메뉴 건너뛰기




Volumn 119, Issue 4, 2010, Pages 389-408

Protein coding of neurodegenerative dementias: The neuropathological basis of biomarker diagnostics

Author keywords

synuclein; Amyloid (A ); Biomarker; FUS; Neurodegenerative disease; Prion protein; Protein code; Tau; TDP 43

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; BIOLOGICAL MARKER; PRION PROTEIN; TAR DNA BINDING PROTEIN; TAU PROTEIN;

EID: 77953023964     PISSN: 00016322     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00401-010-0658-1     Document Type: Review
Times cited : (92)

References (249)
  • 1
    • 33746922758 scopus 로고    scopus 로고
    • Interlabo-ratory comparison of assessments of Alzheimer disease-related lesions: A study of the BrainNet Europe Consortium
    • Alafuzoff I, Pikkarainen M, Al-Sarraj S et al (2006) Interlabo-ratory comparison of assessments of Alzheimer disease-related lesions: a study of the BrainNet Europe Consortium. J Neuro-pathol Exp Neurol 65:740-757.
    • (2006) J Neuro-pathol Exp Neurol , vol.65 , pp. 740-757
    • Alafuzoff, I.1    Pikkarainen, M.2    Al-Sarraj, S.3
  • 2
    • 46849092175 scopus 로고    scopus 로고
    • Abnormally phosphorylated tau is associated with neuronal and axonal loss in experimental autoimmune encephalomyelitis and multiple sclerosis
    • Anderson JM, Hampton DW, Patani R et al (2008) Abnormally phosphorylated tau is associated with neuronal and axonal loss in experimental autoimmune encephalomyelitis and multiple sclerosis. Brain 131:1736-1748.
    • (2008) Brain , vol.131 , pp. 1736-1748
    • Anderson, J.M.1    Hampton, D.W.2    Patani, R.3
  • 3
    • 64449088756 scopus 로고    scopus 로고
    • Evidence for abnormal tau phosphorylation in early aggressive multiple sclerosis
    • Anderson JM, Patani R, Reynolds R et al (2009) Evidence for abnormal tau phosphorylation in early aggressive multiple sclerosis. Acta Neuropathol 117:583-589.
    • (2009) Acta Neuropathol , vol.117 , pp. 583-589
    • Anderson, J.M.1    Patani, R.2    Reynolds, R.3
  • 4
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease
    • Anderson JP, Walker DE, Goldstein JM et al (2006) Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J Biol Chem 281:29739-29752.
    • (2006) J Biol Chem , vol.281 , pp. 29739-29752
    • Anderson, J.P.1    Walker, D.E.2    Goldstein, J.M.3
  • 5
    • 0026488111 scopus 로고
    • Structure and novel exons of the human tau gene
    • Andreadis A, Brown WM, Kosik KS (1992) Structure and novel exons of the human tau gene. Biochemistry 31:10626-10633.
    • (1992) Biochemistry , vol.31 , pp. 10626-10633
    • Andreadis, A.1    Brown, W.M.2    Kosik, K.S.3
  • 6
    • 4644336256 scopus 로고    scopus 로고
    • Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease
    • Andringa G, Lam KY, Chegary M, Wang X, Chase TN, Bennett MC (2004) Tissue transglutaminase catalyzes the formation of alpha-synuclein crosslinks in Parkinson's disease. FASEB J 18:932-934.
    • (2004) FASEB J , vol.18 , pp. 932-934
    • Andringa, G.1    Lam, K.Y.2    Chegary, M.3    Wang, X.4    Chase, T.N.5    Bennett, M.C.6
  • 7
    • 33646862119 scopus 로고    scopus 로고
    • Accelerated Tau deposition in the brains of individuals infected with human immunodeficiency virus-1 before and after the advent of highly active anti-retroviral therapy
    • Anthony IC, Ramage SN, Carnie FW, Simmonds P, Bell JE (2006) Accelerated Tau deposition in the brains of individuals infected with human immunodeficiency virus-1 before and after the advent of highly active anti-retroviral therapy. Acta Neu-ropathol 111:529-538.
    • (2006) Acta Neu-ropathol , vol.111 , pp. 529-538
    • Anthony, I.C.1    Ramage, S.N.2    Carnie, F.W.3    Simmonds, P.4    Bell, J.E.5
  • 8
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H et al (2006) TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem Biophys Res Commun 351:602-611.
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3
  • 9
    • 59249097160 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies
    • Arai T, Mackenzie IR, Hasegawa M et al (2009) Phosphorylated TDP-43 in Alzheimer's disease and dementia with Lewy bodies. Acta Neuropathol 117:125-136.
    • (2009) Acta Neuropathol , vol.117 , pp. 125-136
    • Arai, T.1    Mackenzie, I.R.2    Hasegawa, M.3
  • 11
    • 44849083256 scopus 로고    scopus 로고
    • What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease?
    • Armstrong RA, Lantos PL, Cairns NJ (2008) What determines the molecular composition of abnormal protein aggregates in neurodegenerative disease? Neuropathology 28:351-365.
    • (2008) Neuropathology , vol.28 , pp. 351-365
    • Armstrong, R.A.1    Lantos, P.L.2    Cairns, N.J.3
  • 12
    • 0024795714 scopus 로고
    • Tau and ubiquitin immunoreactivity at different stages of formation of Alzheimer neurofibrillary tangles
    • Bancher C, Brunner C, Lassmann H et al (1989) Tau and ubiquitin immunoreactivity at different stages of formation of Alzheimer neurofibrillary tangles. Prog Clin Biol Res 317:837-848.
    • (1989) Prog Clin Biol Res , vol.317 , pp. 837-848
    • Bancher, C.1    Brunner, C.2    Lassmann, H.3
  • 14
    • 63449129653 scopus 로고    scopus 로고
    • Molecular pathology of Lewy body diseases
    • Beyer K, Domingo-Sabat M, Ariza A (2009) Molecular pathology of Lewy body diseases. Int J Mol Sci 10:724-745.
    • (2009) Int J Mol Sci , vol.10 , pp. 724-745
    • Beyer, K.1    Domingo-Sabat, M.2    Ariza, A.3
  • 15
    • 38649119157 scopus 로고    scopus 로고
    • Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases
    • Beyer K, Domingo-Sabat M, Lao JI, Carrato C, Ferrer I, Ariza A (2008) Identification and characterization of a new alpha-synuclein isoform and its role in Lewy body diseases. Neurogenetics 9:15-23.
    • (2008) Neurogenetics , vol.9 , pp. 15-23
    • Beyer, K.1    Domingo-Sabat, M.2    Lao, J.I.3    Carrato, C.4    Ferrer, I.5    Ariza, A.6
  • 16
    • 33646266021 scopus 로고    scopus 로고
    • CSF amyloid-beta-peptides in Alzheimer's disease, dementia with Lewy bodies and Parkinson's disease dementia
    • Bibl M, Mollenhauer B, Esselmann H et al (2006) CSF amyloid-beta-peptides in Alzheimer's disease, dementia with Lewy bodies and Parkinson's disease dementia. Brain 129:1177-1187.
    • (2006) Brain , vol.129 , pp. 1177-1187
    • Bibl, M.1    Mollenhauer, B.2    Esselmann, H.3
  • 17
    • 34347272662 scopus 로고    scopus 로고
    • Validation of amyloid-beta peptides in CSF diagnosis of neurodegenerative dementias
    • Bibl M, Mollenhauer B, Lewczuk P et al (2007) Validation of amyloid-beta peptides in CSF diagnosis of neurodegenerative dementias. Mol Psychiatry 12:671-680.
    • (2007) Mol Psychiatry , vol.12 , pp. 671-680
    • Bibl, M.1    Mollenhauer, B.2    Lewczuk, P.3
  • 18
    • 0035063346 scopus 로고    scopus 로고
    • Frontal lobe dementia with novel tauopathy: Sporadic multiple system tau-opathy with dementia
    • Bigio EH, Lipton AM, Yen SH et al (2001) Frontal lobe dementia with novel tauopathy: sporadic multiple system tau-opathy with dementia. J Neuropathol Exp Neurol 60:328-341.
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 328-341
    • Bigio, E.H.1    Lipton, A.M.2    Yen, S.H.3
  • 20
    • 58149229648 scopus 로고    scopus 로고
    • Tau forms in CSF as a reliable biomarker for progressive supranuclear palsy
    • Borroni B, Malinverno M, Gardoni F et al (2008) Tau forms in CSF as a reliable biomarker for progressive supranuclear palsy. Neurology 71:1796-1803.
    • (2008) Neurology , vol.71 , pp. 1796-1803
    • Borroni, B.1    Malinverno, M.2    Gardoni, F.3
  • 21
    • 0028362458 scopus 로고
    • A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads
    • Braak E, Braak H, Mandelkow EM (1994) A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads. Acta Neuropathol 87:554-567.
    • (1994) Acta Neuropathol , vol.87 , pp. 554-567
    • Braak, E.1    Braak, H.2    Mandelkow, E.M.3
  • 23
    • 0039707140 scopus 로고    scopus 로고
    • Pathological tau proteins in postencephalitic parkinsonism: Comparison with Alzheimer's disease and other neurodegenerative disorders
    • Buee-Scherrer V, Buee L, Leveugle B et al (1997) Pathological tau proteins in postencephalitic parkinsonism: comparison with Alzheimer's disease and other neurodegenerative disorders. Ann Neurol 42:356-359.
    • (1997) Ann Neurol , vol.42 , pp. 356-359
    • Buee-Scherrer, V.1    Buee, L.2    Leveugle, B.3
  • 24
    • 34447096691 scopus 로고    scopus 로고
    • Neuropatho-logic diagnostic and nosologic criteria for frontotemporal lobar degeneration: Consensus of the Consortium for Frontotemporal Lobar Degeneration
    • Cairns NJ, Bigio EH, Mackenzie IR et al (2007) Neuropatho-logic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol 114:5-22.
    • (2007) Acta Neuropathol , vol.114 , pp. 5-22
    • Cairns, N.J.1    Bigio, E.H.2    Mackenzie, I.R.3
  • 26
    • 0035163412 scopus 로고    scopus 로고
    • The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease
    • Campbell BC, McLean CA, Culvenor JG et al (2001) The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease. J Neurochem 76:87-96.
    • (2001) J Neurochem , vol.76 , pp. 87-96
    • Campbell, B.C.1    McLean, C.A.2    Culvenor, J.G.3
  • 27
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell RW, Lomas DA (1997) Conformational disease. Lancet 350:134-138.
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 28
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • Collinge J, Sidle KC, Meads J, Ironside J, Hill AF (1996) Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 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
  • 29
    • 75149181071 scopus 로고    scopus 로고
    • Neocortical variation of abeta load in fully expressed, pure Alzheimer's disease
    • Cupidi C, Capobianco R, Goffredo D et al (2010) Neocortical Variation of Abeta Load in Fully Expressed, Pure Alzheimer's Disease. J Alzheimers Dis 19:57-68.
    • (2010) J Alzheimers Dis , vol.19 , pp. 57-68
    • Cupidi, C.1    Capobianco, R.2    Goffredo, D.3
  • 30
    • 33646124943 scopus 로고    scopus 로고
    • Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease
    • Dalfo E, Martinez A, Muntane G, Ferrer I (2006) Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease. Neurosci Lett 400:125-129.
    • (2006) Neurosci Lett , vol.400 , pp. 125-129
    • Dalfo, E.1    Martinez, A.2    Muntane, G.3    Ferrer, I.4
  • 31
    • 70349144524 scopus 로고    scopus 로고
    • Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease
    • Danielson SR, Held JM, Schilling B, Oo M, Gibson BW, Andersen JK (2009) Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease. Anal Chem 81:7823-7828.
    • (2009) Anal Chem , vol.81 , pp. 7823-7828
    • Danielson, S.R.1    Held, J.M.2    Schilling, B.3    Oo, M.4    Gibson, B.W.5    Andersen, J.K.6
  • 32
    • 68349095164 scopus 로고    scopus 로고
    • TDP-43 in ubiq-uitinated inclusions in the inferior olives in frontotemporal lobar degeneration and in other neurodegenerative diseases: A degenerative process distinct from normal ageing
    • Davidson Y, Amin H, Kelley T et al (2009) TDP-43 in ubiq-uitinated inclusions in the inferior olives in frontotemporal lobar degeneration and in other neurodegenerative diseases: a degenerative process distinct from normal ageing. Acta Neuropathol 118:359-369.
