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Volumn 109, Issue 1, 2005, Pages 32-48

Pathogenesis of prion diseases

Author keywords

Immune system; Microglia; Oxidative stress; Peripheral nervous system; Prion pathogenesis

Indexed keywords

3 NITROTYROSINE; 4 AMINOBUTYRIC ACID RECEPTOR; CALCIUM; CALPAIN; CASPASE 12; CASPASE 3; COMPLEMENT MEMBRANE ATTACK COMPLEX; COPPER ZINC SUPEROXIDE DISMUTASE; DNA FRAGMENT; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HEME OXYGENASE 1; INTERLEUKIN 1BETA; INTERLEUKIN 6; MANGANESE SUPEROXIDE DISMUTASE; POLY(ADENOSINE DIPHOSPHATE RIBOSE); PRION PROTEIN; REACTIVE NITROGEN SPECIES; RNA; TUMOR NECROSIS FACTOR ALPHA;

EID: 14244268370     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00401-004-0953-9     Document Type: Review
Times cited : (50)

References (153)
  • 1
    • 0022539964 scopus 로고
    • Complement membrane attack complex stimulates production of reactive oxygen metabolites by cultured rat mesangial cells
    • Adler S, Baker PJ, Johnson RJ, Ochi RF, Pritzl P, Couser WG (1986) Complement membrane attack complex stimulates production of reactive oxygen metabolites by cultured rat mesangial cells. J Clin Invest 77:762-767
    • (1986) J. Clin. Invest. , vol.77 , pp. 762-767
    • Adler, S.1    Baker, P.J.2    Johnson, R.J.3    Ochi, R.F.4    Pritzl, P.5    Couser, W.G.6
  • 3
    • 0021716145 scopus 로고
    • Neurone loss in the nucleus basalis of Meynert in Creutzfeldt-Jakob disease
    • Arendt T, Bigl V, Arendt A (1984) Neurone loss in the nucleus basalis of Meynert in Creutzfeldt-Jakob disease. Acta Neuropathol 65:85-88
    • (1984) Acta Neuropathol. , vol.65 , pp. 85-88
    • Arendt, T.1    Bigl, V.2    Arendt, A.3
  • 6
    • 0030949946 scopus 로고    scopus 로고
    • Evidence for an alternative direct route of access for the scrapie agent to the brain bypassing the spinal cord
    • Baldauf E, Beekes M, Diringer H (1997) Evidence for an alternative direct route of access for the scrapie agent to the brain bypassing the spinal cord. J Gen Virol 78:1187-1197
    • (1997) J. Gen. Virol. , vol.78 , pp. 1187-1197
    • Baldauf, E.1    Beekes, M.2    Diringer, H.3
  • 7
    • 0035828142 scopus 로고    scopus 로고
    • Killing of prion-damaged neurones by microglia
    • Bate C, Reid S, Williams A (2001) Killing of prion-damaged neurones by microglia. Neuroreport 12:2589-2594
    • (2001) Neuroreport , vol.12 , pp. 2589-2594
    • Bate, C.1    Reid, S.2    Williams, A.3
  • 8
    • 0031881510 scopus 로고    scopus 로고
    • Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie
    • Beekes M, McBride PA, Baldauf E (1998) Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie. J Gen Virol 79:601-607
    • (1998) J. Gen. Virol. , vol.79 , pp. 601-607
    • Beekes, M.1    McBride, P.A.2    Baldauf, E.3
  • 9
    • 0032885694 scopus 로고    scopus 로고
    • Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease
    • Belichenko PV, Miklossy J, Belser B, Budka H, Celio MR (1999) Early destruction of the extracellular matrix around parvalbumin-immunoreactive interneurons in Creutzfeldt-Jakob disease. Neurobiol Dis 6:269-279
    • (1999) Neurobiol. Dis. , vol.6 , pp. 269-279
    • Belichenko, P.V.1    Miklossy, J.2    Belser, B.3    Budka, H.4    Celio, M.R.5
  • 12
    • 0041852638 scopus 로고    scopus 로고
    • Inducible cytokine gene expression in the brain in the ME7/CV mouse model of scrapie is highly restricted, is at a strikingly low level relative to the degree of gliosis and occurs only late in the disease
    • Brown AR, Webb J, Rebus S, Walker R, Williams A, Fazakerley JK (2003) Inducible cytokine gene expression in the brain in the ME7/CV mouse model of scrapie is highly restricted, is at a strikingly low level relative to the degree of gliosis and occurs only late in the disease. J Gen Virol 84:2605-2611
    • (2003) J. Gen. Virol. , vol.84 , pp. 2605-2611
    • Brown, A.R.1    Webb, J.2    Rebus, S.3    Walker, R.4    Williams, A.5    Fazakerley, J.K.6
  • 13
    • 0032212367 scopus 로고    scopus 로고
    • Prion protein-overexpressing cells show altered response to a neurotoxic prion protein peptide
    • Brown DR (1998) Prion protein-overexpressing cells show altered response to a neurotoxic prion protein peptide. J Neurosci Res 54:331-340
    • (1998) J. Neurosci. Res. , vol.54 , pp. 331-340
    • Brown, D.R.1
  • 14
    • 0032817255 scopus 로고    scopus 로고
    • Prion protein peptide neurotoxicity can be mediated by astrocytes
    • Brown DR (1999) Prion protein peptide neurotoxicity can be mediated by astrocytes. J Neurochem 73:1105-1113
    • (1999) J. Neurochem. , vol.73 , pp. 1105-1113
    • Brown, D.R.1
  • 15
    • 0034533064 scopus 로고    scopus 로고
    • Sc-like prion protein peptide inhibits the function of cellular prion protein
    • Sc-like prion protein peptide inhibits the function of cellular prion protein. Biochem J 352:511-518
    • (2000) Biochem. J. , vol.352 , pp. 511-518
    • Brown, D.R.1
  • 16
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • Brown DR, Besinger A (1998) Prion protein expression and superoxide dismutase activity. Biochem J 334:423-429
    • (1998) Biochem. J. , vol.334 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 17
    • 0036798415 scopus 로고    scopus 로고
    • Copper-dependent functions for the prion protein
    • Brown DR, Sassoon J (2002) Copper-dependent functions for the prion protein. Mol Biotechnol 22:165-178
    • (2002) Mol. Biotechnol. , vol.22 , pp. 165-178
    • Brown, D.R.1    Sassoon, J.2
  • 18
    • 0028143841 scopus 로고
    • Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment
    • Brown DR, Herms J, Kretzschmar HA (1994) Mouse cortical cells lacking cellular PrP survive in culture with a neurotoxic PrP fragment. Neuroreport 5:2057-2060
    • (1994) Neuroreport , vol.5 , pp. 2057-2060
    • Brown, D.R.1    Herms, J.2    Kretzschmar, H.A.3
  • 19
    • 0029997484 scopus 로고    scopus 로고
    • Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
    • Brown DR, Schmidt B, Kretzschmar HA (1996) Role of microglia and host prion protein in neurotoxicity of a prion protein fragment. Nature 380:345-347
    • (1996) Nature , vol.380 , pp. 345-347
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 21
    • 18344403931 scopus 로고    scopus 로고
    • Effects of oxidative stress on prion protein expression in PC12 cells
    • Brown DR, Schmidt B, Kretzschmar HA (1997) Effects of oxidative stress on prion protein expression in PC12 cells. Int J Dev Neurosci 15:961-972
    • (1997) Int. J. Dev. Neurosci. , vol.15 , pp. 961-972
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 22
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown DR, Schulz-Schaeffer WJ, Schmidt B, Kretzschmar HA (1997) Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp Neurol 146:104-112
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 24
    • 0035158321 scopus 로고    scopus 로고
    • Antioxidant activity related to copper binding of native prion protein
