메뉴 건너뛰기




Volumn 66, Issue 10, 2007, Pages 884-891

A reassessment of the neuropathology of frontotemporal dementia linked to chromosome 3

Author keywords

Chromosome 3; Dementia lacking distinctive histopathology; Frontotemporal lobar degeneration; Ubiquitin

Indexed keywords

ALPHA SYNUCLEIN; PRION PROTEIN; PROTEIN P43; PROTEIN P62; TAU PROTEIN;

EID: 34948838317     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/nen.0b013e3181567f02     Document Type: Article
Times cited : (127)

References (65)
  • 2
    • 0037062609 scopus 로고    scopus 로고
    • The prevalence of frontotemporal dementia
    • Ratnavalli E, Brayne C, Dawson K, et al. The prevalence of frontotemporal dementia. Neurology 2002;58:1615-21
    • (2002) Neurology , vol.58 , pp. 1615-1621
    • Ratnavalli, E.1    Brayne, C.2    Dawson, K.3
  • 3
    • 0028223015 scopus 로고    scopus 로고
    • The Lund and Manchester Groups. Clinical and neuropathological criteria for frontotemporal dementia. J Neurol Neurosurg Psychiatry 1994;57:416-18
    • The Lund and Manchester Groups. Clinical and neuropathological criteria for frontotemporal dementia. J Neurol Neurosurg Psychiatry 1994;57:416-18
  • 4
    • 0034764622 scopus 로고    scopus 로고
    • Clinical and pathological diagnosis of frontotemporal dementia: Report of the Work Group on Frontotemporal Dementia and Pick's Disease
    • McKhann GM, Albert MS, Grossman M, et al. Clinical and pathological diagnosis of frontotemporal dementia: Report of the Work Group on Frontotemporal Dementia and Pick's Disease. Arch Neurol 2001;58:1803-09
    • (2001) Arch Neurol , vol.58 , pp. 1803-1809
    • McKhann, G.M.1    Albert, M.S.2    Grossman, M.3
  • 5
    • 0031672540 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria
    • Neary D, Snowden JS, Gustafson L, et al. Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria. Neurology 1998;51:1546-54
    • (1998) Neurology , vol.51 , pp. 1546-1554
    • Neary, D.1    Snowden, J.S.2    Gustafson, L.3
  • 6
    • 33749034719 scopus 로고    scopus 로고
    • The relationship between amyotrophic lateral sclerosis and frontotemporal dementia
    • Ringholz GM, Greene SR. The relationship between amyotrophic lateral sclerosis and frontotemporal dementia. Curr Neurol Neurosci Rep 2006;6:387-92
    • (2006) Curr Neurol Neurosci Rep , vol.6 , pp. 387-392
    • Ringholz, G.M.1    Greene, S.R.2
  • 7
    • 0041320789 scopus 로고    scopus 로고
    • Frontotemporal dementia in The Netherlands: Patient characteristics and prevalence estimates from a population-based study
    • Rosso SM, Donker KL, Baks T, et al. Frontotemporal dementia in The Netherlands: Patient characteristics and prevalence estimates from a population-based study. Brain 2003;126:2016-22
    • (2003) Brain , vol.126 , pp. 2016-2022
    • Rosso, S.M.1    Donker, K.L.2    Baks, T.3
  • 8
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton M, Lendon CL, Rizzu P, et al. Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 1998;393:702-5
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3
  • 9
    • 14444284106 scopus 로고    scopus 로고
    • Tau is a candidate gene for chromosome 17 frontotemporal dementia
    • Poorkaj P, Bird TD, Wijsman E, et al. Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann Neurol 1998;43:815-25
    • (1998) Ann Neurol , vol.43 , pp. 815-825
    • Poorkaj, P.1    Bird, T.D.2    Wijsman, E.3
  • 10
    • 0032568534 scopus 로고    scopus 로고
    • α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, et al. α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci USA 1998;95:6469-73
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3
  • 11
    • 5044235577 scopus 로고    scopus 로고
