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Volumn 7, Issue 11, 2011, Pages

Down-regulation of shadoo in prion infections traces a pre-clinical event inversely related to PrP sc accumulation

Author keywords

[No Author keywords available]

Indexed keywords

ADAN AMYLOID PEPTIDE; AMYLOID PROTEIN; CUPRIZONE; GLYCOPROTEIN; MESSENGER RNA; PRION PROTEIN; PROTEINASE; SHADOO PROTEIN; SPRN PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; NERVE PROTEIN; SHADOO PROTEIN, MOUSE;

EID: 81755177709     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002391     Document Type: Article
Times cited : (32)

References (71)
  • 1
    • 0030775632 scopus 로고    scopus 로고
    • Transmissions to mice indicate that "new variant" CJD is caused by the BSE agent
    • Bruce ME, Will RG, Ironside JW, McConnell I, Drummond D, et al. (1997) Transmissions to mice indicate that "new variant" CJD is caused by the BSE agent. Nature 389: 498-501.
    • (1997) Nature , vol.389 , pp. 498-501
    • Bruce, M.E.1    Will, R.G.2    Ironside, J.W.3    McConnell, I.4    Drummond, D.5
  • 2
    • 33846016529 scopus 로고    scopus 로고
    • The transmissible spongiform encephalopathies: emerging and declining epidemics
    • Manson JC, Cancellotti E, Hart P, Bishop MT, Barron RM, (2006) The transmissible spongiform encephalopathies: emerging and declining epidemics. Biochem Soc Trans 34: 1155-1158.
    • (2006) Biochem Soc Trans , vol.34 , pp. 1155-1158
    • Manson, J.C.1    Cancellotti, E.2    Hart, P.3    Bishop, M.T.4    Barron, R.M.5
  • 3
    • 0023467393 scopus 로고
    • Distinct prion proteins in short and long scrapie incubation period mice
    • Westaway D, Goodman PA, Mirenda CA, McKinley MP, Carlson GA, et al. (1987) Distinct prion proteins in short and long scrapie incubation period mice. Cell 51: 651-662.
    • (1987) Cell , vol.51 , pp. 651-662
    • Westaway, D.1    Goodman, P.A.2    Mirenda, C.A.3    McKinley, M.P.4    Carlson, G.A.5
  • 4
    • 0026739272 scopus 로고
    • Are Sinc and the PrP gene congruent? Evidence from PrP gene analysis in Sinc congenic mice
    • Hunter N, Dann JC, Bennett AD, Somerville RA, McConnell I, et al. (1992) Are Sinc and the PrP gene congruent? Evidence from PrP gene analysis in Sinc congenic mice. J Gen Virol 73: 2751-2755.
    • (1992) J Gen Virol , vol.73 , pp. 2751-2755
    • Hunter, N.1    Dann, J.C.2    Bennett, A.D.3    Somerville, R.A.4    McConnell, I.5
  • 5
    • 0031942579 scopus 로고    scopus 로고
    • Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent
    • Moore RC, Hope J, McBride PA, McConnell I, Selfridge J, et al. (1998) Mice with gene targetted prion protein alterations show that Prnp, Sinc and Prni are congruent. Nat Genet 18: 118-125.
    • (1998) Nat Genet , vol.18 , pp. 118-125
    • Moore, R.C.1    Hope, J.2    McBride, P.A.3    McConnell, I.4    Selfridge, J.5
  • 8
    • 77649213673 scopus 로고    scopus 로고
    • Generating a Prion with Bacterially Expressed Recombinant Prion Protein
    • Wang F, Wang X, Yuan CG, Ma J, (2010) Generating a Prion with Bacterially Expressed Recombinant Prion Protein. Science 327: 1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 9
    • 0026583834 scopus 로고
    • Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent
    • Bessen RA, Marsh RF, (1992) Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent. J Virol 66: 2096-2101.
    • (1992) J Virol , vol.66 , pp. 2096-2101
    • Bessen, R.A.1    Marsh, R.F.2
  • 10
    • 0031592937 scopus 로고    scopus 로고
    • A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform
    • Peretz D, Williamson RA, Matsunaga Y, Serban H, Pinilla C, et al. (1997) A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J Mol Biol 273: 614-622.
