메뉴 건너뛰기




Volumn 101, Issue 10, 2011, Pages 1311-1327

Prion protein aggregation

Author keywords

Alternative pathways; Amyloid fibrils; Oligomers; Prion protein; Structural heterogeneity

Indexed keywords


EID: 84860690734     PISSN: 00113891     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (12)

References (206)
  • 1
    • 0021884354 scopus 로고
    • Identification of scrapie prion proteinspecific mRNA in scrapie-infected and uninfected brain
    • Chesebro, B. et al., Identification of scrapie prion proteinspecific mRNA in scrapie-infected and uninfected brain. Nature, 1985, 315, 331-333.
    • (1985) Nature , vol.315 , pp. 331-333
    • Chesebro, B.1
  • 2
    • 0022005315 scopus 로고
    • A cellular gene encodes scrapie PrP 27-30 protein
    • Oesch, B. et al., A cellular gene encodes scrapie PrP 27-30 protein. Cell, 1985, 40, 735-746.
    • (1985) Cell , vol.40 , pp. 735-746
    • Oesch, B.1
  • 4
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D. R., Hsiao, K. and Prusiner, S. B., Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell, 1987, 51, 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 5
    • 0030569412 scopus 로고    scopus 로고
    • Metal-dependent alphahelix formation promoted by the glycine-rich octapeptide region of prion protein
    • Miura, T., Hori-i, A. and Takeuchi, H., Metal-dependent alphahelix formation promoted by the glycine-rich octapeptide region of prion protein. FEBS Lett., 1996, 396, 248-252.
    • (1996) FEBS Lett. , vol.396 , pp. 248-252
    • Miura, T.1    Hori-i, A.2    Takeuchi, H.3
  • 6
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R. and Wuthrich, K., NMR characterization of the full-length recombinant murine prion protein, mPrP (23-231). FEBS Lett., 1997, 413, 282-288.
    • (1997) FEBS Lett. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wuthrich, K.5
  • 8
    • 65949083115 scopus 로고    scopus 로고
    • Fishing for prion protein function
    • Chiesa, R. and Harris, D. A., Fishing for prion protein function. PLoS Biol., 2009, 7, e75.
    • (2009) PLoS Biol. , vol.7
    • Chiesa, R.1    Harris, D.A.2
  • 9
    • 77649091387 scopus 로고    scopus 로고
    • Axonal prion protein is required for peripheral myelin maintenance
    • Bremer, J. et al., Axonal prion protein is required for peripheral myelin maintenance. Nature Neurosci., 2010, 13, 310-318.
    • (2010) Nature Neurosci. , vol.13 , pp. 310-318
    • Bremer, J.1
  • 10
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B., Novel proteinaceous infectious particles cause scrapie. Science, 1982, 216, 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 12
    • 33746127253 scopus 로고
    • Uber eine eigenartige herdformige Erkrankung des Zentralnervensystems
    • Creutzfeldt, H. G., Uber eine eigenartige herdformige Erkrankung des Zentralnervensystems. Z. Gesamte Neurol. Psychiatr., 1920, 57, 1-18.
    • (1920) Z. Gesamte Neurol. Psychiatr. , vol.57 , pp. 1-18
    • Creutzfeldt, H.G.1
  • 13
    • 51849177198 scopus 로고
    • Uber eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswertem anatomischen Befunde (spatische Pseudoskelerose-Encephalomyelopathie mit disseminierten Degenerationsherden)
    • Jakob, A., Uber eigenartige Erkrankungen des Zentralnervensystems mit bemerkenswertem anatomischen Befunde (spatische Pseudoskelerose-Encephalomyelopathie mit disseminierten Degenerationsherden). Z. Gesamte Neurol. Psychiatr., 1921, 64, 147-228.
    • (1921) Z. Gesamte Neurol. Psychiatr. , vol.64 , pp. 147-228
    • Jakob, A.1
  • 16
    • 84860659986 scopus 로고
    • Myopathies of livestock
    • Hadlow, W. J., Myopathies of livestock. Lab. Invest., 1959, 8, 1478-1498.
    • (1959) Lab. Invest. , vol.8 , pp. 1478-1498
    • Hadlow, W.J.1
  • 17
    • 84872473797 scopus 로고
    • Advances in veterinary research
    • Gordon, W. S., Advances in veterinary research. Vet. Rec., 1946, 58, 516-525.
    • (1946) Vet. Rec. , vol.58 , pp. 516-525
    • Gordon, W.S.1
  • 18
    • 0001168222 scopus 로고
    • Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics
    • Sigurdsson, B., Rida, a chronic encephalitis of sheep with general remarks on infections which develop slowly and some of their special characteristics. Br. Vet. J., 1954, 110, 341-354.
    • (1954) Br. Vet. J. , vol.110 , pp. 341-354
    • Sigurdsson, B.1
  • 19
    • 0028861588 scopus 로고
    • Neuropathology and the scrapie-kuru connection
    • Hadlow, W. J., Neuropathology and the scrapie-kuru connection. Brain Pathol., 1995, 5, 27-31.
    • (1995) Brain Pathol. , vol.5 , pp. 27-31
    • Hadlow, W.J.1
  • 21
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper, T., Cramp, W. A., Haig, D. A. and Clarke, M. C., Does the agent of scrapie replicate without nucleic acid? Nature, 1967, 214, 764-766.
    • (1967) Nature , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 22
    • 0014963710 scopus 로고
    • Inactivation of the scrapie agent by near monochromatic ultraviolet light
    • Latarjet, R., Muel, B., Haig, D. A., Clarke, M. C. and Alper, T., Inactivation of the scrapie agent by near monochromatic ultraviolet light. Nature, 1970, 227, 1341-1343.
    • (1970) Nature , vol.227 , pp. 1341-1343
    • Latarjet, R.1    Muel, B.2    Haig, D.A.3    Clarke, M.C.4    Alper, T.5
  • 23
    • 0018215610 scopus 로고
    • Unusual resistance to ionizing radiation of the viruses of Kuru Creutzfeldt- Jakob disease and scrapie
    • Gibbs Jr, C. J., Gajdusek, D. C. and Latarjet, R., Unusual resistance to ionizing radiation of the viruses of Kuru, Creutzfeldt- Jakob disease and scrapie. Proc. Natl. Acad. Sci. USA, 1978, 75, 6268-6270.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 6268-6270
    • Gibbs Jr., C.J.1    Gajdusek, D.C.2    Latarjet, R.3
  • 24
    • 0001074386 scopus 로고
    • NINDB Monograph 2 (eds Gajdusek, D. C., Gibbs Jr, C. J. and Alpers, M. P.), US Government Printing Office, Washington, DC
    • Pattison, I. H., In Slow, Latent and Temperate Virus Infections, NINDB Monograph 2 (eds Gajdusek, D. C., Gibbs Jr, C. J. and Alpers, M. P.), US Government Printing Office, Washington, DC, 1965, pp. 249-257.
    • (1965) Slow, Latent and Temperate Virus Infections , pp. 249-257
    • Pattison, I.H.1
  • 25
    • 0014190770 scopus 로고
    • Nature of the scrapie agent
    • Gibbons, R. A. and Hunter, G. D., Nature of the scrapie agent. Nature, 1967, 215, 1041-1043.
    • (1967) Nature , vol.215 , pp. 1041-1043
    • Gibbons, R.A.1    Hunter, G.D.2
  • 26
    • 0014190760 scopus 로고
    • Self-replication and scrapie
    • Griffith, J. S., Self-replication and scrapie. Nature, 1967, 215, 1043-1044.