    • (2009) Acta Neuropathol , vol.118 , pp. 359-369
    • Davidson, Y.1    Amin, H.2    Kelley, T.3
  • 33
    • 49849091894 scopus 로고    scopus 로고
    • Association between deposition of beta-amyloid and pathological prion protein in sporadic Creutzfeldt-Jakob disease
    • Debatin L, Streffer J, Geissen M, Matschke J, Aguzzi A, Glatzel M (2008) Association between deposition of beta-amyloid and pathological prion protein in sporadic Creutzfeldt-Jakob disease. Neurodegener Dis 5:347-354.
    • (2008) Neurodegener Dis , vol.5 , pp. 347-354
    • Debatin, L.1    Streffer, J.2    Geissen, M.3    Matschke, J.4    Aguzzi, A.5    Glatzel, M.6
  • 34
    • 22244475384 scopus 로고    scopus 로고
    • Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase
    • Derkinderen P, Scales TM, Hanger DP et al (2005) Tyrosine 394 is phosphorylated in Alzheimer's paired helical filament tau and in fetal tau with c-Abl as the candidate tyrosine kinase. J Neurosci 25:6584-6593.
    • (2005) J Neurosci , vol.25 , pp. 6584-6593
    • Derkinderen, P.1    Scales, T.M.2    Hanger, D.P.3
  • 35
    • 0032833626 scopus 로고    scopus 로고
    • Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration
    • Dickson DW (1999) Neuropathologic differentiation of progressive supranuclear palsy and corticobasal degeneration. J Neurol 246(Suppl 2):II6-II15.
    • (1999) J Neurol , vol.246 , Issue.SUPPL.. 2
    • Dickson, D.W.1
  • 36
    • 41149115508 scopus 로고    scopus 로고
    • Evidence that incidental Lewy body disease is pre-symptomatic Parkinson's disease
    • Dickson DW, Fujishiro H, DelleDonne A et al (2008) Evidence that incidental Lewy body disease is pre-symptomatic Parkinson's disease. Acta Neuropathol 115:437-444.
    • (2008) Acta Neuropathol , vol.115 , pp. 437-444
    • Dickson, D.W.1    Fujishiro, H.2    DelleDonne, A.3
  • 37
    • 67349143998 scopus 로고    scopus 로고
    • Classification and basic pathology of Alzheimer disease
    • Duyckaerts C, Delatour B, Potier MC (2009) Classification and basic pathology of Alzheimer disease. Acta Neuropathol 118:5-36.
    • (2009) Acta Neuropathol , vol.118 , pp. 5-36
    • Duyckaerts, C.1    Delatour, B.2    Potier, M.C.3
  • 38
    • 69249210945 scopus 로고    scopus 로고
    • Oligomeri-zation partially explains the lowering of Abeta42 in Alzheimer's disease cerebrospinal fluid
    • Englund H, Degerman Gunnarsson M et al (2009) Oligomeri-zation partially explains the lowering of Abeta42 in Alzheimer's disease cerebrospinal fluid. Neurodegener Dis 6:139-147.
    • (2009) Neurodegener Dis , vol.6 , pp. 139-147
    • Englund, H.1    Degerman, G.M.2
  • 39
    • 0030049067 scopus 로고    scopus 로고
    • Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration
    • Feany MB, Mattiace LA, Dickson DW (1996) Neuropathologic overlap of progressive supranuclear palsy, Pick's disease and corticobasal degeneration. J Neuropathol Exp Neurol 55:53-67.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 53-67
    • Feany, M.B.1    Mattiace, L.A.2    Dickson, D.W.3
  • 40
    • 0035141524 scopus 로고    scopus 로고
    • Prion protein expression in senile plaques in Alzheimer's disease
    • Ferrer I, Blanco R, Carmona M et al (2001) Prion protein expression in senile plaques in Alzheimer's disease. Acta Neuropathol 101:49-56.
    • (2001) Acta Neuropathol , vol.101 , pp. 49-56
    • Ferrer, I.1    Blanco, R.2    Carmona, M.3
  • 41
    • 0025857173 scopus 로고
    • Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type
    • Flament S, Delacourte A, Verny M, Hauw JJ, Javoy-Agid F (1991) Abnormal Tau proteins in progressive supranuclear palsy. Similarities and differences with the neurofibrillary degeneration of the Alzheimer type. Acta Neuropathol 81:591-596.
    • (1991) Acta Neuropathol , vol.81 , pp. 591-596
    • Flament, S.1    Delacourte, A.2    Verny, M.3    Hauw, J.J.4    Javoy-Agid, F.5
  • 42
    • 70449526407 scopus 로고    scopus 로고
    • Plasma phos-phorylated-TDP-43 protein levels correlate with brain pathology in frontotemporal lobar degeneration
    • Foulds PG, Davidson Y, Mishra M et al (2009) Plasma phos-phorylated-TDP- 43 protein levels correlate with brain pathology in frontotemporal lobar degeneration. Acta Neuropathol 118(5):647-658.
    • (2009) Acta Neuropathol , vol.118 , Issue.5 , pp. 647-658
    • Foulds, P.G.1    Davidson, Y.2    Mishra, M.3
  • 43
    • 70449526373 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: Toward the end of conFUSion
    • Frank S, Tolnay M (2009) Frontotemporal lobar degeneration: toward the end of conFUSion. Acta Neuropathol 118:629-631.
    • (2009) Acta Neuropathol , vol.118 , pp. 629-631
    • Frank, S.1    Tolnay, M.2
  • 45
    • 47749133805 scopus 로고    scopus 로고
    • Co-localization of tau and alpha-synuclein in the olfactory bulb in Alzheimer's disease with amygdala Lewy bodies
    • Fujishiro H, Tsuboi Y, Lin WL, Uchikado H, Dickson DW (2008) Co-localization of tau and alpha-synuclein in the olfactory bulb in Alzheimer's disease with amygdala Lewy bodies. Acta Neuropathol 116:17-24.
    • (2008) Acta Neuropathol , vol.116 , pp. 17-24
    • Fujishiro, H.1    Tsuboi, Y.2    Lin, W.L.3    Uchikado, H.4    Dickson, D.W.5
  • 46
    • 59249100854 scopus 로고    scopus 로고
    • Accumulation of phosphorylated TDP-43 in brains of patients with argyrophilic grain disease
    • Fujishiro H, Uchikado H, Arai T et al (2009) Accumulation of phosphorylated TDP-43 in brains of patients with argyrophilic grain disease. Acta Neuropathol 117:151-158.
    • (2009) Acta Neuropathol , vol.117 , pp. 151-158
    • Fujishiro, H.1    Uchikado, H.2    Arai, T.3
  • 47
    • 51849117597 scopus 로고    scopus 로고
    • Immunohistochemical identification of messenger RNA-related proteins in basophilic inclusions of adult-onset atypical motor neuron disease
    • Fujita K, Ito H, Nakano S, Kinoshita Y, Wate R, Kusaka H (2008) Immunohistochemical identification of messenger RNA-related proteins in basophilic inclusions of adult-onset atypical motor neuron disease. Acta Neuropathol 116:439-445.
    • (2008) Acta Neuropathol , vol.116 , pp. 439-445
    • Fujita, K.1    Ito, H.2    Nakano, S.3    Kinoshita, Y.4    Wate, R.5    Kusaka, H.6
  • 48
    • 0036174010 scopus 로고    scopus 로고
    • Alpha-Synuclein is phosphorylated in synucleinopathy lesions
    • Fujiwara H, Hasegawa M, Dohmae N et al (2002) alpha-Synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol 4:160-164.
    • (2002) Nat Cell Biol , vol.4 , pp. 160-164
    • Fujiwara, H.1    Hasegawa, M.2    Dohmae, N.3
  • 49
    • 46749121818 scopus 로고    scopus 로고
    • A novel human disease with abnormal prion protein sensitive to protease
    • Gambetti P, Dong Z, Yuan J et al (2008) A novel human disease with abnormal prion protein sensitive to protease. Ann Neurol 63:697-708.
    • (2008) Ann Neurol , vol.63 , pp. 697-708
    • Gambetti, P.1    Dong, Z.2    Yuan, J.3
  • 50
    • 68349125007 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: The TDP-43 diseases
    • Geser F, Martinez-Lage M, Kwong LK, Lee VM, Trojanowski JQ (2009) Amyotrophic lateral sclerosis, frontotemporal dementia and beyond: the TDP-43 diseases. J Neurol 256:1205-1214.
    • (2009) J Neurol , vol.256 , pp. 1205-1214
    • Geser, F.1    Martinez-Lage, M.2    Kwong, L.K.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 51
    • 60549117972 scopus 로고    scopus 로고
    • Clinical and pathological continuum of multisystem TDP-43 proteinopathies
    • Geser F, Martinez-Lage M, Robinson J et al (2009) Clinical and pathological continuum of multisystem TDP-43 proteinopathies. Arch Neurol 66:180-189.
    • (2009) Arch Neurol , vol.66 , pp. 180-189
    • Geser, F.1    Martinez-Lage, M.2    Robinson, J.3
  • 54
    • 53849100694 scopus 로고    scopus 로고
    • Tauopathy in human and experimental variant Creutzfeldt-Jakob disease
    • Giaccone G, Mangieri M, Capobianco R et al (2008) Tauopathy in human and experimental variant Creutzfeldt-Jakob disease. Neurobiol Aging 29:1864-1873.
    • (2008) Neurobiol Aging , vol.29 , pp. 1864-1873
    • Giaccone, G.1    Mangieri, M.2    Capobianco, R.3
  • 55
    • 56149116672 scopus 로고    scopus 로고
    • Atypical tau-opathy with massive involvement of the white matter
    • Giaccone G, Marcon G, Mangieri M et al (2008) Atypical tau-opathy with massive involvement of the white matter. Neuropathol Appl Neurobiol 34:468-472.
    • (2008) Neuropathol Appl Neurobiol , vol.34 , pp. 468-472
    • Giaccone, G.1    Marcon, G.2    Mangieri, M.3
  • 56
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • Giasson BI, Duda JE, Murray IV et al (2000) Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 290:985-989.
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3
  • 58
    • 0027984739 scopus 로고
    • Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: Identification of phosphorylation sites in tau protein
    • Goedert M, Jakes R, Crowther RA et al (1994) Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem J 301(Pt 3):871-877.
    • (1994) Biochem J , vol.301 , Issue.PART 3 , pp. 871-877
    • Goedert, M.1    Jakes, R.2    Crowther, R.A.3
  • 59
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA (1989) Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron 3:519-526.
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 60
    • 0029902166 scopus 로고    scopus 로고
    • Evidence of neuronal oxidative damage in Alzheimer's disease
    • Good PF, Werner P, Hsu A, Olanow CW, Perl DP (1996) Evidence of neuronal oxidative damage in Alzheimer's disease. Am J Pathol 149:21-28.
    • (1996) Am J Pathol , vol.149 , pp. 21-28
    • Good, P.F.1    Werner, P.2    Hsu, A.3    Olanow, C.W.4    Perl, D.P.5
  • 61
    • 62049086159 scopus 로고    scopus 로고
    • Biomarkers for Parkinson's disease
    • Graeber MB (2009) Biomarkers for Parkinson's disease. Exp Neurol 216:249-253.
    • (2009) Exp Neurol , vol.216 , pp. 249-253
    • Graeber, M.B.1
  • 62
    • 34247604427 scopus 로고    scopus 로고
    • Phosphorylation and cleavage of tau in non-AD tauopathies
    • Guillozet-Bongaarts AL, Glajch KE et al (2007) Phosphorylation and cleavage of tau in non-AD tauopathies. Acta Neuropathol 113:513-520.
    • (2007) Acta Neuropathol , vol.113 , pp. 513-520
    • Guillozet-Bongaarts, A.L.1    Glajch, K.E.2
  • 63
    • 0036938637 scopus 로고    scopus 로고
    • Alpha-synuclein-immunoreactive deposits in human and animal prion diseases
    • Haik S, Privat N, Adjou KT et al (2002) Alpha-synuclein-immunoreactive deposits in human and animal prion diseases. Acta Neuropathol 103:516-520.
    • (2002) Acta Neuropathol , vol.103 , pp. 516-520
    • Haik, S.1    Privat, N.2    Adjou, K.T.3
  • 65
    • 61849088424 scopus 로고    scopus 로고
    • Tau phosphorylation: The therapeutic challenge for neurodegenerative disease
    • Hanger DP, Anderton BH, Noble W (2009) Tau phosphorylation: the therapeutic challenge for neurodegenerative disease. Trends Mol Med 15:112-119.
