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Volumn 8, Issue 3, 2011, Pages 246-251

Frontotemporal dementia caused by CHMP2B mutations

Author keywords

Autophagy; Brain imaging; CHMP2B; Endosome; Frontotemporal dementia; Lysosome; Neuropathology

Indexed keywords

CHMP2B PROTEIN; CHROMOSOME PROTEIN; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 79956277415     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/156720511795563764     Document Type: Article
Times cited : (78)

References (64)
  • 1
    • 0031672540 scopus 로고    scopus 로고
    • Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria
    • Neary D, Snowden JS, Gustafson L, Passant U, Stuss D, Black S, et al. Frontotemporal lobar degeneration: a consensus on clinical diagnostic criteria. Neurology 51: 1546-1554 (1998).
    • (1998) Neurology , vol.51 , pp. 1546-1554
    • Neary, D.1    Snowden, J.S.2    Gustafson, L.3    Passant, U.4    Stuss, D.5    Black, S.6
  • 2
    • 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, Miller B, Dickson D, Trojanowski JQ. Clinical and pathological diagnosis of frontotemporal dementia: report of the Work Group on Frontotemporal Dementia and Pick's Disease. Arch Neurol 58: 1803-1809 (2001).
    • (2001) Arch Neurol , vol.58 , pp. 1803-1809
    • McKhann, G.M.1    Albert, M.S.2    Grossman, M.3    Miller, B.4    Dickson, D.5    Trojanowski, J.Q.6
  • 3
    • 67650741437 scopus 로고    scopus 로고
    • Frontotemporal dementia and motor neurone disease: Overlapping clinic-pathological disorders
    • Lillo P, Hodges JR. Frontotemporal dementia and motor neurone disease: overlapping clinic-pathological disorders. J Clin Neurosci 16: 1131-1135 (2009).
    • (2009) J Clin Neurosci , vol.16 , pp. 1131-1135
    • Lillo, P.1    Hodges, J.R.2
  • 4
    • 34447096691 scopus 로고    scopus 로고
    • Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: Consensus of the Consortium for Frontotemporal Lobar Degeneration
    • Cairns NJ, Bigio EH, Mackenzie IR, Neumann M, Lee VM, Hatanpaa KJ, et al. Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration. Acta Neuropathol (Berl) 114: 5-22 (2007).
    • (2007) Acta Neuropathol (Berl) , vol.114 , pp. 5-22
    • Cairns, N.J.1    Bigio, E.H.2    Mackenzie, I.R.3    Neumann, M.4    Lee, V.M.5    Hatanpaa, K.J.6
  • 6
    • 0037933407 scopus 로고    scopus 로고
    • Corticobasal degeneration and its relationship to progressive supranuclear palsy and frontotemporal dementia
    • Boeve BF, Lang AE, Litvan I. Corticobasal degeneration and its relationship to progressive supranuclear palsy and frontotemporal dementia. Ann Neurol 54 Suppl 5: S15-S19 (2003).
    • (2003) Ann Neurol , vol.54 , Issue.SUPPL. 5
    • Boeve, B.F.1    Lang, A.E.2    Litvan, I.3
  • 7
    • 2642514673 scopus 로고    scopus 로고
    • Relationship between frontotemporal dementia and corticobasal degeneration/progressive supranuclear palsy
    • Kertesz A, Munoz D. Relationship between frontotemporal dementia and corticobasal degeneration/progressive supranuclear palsy. Dement Geriatr Cogn Disord 17: 282-286 (2004).
    • (2004) Dement Geriatr Cogn Disord , vol.17 , pp. 282-286
    • Kertesz, A.1    Munoz, D.2
  • 8
    • 57049105123 scopus 로고    scopus 로고
    • Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: Consensus recommendations
    • Mackenzie IR, Neumann M, Bigio EH, Cairns NJ, Alafuzoff I, Kril J, et al. Nomenclature for neuropathologic subtypes of frontotemporal lobar degeneration: consensus recommendations. Acta Neuropathol 117: 15-18 (2009).
    • (2009) Acta Neuropathol , vol.117 , pp. 15-18
    • Mackenzie, I.R.1    Neumann, M.2    Bigio, E.H.3    Cairns, N.J.4    Alafuzoff, I.5    Kril, J.6
  • 10
    • 77954459337 scopus 로고    scopus 로고
    • Frequency of ubiquitin and FUS-positive, TDP-43- negative frontotemporal lobar degeneration
    • Seelaar H, Klijnsma KY, de K, I, van der LA, Chiu WZ, Azmani A, et al. Frequency of ubiquitin and FUS-positive, TDP-43- negative frontotemporal lobar degeneration. J Neurol 25(5): 747-53 (2010).
