메뉴 건너뛰기




Volumn 3, Issue 1, 2014, Pages 149-163

Prions and prion-like pathogens in neurodegenerative disorders

Author keywords

Alzheimer's disease; Amyloid ; Neurodegeneration; Parkinson's disease; Prion; Prion like; PrP; Tau; synuclein

Indexed keywords

AMYLOID PRECURSOR PROTEIN; SYNUCLEIN; TAU PROTEIN;

EID: 84928432153     PISSN: None     EISSN: 20760817     Source Type: Journal    
DOI: 10.3390/pathogens3010149     Document Type: Review
Times cited : (15)

References (125)
  • 1
    • 0014194776 scopus 로고
    • The possible nature of the transmissible agent of scrapie
    • Pattison, I.H.; 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
  • 2
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper, T.; Cramp, W.A.; Haig, D.A.; 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
  • 4
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of "new variant" CJD
    • Collinge, J.; Sidle, K.C.; Meads, J.; Ironside, J.; Hill, A.F. Molecular analysis of prion strain variation and the aetiology of "new variant" CJD. Nature 1996, 383, 685-690.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 5
    • 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
  • 6
    • 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
  • 10
    • 0026725538 scopus 로고
    • The phenotypic expression of different mutations in transmissible human spongiform encephalopathy
    • Brown, P. The phenotypic expression of different mutations in transmissible human spongiform encephalopathy. Rev. Neurol. 1992, 148, 317-327.
    • (1992) Rev. Neurol , vol.148 , pp. 317-327
    • Brown, P.1
  • 13
    • 0022416003 scopus 로고
    • Potential epidemic of Creutzfeldt-Jakob disease from human growth hormone therapy
    • Brown, P.; Gajdusek, D.C.; Gibbs, C.J., Jr.; Asher, D.M. Potential epidemic of Creutzfeldt-Jakob disease from human growth hormone therapy. N. Engl. J. Med. 1985, 313, 728-731.
    • (1985) N. Engl. J. Med , vol.313 , pp. 728-731
    • Brown, P.1    Gajdusek, D.C.2    Gibbs Jr., C.J.3    Asher, D.M.4
  • 15
    • 0026667331 scopus 로고
    • Friendly fire" in medicine: Hormones, homografts, and Creutzfeldt-Jakob disease
    • Brown, P.; Preece, M.A.; Will, R.G. "Friendly fire" in medicine: Hormones, homografts, and Creutzfeldt-Jakob disease. Lancet 1992, 340, 24-27.
    • (1992) Lancet , vol.340 , pp. 24-27
    • Brown, P.1    Preece, M.A.2    Will, R.G.3
  • 16
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • Peden, A.H.; Head, M.W.; Ritchie, D.L.; Bell, J.E.; Ironside, J.W. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 2004, 364,527-529.
    • (2004) Lancet , vol.364 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, J.E.4    Ironside, J.W.5
  • 19
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J.T.; Lansbury, P.T., Jr. 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
  • 21
    • 0031963428 scopus 로고    scopus 로고
    • Identification of the end stage of scrapie using infected neural grafts
    • Brandner, S.; Isenmann, S.; Kühne, G.; Aguzzi, A. Identification of the end stage of scrapie using infected neural grafts. Brain Pathol. 1998, 8, 19-27.
    • (1998) Brain Pathol , vol.8 , pp. 19-27
    • Brandner, S.1    Isenmann, S.2    Kühne, G.3    Aguzzi, A.4
  • 22
    • 0027982241 scopus 로고
    • Correlative light and electron microscopy studies of PrP localisation in 87V scrapie
    • Jeffrey, M.; Goodsir, C.M.; Bruce, M.; McBride, P.A.; Scott, J.R.; Halliday, W.G. Correlative light and electron microscopy studies of PrP localisation in 87V scrapie. Brain Res. 1994, 656, 329-343.
    • (1994) Brain Res , vol.656 , pp. 329-343
    • Jeffrey, M.1    Goodsir, C.M.2    Bruce, M.3    McBride, P.A.4    Scott, J.R.5    Halliday, W.G.6
  • 28
    • 36049020231 scopus 로고    scopus 로고
    • A general model of prion strains and their pathogenicity
    • Collinge, J.; Clarke, A.R. A general model of prion strains and their pathogenicity. Science 2007, 318, 930-936.