    • (2009) Trends Mol Med , vol.15 , pp. 112-119
    • Hanger, D.P.1    Anderton, B.H.2    Noble, W.3
  • 66
    • 34548191034 scopus 로고    scopus 로고
    • Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis
    • Hanger DP, Byers HL, Wray S et al (2007) Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis. J Biol Chem 282:23645-23654.
    • (2007) J Biol Chem , vol.282 , pp. 23645-23654
    • Hanger, D.P.1    Byers, H.L.2    Wray, S.3
  • 67
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart GW (1997) Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu Rev Biochem 66:315-335.
    • (1997) Annu Rev Biochem , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 68
    • 34249709931 scopus 로고    scopus 로고
    • TDP-43 is deposited in the Guam parkinsonism-dementia complex brains
    • Hasegawa M, Arai T, Akiyama H et al (2007) TDP-43 is deposited in the Guam parkinsonism-dementia complex brains. Brain 130:1386-1394.
    • (2007) Brain , vol.130 , pp. 1386-1394
    • Hasegawa, M.1    Arai, T.2    Akiyama, H.3
  • 69
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M, Arai T, Nonaka T et al (2008) Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 64:60-70.
    • (2008) Ann Neurol , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3
  • 70
    • 0033578402 scopus 로고    scopus 로고
    • The A beta 3-pyroglutamyl and 11-pyroglutamyl peptides found in senile plaque have greater beta-sheet forming and aggregation propensities in vitro than full-length a beta
    • He W, Barrow CJ (1999) The A beta 3-pyroglutamyl and 11-pyroglutamyl peptides found in senile plaque have greater beta-sheet forming and aggregation propensities in vitro than full-length A beta. Biochemistry 38:10871-10877.
    • (1999) Biochemistry , vol.38 , pp. 10871-10877
    • He, W.1    Barrow, C.J.2
  • 71
    • 0032531735 scopus 로고    scopus 로고
    • Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation
    • Hensley K, Maidt ML, Yu Z, Sang H, Markesbery WR, Floyd RA (1998) Electrochemical analysis of protein nitrotyrosine and dityrosine in the Alzheimer brain indicates region-specific accumulation. J Neurosci 18:8126-8132.
    • (1998) J Neurosci , vol.18 , pp. 8126-8132
    • Hensley, K.1    Maidt, M.L.2    Yu, Z.3    Sang, H.4    Markesbery, W.R.5    Floyd, R.A.6
  • 72
    • 36348972414 scopus 로고    scopus 로고
    • Concurrence of TDP-43, tau and alpha-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies
    • Higashi S, Iseki E, Yamamoto R et al (2007) Concurrence of TDP-43, tau and alpha-synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies. Brain Res 1184:284-294.
    • (2007) Brain Res , vol.1184 , pp. 284-294
    • Higashi, S.1    Iseki, E.2    Yamamoto, R.3
  • 73
    • 0037677595 scopus 로고    scopus 로고
    • Molecular classification of sporadic Creutzfeldt-Jakob disease
    • Hill AF, Joiner S, Wadsworth JD et al (2003) Molecular classification of sporadic Creutzfeldt-Jakob disease. Brain 126:1333-1346.
    • (2003) Brain , vol.126 , pp. 1333-1346
    • Hill, A.F.1    Joiner, S.2    Wadsworth, J.D.3
  • 75
    • 9144229591 scopus 로고    scopus 로고
    • Functional consequences of alpha-synuclein tyrosine nitration: Diminished binding to lipid vesicles and increased fibril formation
    • Hodara R, Norris EH, Giasson BI et al (2004) Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation. J Biol Chem 279:47746-47753.
    • (2004) J Biol Chem , vol.279 , pp. 47746-47753
    • Hodara, R.1    Norris, E.H.2    Giasson, B.I.3
  • 76
    • 0030750558 scopus 로고    scopus 로고
    • Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites
    • Hoffmann R, Lee VM, Leight S, Varga I, Otvos L Jr (1997) Unique Alzheimer's disease paired helical filament specific epitopes involve double phosphorylation at specific sites. Biochemistry 36:8114-8124.
    • (1997) Biochemistry , vol.36 , pp. 8114-8124
    • Hoffmann, R.1    Lee, V.M.2    Leight, S.3    Varga, I.4    Otvos Jr., L.5
  • 77
    • 0042926482 scopus 로고    scopus 로고
    • Nitration of tau protein is linked to neurodegeneration in tauopathies
    • Horiguchi T, Uryu K, Giasson BI et al (2003) Nitration of tau protein is linked to neurodegeneration in tauopathies. Am J Pathol 163:1021-1031.
    • (2003) Am J Pathol , vol.163 , pp. 1021-1031
    • Horiguchi, T.1    Uryu, K.2    Giasson, B.I.3
  • 79
    • 47949084000 scopus 로고    scopus 로고
    • Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease
    • Hu WT, Josephs KA, Knopman DS et al (2008) Temporal lobar predominance of TDP-43 neuronal cytoplasmic inclusions in Alzheimer disease. Acta Neuropathol 116:215-220.
    • (2008) Acta Neuropathol , vol.116 , pp. 215-220
    • Hu, W.T.1    Josephs, K.A.2    Knopman, D.S.3
  • 81
    • 46749138739 scopus 로고    scopus 로고
    • Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplas-mic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Igaz LM, Kwong LK, Xu Y et al (2008) Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplas-mic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am J Pathol 173:182-194.
    • (2008) Am J Pathol , vol.173 , pp. 182-194
    • Igaz, L.M.1    Kwong, L.K.2    Xu, Y.3
  • 82
    • 27644583266 scopus 로고    scopus 로고
    • Subgroups of Alzheimer's disease based on cerebrospinal fluid molecular markers
    • Iqbal K, Flory M, Khatoon S et al (2005) Subgroups of Alzheimer's disease based on cerebrospinal fluid molecular markers. Ann Neurol 58:748-757.
    • (2005) Ann Neurol , vol.58 , pp. 748-757
    • Iqbal, K.1    Flory, M.2    Khatoon, S.3
  • 84
    • 0033537922 scopus 로고    scopus 로고
    • Frequent coexistence of Lewy bodies and neurofibrillary tangles in the same neurons of patients with diffuse Lewy body disease
    • Iseki E, Marui W, Kosaka K, Ueda K (1999) Frequent coexistence of Lewy bodies and neurofibrillary tangles in the same neurons of patients with diffuse Lewy body disease. Neurosci Lett 265:9-12.
    • (1999) Neurosci Lett , vol.265 , pp. 9-12
    • Iseki, E.1    Marui, W.2    Kosaka, K.3    Ueda, K.4
  • 85
    • 0037365572 scopus 로고    scopus 로고
    • Dementia with Lewy bodies from the perspective of tauopathy
    • Iseki E, Togo T, Suzuki K et al (2003) Dementia with Lewy bodies from the perspective of tauopathy. Acta Neuropathol 105:265-270.
    • (2003) Acta Neuropathol , vol.105 , pp. 265-270
    • Iseki, E.1    Togo, T.2    Suzuki, K.3
  • 87
    • 0028169925 scopus 로고
    • Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: Evidence that an initially deposited species is A beta 42(43)
    • Iwatsubo T, Odaka A, Suzuki N, Mizusawa H, Nukina N, Ihara Y (1994) Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43). Neuron 13:45-53.
    • (1994) Neuron , vol.13 , pp. 45-53
    • Iwatsubo, T.1    Odaka, A.2    Suzuki, N.3    Mizusawa, H.4    Nukina, N.5    Ihara, Y.6
  • 88
    • 0029849644 scopus 로고    scopus 로고
    • Full-length amyloid-beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques
    • Iwatsubo T, Saido TC, Mann DM, Lee VM, Trojanowski JQ (1996) Full-length amyloid-beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques. Am J Pathol 149:1823-1830.
    • (1996) Am J Pathol , vol.149 , pp. 1823-1830
    • Iwatsubo, T.1    Saido, T.C.2    Mann, D.M.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 89
    • 68349109646 scopus 로고    scopus 로고
    • Absence of alpha-synuclein pathology in postencephalitic parkinsonism
    • Jellinger KA (2009) Absence of alpha-synuclein pathology in postencephalitic parkinsonism. Acta Neuropathol 118:371-379.
    • (2009) Acta Neuropathol , vol.118 , pp. 371-379
    • Jellinger, K.A.1
  • 90
    • 59349092999 scopus 로고    scopus 로고
    • Criteria for the neuropathological diagnosis of dementing disorders: Routes out of the swamp?
    • Jellinger KA (2009) Criteria for the neuropathological diagnosis of dementing disorders: routes out of the swamp? Acta Neuro-pathol 117:101-110.
    • (2009) Acta Neuro-pathol , vol.117 , pp. 101-110
    • Jellinger, K.A.1
  • 91
    • 7944238570 scopus 로고    scopus 로고
    • Lewy body-related alpha-synucleinopathy in the aged human brain
    • Jellinger KA (2004) Lewy body-related alpha-synucleinopathy in the aged human brain. J Neural Transm 111:1219-1235.
    • (2004) J Neural Transm , vol.111 , pp. 1219-1235
    • Jellinger, K.A.1
  • 92
    • 34547762298 scopus 로고    scopus 로고
    • More frequent Lewy bodies but less frequent Alzheimer-type lesions in multiple system atrophy as compared to age-matched control brains
    • Jellinger KA (2007) More frequent Lewy bodies but less frequent Alzheimer-type lesions in multiple system atrophy as compared to age-matched control brains. Acta Neuropathol 114:299-303.
    • (2007) Acta Neuropathol , vol.114 , pp. 299-303
    • Jellinger, K.A.1
  • 93
    • 69549103145 scopus 로고    scopus 로고
    • Recent advances in our understanding of neurodegeneration
    • Jellinger KA (2009) Recent advances in our understanding of neurodegeneration. J Neural Transm 116:1111-1162.
    • (2009) J Neural Transm , vol.116 , pp. 1111-1162
    • Jellinger, K.A.1
  • 94
    • 34249814045 scopus 로고    scopus 로고
    • Neuropathological evaluation of mixed dementia
    • Jellinger KA, Attems J (2007) Neuropathological evaluation of mixed dementia. J Neurol Sci 257:80-87.
    • (2007) J Neurol Sci , vol.257 , pp. 80-87
    • Jellinger, K.A.1    Attems, J.2
  • 95
    • 0028865755 scopus 로고
    • Ischemic stress induces deposition of amyloid beta immunoreactivity in human brain
    • Jendroska K, Poewe W, Daniel SE et al (1995) Ischemic stress induces deposition of amyloid beta immunoreactivity in human brain. Acta Neuropathol 90:461-466.
    • (1995) Acta Neuropathol , vol.90 , pp. 461-466
    • Jendroska, K.1    Poewe, W.2    Daniel, S.E.3
  • 96
    • 33745007339 scopus 로고    scopus 로고
    • Atypical progressive supranuclear palsy with corticospinal tract degeneration
    • Josephs KA, Katsuse O, Beccano-Kelly DA et al (2006) Atypical progressive supranuclear palsy with corticospinal tract degeneration. J Neuropathol Exp Neurol 65:396-405.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 396-405
    • Josephs, K.A.1    Katsuse, O.2    Beccano-Kelly, D.A.3
  • 97
    • 68349088087 scopus 로고    scopus 로고
    • Evaluation of subcortical pathology and clinical correlations in FTLD-U subtypes
    • Josephs KA, Stroh A, Dugger B, Dickson DW (2009) Evaluation of subcortical pathology and clinical correlations in FTLD-U subtypes. Acta Neuropathol 118:349-358.
    • (2009) Acta Neuropathol , vol.118 , pp. 349-358
    • Josephs, K.A.1    Stroh, A.2    Dugger, B.3    Dickson, D.W.4
  • 98
    • 39749088863 scopus 로고    scopus 로고
    • Argyrophilic grains: A distinct disease or an additive pathology?
    • Josephs KA, Whitwell JL, Parisi JE et al (2008) Argyrophilic grains: a distinct disease or an additive pathology? Neurobiol Aging 29:566-573.
    • (2008) Neurobiol Aging , vol.29 , pp. 566-573
    • Josephs, K.A.1    Whitwell, J.L.2    Parisi, J.E.3
  • 99
    • 0037452813 scopus 로고    scopus 로고
    • Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies
    • Junn E, Ronchetti RD, Quezado MM, Kim SY, Mouradian MM (2003) Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2047-2052
    • Junn, E.1    Ronchetti, R.D.2    Quezado, M.M.3    Kim, S.Y.4    Mouradian, M.M.5
  • 100
    • 70349308579 scopus 로고    scopus 로고
    • Regional distribution of TDP-43 inclusions in Alzheimer disease (AD) brains: Their relation to AD common pathology
    • Kadokura A, Yamazaki T, Lemere CA, Takatama M, Okamoto K (2009) Regional distribution of TDP-43 inclusions in Alzheimer disease (AD) brains: their relation to AD common pathology. Neuropathology 29:566-573.
