메뉴 건너뛰기




Volumn 28, Issue 4, 2008, Pages 351-365

What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?

Author keywords

Cellular inclusion; Disease pathogenesis; Gene mutation; Molecular composition; Neurodegenerative disease; Protein aggregate

Indexed keywords

AMYLOID BETA PROTEIN; PRION PROTEIN; SYNUCLEIN;

EID: 44849083256     PISSN: 09196544     EISSN: 14401789     Source Type: Journal    
DOI: 10.1111/j.1440-1789.2008.00916.x     Document Type: Review
Times cited : (49)

References (151)
  • 1
    • 0031128758 scopus 로고    scopus 로고
    • Rediscovery of the case described by Alois Alzheimer in 1911: Historical, histological and molecular genetic analysis
    • Graeber MB, Kosel S, Egensperger R et al. Rediscovery of the case described by Alois Alzheimer in 1911: historical, histological and molecular genetic analysis. Neurogenetics 1997 1:73 80.
    • (1997) Neurogenetics , vol.1 , pp. 73-80
    • Graeber, M.B.1    Kosel, S.2    Egensperger, R.3
  • 2
    • 0141989061 scopus 로고    scopus 로고
    • The Lewy body variant of Alzheimer's disease: Clinical, pathophysiological and conceptual issues
    • Forstl H. The Lewy body variant of Alzheimer's disease: clinical, pathophysiological and conceptual issues. Eur Arch Psych Clin Neurol 1999 249:64 67.
    • (1999) Eur Arch Psych Clin Neurol , vol.249 , pp. 64-67
    • Forstl, H.1
  • 3
    • 0032866655 scopus 로고    scopus 로고
    • Origins of the Creutzfeldt and Jakob concept
    • Duckett S, Stern J. Origins of the Creutzfeldt and Jakob concept. J Hist Neurosci 1999 8:21 34.
    • (1999) J Hist Neurosci , vol.8 , pp. 21-34
    • Duckett, S.1    Stern, J.2
  • 5
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984 122:1131 1135.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 6
    • 0029824332 scopus 로고    scopus 로고
    • Polymorphism at codon 129 of the prion protein gene determines cerebellar pathology in Creutzfeldt-Jakob disease
    • Schulz-Schaeffer WJ, Giese A, Windl O, Kretschmar HA. Polymorphism at codon 129 of the prion protein gene determines cerebellar pathology in Creutzfeldt-Jakob disease. Clin Neuropathol 1996 15:353 357.
    • (1996) Clin Neuropathol , vol.15 , pp. 353-357
    • Schulz-Schaeffer, W.J.1    Giese, A.2    Windl, O.3    Kretschmar, H.A.4
  • 7
    • 0006164301 scopus 로고    scopus 로고
    • Consensus guidelines for the clinical and pathological diagnosis of dementia with Lewy bodies (DLB): Report of the consortium on DLB international workshop
    • McKeith IG, Galasko D, Kosaka K et al. Consensus guidelines for the clinical and pathological diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop. Neurology 1996 47:1113 1124.
    • (1996) Neurology , vol.47 , pp. 1113-1124
    • McKeith, I.G.1    Galasko, D.2    Kosaka, K.3
  • 8
    • 0023917701 scopus 로고
    • Ubiquitin and tau immunoreactivity of neurofibrillary tangles, Pick bodies and Lewy bodies
    • Love S, Saitoh T, Quijada S, Cole GM, Terry RD. Ubiquitin and tau immunoreactivity of neurofibrillary tangles, Pick bodies and Lewy bodies. J Neuropathol Exp Neurol 1988 47:393 405.
    • (1988) J Neuropathol Exp Neurol , vol.47 , pp. 393-405
    • Love, S.1    Saitoh, T.2    Quijada, S.3    Cole, G.M.4    Terry, R.D.5
  • 9
    • 0030809074 scopus 로고    scopus 로고
    • Basic pathology of corticobasal degeneration
    • Ikeda K. Basic pathology of corticobasal degeneration. Neuropathology 1997 17:127 133.
    • (1997) Neuropathology , vol.17 , pp. 127-133
    • Ikeda, K.1
  • 10
    • 0028339722 scopus 로고
    • The distribution of oligodendroglial inclusions in multiple system atrophy and its relevance to clinical symptomology
    • Papp MI, Lantos PL. The distribution of oligodendroglial inclusions in multiple system atrophy and its relevance to clinical symptomology. Brain 1994 117:235 243.
    • (1994) Brain , vol.117 , pp. 235-243
    • Papp, M.I.1    Lantos, P.L.2
  • 11
    • 0026075602 scopus 로고
    • Early onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene
    • Chartier-Harlin M, Crawford F, Houlden H et al. Early onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene. Nature 1991 353:844 846.
    • (1991) Nature , vol.353 , pp. 844-846
    • Chartier-Harlin, M.1    Crawford, F.2    Houlden, H.3
  • 12
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • Goate R, Chartier-Harlin M, Mullan M et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 1991 349:704 706.
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, R.1    Chartier-Harlin, M.2    Mullan, M.3
  • 13
    • 0029004341 scopus 로고
    • Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease
    • Sherrington R, Rogaev EI, Liang Y et al. Cloning of a gene bearing missense mutations in early onset familial Alzheimer's disease. Nature 1993 375:754 760.
    • (1993) Nature , vol.375 , pp. 754-760
    • Sherrington, R.1    Rogaev, E.I.2    Liang, Y.3
  • 14
    • 0029087026 scopus 로고
    • Candidate gene for chromosome 1 familial Alzheimer's disease locus
    • Levy-Lahad E, Wasco W, Poorkaj P et al. Candidate gene for chromosome 1 familial Alzheimer's disease locus. Science 1995 269:973 977.
    • (1995) Science , vol.269 , pp. 973-977
    • Levy-Lahad, E.1    Wasco, W.2    Poorkaj, P.3
  • 17
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • West AB, Moore DJ, Biskup S et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc Natl Acad Sci USA 2005 102:16842 16847.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16842-16847
    • West, A.B.1    Moore, D.J.2    Biskup, S.3
  • 18
    • 2942689352 scopus 로고    scopus 로고
    • Pathological properties of the Parkinson's disease-associated protein DJ-1 in alpha-synucleinopathies and tauopathies: Relevance for multiple system atrophy and Parkinson's disease
    • Neumann M, Muller V, Gorner K, Kretzschmar HA, Haass C, Kahle PJ. Pathological properties of the Parkinson's disease-associated protein DJ-1 in alpha-synucleinopathies and tauopathies: relevance for multiple system atrophy and Parkinson's disease. Acta Neuropathol 2004 107:489 496.
    • (2004) Acta Neuropathol , vol.107 , pp. 489-496
    • Neumann, M.1    Muller, V.2    Gorner, K.3    Kretzschmar, H.A.4    Haass, C.5    Kahle, P.J.6
  • 19
    • 0026572346 scopus 로고
    • Comparison of the severity of neuropathological changes in familial and sporadic Alzheimer's disease
    • Haupt M, Kurz A, Pollman S, Romero B. Comparison of the severity of neuropathological changes in familial and sporadic Alzheimer's disease. J Neurol 1992 239:248 250.
    • (1992) J Neurol , vol.239 , pp. 248-250
    • Haupt, M.1    Kurz, A.2    Pollman, S.3    Romero, B.4
  • 20
    • 0027438964 scopus 로고
    • Comparison of the severity of neuropathological changes in familial and sporadic Alzheimer's disease
    • Nochlin D, Van Belle G, Bird TD, Sumi SM. Comparison of the severity of neuropathological changes in familial and sporadic Alzheimer's disease. Alzheimer Dis Assoc Disord 1993 7:212 222.
    • (1993) Alzheimer Dis Assoc Disord , vol.7 , pp. 212-222
    • Nochlin, D.1    Van Belle, G.2    Bird, T.D.3    Sumi, S.M.4
  • 21
    • 0026597063 scopus 로고
    • Alzheimer's disease: The amyloid cascade hypothesis
    • Hardy JA, Higgins GA. Alzheimer's disease: the amyloid cascade hypothesis. Science 1992 256:184 185.
    • (1992) Science , vol.256 , pp. 184-185
    • Hardy, J.A.1    Higgins, G.A.2
  • 22
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • Miller DL, Papayannopoulos IA, Styles J et al. Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease. Arch Biochem Biophys 1993 301:41 52.
    • (1993) Arch Biochem Biophys , vol.301 , pp. 41-52
    • Miller, D.L.1    Papayannopoulos, I.A.2    Styles, J.3
  • 23
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • Roher AE, Lowenson JD, Clarke S et al. Structural alterations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 1993 268:3072 3073.