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 31
    • 71549169557 scopus 로고    scopus 로고
    • Neurodegeneration. Could they all be prion diseases?
    • Miller, G. Neurodegeneration. Could they all be prion diseases? Science 2009, 326, 1337-1339.
    • (2009) Science , vol.326 , pp. 1337-1339
    • Miller, G.1
  • 32
    • 84862620376 scopus 로고    scopus 로고
    • Cell biology. A unifying role for prions in neurodegenerative diseases
    • Prusiner, S.B. Cell biology. A unifying role for prions in neurodegenerative diseases. Science 2012, 336, 1511-1513.
    • (2012) Science , vol.336 , pp. 1511-1513
    • Prusiner, S.B.1
  • 33
    • 84884669084 scopus 로고    scopus 로고
    • Pathophysiology and treatment of systemic amyloidosis
    • Gillmore, J.D.; Hawkins, P.N. Pathophysiology and treatment of systemic amyloidosis. Nat. Rev. Nephrol. 2013, 9, 574-586.
    • (2013) Nat. Rev. Nephrol , vol.9 , pp. 574-586
    • Gillmore, J.D.1    Hawkins, P.N.2
  • 38
    • 77951060145 scopus 로고    scopus 로고
    • Proteases and proteolysis in Alzheimer disease: A multifactorial view on the disease process
    • De Strooper, B. Proteases and proteolysis in Alzheimer disease: A multifactorial view on the disease process. Physiol. Rev. 2010, 90, 465-494.
    • (2010) Physiol. Rev , vol.90 , pp. 465-494
    • de Strooper, B.1
  • 39
    • 84877980134 scopus 로고    scopus 로고
    • Abnormal hyperphosphorylation of tau: Sites; regulation; and molecular mechanism of neurofibrillary degeneration
    • Wang, J.Z.; Xia, Y.Y.; Grundke-Iqbal, I.; Iqbal, K. Abnormal hyperphosphorylation of tau: Sites; regulation; and molecular mechanism of neurofibrillary degeneration. J. Alzheimers Dis. 2013, 33, S123-S139.
    • (2013) J. Alzheimers Dis , vol.33
    • Wang, J.Z.1    Xia, Y.Y.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 40
    • 0021338217 scopus 로고
    • Phosphorylation affects the ability of tau protein to promote microtubule assembly
    • Lindwall, G.; Cole, R.D. Phosphorylation affects the ability of tau protein to promote microtubule assembly. J. Biol. Chem. 1984, 259, 5301-5305.
    • (1984) J. Biol. Chem , vol.259 , pp. 5301-5305
    • Lindwall, G.1    Cole, R.D.2
  • 41
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D.N.; Hyman, A.A.; Cobb, M.H.; Kirschner, M.W. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell 1992, 3, 1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 42
    • 77953675879 scopus 로고    scopus 로고
    • Probing the biology of Alzheimer's disease in mice
    • Ashe, K.H.; Zahs, K.R. Probing the biology of Alzheimer's disease in mice. Neuron 2010, 66, 631-645.
    • (2010) Neuron , vol.66 , pp. 631-645
    • Ashe, K.H.1    Zahs, K.R.2
  • 43
    • 0025863618 scopus 로고
    • Neuropathological stageing of Alzheimer-related changes
    • Braak, H.; Braak, E. Neuropathological stageing of Alzheimer-related changes. Acta Neuropathol. 1991, 82, 239-259.
    • (1991) Acta Neuropathol , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 44
    • 0027363383 scopus 로고
    • Evidence for the experimental transmission of cerebral beta-amyloidosis to primates
    • Baker, H.F.; Ridley, R.M.; Duchen, L.W.; Crow, T.J.; Bruton, C.J. Evidence for the experimental transmission of cerebral beta-amyloidosis to primates. Int. J. Exp. Pathol. 1993, 74, 441-454.
    • (1993) Int. J. Exp. Pathol , vol.74 , pp. 441-454
    • Baker, H.F.1    Ridley, R.M.2    Duchen, L.W.3    Crow, T.J.4    Bruton, C.J.5
  • 45
    • 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.; Lipinski, W.J.; Callahan, M.J.; Bian, F.; Durham, R.A.; Schwarz, R.D.; Roher, A.E.; Walker, L.C. 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    Lipinski, W.J.2    Callahan, M.J.3    Bian, F.4    Durham, R.A.5    Schwarz, R.D.6    Roher, A.E.7    Walker, L.C.8
  • 46
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J.; Selkoe, D.J. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 2002, 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 48
    • 80054024011 scopus 로고    scopus 로고
    • Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
    • Jucker, M.; Walker, L.C. Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders. Ann. Neurol. 2011, 70, 532-540.