    • (2009) Neuropathology , vol.29 , pp. 566-573
    • Kadokura, A.1    Yamazaki, T.2    Lemere, C.A.3    Takatama, M.4    Okamoto, K.5
  • 102
    • 70449523595 scopus 로고    scopus 로고
    • The morbid anatomy of dementia in Parkinson's disease
    • Kalaitzakis ME, Pearce RK (2009) The morbid anatomy of dementia in Parkinson's disease. Acta Neuropathol 118:587-598.
    • (2009) Acta Neuropathol , vol.118 , pp. 587-598
    • Kalaitzakis, M.E.1    Pearce, R.K.2
  • 103
    • 57049149602 scopus 로고    scopus 로고
    • Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis
    • Kasai T, Tokuda T, Ishigami N et al (2009) Increased TDP-43 protein in cerebrospinal fluid of patients with amyotrophic lateral sclerosis. Acta Neuropathol 117:55-62.
    • (2009) Acta Neuropathol , vol.117 , pp. 55-62
    • Kasai, T.1    Tokuda, T.2    Ishigami, N.3
  • 104
    • 41749115922 scopus 로고    scopus 로고
    • Cleavage of normal and pathological forms of alpha-synuclein by neurosin in vitro
    • Kasai T, Tokuda T, Yamaguchi N et al (2008) Cleavage of normal and pathological forms of alpha-synuclein by neurosin in vitro. Neurosci Lett 436:52-56.
    • (2008) Neurosci Lett , vol.436 , pp. 52-56
    • Kasai, T.1    Tokuda, T.2    Yamaguchi, N.3
  • 105
    • 33845937335 scopus 로고    scopus 로고
    • Dyrk1A phosphorylates alpha-synuclein and enhances intracellular inclusion formation
    • Kim EJ, Sung JY, Lee HJ et al (2006) Dyrk1A phosphorylates alpha-synuclein and enhances intracellular inclusion formation. J Biol Chem 281:33250-33257.
    • (2006) J Biol Chem , vol.281 , pp. 33250-33257
    • Kim, E.J.1    Sung, J.Y.2    Lee, H.J.3
  • 106
    • 0027361281 scopus 로고
    • Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease
    • Kopke E, Tung YC, Shaikh S, Alonso AC, Iqbal K, Grundke-Iqbal I (1993) Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J Biol Chem 268:24374-24384.
    • (1993) J Biol Chem , vol.268 , pp. 24374-24384
    • Kopke, E.1    Tung, Y.C.2    Shaikh, S.3    Alonso, A.C.4    Iqbal, K.5    Grundke-Iqbal, I.6
  • 107
    • 53449094371 scopus 로고    scopus 로고
    • Mixed brain pathologies in dementia: The BrainNet Europe consortium experience
    • Kovacs GG, Alafuzoff I, Al-Sarraj S et al (2008) Mixed brain pathologies in dementia: the BrainNet Europe consortium experience. Dement Geriatr Cogn Disord 26:343-350.
    • (2008) Dement Geriatr Cogn Disord , vol.26 , pp. 343-350
    • Kovacs, G.G.1    Alafuzoff, I.2    Al-Sarraj, S.3
  • 108
    • 63449087340 scopus 로고    scopus 로고
    • Molecular pathology of human prion diseases
    • Kovacs GG, Budka H (2009) Molecular pathology of human prion diseases. Int J Mol Sci 10:976-999.
    • (2009) Int J Mol Sci , vol.10 , pp. 976-999
    • Kovacs, G.G.1    Budka, H.2
  • 109
    • 63449123544 scopus 로고    scopus 로고
    • Protein-based neuropathology and molecular classification of human neurodegenerative diseases
    • Ovadi J, Orosz F (eds), Springer, the Netherlands
    • Kovacs GG, Budka H (2009) Protein-based neuropathology and molecular classification of human neurodegenerative diseases. In: Ovadi J, Orosz F (eds) Protein folding and misfolding: neu-rodegenerative diseases. Springer, the Netherlands, pp 251-272.
    • (2009) Protein Folding and Misfolding: Neu-rodegenerative Diseases , pp. 251-272
    • Kovacs, G.G.1    Budka, H.2
  • 110
    • 34447344086 scopus 로고    scopus 로고
    • Involvement of the endosomal-lysosomal system correlates with regional pathology in Creutzfeldt-Jakob disease
    • Kovacs GG, Gelpi E, Ströbel T et al (2007) Involvement of the endosomal-lysosomal system correlates with regional pathology in Creutzfeldt-Jakob disease. J Neuropathol Exp Neurol 66:628636.
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 628636
    • Kovacs, G.G.1    Gelpi, E.2    Ströbel, T.3
  • 111
    • 54449096081 scopus 로고    scopus 로고
    • White matter tauopathy with globular glial inclusions: A distinct sporadic frontotemporal lobar degeneration
    • Kovacs GG, Majtenyi K, Spina S et al (2008) White matter tauopathy with globular glial inclusions: a distinct sporadic frontotemporal lobar degeneration. J Neuropathol Exp Neurol 67:963-975.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 963-975
    • Kovacs, G.G.1    Majtenyi, K.2    Spina, S.3
  • 112
    • 53149130592 scopus 로고    scopus 로고
    • Nigral burden of alpha-synuclein correlates with striatal dopamine deficit
    • Kovacs GG, Milenkovic IJ, Preusser M, Budka H (2008) Nigral burden of alpha-synuclein correlates with striatal dopamine deficit. Mov Disord 23:1608-1612.
    • (2008) Mov Disord , vol.23 , pp. 1608-1612
    • Kovacs, G.G.1    Milenkovic, I.J.2    Preusser, M.3    Budka, H.4
  • 113
    • 0037031611 scopus 로고    scopus 로고
    • The prion protein in human neurodegenerative disorders
    • Kovacs GG, Zerbi P, Voigtlander T et al (2002) The prion protein in human neurodegenerative disorders. Neurosci Lett 329:269-272.
    • (2002) Neurosci Lett , vol.329 , pp. 269-272
    • Kovacs, G.G.1    Zerbi, P.2    Voigtlander, T.3
  • 114
    • 33846997878 scopus 로고    scopus 로고
    • Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies
    • Kramer ML, Schulz-Schaeffer WJ (2007) Presynaptic alpha-synuclein aggregates, not Lewy bodies, cause neurodegeneration in dementia with Lewy bodies. J Neurosci 27:1405-1410.
    • (2007) J Neurosci , vol.27 , pp. 1405-1410
    • Kramer, M.L.1    Schulz-Schaeffer, W.J.2
  • 115
    • 0344305371 scopus 로고    scopus 로고
    • Morphogenesis of Lewy bodies: Dissimilar incorporation of alpha-synuclein, ubiquitin, and p62
    • Kuusisto E, Parkkinen L, Alafuzoff I (2003) Morphogenesis of Lewy bodies: dissimilar incorporation of alpha-synuclein, ubiquitin, and p62. J Neuropathol Exp Neurol 62:1241-1253.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 1241-1253
    • Kuusisto, E.1    Parkkinen, L.2    Alafuzoff, I.3
  • 116
    • 61349156118 scopus 로고    scopus 로고
    • Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis
    • Kwiatkowski TJ Jr, Bosco DA, Leclerc AL et al (2009) Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis. Science 323:1205-1208.
    • (2009) Science , vol.323 , pp. 1205-1208
    • Kwiatkowski Jr., T.J.1    Bosco, D.A.2    Leclerc, A.L.3
  • 117
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert MP, Barlow AK, Chromy BA et al (1998) Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci USA 95:6448-6453.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3
  • 118
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers
    • Lauren J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature 457:1128-1132.
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Lauren, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 119
    • 27144512435 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and neurodegenerative disorders
    • Layfield R, Lowe J, Bedford L (2005) The ubiquitin-proteasome system and neurodegenerative disorders. Essays Biochem 41:157-171.
    • (2005) Essays Biochem , vol.41 , pp. 157-171
    • Layfield, R.1    Lowe, J.2    Bedford, L.3
  • 120
    • 0024675418 scopus 로고
    • The microtubule binding domain of tau protein
    • Lee G, Neve RL, Kosik KS (1989) The microtubule binding domain of tau protein. Neuron 2:1615-1624.
    • (1989) Neuron , vol.2 , pp. 1615-1624
    • Lee, G.1    Neve, R.L.2    Kosik, K.S.3
  • 121
    • 12144288564 scopus 로고    scopus 로고
    • Phosphorylation of tau by fyn: Implications for Alzheimer's disease
    • Lee G, Thangavel R, Sharma VM et al (2004) Phosphorylation of tau by fyn: implications for Alzheimer's disease. J Neurosci 24:2304-2312.
    • (2004) J Neurosci , vol.24 , pp. 2304-2312
    • Lee, G.1    Thangavel, R.2    Sharma, V.M.3
  • 123
    • 0037454755 scopus 로고    scopus 로고
    • Evidence of a balance between phosphorylation and O-GlcNAc glyco-sylation of Tau proteins-A role in nuclear localization
    • Lefebvre T, Ferreira S, Dupont-Wallois L et al (2003) Evidence of a balance between phosphorylation and O-GlcNAc glyco-sylation of Tau proteins-a role in nuclear localization. Biochim Biophys Acta 1619:167-176.
    • (2003) Biochim Biophys Acta , vol.1619 , pp. 167-176
    • Lefebvre, T.1    Ferreira, S.2    Dupont-Wallois, L.3
  • 124
    • 33947537591 scopus 로고    scopus 로고
    • Proteomic identification of novel proteins in cortical Lewy bodies
    • Leverenz JB, Umar I, Wang Q et al (2007) Proteomic identification of novel proteins in cortical Lewy bodies. Brain Pathol 17:139-145.
    • (2007) Brain Pathol , vol.17 , pp. 139-145
    • Leverenz, J.B.1    Umar, I.2    Wang, Q.3
  • 125
    • 0031852471 scopus 로고    scopus 로고
    • The frequency of Lewy bodies in a consecutive autopsy series
    • Lindboe CF, Hansen HB (1998) The frequency of Lewy bodies in a consecutive autopsy series. Clin Neuropathol 17:204-209.
    • (1998) Clin Neuropathol , vol.17 , pp. 204-209
    • Lindboe, C.F.1    Hansen, H.B.2
  • 126
    • 0034885731 scopus 로고    scopus 로고
    • Age-dependent deamidation of asparagine residues in proteins
    • Lindner H, Helliger W (2001) Age-dependent deamidation of asparagine residues in proteins. Exp Gerontol 36:1551-1563.
    • (2001) Exp Gerontol , vol.36 , pp. 1551-1563
    • Lindner, H.1    Helliger, W.2
  • 127
    • 20744442130 scopus 로고    scopus 로고
    • A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: Implications for pathogenesis of Parkinson disease
    • Liu CW, Giasson BI, Lewis KA, Lee VM, Demartino GN, Thomas PJ (2005) A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease. J Biol Chem 280:22670-22678.
    • (2005) J Biol Chem , vol.280 , pp. 22670-22678
    • Liu, C.W.1    Giasson, B.I.2    Lewis, K.A.3    Lee, V.M.4    Demartino, G.N.5    Thomas, P.J.6
  • 128
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • Liu F, Iqbal K, Grundke-Iqbal I, Hart GW, Gong CX (2004) O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc Natl Acad Sci USA 101:10804-10809.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 129
    • 64049092888 scopus 로고    scopus 로고
    • Association of alpha-synuclein immunoreactivity with inflammatory activity in multiple sclerosis lesions
    • Lu JQ, Fan Y, Mitha AP, Bell R, Metz L, Moore GR, Yong VW (2009) Association of alpha-synuclein immunoreactivity with inflammatory activity in multiple sclerosis lesions. J Neuropa-thol Exp Neurol 68:179-189.
    • (2009) J Neuropa-thol Exp Neurol , vol.68 , pp. 179-189
    • Lu, J.Q.1    Fan, Y.2    Mitha, A.P.3    Bell, R.4    Metz, L.5    Moore, G.R.6    Yong, V.W.7
  • 130
    • 38049030324 scopus 로고    scopus 로고
    • Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease
    • Luna-Munoz J, Chavez-Macias L, Garcia-Sierra F, Mena R (2007) Earliest stages of tau conformational changes are related to the appearance of a sequence of specific phospho-dependent tau epitopes in Alzheimer's disease. J Alzheimers Dis 12:365-375.