    • (1993) J Biol Chem , vol.268 , pp. 3072-3073
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3
  • 24
    • 0028080483 scopus 로고
    • Presence of apolipoprotein e on extracellular neurofibrillary tangles and on meningeal blood vessels precedes the Alzheimer β-amyloid deposition
    • Yamaguchi H, Ishiguro K, Sugihara S et al. Presence of apolipoprotein e on extracellular neurofibrillary tangles and on meningeal blood vessels precedes the Alzheimer β-amyloid deposition. Acta Neuropathol 1994 88:413 419.
    • (1994) Acta Neuropathol , vol.88 , pp. 413-419
    • Yamaguchi, H.1    Ishiguro, K.2    Sugihara, S.3
  • 25
    • 26944432332 scopus 로고    scopus 로고
    • Apolipoprotein D is a component of compact but not diffuse amyloid-beta plaques in Alzheimer's disease temporal cortex
    • Desai PP, Ikonomovic MD, Abrahamson EE et al. Apolipoprotein D is a component of compact but not diffuse amyloid-beta plaques in Alzheimer's disease temporal cortex. Neurobiol Dis 2005 20:574 582.
    • (2005) Neurobiol Dis , vol.20 , pp. 574-582
    • Desai, P.P.1    Ikonomovic, M.D.2    Abrahamson, E.E.3
  • 27
    • 0025905505 scopus 로고
    • Comparative epitope analysis of neuronal cytoskeletal proteins in Alzheimer's disease senile plaque neurites and neuropil threads
    • Schmidt ML, Lee VMY, Trojanowski JQ. Comparative epitope analysis of neuronal cytoskeletal proteins in Alzheimer's disease senile plaque neurites and neuropil threads. Lab Invest 1991 64:352 357.
    • (1991) Lab Invest , vol.64 , pp. 352-357
    • Schmidt, M.L.1    Lee, V.M.Y.2    Trojanowski, J.Q.3
  • 28
    • 0027583951 scopus 로고
    • Microglia and immune activation in Alzheimer's disease
    • Krzanowski JJ. Microglia and immune activation in Alzheimer's disease. J Flor MA 1993 80:267 270.
    • (1993) J Flor MA , vol.80 , pp. 267-270
    • Krzanowski, J.J.1
  • 29
    • 0025875076 scopus 로고
    • Association of amyloid-P component with complement proteins in neurologically diseases brain tissue
    • Akiyama H, Yamada T, Kawanata T, McGeer PL. Association of amyloid-P component with complement proteins in neurologically diseases brain tissue. Brain Res 1991 548:349 352.
    • (1991) Brain Res , vol.548 , pp. 349-352
    • Akiyama, H.1    Yamada, T.2    Kawanata, T.3    McGeer, P.L.4
  • 30
    • 0028134049 scopus 로고
    • Amyloid-P component like immunoreactivity in β/A4-immunoreactive deposits in Alzheimer-type dementia brains
    • Kimura M, Arai H, Takahashi T, Iwamoto N. Amyloid-P component like immunoreactivity in β/A4-immunoreactive deposits in Alzheimer-type dementia brains. J Neurol 1994 241:170 174.
    • (1994) J Neurol , vol.241 , pp. 170-174
    • Kimura, M.1    Arai, H.2    Takahashi, T.3    Iwamoto, N.4
  • 31
    • 0027332522 scopus 로고
    • β-amyloid accumulation in aged canine brain: A model of early plaque formation in Alzheimer's disease
    • Cummings BJ, Su JH, Cotman CW, White R, Russell MJ. β-amyloid accumulation in aged canine brain: a model of early plaque formation in Alzheimer's disease. Neurobiol Aging 1993 14:547 560.
    • (1993) Neurobiol Aging , vol.14 , pp. 547-560
    • Cummings, B.J.1    Su, J.H.2    Cotman, C.W.3    White, R.4    Russell, M.J.5
  • 32
    • 0024420582 scopus 로고
    • Alzheimer's and Down's patients: Cerebral preamyloid deposits differ ultrastructurally and histochemically from the amyloid of senile plaques
    • Verga L, Frangione B, Tagliavini F, Giaccone G, Migheli A, Bugiani O. Alzheimer's and Down's patients: cerebral preamyloid deposits differ ultrastructurally and histochemically from the amyloid of senile plaques. Neurosci Lett 1989 105:294 299.
    • (1989) Neurosci Lett , vol.105 , pp. 294-299
    • Verga, L.1    Frangione, B.2    Tagliavini, F.3    Giaccone, G.4    Migheli, A.5    Bugiani, O.6
  • 34
    • 0025977827 scopus 로고
    • Ultrastructural localisation of β, tau and ubiquitin epitopes in extracellular neurofibrillary tangles
    • Tabaton M, Cammarata S, Mancardi G et al. Ultrastructural localisation of β, tau and ubiquitin epitopes in extracellular neurofibrillary tangles. Proc Natl Acad Sci USA 1991 88:2098 2102.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2098-2102
    • Tabaton, M.1    Cammarata, S.2    Mancardi, G.3
  • 35
    • 0028233977 scopus 로고
    • Advanced Maillard reaction end products are associated with Alzheimer disease pathology
    • Smith MA, Taneda S, Richey PL. et al. Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proc Natl Acad Sci USA 1994 91:5710 5714.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5710-5714
    • Smith, M.A.1    Taneda, S.2    Richey, P.L.3
  • 36
    • 4444347376 scopus 로고    scopus 로고
    • Staging of agyrophilic grains: An age-associated tauopathy
    • Saito Y, Ruberu NN, Sawabe M et al. Staging of agyrophilic grains: an age-associated tauopathy. J Neuropathol Exp Neurol 2004 63:911 918.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 911-918
    • Saito, Y.1    Ruberu, N.N.2    Sawabe, M.3
  • 37
    • 0027228226 scopus 로고
    • Differential incorporation of processes derived from different classes of neurons into senile plaques in Alzheimer's disease
    • Adams LA, Munoz DG. Differential incorporation of processes derived from different classes of neurons into senile plaques in Alzheimer's disease. Acta Neuropathol 1993 86:365 370.
    • (1993) Acta Neuropathol , vol.86 , pp. 365-370
    • Adams, L.A.1    Munoz, D.G.2
  • 39
    • 4344661358 scopus 로고    scopus 로고
    • Selective PrP-like protein, doppel immunoreactivity in dystrophic neurites of senile plaques in Alzheimer's disease
    • Ferrer I, Freixas M, Blanco R, Carmona M, Puig B. Selective PrP-like protein, doppel immunoreactivity in dystrophic neurites of senile plaques in Alzheimer's disease. Neuropathol Appl Neurobiol 2004 30:329 337.
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 329-337
    • Ferrer, I.1    Freixas, M.2    Blanco, R.3    Carmona, M.4    Puig, B.5
  • 40
    • 0036224884 scopus 로고    scopus 로고
    • Quantification of vacuolation ("spongiform change"), surviving neurones and prion protein deposition in eleven cases of variant Creutzfeldt-Jakob disease
    • Armstrong RA, Cairns NJ, Ironside JW, Lantos PL. Quantification of vacuolation ("spongiform change"), surviving neurones and prion protein deposition in eleven cases of variant Creutzfeldt-Jakob disease. Neuropathol Appl Neurobiol 2002 28:129 135.
    • (2002) Neuropathol Appl Neurobiol , vol.28 , pp. 129-135
    • Armstrong, R.A.1    Cairns, N.J.2    Ironside, J.W.3    Lantos, P.L.4
  • 41
    • 0141625979 scopus 로고    scopus 로고
    • Differences in the density and distribution of florid and diffuse plaques in variant Creutzfeldt-Jakob disease (vCJD)
    • Armstrong RA, Lantos PL, Ironside JW, Cairns NJ. Differences in the density and distribution of florid and diffuse plaques in variant Creutzfeldt-Jakob disease (vCJD). Clin Neuropathol 2003 22:209 214.
    • (2003) Clin Neuropathol , vol.22 , pp. 209-214
    • Armstrong, R.A.1    Lantos, P.L.2    Ironside, J.W.3    Cairns, N.J.4
  • 42
    • 0037728592 scopus 로고    scopus 로고
    • Different chromagranin immunoreactivity between prion and Aβ amyloid plaques
    • Rangon CM, Haik S, Faucheux BA et al. Different chromagranin immunoreactivity between prion and Aβ amyloid plaques. Neuroreport 2003 14:755 758.
    • (2003) Neuroreport , vol.14 , pp. 755-758
    • Rangon, C.M.1    Haik, S.2    Faucheux, B.A.3
  • 44
    • 0034628999 scopus 로고    scopus 로고
    • Cellular prion protein binds laminin and mediates neuritogenesis
    • Graner E, Mercadante AF, Zanata SM et al. Cellular prion protein binds laminin and mediates neuritogenesis. Brain Res Mol Brain Res 2000 76:85 92.