    • (2011) Ann. Neurol , vol.70 , pp. 532-540
    • Jucker, M.1    Walker, L.C.2
  • 56
    • 78049283756 scopus 로고    scopus 로고
    • Transsynaptic progression of amyloid-β-induced neuronal dysfunction within the entorhinal-hippocampal network
    • Harris, J.A.; Devidze, N.; Verret, L.; Ho, K.; Halabisky, B.; Thwin, M.T.; Kim, D.; Hamto, P.; Lo, I.; Yu, G.Q. et al. Transsynaptic progression of amyloid-β-induced neuronal dysfunction within the entorhinal-hippocampal network. Neuron 2010, 68, 428-441.
    • (2010) Neuron , vol.68 , pp. 428-441
    • Harris, J.A.1    Devidze, N.2    Verret, L.3    Ho, K.4    Halabisky, B.5    Thwin, M.T.6    Kim, D.7    Hamto, P.8    Lo, I.9    Yu, G.Q.10
  • 58
    • 67649273927 scopus 로고    scopus 로고
    • Propagation of tau misfolding from the outside to the inside of a cell
    • Frost, B.; Jacks, R.L.; 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
  • 61
    • 34347257068 scopus 로고    scopus 로고
    • Increased Abeta production leads to intracellular accumulation of Abeta in flotillin-1-positive endosomes
    • Rajendran, L.; Knobloch, M.; Geiger, K.D.; Dienel, S.; Nitsch, R.; Simons, K.; Konietzko, U. Increased Abeta production leads to intracellular accumulation of Abeta in flotillin-1-positive endosomes. Neurodegener. Dis. 2007, 4, 164-170.
    • (2007) Neurodegener. Dis , vol.4 , pp. 164-170
    • Rajendran, L.1    Knobloch, M.2    Geiger, K.D.3    Dienel, S.4    Nitsch, R.5    Simons, K.6    Konietzko, U.7
  • 62
    • 33947709328 scopus 로고    scopus 로고
    • Packaging of prions into exosomes is associated with a novel pathway of PrP processing
    • Vella, L.J.; Sharples, R.A.; Lawson, V.A.; Masters, C.L.; Cappai, R.; Hill, A.F. Packaging of prions into exosomes is associated with a novel pathway of PrP processing. J. Pathol. 2007, 211, 582-590.
    • (2007) J. Pathol , vol.211 , pp. 582-590
    • Vella, L.J.1    Sharples, R.A.2    Lawson, V.A.3    Masters, C.L.4    Cappai, R.5    Hill, A.F.6
  • 63
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles; bicelles; and rodlike micelles
    • Georgieva, E.R.; Ramlall, T.F.; Borbat, P.P.; Freed, J.H.; Eliezer, D. Membrane-bound alpha-synuclein forms an extended helix: Long-distance pulsed ESR measurements using vesicles; bicelles; and rodlike micelles. J. Am. Chem. Soc. 2008, 130, 12856-12857.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 65
    • 57249089081 scopus 로고    scopus 로고
    • Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy
    • Veith, N.M.; Plattner, H.; Stuermer, C.A.; Schulz-Schaeffer, W.J.; Bürkle, A. Immunolocalisation of PrPSc in scrapie-infected N2a mouse neuroblastoma cells by light and electron microscopy. Eur. J. Cell Biol. 2009, 88, 45-63.
    • (2009) Eur. J. Cell Biol , vol.88 , pp. 45-63
    • Veith, N.M.1    Plattner, H.2    Stuermer, C.A.3    Schulz-Schaeffer, W.J.4    Bürkle, A.5
  • 67
    • 80052398365 scopus 로고    scopus 로고
    • α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels, T.; Choi, J.G.; Selkoe, D.J. α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 2011, 477, 107-110.
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 69
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes, R.; Spillantini, M.G.; Goedert, M. Identification of two distinct synucleins from human brain. FEBS Lett. 1994, 345, 27-32.
