R. (1995). A candidate marsupial PrP gene reveals two domains conserved in mammalian PrP proteins. Gene 159(2):181-186.
175. Winklhofer, K. F., and Tatzelt, J. (2000). Cationic lipopolyamines induce degradation of PrPSc in scrapie-infected mouse neuroblastoma cells. Biol. Chem. 381(5-6):463-469.
176. Wopfner, F., Weidenhofer, G., Schneider, R., von Brunn, A., Gilch, S., Schwarz, T. F., Werner, T., and Schätzl, H. M. (1999). Analysis of 27 mammalian and 9 avian PrPs reveals high conservation of flexible regions of the prion protein. J. Mol. Biol. 289(5):1163-1178.
177. Wyatt, J. M. (1990). Spongiform encephalopathy in a cat. Vet. Rec. 126(20):513.
178. Yehiely, F., Bamborough, P., Da Costa, M., Perry, B. J., Thinakaran, G., Cohen, F. E., Carlson, G. A., and Prusiner, S. B. (1997). Identification of candidate proteins binding to prion protein. Neurobiol. Dis. 3(4):339-355.
179. Zanata, S. M., Lopes, M. H., Mercadante, A. F., Hajj, G. N., Chiarini, L. B., Nomizo, R., Freitas, A. R., Cabral, A. L., Lee, K. S., Juliano, M. A., de Oliveira, E., Jachieri, S. G., Burlingame, A., Huang, L., Linden, R., Brentani, R. R., and Martins, V. R. (2002). Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection. EMBO J. 21(13):3307-3316.
180. Zhang, J., Wu, X., Qin, C., Qi, J., Ma, S., Zhang, H., Kong, Q., Chen, D., Ba, D., and He, W. (2003). A novel recombinant adeno-associated virus vaccine reduces behavioral impairment and beta-amyloid plaques in a mouse model of Alzheimer's disease. Neurobiol. Dis. 14:365-379.
181. Zhou, J., and Zhong, Y. (2004). Breast cancer immunotherapy. Cell. Mol. Immunol. 1:xs247-255.