메뉴 건너뛰기




Volumn 51, Issue 1, 2007, Pages 1-13

Prion protein gene-deficient cell lines: Powerful tools for prion biology

Author keywords

Apoptosis; BSE; Cell line; Oxidative stress; Prion disease; Prion protein

Indexed keywords

PRION PROTEIN; RETROVIRUS VECTOR; SUPEROXIDE DISMUTASE; VIRUS LARGE T ANTIGEN;

EID: 33846549467     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2007.tb03877.x     Document Type: Short Survey
Times cited : (15)

References (84)
  • 1
    • 23744466841 scopus 로고    scopus 로고
    • Poliovirus type 1 infection of murine PRNP-knockout neuronal cells
    • Baj, A., Bettaccini, A., Nishimura, T., Onodera, T., and Toniolo, A. 2005. Poliovirus type 1 infection of murine PRNP-knockout neuronal cells. J. Neurovirol. 11: 237-246.
    • (2005) J. Neurovirol , vol.11 , pp. 237-246
    • Baj, A.1    Bettaccini, A.2    Nishimura, T.3    Onodera, T.4    Toniolo, A.5
  • 2
    • 0035903461 scopus 로고    scopus 로고
    • Changing a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers
    • Barron, R.M., Thomson, V., Jamieson, E., Melton, D.W., Ironside, J., Will, R., and Manson, J.C. 2001. Changing a single amino acid in the N-terminus of murine PrP alters TSE incubation time across three species barriers. EMBO J. 20: 5070-5078.
    • (2001) EMBO J , vol.20 , pp. 5070-5078
    • Barron, R.M.1    Thomson, V.2    Jamieson, E.3    Melton, D.W.4    Ironside, J.5    Will, R.6    Manson, J.C.7
  • 4
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cell sublines highly susceptible to prion infection
    • Bosque, P.J., and Prusiner, S.B. 2000. Cultured cell sublines highly susceptible to prion infection. J. Virol. 74: 4377-4386.
    • (2000) J. Virol , vol.74 , pp. 4377-4386
    • Bosque, P.J.1    Prusiner, S.B.2
  • 11
    • 0014930651 scopus 로고
    • Evidence for the multiplication of scrapie agent in cell culture
    • Clarke, M.C., and Haig, D.A. 1970. Evidence for the multiplication of scrapie agent in cell culture. Nature 225: 100-101.
    • (1970) Nature , vol.225 , pp. 100-101
    • Clarke, M.C.1    Haig, D.A.2
  • 12
    • 33746770348 scopus 로고    scopus 로고
    • The truncated 23-230 form of the prion protein localizes to the nuclei of inducible cell lines independently of its nuclear localization signals and is not cytotoxic
    • Crozet, C., Vezilier, J., Delfieu, V., Nishimura, T., Onodera, T., Casanova, D., Lehmann, S., and Beranger, F. 2006. The truncated 23-230 form of the prion protein localizes to the nuclei of inducible cell lines independently of its nuclear localization signals and is not cytotoxic. Mol. Cell. Neurosci. 32: 315-323.
    • (2006) Mol. Cell. Neurosci , vol.32 , pp. 315-323
    • Crozet, C.1    Vezilier, J.2    Delfieu, V.3    Nishimura, T.4    Onodera, T.5    Casanova, D.6    Lehmann, S.7    Beranger, F.8
  • 14
    • 0029863648 scopus 로고    scopus 로고
    • Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie
    • Fischer, M., Rulicke, T., Raeber, A., Sailer, A., Moser, M., Oesch, B., Brandner, S., Aguzzi, A., and Weissmann, C. 1996. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15: 1255-1264.
    • (1996) EMBO J , vol.15 , pp. 1255-1264
    • Fischer, M.1    Rulicke, T.2    Raeber, A.3    Sailer, A.4    Moser, M.5    Oesch, B.6    Brandner, S.7    Aguzzi, A.8    Weissmann, C.9
  • 18
    • 33745918650 scopus 로고    scopus 로고
    • Prion protein reduces both oxidative and non-oxidative copper toxicity
    • Haigh, C.L., and Brown, D.R. 2006. Prion protein reduces both oxidative and non-oxidative copper toxicity. J. Neurochem. 98: 677-689.
