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Volumn 45, Issue 6, 2013, Pages 435-441

Prion protein: Structural features and related toxicity

Author keywords

Amyloid; Oligomer; Prion protein; Toxicity

Indexed keywords

AMYLOID; BIOPOLYMER; OLIGOMER; PRION PROTEIN;

EID: 84879210441     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmt035     Document Type: Review
Times cited : (7)

References (89)
  • 1
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S. Novel proteinaceous infectious particles cause scrapie. Science 1982, 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.1
  • 2
    • 0141849876 scopus 로고    scopus 로고
    • Introduction to the transmissible spongiform encephalopathies or prion diseases
    • Chesebro B. Introduction to the transmissible spongiform encephalopathies or prion diseases. Br Med Bull 2003, 66: 1-20.
    • (2003) Br Med Bull , vol.66 , pp. 1-20
    • Chesebro, B.1
  • 5
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • Ma J and Lindquist S. Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 2002, 298: 1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 6
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D and Mehlhorn I, et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993, 90: 10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5    Groth, D.6    Mehlhorn, I.7
  • 7
    • 0023903906 scopus 로고
    • Western Blot Detection of scrapie-associated fibril protein in tissues outside the central nervous system from preclinical scrapie-infected mice
    • Satoshi D, Masako I, Morikazu S, Gihei S, Isomura H and Goto H. Western Blot Detection of scrapie-associated fibril protein in tissues outside the central nervous system from preclinical scrapie-infected mice. J Gen Virol 1988, 69: 955-960.
    • (1988) J Gen Virol , vol.69 , pp. 955-960
    • Satoshi, D.1    Masako, I.2    Morikazu, S.3    Gihei, S.4    Isomura, H.5    Goto, H.6
  • 8
    • 0034916581 scopus 로고    scopus 로고
    • Prion disease of humans and animals: Their causes and molecular basis
    • Collinge J. Prion disease of humans and animals: their causes and molecular basis. Annu Rev Neurosci 2001, 24: 519-550.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 13
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci G, Dickinson A, Linehan J, Klöhn P, Brandner S and Collinge J. Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis. Science 2003, 302: 871-874.
    • (2003) Science , vol.302 , pp. 871-874
    • Mallucci, G.1    Dickinson, A.2    Linehan, J.3    Klöhn, P.4    Brandner, S.5    Collinge, J.6
  • 16
    • 84866183670 scopus 로고    scopus 로고
    • Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C)
    • Kim C, Haldiman T, Surewicz K, Cohen Y, Chen W, Blevins J and Sy M-S, et al. Small protease sensitive oligomers of PrPSc in distinct human prions determine conversion rate of PrP(C). PLoS Pathog 2012, 8: e1002835.
    • (2012) PLoS Pathog , vol.8
    • Kim, C.1    Haldiman, T.2    Surewicz, K.3    Cohen, Y.4    Chen, W.5    Blevins, J.6    Sy, M.-S.7
  • 17
    • 79959351077 scopus 로고    scopus 로고
    • Amyloid-b annular protofibrils evade fibrillar fate in Alzheimer disease brain
    • Lasagna-Reeves CA, Glabe CG and Kayed R. Amyloid-b annular protofibrils evade fibrillar fate in Alzheimer disease brain. J Biol Chem 2011, 286: 22122-22130.
    • (2011) J Biol Chem , vol.286 , pp. 22122-22130
    • Lasagna-Reeves, C.A.1    Glabe, C.G.2    Kayed, R.3
  • 18
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani M and Dobson CM. Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J Mol Med 2003, 81: 678-699.
    • (2003) J Mol Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 21
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl N, Borchelt D, Hsiao K and Prusiner S. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 1987, 51: 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.2    Hsiao, K.3    Prusiner, S.4
  • 22
    • 0033573083 scopus 로고    scopus 로고
    • Functionally different GPI proteins are organized in different domains on the neuronal surface
    • Madore N, Smith KL, Graham CH, Jen A, Brady K, Hall S and Morris R. Functionally different GPI proteins are organized in different domains on the neuronal surface. EMBO J 1999, 18: 6917-6926.