    • (1994) FEBS Lett , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 72
    • 65549150887 scopus 로고    scopus 로고
    • Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant
    • Yonetani, M.; Nonaka, T.; Masuda, M.; Inukai, Y.; Oikawa, T.; Hisanaga, S.; Hasegawa, M. Conversion of wild-type alpha-synuclein into mutant-type fibrils and its propagation in the presence of A30P mutant. J. Biol. Chem. 2009, 284, 7940-7950.
    • (2009) J. Biol. Chem , vol.284 , pp. 7940-7950
    • Yonetani, M.1    Nonaka, T.2    Masuda, M.3    Inukai, Y.4    Oikawa, T.5    Hisanaga, S.6    Hasegawa, M.7
  • 74
    • 52449117926 scopus 로고    scopus 로고
    • Research in motion: The enigma of Parkinson's disease pathology spread
    • Brundin, P.; Li, J.Y.; Holton, J.L.; Lindvall, O.; Revesz, T. Research in motion: The enigma of Parkinson's disease pathology spread. Nat. Rev. Neurosci. 2008, 9, 741-745.
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 741-745
    • Brundin, P.1    Li, J.Y.2    Holton, J.L.3    Lindvall, O.4    Revesz, T.5
  • 75
    • 21344456506 scopus 로고    scopus 로고
    • Intravesicular localization and exocytosis of alpha-synuclein and its aggregates
    • Lee, H.J.; Patel, S.; Lee, S.J. Intravesicular localization and exocytosis of alpha-synuclein and its aggregates. J. Neurosci. 2005, 25, 6016-6024.
    • (2005) J. Neurosci , vol.25 , pp. 6016-6024
    • Lee, H.J.1    Patel, S.2    Lee, S.J.3
  • 76
    • 40749094842 scopus 로고    scopus 로고
    • Origins and effects of extracellular alpha-synuclein: Implications in Parkinson's disease
    • Lee, S.J. Origins and effects of extracellular alpha-synuclein: Implications in Parkinson's disease. J. Mol. Neurosci. 2008, 34, 17-22.
    • (2008) J. Mol. Neurosci , vol.34 , pp. 17-22
    • Lee, S.J.1
  • 77
    • 70349223775 scopus 로고    scopus 로고
    • Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology
    • Danzer, K.M.; Krebs, S.K.; Wolff, M.; Birk, G.; Hengerer, B. Seeding induced by alpha-synuclein oligomers provides evidence for spreading of alpha-synuclein pathology. J. Neurochem. 2009, 111, 192-203.
    • (2009) J. Neurochem , vol.111 , pp. 192-203
    • Danzer, K.M.1    Krebs, S.K.2    Wolff, M.3    Birk, G.4    Hengerer, B.5
  • 80
    • 84862609075 scopus 로고    scopus 로고
    • Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice
    • Luk, K.C.; Kehm, V.M.; Zhang, B.; O'Brien, P.; Trojanowski, J.Q.; Lee, V.M. Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice. J. Exp. Med. 2012, 209, 975-986.
    • (2012) J. Exp. Med , vol.209 , pp. 975-986
    • Luk, K.C.1    Kehm, V.M.2    Zhang, B.3    O'Brien, P.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 81
    • 84869109864 scopus 로고    scopus 로고
    • Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice
    • Luk, K.C.; Kehm, V.; Carroll, J.; Zhang, B.; O'Brien, P.; Trojanowski, J.Q.; Lee, V.M. Pathological α-synuclein transmission initiates Parkinson-like neurodegeneration in nontransgenic mice. Science 2012, 338, 949-953.
    • (2012) Science , vol.338 , pp. 949-953
    • Luk, K.C.1    Kehm, V.2    Carroll, J.3    Zhang, B.4    O'Brien, P.5    Trojanowski, J.Q.6    Lee, V.M.7
  • 85
    • 43249114934 scopus 로고    scopus 로고
    • Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease
    • Kordower, J.H.; Chu, Y.; Hauser, R.A.; Freeman, T.B.; Olanow, C.W. Lewy body-like pathology in long-term embryonic nigral transplants in Parkinson's disease. Nat. Med. 2008, 14, 504-550.