    • (1967) Nature , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 27
    • 0014194776 scopus 로고
    • The possible nature of the transmissible agent of scrapie
    • Pattison, I. H. and Jones, K. M., The possible nature of the transmissible agent of scrapie. Vet. Rec., 1967, 80, 2-9.
    • (1967) Vet. Rec. , vol.80 , pp. 2-9
    • Pattison, I.H.1    Jones, K.M.2
  • 29
    • 0014664401 scopus 로고
    • Susceptibility of scrapie agent to ionizing radiation
    • Field, E. J., Farmer, F., Caspary, E. A. and Joyce, G., Susceptibility of scrapie agent to ionizing radiation. Nature, 1969, 222, 90-91.
    • (1969) Nature , vol.222 , pp. 90-91
    • Field, E.J.1    Farmer, F.2    Caspary, E.A.3    Joyce, G.4
  • 30
    • 0015318003 scopus 로고
    • Scrapie: a prototype slow infection
    • Hunter, G. D., Scrapie: a prototype slow infection. J. Infect. Dis., 1972, 125, 427-440.
    • (1972) J. Infect. Dis. , vol.125 , pp. 427-440
    • Hunter, G.D.1
  • 31
    • 0014102343 scopus 로고
    • Attempts to release the scrapie agent from tissue debris
    • Hunter, G. D. and Millson, G. C., Attempts to release the scrapie agent from tissue debris. J. Comp. Pathol., 1967, 77, 301-307.
    • (1967) J. Comp. Pathol. , vol.77 , pp. 301-307
    • Hunter, G.D.1    Millson, G.C.2
  • 32
    • 0019324430 scopus 로고
    • Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent
    • Prusiner, S. B., Groth, D. F., Cochran, S. P., Masiarz, F. R., McKinley, M. P. and Martinez, H. M., Molecular properties, partial purification, and assay by incubation period measurements of the hamster scrapie agent. Biochemistry, 1980, 19, 4883-4891.
    • (1980) Biochemistry , vol.19 , pp. 4883-4891
    • Prusiner, S.B.1    Groth, D.F.2    Cochran, S.P.3    Masiarz, F.R.4    McKinley, M.P.5    Martinez, H.M.6
  • 34
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C., McKinley, M. P. and Prusiner, S. B., Identification of a protein that purifies with the scrapie prion. Science, 1982, 218, 1309-1311.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 35
    • 0021752457 scopus 로고
    • Purification and structural studies of a major scrapie prion protein
    • Prusiner, S. B., Groth, D. F., Bolton, D. C., Kent, S. B. and Hood, L. E., Purification and structural studies of a major scrapie prion protein. Cell, 1984, 38, 127-134.
    • (1984) Cell , vol.38 , pp. 127-134
    • Prusiner, S.B.1    Groth, D.F.2    Bolton, D.C.3    Kent, S.B.4    Hood, L.E.5
  • 36
    • 0022476747 scopus 로고
    • Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene
    • Basler, K. et al., Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell, 1986, 46, 417-428.
    • (1986) Cell , vol.46 , pp. 417-428
    • Basler, K.1
  • 37
    • 0023001210 scopus 로고
    • Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent
    • Locht, C., Chesebro, B., Race, R. and Keith, J. M., Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Proc. Natl. Acad. Sci. USA, 1986, 83, 6372-6376.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6372-6376
    • Locht, C.1    Chesebro, B.2    Race, R.3    Keith, J.M.4
  • 39
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • Bueler, H. et al., Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature, 1992, 356, 577-582.
    • (1992) Nature , vol.356 , pp. 577-582
    • Bueler, H.1
  • 41
    • 0028052363 scopus 로고
    • Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins
    • Westaway, D. et al., Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell, 1994, 76, 117-129.
    • (1994) Cell , vol.76 , pp. 117-129
    • Westaway, D.1
  • 42
    • 77649213673 scopus 로고    scopus 로고
    • Generating a prion with bacterially expressed recombinant prion protein
    • Wang, F., Wang, X., Yuan, C. G. and Ma, J., Generating a prion with bacterially expressed recombinant prion protein. Science, 2010, 327, 1132-1135.
    • (2010) Science , vol.327 , pp. 1132-1135
    • Wang, F.1    Wang, X.2    Yuan, C.G.3    Ma, J.4
  • 43
    • 77951979579 scopus 로고    scopus 로고
    • Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors
    • Kim, J. I. et al., Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors. J. Biol. Chem., 2010, 285, 14083-14087.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14083-14087
    • Kim, J.I.1
  • 44
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes, E. D. and Glenner, G. G., X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem., 1968, 16, 673-677.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 45
  • 46
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • Selkoe, D. J., Folding proteins in fatal ways. Nature, 2003, 426, 900-904.
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 47
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C. M., Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem., 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 48
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan, K. M. 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
  • 56
    • 0242363656 scopus 로고    scopus 로고
    • Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis
    • Mallucci, G., Dickinson, A., Linehan, J., Klohn, P. C., 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    Klohn, P.C.4    Brandner, S.5    Collinge, J.6
  • 57
    • 33846538022 scopus 로고    scopus 로고
    • Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice
    • Mallucci, G. R. et al., Targeting cellular prion protein reverses early cognitive deficits and neurophysiological dysfunction in prion-infected mice. Neuron, 2007, 53, 325-335.
    • (2007) Neuron , vol.53 , pp. 325-335
    • Mallucci, G.R.1
  • 58
    • 0028878943 scopus 로고
    • Inherited prion diseases and transmission to rodents
    • Tateishi, J. and Kitamoto, T., Inherited prion diseases and transmission to rodents. Brain Pathol., 1995, 5, 53-59.
    • (1995) Brain Pathol. , vol.5 , pp. 53-59
    • Tateishi, J.1    Kitamoto, T.2
  • 59
    • 0030011971 scopus 로고    scopus 로고
    • Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents
    • Tateishi, J., Kitamoto, T., Hoque, M. Z. and Furukawa, H., Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents. Neurology, 1996, 46, 532-537.
    • (1996) Neurology , vol.46 , pp. 532-537
    • Tateishi, J.1    Kitamoto, T.2    Hoque, M.Z.3    Furukawa, H.4
  • 60
    • 0344030333 scopus 로고    scopus 로고
    • Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein
    • Lasmezas, C. I. et al., Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science, 1997, 275, 402-405.
    • (1997) Science , vol.275 , pp. 402-405
    • Lasmezas, C.I.1
  • 61
    • 0038128629 scopus 로고    scopus 로고
    • Molecular distinction between pathogenic and infectious properties of the prion protein
    • Chiesa, R. et al., Molecular distinction between pathogenic and infectious properties of the prion protein. J. Virol., 2003, 77, 7611-7622.
    • (2003) J. Virol. , vol.77 , pp. 7611-7622
    • Chiesa, R.1
  • 62
    • 46749121818 scopus 로고    scopus 로고
    • A novel human disease with abnormal prion protein sensitive to protease
    • Gambetti, P. et al., A novel human disease with abnormal prion protein sensitive to protease. Ann. Neurol., 2008, 63, 697-708.
    • (2008) Ann. Neurol. , vol.63 , pp. 697-708
    • Gambetti, P.1
  • 64
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey, B. and Lansbury, P. T., 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
  • 65
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W. and Glabe, C. G., Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 2003, 300, 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 66
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed, R., Sokolov, Y., Edmonds, B., McIntire, T. M., Milton, S. C., Hall, J. E. and Glabe, C. G., Permeabilization of lipid bilayers is a common conformation-dependent 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
  • 68
    • 33744961169 scopus 로고    scopus 로고
    • Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons
    • Novitskaya, V., Bocharova, O. V., Bronstein, I. and Baskakov, I. V., 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.V.2    Bronstein, I.3    Baskakov, I.V.4
  • 71
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L. and Prusiner, S. B., 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.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 72
    • 0034932318 scopus 로고    scopus 로고
    • Mass spectrometric analysis of prion proteins
    • Baldwin, M. A., Mass spectrometric analysis of prion proteins. Adv. Protein Chem., 2001, 57, 29-54.