    • (2010) J Neurol , vol.25 , Issue.5 , pp. 747-753
    • Seelaar, H.1    Klijnsma, K.Y.2    De, I.K.3    van der, L.A.4    Chiu, W.Z.5    Azmani, A.6
  • 11
    • 77649187519 scopus 로고    scopus 로고
    • Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: An update
    • Mackenzie IR, Neumann M, Bigio EH, Cairns NJ, Alafuzoff I, Kril J, et al. Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update. Acta Neuropathol 119: 1-4 (2010).
    • (2010) Acta Neuropathol , vol.119 , pp. 1-4
    • Mackenzie, I.R.1    Neumann, M.2    Bigio, E.H.3    Cairns, N.J.4    Alafuzoff, I.5    Kril, J.6
  • 12
    • 33746919083 scopus 로고    scopus 로고
    • Mutations in progranulin cause taunegative frontotemporal dementia linked to chromosome 17
    • Baker M, Mackenzie IR, Pickering-Brown SM, Gass J, Rademakers R, Lindholm C, et al. Mutations in progranulin cause taunegative frontotemporal dementia linked to chromosome 17. Nature 442: 916-919 (2006).
    • (2006) Nature , vol.442 , pp. 916-919
    • Baker, M.1    Mackenzie, I.R.2    Pickering-Brown, S.M.3    Gass, J.4    Rademakers, R.5    Lindholm, C.6
  • 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 ZJ, Engelborghs S, Wils H, Pirici D, et al. Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21. Nature 442: 920-924 (2006).
    • (2006) Nature , vol.442 , pp. 920-924
    • Cruts, M.1    Gijselinck, I.2    van der, Z.J.3    Engelborghs, S.4    Wils, H.5    Pirici, D.6
  • 14
    • 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, Baker M, Froelich S, Houlden H, et al. Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17. Nature 393: 702-705 (1998).
    • (1998) Nature , vol.393 , pp. 702-705
    • Hutton, M.1    Lendon, C.L.2    Rizzu, P.3    Baker, M.4    Froelich, S.5    Houlden, H.6
  • 16
    • 70350721803 scopus 로고    scopus 로고
    • Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease
    • Borroni B, Bonvicini C, Alberici A, Buratti E, Agosti C, Archetti S, et al. Mutation within TARDBP leads to frontotemporal dementia without motor neuron disease. Hum Mutat 30: E974-E983 (2009).
    • (2009) Hum Mutat , vol.30
    • Borroni, B.1    Bonvicini, C.2    Alberici, A.3    Buratti, E.4    Agosti, C.5    Archetti, S.6
  • 17
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosincontaining protein
    • Watts GD, Wymer J, Kovach MJ, Mehta SG, Mumm S, Darvish D, et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosincontaining protein. Nat Genet 36: 377-381 (2004).
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6
  • 19
    • 37849023471 scopus 로고    scopus 로고
    • CHMP2B C-truncating mutations in frontotemporal lobar degeneration are associated with an aberrant endosomal phenotype in vitro
    • van der Zee J, Urwin H, Engelborghs S, Bruyland M, Vandenberghe R, Dermaut B, et al. CHMP2B C-truncating mutations in frontotemporal lobar degeneration are associated with an aberrant endosomal phenotype in vitro. Hum Mol Genet 17: 313-322 (2008).
    • (2008) Hum Mol Genet , vol.17 , pp. 313-322
    • van der Zee, J.1    Urwin, H.2    Engelborghs, S.3    Bruyland, M.4    Vandenberghe, R.5    Dermaut, B.6
  • 21
    • 44949251639 scopus 로고    scopus 로고
    • Frontotemporal dementia linked to chromosome 3 (FTD-3)-- current concepts and the detection of a previously unknown branch of the Danish FTD-3 family
    • Lindquist SG, Braedgaard H, Svenstrup K, Isaacs AM, Nielsen JE. Frontotemporal dementia linked to chromosome 3 (FTD-3)- current concepts and the detection of a previously unknown branch of the Danish FTD-3 family. Eur J Neurol 15: 667-670 (2008).