    • Brown DR, Clive C, Haswell SJ (2001) Antioxidant activity related to copper binding of native prion protein. J Neurochem 76:69-76
    • (2001) J. Neurochem. , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.J.3
  • 25
    • 0037080043 scopus 로고    scopus 로고
    • Lack of prion protein expression results in a neuronal phenotype sensitive to stress
    • Brown DR, Nicholas RSJ, Canevari L (2002) Lack of prion protein expression results in a neuronal phenotype sensitive to stress. J Neurosci Res 67:211-224
    • (2002) J. Neurosci. Res. , vol.67 , pp. 211-224
    • Brown, D.R.1    Nicholas, R.S.J.2    Canevari, L.3
  • 27
    • 0141515178 scopus 로고    scopus 로고
    • TSE strain variation
    • Bruce ME (2003) TSE strain variation. Br Med Bull 66:99-108
    • (2003) Br. Med. Bull. , vol.66 , pp. 99-108
    • Bruce, M.E.1
  • 28
    • 28444470232 scopus 로고    scopus 로고
    • Histopathology and immunohistochemistry of human transmissible spongiform encephalopathies (TSEs)
    • Budka H (2000) Histopathology and immunohistochemistry of human transmissible spongiform encephalopathies (TSEs). Arch Virol [Suppl] 16:135 142
    • (2000) Arch. Virol. , vol.16 , Issue.SUPPL. , pp. 135-142
    • Budka, H.1
  • 29
    • 0141849861 scopus 로고    scopus 로고
    • Neuropathology of prion diseases
    • Budka H (2003) Neuropathology of prion diseases. Br Med Bull 66:121-130
    • (2003) Br. Med. Bull. , vol.66 , pp. 121-130
    • Budka, H.1
  • 32
    • 0028535880 scopus 로고
    • High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene
    • Büeler H, Raeber A, Sailer A, Fischer M, Aguzzi A, Weissmann C (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
    • Büeler, H.1    Raeber, A.2    Sailer, A.3    Fischer, M.4    Aguzzi, A.5    Weissmann, C.6
  • 33
    • 0033386245 scopus 로고    scopus 로고
    • Poly(ADP-ribose) immunostaining to detect apoptosis induced by a neurotoxic fragment of prion protein
    • Bürkle A, Kretzschmar HA, Brown DR (1999) Poly(ADP-ribose) immunostaining to detect apoptosis induced by a neurotoxic fragment of prion protein. Histochem J 31:711-716
    • (1999) Histochem. J. , vol.31 , pp. 711-716
    • Bürkle, A.1    Kretzschmar, H.A.2    Brown, D.R.3
  • 35
    • 0031710192 scopus 로고    scopus 로고
    • Mitochondrial dysfunction induced by oxidative stress in the brains of hamsters infected with the 263 K scrapie agent
    • Choi SI, Ju WK, Choi EK, Kim J, Lea HZ, Carp RI, Wisniewski HM, Kim YS (1998) Mitochondrial dysfunction induced by oxidative stress in the brains of hamsters infected with the 263 K scrapie agent. Acta Neuropathol 96:279-286
    • (1998) Acta Neuropathol. , vol.96 , pp. 279-286
    • Choi, S.I.1    Ju, W.K.2    Choi, E.K.3    Kim, J.4    Lea, H.Z.5    Carp, R.I.6    Wisniewski, H.M.7    Kim, Y.S.8
  • 37
    • 0021212843 scopus 로고
    • Pathogenesis of mouse scrapie: Distribution of agent in the pulp and stroma of infected spleens
    • Clarke MC, Kimberlin RH (1984) Pathogenesis of mouse scrapie: distribution of agent in the pulp and stroma of infected spleens. Vet Microbiol 9:215-225
    • (1984) Vet. Microbiol. , vol.9 , pp. 215-225
    • Clarke, M.C.1    Kimberlin, R.H.2
  • 38
    • 0026788002 scopus 로고
    • Key morphological features of apoptosis may occur in the absence of internucleosomal DNA fragmentation
    • Cohen GM, Sun XM, Snowden RT, Dinsdale D, Skilleter DN (1992) Key morphological features of apoptosis may occur in the absence of internucleosomal DNA fragmentation. Biochem J 286:331-334
    • (1992) Biochem. J. , vol.286 , pp. 331-334
    • Cohen, G.M.1    Sun, X.M.2    Snowden, R.T.3    Dinsdale, D.4    Skilleter, D.N.5
  • 39
    • 0021808813 scopus 로고
    • Pathogenesis of mouse scrapie: Dynamics of vacuolation in brain and spinal cord after intraperitoneal infection
    • Cole S, Kimberlin RH (1985) Pathogenesis of mouse scrapie: Dynamics of vacuolation in brain and spinal cord after intraperitoneal infection. Neuropathol Appl Neurobiol 11:213-227
    • (1985) Neuropathol. Appl. Neurobiol. , vol.11 , pp. 213-227
    • Cole, S.1    Kimberlin, R.H.2
  • 42
    • 0026731894 scopus 로고
    • Interleukin 3 protects murine bone marrow cells from apoptosis induced by DNA damaging agents
    • Collins MK, Marvel J, Malde P, Lopez-Rivas A (1992) Interleukin 3 protects murine bone marrow cells from apoptosis induced by DNA damaging agents. J Exp Med 176:1043-1051
    • (1992) J. Exp. Med. , vol.176 , pp. 1043-1051
    • Collins, M.K.1    Marvel, J.2    Malde, P.3    Lopez-Rivas, A.4
  • 44
    • 0036230262 scopus 로고    scopus 로고
    • Transforming growth factor β1, the dominant cytokine in murine prion disease: Influence on inflammatory cytokine synthesis and alteration of vascular extracellular matrix
    • Cunningham C, Boche D, Perry VH (2002) Transforming growth factor β1, the dominant cytokine in murine prion disease: Influence on inflammatory cytokine synthesis and alteration of vascular extracellular matrix. Neuropathol Appl Neurobiol 28:107-119
    • (2002) Neuropathol. Appl. Neurobiol. , vol.28 , pp. 107-119
    • Cunningham, C.1    Boche, D.2    Perry, V.H.3
  • 47
    • 0028330051 scopus 로고
    • C3a activates reactive oxygen radical species production and intracellular calcium transients in human eosinophils
    • Elsner J, Oppermann M, Czech W, Dobos G, Schöpf E, Norgauer J, Kapp A (1994) C3a activates reactive oxygen radical species production and intracellular calcium transients in human eosinophils. Eur J Immunol 24:518-522
    • (1994) Eur. J. Immunol. , vol.24 , pp. 518-522
    • Elsner, J.1    Oppermann, M.2    Czech, W.3    Dobos, G.4    Schöpf, E.5    Norgauer, J.6    Kapp, A.7
  • 48
    • 0033521542 scopus 로고    scopus 로고
    • Mature follicular dendritic cell networks depend on expression of lymphotoxin beta receptor by radioresistant stromal cells and of lymphotoxin beta and tumor necrosis factor by B cells
    • Endres R, Alimzhanov MB, Plitz T, Futterer A, Kosco-Vilbois MH, Nedospasov SA, Rajewsky K, Pfeffer K (1999) Mature follicular dendritic cell networks depend on expression of lymphotoxin beta receptor by radioresistant stromal cells and of lymphotoxin beta and tumor necrosis factor by B cells. J Exp Med 189:159-168
    • (1999) J. Exp. Med. , vol.189 , pp. 159-168
    • Endres, R.1    Alimzhanov, M.B.2    Plitz, T.3    Futterer, A.4    Kosco-Vilbois, M.H.5    Nedospasov, S.A.6    Rajewsky, K.7    Pfeffer, K.8
  • 49
    • 0027276494 scopus 로고
    • The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation
    • Falcieri E, Martelli AM, Bareggi R, Cataldi A, Cocco L (1993) The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation. Biochem Biophys Res Commun 193:19-25
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 19-25
    • Falcieri, E.1    Martelli, A.M.2    Bareggi, R.3    Cataldi, A.4    Cocco, L.5
  • 50
    • 0033002350 scopus 로고    scopus 로고
    • Nuclear DNA fragmentation in Creutzfeldt-Jakob disease: Does a mere positive in situ nuclear end-labeling indicate apoptosis?