    • (2000) Brain Res Mol Brain Res , vol.76 , pp. 85-92
    • Graner, E.1    Mercadante, A.F.2    Zanata, S.M.3
  • 45
    • 0032833626 scopus 로고    scopus 로고
    • Neuropathological differentiation of progressive supranuclear palsy and corticobasal degeneration
    • Suppl 2
    • Dickson DW. Neuropathological differentiation of progressive supranuclear palsy and corticobasal degeneration. J Neurol 1999 246 (Suppl 2 6 15.
    • (1999) J Neurol , vol.246 , pp. 6-15
    • Dickson, D.W.1
  • 46
    • 0037072257 scopus 로고    scopus 로고
    • Analysis of tau haplotypes in Pick's disease
    • Morris HR, Baker M, Yasojima K et al. Analysis of tau haplotypes in Pick's disease. Neurology 2002 59:443 445.
    • (2002) Neurology , vol.59 , pp. 443-445
    • Morris, H.R.1    Baker, M.2    Yasojima, K.3
  • 47
    • 0025971426 scopus 로고
    • Apolipoprotein e immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease
    • Namba Y, Tomonaga M, Kawasaki H, Otomo E, Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res 1991 541:163 166.
    • (1991) Brain Res , vol.541 , pp. 163-166
    • Namba, Y.1    Tomonaga, M.2    Kawasaki, H.3    Otomo, E.4    Ikeda, K.5
  • 48
    • 0025786506 scopus 로고
    • Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease
    • Perry G, Siedlak SL, Richey P et al. Association of heparan sulfate proteoglycan with the neurofibrillary tangles of Alzheimer's disease. J Neurol 1991 11:3679 3683.
    • (1991) J Neurol , vol.11 , pp. 3679-3683
    • Perry, G.1    Siedlak, S.L.2    Richey, P.3
  • 49
    • 0026030994 scopus 로고
    • Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer's disease
    • Bancher C, Grundke-Iqbal I, Iqbal K, Fried VA, Smith HT, Wisniewski HM. Abnormal phosphorylation of tau precedes ubiquitination in neurofibrillary pathology of Alzheimer's disease. Brain Res 1991 539:11 18.
    • (1991) Brain Res , vol.539 , pp. 11-18
    • Bancher, C.1    Grundke-Iqbal, I.2    Iqbal, K.3    Fried, V.A.4    Smith, H.T.5    Wisniewski, H.M.6
  • 50
    • 0032945397 scopus 로고    scopus 로고
    • Immunohistochemical and ultrastructural characterisation of neuritic clusters around ghost tangles in the hippocampal formation in progressive supranuclear palsy
    • Arima K, Nakamura M, Sunohara N et al. Immunohistochemical and ultrastructural characterisation of neuritic clusters around ghost tangles in the hippocampal formation in progressive supranuclear palsy. Acta Neuropathol 1999 97:565 576.
    • (1999) Acta Neuropathol , vol.97 , pp. 565-576
    • Arima, K.1    Nakamura, M.2    Sunohara, N.3
  • 51
    • 0026090776 scopus 로고
    • Secondary deposition of beta amyloid within extracellular tangles in Alzheimer-type dementia
    • Yamaguchi H, Nakazato Y, Shoji M et al. Secondary deposition of beta amyloid within extracellular tangles in Alzheimer-type dementia. Am J Pathol 1991 138:699 705.
    • (1991) Am J Pathol , vol.138 , pp. 699-705
    • Yamaguchi, H.1    Nakazato, Y.2    Shoji, M.3
  • 52
    • 0028217539 scopus 로고
    • Ultrastructural localization of complement membrane attack complex (MAC) -like immunoreactivity in brains of patients with Alzheimer's disease
    • Itagaki S, Akiyama H, Saito H, McGeer PL. Ultrastructural localization of complement membrane attack complex (MAC) -like immunoreactivity in brains of patients with Alzheimer's disease. Brain Res 1994 645:78 84.
    • (1994) Brain Res , vol.645 , pp. 78-84
    • Itagaki, S.1    Akiyama, H.2    Saito, H.3    McGeer, P.L.4
  • 53
    • 0027232334 scopus 로고
    • Neuritic plaques in Alzheimer's disease originate from neurofibrillary tangles
    • Perry G. Neuritic plaques in Alzheimer's disease originate from neurofibrillary tangles. Med Hypotheses 1993 40:257 258.
    • (1993) Med Hypotheses , vol.40 , pp. 257-258
    • Perry, G.1
  • 54
    • 0344298995 scopus 로고    scopus 로고
    • Alpha-synuclein accumulates in Lewy bodies in Parkinson's disease and dementia with Lewy bodies but not in Alzheimer's disease beta amyloid plaque cores
    • Bayer TA, Jakala P, Hartmann T et al. Alpha-synuclein accumulates in Lewy bodies in Parkinson's disease and dementia with Lewy bodies but not in Alzheimer's disease beta amyloid plaque cores. Neurosci Lett 1999 266:213 216.
    • (1999) Neurosci Lett , vol.266 , pp. 213-216
    • Bayer, T.A.1    Jakala, P.2    Hartmann, T.3
  • 55
    • 33746108503 scopus 로고    scopus 로고
    • Cellular pathology in multiple system atrophy
    • Wakabayashi K, Takahashi H. Cellular pathology in multiple system atrophy. Neuropathology 2006 26:338 345.
    • (2006) Neuropathology , vol.26 , pp. 338-345
    • Wakabayashi, K.1    Takahashi, H.2
  • 56
    • 0032849237 scopus 로고    scopus 로고
    • Cellular co-localisiation of phosphorylated tau and NACP/alpha-synuclein epitopes in Lewy bodies in sporadic Parkinsons's disease and in dementia with Lewy bodies
    • Arima K, Hirai S, Sunohara N et al. Cellular co-localisiation of phosphorylated tau and NACP/alpha-synuclein epitopes in Lewy bodies in sporadic Parkinsons's disease and in dementia with Lewy bodies. Brain Res 1999 843:53 61.
    • (1999) Brain Res , vol.843 , pp. 53-61
    • Arima, K.1    Hirai, S.2    Sunohara, N.3
  • 57
    • 0029866793 scopus 로고    scopus 로고
    • Purification and characterisation of Lewy bodies from the brains of patients with diffuse Lewy body disease
    • Iwatsubo T, Yamaguchi H, Fujimuro M et al. Purification and characterisation of Lewy bodies from the brains of patients with diffuse Lewy body disease. Am J Pathol 1996 148:1517 1529.
    • (1996) Am J Pathol , vol.148 , pp. 1517-1529
    • Iwatsubo, T.1    Yamaguchi, H.2    Fujimuro, M.3
  • 58
    • 0037127216 scopus 로고    scopus 로고
    • Tubulin seeds alpha-synuclein fibril formation
    • Alim MA, Hossain MS, Arima K et al. Tubulin seeds alpha-synuclein fibril formation. J Biol Chem 2002 277:2112 2117.
    • (2002) J Biol Chem , vol.277 , pp. 2112-2117
    • Alim, M.A.1    Hossain, M.S.2    Arima, K.3
  • 59
    • 0028828550 scopus 로고
    • Cortical and brain stem type Lewy bodies are immunoreactive for the cyclin dependent kinase-5
    • Brion JP, Couk AM. Cortical and brain stem type Lewy bodies are immunoreactive for the cyclin dependent kinase-5. Am J Pathol 1995 147:1465 1476.
    • (1995) Am J Pathol , vol.147 , pp. 1465-1476
    • Brion, J.P.1    Couk, A.M.2
  • 60
    • 0027503917 scopus 로고
    • Immunohistochemistry of neuronal inclusions in the cerebral cortex and brain stem in Lewy body dementia
    • Fukuda T, Tanaka J, Watabe K, Numoto RT, Minamitani M. Immunohistochemistry of neuronal inclusions in the cerebral cortex and brain stem in Lewy body dementia. Acta Pathol Jpn 1993 43:545 551.
    • (1993) Acta Pathol Jpn , vol.43 , pp. 545-551
    • Fukuda, T.1    Tanaka, J.2    Watabe, K.3    Numoto, R.T.4    Minamitani, M.5
  • 61
    • 0027407247 scopus 로고
    • Ubiquitin in neurodegenerative diseases
    • Lowe J, Mayer RJ, Landon M. Ubiquitin in neurodegenerative diseases. Brain Pathol 1993 3:55 65.