    • (2008) Eur J Neurol , vol.15 , pp. 667-670
    • Lindquist, S.G.1    Braedgaard, H.2    Svenstrup, K.3    Isaacs, A.M.4    Nielsen, J.E.5
  • 22
    • 77953583994 scopus 로고    scopus 로고
    • Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations
    • Urwin H, Authier A, Nielsen JE, Metcalf D, Powell C, Froud K, et al. Disruption of endocytic trafficking in frontotemporal dementia with CHMP2B mutations. Hum Mol Genet 19: 2228-38 (2010).
    • (2010) Hum Mol Genet , vol.19 , pp. 2228-2238
    • Urwin, H.1    Authier, A.2    Nielsen, J.E.3    Metcalf, D.4    Powell, C.5    Froud, K.6
  • 28
    • 70449517337 scopus 로고    scopus 로고
    • Absence of FUSimmunoreactive pathology in frontotemporal dementia linked to chromosome 3 (FTD-3) caused by mutation in the CHMP2B gene
    • Holm IE, Isaacs AM, Mackenzie IR. Absence of FUSimmunoreactive pathology in frontotemporal dementia linked to chromosome 3 (FTD-3) caused by mutation in the CHMP2B gene. Acta Neuropathol 118: 719-720 (2009).
    • (2009) Acta Neuropathol , vol.118 , pp. 719-720
    • Holm, I.E.1    Isaacs, A.M.2    Mackenzie, I.R.3
  • 29
  • 30
    • 48249095748 scopus 로고    scopus 로고
    • Down syndrome fibroblast model of Alzheimer-related endosome pathology: Accelerated endocytosis promotes late endocytic defects
    • Cataldo AM, Mathews PM, Boiteau AB, Hassinger LC, Peterhoff CM, Jiang Y, et al. Down syndrome fibroblast model of Alzheimer-related endosome pathology: accelerated endocytosis promotes late endocytic defects. Am J Pathol 173: 370-384 (2008).
    • (2008) Am J Pathol , vol.173 , pp. 370-384
    • Cataldo, A.M.1    Mathews, P.M.2    Boiteau, A.B.3    Hassinger, L.C.4    Peterhoff, C.M.5    Jiang, Y.6
  • 31
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: Differential effects of APOE genotype and presenilin mutations
    • Cataldo AM, Peterhoff CM, Troncoso JC, Gomez-Isla T, Hyman BT, Nixon RA. Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am J Pathol 157: 277-286 (2000).
    • (2000) Am J Pathol , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 32
    • 0030836345 scopus 로고    scopus 로고
    • Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: Neuropathologic evidence for a mechanism of increased beta-amyloidogenesis
    • Cataldo AM, Barnett JL, Pieroni C, Nixon RA. Increased neuronal endocytosis and protease delivery to early endosomes in sporadic Alzheimer's disease: neuropathologic evidence for a mechanism of increased beta-amyloidogenesis. J Neurosci 17: 6142-6151 (1997).
    • (1997) J Neurosci , vol.17 , pp. 6142-6151
    • Cataldo, A.M.1    Barnett, J.L.2    Pieroni, C.3    Nixon, R.A.4
  • 34
    • 0031949083 scopus 로고    scopus 로고
    • Senile dementia with tangles (tangle predominant form of senile dementia)
    • Jellinger KA, Bancher C. Senile dementia with tangles (tangle predominant form of senile dementia). Brain Pathol 8: 367-376 (1998).
    • (1998) Brain Pathol , vol.8 , pp. 367-376
    • Jellinger, K.A.1    Bancher, C.2
  • 35
    • 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 23: 311-317 (2003).
    • (2003) Neuropathology , vol.23 , pp. 311-317
    • Yamada, M.1
  • 38
    • 0037371509 scopus 로고    scopus 로고
    • Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy
    • Verhoeven K, De Jonghe P, Coen K, Verpoorten N, Auer- Grumbach M, Kwon JM, et al. Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy. Am J Hum Genet 72: 722-727 (2003).
    • (2003) Am J Hum Genet , vol.72 , pp. 722-727
    • Verhoeven, K.1    de Jonghe, P.2    Coen, K.3    Verpoorten, N.4    Auer-Grumbach, M.5    Kwon, J.M.6
  • 39
    • 0036902646 scopus 로고    scopus 로고
    • Receptor downregulation and multivesicular-body sorting
    • Katzmann DJ, Odorizzi G, Emr SD. Receptor downregulation and multivesicular-body sorting. Nat Rev Mol Cell Biol 3: 893-905 (2002).