    • (2006) J. Neurochem , vol.98 , pp. 677-689
    • Haigh, C.L.1    Brown, D.R.2
  • 19
    • 0035033675 scopus 로고    scopus 로고
    • Prion protein affects Ca2+-activated K+ currents in cerebellar purkinje cells
    • Herms, J.W., Tings, T., Dunker, S., and Kretzschmar, H.A. 2001. Prion protein affects Ca2+-activated K+ currents in cerebellar purkinje cells. Neurobiol. Dis. 8: 324-330.
    • (2001) Neurobiol. Dis , vol.8 , pp. 324-330
    • Herms, J.W.1    Tings, T.2    Dunker, S.3    Kretzschmar, H.A.4
  • 21
    • 0042381229 scopus 로고    scopus 로고
    • A novel method of generating neuronal cell lines from gene-knockout mice to study prion protein membrane orientation
    • Holme, A., Daniels, M., Sassoon, J., and Brown, D.R. 2003. A novel method of generating neuronal cell lines from gene-knockout mice to study prion protein membrane orientation. Eur. J. Neurosci. 18: 571-579.
    • (2003) Eur. J. Neurosci , vol.18 , pp. 571-579
    • Holme, A.1    Daniels, M.2    Sassoon, J.3    Brown, D.R.4
  • 22
    • 0031594587 scopus 로고    scopus 로고
    • Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation
    • Holscher, C., Delius, H., and Burkle, A. 1998. Overexpression of nonconvertible PrPc delta114-121 in scrapie-infected mouse neuroblastoma cells leads to trans-dominant inhibition of wild-type PrP(Sc) accumulation. J. Virol. 72: 1153-1159.
    • (1998) J. Virol , vol.72 , pp. 1153-1159
    • Holscher, C.1    Delius, H.2    Burkle, A.3
  • 24
    • 16444374116 scopus 로고    scopus 로고
    • A neuronal cell line that does not express either prion or doppel proteins
    • Kim, B.H., Kim, J.I., Choi, E.K., Carp, R.I., and Kim, Y.S. 2005. A neuronal cell line that does not express either prion or doppel proteins. Neuroreport 16: 425-429.
    • (2005) Neuroreport , vol.16 , pp. 425-429
    • Kim, B.H.1    Kim, J.I.2    Choi, E.K.3    Carp, R.I.4    Kim, Y.S.5
  • 25
    • 1942485480 scopus 로고    scopus 로고
    • The cellular prion protein (PrPC) prevents apoptotic neuronal cell death and mitochondrial dysfunction induced by serum deprivation
    • Kim, B.H., Lee, H.G., Choi, J.K., Kim, J.I., Choi, E.K., Carp, R.I., and Kim, Y.S. 2004. The cellular prion protein (PrPC) prevents apoptotic neuronal cell death and mitochondrial dysfunction induced by serum deprivation. Brain Res. Mol. Brain Res. 124: 40-50.
    • (2004) Brain Res. Mol. Brain Res , vol.124 , pp. 40-50
    • Kim, B.H.1    Lee, H.G.2    Choi, J.K.3    Kim, J.I.4    Choi, E.K.5    Carp, R.I.6    Kim, Y.S.7
  • 26
    • 0141593548 scopus 로고    scopus 로고
    • A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions
    • Klohn, P.C., Stoltze, L., Flechsig, E., Enari, M., and Weissmann, C. 2003. A quantitative, highly sensitive cell-based infectivity assay for mouse scrapie prions. Proc. Natl. Acad. Sci. U.S.A. 100: 11666-11671.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 11666-11671
    • Klohn, P.C.1    Stoltze, L.2    Flechsig, E.3    Enari, M.4    Weissmann, C.5
  • 29
    • 0028967732 scopus 로고
    • Proteinase-resistant protein in human neuroblastoma cells infected with brain material from Creutzfeldt-Jakob patient
    • Ladogana, A., Liu, Q., Xi, Y.G., and Pocchiari, M. 1995. Proteinase-resistant protein in human neuroblastoma cells infected with brain material from Creutzfeldt-Jakob patient. Lancet 345: 594-595.
    • (1995) Lancet , vol.345 , pp. 594-595
    • Ladogana, A.1    Liu, Q.2    Xi, Y.G.3    Pocchiari, M.4
  • 30
    • 0035929635 scopus 로고    scopus 로고
    • N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro
    • Lawson, V.A., Priola, S.A., Wehrly, K., and Chesebro, B. 2001. N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro. J. Biol. Chem. 276: 35265-35271.