    • (1993) Brain Pathol , vol.3 , pp. 55-65
    • Lowe, J.1    Mayer, R.J.2    Landon, M.3
  • 62
    • 0029655750 scopus 로고    scopus 로고
    • Microtubule-associated protein-5 is a component of Lewy bodies and Lewy body neurites in the brainstem and forebrain regions affected in Parkinson's disease
    • Gai WP, Blumbergs PC, Blessing WW. Microtubule-associated protein-5 is a component of Lewy bodies and Lewy body neurites in the brainstem and forebrain regions affected in Parkinson's disease. Acta Neuropathol 1996 91:78 81.
    • (1996) Acta Neuropathol , vol.91 , pp. 78-81
    • Gai, W.P.1    Blumbergs, P.C.2    Blessing, W.W.3
  • 63
    • 0031951053 scopus 로고    scopus 로고
    • Pick's disease: Selective occurrence of apolipoprotein e immunoreactive Pick bodies in the limbic system
    • Hayashi S, Wakabayashi K, Iwanaga K et al. Pick's disease: selective occurrence of apolipoprotein E immunoreactive Pick bodies in the limbic system. Acta Neuropathol 1998 95:1 4.
    • (1998) Acta Neuropathol , vol.95 , pp. 1-4
    • Hayashi, S.1    Wakabayashi, K.2    Iwanaga, K.3
  • 64
    • 0030598374 scopus 로고    scopus 로고
    • Identification of advanced glycylation end-products of the Maillard reaction in Pick's disease
    • Kimura M, Ikeda K, Takamatsu J et al. Identification of advanced glycylation end-products of the Maillard reaction in Pick's disease. Neurosci Lett 1996 279:95 98.
    • (1996) Neurosci Lett , vol.279 , pp. 95-98
    • Kimura, M.1    Ikeda, K.2    Takamatsu, J.3
  • 65
    • 0028109846 scopus 로고
    • The apolipoprotein-E alleles as major susceptibility factors for Creutzfeldt-Jakob disease
    • Amouyel P, Vidal O, Launay JM, Laplanche JL. The apolipoprotein-E alleles as major susceptibility factors for Creutzfeldt-Jakob disease. Lancet 1994 344:1315 1318.
    • (1994) Lancet , vol.344 , pp. 1315-1318
    • Amouyel, P.1    Vidal, O.2    Launay, J.M.3    Laplanche, J.L.4
  • 66
    • 0028051894 scopus 로고
    • Involvement of clathrin light chains in the pathology of Pick's disease: Implications for impairment of axonal transport
    • Nakamura Y, Takeda M, Yoshimi K et al. Involvement of clathrin light chains in the pathology of Pick's disease: implications for impairment of axonal transport. Neurosci Lett 1994 180:25 28.
    • (1994) Neurosci Lett , vol.180 , pp. 25-28
    • Nakamura, Y.1    Takeda, M.2    Yoshimi, K.3
  • 68
    • 0031842931 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 and mitogen activated protein kinase in glial cytoplasmic inclusions in multiple system atrophy
    • Nakamura S, Kawamoto Y, Nakano S, Akiguchi I, Kimura J. Cyclin-dependent kinase 5 and mitogen activated protein kinase in glial cytoplasmic inclusions in multiple system atrophy. J Neuropathol Exp Neurol 1998 57:690 698.
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 690-698
    • Nakamura, S.1    Kawamoto, Y.2    Nakano, S.3    Akiguchi, I.4    Kimura, J.5
  • 69
    • 0027954290 scopus 로고
    • Extracellular or ghost Pick bodies and their lack of tau immunoreactivity: A histological, immunohistochemical and electron microscope study
    • Izumiyama Y, Ikeda K, Oyanagi S. Extracellular or ghost Pick bodies and their lack of tau immunoreactivity: a histological, immunohistochemical and electron microscope study. Acta Neuropathol 1994 87:277 283.
    • (1994) Acta Neuropathol , vol.87 , pp. 277-283
    • Izumiyama, Y.1    Ikeda, K.2    Oyanagi, S.3
  • 70
    • 0032976201 scopus 로고    scopus 로고
    • From genotype to phenotype: A clinical pathological and biochemical investigation of frontotemporal dementia and parkinsonism (FTDP-17) caused by the P300L tau mutation
    • Nasreddine ZS, Logimov M, Clark LN et al. From genotype to phenotype: a clinical pathological and biochemical investigation of frontotemporal dementia and parkinsonism (FTDP-17) caused by the P300L tau mutation. Ann Neurol 1999 45:705 715.
    • (1999) Ann Neurol , vol.45 , pp. 705-715
    • Nasreddine, Z.S.1    Logimov, M.2    Clark, L.N.3
  • 71
    • 0032774891 scopus 로고    scopus 로고
    • Fronto-temporal dementia with parkinsonism linked to chromosome 17 (FTDP-17): A clinician's guide
    • Foster NL. Fronto-temporal dementia with parkinsonism linked to chromosome 17 (FTDP-17): a clinician's guide. Neurologist 1999 5:213 221.
    • (1999) Neurologist , vol.5 , pp. 213-221
    • Foster, N.L.1
  • 72
    • 0028889282 scopus 로고
    • Thorn-shaped atrocytes: Possible secondarily induced tau-positive glial fibrillary tangles
    • Ikeda K, Akiyama H, Kondo H et al. Thorn-shaped atrocytes: possible secondarily induced tau-positive glial fibrillary tangles. Acta Neuropathol 1995 90:620 625.
    • (1995) Acta Neuropathol , vol.90 , pp. 620-625
    • Ikeda, K.1    Akiyama, H.2    Kondo, H.3
  • 73
    • 0029062956 scopus 로고
    • Widespread cytoskeletal pathology characterises corticobasal degeneration
    • Feany MB, Dickson DW. Widespread cytoskeletal pathology characterises corticobasal degeneration. Am J Pathol 1995 146:1388 1396.
    • (1995) Am J Pathol , vol.146 , pp. 1388-1396
    • Feany, M.B.1    Dickson, D.W.2
  • 74
    • 0026543843 scopus 로고
    • Appearance of paired nucleated tau positive glia in patients with progressive supranuclaer palsy brain tissue
    • Yamada T, McGeer PL, McGeer EG. Appearance of paired nucleated tau positive glia in patients with progressive supranuclaer palsy brain tissue. Neurosci Lett 1992 135:99 102.
    • (1992) Neurosci Lett , vol.135 , pp. 99-102
    • Yamada, T.1    McGeer, P.L.2    McGeer, E.G.3
  • 75
    • 0030611366 scopus 로고    scopus 로고
    • Tau immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy
    • Takeda A, Arai N, Komori T, Iseki E, Kato S, Oda M. Tau immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy. Neurosci Lett 1997 234:63 66.
    • (1997) Neurosci Lett , vol.234 , pp. 63-66
    • Takeda, A.1    Arai, N.2    Komori, T.3    Iseki, E.4    Kato, S.5    Oda, M.6
  • 76
    • 0035108490 scopus 로고    scopus 로고
    • Co-localisation of α-synuclein and phosphorylated tau and glial cytoplasmic inclusions in a patient with multiple system atrophy of long duration
    • Piao YS, Hayashi S, Hasegawa M et al. Co-localisation of α-synuclein and phosphorylated tau and glial cytoplasmic inclusions in a patient with multiple system atrophy of long duration. Acta Neuropathol 2001 101:285 293.
    • (2001) Acta Neuropathol , vol.101 , pp. 285-293
    • Piao, Y.S.1    Hayashi, S.2    Hasegawa, M.3
  • 77
    • 0034091659 scopus 로고    scopus 로고
    • Expression of the endocytosis regulatory proteins Rab5 and Rabaptin 5 in glial cytoplasmic inclusions from brains with multiple system atrophy
    • Nakamura S, Kawamoto Y, Nakano S, Akiguchi I. Expression of the endocytosis regulatory proteins Rab5 and Rabaptin 5 in glial cytoplasmic inclusions from brains with multiple system atrophy. Clin Neuropath 2000 19:51 56.
    • (2000) Clin Neuropath , vol.19 , pp. 51-56
    • Nakamura, S.1    Kawamoto, Y.2    Nakano, S.3    Akiguchi, I.4
  • 78
    • 0031564828 scopus 로고    scopus 로고
    • Tau protein in the glial cytoplasmic inclusions of multiple system atrophy can be distinguished from abnormal tau in Alzheimer's disease
    • Cairns NJ, Atkinson PF, Hanger DP, Anderton BH, Daniel SE, Lantos PL. Tau protein in the glial cytoplasmic inclusions of multiple system atrophy can be distinguished from abnormal tau in Alzheimer's disease. Neurosci Lett 1997 230:49 52.