    • (2007) J Alzheimers Dis , vol.12 , pp. 365-375
    • Luna-Munoz, J.1    Chavez-Macias, L.2    Garcia-Sierra, F.3    Mena, R.4
  • 131
    • 77649187519 scopus 로고    scopus 로고
    • Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update
    • Mackenzie IR, Neumann M, Bigio EH et al (2010) Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update. Acta Neuropathol 119:1-4.
    • (2010) Acta Neuropathol , vol.119 , pp. 1-4
    • Mackenzie, I.R.1    Neumann, M.2    Bigio, E.H.3
  • 134
    • 60249089748 scopus 로고    scopus 로고
    • TDP-43 is not present in brain tissue of patients with schizophrenia
    • Mateen FJ, Josephs KA (2009) TDP-43 is not present in brain tissue of patients with schizophrenia. Schizophr Res 108:297-298.
    • (2009) Schizophr Res , vol.108 , pp. 297-298
    • Mateen, F.J.1    Josephs, K.A.2
  • 135
    • 68249157080 scopus 로고    scopus 로고
    • Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury
    • McKee AC, Cantu RC, Nowinski CJ et al (2009) Chronic traumatic encephalopathy in athletes: progressive tauopathy after repetitive head injury. J Neuropathol Exp Neurol 68:709-735.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 709-735
    • Mckee, A.C.1    Cantu, R.C.2    Nowinski, C.J.3
  • 136
    • 0029997922 scopus 로고    scopus 로고
    • Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease
    • Mena R, Edwards PC, Harrington CR, Mukaetova-Ladinska EB, Wischik CM (1996) Staging the pathological assembly of truncated tau protein into paired helical filaments in Alzheimer's disease. Acta Neuropathol 91:633-641.
    • (1996) Acta Neuropathol , vol.91 , pp. 633-641
    • Mena, R.1    Edwards, P.C.2    Harrington, C.R.3    Mukaetova-Ladinska, E.B.4    Wischik, C.M.5
  • 138
    • 68949099356 scopus 로고    scopus 로고
    • Total prion protein levels in the cerebrospinal fluid are reduced in patients with various neurological disorders
    • doi:12G39G6736J3K264[pii]10.3233/JAD-2009-1110
    • Meyne F, Gloeckner SF, Ciesielczyk B et al (2009) Total prion protein levels in the cerebrospinal fluid are reduced in patients with various neurological disorders. J Alzheimers Dis. doi:12G39G6736J3K264[pii]10.3233/JAD- 2009-1110.
    • (2009) J Alzheimers Dis.
    • Meyne, F.1    Gloeckner, S.F.2    Ciesielczyk, B.3
  • 139
    • 67349174242 scopus 로고    scopus 로고
    • Hippocampal sclerosis with four-repeat tau-positive round inclusions in the dentate gyrus: A new type of four-repeat tauopathy
    • Miki Y, Mori F, Hori E, Kaimori M, Wakabayashi K (2009) Hippocampal sclerosis with four-repeat tau-positive round inclusions in the dentate gyrus: a new type of four-repeat tauopathy. Acta Neuropathol 117:713-718.
    • (2009) Acta Neuropathol , vol.117 , pp. 713-718
    • Miki, Y.1    Mori, F.2    Hori, E.3    Kaimori, M.4    Wakabayashi, K.5
  • 140
    • 14844333173 scopus 로고    scopus 로고
    • Alpha-synuclein lesions in normal aging, Parkinson disease, and Alzheimer disease: Evidence from the Baltimore Longitudinal Study of Aging (BLSA)
    • Mikolaenko I, Pletnikova O, Kawas CH et al (2005) Alpha-synuclein lesions in normal aging, Parkinson disease, and Alzheimer disease: evidence from the Baltimore Longitudinal Study of Aging (BLSA). J Neuropathol Exp Neurol 64:156-162.
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 156-162
    • Mikolaenko, I.1    Pletnikova, O.2    Kawas, C.H.3
  • 141
    • 27744484059 scopus 로고    scopus 로고
    • Glial cell inclusions and the pathogenesis of neurodegenerative diseases
    • Miller DW, Cookson MR, Dickson DW (2004) Glial cell inclusions and the pathogenesis of neurodegenerative diseases. Neuron Glia Biol 1:13-21.
    • (2004) Neuron Glia Biol , vol.1 , pp. 13-21
    • Miller, D.W.1    Cookson, M.R.2    Dickson, D.W.3
  • 143
    • 0036942389 scopus 로고    scopus 로고
    • Pick's disease: Alpha-and beta-synuclein-immunoreactive Pick bodies in the dentate gyrus
    • Mori F, Hayashi S, Yamagishi S et al (2002) Pick's disease: alpha-and beta-synuclein-immunoreactive Pick bodies in the dentate gyrus. Acta Neuropathol 104:455-461.
    • (2002) Acta Neuropathol , vol.104 , pp. 455-461
    • Mori, F.1    Hayashi, S.2    Yamagishi, S.3
  • 144
    • 0028899714 scopus 로고
    • Proline-directed and non-proline-directed phosphorylation of PHF-tau
    • Morishima-Kawashima M, Hasegawa M, Takio K et al (1995) Proline-directed and non-proline-directed phosphorylation of PHF-tau. J Biol Chem 270:823-829.
    • (1995) J Biol Chem , vol.270 , pp. 823-829
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3
  • 145
    • 70449517359 scopus 로고    scopus 로고
    • FUS pathology in basophilic inclusion body disease
    • Munoz DG, Neumann M, Kusaka H et al (2009) FUS pathology in basophilic inclusion body disease. Acta Neuropathol 118:617-627.
    • (2009) Acta Neuropathol , vol.118 , pp. 617-627
    • Munoz, D.G.1    Neumann, M.2    Kusaka, H.3
  • 146
    • 41549154550 scopus 로고    scopus 로고
    • Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha-synucleinopathies
    • Muntane G, Dalfo E, Martinez A, Ferrer I (2008) Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha- synucleinopathies. Neuroscience 152:913-923.
    • (2008) Neuroscience , vol.152 , pp. 913-923
    • Muntane, G.1    Dalfo, E.2    Martinez, A.3    Ferrer, I.4
  • 147
    • 0038116620 scopus 로고    scopus 로고
    • Role of alpha-synuclein carboxy-terminus on fibril formation in vitro
    • Murray IV, Giasson BI, Quinn SM et al (2003) Role of alpha-synuclein carboxy-terminus on fibril formation in vitro. Biochemistry 42:8530-8540.
    • (2003) Biochemistry , vol.42 , pp. 8530-8540
    • Murray, I.V.1    Giasson, B.I.2    Quinn, S.M.3
  • 149
    • 34547733547 scopus 로고    scopus 로고
    • Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases
    • Nakashima-Yasuda H, Uryu K, Robinson J et al (2007) Co-morbidity of TDP-43 proteinopathy in Lewy body related diseases. Acta Neuropathol 114:221-229.
    • (2007) Acta Neuropathol , vol.114 , pp. 221-229
    • Nakashima-Yasuda, H.1    Uryu, K.2    Robinson, J.3
  • 150
    • 0028106152 scopus 로고
    • Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging
    • Naslund J, Schierhorn A, Hellman U et al (1994) Relative abundance of Alzheimer A beta amyloid peptide variants in Alzheimer disease and normal aging. Proc Natl Acad Sci USA 91:8378-8382.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8378-8382
    • Naslund, J.1    Schierhorn, A.2    Hellman, U.3
  • 151
    • 0036484302 scopus 로고    scopus 로고
    • Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation
    • Negro A, Brunati AM, Donella-Deana A, Massimino ML, Pinna LA (2002) Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation. FASEB J 16:210-212.
    • (2002) FASEB J , vol.16 , pp. 210-212
    • Negro, A.1    Brunati, A.M.2    Donella-Deana, A.3    Massimino, M.L.4    Pinna, L.A.5
  • 152
    • 4944267025 scopus 로고    scopus 로고
    • Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer's neurofibrillary tangles
    • Nemes Z, Devreese B, Steinert PM, Van Beeumen J, Fesus L (2004) Cross-linking of ubiquitin, HSP27, parkin, and alpha-synuclein by gamma-glutamyl-epsilon-lysine bonds in Alzheimer's neurofibrillary tangles. FASEB J 18:1135-1137.
    • (2004) FASEB J , vol.18 , pp. 1135-1137
    • Nemes, Z.1    Devreese, B.2    Steinert, P.M.3    Van, B.J.4    Fesus, L.5
  • 153
    • 70350437632 scopus 로고    scopus 로고
    • Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies
    • Nemes Z, Petrovski G, Aerts M, Sergeant K, Devreese B, Fesus L (2009) Transglutaminase-mediated intramolecular cross-linking of membrane-bound alpha-synuclein promotes amyloid formation in Lewy bodies. J Biol Chem 284:27252-27264.
    • (2009) J Biol Chem , vol.284 , pp. 27252-27264
    • Nemes, Z.1    Petrovski, G.2    Aerts, M.3    Sergeant, K.4    Devreese, B.5    Fesus, L.6
  • 154
    • 0036855635 scopus 로고    scopus 로고
    • Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies
    • Neumann M, Kahle PJ, Giasson BI et al (2002) Misfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathies. J Clin Invest 110:1429-1439.
    • (2002) J Clin Invest , vol.110 , pp. 1429-1439
    • Neumann, M.1    Kahle, P.J.2    Giasson, B.I.3
  • 155
    • 59249085091 scopus 로고    scopus 로고
    • Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies
    • Neumann M, Kwong LK, Lee EB et al (2009) Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies. Acta Neuropathol 117:137-149.
    • (2009) Acta Neuropathol , vol.117 , pp. 137-149
    • Neumann, M.1    Kwong, L.K.2    Lee, E.B.3
  • 158
    • 33749632259 scopus 로고    scopus 로고
    • Ubiqui-tinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK et al (2006) Ubiqui-tinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314:130-133.
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 159
    • 0022827447 scopus 로고
    • Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2
    • Neve RL, Harris P, Kosik KS, Kurnit DM, Donlon TA (1986) Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2. Brain Res 387:271-280.
    • (1986) Brain Res , vol.387 , pp. 271-280
    • Neve, R.L.1    Harris, P.2    Kosik, K.S.3    Kurnit, D.M.4    Donlon, T.A.5
  • 160
    • 24344508845 scopus 로고    scopus 로고
    • Caspase-cleaved tau accumulation in neurodegenerative diseases associated with tau and alpha-synuclein pathology
    • Newman J, Rissman RA, Sarsoza F et al (2005) Caspase-cleaved tau accumulation in neurodegenerative diseases associated with tau and alpha-synuclein pathology. Acta Neuropathol 110:135-144.
    • (2005) Acta Neuropathol , vol.110 , pp. 135-144
    • Newman, J.1    Rissman, R.A.2    Sarsoza, F.3
  • 161
    • 0033373675 scopus 로고    scopus 로고
    • Elevated transglutaminase-induced bonds in PHF tau in Alzheimer's disease
    • Norlund MA, Lee JM, Zainelli GM, Muma NA (1999) Elevated transglutaminase-induced bonds in PHF tau in Alzheimer's disease. Brain Res 851:154-163.
    • (1999) Brain Res , vol.851 , pp. 154-163
    • Norlund, M.A.1    Lee, J.M.2    Zainelli, G.M.3    Muma, N.A.4
  • 162
    • 41149084580 scopus 로고    scopus 로고
    • Relationship of phosphorylated alpha-synuclein and tau accumulation to Abeta deposition in the cerebral cortex of dementia with Lewy bodies
    • Obi K, Akiyama H, Kondo H et al (2008) Relationship of phosphorylated alpha-synuclein and tau accumulation to Abeta deposition in the cerebral cortex of dementia with Lewy bodies. Exp Neurol 210:409-420.
    • (2008) Exp Neurol , vol.210 , pp. 409-420
    • Obi, K.1    Akiyama, H.2    Kondo, H.3
  • 163
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou SH, Wu F, Harrich D, Garcia-Martinez LF, Gaynor RB (1995) Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol 69:3584-3596.