    • Ferrer I (1999) Nuclear DNA fragmentation in Creutzfeldt-Jakob disease: does a mere positive in situ nuclear end-labeling indicate apoptosis? Acta Neuropathol 97:5-12
    • (1999) Acta Neuropathol. , vol.97 , pp. 5-12
    • Ferrer, I.1
  • 52
    • 0027768576 scopus 로고
    • Demonstration of extensive chromatin cleavage in transplanted Morris hepatoma 7777 tissue: Apoptosis or necrosis?
    • 1:CAS:528:DyaK3sXkvFanu78%3D
    • K, Kojiro M, Chiu JF (1993) Demonstration of extensive chromatin cleavage in transplanted Morris hepatoma 7777 tissue: Apoptosis or necrosis? Am J Pathol 142:935-946 1:CAS:528:DyaK3sXkvFanu78%3D
    • (1993) Am. J. Pathol. , vol.142 , pp. 935-946
    • Fukuda, K.1    Kojiro, M.2    Chiu, J.F.3
  • 53
    • 0033921540 scopus 로고    scopus 로고
    • Complement components of the innate immune system in health and disease in the CNS
    • Gasque P, Dean YD, McGreal EP, VanBeek J, Morgan BP (2000) Complement components of the innate immune system in health and disease in the CNS. Immunopharmacology 49:171-186
    • (2000) Immunopharmacology , vol.49 , pp. 171-186
    • Gasque, P.1    Dean, Y.D.2    McGreal, E.P.3    VanBeek, J.4    Morgan, B.P.5
  • 54
    • 0026648674 scopus 로고
    • Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation
    • 10.1083/jcb.119.3.493
    • Gavrieli Y, Sherman Y, Ben-Sasson SA (1992) Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J Cell Biol 119:493-501 10.1083/jcb.119.3.493
    • (1992) J Cell Biol , vol.119 , pp. 493-501
    • Gavrieli, Y.1    Sherman, Y.2    Ben-Sasson, S.A.3
  • 55
    • 0029085515 scopus 로고
    • Neuronal cell death in scrapie-infected mice is due to apoptosis
    • 1:STN:280:BymD2cfhsFU%3D
    • Giese A, Groschup MH, Hess B, Kretzschmar HA (1995) Neuronal cell death in scrapie-infected mice is due to apoptosis. Brain Pathol 5:213-221 1:STN:280:BymD2cfhsFU%3D
    • (1995) Brain Pathol. , vol.5 , pp. 213-221
    • Giese, A.1    Groschup, M.H.2    Hess, B.3    Kretzschmar, H.A.4
  • 57
    • 0035013510 scopus 로고    scopus 로고
    • Prion-induced neuronal damage-the mechanisms of neuronal destruction in the subacute spongiform encephalopathies
    • 1:CAS:528:DC%2BD3MXks1agt74%3D
    • Giese A, Kretzschmar HA (2001) Prion-induced neuronal damage-the mechanisms of neuronal destruction in the subacute spongiform encephalopathies. Curr Top Microbiol Immunol 253:203-217 1:CAS:528:DC%2BD3MXks1agt74%3D
    • (2001) Curr. Top. Microbiol. Immunol. , vol.253 , pp. 203-217
    • Giese, A.1    Kretzschmar, H.A.2
  • 58
    • 0034891027 scopus 로고    scopus 로고
    • Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion
    • 10.1016/S0896-6273(01)00331-2
    • Glatzel M, Heppner FL, Albers KM, Aguzzi A (2001) Sympathetic innervation of lymphoreticular organs is rate limiting for prion neuroinvasion. Neuron 31:25-34 10.1016/S0896-6273(01)00331-2
    • (2001) Neuron , vol.31 , pp. 25-34
    • Glatzel, M.1    Heppner, F.L.2    Albers, K.M.3    Aguzzi, A.4
  • 59
    • 0032489912 scopus 로고    scopus 로고
    • The sequential role of lymphotoxin and B cells in the development of splenic follicles
    • 10.1084/jem.187.7.997
    • Gonzalez M, Mackay F, Browning JL, Kosco-Vilbois MH, Noelle RJ (1998) The sequential role of lymphotoxin and B cells in the development of splenic follicles. J Exp Med 187:997-1007 10.1084/jem.187.7.997
    • (1998) J. Exp. Med. , vol.187 , pp. 997-1007
    • Gonzalez, M.1    Mackay, F.2    Browning, J.L.3    Kosco-Vilbois, M.H.4    Noelle, R.J.5
  • 61
    • 0030929562 scopus 로고    scopus 로고
    • Distribution of parvalbumin-immunoreactive neurons in brain correlates with hippocampal and temporal cortical pathology in Creutzfeldt-Jakob disease
    • 1:CAS:528:DyaK2sXmvVyrsr4%3D
    • Guentchev M, Hainfellner JA, Trabattoni GR, Budka H (1997) Distribution of parvalbumin-immunoreactive neurons in brain correlates with hippocampal and temporal cortical pathology in Creutzfeldt-Jakob disease. J Neuropathol Exp Neurol 56:1119-1124 1:CAS:528:DyaK2sXmvVyrsr4%3D
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 1119-1124
    • Guentchev, M.1    Hainfellner, J.A.2    Trabattoni, G.R.3    Budka, H.4
  • 62
    • 0031661397 scopus 로고    scopus 로고
    • Severe, early and selective loss of a subpopulation of GABAergic inhibitory neurons in experimental transmissible spongiform encephalopathies
    • 1:CAS:528:DyaK1cXmvF2ju7g%3D
    • Guentchev M, Groschup MH, Kordek R, Liberski PP, Budka H (1998) Severe, early and selective loss of a subpopulation of GABAergic inhibitory neurons in experimental transmissible spongiform encephalopathies. Brain Pathol 8:615-623 1:CAS:528:DyaK1cXmvF2ju7g%3D
    • (1998) Brain Pathol. , vol.8 , pp. 615-623
    • Guentchev, M.1    Groschup, M.H.2    Kordek, R.3    Liberski, P.P.4    Budka, H.5
  • 63
    • 0032726882 scopus 로고    scopus 로고
    • Selective neuronal vulnerability in human prion diseases. Fatal familial insomnia differs from other types of prion diseases
    • 1:STN:280:DC%2BD3c%2FhvFKgug%3D%3D
    • Guentchev M, Wanschitz J, Voigtländer T, Flicker H, Budka H (1999) Selective neuronal vulnerability in human prion diseases. Fatal familial insomnia differs from other types of prion diseases. Am J Pathol 155:1453-1457 1:STN:280:DC%2BD3c%2FhvFKgug%3D%3D
    • (1999) Am. J. Pathol. , vol.155 , pp. 1453-1457
    • Guentchev, M.1    Wanschitz, J.2    Voigtländer, T.3    Flicker, H.4    Budka, H.5
  • 66
    • 0032828301 scopus 로고    scopus 로고
    • Disease associated prion protein may deposit in the peripheral nervous system in human transmissible spongiform encephalopathies
    • 10.1007/s004010051109
    • Hainfellner JA, Budka H (1999) Disease associated prion protein may deposit in the peripheral nervous system in human transmissible spongiform encephalopathies. Acta Neuropathol 98:458-460 10.1007/ s004010051109