    • The role of tau (MAPT) in frontotemporal dementia and related tauopathies
    • Rademakers R, Cruts M, Van Broeckhoven C. The role of tau (MAPT) in frontotemporal dementia and related tauopathies. Hum Mutat 2004;24:277-95
    • (2004) Hum Mutat , vol.24 , pp. 277-295
    • Rademakers, R.1    Cruts, M.2    Van Broeckhoven, C.3
  • 12
    • 33746919083 scopus 로고    scopus 로고
    • Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
    • Baker M, Mackenzie IR, Pickering-Brown SM, et al. Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature 2006;442:916-19
    • (2006) Nature , vol.442 , pp. 916-919
    • Baker, M.1    Mackenzie, I.R.2    Pickering-Brown, S.M.3
  • 13
    • 33746910649 scopus 로고    scopus 로고
    • Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21
    • Cruts M, Gijselinck I, van der Zee J, et al. Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature 2006;442:920-24
    • (2006) Nature , vol.442 , pp. 920-924
    • Cruts, M.1    Gijselinck, I.2    van der Zee, J.3
  • 14
    • 33749568019 scopus 로고    scopus 로고
    • Mutations in progranulin are a major cause of ubiquitin-positive frontotemporal lobar degeneration
    • Gass J, Cannon A, Mackenzie IR, et al. Mutations in progranulin are a major cause of ubiquitin-positive frontotemporal lobar degeneration. Hum Mol Genet 2006;15:2988-3001
    • (2006) Hum Mol Genet , vol.15 , pp. 2988-3001
    • Gass, J.1    Cannon, A.2    Mackenzie, I.R.3
  • 15
    • 33645062075 scopus 로고    scopus 로고
    • A locus on chromosome 9p confers susceptibility to ALS and frontotemporal dementia
    • Morita M, Al Chalabi A, Andersen PM, et al. A locus on chromosome 9p confers susceptibility to ALS and frontotemporal dementia. Neurology 2006;66:839-44
    • (2006) Neurology , vol.66 , pp. 839-844
    • Morita, M.1    Al Chalabi, A.2    Andersen, P.M.3
  • 16
    • 33645069660 scopus 로고    scopus 로고
    • Familial amyotrophic lateral sclerosis with frontotemporal dementia is linked to a locus on chromosome 9p13.2-21.3
    • Vance C, Al Chalabi A, Ruddy D, et al. Familial amyotrophic lateral sclerosis with frontotemporal dementia is linked to a locus on chromosome 9p13.2-21.3. Brain 2006;129:868-76
    • (2006) Brain , vol.129 , pp. 868-876
    • Vance, C.1    Al Chalabi, A.2    Ruddy, D.3
  • 17
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 2004;36:377-81
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3
  • 18
    • 23044471011 scopus 로고    scopus 로고
    • Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
    • Skibinski G, Parkinson NJ, Brown JM, et al. Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia. Nat Genet 2005;37:806-8
    • (2005) Nat Genet , vol.37 , pp. 806-808
    • Skibinski, G.1    Parkinson, N.J.2    Brown, J.M.3
  • 19
    • 0035209337 scopus 로고    scopus 로고
    • Update on the neuropathological diagnosis of frontotemporal dementias
    • Trojanowski JQ, Dickson D. Update on the neuropathological diagnosis of frontotemporal dementias. J Neuropathol Exp Neurol 2001;60:1123-26
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1123-1126
    • Trojanowski, J.Q.1    Dickson, D.2
  • 20
    • 27944491570 scopus 로고    scopus 로고
    • Histopathological changes underlying frontotemporal lobar degeneration with clinicopathological correlation
    • Shi J, Shaw CL, Du PD, et al. Histopathological changes underlying frontotemporal lobar degeneration with clinicopathological correlation. Acta Neuropathol (Berl) 2005;110:501-12
    • (2005) Acta Neuropathol (Berl) , vol.110 , pp. 501-512
    • Shi, J.1    Shaw, C.L.2    Du, P.D.3
  • 21
    • 0842265475 scopus 로고    scopus 로고