    • (2008) Nat. Med , vol.14 , pp. 504-550
    • Kordower, J.H.1    Chu, Y.2    Hauser, R.A.3    Freeman, T.B.4    Olanow, C.W.5
  • 87
    • 59649095699 scopus 로고    scopus 로고
    • Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates
    • Ren, P.H.; Lauckner, J.E.; Kachirskaia, I.; Heuser, J.E.; Melki, R.; Kopito, R.R. Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat. Cell Biol. 2009, 11, 219-225.
    • (2009) Nat. Cell Biol , vol.11 , pp. 219-225
    • Ren, P.H.1    Lauckner, J.E.2    Kachirskaia, I.3    Heuser, J.E.4    Melki, R.5    Kopito, R.R.6
  • 88
    • 84876945450 scopus 로고    scopus 로고
    • The cell biology of prion-like spread of protein aggregates: Mechanisms and implication in neurodegeneration
    • Costanzo, M.; Zurzolo, C. The cell biology of prion-like spread of protein aggregates: Mechanisms and implication in neurodegeneration. Biochem. J. 2013, 452, 1-17.
    • (2013) Biochem. J , vol.452 , pp. 1-17
    • Costanzo, M.1    Zurzolo, C.2
  • 89
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D.; Jucker, M. The amyloid state of proteins in human diseases. Cell 2012, 148, 1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 90
    • 0141514771 scopus 로고    scopus 로고
    • Sporadic and familial CJD: Classification and characterisation
    • Gambetti, P.; Kong, Q.; Zou, W.; Parchi, P.; Chen, S.G. Sporadic and familial CJD: Classification and characterisation. Br. Med. Bull. 2003, 66, 213-239.
    • (2003) Br. Med. Bull , vol.66 , pp. 213-239
    • Gambetti, P.1    Kong, Q.2    Zou, W.3    Parchi, P.4    Chen, S.G.5
  • 92
    • 77949300796 scopus 로고    scopus 로고
    • 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: A phase 2; double-blind; placebo-controlled; ascending-dose study
    • Rinne, J.O.; Brooks, D.J.; Rossor, M.N.; Fox, N.C.; Bullock, R.; Klunk, W.E.; Mathis, C.A.; Blennow, K.; Barakos, J.; Okello, A.A. et al. 11C-PiB PET assessment of change in fibrillar amyloid-beta load in patients with Alzheimer's disease treated with bapineuzumab: A phase 2; double-blind; placebo-controlled; ascending-dose study. Lancet Neurol. 2010, 9, 363-372.
    • (2010) Lancet Neurol , vol.9 , pp. 363-372
    • Rinne, J.O.1    Brooks, D.J.2    Rossor, M.N.3    Fox, N.C.4    Bullock, R.5    Klunk, W.E.6    Mathis, C.A.7    Blennow, K.8    Barakos, J.9    Okello, A.A.10
  • 94
    • 84874639389 scopus 로고    scopus 로고
    • Molecular structures of amyloid and prion fibrils: Consensus versus controversy
    • Tycko, R.; Wickner, R.B. Molecular structures of amyloid and prion fibrils: Consensus versus controversy. Acc. Chem. Res. 2013, 46, 1487-1496.
    • (2013) Acc. Chem. Res , vol.46 , pp. 1487-1496
    • Tycko, R.1    Wickner, R.B.2
  • 95
    • 0034681471 scopus 로고    scopus 로고
    • Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders
    • Masliah, E.; Rockenstein, E.; Veinbergs, I.; Mallory, M.; Hashimoto, M.; Takeda, A.; Sagara, Y.; Sisk, A.; Mucke, L. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: Implications for neurodegenerative disorders. Science 2000, 287, 1265-1269.
    • (2000) Science , vol.287 , pp. 1265-1269
    • Masliah, E.1    Rockenstein, E.2    Veinbergs, I.3    Mallory, M.4    Hashimoto, M.5    Takeda, A.6    Sagara, Y.7    Sisk, A.8    Mucke, L.9
  • 99
    • 38949208262 scopus 로고    scopus 로고
    • Plaque-bearing mice with reduced levels of oligomeric amyloid-beta assemblies have intact memory function
    • Lesné, S.; Kotilinek, L.; Ashe, K.H. Plaque-bearing mice with reduced levels of oligomeric amyloid-beta assemblies have intact memory function. Neuroscience 2008, 151, 745-749.