    • (1999) EMBO J , vol.18 , pp. 6917-6926
    • Madore, N.1    Smith, K.L.2    Graham, C.H.3    Jen, A.4    Brady, K.5    Hall, S.6    Morris, R.7
  • 24
    • 65949115708 scopus 로고    scopus 로고
    • Málaga-Trillo E, Solis GP, Schrock Y, Geiss C, Luncz L, Thomanetz V and Stuermer CAO
    • Málaga-Trillo E, Solis GP, Schrock Y, Geiss C, Luncz L, Thomanetz V and Stuermer CAO. Regulation of embryonic cell adhesion by the prion protein. PLoS Biol 2009, 7: e1000055.
    • (2009) Regulation of Embryonic Cell Adhesion by the Prion Protein. PLoS Biol , vol.7
  • 25
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl N, Baldwin M, Teplow D, Hood L, Gibson B, Burlingame A and Prusiner S. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 1993, 32: 1991-2002.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.2    Teplow, D.3    Hood, L.4    Gibson, B.5    Burlingame, A.6    Prusiner, S.7
  • 28
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • McKinley M, Meyer R, Kenaga L, Rahbar F, Cotter R, Serban A and Prusiner S. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 1991, 65: 1340-1351.
    • (1991) J Virol , vol.65 , pp. 1340-1351
    • McKinley, M.1    Meyer, R.2    Kenaga, L.3    Rahbar, F.4    Cotter, R.5    Serban, A.6    Prusiner, S.7
  • 30
    • 0034079165 scopus 로고    scopus 로고
    • Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathy
    • Bartz JC, Bessen RA, McKenzie D, Marsh RF and Aiken JM. Adaptation and selection of prion protein strain conformations following interspecies transmission of transmissible mink encephalopathy. J Virol 2000, 74: 5542-5547.
    • (2000) J Virol , vol.74 , pp. 5542-5547
    • Bartz, J.C.1    Bessen, R.A.2    McKenzie, D.3    Marsh, R.F.4    Aiken, J.M.5
  • 32
    • 4544282941 scopus 로고    scopus 로고
    • Variable patterns of distribution of PrP CWD in the obex and cranial lympoid tissues of rock mountain elk (Cervus elaphus nelsoni) with subclinical chronic wasting disease
    • Spraker TR, Balachandran A, Zhuang D and O'Rourke KI. Variable patterns of distribution of PrP CWD in the obex and cranial lympoid tissues of rock mountain elk (Cervus elaphus nelsoni) with subclinical chronic wasting disease. Vet Rec 2004, 155: 295-302.
    • (2004) Vet Rec , vol.155 , pp. 295-302
    • Spraker, T.R.1    Balachandran, A.2    Zhuang, D.3    O'Rourke, K.I.4
  • 33
    • 0344021409 scopus 로고    scopus 로고
    • Prions and the immune system: A journey through gut, spleen, and nerves
    • Aguzzi A. Prions and the immune system: a journey through gut, spleen, and nerves. Adv Immunol 2003, 81: 123-171.
    • (2003) Adv Immunol , vol.81 , pp. 123-171
    • Aguzzi, A.1
  • 34
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith J. Self-replication and scrapie. Nature 1967, 215: 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.1
  • 35
    • 34249993165 scopus 로고    scopus 로고
    • The prion strain phenomenon: Molecular basis and unprecedented features
    • Morales R, Abid K and Soto C. The prion strain phenomenon: Molecular basis and unprecedented features. Biochim Biophys Acta 2007, 1772: 681-691.
    • (2007) Biochim Biophys Acta , vol.1772 , pp. 681-691
    • Morales, R.1    Abid, K.2    Soto, C.3
  • 36
    • 84961034678 scopus 로고
    • Scrapie produced experimentally in goats with special reference to the clinical syndrome
    • Pattison IH and Millson GC. Scrapie produced experimentally in goats with special reference to the clinical syndrome. J Comp Pathol 1961, 71: 101-109.
    • (1961) J Comp Pathol , vol.71 , pp. 101-109
    • Pattison, I.H.1    Millson, G.C.2
  • 37
    • 0027740178 scopus 로고
    • Scrapie strain variation and mutation
    • Bruce M. Scrapie strain variation and mutation. Br Med Bull 1993, 49: 822-838.
    • (1993) Br Med Bull , vol.49 , pp. 822-838
    • Bruce, M.1
  • 39
    • 0029922585 scopus 로고    scopus 로고
    • Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy
    • Lasmzas CI, Deslys J-P, Demaimay R, Adjou KT, Hauw J-J and Dormont D. Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy. J Gen Virol 1996, 77: 1601-1609.