    • (1997) Neurosci Lett , vol.230 , pp. 49-52
    • Cairns, N.J.1    Atkinson, P.F.2    Hanger, D.P.3    Anderton, B.H.4    Daniel, S.E.5    Lantos, P.L.6
  • 79
    • 0032692501 scopus 로고    scopus 로고
    • Alpha-synuclein immunoisolation of glial inclusions from multiple system atrophy brain tissue reveals multiprotein components
    • Gai WP, Power JHT, Blumbergs PC, Culvenor JG, Jensen PH. Alpha-synuclein immunoisolation of glial inclusions from multiple system atrophy brain tissue reveals multiprotein components. J Neurochem 1999 73:2093 2100.
    • (1999) J Neurochem , vol.73 , pp. 2093-2100
    • Gai, W.P.1    Power, J.H.T.2    Blumbergs, P.C.3    Culvenor, J.G.4    Jensen, P.H.5
  • 80
    • 0038509194 scopus 로고    scopus 로고
    • Frontotemporal dementia and motor neurone degeneration with neurofilament inclusion bodies: Additional evidence for overlap between FTD and ALS
    • Bigio EH, Lipton AM, White CL, Dickson DW, Hirano A. Frontotemporal dementia and motor neurone degeneration with neurofilament inclusion bodies: additional evidence for overlap between FTD and ALS. Neuropathol Appl Neurobiol 2003 29:239 253.
    • (2003) Neuropathol Appl Neurobiol , vol.29 , pp. 239-253
    • Bigio, E.H.1    Lipton, A.M.2    White, C.L.3    Dickson, D.W.4    Hirano, A.5
  • 81
    • 0037426557 scopus 로고    scopus 로고
    • Patients with a novel neurofilamentopathy: Dementia with neurofilament inclusions
    • Cairns NJ, Perry RH, Jaros E et al. Patients with a novel neurofilamentopathy: dementia with neurofilament inclusions. Neurosci Lett 2003 341:177 180.
    • (2003) Neurosci Lett , vol.341 , pp. 177-180
    • Cairns, N.J.1    Perry, R.H.2    Jaros, E.3
  • 82
    • 0242336433 scopus 로고    scopus 로고
    • Neurofilament inclusion body disease: A new proteinopathy?
    • Josephs KA, Holton JL, Rossor MN et al. Neurofilament inclusion body disease: a new proteinopathy? Brain 2003 126:2291 2303.
    • (2003) Brain , vol.126 , pp. 2291-2303
    • Josephs, K.A.1    Holton, J.L.2    Rossor, M.N.3
  • 83
    • 33744744717 scopus 로고    scopus 로고
    • Topography of α-internexin-positive neuronal aggregates in 10 patients with neuronal intermediate filament inclusion disease
    • Armstrong RA, Cairns NJ. Topography of α-internexin-positive neuronal aggregates in 10 patients with neuronal intermediate filament inclusion disease. Eur J Neurol 2006 13:528 532.
    • (2006) Eur J Neurol , vol.13 , pp. 528-532
    • Armstrong, R.A.1    Cairns, N.J.2
  • 84
    • 33747893766 scopus 로고    scopus 로고
    • Neuropathological changes in ten cases on neuronal intermediate filament inclusion disease (NIFID): A study using a-internexin immunohistochemistry and principal components analysis
    • Armstrong RA, Kerty E, Skullerud K, Cairns NJ. Neuropathological changes in ten cases on neuronal intermediate filament inclusion disease (NIFID): a study using a-internexin immunohistochemistry and principal components analysis. J Neural Transm 2006 113:1207 1215.
    • (2006) J Neural Transm , vol.113 , pp. 1207-1215
    • Armstrong, R.A.1    Kerty, E.2    Skullerud, K.3    Cairns, N.J.4
  • 85
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquinated TDP-43 in frontotemporal lobar degeneration and amylotrophic lateral scerosis
    • Neumann M, Sampathu DM, Kwong LK et al. Ubiquinated TDP-43 in frontotemporal lobar degeneration and amylotrophic lateral scerosis. Science 2006 314:130 133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 86
    • 0036711238 scopus 로고    scopus 로고
    • Are pathological lesions in neurodegenerative disorders the cause or the effect of the degeneration?
    • Armstrong RA, Cairns NJ, Lantos PL. Are pathological lesions in neurodegenerative disorders the cause or the effect of the degeneration? Neuropathology 2002 22:114 127.
    • (2002) Neuropathology , vol.22 , pp. 114-127
    • Armstrong, R.A.1    Cairns, N.J.2    Lantos, P.L.3
  • 87
    • 33745604012 scopus 로고    scopus 로고
    • Size frequency distributions of the florid prion protein aggregates in variant Creutzfeldt-Jakob disease follow a power-law function
    • Armstrong RA, Cairns NJ, Ironside JW. Size frequency distributions of the florid prion protein aggregates in variant Creutzfeldt-Jakob disease follow a power-law function. Neuro Sci 2006 27:104 109.
    • (2006) Neuro Sci , vol.27 , pp. 104-109
    • Armstrong, R.A.1    Cairns, N.J.2    Ironside, J.W.3
  • 88
    • 27144510914 scopus 로고    scopus 로고
    • Size frequency distributions of prion protein (PrP) aggregates in variant Creutzfeldt-Jakob disease
    • Armstrong RA, Cairns NJ, Ironside JW, Lantos PL. Size frequency distributions of prion protein (PrP) aggregates in variant Creutzfeldt-Jakob disease. J Neural Transm 2005 112:1565 1573.
    • (2005) J Neural Transm , vol.112 , pp. 1565-1573
    • Armstrong, R.A.1    Cairns, N.J.2    Ironside, J.W.3    Lantos, P.L.4
  • 89
    • 0026065020 scopus 로고
    • Subtypes and differential laminar distribution of β/A4 deposits in Alzheimer's disease: Relationship with the intellectual status of 26 cases
    • Delaere P, Duyckaerts C, He Y, Piette F, Hauw JJ. Subtypes and differential laminar distribution of β/A4 deposits in Alzheimer's disease: relationship with the intellectual status of 26 cases. Acta Neuropathol 1991 81:328 335.
    • (1991) Acta Neuropathol , vol.81 , pp. 328-335
    • Delaere, P.1    Duyckaerts, C.2    He, Y.3    Piette, F.4    Hauw, J.J.5
  • 90
    • 0028891760 scopus 로고
    • The COOH-terminus of the Alzheimer amyloid Aβ peptide: Differences in length influence the process of amyloid deposition in Alzheimer brain, and tell us something about relationships among parenchymal and vessel-asssociated amyloid deposits
    • Greenberg BD. The COOH-terminus of the Alzheimer amyloid Aβ peptide: differences in length influence the process of amyloid deposition in Alzheimer brain, and tell us something about relationships among parenchymal and vessel-asssociated amyloid deposits. Amyloid 1995 21:195 203.
    • (1995) Amyloid , vol.21 , pp. 195-203
    • Greenberg, B.D.1
  • 91
    • 0031811820 scopus 로고    scopus 로고
    • β-amyloid plaques: Stages in life history or independent origin?
    • Armstrong RA. β-amyloid plaques: stages in life history or independent origin? Dement Geriatr Cogn Disord 1998 9:227 238.
    • (1998) Dement Geriatr Cogn Disord , vol.9 , pp. 227-238
    • Armstrong, R.A.1
  • 92
    • 0037072278 scopus 로고    scopus 로고
    • Nonoverlapping but synergetic tau and amyloid precursor protein pathologies in sporadic Alzheimer's disease
    • Delacourte A, Sergeant N, Champain D et al. Nonoverlapping but synergetic tau and amyloid precursor protein pathologies in sporadic Alzheimer's disease. Neurology 2002 59:398 407.
    • (2002) Neurology , vol.59 , pp. 398-407
    • Delacourte, A.1    Sergeant, N.2    Champain, D.3
  • 93
    • 0031824433 scopus 로고    scopus 로고
    • Amyloid beta protein (Aβ) deposition in dementia with Lewy bodies: Predominance of Aβ42/43 and a paucity of Aβ40 compared with sporadic Alzheimer's disease
    • Mann DMA, Brown SMP, Owen F, Baba M, Iwasubo T. Amyloid beta protein (Aβ) deposition in dementia with Lewy bodies: predominance of Aβ42/43 and a paucity of Aβ40 compared with sporadic Alzheimer's disease. Neuropathol Appl Neurobiol 1998 24:187 194.