    • (1997) J Mol Biol , vol.273 , pp. 614-622
    • Peretz, D.1    Williamson, R.A.2    Matsunaga, Y.3    Serban, H.4    Pinilla, C.5
  • 11
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrPSc molecules with different conformations
    • Safar J, Wille H, Itri V, Groth D, Serban H, et al. (1998) Eight prion strains have PrPSc molecules with different conformations. Nat Med 4: 1157-1165.
    • (1998) Nat Med , vol.4 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3    Groth, D.4    Serban, H.5
  • 12
    • 28444470228 scopus 로고    scopus 로고
    • PrP(Sc) typing by N-terminal sequencing and mass spectrometry
    • Chen SG, Zou W, Parchi P, Gambetti P, (2000) PrP(Sc) typing by N-terminal sequencing and mass spectrometry. Arch Virol Suppl pp. 209-216.
    • (2000) Arch Virol Suppl , pp. 209-216
    • Chen, S.G.1    Zou, W.2    Parchi, P.3    Gambetti, P.4
  • 13
    • 0035086136 scopus 로고    scopus 로고
    • Strain-specified relative conformational stability of the scrapie prion protein
    • Peretz D, Scott MR, Groth D, Williamson RA, Burton DR, et al. (2001) Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci 10: 854-863.
    • (2001) Protein Sci , vol.10 , pp. 854-863
    • Peretz, D.1    Scott, M.R.2    Groth, D.3    Williamson, R.A.4    Burton, D.R.5
  • 14
    • 45749138009 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathy strain-associated diversity of N-terminal proteinase K cleavage sites of PrP(Sc) from scrapie-infected and bovine spongiform encephalopathy-infected mice
    • Howells LC, Anderson S, Coldham NG, Sauer MJ, (2008) Transmissible spongiform encephalopathy strain-associated diversity of N-terminal proteinase K cleavage sites of PrP(Sc) from scrapie-infected and bovine spongiform encephalopathy-infected mice. Biomarkers 13: 393-412.
    • (2008) Biomarkers , vol.13 , pp. 393-412
    • Howells, L.C.1    Anderson, S.2    Coldham, N.G.3    Sauer, M.J.4
  • 15
    • 1442302400 scopus 로고    scopus 로고
    • Murine scrapie infection causes an abnormal germinal centre reaction in the spleen
    • McGovern G, Brown KL, Bruce ME, Jeffrey M, (2004) Murine scrapie infection causes an abnormal germinal centre reaction in the spleen. J Comp Pathol 130: 181-194.
    • (2004) J Comp Pathol , vol.130 , pp. 181-194
    • McGovern, G.1    Brown, K.L.2    Bruce, M.E.3    Jeffrey, M.4
  • 16
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge J, Clarke AR, (2007) A general model of prion strains and their pathogenicity. Science 318: 930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 17
    • 34548384916 scopus 로고    scopus 로고
    • The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections
    • Watts JC, Drisaldi B, Ng V, Yang J, Strome B, et al. (2007) The CNS glycoprotein Shadoo has PrP(C)-like protective properties and displays reduced levels in prion infections. Embo J 26: 4038-4050.
    • (2007) Embo J , vol.26 , pp. 4038-4050
    • Watts, J.C.1    Drisaldi, B.2    Ng, V.3    Yang, J.4    Strome, B.5
  • 18
  • 19
    • 77749264931 scopus 로고    scopus 로고
    • Wild-type Shadoo proteins convert to amyloid-like forms under native conditions
    • Daude N, Ng V, Watts JC, Genovesi S, Glaves JP, et al. (2010) Wild-type Shadoo proteins convert to amyloid-like forms under native conditions. J Neurochem 113: 92-104.
    • (2010) J Neurochem , vol.113 , pp. 92-104
    • Daude, N.1    Ng, V.2    Watts, J.C.3    Genovesi, S.4    Glaves, J.P.5
  • 20
    • 79953174915 scopus 로고    scopus 로고
    • Conserved Stress-protective Activity between Prion Protein and Shadoo
    • Sakthivelu V, Seidel RP, Winklhofer KF, Tatzelt J, (2011) Conserved Stress-protective Activity between Prion Protein and Shadoo. J Biol Chem 286: 8901-8908.
    • (2011) J Biol Chem , vol.286 , pp. 8901-8908
    • Sakthivelu, V.1    Seidel, R.P.2    Winklhofer, K.F.3    Tatzelt, J.4
  • 21
    • 0024272862 scopus 로고
    • Genetics and polymorphism of the mouse prion gene complex: the control of scrapie incubation time
    • Carlson GA, Goodman PA, Lovett M, Taylor BA, Marshall ST, et al. (1988) Genetics and polymorphism of the mouse prion gene complex: the control of scrapie incubation time. Mol Cell Biol 8: 5528-5540.