    • (1996) J Gen Virol , vol.77 , pp. 1601-1609
    • Lasmzas, C.I.1    Deslys, J.-P.2    Demaimay, R.3    Adjou, K.T.4    Hauw, J.-J.5    Dormont, D.6
  • 40
    • 0027076372 scopus 로고
    • Successful transmission of Creutzfeldt-Jakob disease from human to mouse verified by prion protein accumulation in mouse brains
    • Muramoto T, Kitamoto T, Tateishi J and Goto I. Successful transmission of Creutzfeldt-Jakob disease from human to mouse verified by prion protein accumulation in mouse brains. Brain Res 1992, 599: 309-316.
    • (1992) Brain Res , vol.599 , pp. 309-316
    • Muramoto, T.1    Kitamoto, T.2    Tateishi, J.3    Goto, I.4
  • 42
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; Protein refolding and therapy
    • Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett 2001, 498: 204-207.
    • (2001) FEBS Lett , vol.498 , pp. 204-207
    • Soto, C.1
  • 43
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurodegeneration
    • Soto C and Estrada L. Protein misfolding and neurodegeneration. Arch Neurol 2008, 65: 184-189.
    • (2008) Arch Neurol , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.2
  • 44
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B and Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 2003, 26: 267-298.
    • (2003) Annu Rev Neurosci , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 45
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass C and Selkoe DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 2007, 8: 101-112.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 46
    • 33644816759 scopus 로고    scopus 로고
    • Amyloids, prions and the inherent infectious nature of misfolded protein aggregates
    • Soto C, Estrada L and Castilla J. Amyloids, prions and the inherent infectious nature of misfolded protein aggregates. Trends Biochem Sci 2006, 31: 150-155.
    • (2006) Trends Biochem Sci , vol.31 , pp. 150-155
    • Soto, C.1    Estrada, L.2    Castilla, J.3
  • 47
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT and Lansbury PT. Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993, 73: 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 48
    • 0142040121 scopus 로고    scopus 로고
    • Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein
    • Sokolowski F, Modler AJ, Masuch R, Zirwer D, Baier M, Lutsch G and Moss DA, et al. Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein. J Biol Chem 2003, 278: 40481-40492.
    • (2003) J Biol Chem , vol.278 , pp. 40481-40492
    • Sokolowski, F.1    Modler, A.J.2    Masuch, R.3    Zirwer, D.4    Baier, M.5    Lutsch, G.6    Moss, D.A.7
  • 49
    • 84862620376 scopus 로고    scopus 로고
    • A unifying role for prions in neurodegenerative diseases
    • Prusiner SB. A unifying role for prions in neurodegenerative diseases. Science 2012, 336: 1511-1513.
    • (2012) Science , vol.336 , pp. 1511-1513
    • Prusiner, S.B.1
  • 50
    • 12244255795 scopus 로고    scopus 로고
    • Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation
    • Modler A, Fabian H, Sokolowski F, Lutsch G, Gast K and Damaschun G. Polymerization of proteins into amyloid protofibrils shares common critical oligomeric states but differs in the mechanisms of their formation. Amyloid 2004, 11: 215-231.
    • (2004) Amyloid , vol.11 , pp. 215-231
    • Modler, A.1    Fabian, H.2    Sokolowski, F.3    Lutsch, G.4    Gast, K.5    Damaschun, G.6
  • 51
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: Protofibril formation of the prion protein
    • DeMarco ML and Daggett V. From conversion to aggregation: protofibril formation of the prion protein. Proc Natl Acad Sci USA 2004, 101: 2293-2298.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 2293-2298
    • Demarco, M.L.1    Daggett, V.2
  • 52
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates
    • Walsh DM, Hartley DM, Kusumoto Y, Fezoui Y, Condron MM, Lomakin A and Benedek GB, et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999, 274: 25945-25952.
    • (1999) J Biol Chem , vol.274 , pp. 25945-25952
    • Walsh, D.M.1    Hartley, D.M.2    Kusumoto, Y.3    Fezoui, Y.4    Condron, M.M.5    Lomakin, A.6    Benedek, G.B.7
  • 53
    • 2542483823 scopus 로고    scopus 로고
    • ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures
    • Srinivasan R, Marchant R and Zagorski M. ABri peptide associated with familial British dementia forms annular and ring-like protofibrillar structures. Amyloid 2004, 11: 10-13.