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 893-905
    • Katzmann, D.J.1    Odorizzi, G.2    Emr, S.D.3
  • 40
    • 60249084756 scopus 로고    scopus 로고
    • GISP increases neurotransmitter receptor stability by downregulating ESCRT-mediated lysosomal degradation
    • Kantamneni S, Holman D, Wilkinson KA, Nishimune A, Henley JM. GISP increases neurotransmitter receptor stability by downregulating ESCRT-mediated lysosomal degradation. Neurosci Lett 452: 106-110 (2009).
    • (2009) Neurosci Lett , vol.452 , pp. 106-110
    • Kantamneni, S.1    Holman, D.2    Wilkinson, K.A.3    Nishimune, A.4    Henley, J.M.5
  • 41
    • 51849092615 scopus 로고    scopus 로고
    • GISP binding to TSG101 increases GABA receptor stability by down-regulating ESCRT-mediated lysosomal degradation
    • Kantamneni S, Holman D, Wilkinson KA, Correa SA, Feligioni M, Ogden S, et al. GISP binding to TSG101 increases GABA receptor stability by down-regulating ESCRT-mediated lysosomal degradation. J Neurochem 107: 86-95 (2008).
    • (2008) J Neurochem , vol.107 , pp. 86-95
    • Kantamneni, S.1    Holman, D.2    Wilkinson, K.A.3    Correa, S.A.4    Feligioni, M.5    Ogden, S.6
  • 42
    • 67749145743 scopus 로고    scopus 로고
    • Genetic screen identifies serpin5 as a regulator of the toll pathway and CHMP2B toxicity associated with frontotemporal dementia
    • Ahmad ST, Sweeney ST, Lee JA, Sweeney NT, Gao FB. Genetic screen identifies serpin5 as a regulator of the toll pathway and CHMP2B toxicity associated with frontotemporal dementia. Proc Natl Acad Sci USA 106: 12168-12173 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 12168-12173
    • Ahmad, S.T.1    Sweeney, S.T.2    Lee, J.A.3    Sweeney, N.T.4    Gao, F.B.5
  • 44
    • 74949090299 scopus 로고    scopus 로고
    • An overview of the molecular mechanism of autophagy
    • Yang Z, Klionsky DJ. An overview of the molecular mechanism of autophagy. Curr Top Microbiol Immunol 335: 1-32 (2009).
    • (2009) Curr Top Microbiol Immunol , vol.335 , pp. 1-32
    • Yang, Z.1    Klionsky, D.J.2
  • 45
    • 0024299286 scopus 로고
    • Prelysosomal convergence of autophagic and endocytic pathways
    • Gordon PB, Seglen PO. Prelysosomal convergence of autophagic and endocytic pathways. Biochem Biophys Res Commun 151: 40-47 (1988).
    • (1988) Biochem Biophys Res Commun , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 46
    • 0025362656 scopus 로고
    • In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome
    • Tooze J, Hollinshead M, Ludwig T, Howell K, Hoflack B, Kern H. In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome. J Cell Biol 111: 329-345 (1990).
    • (1990) J Cell Biol , vol.111 , pp. 329-345
    • Tooze, J.1    Hollinshead, M.2    Ludwig, T.3    Howell, K.4    Hoflack, B.5    Kern, H.6
  • 47
    • 35948983328 scopus 로고    scopus 로고
    • Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease
    • Filimonenko M, Stuffers S, Raiborg C, Yamamoto A, Malerod L, Fisher EM, et al. Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease. J Cell Biol 179: 485-500 (2007).
    • (2007) J Cell Biol , vol.179 , pp. 485-500
    • Filimonenko, M.1    Stuffers, S.2    Raiborg, C.3    Yamamoto, A.4    Malerod, L.5    Fisher, E.M.6
  • 48
    • 34548492271 scopus 로고    scopus 로고
    • ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration
    • Lee JA, Beigneux A, Ahmad ST, Young SG, Gao FB. ESCRT-III dysfunction causes autophagosome accumulation and neurodegeneration. Curr Biol 17: 1561-1567 (2007).
    • (2007) Curr Biol , vol.17 , pp. 1561-1567
    • Lee, J.A.1    Beigneux, A.2    Ahmad, S.T.3    Young, S.G.4    Gao, F.B.5
  • 50
    • 14844303381 scopus 로고    scopus 로고
    • Extensive involvement of autophagy in Alzheimer disease: An immuno-electron microscopy study
    • Nixon RA, Wegiel J, Kumar A, Yu WH, Peterhoff C, Cataldo A, et al. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J Neuropathol Exp Neurol 64: 113-122 (2005).