    • (1988) Mol Cell Biol , vol.8 , pp. 5528-5540
    • Carlson, G.A.1    Goodman, P.A.2    Lovett, M.3    Taylor, B.A.4    Marshall, S.T.5
  • 22
    • 0028276015 scopus 로고
    • Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice
    • Carlson GA, Ebeling C, Yang S-L, Telling G, Torchia M, et al. (1994) Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice. Proc Natl Acad Sci USA 91: 5690-5694.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5690-5694
    • Carlson, G.A.1    Ebeling, C.2    Yang, S.-L.3    Telling, G.4    Torchia, M.5
  • 24
    • 0028535880 scopus 로고
    • High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene
    • Bueler H, Raeber A, Sailer A, Fischer M, Aguzzi A, et al. (1994) High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol Med 1: 19-30.
    • (1994) Mol Med , vol.1 , pp. 19-30
    • Bueler, H.1    Raeber, A.2    Sailer, A.3    Fischer, M.4    Aguzzi, A.5
  • 25
    • 0036184403 scopus 로고    scopus 로고
    • Strain characterization of natural sheep scrapie and comparison with BSE
    • Bruce ME, Boyle A, Cousens S, McConnell I, Foster J, et al. (2002) Strain characterization of natural sheep scrapie and comparison with BSE. J Gen Virol 83: 695-704.
    • (2002) J Gen Virol , vol.83 , pp. 695-704
    • Bruce, M.E.1    Boyle, A.2    Cousens, S.3    McConnell, I.4    Foster, J.5
  • 26
    • 0035877756 scopus 로고    scopus 로고
    • Early-onset amyloid deposition and cognitive deficits in transgenic mice expressing a double mutant form of amyloid precursor protein 695
    • Chishti MA, Yang DS, Janus C, Phinney AL, Horne P, et al. (2001) Early-onset amyloid deposition and cognitive deficits in transgenic mice expressing a double mutant form of amyloid precursor protein 695. J Biol Chem 276: 21562-21570.
    • (2001) J Biol Chem , vol.276 , pp. 21562-21570
    • Chishti, M.A.1    Yang, D.S.2    Janus, C.3    Phinney, A.L.4    Horne, P.5
  • 27
    • 0014530743 scopus 로고
    • Spongiform encephalopathy induced in rats and guinea pigs by cuprizone
    • Carlton WW, (1969) Spongiform encephalopathy induced in rats and guinea pigs by cuprizone. Exp Mol Pathol 10: 274-287.
    • (1969) Exp Mol Pathol , vol.10 , pp. 274-287
    • Carlton, W.W.1
  • 28
    • 0015090051 scopus 로고
    • Clinical and histological observations on cuprizone toxicity and scrapie in mice
    • Pattison IH, Jebbett JN, (1971) Clinical and histological observations on cuprizone toxicity and scrapie in mice. Res Vet Sci 12: 378-380.
    • (1971) Res Vet Sci , vol.12 , pp. 378-380
    • Pattison, I.H.1    Jebbett, J.N.2
  • 29
    • 0016193449 scopus 로고
    • A comparison of the biochemical changes induced in mouse brain cuprizone toxicity and by scrapie infection
    • Kimberlin RH, Millson GC, Bountiff L, Collis SC, (1974) A comparison of the biochemical changes induced in mouse brain cuprizone toxicity and by scrapie infection. J Comp Pathol 84: 263-270.
    • (1974) J Comp Pathol , vol.84 , pp. 263-270
    • Kimberlin, R.H.1    Millson, G.C.2    Bountiff, L.3    Collis, S.C.4
  • 30
    • 0015472801 scopus 로고
    • Observations on oligodendrocyte degeneration, the resolution of status spongiosus and remyelination in cuprizone intoxication in mice
    • Blakemore WF, (1972) Observations on oligodendrocyte degeneration, the resolution of status spongiosus and remyelination in cuprizone intoxication in mice. J Neurocytol 1: 413-426.