    • (2001) J. Biol. Chem , vol.276 , pp. 35265-35271
    • Lawson, V.A.1    Priola, S.A.2    Wehrly, K.3    Chesebro, B.4
  • 31
    • 1842791529 scopus 로고    scopus 로고
    • Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro
    • Lawson, V.A., Priola, S.A., Meade-White, K., Lawson, M., and Chesebro, B. 2004. Flexible N-terminal region of prion protein influences conformation of protease-resistant prion protein isoforms associated with cross-species scrapie infection in vivo and in vitro. J. Biol. Chem. 279: 13689-13695.
    • (2004) J. Biol. Chem , vol.279 , pp. 13689-13695
    • Lawson, V.A.1    Priola, S.A.2    Meade-White, K.3    Lawson, M.4    Chesebro, B.5
  • 32
  • 33
    • 30544444183 scopus 로고    scopus 로고
    • Interaction of cellular prion and stressinducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways
    • Lopes, M.H., Hajj, G.N., Muras, A.G., Mancini, G.L., Castro, R.M., Ribeiro, K.C., Brentani, R.R., Linden, R., and Martins, V.R. 2005. Interaction of cellular prion and stressinducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways. J. Neurosci. 25: 11330-11339.
    • (2005) J. Neurosci , vol.25 , pp. 11330-11339
    • Lopes, M.H.1    Hajj, G.N.2    Muras, A.G.3    Mancini, G.L.4    Castro, R.M.5    Ribeiro, K.C.6    Brentani, R.R.7    Linden, R.8    Martins, V.R.9
  • 34
    • 1642410070 scopus 로고    scopus 로고
    • Alpha- and beta-cleavages of the amino-terminus of the cellular prion protein
    • Mange A., Beranger, F., Peoc'h, K., Onodera, T., Frobert, Y., and Lehmann, S. 2004. Alpha- and beta-cleavages of the amino-terminus of the cellular prion protein. Biol. Cell 96: 125-132.
    • (2004) Biol. Cell , vol.96 , pp. 125-132
    • Mange, A.1    Beranger, F.2    Peoc'h, K.3    Onodera, T.4    Frobert, Y.5    Lehmann, S.6
  • 36
    • 0346752203 scopus 로고    scopus 로고
    • Transfection of prion protein gene suppresses coxsackievirus B3 replication in prion protein gene-deficient cells
    • Nakamura, Y., Sakudo, A., Saeki, K., Kaneko, T., Matsumoto, Y., Toniolo, A., Itohara, S., and Onodera, T. 2003. Transfection of prion protein gene suppresses coxsackievirus B3 replication in prion protein gene-deficient cells. J. Gen. Virol. 84: 3495-3502.
    • (2003) J. Gen. Virol , vol.84 , pp. 3495-3502
    • Nakamura, Y.1    Sakudo, A.2    Saeki, K.3    Kaneko, T.4    Matsumoto, Y.5    Toniolo, A.6    Itohara, S.7    Onodera, T.8
  • 37
    • 0033988236 scopus 로고    scopus 로고
    • Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein
    • Nishida, N., Harris, D.A., Vilette, D., Laude, H., Frobert, Y., Grassi, J., Casanova, D., Milhavet, O., and Lehmann, S. 2000. Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cell lines overexpressing wild-type mouse prion protein. J. Virol. 74: 320-325.
    • (2000) J. Virol , vol.74 , pp. 320-325
    • Nishida, N.1    Harris, D.A.2    Vilette, D.3    Laude, H.4    Frobert, Y.5    Grassi, J.6    Casanova, D.7    Milhavet, O.8    Lehmann, S.9
  • 38
    • 33747865458 scopus 로고    scopus 로고
    • Bovine spongiform encephalopathy in Japan: History and recent studies on oxidative stress in prion diseases
    • Onodera, T., Sakudo, A., Wu, G., and Saeki, K. 2006. Bovine spongiform encephalopathy in Japan: history and recent studies on oxidative stress in prion diseases. Microbiol. Immunol. 50: 565-578.
    • (2006) Microbiol. Immunol , vol.50 , pp. 565-578
    • Onodera, T.1    Sakudo, A.2    Wu, G.3    Saeki, K.4
  • 40
    • 25144472636 scopus 로고    scopus 로고
    • Tissue safety in view of CJD and variant CJD
    • Pauli, G. 2005. Tissue safety in view of CJD and variant CJD. Cell Tissue Bank 6: 191-200.
    • (2005) Cell Tissue Bank , vol.6 , pp. 191-200
    • Pauli, G.1
  • 41
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P.C., and Harris, D.A. 1998. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273: 33107-33110.