    • (1999) Acta Neuropathol. , vol.98 , pp. 458-460
    • Hainfellner, J.A.1    Budka, H.2
  • 67
    • 0023098327 scopus 로고
    • Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein
    • 1:CAS:528:DyaL2sXhtleqs7Y%3D
    • Hay B, Barry RA, Lieberburg I, Prusiner SB, Lingappa VR (1987) Biogenesis and transmembrane orientation of the cellular isoform of the scrapie prion protein. Mol Cell Biol 7:914-920 1:CAS:528:DyaL2sXhtleqs7Y%3D
    • (1987) Mol. Cell Biol. , vol.7 , pp. 914-920
    • Hay, B.1    Barry, R.A.2    Lieberburg, I.3    Prusiner, S.B.4    Lingappa, V.R.5
  • 68
    • 0023566948 scopus 로고
    • Evidence for a secretory form of the cellular prion protein
    • 1:CAS:528:DyaL1cXktFej
    • Hay B, Prusiner SB, Lingappa VR (1987) Evidence for a secretory form of the cellular prion protein. Biochemistry 26:8110-8115 1:CAS:528:DyaL1cXktFej
    • (1987) Biochemistry , vol.26 , pp. 8110-8115
    • Hay, B.1    Prusiner, S.B.2    Lingappa, V.R.3
  • 69
    • 1142267004 scopus 로고    scopus 로고
    • Peripheral tissue involvement in sporadic, iatrogenic, and variant Creutzfeldt-Jakob disease: An immunohistochemical, quantitative, and biochemical study
    • 1:CAS:528:DC%2BD2cXlsVCgtw%3D%3D
    • Head MW, Ritchie D, Smith N, McLoughlin V, Nailon W, Samad S, Masson S, Bishop M, McCardle L, Ironside JW (2004) Peripheral tissue involvement in sporadic, iatrogenic, and variant Creutzfeldt-Jakob disease: An immunohistochemical, quantitative, and biochemical study. Am J Pathol 164:143-153 1:CAS:528:DC%2BD2cXlsVCgtw%3D%3D
    • (2004) Am. J. Pathol. , vol.164 , pp. 143-153
    • Head, M.W.1    Ritchie, D.2    Smith, N.3    McLoughlin, V.4    Nailon, W.5    Samad, S.6    Masson, S.7    Bishop, M.8    McCardle, L.9    Ironside, J.W.10
  • 71
    • 0033576323 scopus 로고    scopus 로고
    • Transmissible and genetic prion diseases share a common pathway of neurodegeneration
    • 10.1038/45574
    • Hegde RS, Tremblay P, Groth D, DeArmond SJ, Prusiner SB, Lingappa VR (1999) Transmissible and genetic prion diseases share a common pathway of neurodegeneration. Nature 402:822-826 10.1038/45574
    • (1999) Nature , vol.402 , pp. 822-826
    • Hegde, R.S.1    Tremblay, P.2    Groth, D.3    DeArmond, S.J.4    Prusiner, S.B.5    Lingappa, V.R.6
  • 73
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • 10.1093/emboj/cdg537
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J, Soto C (2003) Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 22:5435-5445 10.1093/emboj/cdg537
    • (2003) EMBO J. , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 76
    • 0028883341 scopus 로고
    • Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein
    • 10.1006/bbrc.1995.1233
    • Hornshaw MP, McDermott JR, Candy JM (1995) Copper binding to the N-terminal tandem repeat regions of mammalian and avian prion protein. Biochem Biophys Res Commun 207:621-629 10.1006/bbrc.1995.1233
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 621-629
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3
  • 77
    • 0036135693 scopus 로고    scopus 로고
    • Migrating intestinal dendritic cells transport PrP(Sc) from the gut
    • 1:CAS:528:DC%2BD38Xlt1Gkug%3D%3D
    • Huang FP, Farquhar CF, Mabbott NA, Bruce ME, MacPherson GG (2002) Migrating intestinal dendritic cells transport PrP(Sc) from the gut. J Gen Virol 83:267-271 1:CAS:528:DC%2BD38Xlt1Gkug%3D%3D
    • (2002) J. Gen. Virol. , vol.83 , pp. 267-271
    • Huang, F.P.1    Farquhar, C.F.2    Mabbott, N.A.3    Bruce, M.E.4    MacPherson, G.G.5
  • 78
    • 0021543112 scopus 로고
    • The presence of complements in amyloid plaques of Creutzfeldt-Jakob disease and Gerstmann-Straussler-Scheinker disease
    • 1:STN:280:BiiD3c%2FivVE%3D
    • Ishii T, Haga S, Yagishita S, Tateishi J (1984) The presence of complements in amyloid plaques of Creutzfeldt-Jakob disease and Gerstmann-Straussler-Scheinker disease. Appl Pathol 2:370-379 1:STN:280:BiiD3c%2FivVE%3D
    • (1984) Appl. Pathol. , vol.2 , pp. 370-379
    • Ishii, T.1    Haga, S.2    Yagishita, S.3    Tateishi, J.4
  • 79
    • 0033947543 scopus 로고    scopus 로고
    • Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy
    • 10.1002/1096-9896(200007)191:3<323::AID-PATH629>3.3.CO;2-Q
    • Jeffrey M, McGovern G, Goodsir CM, Brown KL, Bruce ME (2000) Sites of prion protein accumulation in scrapie-infected mouse spleen revealed by immuno-electron microscopy. J Pathol 191:323-332 10.1002/ 1096-9896(200007)191:3<323::AID-PATH629>3.3.CO;2-Q
    • (2000) J. Pathol. , vol.191 , pp. 323-332
    • Jeffrey, M.1    McGovern, G.2    Goodsir, C.M.3    Brown, K.L.4    Bruce, M.E.5
  • 80
    • 2542638001 scopus 로고    scopus 로고
    • Scrapie-specific neuronal lesions are independent of neuronal PrP expression
    • 10.1002/ana.20093
    • Jeffrey M, Goodsir CM, Race RE, Chesebro B (2004) Scrapie-specific neuronal lesions are independent of neuronal PrP expression. Ann Neurol 55:781-792 10.1002/ana.20093
    • (2004) Ann. Neurol. , vol.55 , pp. 781-792
    • Jeffrey, M.1    Goodsir, C.M.2    Race, R.E.3    Chesebro, B.4
  • 81
    • 0026069894 scopus 로고
    • Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity
    • 1:CAS:528:DyaK3MXmslKrsbs%3D
    • Jendroska K, Heinzel FP, Torchia M, Stowring L, Kretzschmar HA, Kon A, Stern A, Prusiner SB, DeArmond SJ (1991) Proteinase-resistant prion protein accumulation in Syrian hamster brain correlates with regional pathology and scrapie infectivity. Neurology 41:1482-1490 1:CAS:528:DyaK3MXmslKrsbs%3D
    • (1991) Neurology , vol.41 , pp. 1482-1490
    • Jendroska, K.1    Heinzel, F.P.2    Torchia, M.3    Stowring, L.4    Kretzschmar, H.A.5    Kon, A.6    Stern, A.7    Prusiner, S.B.8    DeArmond, S.J.9
  • 82
    • 0038946003 scopus 로고    scopus 로고
    • Conversion by Peyer's patch lymphocytes of human enterocytes into M cells that transport bacteria