    • The neuropathology of frontotemporal lobar degeneration with respect to the cytological and biochemical characteristics of tau protein
    • Taniguchi S, McDonagh AM, Pickering-Brown SM, et al. The neuropathology of frontotemporal lobar degeneration with respect to the cytological and biochemical characteristics of tau protein. Neuropathol Appl Neurobiol 2004;30:1-18
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 1-18
    • Taniguchi, S.1    McDonagh, A.M.2    Pickering-Brown, S.M.3
  • 22
    • 0025341975 scopus 로고
    • Dementia lacking distinctive histologic features: A common non-Alzheimer degenerative dementia
    • Knopman DS, Mastri AR, Frey WH, et al. Dementia lacking distinctive histologic features: A common non-Alzheimer degenerative dementia. Neurology 1990;40:251-56
    • (1990) Neurology , vol.40 , pp. 251-256
    • Knopman, D.S.1    Mastri, A.R.2    Frey, W.H.3
  • 23
    • 4344642855 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration and ubiquitin immunohistochemistry
    • Josephs KA, Holton JL, Rossor MN, et al. Frontotemporal lobar degeneration and ubiquitin immunohistochemistry. Neuropathol Appl Neurobiol 2004;30:369-73
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 369-373
    • Josephs, K.A.1    Holton, J.L.2    Rossor, M.N.3
  • 24
    • 7744220605 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration with motor neuron disease-type inclusions predominates in 76 cases of frontotemporal degeneration
    • Lipton AM, White CL III, Bigio EH. Frontotemporal lobar degeneration with motor neuron disease-type inclusions predominates in 76 cases of frontotemporal degeneration. Acta Neuropathol (Berl) 2004;108:379-85
    • (2004) Acta Neuropathol (Berl) , vol.108 , pp. 379-385
    • Lipton, A.M.1    White III, C.L.2    Bigio, E.H.3
  • 25
    • 33749685354 scopus 로고    scopus 로고
    • Dementia lacking distinctive histology (DLDH) revisited
    • Mackenzie IR, Shi J, Shaw CL, et al. Dementia lacking distinctive histology (DLDH) revisited. Acta Neuropathol (Berl) 2006;112:551-59
    • (2006) Acta Neuropathol (Berl) , vol.112 , pp. 551-559
    • Mackenzie, I.R.1    Shi, J.2    Shaw, C.L.3
  • 26
    • 0026756463 scopus 로고
    • Ubiquitin-positive intraneuronal inclusions in the extramotor cortices of presenile dementia patients with motor neuron disease
    • Okamoto K, Murakami N, Kusaka H, et al. Ubiquitin-positive intraneuronal inclusions in the extramotor cortices of presenile dementia patients with motor neuron disease. J Neurol 1992;239:426-30
    • (1992) J Neurol , vol.239 , pp. 426-430
    • Okamoto, K.1    Murakami, N.2    Kusaka, H.3
  • 27
    • 0026691337 scopus 로고
    • Hippocampal and neocortical ubiquitin-immunoreactive inclusions in amyotrophic lateral sclerosis with dementia
    • Wightman G, Anderson VE, Martin J, et al. Hippocampal and neocortical ubiquitin-immunoreactive inclusions in amyotrophic lateral sclerosis with dementia. Neurosci Lett 1992;139:269-74
    • (1992) Neurosci Lett , vol.139 , pp. 269-274
    • Wightman, G.1    Anderson, V.E.2    Martin, J.3
  • 28
  • 29
    • 4444255628 scopus 로고    scopus 로고
    • α-Internexin aggregates are abundant in neuronal intermediate filament inclusion disease (NIFID) but rare in other neurodegenerative diseases
    • Cairns NJ, Uryu K, Bigio EH, et al. α-Internexin aggregates are abundant in neuronal intermediate filament inclusion disease (NIFID) but rare in other neurodegenerative diseases. Acta Neuropathol (Berl) 2004;108:213-23
    • (2004) Acta Neuropathol (Berl) , vol.108 , pp. 213-223
    • Cairns, N.J.1    Uryu, K.2    Bigio, E.H.3
  • 30
    • 0242336433 scopus 로고    scopus 로고
    • Neurofilament inclusion body disease: A new proteinopathy?