    • (1998) Neuropathol Appl Neurobiol , vol.24 , pp. 187-194
    • Mann, D.M.A.1    Brown, S.M.P.2    Owen, F.3    Baba, M.4    Iwasubo, T.5
  • 94
    • 0035961293 scopus 로고    scopus 로고
    • From genetics to pathology: Tau and alpha-synuclein assemblies in neurodegenerative diseases
    • Goedert M, Spillantini MG, Serpell LC et al. From genetics to pathology: tau and alpha-synuclein assemblies in neurodegenerative diseases. Philos Trans R Soc Lond B Biol Sci 2001 356:213 227.
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 213-227
    • Goedert, M.1    Spillantini, M.G.2    Serpell, L.C.3
  • 95
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple systems atrophy with Parkinsons's disease and dementia with Lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, Cairns NJ, Lantos PL, Goedert M. Filamentous alpha-synuclein inclusions link multiple systems atrophy with Parkinsons's disease and dementia with Lewy bodies. Neurosci Lett 1998 251:205 208.
    • (1998) Neurosci Lett , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 96
    • 34648819365 scopus 로고    scopus 로고
    • The Lewy body in Parkinsons's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates
    • Wakabayashi K, Tanji K, Mori F, Takahashi H. The Lewy body in Parkinsons's disease: molecules implicated in the formation and degradation of alpha-synuclein aggregates. Neuropathology 2007 27:506 518.
    • (2007) Neuropathology , vol.27 , pp. 506-518
    • Wakabayashi, K.1    Tanji, K.2    Mori, F.3    Takahashi, H.4
  • 97
    • 0031715512 scopus 로고    scopus 로고
    • Monogenetic determinants of Alzheimer's disease: Amyloid precursor protein mutations
    • Goate AM. Monogenetic determinants of Alzheimer's disease: amyloid precursor protein mutations. Cell Mol Life Sci 1998 54:897 901.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 897-901
    • Goate, A.M.1
  • 98
    • 0025239720 scopus 로고
    • The Alzheimer's amyloid precursor protein is produced by type 1 astrocytes in primary cultures of rat microglia
    • Berkenbosch F, Refolo LM, Friedrich VL, Casper D, Blum M, Robakis NK. The Alzheimer's amyloid precursor protein is produced by type 1 astrocytes in primary cultures of rat microglia. J Neurosci Res 1990 25:431 440.
    • (1990) J Neurosci Res , vol.25 , pp. 431-440
    • Berkenbosch, F.1    Refolo, L.M.2    Friedrich, V.L.3    Casper, D.4    Blum, M.5    Robakis, N.K.6
  • 99
    • 0029450271 scopus 로고
    • The amyloid peptide precursor in Alzheimer's disease
    • Octave JN. The amyloid peptide precursor in Alzheimer's disease. Acta Neurol Belg 1995 95:197 209.
    • (1995) Acta Neurol Belg , vol.95 , pp. 197-209
    • Octave, J.N.1
  • 100
    • 7244245842 scopus 로고    scopus 로고
    • Urea modulation of beta-amyloid fibril growth: Experimental studies and kinetic models
    • Kim JR, Muresan A, Lee KYC, Murphy RM. Urea modulation of beta-amyloid fibril growth: experimental studies and kinetic models. Protein Sci 2004 13:2888 2898.
    • (2004) Protein Sci , vol.13 , pp. 2888-2898
    • Kim, J.R.1    Muresan, A.2    Lee, K.Y.C.3    Murphy, R.M.4
  • 101
    • 0026176190 scopus 로고
    • Homology of amyloid Beta protein precursor in monkey and human supports a primate model for Beta amyloidosis in Alzheimer's disease
    • Podlisny MB, Tolan DR, Selkoe DJ. Homology of amyloid Beta protein precursor in monkey and human supports a primate model for Beta amyloidosis in Alzheimer's disease. Am J Pathol 1991 138:1423 1433.
    • (1991) Am J Pathol , vol.138 , pp. 1423-1433
    • Podlisny, M.B.1    Tolan, D.R.2    Selkoe, D.J.3
  • 102
    • 0033452874 scopus 로고    scopus 로고
    • Genes and mechanisms involved in beta-amyloid generation and Alzheimer's disease
    • Steiner H, Capell A, Leimer U, Haass C. Genes and mechanisms involved in beta-amyloid generation and Alzheimer's disease. Eur Arch Psych Clin Neurol 1999 249:266 270.
    • (1999) Eur Arch Psych Clin Neurol , vol.249 , pp. 266-270
    • Steiner, H.1    Capell, A.2    Leimer, U.3    Haass, C.4
  • 103
    • 33646377385 scopus 로고    scopus 로고
    • Presenilin mutations linked to familial Alzheimer's disease reduce endoplasmic reticulum and Golgi apparatues calcium levels
    • Zatti G, Burgo A, Giacomello M et al. Presenilin mutations linked to familial Alzheimer's disease reduce endoplasmic reticulum and Golgi apparatues calcium levels. Cell Calcium 2006 39:539 550.
    • (2006) Cell Calcium , vol.39 , pp. 539-550
    • Zatti, G.1    Burgo, A.2    Giacomello, M.3
  • 104
    • 33745048523 scopus 로고    scopus 로고
    • CREB-binding protein activation by presenilin 1 but not by its M146L mutant
    • Francis YI, Stephanou A, Latchman DS. CREB-binding protein activation by presenilin 1 but not by its M146L mutant. Neuroreport 2006 17:917 921.
    • (2006) Neuroreport , vol.17 , pp. 917-921
    • Francis, Y.I.1    Stephanou, A.2    Latchman, D.S.3
  • 105
    • 0031686460 scopus 로고    scopus 로고
    • Presenilin-1 mutations linked to FAD increase the intracellular levels of amyloid beta protein 1-42 and its n-terminally truncated variant (s) which are generated at distinct sites
    • Sudoh S, Kawamura Y, Sato K et al. Presenilin-1 mutations linked to FAD increase the intracellular levels of amyloid beta protein 1-42 and its n-terminally truncated variant (s) which are generated at distinct sites. J Neurochem 1998 71:1535 1543.
    • (1998) J Neurochem , vol.71 , pp. 1535-1543
    • Sudoh, S.1    Kawamura, Y.2    Sato, K.3
  • 107
    • 0035154217 scopus 로고    scopus 로고
    • Quantification of the vacuolation ("spongiform change") and prion protein deposition in 11 patients with sporadic Creutzfeldt-Jakob disease
    • Armstrong RA, Cairns NJ, Lantos PL. Quantification of the vacuolation ("spongiform change") and prion protein deposition in 11 patients with sporadic Creutzfeldt-Jakob disease. Acta Neuropathol 2001 102:591 596.
    • (2001) Acta Neuropathol , vol.102 , pp. 591-596
    • Armstrong, R.A.1    Cairns, N.J.2    Lantos, P.L.3
  • 108
    • 0344196964 scopus 로고    scopus 로고
    • Spatial correlations between the vacuolation, prion protein deposition, and surviving neurons in variant Creutzfeldt-Jakob disease in variant Creutzfeldt-Jakob disease
    • Armstrong RA, Cairns NJ, Ironside JW, Lantos PJ. Spatial correlations between the vacuolation, prion protein deposition, and surviving neurons in variant Creutzfeldt-Jakob disease in variant Creutzfeldt-Jakob disease. J Neural Transm 2003 110:1303 1311.
    • (2003) J Neural Transm , vol.110 , pp. 1303-1311
    • Armstrong, R.A.1    Cairns, N.J.2    Ironside, J.W.3    Lantos, P.J.4
  • 109
    • 0032816292 scopus 로고    scopus 로고
    • Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analyis of 300 subjects
    • Parchi P, Giese A, Capillari S et al. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analyis of 300 subjects. Ann Neurol 1999 46:224 233.
    • (1999) Ann Neurol , vol.46 , pp. 224-233
    • Parchi, P.1    Giese, A.2    Capillari, S.3
  • 110
    • 0029782193 scopus 로고    scopus 로고
    • Prion protein genotype and pathological phenotype studies in sporadic Creutzfeldt-Jakob disease
    • MacDonald ST, Sutherland K, Ironside JW. Prion protein genotype and pathological phenotype studies in sporadic Creutzfeldt-Jakob disease. Neuropath Appl Neurobiol 1996 22:285 292.
    • (1996) Neuropath Appl Neurobiol , vol.22 , pp. 285-292
    • MacDonald, S.T.1    Sutherland, K.2    Ironside, J.W.3
  • 111
    • 0036205905 scopus 로고    scopus 로고
    • Inherited frontotemporal dementia in nine British families associated with intronic mutations of the tau gene
    • Pickering-Brown SM, Richardson AMT, Snowden JS et al. Inherited frontotemporal dementia in nine British families associated with intronic mutations of the tau gene. Brain 2002 125:732 751.