    • (2004) Amyloid , vol.11 , pp. 10-13
    • Srinivasan, R.1    Marchant, R.2    Zagorski, M.3
  • 54
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative disease: Amyloid pores from pathogenic mutations
    • Lashuel HA, Hartley D, Petre BM, Walz T and Lansbury PT. Neurodegenerative disease: amyloid pores from pathogenic mutations. Nature 2002, 418: 291.
    • (2002) Nature , vol.418 , pp. 291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 55
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers - A novel pathway of amyloid formation
    • Modler AJ, Gast K, Lutsch G and Damaschun G. Assembly of amyloid protofibrils via critical oligomers - a novel pathway of amyloid formation. J Mol Biol. 2003, 325: 135-148.
    • (2003) J Mol Biol. , vol.325 , pp. 135-148
    • Modler, A.J.1    Gast, K.2    Lutsch, G.3    Damaschun, G.4
  • 56
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • Winkler J, Tyedmers J, Bukau B and Mogk A. Chaperone networks in protein disaggregation and prion propagation. J Struct Biol 2012, 179: 152-160.
    • (2012) J Struct Biol , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 57
    • 0142105406 scopus 로고    scopus 로고
    • Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein
    • Hetz C, Russelakis-Carneiro M, Maundrell K, Castilla J and Soto C. Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein. EMBO J 2003, 22: 5435-5445.
    • (2003) EMBO J , vol.22 , pp. 5435-5445
    • Hetz, C.1    Russelakis-Carneiro, M.2    Maundrell, K.3    Castilla, J.4    Soto, C.5
  • 59
    • 0001552281 scopus 로고    scopus 로고
    • Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions
    • Shmerling D, Hegyi I, Fischer M, Blättler T, Brandner S, Götz J and Rülicke T, et al. Expression of amino-terminally truncated PrP in the mouse leading to ataxia and specific cerebellar lesions. Cell 1998, 93: 203-214.
    • (1998) Cell , Issue.93 , pp. 203-214
    • Shmerling, D.1    Hegyi, I.2    Fischer, M.3    Blättler, T.4    Brandner, S.5    Götz, J.6    Rülicke, T.7
  • 60
    • 77956220439 scopus 로고    scopus 로고
    • Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells
    • Solomon IH, Huettner JE and Harris DA. Neurotoxic mutants of the prion protein induce spontaneous ionic currents in cultured cells. J Biol Chem 2010, 285: 26719-26726.
    • (2010) J Biol Chem , vol.285 , pp. 26719-26726
    • Solomon, I.H.1    Huettner, J.E.2    Harris, D.A.3
  • 61
    • 78650994378 scopus 로고    scopus 로고
    • The intricate mechanisms of neurodegeneration in prion diseases
    • Soto C and Satani N. The intricate mechanisms of neurodegeneration in prion diseases. Trends Mol Med 2010, 17: 14-24.
    • (2010) Trends Mol Med , vol.17 , pp. 14-24
    • Soto, C.1    Satani, N.2
  • 63
    • 34248396416 scopus 로고    scopus 로고
    • Accumulation of prion protein in the brain that is not associated with transmissible disease
    • Piccardo P, Manson JC, King D, Ghetti B and Barron RM. Accumulation of prion protein in the brain that is not associated with transmissible disease. Proc Natl Acad Sci USA 2007, 104: 4712-4717.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4712-4717
    • Piccardo, P.1    Manson, J.C.2    King, D.3    Ghetti, B.4    Barron, R.M.5
  • 64
    • 58149399384 scopus 로고    scopus 로고
    • Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities
    • Chiesa R, Piccardo P, Biasini E, Ghetti B and Harris DA. Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities. J Neurosci 2008, 28: 13258-13267.
    • (2008) J Neurosci , vol.28 , pp. 13258-13267
    • Chiesa, R.1    Piccardo, P.2    Biasini, E.3    Ghetti, B.4    Harris, D.A.5
  • 65
    • 0025237594 scopus 로고
    • Scrapie-associated precursor proteins antigenic relationship between species and immunocytochemical localization in normal, scrapie, and Creutzfeldt-Jakob disease brains
    • Safar J, Ceroni M, Piccardo P, Gajdusek DC and Gibbs CJ. Scrapie-associated precursor proteins antigenic relationship between species and immunocytochemical localization in normal, scrapie, and Creutzfeldt-Jakob disease brains. Neurology 1990, 40: 513-517.