    • 10.1126/science.277.5328.949
    • Kerneis S, Bogdanova A, Kraehenbuhl JP, Pringault E (1997) Conversion by Peyer's patch lymphocytes of human enterocytes into M cells that transport bacteria. Science 277:949-952 10.1126/science.277.5328.949
    • (1997) Science , vol.277 , pp. 949-952
    • Kerneis, S.1    Bogdanova, A.2    Kraehenbuhl, J.P.3    Pringault, E.4
  • 83
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • 1:STN:280:CSyD3crgslU%3D
    • Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239-257 1:STN:280:CSyD3crgslU%3D
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 84
    • 0021088568 scopus 로고
    • Pathogenesis of mouse scrapie. Evidence for direct neural spread of infection to the CNS after injection of sciatic nerve
    • 10.1016/0022-510X(83)90165-X
    • Kimberlin RH, Hall SM, Walker CA (1983) Pathogenesis of mouse scrapie. Evidence for direct neural spread of infection to the CNS after injection of sciatic nerve. J Neurol Sci 61:315-325 10.1016/ 0022-510X(83)90165-X
    • (1983) J. Neurol. Sci. , vol.61 , pp. 315-325
    • Kimberlin, R.H.1    Hall, S.M.2    Walker, C.A.3
  • 85
    • 0025983158 scopus 로고
    • Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt-Jakob disease
    • 1:CAS:528:DyaK3MXmsFeisLY%3D
    • Kitamoto T, Muramoto T, Mohri S, Doh-Ura K, Tateishi J (1991) Abnormal isoform of prion protein accumulates in follicular dendritic cells in mice with Creutzfeldt-Jakob disease. J Virol 65:6292-6295 1:CAS:528:DyaK3MXmsFeisLY%3D
    • (1991) J. Virol. , vol.65 , pp. 6292-6295
    • Kitamoto, T.1    Muramoto, T.2    Mohri, S.3    Doh-Ura, K.4    Tateishi, J.5
  • 90
    • 0032731551 scopus 로고    scopus 로고
    • Deposition of the prion protein (PrP) during the evolution of experimental Creutzfeldt-Jakob disease
    • 10.1007/s004010051124
    • Kordek R, Hainfellner JA, Liberski PP, Budka H (1999) Deposition of the prion protein (PrP) during the evolution of experimental Creutzfeldt-Jakob disease. Acta Neuropathol 98:597-602 10.1007/ s004010051124
    • (1999) Acta Neuropathol. , vol.98 , pp. 597-602
    • Kordek, R.1    Hainfellner, J.A.2    Liberski, P.P.3    Budka, H.4
  • 91
    • 0036934561 scopus 로고    scopus 로고
    • Distribution of intraneuronal immunoreactivity for the prion protein in human prion diseases
    • 1:CAS:528:DC%2BD38Xls12ntr8%3D
    • Kovacs GG, Voigtländer T, Hainfellner JA, Budka H (2002) Distribution of intraneuronal immunoreactivity for the prion protein in human prion diseases. Acta Neuropathol 104:320-326 1:CAS:528:DC%2BD38Xls12ntr8%3D
    • (2002) Acta Neuropathol. , vol.104 , pp. 320-326
    • Kovacs, G.G.1    Voigtländer, T.2    Hainfellner, J.A.3    Budka, H.4
  • 94
    • 11144231706 scopus 로고    scopus 로고
    • Subcellular localization of disease associated prion protein in the human brain
    • (in press)
    • Kovacs GG, Preusser M, Strohschneider M, Budka H (2004) Subcellular localization of disease associated prion protein in the human brain. Am J Pathol (in press)
    • (2004) Am. J. Pathol.
    • Kovacs, G.G.1    Preusser, M.2    Strohschneider, M.3    Budka, H.4
  • 96
    • 0036759121 scopus 로고    scopus 로고
    • Unhampered prion neuroinvasion despite impaired fast axonal transport in transgenic mice overexpressing four-repeat tau
    • Kunzi V, Glatzel M, Nakano MY, Greber UF, Van Leuven F, Aguzzi A (2002) Unhampered prion neuroinvasion despite impaired fast axonal transport in transgenic mice overexpressing four-repeat tau. J Neurosci 22:7471-7477
    • (2002) J. Neurosci. , vol.22 , pp. 7471-7477
    • Kunzi, V.1    Glatzel, M.2    Nakano, M.Y.3    Greber, U.F.4    Van Leuven, F.5    Aguzzi, A.6
  • 97
    • 0032772928 scopus 로고    scopus 로고
    • Alteration of free radical metabolism in the brain of mice infected with scrapie agent
    • 1:CAS:528:DyaK1MXktFWltLo%3D
    • Lee DW, Sohn HO, Lim HB, Lee YG, Kim YS, Carp RI, Wisniewski HM (1999) Alteration of free radical metabolism in the brain of mice infected with scrapie agent. Free Radic Res 30:499-507 1:CAS:528:DyaK1MXktFWltLo%3D
    • (1999) Free Radic. Res. , vol.30 , pp. 499-507
    • Lee, D.W.1    Sohn, H.O.2    Lim, H.B.3    Lee, Y.G.4    Kim, Y.S.5    Carp, R.I.6    Wisniewski, H.M.7
  • 99
    • 4344656906 scopus 로고    scopus 로고
    • Neuronal cell death in transmissible spongiform encephalopathies (prion diseases) revisited: From apoptosis to autophagy
    • 10.1016/j.biocel.2004.04.016
    • Liberski PP, Sikorska B, Bratosiewicz-Wasik J, Gajdusek DC, Brown P (2004) Neuronal cell death in transmissible spongiform encephalopathies (prion diseases) revisited: From apoptosis to autophagy. Int J Biochem Cell Biol 36:2473-2490 10.1016/j.biocel.2004.04.016
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2473-2490
    • Liberski, P.P.1    Sikorska, B.2    Bratosiewicz-Wasik, J.3    Gajdusek, D.C.4    Brown, P.5
  • 100
    • 0034099095 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha-deficient, but not interleukin-6-deficient, mice resist peripheral infection with scrapie
    • 10.1128/JVI.74.7.3338-3344.2000
    • Mabbott NA, Williams A, Farquhar CF, Pasparakis M, Kollias G, Bruce ME (2000) Tumor necrosis factor alpha-deficient, but not interleukin-6-deficient, mice resist peripheral infection with scrapie. J Virol 74:3338-3344 10.1128/JVI.74.7.3338-3344.2000
    • (2000) J. Virol. , vol.74 , pp. 3338-3344
    • Mabbott, N.A.1    Williams, A.2    Farquhar, C.F.3    Pasparakis, M.4    Kollias, G.5    Bruce, M.E.6
  • 101
    • 0035053039 scopus 로고    scopus 로고
    • Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie
    • Mabbott NA, Bruce ME, Botto M, Walport MJ, Pepys MB (2001) Temporary depletion of complement component C3 or genetic deficiency of C1q significantly delays onset of scrapie. Nat Med 7:485-487
    • (2001) Nat. Med. , vol.7 , pp. 485-487