    • (2001) Adv. Protein Chem. , vol.57 , pp. 29-54
    • Baldwin, M.A.1
  • 73
    • 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. et al., A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol., 1997, 273, 614-622.
    • (1997) J. Mol. Biol. , vol.273 , pp. 614-622
    • Peretz, D.1
  • 74
    • 0037133587 scopus 로고    scopus 로고
    • Structural studies of the scrapie prion protein by electron crystallography
    • Wille, H. et al., Structural studies of the scrapie prion protein by electron crystallography. Proc. Natl. Acad. Sci. USA, 2002, 99, 3563-3568.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3563-3568
    • Wille, H.1
  • 75
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed beta-helices into trimers
    • Govaerts, C., Wille, H., Prusiner, S. B. and Cohen, F. E., Evidence for assembly of prions with left-handed beta-helices into trimers. Proc. Natl. Acad. Sci. USA, 2004, 101, 8342-8347.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 76
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: protofibril formation of the prion protein
    • DeMarco, M. L. 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
  • 77
    • 33845932931 scopus 로고    scopus 로고
    • Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models
    • DeMarco, M. L., Silveira, J., Caughey, B. and Daggett, V., Structural properties of prion protein protofibrils and fibrils: an experimental assessment of atomic models. Biochemistry, 2006, 45, 15573-15582.
    • (2006) Biochemistry , vol.45 , pp. 15573-15582
    • DeMarco, M.L.1    Silveira, J.2    Caughey, B.3    Daggett, V.4
  • 78
    • 0036708438 scopus 로고    scopus 로고
    • Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments
    • Dima, R. I. and Thirumalai, D., Exploring the propensities of helices in PrP(C) to form beta sheet using NMR structures and sequence alignments. Biophys. J., 2002, 83, 1268-1280.
    • (2002) Biophys. J. , vol.83 , pp. 1268-1280
    • Dima, R.I.1    Thirumalai, D.2
  • 79
    • 7444240183 scopus 로고    scopus 로고
    • Probing the instabilities in the dynamics of helical fragments from mouse PrPC
    • Dima, R. I. and Thirumalai, D., Probing the instabilities in the dynamics of helical fragments from mouse PrPC. Proc. Natl. Acad. Sci. USA, 2004, 101, 15335-15340.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15335-15340
    • Dima, R.I.1    Thirumalai, D.2
  • 81
    • 33846811599 scopus 로고    scopus 로고
    • Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/ deuterium exchange
    • Lu, X., Wintrode, P. L. and Surewicz, W. K., Beta-sheet core of human prion protein amyloid fibrils as determined by hydrogen/ deuterium exchange. Proc. Natl. Acad. Sci. USA, 2007, 104, 1510-1515.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 82
    • 37649000487 scopus 로고    scopus 로고
    • Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure
    • Cobb, N. J., Sonnichsen, F. D., McHaourab, H. and Surewicz, W. K., Molecular architecture of human prion protein amyloid: a parallel, in-register beta-structure. Proc. Natl. Acad. Sci. USA, 2007, 104, 18946-18951.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18946-18951
    • Cobb, N.J.1    Sonnichsen, F.D.2    McHaourab, H.3    Surewicz, W.K.4
  • 83
    • 78149307698 scopus 로고    scopus 로고
    • The alpha-helical C-terminal domain of fulllength recombinant PrP converts to an in-register parallel betasheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance
    • Tycko, R., Savtchenko, R., Ostapchenko, V. G., Makarava, N. and Baskakov, I. V., The alpha-helical C-terminal domain of fulllength recombinant PrP converts to an in-register parallel betasheet structure in PrP fibrils: evidence from solid state nuclear magnetic resonance. Biochemistry, 2010, 49, 9488-9497.
    • (2010) Biochemistry , vol.49 , pp. 9488-9497
    • Tycko, R.1    Savtchenko, R.2    Ostapchenko, V.G.3    Makarava, N.4    Baskakov, I.V.5
  • 84
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils
    • Antzutkin, O. N., Balbach, J. J., Leapman, R. D., Rizzo, N. W., Reed, J. and Tycko, R., Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc. Natl. Acad. Sci. USA, 2000, 97, 13045-13050.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13045-13050
    • Antzutkin, O.N.1    Balbach, J.J.2    Leapman, R.D.3    Rizzo, N.W.4    Reed, J.5    Tycko, R.6
  • 86
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of alpha-synuclein fibrils studied by sitedirected spin labelling
    • Der-Sarkissian, A., Jao, C. C., Chen, J. and Langen, R., Structural organization of alpha-synuclein fibrils studied by sitedirected spin labelling. J. Biol. Chem., 2003, 278, 37530-37535.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 87
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • Margittai, M. and Langen, R., Template-assisted filament growth by parallel stacking of tau. Proc. Natl. Acad. Sci. USA, 2004, 101, 10278-10283.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 88
    • 70350134740 scopus 로고    scopus 로고
    • Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of sitespecific fluorescence anisotropy decay kinetics
    • Jha, A., Udgaonkar, J. B. and Krishnamoorthy, G., Characterization of the heterogeneity and specificity of interpolypeptide interactions in amyloid protofibrils by measurement of sitespecific fluorescence anisotropy decay kinetics. J. Mol. Biol., 2009, 393, 735-752.
    • (2009) J. Mol. Biol. , vol.393 , pp. 735-752
    • Jha, A.1    Udgaonkar, J.B.2    Krishnamoorthy, G.3
  • 89
    • 33845938549 scopus 로고    scopus 로고
    • Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure
    • Shewmaker, F., Wickner, R. B. and Tycko, R., Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure. Proc. Natl. Acad. Sci. USA, 2006, 103, 19754-19759.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19754-19759
    • Shewmaker, F.1    Wickner, R.B.2    Tycko, R.3
  • 90
    • 36048969163 scopus 로고    scopus 로고
    • Characterization of betasheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance
    • Baxa, U., Wickner, R. B., Steven, A. C., Anderson, D. E., Marekov, L. N., Yau, W. M. and Tycko, R., Characterization of betasheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance. Biochemistry, 2007, 46, 13149-13162.
    • (2007) Biochemistry , vol.46 , pp. 13149-13162
    • Baxa, U.1    Wickner, R.B.2    Steven, A.C.3    Anderson, D.E.4    Marekov, L.N.5    Yau, W.M.6    Tycko, R.7
  • 91
    • 40649098246 scopus 로고    scopus 로고
    • Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure
    • Wickner, R. B., Dyda, F. and Tycko, R., Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure. Proc. Natl. Acad. Sci. USA, 2008, 105, 2403-2408.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2403-2408
    • Wickner, R.B.1    Dyda, F.2    Tycko, R.3
  • 92
    • 44049102092 scopus 로고    scopus 로고
    • Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils
    • Helmus, J. J., Surewicz, K., Nadaud, P. S., Surewicz, W. K. and Jaroniec, C. P., Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrils. Proc. Natl. Acad. Sci. USA, 2008, 105, 6284-6289.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6284-6289
    • Helmus, J.J.1    Surewicz, K.2    Nadaud, P.S.3    Surewicz, W.K.4    Jaroniec, C.P.5
  • 93
    • 29144451322 scopus 로고    scopus 로고
    • Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L)
    • Lim, K. H. et al., Solid-state NMR structural studies of the fibril form of a mutant mouse prion peptide PrP89-143(P101L). Solid State Nucl. Magn. Reson., 2006, 29, 183-190.