    • (1990) Neurology , vol.40 , pp. 513-517
    • Safar, J.1    Ceroni, M.2    Piccardo, P.3    Gajdusek, D.C.4    Gibbs, C.J.5
  • 66
    • 84865749298 scopus 로고    scopus 로고
    • Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Sträussler-Scheinker disease
    • Cortes CJ, Qin K, Cook J, Solanki A and Mastrianni JA. Rapamycin delays disease onset and prevents PrP plaque deposition in a mouse model of Gerstmann-Sträussler-Scheinker disease. J Neurosci 2012, 32: 12396-12405.
    • (2012) J Neurosci , vol.32 , pp. 12396-12405
    • Cortes, C.J.1    Qin, K.2    Cook, J.3    Solanki, A.4    Mastrianni, J.A.5
  • 67
    • 11844286389 scopus 로고    scopus 로고
    • Efficient inhibition of prion replication by PrP-Fc2 suggests that the prion is a PrPSc oligomer
    • Masel J, Genoud N and Aguzzi A. Efficient inhibition of prion replication by PrP-Fc2 suggests that the prion is a PrPSc oligomer. J Mol Biol. 2005, 345: 1243-1251.
    • (2005) J Mol Biol. , vol.345 , pp. 1243-1251
    • Masel, J.1    Genoud, N.2    Aguzzi, A.3
  • 68
    • 0032968132 scopus 로고    scopus 로고
    • Quantifying the kinetic parameters of prion replication
    • Masel J, Jansen V and Nowak M. Quantifying the kinetic parameters of prion replication. Biophys Chem 1999, 77: 139-152.
    • (1999) Biophys Chem , vol.77 , pp. 139-152
    • Masel, J.1    Jansen, V.2    Nowak, M.3
  • 69
    • 33646558563 scopus 로고    scopus 로고
    • Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and nonneuronal cells
    • Grenier C, Bissonnette C, Volkov L and Roucou X. Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and nonneuronal cells. J Neurochem 2006, 97: 1456-1466.
    • (2006) J Neurochem , vol.97 , pp. 1456-1466
    • Grenier, C.1    Bissonnette, C.2    Volkov, L.3    Roucou, X.4
  • 72
    • 2642544056 scopus 로고    scopus 로고
    • Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy
    • Zhu M, Han S, Zhou F, Carter SA and Fink AL. Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy. J Biol Chem 2004, 279: 24452-24459.
    • (2004) J Biol Chem , vol.279 , pp. 24452-24459
    • Zhu, M.1    Han, S.2    Zhou, F.3    Carter, S.A.4    Fink, A.L.5
  • 74
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya V, Bocharova O, Bronstein I and Baskakov I. Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons. J Biol Chem 2006, 281: 13828-13836.
    • (2006) J Biol Chem , vol.281 , pp. 13828-13836
    • Novitskaya, V.1    Bocharova, O.2    Bronstein, I.3    Baskakov, I.4
  • 75
    • 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 and Weissmann C. High prion and PrPSc levels but delayed onset of disease in scrapie-inoculated mice heterozygous for a disrupted PrP gene. Mol Med 1994, 1: 19-30.
    • (1994) Mol Med , Issue.1 , pp. 19-30
    • Bueler, H.1    Raeber, A.2    Sailer, A.3    Fischer, M.4    Aguzzi, A.5    Weissmann, C.6
  • 76
    • 79956110918 scopus 로고    scopus 로고
    • The cellular prion protein mediates neurotoxic signalling of b-sheet-rich conformers independent of prion replication
    • Resenberger U, Harmeier A, Woerner A, Goodman J, Mü ller V, Krishnan R and Vabulas R, et al. The cellular prion protein mediates neurotoxic signalling of b-sheet-rich conformers independent of prion replication. EMBO J 2011, 30: 2057-2070.
    • (2011) EMBO J , vol.30 , pp. 2057-2070
    • Resenberger, U.1    Harmeier, A.2    Woerner, A.3    Goodman, J.4    Müller, V.5    Krishnan, R.6    Vabulas, R.7
  • 78
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg MK, Al-Doujaily H, Sharps B, Clarke AR and Collinge J. Prion propagation and toxicity in vivo occur in two distinct mechanistic phases. Nature 2011, 470: 540-542.