    • (1998) J. Biol. Chem , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 43
    • 0028822204 scopus 로고
    • A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells
    • Priola, S.A., and Chesebro, B. 1995. A single hamster PrP amino acid blocks conversion to protease-resistant PrP in scrapie-infected mouse neuroblastoma cells. J. Virol. 69: 7754-7758.
    • (1995) J. Virol , vol.69 , pp. 7754-7758
    • Priola, S.A.1    Chesebro, B.2
  • 44
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S.B. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 46
    • 0023785139 scopus 로고
    • Analyses of frequency of infection, specific infectivity, and prion protein biosynthesis in scrapie-infected neuroblastoma cell clones
    • Race, R.E., Caughey, B., Graham, K., Ernst, D., and Chesebro, B. 1988. Analyses of frequency of infection, specific infectivity, and prion protein biosynthesis in scrapie-infected neuroblastoma cell clones. J. Virol. 62: 2845-2849.
    • (1988) J. Virol , vol.62 , pp. 2845-2849
    • Race, R.E.1    Caughey, B.2    Graham, K.3    Ernst, D.4    Chesebro, B.5
  • 47
    • 0023091197 scopus 로고
    • Characterization of scrapie infection in mouse neuroblastoma cells
    • Race, R.E., Fadness, L.H., and Chesebro, B. 1987. Characterization of scrapie infection in mouse neuroblastoma cells. J. Gen. Virol. 68: 1391-1399.
    • (1987) J. Gen. Virol , vol.68 , pp. 1391-1399
    • Race, R.E.1    Fadness, L.H.2    Chesebro, B.3
  • 48
    • 0028876414 scopus 로고
    • Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent
    • Race, R.E., Priola, S.A., Bessen, R.A., Ernst, D., Dockter, J., Rall, G.F., Mucke, L., Chesebro, B., and Oldstone, M.B. 1995. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron 15: 1183-1191.
    • (1995) Neuron , vol.15 , pp. 1183-1191
    • Race, R.E.1    Priola, S.A.2    Bessen, R.A.3    Ernst, D.4    Dockter, J.5    Rall, G.F.6    Mucke, L.7    Chesebro, B.8    Oldstone, M.B.9
  • 50
    • 0027520888 scopus 로고
    • Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells
    • 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. U.S.A. 90: 3182-3186.
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 3182-3186
    • Rogers, M.1    Yehiely, F.2    Scott, M.3    Prusiner, S.B.4
  • 51
    • 0021745705 scopus 로고
    • In vitro replication of scrapie agent in a neuronal model: Infection of PC12 cells
    • Rubenstein, R., Carp, R.I., and Callahan, S.M. 1984. In vitro replication of scrapie agent in a neuronal model: infection of PC12 cells. J. Gen. Virol. 65: 2191-2198.
    • (1984) J. Gen. Virol , vol.65 , pp. 2191-2198
    • Rubenstein, R.1    Carp, R.I.2    Callahan, S.M.3
  • 55
    • 0141868913 scopus 로고    scopus 로고
    • Tumor necrosis factor attenuates prion protein-deficient neuronal cell death by increases in anti-apoptotic Bcl-2 family proteins
    • 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.
    • (2003) Biochem. Biophys. Res. Commun , vol.310 , pp. 725-729
    • Sakudo, A.1    Lee, D.C.2    Saeki, K.3    Matsumoto, Y.4    Itohara, S.5    Onodera, T.6
  • 56
    • 0041664024 scopus 로고    scopus 로고
    • Impairment of superoxide dismutase activation by N-terminally truncated prion protein (PrP) in PrP-deficient neuronal cell line
    • Sakudo, A., Lee, D.C., Saeki, K., Nakamura, Y., Inoue, K., Matsumoto, Y., Itohara, S., and Onodera, T. 2003. Impairment of superoxide dismutase activation by N-terminally truncated prion protein (PrP) in PrP-deficient neuronal cell line. Biochem. Biophys. Res. Commun. 308: 660-667.
    • (2003) Biochem. Biophys. Res. Commun , vol.308 , pp. 660-667
    • Sakudo, A.1    Lee, D.C.2    Saeki, K.3    Nakamura, Y.4    Inoue, K.5    Matsumoto, Y.6    Itohara, S.7    Onodera, T.8
  • 58
    • 33646571843 scopus 로고    scopus 로고
    • Recent advances in clarifying prion protein functions using knockout mice and derived cell lines
    • Sakudo, A., Onodera, T., Suganuma, Y., Kobayashi, T., Saeki, K., and Ikuta, K. 2006. Recent advances in clarifying prion protein functions using knockout mice and derived cell lines. Mini Rev. Med. Chem. 6: 589-601.