    • Mabbott, N.A.1    Bruce, M.E.2    Botto, M.3    Walport, M.J.4    Pepys, M.B.5
  • 102
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • 10.1093/emboj/21.3.202
    • Mallucci GR, Ratté S, Asante EA, Linehan J, Gowland I, Jefferys JGR, Collinge J (2002) Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J 21:202-210 10.1093/emboj/21.3.202
    • (2002) EMBO J. , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratté, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5    Jefferys, J.G.R.6    Collinge, J.7
  • 103
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • 10.1126/science.1090187
    • Mallucci G, Dickinson A, Linehan J, Klöhn PC, Brandner S, Collinge J (2003) Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 302:871-874 10.1126/science.1090187
    • (2003) Science , vol.302 , pp. 871-874
    • Mallucci, G.1    Dickinson, A.2    Linehan, J.3    Klöhn, P.C.4    Brandner, S.5    Collinge, J.6
  • 104
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • 1:CAS:528:DyaK2cXmt1Olu74%3D
    • Manson JC, Clarke AR, Hooper ML, Aitchison L, McConnell I, Hope J (1994) 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Mol Neurobiol 8:121-127 1:CAS:528:DyaK2cXmt1Olu74%3D
    • (1994) Mol. Neurobiol. , vol.8 , pp. 121-127
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3    Aitchison, L.4    McConnell, I.5    Hope, J.6
  • 105
    • 0028703452 scopus 로고
    • PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology
    • 1:STN:280:ByqC2cvlsFM%3D
    • Manson JC, Clarke AR, McBride PA, McConnell I, Hope J (1994) PrP gene dosage determines the timing but not the final intensity or distribution of lesions in scrapie pathology. Neurodegeneration 3:331-340 1:STN:280:ByqC2cvlsFM%3D
    • (1994) Neurodegeneration , vol.3 , pp. 331-340
    • Manson, J.C.1    Clarke, A.R.2    McBride, P.A.3    McConnell, I.4    Hope, J.5
  • 106
    • 2642623590 scopus 로고    scopus 로고
    • Distinct roles of lymphotoxin alpha and the type I tumor necrosis factor (TNF) receptor in the establishment of follicular dendritic cells from non-bone marrow-derived cells
    • 10.1084/jem.186.12.1997
    • Matsumoto M, Fu YX, Molina H, Huang G, Kim J, Thomas DA, Nahm MH, Chaplin DD (1997) Distinct roles of lymphotoxin alpha and the type I tumor necrosis factor (TNF) receptor in the establishment of follicular dendritic cells from non-bone marrow-derived cells. J Exp Med 186:1997-2004 10.1084/jem.186.12.1997
    • (1997) J. Exp. Med. , vol.186 , pp. 1997-2004
    • Matsumoto, M.1    Fu, Y.X.2    Molina, H.3    Huang, G.4    Kim, J.5    Thomas, D.A.6    Nahm, M.H.7    Chaplin, D.D.8
  • 107
    • 0033574604 scopus 로고    scopus 로고
    • Pathological PrP is abundant in sympathetic and sensory ganglia of hamsters fed with scrapie
    • McBride PA, Beekes M (1999) Pathological PrP is abundant in sympathetic and sensory ganglia of hamsters fed with scrapie. Neurosci Lett 265:135-138
    • (1999) Neurosci. Lett. , vol.265 , pp. 135-138
    • McBride, P.A.1    Beekes, M.2
  • 108
    • 0035910498 scopus 로고    scopus 로고
    • Cleavage of the amino terminus of the prion protein by reactive oxygen species
    • 10.1074/jbc.M007243200
    • McMahon HEM, Mangé A, Nishida N, Créminon C, Casanova D, Lehmann S (2001) Cleavage of the amino terminus of the prion protein by reactive oxygen species. J Biol Chem 276:2286-2291 10.1074/jbc.M007243200
    • (2001) J. Biol. Chem. , vol.276 , pp. 2286-2291
    • McMahon, H.E.M.1    Mangé, A.2    Nishida, N.3    Créminon, C.4    Casanova, D.5    Lehmann, S.6
  • 109
    • 0023095066 scopus 로고
    • Lack of effect of thymus and spleen on the incubation period of Creutzfeldt-Jakob disease in mice
    • 3553423
    • Mohri S, Handa S, Tateishi J (1987) Lack of effect of thymus and spleen on the incubation period of Creutzfeldt-Jakob disease in mice. J Gen Virol 68:1187-1189 3553423
    • (1987) J. Gen. Virol. , vol.68 , pp. 1187-1189
    • Mohri, S.1    Handa, S.2    Tateishi, J.3
  • 110
    • 0034686002 scopus 로고    scopus 로고
    • Impaired prion replication in spleens of mice lacking functional follicular dendritic cells
    • 10.1126/science.288.5469.1257
    • Montrasio F, Frigg R, Glatzel M, Klein MA, Mackay F, Aguzzi A, Weissmann C (2000) Impaired prion replication in spleens of mice lacking functional follicular dendritic cells. Science 288:1257-1259 10.1126/ science.288.5469.1257
    • (2000) Science , vol.288 , pp. 1257-1259
    • Montrasio, F.1    Frigg, R.2    Glatzel, M.3    Klein, M.A.4    Mackay, F.5    Aguzzi, A.6    Weissmann, C.7
  • 112
    • 0035941307 scopus 로고    scopus 로고
    • Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells
    • 10.1074/jbc.M103894200
    • O'Donovan CN, Tobin D, Cotter TG (2001) Prion protein fragment PrP-(106-126) induces apoptosis via mitochondrial disruption in human neuronal SH-SY5Y cells. J Biol Chem 276:43516-43523 10.1074/ jbc.M103894200
    • (2001) J. Biol. Chem. , vol.276 , pp. 43516-43523
    • O'Donovan, C.N.1    Tobin, D.2    Cotter, T.G.3
  • 113
    • 0026732669 scopus 로고
    • Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species
    • 1:CAS:528:DyaK38XltVOjt7s%3D
    • Ookawara T, Kawamura N, Kitagawa Y, Taniguchi N (1992) Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J Biol Chem 267:18505-18510 1:CAS:528:DyaK38XltVOjt7s%3D
    • (1992) J. Biol. Chem. , vol.267 , pp. 18505-18510
    • Ookawara, T.1    Kawamura, N.2    Kitagawa, Y.3    Taniguchi, N.4
  • 115
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • 10.1074/jbc.273.50.33107
    • Pauly PC, Harris DA (1998) Copper stimulates endocytosis of the prion protein. J Biol Chem 273:33107-33110 10.1074/jbc.273.50.33107
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 116
    • 0036267207 scopus 로고    scopus 로고
    • A typical inflammation in the central nervous system in prion disease
    • 10.1097/00019052-200206000-00020