    • (2002) Brain , vol.125 , pp. 732-751
    • Pickering-Brown, S.M.1    Richardson, A.M.T.2    Snowden, J.S.3
  • 112
    • 0033674152 scopus 로고    scopus 로고
    • Frontotemporal dementia with novel tau pathology and a Glu342Val tau mutation
    • Lippa CF, Zhukareva V, Kawari T et al. Frontotemporal dementia with novel tau pathology and a Glu342Val tau mutation. Ann Neurol 2000 48:850 858.
    • (2000) Ann Neurol , vol.48 , pp. 850-858
    • Lippa, C.F.1    Zhukareva, V.2    Kawari, T.3
  • 114
    • 0033638377 scopus 로고    scopus 로고
    • Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells
    • Vogelsberg-Ragaglia V, Bruce J, Richter-Landsberg C et al. Distinct FTDP-17 missense mutations in tau produce tau aggregates and other pathological phenotypes in transfected CHO cells. Mol Biol Cell 2000 11:4093 4104.
    • (2000) Mol Biol Cell , vol.11 , pp. 4093-4104
    • Vogelsberg-Ragaglia, V.1    Bruce, J.2    Richter-Landsberg, C.3
  • 115
    • 0035229852 scopus 로고    scopus 로고
    • Tau gene mutations and neurodegeneration
    • Goedert M, Spillantini MG. Tau gene mutations and neurodegeneration. Biochem Soc Symp 2001 67:59 71.
    • (2001) Biochem Soc Symp , vol.67 , pp. 59-71
    • Goedert, M.1    Spillantini, M.G.2
  • 116
    • 0032744571 scopus 로고    scopus 로고
    • Mutational analysis of the tau gene in progressive supranuclear palsy
    • Higgins JJ, Adler RL, Loveless JM. Mutational analysis of the tau gene in progressive supranuclear palsy. Neurology 1999 53:1421 1424.
    • (1999) Neurology , vol.53 , pp. 1421-1424
    • Higgins, J.J.1    Adler, R.L.2    Loveless, J.M.3
  • 117
    • 1842710478 scopus 로고    scopus 로고
    • Spatial patterns of α-synuclein positive glial cytoplasmic inclusions in multiple system atrophy
    • Armstrong RA, Lantos PL, Cairns NJ. Spatial patterns of α-synuclein positive glial cytoplasmic inclusions in multiple system atrophy. Mov Disord 2004 19:109 112.
    • (2004) Mov Disord , vol.19 , pp. 109-112
    • Armstrong, R.A.1    Lantos, P.L.2    Cairns, N.J.3
  • 118
    • 0034017710 scopus 로고    scopus 로고
    • Alpha-synuclein and Parkinson's disease: Selective neurodegenerative effect of alpha-synuclein fragment on dopaminergic neurons in vitro and in vivo
    • Forloni G, Bertain I, Catella AM, Thaler F, Invernizzi R. Alpha-synuclein and Parkinson's disease: selective neurodegenerative effect of alpha-synuclein fragment on dopaminergic neurons in vitro and in vivo. Ann Neurol 2000 47:632 640.
    • (2000) Ann Neurol , vol.47 , pp. 632-640
    • Forloni, G.1    Bertain, I.2    Catella, A.M.3    Thaler, F.4    Invernizzi, R.5
  • 119
    • 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. et al. 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
  • 120
    • 33644824239 scopus 로고    scopus 로고
    • Interface between tauopathies and synucleinopathies: A tale of two proteins
    • Galpern WR, Lang AE. Interface between tauopathies and synucleinopathies: a tale of two proteins. Ann Neurol 2006 59:449 458.
    • (2006) Ann Neurol , vol.59 , pp. 449-458
    • Galpern, W.R.1    Lang, A.E.2
  • 121
    • 0035957112 scopus 로고    scopus 로고
    • Clinical and pathologic abnormalities in a family with parkinsonism and parkin gene mutations
    • Van de Warrenburg BPC, Lammens M et al. Clinical and pathologic abnormalities in a family with parkinsonism and parkin gene mutations. Neurology 2001 56:555 557.
    • (2001) Neurology , vol.56 , pp. 555-557
    • Van De Warrenburg, B.P.C.1    Lammens, M.2
  • 122
    • 33749168030 scopus 로고    scopus 로고
    • Genes in Alzheimer's disease
    • Hoenicka J. Genes in Alzheimer's disease. Rev Neurol 2006 42:302 305.
    • (2006) Rev Neurol , vol.42 , pp. 302-305
    • Hoenicka, J.1
  • 123
    • 7044238416 scopus 로고    scopus 로고
    • Neurodegenerative diseases: A decade of discoveries paves the way for therapeutic breakthroughs
    • Forman MS, Trojanowski JQ, Lee VM-Y. Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat Med 2004 10:1055 1063.
    • (2004) Nat Med , vol.10 , pp. 1055-1063
    • Forman, M.S.1    Trojanowski, J.Q.2    Lee, V.M.-Y.3
  • 124
    • 0027422751 scopus 로고
    • Genetic and molecular advances in Alzheimer's disease
    • Mullan M, Crawford F. Genetic and molecular advances in Alzheimer's disease. Trends Neurosci 1993 16:398 403.
    • (1993) Trends Neurosci , vol.16 , pp. 398-403
    • Mullan, M.1    Crawford, F.2
  • 126
    • 0027934214 scopus 로고
    • Cleavage at the N-terminal site of Alzheimer amyloid β/A4 protein is essential for its secretion
    • Maruyama K, Kawamura Y, Asada H, Ishuira S, Obata K. Cleavage at the N-terminal site of Alzheimer amyloid β/A4 protein is essential for its secretion. Biochem Biophys Res Commun 1994 202:1517 1523.
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 1517-1523
    • Maruyama, K.1    Kawamura, Y.2    Asada, H.3    Ishuira, S.4    Obata, K.5
  • 127
    • 0026070557 scopus 로고
    • Increased biosynthesis of Alzheimer amyloid precursor protein in the cerebral cortex of rats with lesions of the nucleus basalis of Meynert
    • Wallace WC, Bragin V, Robakis NK et al. Increased biosynthesis of Alzheimer amyloid precursor protein in the cerebral cortex of rats with lesions of the nucleus basalis of Meynert. Brain Res Mol Brain Res 1991 10:173 178.
    • (1991) Brain Res Mol Brain Res , vol.10 , pp. 173-178
    • Wallace, W.C.1    Bragin, V.2    Robakis, N.K.3
  • 128
    • 0027691633 scopus 로고
    • Early and rapid de novo synthesis of Alzheimer βa4-amyloid precursor protein (APP) in activated microglia
    • Banati RB, Gehrmann J, Czech C et al. Early and rapid de novo synthesis of Alzheimer βA4-amyloid precursor protein (APP) in activated microglia. Glia 1993 9:199 210.
    • (1993) Glia , vol.9 , pp. 199-210
    • Banati, R.B.1    Gehrmann, J.2    Czech, C.3
  • 129
    • 0026646280 scopus 로고
    • Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischaemia in the rat
    • Stephenson DT, Rash K, Clemens JA. Amyloid precursor protein accumulates in regions of neurodegeneration following focal cerebral ischaemia in the rat. Brain Res 1992 593:128 135.
    • (1992) Brain Res , vol.593 , pp. 128-135
    • Stephenson, D.T.1    Rash, K.2    Clemens, J.A.3
  • 130
    • 0028345162 scopus 로고
    • Age and damage induced changes in amyloid precursor protein immunohistochemistry in the rat brain
    • Beeson JG, Shelton ER, Chan HW, Gage FH. Age and damage induced changes in amyloid precursor protein immunohistochemistry in the rat brain. J Comp Neurol 1994 342:69 77.
    • (1994) J Comp Neurol , vol.342 , pp. 69-77
    • Beeson, J.G.1    Shelton, E.R.2    Chan, H.W.3    Gage, F.H.4
  • 131
    • 0026781306 scopus 로고
    • The role of amyloid β-protein in Alzheimer's disease
    • Regland B, Gottfries CG. The role of amyloid β-protein in Alzheimer's disease. Lancet 1992 340:467 469.
    • (1992) Lancet , vol.340 , pp. 467-469
    • Regland, B.1    Gottfries, C.G.2
  • 133
    • 0030296317 scopus 로고    scopus 로고
    • Amyloid load and neural elements in Alzheimer's disease and nondemented individuals with high amyloid plaque density
    • Mochizuki A, Peterson JW, Mufson EJ, Trapp BD. Amyloid load and neural elements in Alzheimer's disease and nondemented individuals with high amyloid plaque density. Exp Neurol 1996 142:89 102.