    • (1995) J Virol , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    Garcia-Martinez, L.F.4    Gaynor, R.B.5
  • 164
    • 65249162241 scopus 로고    scopus 로고
    • Detection of elevated levels of soluble alpha-synuclein oligomers in postmortem brain extracts from patients with dementia with Lewy bodies
    • Paleologou KE, Kragh CL, Mann DM et al (2009) Detection of elevated levels of soluble alpha-synuclein oligomers in postmortem brain extracts from patients with dementia with Lewy bodies. Brain 132:1093-1101.
    • (2009) Brain , vol.132 , pp. 1093-1101
    • Paleologou, K.E.1    Kragh, C.L.2    Mann, D.M.3
  • 165
    • 47749107973 scopus 로고    scopus 로고
    • Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein
    • Paleologou KE, Schmid AW, Rospigliosi CC et al (2008) Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein. J Biol Chem 283:16895-16905.
    • (2008) J Biol Chem , vol.283 , pp. 16895-16905
    • Paleologou, K.E.1    Schmid, A.W.2    Rospigliosi, C.C.3
  • 166
    • 33645343557 scopus 로고    scopus 로고
    • Upregulation of alpha-synuclein in neurons and glia in inflammatory demyelinating disease
    • Papadopoulos D, Ewans L, Pham-Dinh D, Knott J, Reynolds R (2006) Upregulation of alpha-synuclein in neurons and glia in inflammatory demyelinating disease. Mol Cell Neurosci 31:597-612.
    • (2006) Mol Cell Neurosci , vol.31 , pp. 597-612
    • Papadopoulos, D.1    Ewans, L.2    Pham-Dinh, D.3    Knott, J.4    Reynolds, R.5
  • 167
    • 0024843373 scopus 로고
    • Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome)
    • Papp MI, Kahn JE, Lantos PL (1989) Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome). J Neurol Sci 94:79-100.
    • (1989) J Neurol Sci , vol.94 , pp. 79-100
    • Papp, M.I.1    Kahn, J.E.2    Lantos, P.L.3
  • 168
    • 8944259890 scopus 로고    scopus 로고
    • Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease
    • Parchi P, Castellani R, Capellari S et al (1996) Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann Neurol 39:767-778.
    • (1996) Ann Neurol , vol.39 , pp. 767-778
    • Parchi, P.1    Castellani, R.2    Capellari, S.3
  • 169
    • 0032816292 scopus 로고    scopus 로고
    • Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects
    • Parchi P, Giese A, Capellari S et al (1999) Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann Neurol 46:224-233.
    • (1999) Ann Neurol , vol.46 , pp. 224-233
    • Parchi, P.1    Giese, A.2    Capellari, S.3
  • 170
    • 70449524296 scopus 로고    scopus 로고
    • Incidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with mixed phenotype and co-occurrence of PrP(Sc) types: An updated classification
    • Parchi P, Strammiello R, Notari S et al. (2009) Incidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with mixed phenotype and co-occurrence of PrP(Sc) types: an updated classification. Acta Neuropathol 118:659-671.
    • (2009) Acta Neuropathol , vol.118 , pp. 659-671
    • Parchi, P.1    Strammiello, R.2    Notari, S.3
  • 171
    • 34547400403 scopus 로고    scopus 로고
    • Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein
    • Parkin ET, Watt NT, Hussain I et al (2007) Cellular prion protein regulates beta-secretase cleavage of the Alzheimer's amyloid precursor protein. Proc Natl Acad Sci USA 104:11062-11067.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11062-11067
    • Parkin, E.T.1    Watt, N.T.2    Hussain, I.3
  • 172
    • 11144241275 scopus 로고    scopus 로고
    • Alpha-synuclein pathology does not predict extrapyra-midal symptoms or dementia
    • Parkkinen L, Kauppinen T, Pirttila T, Autere JM, Alafuzoff I (2005) Alpha-synuclein pathology does not predict extrapyra-midal symptoms or dementia. Ann Neurol 57:82-91.
    • (2005) Ann Neurol , vol.57 , pp. 82-91
    • Parkkinen, L.1    Kauppinen, T.2    Pirttila, T.3    Autere, J.M.4    Alafuzoff, I.5
  • 173
    • 0037383760 scopus 로고    scopus 로고
    • Regional distribution of alpha-synuclein pathology in unimpaired aging and Alzheimer disease
    • Parkkinen L, Soininen H, Alafuzoff I (2003) Regional distribution of alpha-synuclein pathology in unimpaired aging and Alzheimer disease. J Neuropathol Exp Neurol 62:363-367.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 363-367
    • Parkkinen, L.1    Soininen, H.2    Alafuzoff, I.3
  • 174
    • 63449129270 scopus 로고    scopus 로고
    • The role of cerebrospinal fluid proteins as early diagnostic markers for sporadic Creutzfeldt-Jakob disease
    • Pennington C, Chohan G, Mackenzie J et al (2009) The role of cerebrospinal fluid proteins as early diagnostic markers for sporadic Creutzfeldt-Jakob disease. Neurosci Lett 455:56-59.
    • (2009) Neurosci Lett , vol.455 , pp. 56-59
    • Pennington, C.1    Chohan, G.2    Mackenzie, J.3
  • 175
    • 33646392455 scopus 로고    scopus 로고
    • Neuropatho-logic features of amnestic mild cognitive impairment
    • Petersen RC, Parisi JE, Dickson DW et al (2006) Neuropatho-logic features of amnestic mild cognitive impairment. Arch Neurol 63:665-672.
    • (2006) Arch Neurol , vol.63 , pp. 665-672
    • Petersen, R.C.1    Parisi, J.E.2    Dickson, D.W.3
  • 176
    • 28844446287 scopus 로고    scopus 로고
    • Sporadic four-repeat tauopathy with frontotemporal degeneration, parkinsonism and motor neuron disease
    • Piao YS, Tan CF, Iwanaga K et al (2005) Sporadic four-repeat tauopathy with frontotemporal degeneration, parkinsonism and motor neuron disease. Acta Neuropathol 110:600-609.
    • (2005) Acta Neuropathol , vol.110 , pp. 600-609
    • Piao, Y.S.1    Tan, C.F.2    Iwanaga, K.3
  • 177
    • 10044281817 scopus 로고    scopus 로고
    • Lewy bodies in the amygdala: Increase of alpha-synuclein aggregates in neurodegenerative diseases with tau-based inclusions
    • Popescu A, Lippa CF, Lee VM, Trojanowski JQ (2004) Lewy bodies in the amygdala: increase of alpha-synuclein aggregates in neurodegenerative diseases with tau-based inclusions. Arch Neurol 61:1915-1919.
    • (2004) Arch Neurol , vol.61 , pp. 1915-1919
    • Popescu, A.1    Lippa, C.F.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 178
    • 0037592402 scopus 로고    scopus 로고
    • A novel leukoen-cephalopathy associated with tau deposits primarily in white matter glia
    • Powers JM, Byrne NP, Ito M et al (2003) A novel leukoen-cephalopathy associated with tau deposits primarily in white matter glia. Acta Neuropathol 106:181-187.
    • (2003) Acta Neuropathol , vol.106 , pp. 181-187
    • Powers, J.M.1    Byrne, N.P.2    Ito, M.3
  • 179
    • 26444439124 scopus 로고    scopus 로고
    • Individual and regional variations of phospho-tau species in progressive supranuclear palsy
    • Puig B, Rey MJ, Ferrer I (2005) Individual and regional variations of phospho-tau species in progressive supranuclear palsy. Acta Neuropathol 110:261-268.
    • (2005) Acta Neuropathol , vol.110 , pp. 261-268
    • Puig, B.1    Rey, M.J.2    Ferrer, I.3
  • 180
    • 33745259502 scopus 로고    scopus 로고
    • Alpha-synuclein is upregulated in neurones in response to chronic oxidative stress and is associated with neuroprotection
    • Quilty MC, King AE, Gai WP et al (2006) Alpha-synuclein is upregulated in neurones in response to chronic oxidative stress and is associated with neuroprotection. Exp Neurol 199:249-256.
    • (2006) Exp Neurol , vol.199 , pp. 249-256
    • Quilty, M.C.1    King, A.E.2    Gai, W.P.3
  • 181
    • 26444478269 scopus 로고    scopus 로고
    • Advanced glycation end products and RAGE: A common thread in aging, diabetes, neurodegeneration, and inflammation
    • Ramasamy R, Vannucci SJ, Yan SS, Herold K, Yan SF, Schmidt AM (2005) Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation. Glycobiology 15:16R-28R.
    • (2005) Glycobiology , vol.15
    • Ramasamy, R.1    Vannucci, S.J.2    Yan, S.S.3    Herold, K.4    Yan, S.F.5    Schmidt, A.M.6
  • 182
    • 35948933394 scopus 로고    scopus 로고
    • Classification and prediction of clinical Alzheimer's diagnosis based on plasma signaling proteins
    • Ray S, Britschgi M, Herbert C et al (2007) Classification and prediction of clinical Alzheimer's diagnosis based on plasma signaling proteins. Nat Med 13:1359-1362.
    • (2007) Nat Med , vol.13 , pp. 1359-1362
    • Ray, S.1    Britschgi, M.2    Herbert, C.3
  • 183
    • 47149100286 scopus 로고    scopus 로고
    • A possible link between astrocyte activation and tau nitration in Alzheimer's disease
    • Reyes JF, Reynolds MR, Horowitz PM et al (2008) A possible link between astrocyte activation and tau nitration in Alzheimer's disease. Neurobiol Dis 31:198-208.
    • (2008) Neurobiol Dis , vol.31 , pp. 198-208
    • Reyes, J.F.1    Reynolds, M.R.2    Horowitz, P.M.3
  • 184
    • 49649119504 scopus 로고    scopus 로고
    • Phosphoryla-tion regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases
    • Reynolds CH, Garwood CJ, Wray S et al (2008) Phosphoryla-tion regulates tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases. J Biol Chem 283:18177-18186.
    • (2008) J Biol Chem , vol.283 , pp. 18177-18186
    • Reynolds, C.H.1    Garwood, C.J.2    Wray, S.3
  • 185
    • 13444287877 scopus 로고    scopus 로고
    • Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: Implications for Alzheimer's disease
    • Reynolds MR, Berry RW, Binder LI (2005) Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease. Biochemistry 44:1690-1700.
    • (2005) Biochemistry , vol.44 , pp. 1690-1700
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 186
    • 33750940057 scopus 로고    scopus 로고
    • Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies
    • Reynolds MR, Reyes JF, Fu Y et al (2006) Tau nitration occurs at tyrosine 29 in the fibrillar lesions of Alzheimer's disease and other tauopathies. J Neurosci 26:10636-10645.
    • (2006) J Neurosci , vol.26 , pp. 10636-10645
    • Reynolds, M.R.1    Reyes, J.F.2    Fu, Y.3
  • 187
    • 73949142307 scopus 로고    scopus 로고
    • Amyloid-beta and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice
    • Rhein V, Song X, Wiesner A et al (2009) Amyloid-beta and tau synergistically impair the oxidative phosphorylation system in triple transgenic Alzheimer's disease mice. Proc Natl Acad Sci USA 106:20057-20062.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20057-20062
    • Rhein, V.1    Song, X.2    Wiesner, A.3
  • 188
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease
    • Roher AE, Lowenson JD, Clarke S et al (1993) Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 268:3072-3083.
    • (1993) J Biol Chem , vol.268 , pp. 3072-3083
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3
  • 189
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue
    • Roher AE, Palmer KC, Yurewicz EC, Ball MJ, Greenberg BD (1993) Morphological and biochemical analyses of amyloid plaque core proteins purified from Alzheimer disease brain tissue. J Neurochem 61:1916-1926.
    • (1993) J Neurochem , vol.61 , pp. 1916-1926
    • Roher, A.E.1    Palmer, K.C.2    Yurewicz, E.C.3    Ball, M.J.4    Greenberg, B.D.5
  • 190
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrP(Sc) molecules with different conformations
    • Safar J, Wille H, Itri V et al (1998) Eight prion strains have PrP(Sc) molecules with different conformations. Nat Med 4:1157-1165.
    • (1998) Nat Med , vol.4 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3
  • 191
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain
    • Saido TC, Yamao-Harigaya W, Iwatsubo T, Kawashima S (1996) Amino- and carboxyl-terminal heterogeneity of beta-amyloid peptides deposited in human brain. Neurosci Lett 215:173-176.
    • (1996) Neurosci Lett , vol.215 , pp. 173-176
    • Saido, T.C.1    Yamao-Harigaya, W.2    Iwatsubo, T.3    Kawashima, S.4
  • 192
    • 0037604508 scopus 로고    scopus 로고
    • Accumulation of phosphorylated alpha-synuclein in aging human brain
    • Saito Y, Kawashima A, Ruberu NN et al (2003) Accumulation of phosphorylated alpha-synuclein in aging human brain. J Neuropathol Exp Neurol 62:644-654.