    • (2011) Nature , vol.470 , pp. 540-542
    • Sandberg, M.K.1    Al-Doujaily, H.2    Sharps, B.3    Clarke, A.R.4    Collinge, J.5
  • 79
    • 84857198808 scopus 로고    scopus 로고
    • Ion channels induced by the prion protein
    • Solomon IH, Biasini E and Harris DA. Ion channels induced by the prion protein. Prion 2012, 6: 40-45.
    • (2012) Prion , vol.6 , pp. 40-45
    • Solomon, I.H.1    Biasini, E.2    Harris, D.A.3
  • 80
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • Lin M-C, Mirzabekov T and Kagan BL. Channel formation by a neurotoxic prion protein fragment. J Biol Chem 1997, 272: 44-47.
    • (1997) J Biol Chem , vol.272 , pp. 44-47
    • Lin, M.-C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 82
    • 84861722732 scopus 로고    scopus 로고
    • Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins away
    • Madampage C, Tavassoly O, Christensen C, Kumari M and Lee JS. Nanopore analysis: an emerging technique for studying the folding and misfolding of proteins away. Prion 2012, 6: 116-123.
    • (2012) Prion , vol.6 , pp. 116-123
    • Madampage, C.1    Tavassoly, O.2    Christensen, C.3    Kumari, M.4    Lee, J.S.5
  • 83
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformationdependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B, McIntire TM, Milton SC, Hall JE and Glabe CG. Permeabilization of lipid bilayers is a common conformationdependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 2004, 279: 46363-46366.
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3    McIntire, T.M.4    Milton, S.C.5    Hall, J.E.6    Glabe, C.G.7
  • 84
    • 0036381074 scopus 로고    scopus 로고
    • Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules
    • Kourie JI and Henry CL. Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: the role of dangerous unchaperoned molecules. Clin Exp Pharmacol Physiol 2002, 29: 741-753.
    • (2002) Clin Exp Pharmacol Physiol , vol.29 , pp. 741-753
    • Kourie, J.I.1    Henry, C.L.2
  • 85
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • Kawahara M, Kuroda Y, Arispe N and Rojas E. Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J Biol Chem 2000, 275: 14077-14083.
    • (2000) J Biol Chem , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 86
    • 27444443817 scopus 로고    scopus 로고
    • Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins
    • Magzoub M, Oglecka K, Pramanik A, Eriksson LEG and Gräslund A. Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins. Biochim Biophys Acta 2005, 1716: 126-136.
    • (2005) Biochim Biophys Acta , vol.1716 , pp. 126-136
    • Magzoub, M.1    Oglecka, K.2    Pramanik, A.3    Eriksson, L.E.G.4    Gräslund, A.5
  • 87
    • 1242293757 scopus 로고    scopus 로고
    • Astrocytic regulation of NMDA receptor subunit composition modulates the toxicity of prion peptide PrP106-126
    • Sassoon J, Daniels M and Brown DR. Astrocytic regulation of NMDA receptor subunit composition modulates the toxicity of prion peptide PrP106-126. Mol Cell Neurosci 2004, 25: 181-191.
    • (2004) Mol Cell Neurosci , vol.25 , pp. 181-191
    • Sassoon, J.1    Daniels, M.2    Brown, D.R.3
  • 88
    • 51549093536 scopus 로고    scopus 로고
    • Hippocampal bursts caused by changes in NMDA receptor-dependent excitation in a mouse model of variant CJD
    • Ratté S, Prescott SA, Collinge J and Jefferys JGR. Hippocampal bursts caused by changes in NMDA receptor-dependent excitation in a mouse model of variant CJD. Neurobiol Dis 2008, 32: 96-104.
    • (2008) Neurobiol Dis , vol.32 , pp. 96-104
    • Ratté, S.1    Prescott, S.A.2    Collinge, J.3    Jefferys, J.G.R.4
  • 89
    • 43149109488 scopus 로고    scopus 로고
    • Prion protein attenuates excitotoxicity by inhibiting NMDA receptors
    • Khosravani H, Zhang Y, Tsutsui S, Hameed S, Altier C, Hamid J and Chen L, et al. Prion protein attenuates excitotoxicity by inhibiting NMDA receptors. J Cell Biol 2008, 181: 551-565. Southwest China University
    • (2008) J Cell Biol , vol.181 , pp. 551-565
    • Khosravani, H.1    Zhang, Y.2    Tsutsui, S.3    Hameed, S.4    Altier, C.5    Hamid, J.6    Chen, L.7


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