    • (2006) Mini Rev. Med. Chem , vol.6 , pp. 589-601
    • Sakudo, A.1    Onodera, T.2    Suganuma, Y.3    Kobayashi, T.4    Saeki, K.5    Ikuta, K.6
  • 59
    • 18544376071 scopus 로고    scopus 로고
    • Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth
    • Santuccione, A., Sytnyk, V., Leshchyns'ka, I., and Schachner, M. 2005. Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth. J. Cell Biol. 169: 341-354.
    • (2005) J. Cell Biol , vol.169 , pp. 341-354
    • Santuccione, A.1    Sytnyk, V.2    Leshchyns'ka, I.3    Schachner, M.4
  • 60
    • 0033900833 scopus 로고    scopus 로고
    • Gene expression profile in prion protein-deficient fibroblasts in culture
    • Satoh, J., Kuroda, Y., and Katamine, S. 2000. Gene expression profile in prion protein-deficient fibroblasts in culture. Am. J. Pathol. 157: 59-68.
    • (2000) Am. J. Pathol , vol.157 , pp. 59-68
    • Satoh, J.1    Kuroda, Y.2    Katamine, S.3
  • 61
    • 0032079515 scopus 로고    scopus 로고
    • Cultured skin fibroblasts isolated from mice devoid of the prion protein gene express major heat shock proteins in response to heat stress
    • Satoh, J., Yukitake, M., Kurohara, K., Nishida, N., Katamine, S., Miyamoto, T., and Kuroda, Y. 1998. Cultured skin fibroblasts isolated from mice devoid of the prion protein gene express major heat shock proteins in response to heat stress. Exp. Neurol. 151: 105-115.
    • (1998) Exp. Neurol , vol.151 , pp. 105-115
    • Satoh, J.1    Yukitake, M.2    Kurohara, K.3    Nishida, N.4    Katamine, S.5    Miyamoto, T.6    Kuroda, Y.7
  • 62
    • 0030576839 scopus 로고    scopus 로고
    • Survival factor-insensitive generation of reactive oxygen species induced by serum deprivation in neuronal cells
    • Satoh, T., Sakai, N., Enokido, Y., Uchiyama, Y., and Hatanaka, H. 1996. Survival factor-insensitive generation of reactive oxygen species induced by serum deprivation in neuronal cells. Brain Res. 733: 9-14.
    • (1996) Brain Res , vol.733 , pp. 9-14
    • Satoh, T.1    Sakai, N.2    Enokido, Y.3    Uchiyama, Y.4    Hatanaka, H.5
  • 64
    • 0345687168 scopus 로고    scopus 로고
    • NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells
    • Schneider, B., Mutel, V., Pietri, M., Ermonval, M., Mouillet-Richard, S., and Kellermann, O. 2003. NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells. Proc. Natl. Acad. Sci. U.S.A. 100: 13326-13331.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 13326-13331
    • Schneider, B.1    Mutel, V.2    Pietri, M.3    Ermonval, M.4    Mouillet-Richard, S.5    Kellermann, O.6
  • 66
    • 0027229676 scopus 로고    scopus 로고
    • Scott, M., Groth, D., Foster, D., Torchia, M., Yang, S.L., DeArmond, S.J., and Prusiner, S.B. 1993. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 73: 979-988.
    • Scott, M., Groth, D., Foster, D., Torchia, M., Yang, S.L., DeArmond, S.J., and Prusiner, S.B. 1993. Propagation of prions with artificial properties in transgenic mice expressing chimeric PrP genes. Cell 73: 979-988.
  • 68
    • 0141738247 scopus 로고    scopus 로고
    • Prion propagation in cultured cells
    • Solassol, J., Crozet, C., and Lehmann, S. 2003. Prion propagation in cultured cells. Br. Med. Bull. 66: 87-97.
    • (2003) Br. Med. Bull , vol.66 , pp. 87-97
    • Solassol, J.1    Crozet, C.2    Lehmann, S.3
  • 72
    • 0029740354 scopus 로고    scopus 로고
    • Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice
    • Telling, G.C., Haga, T., Torchia, M., Tremblay, P., DeArmond, S.J., and Prusiner, S.B. 1996. Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice. Genes Dev. 10: 1736-1750.