    • (1972) J Neurocytol , vol.1 , pp. 413-426
    • Blakemore, W.F.1
  • 31
    • 67649352679 scopus 로고    scopus 로고
    • Comparative prion disease gene expression profiling using the prion disease mimetic, cuprizone
    • Moody LR, Herbst AJ, Yoo HS, Vanderloo JP, Aiken JM, (2009) Comparative prion disease gene expression profiling using the prion disease mimetic, cuprizone. Prion 3: 99-109.
    • (2009) Prion , vol.3 , pp. 99-109
    • Moody, L.R.1    Herbst, A.J.2    Yoo, H.S.3    Vanderloo, J.P.4    Aiken, J.M.5
  • 32
    • 34447323183 scopus 로고    scopus 로고
    • Cortical neuronal and glial pathology in TgTauP301L transgenic mice: neuronal degeneration, memory disturbance, and phenotypic variation
    • Murakami T, Paitel E, Kawarabayashi T, Ikeda M, Chishti MA, et al. (2006) Cortical neuronal and glial pathology in TgTauP301L transgenic mice: neuronal degeneration, memory disturbance, and phenotypic variation. Am J Pathol 169: 1365-1375.
    • (2006) Am J Pathol , vol.169 , pp. 1365-1375
    • Murakami, T.1    Paitel, E.2    Kawarabayashi, T.3    Ikeda, M.4    Chishti, M.A.5
  • 33
    • 77952418165 scopus 로고    scopus 로고
    • Modeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease
    • Coomaraswamy J, Kilger E, Wolfing H, Schafer C, Kaeser SA, et al. (2010) Modeling familial Danish dementia in mice supports the concept of the amyloid hypothesis of Alzheimer's disease. Proc Natl Acad Sci U S A 107: 7969-7974.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7969-7974
    • Coomaraswamy, J.1    Kilger, E.2    Wolfing, H.3    Schafer, C.4    Kaeser, S.A.5
  • 35
    • 0021884354 scopus 로고
    • Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain
    • Chesebro B, Race R, Wehrly K, Nishio J, Bloom M, et al. (1985) Identification of scrapie prion protein-specific mRNA in scrapie-infected and uninfected brain. Nature 315: 331-333.
    • (1985) Nature , vol.315 , pp. 331-333
    • Chesebro, B.1    Race, R.2    Wehrly, K.3    Nishio, J.4    Bloom, M.5
  • 36
    • 84908106285 scopus 로고    scopus 로고
    • The Prion Disease Database: a comprehensive transcriptome resource for systems biology research in prion diseases
    • Database (Oxford) 2009: bap011
    • Gehlenborg N, Hwang D, Lee IY, Yoo H, Baxter D, et al. (2009) The Prion Disease Database: a comprehensive transcriptome resource for systems biology research in prion diseases. Database (Oxford) 2009: bap011.
    • (2009)
    • Gehlenborg, N.1    Hwang, D.2    Lee, I.Y.3    Yoo, H.4    Baxter, D.5
  • 37
    • 0141760321 scopus 로고    scopus 로고
    • Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein
    • Premzl M, Sangiorgio L, Strumbo B, Marshall Graves JA, Simonic T, et al. (2003) Shadoo, a new protein highly conserved from fish to mammals and with similarity to prion protein. Gene 314: 89-102.
    • (2003) Gene , vol.314 , pp. 89-102
    • Premzl, M.1    Sangiorgio, L.2    Strumbo, B.3    Marshall, G.J.A.4    Simonic, T.5
  • 38
    • 77249092467 scopus 로고    scopus 로고
    • Agent-specific Shadoo Responses in Transmissible Encephalopathies
    • Miyazawa K, Manuelidis L, (2010) Agent-specific Shadoo Responses in Transmissible Encephalopathies. J Neuroimmune Pharmacol 5: 155-163.
    • (2010) J Neuroimmune Pharmacol , vol.5 , pp. 155-163
    • Miyazawa, K.1    Manuelidis, L.2
  • 39
    • 67651149482 scopus 로고    scopus 로고
    • Shadoo (Sprn) and prion disease incubation time in mice
    • Lloyd SE, Grizenkova J, Pota H, Collinge J, (2009) Shadoo (Sprn) and prion disease incubation time in mice. Mamm Genome 20: 367-374.
    • (2009) Mamm Genome , vol.20 , pp. 367-374
    • Lloyd, S.E.1    Grizenkova, J.2    Pota, H.3    Collinge, J.4
  • 40
    • 0027291065 scopus 로고
    • Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor
    • Borchelt DR, Rogers M, Stahl N, Telling G, Prusiner SB, (1993) Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor. Glycobiology 3: 319-329.