    • (2006) Solid State Nucl. Magn. Reson. , vol.29 , pp. 183-190
    • Lim, K.H.1
  • 94
    • 77957756752 scopus 로고    scopus 로고
    • Probing the conformation of a prion protein fibril with hydrogen exchange
    • Damo, S. M., Phillips, A. H., Young, A. L., Li, S., Woods Jr, V. L. and Wemmer, D. E., Probing the conformation of a prion protein fibril with hydrogen exchange. J. Biol. Chem., 2010, 285, 32303-32311.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32303-32311
    • Damo, S.M.1    Phillips, A.H.2    Young, A.L.3    Li, S.4    Woods Jr., V.L.5    Wemmer, D.E.6
  • 95
    • 67049087912 scopus 로고    scopus 로고
    • Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration
    • Shewmaker, F., Kryndushkin, D., Chen, B., Tycko, R. and Wickner, R. B., Two prion variants of Sup35p have in-register parallel beta-sheet structures, independent of hydration. Biochemistry, 2009, 48, 5074-5082.
    • (2009) Biochemistry , vol.48 , pp. 5074-5082
    • Shewmaker, F.1    Kryndushkin, D.2    Chen, B.3    Tycko, R.4    Wickner, R.B.5
  • 98
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R. et al., Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature, 1997, 385, 787-793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1
  • 99
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly, J. W., The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol., 1998, 8, 101-106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 100
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky, V. N. and Fink, A. L., Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta, 2004, 1698, 131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 101
    • 0033813424 scopus 로고    scopus 로고
    • A glimpse of a possible amyloidogenic intermediate of transthyretin
    • Liu, K., Cho, H. S., Lashuel, H. A., Kelly, J. W. and Wemmer, D. E., A glimpse of a possible amyloidogenic intermediate of transthyretin. Nature Struct. Biol., 2000, 7, 754-757.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 754-757
    • Liu, K.1    Cho, H.S.2    Lashuel, H.A.3    Kelly, J.W.4    Wemmer, D.E.5
  • 102
  • 104
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F. and Dobson, C. M., Amyloid formation by globular proteins under native conditions. Nature Chem. Biol., 2009, 5, 15-22.
    • (2009) Nature Chem. Biol. , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 105
    • 0021527508 scopus 로고
    • Kinetics of nucleationcontrolled polymerization A perturbation treatment for use with a secondary pathway
    • Bishop, M. F. and Ferrone, F. A., Kinetics of nucleationcontrolled polymerization. A perturbation treatment for use with a secondary pathway. Biophys. J., 1984, 46, 631-644.
    • (1984) Biophys. J. , vol.46 , pp. 631-644
    • Bishop, M.F.1    Ferrone, F.A.2
  • 106
    • 33947613349 scopus 로고
    • A theory of linear and helical aggregations of macromolecules
    • Oosawa, F. and Kasai, M., A theory of linear and helical aggregations of macromolecules. J. Mol. Biol., 1962, 4, 10-21.
    • (1962) J. Mol. Biol. , vol.4 , pp. 10-21
    • Oosawa, F.1    Kasai, M.2
  • 107
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D. and Lansbury Jr, P. T., Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu. Rev. Biochem., 1997, 66, 385-407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury Jr., P.T.2
  • 108
    • 0032877134 scopus 로고    scopus 로고
    • Analysis of protein aggregation kinetics
    • Ferrone, F., Analysis of protein aggregation kinetics. Methods Enzymol., 1999, 309, 256-274.
    • (1999) Methods Enzymol. , vol.309 , pp. 256-274
    • Ferrone, F.1
  • 109
    • 77953341846 scopus 로고    scopus 로고
    • Mechanisms of amyloid fibril formation by proteins
    • Kumar, S. and Udgaonkar, J. B., Mechanisms of amyloid fibril formation by proteins. Curr. Sci., 2010, 98, 639-656.
    • (2010) Curr. Sci. , vol.98 , pp. 639-656
    • Kumar, S.1    Udgaonkar, J.B.2
  • 110
    • 0035853825 scopus 로고    scopus 로고
    • Polymerization of Ftsz, a bacterial homolog of tubulin, assembly cooperative?
    • Romberg, L., Simon, M. and Erickson, H. P., Polymerization of Ftsz, a bacterial homolog of tubulin, assembly cooperative? J. Biol. Chem., 2001, 276, 11743-11753.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11743-11753
    • Romberg, L.1    Simon, M.2    Erickson, H.P.3
  • 111
    • 35648945914 scopus 로고    scopus 로고
    • Protein aggregation processes: in search of the mechanism
    • Frieden, C., Protein aggregation processes: in search of the mechanism. Protein Sci., 2007, 16, 2334-2344.
    • (2007) Protein Sci. , vol.16 , pp. 2334-2344
    • Frieden, C.1
  • 112
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio, T. R. et al., Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science, 2000, 289, 1317-1321.
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.R.1
  • 113
    • 8844247180 scopus 로고    scopus 로고
    • Mechanism of prion propagation: amyloid growth occurs by monomer addition
    • Collins, S. R., Douglass, A., Vale, R. D. and Weissman, J. S., Mechanism of prion propagation: amyloid growth occurs by monomer addition. PLoS Biol., 2004, 2, e321.
    • (2004) PLoS Biol. , vol.2
    • Collins, S.R.1    Douglass, A.2    Vale, R.D.3    Weissman, J.S.4
  • 114
    • 14044250915 scopus 로고    scopus 로고
    • In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features
    • Baskakov, I. V. and Bocharova, O. V., In vitro conversion of mammalian prion protein into amyloid fibrils displays unusual features. Biochemistry, 2005, 44, 2339-2348.
    • (2005) Biochemistry , vol.44 , pp. 2339-2348
    • Baskakov, I.V.1    Bocharova, O.V.2
  • 115
    • 27344435254 scopus 로고    scopus 로고
    • Polyglutamine aggregation nucleation: thermodynamics of a highly unfavourable protein folding reaction
    • Bhattacharyya, A. M., Thakur, A. K. and Wetzel, R., Polyglutamine aggregation nucleation: thermodynamics of a highly unfavourable protein folding reaction. Proc. Natl. Acad. Sci. USA, 2005, 102, 15400-15405.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15400-15405
    • Bhattacharyya, A.M.1    Thakur, A.K.2    Wetzel, R.3
  • 116
    • 48249092311 scopus 로고    scopus 로고
    • Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
    • Xue, W. F., Homans, S. W. and Radford, S. E., Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proc. Natl. Acad. Sci. USA, 2008, 105, 8926-8931.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 8926-8931
    • Xue, W.F.1    Homans, S.W.2    Radford, S.E.3
  • 117
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • Chen, S., Ferrone, F. A. and Wetzel, R., Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation. Proc. Natl. Acad. Sci. USA, 2002, 99, 11884-11889.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 118
    • 0019072559 scopus 로고
    • Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism
    • Ferrone, F. A., Hofrichter, J., Sunshine, H. R. and Eaton, W. A., Kinetic studies on photolysis-induced gelation of sickle cell hemoglobin suggest a new mechanism. Biophys. J., 1980, 32, 361-380.