    • (1996) Genes Dev , vol.10 , pp. 1736-1750
    • Telling, G.C.1    Haga, T.2    Torchia, M.3    Tremblay, P.4    DeArmond, S.J.5    Prusiner, S.B.6
  • 74
    • 19344370943 scopus 로고    scopus 로고
    • Vassallo, N., Herms, J., Behrens, C., Krebs, B., Saeki, K., Onodera, T., Windl, O., and Kretzschmar, H.A. 2005. Activation of phosphatidylinositol 3-kinase by cellular prion protein and its role in cell survival. Biochem. Biophys. Res. Commun. 332: 75-82.
    • Vassallo, N., Herms, J., Behrens, C., Krebs, B., Saeki, K., Onodera, T., Windl, O., and Kretzschmar, H.A. 2005. Activation of phosphatidylinositol 3-kinase by cellular prion protein and its role in cell survival. Biochem. Biophys. Res. Commun. 332: 75-82.
  • 76
    • 0034789531 scopus 로고    scopus 로고
    • Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform
    • Vorberg, I., Chan, K., and Priola, S.A. 2001. Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform. J. Virol. 75: 10024-10032.
    • (2001) J. Virol , vol.75 , pp. 10024-10032
    • Vorberg, I.1    Chan, K.2    Priola, S.A.3
  • 77
    • 0037301367 scopus 로고    scopus 로고
    • Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform
    • Vorberg, I., Groschup, M.H., Pfaff, E., and Priola, S.A. 2003. Multiple amino acid residues within the rabbit prion protein inhibit formation of its abnormal isoform. J. Virol. 77: 2003-2009.
    • (2003) J. Virol , vol.77 , pp. 2003-2009
    • Vorberg, I.1    Groschup, M.H.2    Pfaff, E.3    Priola, S.A.4
  • 78
    • 3142726518 scopus 로고    scopus 로고
    • Acute formation of protease-resistant prion protein does not always lead to persistent scrapie infection in vitro
    • Vorberg, I., Raines, A., and Priola, S.A. 2004. Acute formation of protease-resistant prion protein does not always lead to persistent scrapie infection in vitro. J. Biol. Chem. 279: 29218-29225.
    • (2004) J. Biol. Chem , vol.279 , pp. 29218-29225
    • Vorberg, I.1    Raines, A.2    Priola, S.A.3
  • 79
    • 1142285202 scopus 로고    scopus 로고
    • Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents
    • Vorberg, I., Raines, A., Story, B., and Priola, S.A. 2004. Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. J. Infect. Dis. 189: 431-439.
    • (2004) J. Infect. Dis , vol.189 , pp. 431-439
    • Vorberg, I.1    Raines, A.2    Story, B.3    Priola, S.A.4
  • 80
    • 33646695909 scopus 로고    scopus 로고
    • Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury
    • Weise, J., Sandau, R., Schwarting, S., Crome, O., Wrede, A., Schulz-Schaeffer, W., Zerr, I., and Bahr, M. 2006. Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury. Stroke 37: 1296-1300.
    • (2006) Stroke , vol.37 , pp. 1296-1300
    • Weise, J.1    Sandau, R.2    Schwarting, S.3    Crome, O.4    Wrede, A.5    Schulz-Schaeffer, W.6    Zerr, I.7    Bahr, M.8
  • 81
    • 0033615415 scopus 로고    scopus 로고
    • Perspectives: Neurobiology. PrP's double causes trouble
    • Weissmann, C., and Aguzzi, A. 1999. Perspectives: neurobiology. PrP's double causes trouble. Science 286: 914-915.
    • (1999) Science , vol.286 , pp. 914-915
    • Weissmann, C.1    Aguzzi, A.2
  • 83
    • 0035815709 scopus 로고    scopus 로고
    • In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies
    • Yokoyama, T., Kimura, K.M., Ushiki, Y., Yamada, S., Morooka, A., Nakashiba, T., Sassa, T., and Itohara, S. 2001. In vivo conversion of cellular prion protein to pathogenic isoforms, as monitored by conformation-specific antibodies. J. Biol. Chem. 276: 11265-11271.
    • (2001) J. Biol. Chem , vol.276 , pp. 11265-11271
    • Yokoyama, T.1    Kimura, K.M.2    Ushiki, Y.3    Yamada, S.4    Morooka, A.5    Nakashiba, T.6    Sassa, T.7    Itohara, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.