    • (1993) Glycobiology , vol.3 , pp. 319-329
    • Borchelt, D.R.1    Rogers, M.2    Stahl, N.3    Telling, G.4    Prusiner, S.B.5
  • 41
    • 0025091084 scopus 로고
    • Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein
    • Stahl N, Baldwin MA, Burlingame AL, Prusiner SB, (1990) Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein. Biochemistry 29: 8879-8884.
    • (1990) Biochemistry , vol.29 , pp. 8879-8884
    • Stahl, N.1    Baldwin, M.A.2    Burlingame, A.L.3    Prusiner, S.B.4
  • 42
    • 0027086835 scopus 로고
    • Chimeric prion protein expression in cultured cells and transgenic mice
    • Scott MR, Köhler R, Foster D, Prusiner SB, (1992) Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci 1: 986-997.
    • (1992) Protein Sci , vol.1 , pp. 986-997
    • Scott, M.R.1    Köhler, R.2    Foster, D.3    Prusiner, S.B.4
  • 43
    • 0032032493 scopus 로고    scopus 로고
    • Turnover of amyloid beta-protein in mouse brain and acute reduction of its level by phorbol ester
    • Savage MJ, Trusko SP, Howland DS, Pinsker LR, Mistretta S, et al. (1998) Turnover of amyloid beta-protein in mouse brain and acute reduction of its level by phorbol ester. J Neurosci 18: 1743-1752.
    • (1998) J Neurosci , vol.18 , pp. 1743-1752
    • Savage, M.J.1    Trusko, S.P.2    Howland, D.S.3    Pinsker, L.R.4    Mistretta, S.5
  • 44
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • Eckman EA, Watson M, Marlow L, Sambamurti K, Eckman CB, (2003) Alzheimer's disease beta-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J Biol Chem 278: 2081-2084.
    • (2003) J Biol Chem , vol.278 , pp. 2081-2084
    • Eckman, E.A.1    Watson, M.2    Marlow, L.3    Sambamurti, K.4    Eckman, C.B.5
  • 45
    • 79955621862 scopus 로고    scopus 로고
    • Overexpression of Shadoo protein in transgenic mice does not impact the pathogenesis of scrapie
    • Wang H, Wan J, Wang W, Wang D, Li S, et al. (2011) Overexpression of Shadoo protein in transgenic mice does not impact the pathogenesis of scrapie. Neurosci Lett 496: 1-4.
    • (2011) Neurosci Lett , vol.496 , pp. 1-4
    • Wang, H.1    Wan, J.2    Wang, W.3    Wang, D.4    Li, S.5
  • 46
    • 0037611374 scopus 로고    scopus 로고
    • A hypothalamic neuronal cell line persistently infected with scrapie prions exhibits apoptosis
    • Schatzl HM, Laszlo L, Holtzman DM, Tatzelt J, DeArmond SJ, et al. (1997) A hypothalamic neuronal cell line persistently infected with scrapie prions exhibits apoptosis. J Virol 71: 8821-8831.
    • (1997) J Virol , vol.71 , pp. 8821-8831
    • Schatzl, H.M.1    Laszlo, L.2    Holtzman, D.M.3    Tatzelt, J.4    DeArmond, S.J.5
  • 47
    • 0035796463 scopus 로고    scopus 로고
    • Scrapie strains maintain biological phenotypes on propagation in a cell line in culture
    • Birkett CR, Hennion RM, Bembridge DA, Clarke MC, Chree A, et al. (2001) Scrapie strains maintain biological phenotypes on propagation in a cell line in culture. EMBO J 20: 3351-3358.
    • (2001) EMBO J , vol.20 , pp. 3351-3358
    • Birkett, C.R.1    Hennion, R.M.2    Bembridge, D.A.3    Clarke, M.C.4    Chree, A.5
  • 48
    • 0025876226 scopus 로고
    • N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state
    • Caughey B, Raymond GJ, Ernst D, Race RE, (1991) N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J Virol 65: 6597-6603.
    • (1991) J Virol , vol.65 , pp. 6597-6603
    • Caughey, B.1    Raymond, G.J.2    Ernst, D.3    Race, R.E.4
  • 50
    • 0034700471 scopus 로고    scopus 로고
    • Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease
    • Janus C, Pearson J, McLaurin J, Mathews PM, Jiang Y, et al. (2000) Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease. Nature 408: 979-982.