    • Josephs KA, Holton JL, Rossor MN, et al. Neurofilament inclusion body disease: A new proteinopathy? Brain 2003;126:2291-2303
    • (2003) Brain , vol.126 , pp. 2291-2303
    • Josephs, K.A.1    Holton, J.L.2    Rossor, M.N.3
  • 31
    • 33749668518 scopus 로고    scopus 로고
    • Heterogeneity of ubiquitin pathology in frontotemporal lobar degeneration: Classification and relation to clinical phenotype
    • Mackenzie IR, Baborie A, Pickering-Brown S, et al. Heterogeneity of ubiquitin pathology in frontotemporal lobar degeneration: Classification and relation to clinical phenotype. Acta Neuropathol (Berl) 2006;112:539-49
    • (2006) Acta Neuropathol (Berl) , vol.112 , pp. 539-549
    • Mackenzie, I.R.1    Baborie, A.2    Pickering-Brown, S.3
  • 32
    • 33846076379 scopus 로고    scopus 로고
    • Pathological heterogeneity of frontotemporal lobar degeneration with ubiquitin-positive inclusions delineated by ubiquitin immunohistochemistry and novel monoclonal antibodies
    • Sampathu DM, Neumann M, Kwong LK, et al. Pathological heterogeneity of frontotemporal lobar degeneration with ubiquitin-positive inclusions delineated by ubiquitin immunohistochemistry and novel monoclonal antibodies. Am J Pathol 2006;169:1343-52
    • (2006) Am J Pathol , vol.169 , pp. 1343-1352
    • Sampathu, D.M.1    Neumann, M.2    Kwong, L.K.3
  • 33
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006;314:130-33
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 34
    • 0035794665 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
    • Buratti E, Dork T, Zuccato E, et al. Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. EMBO J 2001;20:1774-84
    • (2001) EMBO J , vol.20 , pp. 1774-1784
    • Buratti, E.1    Dork, T.2    Zuccato, E.3
  • 35
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • Mercado PA, Ayala YM, Romano M, et al. Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res 2005;33:6000-10
    • (2005) Nucleic Acids Res , vol.33 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3
  • 36
    • 2442676753 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance
    • Buratti E, Brindisi A, Pagani F, et al. Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance. Am J Hum Genet 2004;74:1322-25
    • (2004) Am J Hum Genet , vol.74 , pp. 1322-1325
    • Buratti, E.1    Brindisi, A.2    Pagani, F.3
  • 37
    • 0037108967 scopus 로고    scopus 로고
    • Higher order arrangement of the eukaryotic nuclear bodies
    • Wang IF, Reddy NM, Shen CK. Higher order arrangement of the eukaryotic nuclear bodies. Proc Natl Acad Sci USA 2002;99:13583-88
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13583-13588
    • Wang, I.F.1    Reddy, N.M.2    Shen, C.K.3
  • 38
    • 0037180476 scopus 로고    scopus 로고
    • Chromosome 3 linked frontotemporal dementia (FTD-3)
    • Gydesen S, Brown JM, Brun A, et al. Chromosome 3 linked frontotemporal dementia (FTD-3). Neurology 2002;59:1585-94
    • (2002) Neurology , vol.59 , pp. 1585-1594
    • Gydesen, S.1    Brown, J.M.2    Brun, A.3
  • 39
    • 1842638333 scopus 로고    scopus 로고
    • Extrapyramidal features in patients with motor neuron disease and dementia; a clinicopathological correlative study
    • Mackenzie IR, Feldman H. Extrapyramidal features in patients with motor neuron disease and dementia; a clinicopathological correlative study. Acta Neuropathol (Berl) 2004;107:336-40
    • (2004) Acta Neuropathol (Berl) , vol.107 , pp. 336-340
    • Mackenzie, I.R.1    Feldman, H.2
  • 40
    • 0025863618 scopus 로고
    • Neuropathological staging of Alzheimer-related changes
    • Braak H, Braak E. Neuropathological staging of Alzheimer-related changes. Acta Neuropathol (Berl) 1991;82:239-59
    • (1991) Acta Neuropathol (Berl) , vol.82 , pp. 239-259
    • Braak, H.1    Braak, E.2
  • 41
    • 0025908356 scopus 로고
    • The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease
    • Mirra SS, Heyman A, McKeel D, et al. The Consortium to Establish a Registry for Alzheimer's Disease (CERAD). Part II. Standardization of the neuropathologic assessment of Alzheimer's disease. Neurology 1991;41:479-86
    • (1991) Neurology , vol.41 , pp. 479-486
    • Mirra, S.S.1    Heyman, A.2    McKeel, D.3
  • 42
    • 33746693220 scopus 로고    scopus 로고
    • Novel ubiquitin neuropathology in frontotemporal dementia with valosin-containing protein gene mutations
    • Forman MS, Mackenzie IR, Cairns NJ, et al. Novel ubiquitin neuropathology in frontotemporal dementia with valosin-containing protein gene mutations. J Neuropathol Exp Neurol 2006;65:571-81
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 571-581
    • Forman, M.S.1    Mackenzie, I.R.2    Cairns, N.J.3
  • 43
    • 33645642025 scopus 로고    scopus 로고
    • Ubiquitin immunohistochemistry of frontotemporal lobar degeneration differentiates cases with and without motor neuron disease
    • Katsuse O, Dickson DW. Ubiquitin immunohistochemistry of frontotemporal lobar degeneration differentiates cases with and without motor neuron disease. Alzheimer Dis Assoc Disord 2005;19(Suppl 1):S37-43
    • (2005) Alzheimer Dis Assoc Disord , vol.19 , Issue.SUPPL. 1
    • Katsuse, O.1    Dickson, D.W.2
  • 44
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E, Salminen A, Alafuzoff I. Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuroreport 2001;12:2085-90
    • (2001) Neuroreport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 45
    • 33749003187 scopus 로고    scopus 로고
    • Heterogeneous inclusions in neurofilament inclusion disease
    • Uchikado H, Li A, Lin WL, et al. Heterogeneous inclusions in neurofilament inclusion disease. Neuropathology 2006;26:417-21
    • (2006) Neuropathology , vol.26 , pp. 417-421
    • Uchikado, H.1    Li, A.2    Lin, W.L.3
  • 46
    • 33947248608 scopus 로고    scopus 로고
    • The ubiquitin-binding protein p62 identifies argyrophilic grain pathology with greater sensitivity than conventional silver stains
    • Scott IS, Lowe JS. The ubiquitin-binding protein p62 identifies argyrophilic grain pathology with greater sensitivity than conventional silver stains. Acta Neuropathol 2007;113:417-20
    • (2007) Acta Neuropathol , vol.113 , pp. 417-420
    • Scott, I.S.1    Lowe, J.S.2
  • 47
    • 0025278909 scopus 로고
    • Ubiquitin immunoreactive structures in normal human brains: Distribution and developmental aspects
    • Dickson DW, Wertkin A, Kress Y, et al. Ubiquitin immunoreactive structures in normal human brains: Distribution and developmental aspects. Lab Invest 1990;63:87-99
    • (1990) Lab Invest , vol.63 , pp. 87-99
    • Dickson, D.W.1    Wertkin, A.2    Kress, Y.3
  • 48
    • 0346847507 scopus 로고    scopus 로고
    • Senile dementia of the neurofibrillary tangle type (tangle-only dementia): Neuropathological criteria and clinical guidelines for diagnosis
    • Yamada M. Senile dementia of the neurofibrillary tangle type (tangle-only dementia): Neuropathological criteria and clinical guidelines for diagnosis. Neuropathology 2003;23:311-17
    • (2003) Neuropathology , vol.23 , pp. 311-317
    • Yamada, M.1
  • 49
    • 0031949083 scopus 로고    scopus 로고
    • Senile dementia with tangles (Tangle predominant form of senile dementia)
    • Jellinger K, Bancher C. Senile dementia with tangles (Tangle predominant form of senile dementia). Brain Pathol 1998;8:367-76
    • (1998) Brain Pathol , vol.8 , pp. 367-376
    • Jellinger, K.1    Bancher, C.2
  • 50
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst M, Katzmann DJ, Estepa-Sabal EJ, et al. Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting. Dev Cell 2002;3:271-82
    • (2002) Dev Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3
  • 51
  • 52
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross CA, Poirier MA. Opinion: What is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol 2005;6:891-98