    • (2003) J Neuropathol Exp Neurol , vol.62 , pp. 644-654
    • Saito, Y.1    Kawashima, A.2    Ruberu, N.N.3
  • 193
    • 35748959326 scopus 로고    scopus 로고
    • Neuropathology of mild cognitive impairment
    • Saito Y, Murayama S (2007) Neuropathology of mild cognitive impairment. Neuropathology 27:578-584.
    • (2007) Neuropathology , vol.27 , pp. 578-584
    • Saito, Y.1    Murayama, S.2
  • 194
    • 4444347376 scopus 로고    scopus 로고
    • Staging of argyr-ophilic grains: An age-associated tauopathy
    • Saito Y, Ruberu NN, Sawabe M et al (2004) Staging of argyr-ophilic grains: an age-associated tauopathy. J Neuropathol Exp Neurol 63:911-918.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 911-918
    • Saito, Y.1    Ruberu, N.N.2    Sawabe, M.3
  • 195
    • 61649090016 scopus 로고    scopus 로고
    • Delineation of early changes in cases with progressive supranuclear palsy-like pathology. Astrocytes in striatum are primary targets of tau phosphorylation and GFAP oxidation
    • Santpere G, Ferrer I (2009) Delineation of early changes in cases with progressive supranuclear palsy-like pathology. Astrocytes in striatum are primary targets of tau phosphorylation and GFAP oxidation. Brain Pathol 19:177-187.
    • (2009) Brain Pathol , vol.19 , pp. 177-187
    • Santpere, G.1    Ferrer, I.2
  • 196
    • 35748959415 scopus 로고    scopus 로고
    • Mixed brain pathologies account for most dementia cases in community-dwelling older persons
    • Schneider JA, Arvanitakis Z, Bang W, Bennett DA (2007) Mixed brain pathologies account for most dementia cases in community-dwelling older persons. Neurology 69:2197-2204.
    • (2007) Neurology , vol.69 , pp. 2197-2204
    • Schneider, J.A.1    Arvanitakis, Z.2    Bang, W.3    Bennett, D.A.4
  • 197
    • 70149097327 scopus 로고    scopus 로고
    • The neuropathology of probable Alzheimer disease and mild cognitive impairment
    • Schneider JA, Arvanitakis Z, Leurgans SE, Bennett DA (2009) The neuropathology of probable Alzheimer disease and mild cognitive impairment. Ann Neurol 66:200-208.
    • (2009) Ann Neurol , vol.66 , pp. 200-208
    • Schneider, J.A.1    Arvanitakis, Z.2    Leurgans, S.E.3    Bennett, D.A.4
  • 198
    • 12444337654 scopus 로고    scopus 로고
    • Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach
    • Sergeant N, Bombois S, Ghestem A et al (2003) Truncated beta-amyloid peptide species in pre-clinical Alzheimer's disease as new targets for the vaccination approach. J Neurochem 85:1581-1591.
    • (2003) J Neurochem , vol.85 , pp. 1581-1591
    • Sergeant, N.1    Bombois, S.2    Ghestem, A.3
  • 199
    • 10944223484 scopus 로고    scopus 로고
    • Tau protein as a differential biomarker of tauopathies
    • Sergeant N, Delacourte A, Buee L (2005) Tau protein as a differential biomarker of tauopathies. Biochim Biophys Acta 1739:179-197.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 179-197
    • Sergeant, N.1    Delacourte, A.2    Buee, L.3
  • 200
    • 0033009603 scopus 로고    scopus 로고
    • Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: Tau pathologies with exclusively "exon 10" iso-forms
    • Sergeant N, Wattez A, Delacourte A (1999) Neurofibrillary degeneration in progressive supranuclear palsy and corticobasal degeneration: tau pathologies with exclusively "exon 10" iso-forms. J Neurochem 72:1243-1249.
    • (1999) J Neurochem , vol.72 , pp. 1243-1249
    • Sergeant, N.1    Wattez, A.2    Delacourte, A.3
  • 202
    • 38149027097 scopus 로고    scopus 로고
    • Spinal cord tau pathology in cervical spondylotic myelopathy
    • Shimizu H, Kakita A, Takahashi H (2008) Spinal cord tau pathology in cervical spondylotic myelopathy. Acta Neuropathol 115:185-192.
    • (2008) Acta Neuropathol , vol.115 , pp. 185-192
    • Shimizu, H.1    Kakita, A.2    Takahashi, H.3
  • 203
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: Implications for Parkinson's disease
    • Shimura H, Schlossmacher MG, Hattori N et al (2001) Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 293:263-269.
    • (2001) Science , vol.293 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3
  • 204
    • 70449518182 scopus 로고    scopus 로고
    • Concomitant progressive supranuclear palsy and multiple system atrophy: More than a simple twist of fate?
    • Silveira-Moriyama L, Gonzalez AM, O'Sullivan SS et al (2009) Concomitant progressive supranuclear palsy and multiple system atrophy: more than a simple twist of fate? Neurosci Lett 467:208-211.
    • (2009) Neurosci Lett , vol.467 , pp. 208-211
    • Silveira-Moriyama, L.1    Gonzalez, A.M.2    O'Sullivan, S.S.3
  • 205
    • 0036134831 scopus 로고    scopus 로고
    • Transglutaminase bonds in neurofibrillary tangles and paired helical filament tau early in Alzheimer's disease
    • Singer SM, Zainelli GM, Norlund MA, Lee JM, Muma NA Transglutaminase bonds in neurofibrillary tangles and paired helical filament tau early in Alzheimer's disease. Neurochem Int 40:17-30.
    • Neurochem Int , vol.40 , pp. 17-30
    • Singer, S.M.1    Zainelli, G.M.2    Norlund, M.A.3    Lee, J.M.4    Muma, N.A.5
  • 207
    • 0025223441 scopus 로고
    • Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome
    • Snow AD, Mar H, Nochlin D et al (1990) Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome. Am J Pathol 137:1253-1270.
    • (1990) Am J Pathol , vol.137 , pp. 1253-1270
    • Snow, A.D.1    Mar, H.2    Nochlin, D.3
  • 208
    • 70349736190 scopus 로고    scopus 로고
    • Degeneration in different parkinsonian syndromes relates to astrocyte type and astrocyte protein expression
    • Song YJ, Halliday GM, Holton JL et al (2009) Degeneration in different parkinsonian syndromes relates to astrocyte type and astrocyte protein expression. J Neuropathol Exp Neurol 68:1073-1083.
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 1073-1083
    • Song, Y.J.1    Halliday, G.M.2    Holton, J.L.3
  • 209
    • 39049126210 scopus 로고    scopus 로고
    • Protein misfolding and neurode-generation
    • Soto C, Estrada LD (2008) Protein misfolding and neurode-generation. Arch Neurol 65:184-189.
    • (2008) Arch Neurol , vol.65 , pp. 184-189
    • Soto, C.1    Estrada, L.D.2
  • 210
    • 0032922482 scopus 로고    scopus 로고
    • Glycosylation of microtubule-associated protein tau in Alzheimer's disease brain
    • Takahashi M, Tsujioka Y, Yamada T et al (1999) Glycosylation of microtubule-associated protein tau in Alzheimer's disease brain. Acta Neuropathol 97:635-641.
    • (1999) Acta Neuropathol , vol.97 , pp. 635-641
    • Takahashi, M.1    Tsujioka, Y.2    Yamada, T.3
  • 211
    • 23844523232 scopus 로고    scopus 로고
    • Frontotemporal dementia with co-occurrence of astrocytic plaques and tufted astrocytes, and severe degeneration of the cerebral white matter: A variant of corticobasal degeneration?
    • Tan CF, Piao YS, Kakita A et al (2005) Frontotemporal dementia with co-occurrence of astrocytic plaques and tufted astrocytes, and severe degeneration of the cerebral white matter: a variant of corticobasal degeneration? Acta Neuropathol 109:329-338.
    • (2005) Acta Neuropathol , vol.109 , pp. 329-338
    • Tan, C.F.1    Piao, Y.S.2    Kakita, A.3
  • 212
    • 0031985080 scopus 로고    scopus 로고
    • N-terminal heterogeneity of parenchymal and cerebrovascular Abeta deposits
    • Tekirian TL, Saido TC, Markesbery WR et al (1998) N-terminal heterogeneity of parenchymal and cerebrovascular Abeta deposits. J Neuropathol Exp Neurol 57:76-94.
    • (1998) J Neuropathol Exp Neurol , vol.57 , pp. 76-94
    • Tekirian, T.L.1    Saido, T.C.2    Markesbery, W.R.3
  • 214
    • 0037172826 scopus 로고    scopus 로고
    • Phases of A beta-deposition in the human brain and its relevance for the development of AD
    • Thal DR, Rub U, Orantes M, Braak H (2002) Phases of A beta-deposition in the human brain and its relevance for the development of AD. Neurology 58:1791-1800.
    • (2002) Neurology , vol.58 , pp. 1791-1800
    • Thal, D.R.1    Rub, U.2    Orantes, M.3    Braak, H.4
  • 215
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of protea-some function
    • Tofaris GK, Razzaq A, Ghetti B, Lilley KS, Spillantini MG (2003) Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of protea-some function. J Biol Chem 278:44405-44411.
    • (2003) J Biol Chem , vol.278 , pp. 44405-44411
    • Tofaris, G.K.1    Razzaq, A.2    Ghetti, B.3    Lilley, K.S.4    Spillantini, M.G.5
  • 216
    • 10844254688 scopus 로고    scopus 로고
    • Argyrophilic grain disease: A late-onset dementia with distinctive features among tauopathies
    • Tolnay M, Clavaguera F (2004) Argyrophilic grain disease: a late-onset dementia with distinctive features among tauopathies. Neuropathology 24:269-283.
    • (2004) Neuropathology , vol.24 , pp. 269-283
    • Tolnay, M.1    Clavaguera, F.2
  • 217
    • 0034513218 scopus 로고    scopus 로고
    • "Fatal attractions" of proteins. A comprehensive hypothetical mechanism underlying Alzheimer's disease and other neurodegenerative disorders
    • Trojanowski JQ, Lee VM (2000) "Fatal attractions" of proteins. A comprehensive hypothetical mechanism underlying Alzheimer's disease and other neurodegenerative disorders. Ann N Y Acad Sci 924:62-67.
    • (2000) Ann N y Acad Sci , vol.924 , pp. 62-67
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 218
    • 0142200946 scopus 로고    scopus 로고
    • Overview of protein aggregation in single, double, and triple neurodegenerative brain amyloidoses
    • Trojanowski JQ, Mattson MP (2003) Overview of protein aggregation in single, double, and triple neurodegenerative brain amyloidoses. Neuromolecular Med 4:1-6.
    • (2003) Neuromolecular Med , vol.4 , pp. 1-6
    • Trojanowski, J.Q.1    Mattson, M.P.2
  • 219
    • 0035856450 scopus 로고    scopus 로고
    • Lewy bodies are not increased in progressive supranuclear palsy compared with normal controls
    • Tsuboi Y, Ahlskog JE, Apaydin H, Parisi JE, Dickson DW (2001) Lewy bodies are not increased in progressive supranuclear palsy compared with normal controls. Neurology 57:1675-1678.
    • (2001) Neurology , vol.57 , pp. 1675-1678
    • Tsuboi, Y.1    Ahlskog, J.E.2    Apaydin, H.3    Parisi, J.E.4    Dickson, D.W.5
  • 220
    • 33744974990 scopus 로고    scopus 로고
    • Lewy bodies in progressive supranuclear palsy represent an independent disease process
    • Uchikado H, DelleDonne A, Ahmed Z, Dickson DW (2006) Lewy bodies in progressive supranuclear palsy represent an independent disease process. J Neuropathol Exp Neurol 65:387-395.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 387-395
    • Uchikado, H.1    DelleDonne, A.2    Ahmed, Z.3    Dickson, D.W.4
  • 221
    • 33646197123 scopus 로고    scopus 로고
    • Coexistence of PSP and MSA: A case report and review of the literature
    • Uchikado H, DelleDonne A, Uitti R, Dickson DW (2006) Coexistence of PSP and MSA: a case report and review of the literature. Acta Neuropathol 111:186-192.