    • (2000) Nature , vol.408 , pp. 979-982
    • Janus, C.1    Pearson, J.2    McLaurin, J.3    Mathews, P.M.4    Jiang, Y.5
  • 51
    • 81755166672 scopus 로고    scopus 로고
    • Protease resistant prion proteins selectively decrease Shadoo protein
    • Watts JC, Stohr J, Bhardwaj S, Wille H, Oehler A, et al. (2011) Protease resistant prion proteins selectively decrease Shadoo protein. PLoS Path 7: e1002382.
    • (2011) PLoS Path , vol.7
    • Watts, J.C.1    Stohr, J.2    Bhardwaj, S.3    Wille, H.4    Oehler, A.5
  • 52
    • 0025244011 scopus 로고
    • Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication
    • Prusiner S, Scott M, Foster D, Westaway D, DeArmond S, (1990) Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63: 673-686.
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.1    Scott, M.2    Foster, D.3    Westaway, D.4    DeArmond, S.5
  • 53
    • 73349140865 scopus 로고    scopus 로고
    • Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones
    • Watts JC, Huo H, Bai Y, Ehsani S, Jeon AH, et al. (2009) Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones. PLoS Pathog 5: e1000608.
    • (2009) PLoS Pathog , vol.5
    • Watts, J.C.1    Huo, H.2    Bai, Y.3    Ehsani, S.4    Jeon, A.H.5
  • 54
    • 0032440093 scopus 로고    scopus 로고
    • Microglial/macrophage accumulation during cuprizone-induced demyelination in C57BL/6 mice
    • Hiremath MM, Saito Y, Knapp GW, Ting JP, Suzuki K, et al. (1998) Microglial/macrophage accumulation during cuprizone-induced demyelination in C57BL/6 mice. J Neuroimmunol 92: 38-49.
    • (1998) J Neuroimmunol , vol.92 , pp. 38-49
    • Hiremath, M.M.1    Saito, Y.2    Knapp, G.W.3    Ting, J.P.4    Suzuki, K.5
  • 56
    • 0023928927 scopus 로고
    • Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins
    • Butler DA, Scott MRD, Bockman JM, Borchelt DR, Taraboulos A, et al. (1988) Scrapie-infected murine neuroblastoma cells produce protease-resistant prion proteins. J Virol 62: 1558-1564.
    • (1988) J Virol , vol.62 , pp. 1558-1564
    • Butler, D.A.1    Scott, M.R.D.2    Bockman, J.M.3    Borchelt, D.R.4    Taraboulos, A.5
  • 57
    • 0025786830 scopus 로고
    • The scrapie agent in vitro
    • Race R, (1991) The scrapie agent in vitro. Curr Top Microbiol Immunol 172: 181-193.
    • (1991) Curr Top Microbiol Immunol , vol.172 , pp. 181-193
    • Race, R.1
  • 58
    • 77955607650 scopus 로고    scopus 로고
    • Peripheral protein quality control removes unfolded CFTR from the plasma membrane
    • Okiyoneda T, Barriere H, Bagdany M, Rabeh WM, Du K, et al. (2010) Peripheral protein quality control removes unfolded CFTR from the plasma membrane. Science 329: 805-810.
    • (2010) Science , vol.329 , pp. 805-810
    • Okiyoneda, T.1    Barriere, H.2    Bagdany, M.3    Rabeh, W.M.4    Du, K.5
  • 59
    • 70350516506 scopus 로고    scopus 로고
    • Genetic analysis of the SPRN gene in ruminants reveals polymorphisms in the alanine-rich segment of shadoo protein
    • Stewart P, Shen C, Zhao D, Goldmann W, (2009) Genetic analysis of the SPRN gene in ruminants reveals polymorphisms in the alanine-rich segment of shadoo protein. J Gen Virol 90: 2575-2580.
    • (2009) J Gen Virol , vol.90 , pp. 2575-2580
    • Stewart, P.1    Shen, C.2    Zhao, D.3    Goldmann, W.4
  • 60
    • 68349128297 scopus 로고    scopus 로고
    • Frequent missense and insertion/deletion polymorphisms in the ovine Shadoo gene parallel species-specific variation in PrP
    • Daude N, Wohlgemuth S, Rogaeva E, Farid AH, Heaton M, et al. (2009) Frequent missense and insertion/deletion polymorphisms in the ovine Shadoo gene parallel species-specific variation in PrP. PLoS One 4: e6538.