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 113-122
    • Nixon, R.A.1    Wegiel, J.2    Kumar, A.3    Yu, W.H.4    Peterhoff, C.5    Cataldo, A.6
  • 51
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy--a novel Beta-amyloid peptidegenerating pathway activated in Alzheimer's disease
    • Yu WH, Cuervo AM, Kumar A, Peterhoff CM, Schmidt SD, Lee JH, et al. Macroautophagy--a novel Beta-amyloid peptidegenerating pathway activated in Alzheimer's disease. J Cell Biol 171: 87-98 (2005).
    • (2005) J Cell Biol , vol.171 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3    Peterhoff, C.M.4    Schmidt, S.D.5    Lee, J.H.6
  • 53
    • 0024328518 scopus 로고
    • Neuronal autophagy in experimental Creutzfeldt-Jakob's disease
    • Boellaard JW, Schlote W, Tateishi J. Neuronal autophagy in experimental Creutzfeldt-Jakob's disease. Acta Neuropathol (Berl) 78: 410-418 (1989).
    • (1989) Acta Neuropathol (Berl) , vol.78 , pp. 410-418
    • Boellaard, J.W.1    Schlote, W.2    Tateishi, J.3
  • 55
    • 4344656905 scopus 로고    scopus 로고
    • Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: A brain biopsy study
    • Sikorska B, Liberski PP, Giraud P, Kopp N, Brown P. Autophagy is a part of ultrastructural synaptic pathology in Creutzfeldt-Jakob disease: a brain biopsy study. Int J Biochem Cell Biol 36: 2563-2573 (2004).
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2563-2573
    • Sikorska, B.1    Liberski, P.P.2    Giraud, P.3    Kopp, N.4    Brown, P.5
  • 56
    • 38549160084 scopus 로고    scopus 로고
    • Neuronal autophagy and aggresomes constitute a consistent part of neurodegeneration in experimental scrapie
    • Sikorska B, Liberski PP, Brown P. Neuronal autophagy and aggresomes constitute a consistent part of neurodegeneration in experimental scrapie. Folia Neuropathol 45: 170-178 (2007).
    • (2007) Folia Neuropathol , vol.45 , pp. 170-178
    • Sikorska, B.1    Liberski, P.P.2    Brown, P.3
  • 57
    • 0026720748 scopus 로고
    • Comparative ultrastructural neuropathology of naturally occurring bovine spongiform encephalopathy and experimentally induced scrapie and Creutzfeldt-Jakob disease
    • Liberski PP, Yanagihara R, Wells GA, Gibbs CJ, Jr., Gajdusek DC. Comparative ultrastructural neuropathology of naturally occurring bovine spongiform encephalopathy and experimentally induced scrapie and Creutzfeldt-Jakob disease. J Comp Pathol 106: 361-381 (1992).
    • (1992) J Comp Pathol , vol.106 , pp. 361-381
    • Liberski, P.P.1    Yanagihara, R.2    Wells, G.A.3    Gibbs Jr., C.J.4    Gajdusek, D.C.5
  • 58
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441: 885-889 (2006).
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 59
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441: 880-884 (2006).
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 63
    • 33845464416 scopus 로고    scopus 로고
    • CHMP2B mutations are not a cause of dementia in Dutch patients with familial and sporadic frontotemporal dementia
    • Rizzu P, van Mil SE, Anar B, Rosso SM, Kaat LD, Heutink P, et al. CHMP2B mutations are not a cause of dementia in Dutch patients with familial and sporadic frontotemporal dementia. Am J Med Genet B Neuropsychiatr Genet 141B: 944-946 (2006).
    • (2006) Am J Med Genet B Neuropsychiatr Genet , vol.141 B , pp. 944-946
    • Rizzu, P.1    van Mil, S.E.2    Anar, B.3    Rosso, S.M.4    Kaat, L.D.5    Heutink, P.6
  • 64
    • 33646000253 scopus 로고    scopus 로고
    • CHMP2B mutations are not a common cause of frontotemporal lobar degeneration
    • Cannon A, Baker M, Boeve B, Josephs K, Knopman D, Petersen R, et al. CHMP2B mutations are not a common cause of frontotemporal lobar degeneration. Neurosci Lett 398: 83-84 (2006).
    • (2006) Neurosci Lett , vol.398 , pp. 83-84
    • Cannon, A.1    Baker, M.2    Boeve, B.3    Josephs, K.4    Knopman, D.5    Petersen, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.