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 53
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006;441:885-89
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 54
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006;441:880-84
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3
  • 55
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught KS, Perl DP, Brownell AL, et al. Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 2004;56:149-62
    • (2004) Ann Neurol , vol.56 , pp. 149-162
    • McNaught, K.S.1    Perl, D.P.2    Brownell, A.L.3
  • 56
    • 33646461282 scopus 로고    scopus 로고
    • β-Amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system
    • Almeida CG, Takahashi RH, Gouras GK. β-Amyloid accumulation impairs multivesicular body sorting by inhibiting the ubiquitin-proteasome system. J Neurosci 2006;26:4277-88
    • (2006) J Neurosci , vol.26 , pp. 4277-4288
    • Almeida, C.G.1    Takahashi, R.H.2    Gouras, G.K.3
  • 57
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • Longva KE, Blystad FD, Stang E, et al. Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J Cell Biol 2002;156:843-54
    • (2002) J Cell Biol , vol.156 , pp. 843-854
    • Longva, K.E.1    Blystad, F.D.2    Stang, E.3
  • 58
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann DJ, Babst M, Emr SD. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 2001;106:145-55
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 59
    • 0032560487 scopus 로고    scopus 로고
    • Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
    • Spillantini MG, Murrell JR, Goedert M, et al. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc Natl Acad Sci USA 1998;95:7737-41
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7737-7741
    • Spillantini, M.G.1    Murrell, J.R.2    Goedert, M.3
  • 60
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge J. Prion diseases of humans and animals: Their causes and molecular basis. Annu Rev Neurosci 2001;24:519-50
    • (2001) Annu Rev Neurosci , vol.24 , pp. 519-550
    • Collinge, J.1
  • 61
    • 33846815066 scopus 로고    scopus 로고
    • TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations
    • Neumann M, Mackenzie IR, Cairns NJ, et al. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J Neuropathol Exp Neurol 2007;66:152-57
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 152-157
    • Neumann, M.1    Mackenzie, I.R.2    Cairns, N.J.3
  • 62
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005;171:603-14
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3
  • 63
    • 0037986268 scopus 로고    scopus 로고
    • Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling
    • Geetha T, Wooten MW. Association of the atypical protein kinase C-interacting protein p62/ZIP with nerve growth factor receptor TrkA regulates receptor trafficking and Erk5 signaling. J Biol Chem 2003;278:4730-39
    • (2003) J Biol Chem , vol.278 , pp. 4730-4739
    • Geetha, T.1    Wooten, M.W.2
  • 64
    • 0029616212 scopus 로고
    • Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the Ick unique N-terminal region
    • Park I, Chung J, Walsh CT, et al. Phosphotyrosine-independent binding of a 62-kDa protein to the src homology 2 (SH2) domain of p56lck and its regulation by phosphorylation of Ser-59 in the Ick unique N-terminal region. Proc Natl Acad Sci USA 1995;92:12338-42
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12338-12342
    • Park, I.1    Chung, J.2    Walsh, C.T.3
  • 65
    • 0033153320 scopus 로고    scopus 로고
    • The interaction of p62 with RIP links the atypical PKCs to NF-JB activation
    • Sanz L, Sanchez P, Lallena MJ, et al. The interaction of p62 with RIP links the atypical PKCs to NF-JB activation. EMBO J 1999;18:3044-53
    • (1999) EMBO J , vol.18 , pp. 3044-3053
    • Sanz, L.1    Sanchez, P.2    Lallena, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.