    • (1980) Biophys. J. , vol.32 , pp. 361-380
    • Ferrone, F.A.1    Hofrichter, J.2    Sunshine, H.R.3    Eaton, W.A.4
  • 119
    • 0019968097 scopus 로고
    • Spontaneous fragmentation of actin filaments in physiological conditions
    • Wegner, A., Spontaneous fragmentation of actin filaments in physiological conditions. Nature, 1982, 296, 266-267.
    • (1982) Nature , vol.296 , pp. 266-267
    • Wegner, A.1
  • 120
    • 0020481585 scopus 로고
    • Fragmentation of actin filaments
    • Wegner, A. and Savko, P., Fragmentation of actin filaments. Biochemistry, 1982, 21, 1909-1913.
    • (1982) Biochemistry , vol.21 , pp. 1909-1913
    • Wegner, A.1    Savko, P.2
  • 121
    • 0037255361 scopus 로고    scopus 로고
    • Assembly of amyloid protofibrils via critical oligomers - a novel pathway of amyloid formation
    • Modler, A. J., 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
  • 122
    • 67650079178 scopus 로고    scopus 로고
    • Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein
    • Kumar, S. and Udgaonkar, J. B., Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein. Biochemistry, 2009, 48, 6441-6449.
    • (2009) Biochemistry , vol.48 , pp. 6441-6449
    • Kumar, S.1    Udgaonkar, J.B.2
  • 123
    • 58149400915 scopus 로고    scopus 로고
    • Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation
    • Kumar, S. and Udgaonkar, J. B., Conformational conversion may precede or follow aggregate elongation on alternative pathways of amyloid protofibril formation. J. Mol. Biol., 2009, 385, 1266-1276.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1266-1276
    • Kumar, S.1    Udgaonkar, J.B.2
  • 124
    • 0030799122 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis Detection of a protofibrillar intermediate
    • Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M. and Teplow, D. B., Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. J. Biol. Chem., 1997, 272, 22364-22372.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22364-22372
    • Walsh, D.M.1    Lomakin, A.2    Benedek, G.B.3    Condron, M.M.4    Teplow, D.B.5
  • 125
    • 0033520461 scopus 로고    scopus 로고
    • Amyloid beta-protein fibrillogenesis Structure and biological activity of protofibrillar intermediates
    • Walsh, D. M. 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
  • 126
    • 33746781304 scopus 로고    scopus 로고
    • Structural differences in Aβ amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation
    • Kheterpal, I., Chen, M., Cook, K. D. and Wetzel, R., Structural differences in Aβ amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation. J. Mol. Biol., 2006, 361, 785-795.
    • (2006) J. Mol. Biol. , vol.361 , pp. 785-795
    • Kheterpal, I.1    Chen, M.2    Cook, K.D.3    Wetzel, R.4
  • 127
    • 36849084640 scopus 로고    scopus 로고
    • Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid
    • Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B. and Ishii, Y., Evidence of fibril-like beta-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's beta-amyloid. Nature Struct. Mol. Biol., 2007, 14, 1157-1164.
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 1157-1164
    • Chimon, S.1    Shaibat, M.A.2    Jones, C.R.3    Calero, D.C.4    Aizezi, B.5    Ishii, Y.6
  • 128
    • 51349098137 scopus 로고    scopus 로고
    • Evidence for stepwise formation of amyloid fibrils by the mouse prion protein
    • Jain, S. and Udgaonkar, J. B., Evidence for stepwise formation of amyloid fibrils by the mouse prion protein. J. Mol. Biol., 2008, 382, 1228-1241.
    • (2008) J. Mol. Biol. , vol.382 , pp. 1228-1241
    • Jain, S.1    Udgaonkar, J.B.2
  • 129
    • 79951607134 scopus 로고    scopus 로고
    • Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions
    • Jain, S. and Udgaonkar, J. B., Defining the pathway of worm-like amyloid fibril formation by the mouse prion protein by delineation of the productive and unproductive oligomerization reactions. Biochemistry, 2011, 50, 1153-1161.
    • (2011) Biochemistry , vol.50 , pp. 1153-1161
    • Jain, S.1    Udgaonkar, J.B.2
  • 130
    • 0034733023 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism
    • Esler, W. P. et al., Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry, 2000, 39, 6288-6295.
    • (2000) Biochemistry , vol.39 , pp. 6288-6295
    • Esler, W.P.1
  • 131
    • 1442330505 scopus 로고    scopus 로고
    • The elongation of yeast prion fibers involves separable steps of association and conversion
    • Scheibel, T., Bloom, J. and Lindquist, S. L., The elongation of yeast prion fibers involves separable steps of association and conversion. Proc. Natl. Acad. Sci. USA, 2004, 101, 2287-2292.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2287-2292
    • Scheibel, T.1    Bloom, J.2    Lindquist, S.L.3
  • 132
    • 33847769109 scopus 로고    scopus 로고
    • Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion
    • Kumar, S., Mohanty, S. K. and Udgaonkar, J. B., Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion. J. Mol. Biol., 2007, 367, 1186-1204.
    • (2007) J. Mol. Biol. , vol.367 , pp. 1186-1204
    • Kumar, S.1    Mohanty, S.K.2    Udgaonkar, J.B.3
  • 133
    • 77956138054 scopus 로고    scopus 로고
    • Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein
    • Jain, S. and Udgaonkar, J. B., Salt-induced modulation of the pathway of amyloid fibril formation by the mouse prion protein. Biochemistry, 2010, 49, 7615-7624.
    • (2010) Biochemistry , vol.49 , pp. 7615-7624
    • Jain, S.1    Udgaonkar, J.B.2
  • 134
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: conformational diversity and consequences
    • Toyama, B. H. and Weissman, J. S., Amyloid structure: conformational diversity and consequences. Annu. Rev. Biochem., 2011, 80, 557-585.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 135
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S. B., Molecular biology of prion diseases. Science, 1991, 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 136
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T. and Lansbury Jr, P. T., 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 Jr., P.T.2
  • 137
  • 138
    • 84961034678 scopus 로고
    • Scrapie produced experimentally in goats with special reference to the clinical syndrome
    • Pattison, I. H. and Millson, G. C., Scrapie produced experimentally in goats with special reference to the clinical syndrome. J. Comp. Pathol., 1961, 71, 101-108.
    • (1961) J. Comp. Pathol. , vol.71 , pp. 101-108
    • Pattison, I.H.1    Millson, G.C.2
  • 139
    • 0014308027 scopus 로고
    • The sequential development of the brain lesion of scrapie in three strains of mice
    • Fraser, H. and Dickinson, A. G., The sequential development of the brain lesion of scrapie in three strains of mice. J. Comp. Pathol., 1968, 78, 301-311.
    • (1968) J. Comp. Pathol. , vol.78 , pp. 301-311
    • Fraser, H.1    Dickinson, A.G.2
  • 140
    • 0015550206 scopus 로고
    • Scrapie in mice. Agent-strain differences in the distribution and intensity of grey matter vacuolation
    • Fraser, H. and Dickinson, A. G., Scrapie in mice. Agent-strain differences in the distribution and intensity of grey matter vacuolation. J. Comp. Pathol., 1973, 83, 29-40.
    • (1973) J. Comp. Pathol. , vol.83 , pp. 29-40
    • Fraser, H.1    Dickinson, A.G.2
  • 141
    • 0026729945 scopus 로고
    • Replication of distinct scrapie prion isolates is region specific in brains of transgenic mice and hamsters
    • Hecker, R. et al., Replication of distinct scrapie prion isolates is region specific in brains of transgenic mice and hamsters. Genes Dev., 1992, 6, 1213-1228.