    • Perry VH, Cunningham C, Boche D (2002) Atypical inflammation in the central nervous system in prion disease. Curr Opin Neurol 15:349-354 10.1097/00019052-200206000-00020
    • (2002) Curr. Opin. Neurol. , vol.15 , pp. 349-354
    • Perry, V.H.1    Cunningham, C.2    Boche, D.3
  • 119
    • 0037377727 scopus 로고    scopus 로고
    • Oral prion infection requires normal numbers of Peyer's patches but not of enteric lymphocytes
    • 1:CAS:528:DC%2BD3sXjtVemt7c%3D
    • Prinz M, Huber G, Macpherson AJ, Heppner FL, Glatzel M, Eugster HP, Wagner N, Aguzzi A (2003) Oral prion infection requires normal numbers of Peyer's patches but not of enteric lymphocytes. Am J Pathol 162:1103-1111 1:CAS:528:DC%2BD3sXjtVemt7c%3D
    • (2003) Am. J. Pathol. , vol.162 , pp. 1103-1111
    • Prinz, M.1    Huber, G.2    Macpherson, A.J.3    Heppner, F.L.4    Glatzel, M.5    Eugster, H.P.6    Wagner, N.7    Aguzzi, A.8
  • 121
    • 0032506187 scopus 로고    scopus 로고
    • Prions
    • 10.1073/pnas.95.23.13363
    • Prusiner SB (1998) Prions. Proc Natl Acad Sci USA 95:13363-13383 10.1073/pnas.95.23.13363
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13363-13383
    • Prusiner, S.B.1
  • 122
    • 0034705438 scopus 로고    scopus 로고
    • Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation
    • 10.1074/jbc.275.25.19121
    • Qin K, Yang DS, Yang Y, Chishti MA, Meng LJ, Kretzschmar HA, Yip CM, Fraser PE, Westaway D (2000) Copper(II)-induced conformational changes and protease resistance in recombinant and cellular PrP. Effect of protein age and deamidation. J Biol Chem 275:19121-19131 10.1074/ jbc.275.25.19121
    • (2000) J. Biol. Chem. , vol.275 , pp. 19121-19131
    • Qin, K.1    Yang, D.S.2    Yang, Y.3    Chishti, M.A.4    Meng, L.J.5    Kretzschmar, H.A.6    Yip, C.M.7    Fraser, P.E.8    Westaway, D.9
  • 123
    • 0035815738 scopus 로고    scopus 로고
    • Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform
    • 10.1074/jbc.M009666200
    • Quaglio E, Chiesa R, Harris DA (2001) Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform. J Biol Chem 276:11432-11438 10.1074/jbc.M009666200
    • (2001) J. Biol. Chem. , vol.276 , pp. 11432-11438
    • Quaglio, E.1    Chiesa, R.2    Harris, D.A.3
  • 124
    • 0028876414 scopus 로고
    • Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent
    • 10.1016/0896-6273(95)90105-1
    • Race RE, Priola SA, Bessen RA, Ernst D, Dockter J, Rall GF, Mucke L, Chesebro B, Oldstone MB (1995) Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron 15:1183-1191 10.1016/0896-6273(95)90105-1
    • (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
  • 125
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • 10.1074/jbc.M211830200
    • Rachidi W, Vilette D, Guiraud P, Arlotto M, Riondel J, Laude H, Lehmann S, Favier A (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J Biol Chem 278:9064-9072 10.1074/jbc.M211830200
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1    Vilette, D.2    Guiraud, P.3    Arlotto, M.4    Riondel, J.5    Laude, H.6    Lehmann, S.7    Favier, A.8
  • 127
    • 0031443822 scopus 로고    scopus 로고
    • Apoptosis and necrosis in toxicology: A continuum or distinct modes of cell death?
    • 10.1016/S0163-7258(97)00037-5
    • Raffray M, Cohen GM (1997) Apoptosis and necrosis in toxicology: A continuum or distinct modes of cell death? Pharmacol Ther 75:153-177 10.1016/S0163-7258(97)00037-5
    • (1997) Pharmacol. Ther. , vol.75 , pp. 153-177
    • Raffray, M.1    Cohen, G.M.2
  • 128
    • 0035865398 scopus 로고    scopus 로고
    • Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain
    • 1:CAS:528:DC%2BD3MXhsVyhtrk%3D
    • Rossi D, Cozzio A, Flechsig E, Klein MA, Rülicke T, Aguzzi A, Weissmann C (2001) Onset of ataxia and Purkinje cell loss in PrP null mice inversely correlated with Dpl level in brain. EMBO J 20:694-702 1:CAS:528:DC%2BD3MXhsVyhtrk%3D
    • (2001) EMBO J. , vol.20 , pp. 694-702
    • Rossi, D.1    Cozzio, A.2    Flechsig, E.3    Klein, M.A.4    Rülicke, T.5    Aguzzi, A.6    Weissmann, C.7
  • 130
    • 0027257501 scopus 로고
    • Immunohistochemical study of microglia in the Creutzfeldt-Jakob diseased brain
    • 10.1007/BF00369445
    • Sasaki A, Hirato J, Nakazato Y (1993) Immunohistochemical study of microglia in the Creutzfeldt-Jakob diseased brain. Acta Neuropathol 86:337-344 10.1007/BF00369445
    • (1993) Acta Neuropathol. , vol.86 , pp. 337-344
    • Sasaki, A.1    Hirato, J.2    Nakazato, Y.3
  • 131
    • 0033985183 scopus 로고    scopus 로고
    • Apoptosis and the nervous system
    • Sastry PS, Rao KS (2000) Apoptosis and the nervous system. J Neurochem 74:1-20
    • (2000) J. Neurochem. , vol.74 , pp. 1-20
    • Sastry, P.S.1    Rao, K.S.2
  • 133
    • 4344656905 scopus 로고    scopus 로고
    • Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: A brain biopsy study
    • 10.1016/j.biocel.2004.04.014
    • Sikorska B, Liberski PP, Giraud P, Kopp N, Brown P (2004) Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: a brain biopsy study. Int J Biochem Cell Biol 36:2563-2573 10.1016/ j.biocel.2004.04.014
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2563-2573
    • Sikorska, B.1    Liberski, P.P.2    Giraud, P.3    Kopp, N.4    Brown, P.5
  • 134
    • 0029888496 scopus 로고    scopus 로고
    • Oxidative stress in neurodegenerative diseases
    • 10.1146/annurev.pa.36.040196.000503
    • Simonian NA, Coyle JT (1996) Oxidative stress in neurodegenerative diseases. Annu Rev Pharmacol Toxicol 36:83-106 10.1146/ annurev.pa.36.040196.000503
    • (1996) Annu. Rev. Pharmacol. Toxicol. , vol.36 , pp. 83-106
    • Simonian, N.A.1    Coyle, J.T.2
  • 135
    • 0035910518 scopus 로고    scopus 로고
    • Most pathogenic mutations do not alter the membrane topology of the prion protein
    • 10.1074/jbc.M006763200