    • (2009) PLoS One , vol.4
    • Daude, N.1    Wohlgemuth, S.2    Rogaeva, E.3    Farid, A.H.4    Heaton, M.5
  • 61
    • 57349086072 scopus 로고    scopus 로고
    • Association of a null allele of SPRN with variant Creutzfeldt-Jakob disease
    • Beck JA, Campbell TA, Adamson G, Poulter M, Uphill JB, et al. (2008) Association of a null allele of SPRN with variant Creutzfeldt-Jakob disease. J Med Genet 45: 813-817.
    • (2008) J Med Genet , vol.45 , pp. 813-817
    • Beck, J.A.1    Campbell, T.A.2    Adamson, G.3    Poulter, M.4    Uphill, J.B.5
  • 62
    • 0028276015 scopus 로고
    • Prion isolate specific allotypic interactions between cellular and scrapie prion proteins in congenic and transgenic mice
    • Carlson G, Ebeling C, Yang SL, Telling G, Torchia M, et al. (1994) Prion isolate specific allotypic interactions between cellular and scrapie prion proteins in congenic and transgenic mice. Proc Natl Acad Sci USA 91: 5690-5694.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5690-5694
    • Carlson, G.1    Ebeling, C.2    Yang, S.L.3    Telling, G.4    Torchia, M.5
  • 63
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Büeler H, Fischer M, Lang Y, Bluethmann H, Lipp HP, et al. (1992) Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356: 577-582.
    • (1992) Nature , vol.356 , pp. 577-582
    • Büeler, H.1    Fischer, M.2    Lang, Y.3    Bluethmann, H.4    Lipp, H.P.5
  • 65
    • 21144447065 scopus 로고    scopus 로고
    • Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases
    • Mastrangelo P, Mathews PM, Chishti MA, Schmidt SD, Gu Y, et al. (2005) Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases. Proc Natl Acad Sci U S A 102: 8972-8977.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 8972-8977
    • Mastrangelo, P.1    Mathews, P.M.2    Chishti, M.A.3    Schmidt, S.D.4    Gu, Y.5
  • 66
    • 0020787415 scopus 로고
    • An optimized freeze-squeeze method for the recovery of DNA fragments from agarose gels
    • Tautz D, Renz M, (1983) An optimized freeze-squeeze method for the recovery of DNA fragments from agarose gels. Anal Biochem 132: 14-19.
    • (1983) Anal Biochem , vol.132 , pp. 14-19
    • Tautz, D.1    Renz, M.2
  • 67
    • 0024820814 scopus 로고
    • Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques
    • Scott M, Foster D, Mirenda C, Serban D, Coufal F, et al. (1989) Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59: 847-857.
    • (1989) Cell , vol.59 , pp. 847-857
    • Scott, M.1    Foster, D.2    Mirenda, C.3    Serban, D.4    Coufal, F.5
  • 68
    • 0014078779 scopus 로고
    • In-vitro growth of pieces of brain from scrapie-affected mice
    • Haig DA, Pattison IH, (1967) In-vitro growth of pieces of brain from scrapie-affected mice. J Path Bact 93: 724-727.
    • (1967) J Path Bact , vol.93 , pp. 724-727
    • Haig, D.A.1    Pattison, I.H.2
  • 69
    • 0000122678 scopus 로고
    • Infection of cell cultures with scrapie agent
    • In: Prusiner SB, Hadlow WJ, editors, New York, Academic Press
    • Clarke MC, (1979) Infection of cell cultures with scrapie agent. In: Prusiner SB, Hadlow WJ, editors. Slow Transmissible Diseases of the Nervous System, Vol 2 New York Academic Press pp. 225-234.
    • (1979) Slow Transmissible Diseases of the Nervous System , vol.2 , pp. 225-234
    • Clarke, M.C.1
  • 71
    • 0035899413 scopus 로고    scopus 로고
    • Antibodies inhibit prion propagation and clear cell cultures of prion infectivity
    • Peretz D, Williamson RA, Kaneko K, Vergara J, Leclerc E, et al. (2001) Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412: 739-743.
    • (2001) Nature , vol.412 , pp. 739-743
    • Peretz, D.1    Williamson, R.A.2    Kaneko, K.3    Vergara, J.4    Leclerc, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.