    • (1992) Genes Dev. , vol.6 , pp. 1213-1228
    • Hecker, R.1
  • 143
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: their causes and molecular basis
    • Collinge, J., Prion diseases 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
  • 144
    • 0028043661 scopus 로고
    • Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy
    • Bessen, R. A. and Marsh, R. F., Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol., 1994, 68, 7859-7868.
    • (1994) J. Virol. , vol.68 , pp. 7859-7868
    • Bessen, R.A.1    Marsh, R.F.2
  • 145
    • 0033610870 scopus 로고    scopus 로고
    • Straindependent differences in beta-sheet conformations of abnormal prion protein
    • Caughey, B., Raymond, G. J. and Bessen, R. A., Straindependent differences in beta-sheet conformations of abnormal prion protein. J. Biol. Chem., 1998, 273, 32230-32235.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32230-32235
    • Caughey, B.1    Raymond, G.J.2    Bessen, R.A.3
  • 146
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrP(Sc) molecules with different conformations
    • Safar, J. et al., Eight prion strains have PrP(Sc) molecules with different conformations. Nature Med., 1998, 4, 1157-1165.
    • (1998) Nature Med. , vol.4 , pp. 1157-1165
    • Safar, J.1
  • 147
    • 0036900691 scopus 로고    scopus 로고
    • TSE agent strains and PrP: reconciling structure and function
    • Somerville, R. A., TSE agent strains and PrP: reconciling structure and function. Trends Biochem. Sci., 2002, 27, 606-612.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 606-612
    • Somerville, R.A.1
  • 148
    • 0025836628 scopus 로고
    • Scrapie strain variation and its implications
    • Bruce, M. E. and Fraser, H., Scrapie strain variation and its implications. Curr. Top. Microbiol. Immunol., 1991, 172, 125-138.
    • (1991) Curr. Top. Microbiol. Immunol. , vol.172 , pp. 125-138
    • Bruce, M.E.1    Fraser, H.2
  • 149
    • 0035803405 scopus 로고    scopus 로고
    • Glycosylation influences crossspecies formation of protease-resistant prion protein
    • Priola, S. A. and Lawson, V. A., Glycosylation influences crossspecies formation of protease-resistant prion protein. EMBO J., 2001, 20, 6692-6699.
    • (2001) EMBO J. , vol.20 , pp. 6692-6699
    • Priola, S.A.1    Lawson, V.A.2
  • 150
    • 0037184057 scopus 로고    scopus 로고
    • Molecular basis of scrapie strain glycoform variation
    • Vorberg, I. and Priola, S. A., Molecular basis of scrapie strain glycoform variation. J. Biol. Chem., 2002, 277, 36775-36781.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36775-36781
    • Vorberg, I.1    Priola, S.A.2
  • 151
    • 3943084181 scopus 로고    scopus 로고
    • Emerging principles of conformation-based prion inheritance
    • Chien, P., Weissman, J. S. and DePace, A. H., Emerging principles of conformation-based prion inheritance. Annu. Rev. Biochem., 2004, 73, 617-656.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 617-656
    • Chien, P.1    Weissman, J.S.2    DePace, A.H.3
  • 152
    • 12144271772 scopus 로고    scopus 로고
    • NMR structure of the bovine prion protein isolated from healthy calf brains
    • Hornemann, S., Schorn, C. and Wuthrich, K., NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep., 2004, 5, 1159-1164.
    • (2004) EMBO Rep. , vol.5 , pp. 1159-1164
    • Hornemann, S.1    Schorn, C.2    Wuthrich, K.3
  • 153
    • 0032979289 scopus 로고    scopus 로고
    • Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates
    • Wildegger, G., Liemann, S. and Glockshuber, R., Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates. Nature Struct. Biol., 1999, 6, 550-553.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 550-553
    • Wildegger, G.1    Liemann, S.2    Glockshuber, R.3
  • 154
    • 0037160126 scopus 로고    scopus 로고
    • Kinetic intermediate in the folding of human prion protein
    • Apetri, A. C. and Surewicz, W. K., Kinetic intermediate in the folding of human prion protein. J. Biol. Chem., 2002, 277, 44589-44592.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44589-44592
    • Apetri, A.C.1    Surewicz, W.K.2
  • 155
    • 33748342540 scopus 로고    scopus 로고
    • Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments
    • Apetri, A. C., Maki, K., Roder, H. and Surewicz, W. K., Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J. Am. Chem. Soc., 2006, 128, 11673-11678.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11673-11678
    • Apetri, A.C.1    Maki, K.2    Roder, H.3    Surewicz, W.K.4
  • 156
    • 0036304151 scopus 로고    scopus 로고
    • Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation
    • Nicholson, E. M., Mo, H., Prusiner, S. B., Cohen, F. E. and Marqusee, S., Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation. J. Mol. Biol., 2002, 316, 807-815.
    • (2002) J. Mol. Biol. , vol.316 , pp. 807-815
    • Nicholson, E.M.1    Mo, H.2    Prusiner, S.B.3    Cohen, F.E.4    Marqusee, S.5
  • 157
    • 0037108168 scopus 로고    scopus 로고
    • Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc?
    • Kuwata, K., Li, H., Yamada, H., Legname, G., Prusiner, S. B., Akasaka, K. and James, T. L., Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc? Biochemistry, 2002, 41, 12277-12283.
    • (2002) Biochemistry , vol.41 , pp. 12277-12283
    • Kuwata, K.1    Li, H.2    Yamada, H.3    Legname, G.4    Prusiner, S.B.5    Akasaka, K.6    James, T.L.7
  • 160
    • 0032553530 scopus 로고    scopus 로고
    • Familial mutations and the thermodynamic stability of the recombinant human prion protein
    • Swietnicki, W., Petersen, R. B., Gambetti, P. and Surewicz, W. K., Familial mutations and the thermodynamic stability of the recombinant human prion protein. J. Biol. Chem., 1998, 273, 31048-31052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31048-31052
    • Swietnicki, W.1    Petersen, R.B.2    Gambetti, P.3    Surewicz, W.K.4
  • 161
    • 2342432162 scopus 로고    scopus 로고
    • The effect of disease-associated mutations on the folding pathway of human prion protein
    • Apetri, A. C., Surewicz, K. and Surewicz, W. K., The effect of disease-associated mutations on the folding pathway of human prion protein. J. Biol. Chem., 2004, 279, 18008-18014.
    • (2004) J. Biol. Chem. , vol.279 , pp. 18008-18014
    • Apetri, A.C.1    Surewicz, K.2    Surewicz, W.K.3
  • 162
    • 0035849540 scopus 로고    scopus 로고
    • On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein
    • Morillas, M., Vanik, D. L. and Surewicz, W. K., On the mechanism of alpha-helix to beta-sheet transition in the recombinant prion protein. Biochemistry, 2001, 40, 6982-6987.
    • (2001) Biochemistry , vol.40 , pp. 6982-6987
    • Morillas, M.1    Vanik, D.L.2    Surewicz, W.K.3
  • 163
    • 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, G. J., Ernst, D. and Race, R. E., 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., 1991, 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
  • 164
    • 0026775909 scopus 로고
    • Evidence for synthesis of scrapie prion proteins in the endocytic pathway
    • Borchelt, D. R., Taraboulos, A. and Prusiner, S. B., Evidence for synthesis of scrapie prion proteins in the endocytic pathway. J. Biol. Chem., 1992, 267, 16188-16199.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16188-16199
    • Borchelt, D.R.1    Taraboulos, A.2    Prusiner, S.B.3
  • 165
    • 0030781922 scopus 로고    scopus 로고
    • K., pH-dependent stability and conformation of the recombinant human prion protein PrP (90-231)
    • Swietnicki, W., Petersen, R., Gambetti, P. and Surewicz, W. K., pH-dependent stability and conformation of the recombinant human prion protein PrP (90-231). J. Biol. Chem., 1997, 272, 27517-27520.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27517-27520
    • Swietnicki, W.1    Petersen, R.2    Gambetti, P.3    Surewicz, W.4
  • 166
    • 0034681173 scopus 로고    scopus 로고
    • Aggregation and fibrillization of the recombinant human prion protein huPrP90-231
    • Swietnicki, W., Morillas, M., Chen, S. G., Gambetti, P. and Surewicz, W. K., Aggregation and fibrillization of the recombinant human prion protein huPrP90-231. Biochemistry, 2000, 39, 424-431.