    • Stewart RS, Harris DA (2001) Most pathogenic mutations do not alter the membrane topology of the prion protein. J Biol Chem 276:2212-2220 10.1074/jbc.M006763200
    • (2001) J. Biol. Chem. , vol.276 , pp. 2212-2220
    • Stewart, R.S.1    Harris, D.A.2
  • 136
    • 0242412541 scopus 로고    scopus 로고
    • Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection
    • 10.1074/jbc.M307833200
    • Stewart RS, Harris DA (2003) Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J Biol Chem 278:45960-45968 10.1074/jbc.M307833200
    • (2003) J. Biol. Chem. , vol.278 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 137
    • 0035158658 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic reticulum
    • 1:CAS:528:DC%2BD3MXjtVaqsLo%3D
    • Stewart RS, Drisaldi B, Harris DA (2001) A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic reticulum. Mol Biol Cell 12:881-889 1:CAS:528:DC%2BD3MXjtVaqsLo%3D
    • (2001) Mol. Biol. Cell , vol.12 , pp. 88-89
    • Stewart, R.S.1    Drisaldi, B.2    Harris, D.A.3
  • 138
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • 10.1042/0264-6021:3620253
    • Thackray AM, Knight R, Haswell SJ, Bujdoso R, Brown DR (2002) Metal imbalance and compromised antioxidant function are early changes in prion disease. Biochem J 362:253-258 10.1042/0264-6021:3620253
    • (2002) Biochem. J. , vol.362 , pp. 253-258
    • Thackray, A.M.1    Knight, R.2    Haswell, S.J.3    Bujdoso, R.4    Brown, D.R.5
  • 140
    • 0037461576 scopus 로고    scopus 로고
    • Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126
    • Turnbull S, Tabner BJ, Brown DR, Allsop D (2003) Copper-dependent generation of hydrogen peroxide from the toxic prion protein fragment PrP106-126. Neurosci Lett 336:159-162
    • (2003) Neurosci. Lett. , vol.336 , pp. 159-162
    • Turnbull, S.1    Tabner, B.J.2    Brown, D.R.3    Allsop, D.4
  • 143
    • 0024834589 scopus 로고
    • Non-enzymic activation of the fifth component of human complement, by oxygen radicals. Some properties of the activation product, C5b-like C5
    • Vogt W, Damerau B, Zabern I von, Nolte R, Brunahl D (1989) Non-enzymic activation of the fifth component of human complement, by oxygen radicals. Some properties of the activation product, C5b-like C5. Mol Immunol 26:1133-1142
    • (1989) Mol. Immunol. , vol.26 , pp. 1133-1142
    • Vogt, W.1    Damerau, B.2    von Zabern, I.3    Nolte, R.4    Brunahl, D.5
  • 146
    • 0032724766 scopus 로고    scopus 로고
    • Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity
    • 1:CAS:528:DyaK1MXnvVKisb4%3D
    • White AR, Collins SJ, Maher F, Jobling MF, Stewart LR, Thyer JM, Beyreuther K, Masters CL, Cappai R (1999) Prion protein-deficient neurons reveal lower glutathione reductase activity and increased susceptibility to hydrogen peroxide toxicity. Am J Pathol 155:1723-1730 1:CAS:528:DyaK1MXnvVKisb4%3D
    • (1999) Am. J. Pathol. , vol.155 , pp. 1723-1730
    • White, A.R.1    Collins, S.J.2    Maher, F.3    Jobling, M.F.4    Stewart, L.R.5    Thyer, J.M.6    Beyreuther, K.7    Masters, C.L.8    Cappai, R.9
  • 147
    • 0035029801 scopus 로고    scopus 로고
    • Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons
    • 10.1006/nbdi.2001.0386
    • White AR, Guirguis R, Brazier MW, Jobling MF, Hill AF, Beyreuther K, Barrow CJ, Masters CL, Collins SJ, Cappai R (2001) Sublethal concentrations of prion peptide PrP106-126 or the amyloid beta peptide of Alzheimer's disease activates expression of proapoptotic markers in primary cortical neurons. Neurobiol Dis 8:299-316 10.1006/nbdi.2001.0386
    • (2001) Neurobiol. Dis. , vol.8 , pp. 299-316
    • White, A.R.1    Guirguis, R.2    Brazier, M.W.3    Jobling, M.F.4    Hill, A.F.5    Beyreuther, K.6    Barrow, C.J.7    Masters, C.L.8    Collins, S.J.9    Cappai, R.10
  • 148
  • 149
    • 0031127379 scopus 로고    scopus 로고
    • PrP deposition, microglial activation, and neuronal apoptosis in murine scrapie
    • 10.1006/exnr.1997.6424
    • Williams A, Lucassen PJ, Ritchie D, Bruce M (1997) PrP deposition, microglial activation, and neuronal apoptosis in murine scrapie. Exp Neurol 144:433-438 10.1006/exnr.1997.6424
    • (1997) Exp. Neurol. , vol.144 , pp. 433-438
    • Williams, A.1    Lucassen, P.J.2    Ritchie, D.3    Bruce, M.4
  • 150
    • 0030937917 scopus 로고    scopus 로고
    • 2 and lipocortin-1 in the CNS during the incubation period of murine scrapie correlates with progressive PrP accumulations
    • 10.1016/S0006-8993(97)00067-X
    • 2 and lipocortin-1 in the CNS during the incubation period of murine scrapie correlates with progressive PrP accumulations. Brain Res 754:171-180 10.1016/S0006-8993(97)00067-X
    • (1997) Brain Res. , vol.754 , pp. 171-180
    • Williams, A.1    Van Dam, A.M.2    Ritchie, D.3    Eikelenboom, P.4    Fraser, H.5
  • 151
    • 0034764599 scopus 로고    scopus 로고
    • Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities
    • 10.1046/j.1471-4159.2001.00625.x
    • Wong BS, Brown DR, Pan T, Whiteman M, Liu T, Bu X, Li R, Gambetti P, Olesik J, Rubenstein R, Sy MS (2001) Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities. J Neurochem 79:689-698 10.1046/ j.1471-4159.2001.00625.x
    • (2001) J. Neurochem. , vol.79 , pp. 689-698
    • Wong, B.S.1    Brown, D.R.2    Pan, T.3    Whiteman, M.4    Liu, T.5    Bu, X.6    Li, R.7    Gambetti, P.8    Olesik, J.9    Rubenstein, R.10    Sy, M.S.11
  • 153
    • 0027419446 scopus 로고
    • Delayed internucleosomal DNA fragmentation in programmed cell death
    • 1:CAS:528:DyaK3sXitlWisbo%3D
    • Zakeri ZF, Quaglino D, Latham T, Lockshin RA (1993) Delayed internucleosomal DNA fragmentation in programmed cell death. FASEB J 7:470-478 1:CAS:528:DyaK3sXitlWisbo%3D
    • (1993) FASEB J. , vol.7 , pp. 470-478
    • Zakeri, Z.F.1    Quaglino, D.2    Latham, T.3    Lockshin, R.A.4


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