    • (1996) Exp Neurol , vol.142 , pp. 89-102
    • Mochizuki, A.1    Peterson, J.W.2    Mufson, E.J.3    Trapp, B.D.4
  • 134
    • 0030462485 scopus 로고    scopus 로고
    • Correlations between the morphology of diffuse and primitive β-amyloid (Aβ) deposits and the frequency of associated cells in Down's syndrome
    • Armstrong RA. Correlations between the morphology of diffuse and primitive β-amyloid (Aβ) deposits and the frequency of associated cells in Down's syndrome. Neuropath Appl Neurobiol 1996 22:527 530.
    • (1996) Neuropath Appl Neurobiol , vol.22 , pp. 527-530
    • Armstrong, R.A.1
  • 135
    • 23044522405 scopus 로고    scopus 로고
    • Diffuse β-amyloid (Aβ) deposits and neurons: In situ secretion or diffusion of Aβ?
    • Armstrong RA. Diffuse β-amyloid (Aβ) deposits and neurons: in situ secretion or diffusion of Aβ? Alzheimers Rep 2001 3:289 294.
    • (2001) Alzheimers Rep , vol.3 , pp. 289-294
    • Armstrong, R.A.1
  • 136
    • 0025779349 scopus 로고
    • Chromagranin A-like immunoreactive neuritis are major constituents of senile plaques
    • Munoz DG. Chromagranin A-like immunoreactive neuritis are major constituents of senile plaques. Lab Invest 1991 64:826 832.
    • (1991) Lab Invest , vol.64 , pp. 826-832
    • Munoz, D.G.1
  • 137
    • 0025832709 scopus 로고
    • Tangle-bearing neurons show more extensive dendritic trees than tangle-free neurons in area CA1 of the hippocampus in Alzheimer's disease
    • Gertz HJ, Kruger H, Patt S, Cervos-Navarro J. Tangle-bearing neurons show more extensive dendritic trees than tangle-free neurons in area CA1 of the hippocampus in Alzheimer's disease. Brain Res 1991 548:260 266.
    • (1991) Brain Res , vol.548 , pp. 260-266
    • Gertz, H.J.1    Kruger, H.2    Patt, S.3    Cervos-Navarro, J.4
  • 138
    • 0028270318 scopus 로고
    • Immunoreactive changes resulting from dopaminergic denervation of the dentate gyrus of the rat hippocampal formation
    • Torack RM, Miller JW. Immunoreactive changes resulting from dopaminergic denervation of the dentate gyrus of the rat hippocampal formation. Neurosci Lett 1994 169:9 12.
    • (1994) Neurosci Lett , vol.169 , pp. 9-12
    • Torack, R.M.1    Miller, J.W.2
  • 139
    • 0032786711 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactivity is present in axonal swellings in neuroaxonal dystrophy and acute traumatic brain injury
    • Newell KL, Boyer P, Gomez-Tortosa E et al. Alpha-synuclein immunoreactivity is present in axonal swellings in neuroaxonal dystrophy and acute traumatic brain injury. J Neuropath Exp Neurol 1999 58:1263 1268.
    • (1999) J Neuropath Exp Neurol , vol.58 , pp. 1263-1268
    • Newell, K.L.1    Boyer, P.2    Gomez-Tortosa, E.3
  • 141
    • 33746089104 scopus 로고    scopus 로고
    • Rat model of Parkinson's disease: Chronic central delivery of 1-methyl-4-phenylpyridinium (MPP (+)
    • Yazdani U, German DC, Liang CL, Manzino L, Sonsalla PK, Zeevalk GD. Rat model of Parkinson's disease: chronic central delivery of 1-methyl-4- phenylpyridinium (MPP (+). Exp Neurol 2006 200:172 183.
    • (2006) Exp Neurol , vol.200 , pp. 172-183
    • Yazdani, U.1    German, D.C.2    Liang, C.L.3    Manzino, L.4    Sonsalla, P.K.5    Zeevalk, G.D.6
  • 143
    • 0021691350 scopus 로고
    • Ultrastructure of paired helical filaments of Alzheimer's neurofibrillary tangle
    • Wisniewski HM, Merz PA, Iqbal K. Ultrastructure of paired helical filaments of Alzheimer's neurofibrillary tangle. J Neuropath Exp Neurol 1984 43:643 656.
    • (1984) J Neuropath Exp Neurol , vol.43 , pp. 643-656
    • Wisniewski, H.M.1    Merz, P.A.2    Iqbal, K.3
  • 144
    • 0029977028 scopus 로고    scopus 로고
    • Inconstant apolipoprotein (Apo E) - Like immunoreactivity in amyloid beta deposits: Relationship with Apo e genotype in aging brain and Alzheimer's disease
    • Uchihara T, Duyckaerts C, Lazarini F et al. Inconstant apolipoprotein (Apo E) - like immunoreactivity in amyloid beta deposits: relationship with Apo E genotype in aging brain and Alzheimer's disease. Acta Neuropathol 1996 92:180 185.
    • (1996) Acta Neuropathol , vol.92 , pp. 180-185
    • Uchihara, T.1    Duyckaerts, C.2    Lazarini, F.3
  • 145
    • 12044254746 scopus 로고
    • Binding of human apolipoprotein e to synthetic amyloid-β peptide: Isoform specific effects and implications for late-onset Alzheimer's disease
    • Strittmatter WJ, Wiesgraber KH, Huang DY et al. Binding of human apolipoprotein E to synthetic amyloid-β peptide: isoform specific effects and implications for late-onset Alzheimer's disease. Proc Natl Acad Sci USA 1993 90:8098 8102.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8098-8102
    • Strittmatter, W.J.1    Wiesgraber, K.H.2    Huang, D.Y.3
  • 146
    • 33750709236 scopus 로고    scopus 로고
    • Classic β-amyloid deposits cluster around large diameter blood vessels rather than capillaries in sporadic Alzheimer's disease
    • Armstrong RA. Classic β-amyloid deposits cluster around large diameter blood vessels rather than capillaries in sporadic Alzheimer's disease. Curr Neurovasc Res 2006 3:289 294.
    • (2006) Curr Neurovasc Res , vol.3 , pp. 289-294
    • Armstrong, R.A.1
  • 147
    • 0029032732 scopus 로고
    • Apolipoprotein e immunoreactivity within neurofibrillary tangles: Relationship to tau and paired helical filaments in Alzheimer's disease
    • Benzing WC, Mufson EJ. Apolipoprotein E immunoreactivity within neurofibrillary tangles: relationship to tau and paired helical filaments in Alzheimer's disease. Exp Neurol 1995 132:162 171.
    • (1995) Exp Neurol , vol.132 , pp. 162-171
    • Benzing, W.C.1    Mufson, E.J.2
  • 148
    • 0034717256 scopus 로고    scopus 로고
    • Degeneration process of Lewy bodies in the brains of patients with dementia with Lewy bodies using alpha-synuclein immunohistochemistry
    • Iseki E, Marui W, Akiyama H, Ueda K, Kosaka K. Degeneration process of Lewy bodies in the brains of patients with dementia with Lewy bodies using alpha-synuclein immunohistochemistry. Neurosci Lett 2000 286:69 73.
    • (2000) Neurosci Lett , vol.286 , pp. 69-73
    • Iseki, E.1    Marui, W.2    Akiyama, H.3    Ueda, K.4    Kosaka, K.5
  • 149
    • 3042806534 scopus 로고    scopus 로고
    • A "mitochondrial cascade hypothesis" for sporadic Alzheimer's disease
    • Swerdlow RH, Khan SM. A "mitochondrial cascade hypothesis" for sporadic Alzheimer's disease. Med Hypotheses 2004 63:8 20.
    • (2004) Med Hypotheses , vol.63 , pp. 8-20
    • Swerdlow, R.H.1    Khan, S.M.2
  • 150
    • 33645650515 scopus 로고
    • The amyloid precursor protein in ischaemic brain injury and chronic hypoperfusion. Proceedings of the 7th Inter Study Group
    • Kalaria RN, Bhatti SU, Perry G, Lust WD. The amyloid precursor protein in ischaemic brain injury and chronic hypoperfusion. Proceedings of the 7th Inter Study Group. Pharm Mem Dis Assoc Aging 1993:291 294.
    • (1993) Pharm Mem Dis Assoc Aging , pp. 291-294
    • Kalaria, R.N.1    Bhatti, S.U.2    Perry, G.3    Lust, W.D.4
  • 151
    • 0036362338 scopus 로고    scopus 로고
    • Ageing, stress and the brain. Endocrine facets of ageing
    • Carroll BJ. Ageing, stress and the brain. Endocrine facets of ageing. Novartis Found Symp 2002 242:26 36.
    • (2002) Novartis Found Symp , vol.242 , pp. 26-36
    • Carroll, B.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.