    • (2000) Biochemistry , vol.39 , pp. 424-431
    • Swietnicki, W.1    Morillas, M.2    Chen, S.G.3    Gambetti, P.4    Surewicz, W.K.5
  • 167
    • 0035827614 scopus 로고    scopus 로고
    • Folding of prion protein to its native alpha-helical conformation is under kinetic control
    • Baskakov, I. V., Legname, G., Prusiner, S. B. and Cohen, F. E., Folding of prion protein to its native alpha-helical conformation is under kinetic control. J. Biol. Chem., 2001, 276, 19687-19690.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19687-19690
    • Baskakov, I.V.1    Legname, G.2    Prusiner, S.B.3    Cohen, F.E.4
  • 169
    • 1542379868 scopus 로고    scopus 로고
    • Autocatalytic conversion of recombinant prion proteins displays a species barrier
    • Baskakov, I. V., Autocatalytic conversion of recombinant prion proteins displays a species barrier. J. Biol. Chem., 2004, 279, 7671-7677.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7671-7677
    • Baskakov, I.V.1
  • 170
    • 12544257523 scopus 로고    scopus 로고
    • In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc)
    • Bocharova, O. V., Breydo, L., Parfenov, A. S., Salnikov, V. V. and Baskakov, I. V., In vitro conversion of full-length mammalian prion protein produces amyloid form with physical properties of PrP(Sc). J. Mol. Biol., 2005, 346, 645-659.
    • (2005) J. Mol. Biol. , vol.346 , pp. 645-659
    • Bocharova, O.V.1    Breydo, L.2    Parfenov, A.S.3    Salnikov, V.V.4    Baskakov, I.V.5
  • 171
    • 0033583190 scopus 로고    scopus 로고
    • Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations
    • Jackson, G. S. et al., Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. Science, 1999, 283, 1935-1937.
    • (1999) Science , vol.283 , pp. 1935-1937
    • Jackson, G.S.1
  • 172
    • 0035951859 scopus 로고    scopus 로고
    • The role of disulfide bridge in the folding and stability of the recombinant human prion protein
    • Maiti, N. R. and Surewicz, W. K., The role of disulfide bridge in the folding and stability of the recombinant human prion protein. J. Biol. Chem., 2001, 276, 2427-2431.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2427-2431
    • Maiti, N.R.1    Surewicz, W.K.2
  • 173
    • 14744284214 scopus 로고    scopus 로고
    • Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities
    • Rezaei, H., Eghiaian, F., Perez, J., Doublet, B., Choiset, Y., Haertle, T. and Grosclaude, J., Sequential generation of two structurally distinct ovine prion protein soluble oligomers displaying different biochemical reactivities. J. Mol. Biol., 2005, 347, 665-679.
    • (2005) J. Mol. Biol. , vol.347 , pp. 665-679
    • Rezaei, H.1    Eghiaian, F.2    Perez, J.3    Doublet, B.4    Choiset, Y.5    Haertle, T.6    Grosclaude, J.7
  • 174
    • 23144463784 scopus 로고
    • Assembly of the full-length recombinant mouse prion protein I Formation of soluble oligomers
    • Vendrely, C. et al., Assembly of the full-length recombinant mouse prion protein I. Formation of soluble oligomers. Biochim. Biophys. Acta, 2005, 1724, 355-366.
    • (1724) Biochim. Biophys. Acta , vol.2005 , pp. 355-366
    • Vendrely, C.1
  • 175
    • 34250681413 scopus 로고    scopus 로고
    • Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/deuterium exchange and disulfide linkage
    • Eghiaian, F. et al., Diversity in prion protein oligomerization pathways results from domain expansion as revealed by hydrogen/ deuterium exchange and disulfide linkage. Proc. Natl. Acad. Sci. USA, 2007, 104, 7414-7419.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7414-7419
    • Eghiaian, F.1
  • 176
    • 33646093028 scopus 로고    scopus 로고
    • Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy
    • Anderson, M., Bocharova, O. V., Makarava, N., Breydo, L., Salnikov, V. V. and Baskakov, I. V., Polymorphism and ultrastructural organization of prion protein amyloid fibrils: an insight from high resolution atomic force microscopy. J. Mol. Biol., 2006, 358, 580-596.
    • (2006) J. Mol. Biol. , vol.358 , pp. 580-596
    • Anderson, M.1    Bocharova, O.V.2    Makarava, N.3    Breydo, L.4    Salnikov, V.V.5    Baskakov, I.V.6
  • 178
    • 47049117171 scopus 로고    scopus 로고
    • The same primary structure of the prion protein yields two distinct self-propagating states
    • Makarava, N. and Baskakov, I. V., The same primary structure of the prion protein yields two distinct self-propagating states. J. Biol. Chem., 2008, 283, 15988-15996.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15988-15996
    • Makarava, N.1    Baskakov, I.V.2
  • 179
    • 53549084326 scopus 로고    scopus 로고
    • The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP
    • Ostapchenko, V. G., Makarava, N., Savtchenko, R. and Baskakov, I. V., The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP. J. Mol. Biol., 2008, 383, 1210-1224.
    • (2008) J. Mol. Biol. , vol.383 , pp. 1210-1224
    • Ostapchenko, V.G.1    Makarava, N.2    Savtchenko, R.3    Baskakov, I.V.4
  • 181
    • 23444445907 scopus 로고    scopus 로고
    • Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid
    • Gosal, W. S., Morten, I. J., Hewitt, E. W., Smith, D. A., Thomson, N. H. and Radford, S. E., Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J. Mol. Biol., 2005, 351, 850-864.
    • (2005) J. Mol. Biol. , vol.351 , pp. 850-864
    • Gosal, W.S.1    Morten, I.J.2    Hewitt, E.W.3    Smith, D.A.4    Thomson, N.H.5    Radford, S.E.6
  • 182
    • 28544443624 scopus 로고    scopus 로고
    • Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231
    • Apetri, A. C., Vanik, D. L. and Surewicz, W. K., Polymorphism at residue 129 modulates the conformational conversion of the D178N variant of human prion protein 90-231. Biochemistry, 2005, 44, 15880-15888.
    • (2005) Biochemistry , vol.44 , pp. 15880-15888
    • Apetri, A.C.1    Vanik, D.L.2    Surewicz, W.K.3
  • 183
    • 58049199406 scopus 로고    scopus 로고
    • Prion protein amyloid formation under native like conditions involves refolding of the C-terminal α-helical domain
    • Cobb, N. J., Apetri, A. C. and Surewicz, W. K., Prion protein amyloid formation under native like conditions involves refolding of the C-terminal α-helical domain. J. Biol. Chem., 2008, 283, 34704-34711.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34704-34711
    • Cobb, N.J.1    Apetri, A.C.2    Surewicz, W.K.3
  • 186
    • 78349247103 scopus 로고    scopus 로고
    • Prion amyloid structure explains templating: how proteins can be genes
    • Wickner, R. B. et al., Prion amyloid structure explains templating: how proteins can be genes. FEMS Yeast Res., 2010, 10, 980-991.