    • (2006) Acta Neuropathol , vol.111 , pp. 186-192
    • Uchikado, H.1    DelleDonne, A.2    Uitti, R.3    Dickson, D.W.4
  • 222
    • 33747821466 scopus 로고    scopus 로고
    • Alzheimer disease with amygdala Lewy bodies: A distinct form of alpha-synucleinopathy
    • Uchikado H, Lin WL, DeLucia MW, Dickson DW (2006) Alzheimer disease with amygdala Lewy bodies: a distinct form of alpha-synucleinopathy. J Neuropathol Exp Neurol 65:685-697.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 685-697
    • Uchikado, H.1    Lin, W.L.2    Delucia, M.W.3    Dickson, D.W.4
  • 223
    • 44649137415 scopus 로고    scopus 로고
    • Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies
    • Uryu K, Nakashima-Yasuda H, Forman MS et al (2008) Concomitant TAR-DNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies. J Neuropathol Exp Neurol 67:555-564.
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 555-564
    • Uryu, K.1    Nakashima-Yasuda, H.2    Forman, M.S.3
  • 224
    • 67650369989 scopus 로고    scopus 로고
    • Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases
    • Uversky VN, Oldfield CJ, Midic U et al (2009) Unfoldomics of human diseases: linking protein intrinsic disorder with diseases. BMC Genomics 10(Suppl 1):S7.
    • (2009) BMC Genomics , vol.10 , Issue.SUPPL. 1
    • Uversky, V.N.1    Oldfield, C.J.2    Midic, U.3
  • 225
    • 15544381031 scopus 로고    scopus 로고
    • Effects of nitration on the structure and aggregation of alpha-synuclein
    • Uversky VN, Yamin G, Munishkina LA et al (2005) Effects of nitration on the structure and aggregation of alpha-synuclein. Brain Res Mol Brain Res 134:84-102.
    • (2005) Brain Res Mol Brain Res , vol.134 , pp. 84-102
    • Uversky, V.N.1    Yamin, G.2    Munishkina, L.A.3
  • 226
    • 61349162349 scopus 로고    scopus 로고
    • Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6
    • Vance C, Rogelj B, Hortobagyi T et al (2009) Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6. Science 323:1208-1211.
    • (2009) Science , vol.323 , pp. 1208-1211
    • Vance, C.1    Rogelj, B.2    Hortobagyi, T.3
  • 227
    • 23744482703 scopus 로고    scopus 로고
    • Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates
    • Vega IE, Cui L, Propst JA, Hutton ML, Lee G, Yen SH (2005) Increase in tau tyrosine phosphorylation correlates with the formation of tau aggregates. Brain Res Mol Brain Res 138:135-144.
    • (2005) Brain Res Mol Brain Res , vol.138 , pp. 135-144
    • Vega, I.E.1    Cui, L.2    Propst, J.A.3    Hutton, M.L.4    Lee, G.5    Yen, S.H.6
  • 228
    • 68249111164 scopus 로고    scopus 로고
    • MRI and CSF biomarkers in normal, MCI, and AD subjects: Predicting future clinical change
    • Vemuri P, Wiste HJ, Weigand SD et al (2009) MRI and CSF biomarkers in normal, MCI, and AD subjects: predicting future clinical change. Neurology 73:294-301.
    • (2009) Neurology , vol.73 , pp. 294-301
    • Vemuri, P.1    Wiste, H.J.2    Weigand, S.D.3
  • 229
    • 0033973421 scopus 로고    scopus 로고
    • NACP/alpha-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains
    • Wakabayashi K, Hayashi S, Yoshimoto M, Kudo H, Takahashi H (2000) NACP/alpha-synuclein-positive filamentous inclusions in astrocytes and oligodendrocytes of Parkinson's disease brains. Acta Neuropathol 99:14-20.
    • (2000) Acta Neuropathol , vol.99 , pp. 14-20
    • Wakabayashi, K.1    Hayashi, S.2    Yoshimoto, M.3    Kudo, H.4    Takahashi, H.5
  • 230
    • 0033027032 scopus 로고    scopus 로고
    • Occurrence of argyrophilic grains in multiple system atrophy: Histopathological examination of 26 autopsy cases
    • Wakabayashi K, Kawachi I, Toyoshima Y, Takahashi H (1999) Occurrence of argyrophilic grains in multiple system atrophy: histopathological examination of 26 autopsy cases. No To Shinkei 51:433-437.
    • (1999) No to Shinkei , vol.51 , pp. 433-437
    • Wakabayashi, K.1    Kawachi, I.2    Toyoshima, Y.3    Takahashi, H.4
  • 231
    • 33746108503 scopus 로고    scopus 로고
    • Cellular pathology in multiple system atrophy
    • Wakabayashi K, Takahashi H (2006) Cellular pathology in multiple system atrophy. Neuropathology 26:338-345.
    • (2006) Neuropathology , vol.26 , pp. 338-345
    • Wakabayashi, K.1    Takahashi, H.2
  • 232
    • 34648819365 scopus 로고    scopus 로고
    • The Lewy body in Parkinson's disease: Molecules implicated in the formation and degradation of alpha-synuclein aggregates
    • Wakabayashi K, Tanji K, Mori F, Takahashi H (2007) The Lewy body in Parkinson's disease: molecules implicated in the formation and degradation of alpha-synuclein aggregates. Neuropathology 27:494-506.
    • (2007) Neuropathology , vol.27 , pp. 494-506
    • Wakabayashi, K.1    Tanji, K.2    Mori, F.3    Takahashi, H.4
  • 233
    • 0029815467 scopus 로고    scopus 로고
    • Glycosylation of microtubule-associated protein tau: An abnormal posttransla-tional modification in Alzheimer's disease
    • Wang JZ, Grundke-Iqbal I, Iqbal K (1996) Glycosylation of microtubule-associated protein tau: an abnormal posttransla-tional modification in Alzheimer's disease. Nat Med 2:871-875.
    • (1996) Nat Med , vol.2 , pp. 871-875
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 234
    • 18144406844 scopus 로고    scopus 로고
    • Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein
    • Wang Q, Woltjer RL, Cimino PJ, Pan C, Montine KS, Zhang J, Montine TJ (2005) Proteomic analysis of neurofibrillary tangles in Alzheimer disease identifies GAPDH as a detergent-insoluble paired helical filament tau binding protein. FASEB J 19:869-871.
    • (2005) FASEB J , vol.19 , pp. 869-871
    • Wang, Q.1    Woltjer, R.L.2    Cimino, P.J.3    Pan, C.4    Montine, K.S.5    Zhang, J.6    Montine, T.J.7
  • 235
    • 76649126396 scopus 로고    scopus 로고
    • Enrichment and site-mapping of O-Linked N-Acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation (ETD) mass spectrometry
    • in press
    • Wang Z, Udeshi ND, O'Malley M, Shabanowitz J, Hunt DF, Hart GW (2009) Enrichment and site-mapping of O-Linked N-Acetylglucosamine by a combination of chemical/enzymatic tagging, photochemical cleavage, and electron transfer dissociation (ETD) mass spectrometry. Mol Cell Proteomics (in press).
    • (2009) Mol Cell Proteomics
    • Wang, Z.1    Udeshi, N.D.2    O'Malley, M.3    Shabanowitz, J.4    Hunt, D.F.5    Hart, G.W.6
  • 236
    • 4544300178 scopus 로고    scopus 로고
    • Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo
    • Watanabe A, Hong WK, Dohmae N, Takio K, Morishima-Kawashima M, Ihara Y (2004) Molecular aging of tau: disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo. J Neurochem 90:1302-1311.
    • (2004) J Neurochem , vol.90 , pp. 1302-1311
    • Watanabe, A.1    Hong, W.K.2    Dohmae, N.3    Takio, K.4    Morishima-Kawashima, M.5    Ihara, Y.6
  • 237
    • 0033548661 scopus 로고    scopus 로고
    • Deamidation and isoas-partate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau
    • Watanabe A, Takio K, Ihara Y (1999) Deamidation and isoas-partate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J1 Biol Chem 274:7368-7378.
    • (1999) J1 Biol Chem , vol.274 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 239
    • 34250865548 scopus 로고    scopus 로고
    • Pathological tau burden and distribution distinguishes progressive supranuclear palsy-parkinsonism from Richardson's syndrome
    • Williams DR, Holton JL, Strand C, Pittman A, de Silva R, Lees AJ, Revesz T (2007) Pathological tau burden and distribution distinguishes progressive supranuclear palsy-parkinsonism from Richardson's syndrome. Brain 130:1566-1576.
    • (2007) Brain , vol.130 , pp. 1566-1576
    • Williams, D.R.1    Holton, J.L.2    Strand, C.3    Pittman, A.4    De Silva, R.5    Lees, A.J.6    Revesz, T.7
  • 240
    • 0042845853 scopus 로고    scopus 로고
    • Beta-amyloid peptides in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease
    • Wiltfang J, Esselmann H, Smirnov A et al (2003) Beta-amyloid peptides in cerebrospinal fluid of patients with Creutzfeldt-Jakob disease. Ann Neurol 54:263-267.
    • (2003) Ann Neurol , vol.54 , pp. 263-267
    • Wiltfang, J.1    Esselmann, H.2    Smirnov, A.3
  • 241
    • 0034722590 scopus 로고    scopus 로고
    • Lewy body variant of Alzheimer's disease: Alpha-synuclein in dystrophic neurites of A beta plaques
    • Wirths O, Weickert S, Majtenyi K et al (2000) Lewy body variant of Alzheimer's disease: alpha-synuclein in dystrophic neurites of A beta plaques. Neuroreport 11:3737-3741.
    • (2000) Neuroreport , vol.11 , pp. 3737-3741
    • Wirths, O.1    Weickert, S.2    Majtenyi, K.3
  • 242
    • 77950788517 scopus 로고    scopus 로고
    • FUS-immunoreactive intranuclear inclusions in neurodegenerative disease
    • doi:BPA337[pii]10.1111/j.1750-3639.2009.00337.x
    • Woulfe J, Gray DA, Mackenzie IR (2009) FUS-immunoreactive intranuclear inclusions in neurodegenerative disease. Brain Pathol. doi:BPA337[pii]10.1111/j. 1750-3639.2009.00337.x.
    • (2009) Brain Pathol
    • Woulfe, J.1    Gray, D.A.2    Mackenzie, I.R.3
  • 243
    • 44649100169 scopus 로고    scopus 로고
    • Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats
    • Wray S, Saxton M, Anderton BH, Hanger DP (2008) Direct analysis of tau from PSP brain identifies new phosphorylation sites and a major fragment of N-terminally cleaved tau containing four microtubule-binding repeats. J Neurochem 105:2343-2352.
    • (2008) J Neurochem , vol.105 , pp. 2343-2352
    • Wray, S.1    Saxton, M.2    Anderton, B.H.3    Hanger, D.P.4
  • 244
    • 0033936784 scopus 로고    scopus 로고
    • Alpha-synuclein inclusions in amygdala in the brains of patients with the parkinsonism-dementia complex of Guam
    • Yamazaki M, Arai Y, Baba M et al (2000) Alpha-synuclein inclusions in amygdala in the brains of patients with the parkinsonism-dementia complex of Guam. J Neuropathol Exp Neurol 59:585-591.
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 585-591
    • Yamazaki, M.1    Arai, Y.2    Baba, M.3
  • 246
    • 33845925066 scopus 로고    scopus 로고
    • Insoluble aggregates and protease-resistant conformers of prion protein in uninfected human brains
    • Yuan J, Xiao X, McGeehan J et al (2006) Insoluble aggregates and protease-resistant conformers of prion protein in uninfected human brains. J Biol Chem 281:34848-34858.
    • (2006) J Biol Chem , vol.281 , pp. 34848-34858
    • Yuan, J.1    Xiao, X.2    McGeehan, J.3
  • 247
    • 0033764710 scopus 로고    scopus 로고
    • Transglutaminase-induced cross-linking of tau proteins in progressive supranuclear palsy
    • Zemaitaitis MO, Lee JM, Troncoso JC, Muma NA (2000) Transglutaminase- induced cross-linking of tau proteins in progressive supranuclear palsy. J Neuropathol Exp Neurol 59:983-989.
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 983-989
    • Zemaitaitis, M.O.1    Lee, J.M.2    Troncoso, J.C.3    Muma, N.A.4
  • 248
  • 249
    • 39749137597 scopus 로고    scopus 로고
    • Prion: The chameleon protein
    • Zou WQ, Gambetti P (2007) Prion: the chameleon protein. Cell Mol Life Sci 64:3266-3270.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 3266-3270
    • Zou, W.Q.1    Gambetti, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.