    • (2008) Neuroscience , vol.151 , pp. 745-749
    • Lesné, S.1    Kotilinek, L.2    Ashe, K.H.3
  • 101
    • 79952167224 scopus 로고    scopus 로고
    • Prion propagation and toxicity in vivo occur in two distinct mechanistic phases
    • Sandberg, M.K.; Al-Doujaily, H.; Sharps, B.; Clarke, A.R.; 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
  • 102
    • 0025681138 scopus 로고
    • Spontaneous neurodegeneration in transgenic mice with mutant prion protein
    • Hsiao, K.K.; Scott, M.; Foster, D.; Groth, D.F.; DeArmond, S.J.; Prusiner, S.B. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 1990, 250, 1587-1590.
    • (1990) Science , vol.250 , pp. 1587-1590
    • Hsiao, K.K.1    Scott, M.2    Foster, D.3    Groth, D.F.4    Dearmond, S.J.5    Prusiner, S.B.6
  • 103
    • 18444386197 scopus 로고    scopus 로고
    • A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration
    • Watase, K.; Weeber, E.J.; Xu, B.; Antalffy, B.; Yuva-Paylor, L.; Hashimoto, K.; Kano, M.; Atkinson, R.; Sun, Y.; Armstrong, D.L. et al. A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration. Neuron 2002, 34, 905-919.
    • (2002) Neuron , vol.34 , pp. 905-919
    • Watase, K.1    Weeber, E.J.2    Xu, B.3    Antalffy, B.4    Yuva-Paylor, L.5    Hashimoto, K.6    Kano, M.7    Atkinson, R.8    Sun, Y.9    Armstrong, D.L.10
  • 108
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • Mallucci, G.R.; Ratté, S.; Asante, E.A.; Linehan, J.; Gowland, I.; Jefferys, J.G.; Collinge, J. Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 2002, 21, 202-210.
    • (2002) EMBO J , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratté, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5    Jefferys, J.G.6    Collinge, J.7
  • 112
    • 47949104726 scopus 로고    scopus 로고
    • Stress-protective signalling of prion protein is corrupted by scrapie prions
    • Rambold, A.S.; Müller, V.; Ron, U.; Ben-Tal, N.; Winklhofer, K.F.; Tatzelt, J. Stress-protective signalling of prion protein is corrupted by scrapie prions. EMBO J. 2008, 27, 1974-1984.
    • (2008) EMBO J , vol.27 , pp. 1974-1984
    • Rambold, A.S.1    Müller, V.2    Ron, U.3    Ben-Tal, N.4    Winklhofer, K.F.5    Tatzelt, J.6
  • 114
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Laurén, J.; Gimbel, D.A.; Nygaard, H.B.; Gilbert, J.W.; Strittmatter, S.M. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 2009, 457, 1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 120
    • 2442711560 scopus 로고    scopus 로고
    • Fyn kinase modulates synaptotoxicity; but not aberrant sprouting; in human amyloid precursor protein transgenic mice
    • Chin, J.; Palop, J.J.; Yu, G.Q.; Kojima, N.; Masliah, E.; Mucke, L. Fyn kinase modulates synaptotoxicity; but not aberrant sprouting; in human amyloid precursor protein transgenic mice. J. Neurosci. 2004, 24, 4692-4697.
    • (2004) J. Neurosci , vol.24 , pp. 4692-4697
    • Chin, J.1    Palop, J.J.2    Yu, G.Q.3    Kojima, N.4    Masliah, E.5    Mucke, L.6
  • 122
    • 33947314641 scopus 로고    scopus 로고
    • Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway
    • Shankar, G.M.; Bloodgood, B.L.; Townsend, M.; Walsh, D.M.; Selkoe, D.J.; Sabatini, B. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J. Neurosci. 2007, 27, 2866-2875.
    • (2007) J. Neurosci , vol.27 , pp. 2866-2875
    • Shankar, G.M.1    Bloodgood, B.L.2    Townsend, M.3    Walsh, D.M.4    Selkoe, D.J.5    Sabatini, B.6
  • 125
    • 77956965281 scopus 로고    scopus 로고
    • Prion protein in Alzheimer's pathogenesis: A hot and controversial issue
    • Benilova, I.; de Strooper, B. Prion protein in Alzheimer's pathogenesis: A hot and controversial issue. EMBO Mol. Med. 2010, 2, 289-290.
    • (2010) EMBO Mol. Med , vol.2 , pp. 289-290
    • Benilova, I.1    de Strooper, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.