    • (2010) FEMS Yeast Res. , vol.10 , pp. 980-991
    • Wickner, R.B.1
  • 187
    • 69949187643 scopus 로고    scopus 로고
    • Molecular mechanisms for proteinencoded inheritance
    • Wiltzius, J. J. W. et al., Molecular mechanisms for proteinencoded inheritance. Nature Struct. Mol. Biol., 2009, 16, 973-979.
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 973-979
    • Wiltzius, J.J.W.1
  • 189
    • 1842766124 scopus 로고    scopus 로고
    • Molecular basis of barriers for interspecies transmissibility of mammalian prions
    • Vanik, D. L., Surewicz, K. A. and Surewicz, W. K., Molecular basis of barriers for interspecies transmissibility of mammalian prions. Mol. Cell, 2004, 14, 139-145.
    • (2004) Mol. Cell , vol.14 , pp. 139-145
    • Vanik, D.L.1    Surewicz, K.A.2    Surewicz, W.K.3
  • 190
    • 17044381327 scopus 로고    scopus 로고
    • Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids
    • Jones, E. M. and Surewicz, W. K., Fibril conformation as the basis of species- and strain-dependent seeding specificity of mammalian prion amyloids. Cell, 2005, 121, 63-72.
    • (2005) Cell , vol.121 , pp. 63-72
    • Jones, E.M.1    Surewicz, W.K.2
  • 191
    • 0142091396 scopus 로고    scopus 로고
    • Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation
    • Kundu, B., Maiti, N. R., Jones, E. M., Surewicz, K. A., Vanik, D. L. and Surewicz, W. K., Nucleation-dependent conformational conversion of the Y145Stop variant of human prion protein: structural clues for prion propagation. Proc. Natl. Acad. Sci. USA, 2003, 100, 12069-12074.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12069-12074
    • Kundu, B.1    Maiti, N.R.2    Jones, E.M.3    Surewicz, K.A.4    Vanik, D.L.5    Surewicz, W.K.6
  • 192
    • 79953183597 scopus 로고    scopus 로고
    • Atomic structures suggest determinants of transmission barriers in mammalian prion disease
    • Apostol, M. I., Wiltzius, J. J. W., Sawaya, M. R., Cascio, D. and Eisenberg, D., Atomic structures suggest determinants of transmission barriers in mammalian prion disease. Biochemistry, 2011, 50, 2456-2463.
    • (2011) Biochemistry , vol.50 , pp. 2456-2463
    • Apostol, M.I.1    Wiltzius, J.J.W.2    Sawaya, M.R.3    Cascio, D.4    Eisenberg, D.5
  • 193
    • 34547101740 scopus 로고    scopus 로고
    • Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau
    • Aoyagi, H., Hasegawa, M. and Tamaoka, A., Fibrillogenic nuclei composed of P301L mutant tau induce elongation of P301L tau but not wild-type tau. J. Biol. Chem., 2007, 282, 20309-20318.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20309-20318
    • Aoyagi, H.1    Hasegawa, M.2    Tamaoka, A.3
  • 194
    • 63649160214 scopus 로고    scopus 로고
    • Conformational diversity of wild-type Tau fibrils specified by templated conformation change
    • Frost, B., Ollesch, J., Wille, H. and Diamond, M. I., Conformational diversity of wild-type Tau fibrils specified by templated conformation change. J. Biol. Chem., 2009, 284, 3546-3551.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3546-3551
    • Frost, B.1    Ollesch, J.2    Wille, H.3    Diamond, M.I.4
  • 195
    • 70349581486 scopus 로고    scopus 로고
    • The expanding realm of prion phenomena in neurodegenerative disease
    • Frost, B. and Diamond, M. I., The expanding realm of prion phenomena in neurodegenerative disease. Prion, 2009, 3, 74-77.
    • (2009) Prion , vol.3 , pp. 74-77
    • Frost, B.1    Diamond, M.I.2
  • 196
    • 0034657130 scopus 로고    scopus 로고
    • Evidence for seeding of beta-amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein-transgenic mice
    • Kane, M. D. et al., Evidence for seeding of beta-amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein-transgenic mice. J. Neurosci., 2000, 20, 3606-3611.
    • (2000) J. Neurosci. , vol.20 , pp. 3606-3611
    • Kane, M.D.1
  • 198
    • 0035997227 scopus 로고    scopus 로고
    • Exogenous induction of cerebral betaamyloidosis in betaAPP-transgenic mice
    • Walker, L. C., Callahan, M. J., Bian, F., Durham, R. A., Roher, A. E. and Lipinski, W. J., Exogenous induction of cerebral betaamyloidosis in betaAPP-transgenic mice. Peptides, 2002, 23, 1241-1247.
    • (2002) Peptides , vol.23 , pp. 1241-1247
    • Walker, L.C.1    Callahan, M.J.2    Bian, F.3    Durham, R.A.4    Roher, A.E.5    Lipinski, W.J.6
  • 199
    • 0036850529 scopus 로고    scopus 로고
    • Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells
    • Yang, W., Dunlap, J. R., Andrews, R. B. and Wetzel, R., Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells. Hum. Mol. Genet., 2002, 11, 2905-2917.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2905-2917
    • Yang, W.1    Dunlap, J.R.2    Andrews, R.B.3    Wetzel, R.4
  • 201
    • 56349116391 scopus 로고    scopus 로고
    • Molecular genetics of Alzheimer's disease: an update
    • Brouwers, N., Sleegers, K. and Van Broeckhoven, C., Molecular genetics of Alzheimer's disease: an update. Annu. Med., 2008, 40, 562-583.
    • (2008) Annu. Med. , vol.40 , pp. 562-583
    • Brouwers, N.1    Sleegers, K.2    Van Broeckhoven, C.3
  • 202
    • 43249110200 scopus 로고    scopus 로고
    • Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation
    • Li, J. Y. et al., Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nature Med., 2008, 14, 501-503.
    • (2008) Nature Med. , vol.14 , pp. 501-503
    • Li, J.Y.1
  • 203
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera, F. et al., Transmission and spreading of tauopathy in transgenic mouse brain. Nature Cell Biol., 2009, 11, 909-913.
    • (2009) Nature Cell Biol. , vol.11 , pp. 909-913
    • Clavaguera, F.1
  • 204
    • 69149089854 scopus 로고    scopus 로고
    • Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein
    • Desplats, P. et al., Inclusion formation and neuronal cell death through neuron-to-neuron transmission of alpha-synuclein. Proc. Natl. Acad. Sci. USA, 2009, 106, 13010-13015.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13010-13015
    • Desplats, P.1
  • 205
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B., Jacks, R. L. and Diamond, M. I., Propagation of tau misfolding from the outside to the inside of a cell. J. Biol. Chem., 2009, 284, 12845-12852.
    • (2009) J. Biol. Chem. , vol.284 , pp. 12845-12852
    • Frost, B.1    Jacks, R.L.2    Diamond, M.I.3
  • 206
    • 77149123027 scopus 로고    scopus 로고
    • GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells
    • Speare, J. O., Offerdahl, D. K., Hasenkrug, A., Carmody, A. B. and Baron, G. S., GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells. EMBO J., 2010, 29, 782-794.
    • (2010) EMBO J. , vol.29 , pp. 782-794
    • Speare, J.O.1    Offerdahl, D.K.2    Hasenkrug, A.3    Carmody, A.B.4    Baron, G.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.