메뉴 건너뛰기




Volumn 11, Issue 6, 2015, Pages 360-366

FTD and ALS-translating mouse studies into clinical trials

Author keywords

[No Author keywords available]

Indexed keywords

TAU PROTEIN;

EID: 84930572922     PISSN: 17594758     EISSN: 17594766     Source Type: Journal    
DOI: 10.1038/nrneurol.2015.65     Document Type: Article
Times cited : (63)

References (122)
  • 1
    • 4444248435 scopus 로고    scopus 로고
    • Clinicopathological correlates in frontotemporal dementia
    • Hodges, J. R. et al. Clinicopathological correlates in frontotemporal dementia. Ann. Neurol. 56, 399-406 (2004).
    • (2004) Ann. Neurol , vol.56 , pp. 399-406
    • Hodges, J.R.1
  • 2
    • 80755128213 scopus 로고    scopus 로고
    • Clinical diagnosis and management of amyotrophic lateral sclerosis
    • Hardiman, O., van den Berg, L. H. & Kiernan, M. C. Clinical diagnosis and management of amyotrophic lateral sclerosis. Nat. Rev. Neurol. 7, 639-649 (2011).
    • (2011) Nat. Rev. Neurol , vol.7 , pp. 639-649
    • Hardiman, O.1    Vanden Berg, L.H.2    Kiernan, M.C.3
  • 3
    • 84876466100 scopus 로고    scopus 로고
    • An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: A phase 1, randomised, first-in-man study
    • Miller, T. M. et al. An antisense oligonucleotide against SOD1 delivered intrathecally for patients with SOD1 familial amyotrophic lateral sclerosis: a phase 1, randomised, first-in-man study. Lancet Neurol. 12, 435-442 (2013).
    • (2013) Lancet Neurol , vol.12 , pp. 435-442
    • Miller, T.M.1
  • 4
    • 84870572714 scopus 로고    scopus 로고
    • Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models
    • Armakola, M. et al. Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models. Nat. Genet. 44, 1302-1309 (2012).
    • (2012) Nat. Genet , vol.44 , pp. 1302-1309
    • Armakola, M.1
  • 5
    • 84860859794 scopus 로고    scopus 로고
    • Progranulin: An emerging target for FTLD therapies
    • Gass, J., Prudencio, M., Stetler, C. & Petrucelli, L. Progranulin: an emerging target for FTLD therapies. Brain Res. 1462, 118-128 (2012).
    • (2012) Brain Res , vol.1462 , pp. 118-128
    • Gass, J.1    Prudencio, M.2    Stetler, C.3    Petrucelli, L.4
  • 6
    • 84908481936 scopus 로고    scopus 로고
    • The phenotypic variability of amyotrophic lateral sclerosis
    • Swinnen, B. & Robberecht, W. The phenotypic variability of amyotrophic lateral sclerosis. Nat. Rev. Neurol. 10, 661-670 (2014).
    • (2014) Nat. Rev. Neurol , vol.10 , pp. 661-670
    • Swinnen, B.1    Robberecht, W.2
  • 7
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis
    • Ling, S. C., Polymenidou, M. & Cleveland, D. W. Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis. Neuron 79, 416-438 (2013).
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 8
    • 84865862939 scopus 로고    scopus 로고
    • The genetics and neuropathology of frontotemporal lobar degeneration
    • Sieben, A. et al. The genetics and neuropathology of frontotemporal lobar degeneration. Acta Neuropathol. 124, 353-372 (2012).
    • (2012) Acta Neuropathol , vol.124 , pp. 353-372
    • Sieben, A.1
  • 9
    • 84902509590 scopus 로고    scopus 로고
    • Frontotemporal dementia and its subtypes: A genome-wide association study
    • Ferrari, R. et al. Frontotemporal dementia and its subtypes: a genome-wide association study. Lancet Neurol. 13, 686-699 (2014).
    • (2014) Lancet Neurol , vol.13 , pp. 686-699
    • Ferrari, R.1
  • 10
    • 79451472241 scopus 로고    scopus 로고
    • Distinct pathological subtypes of FTLD-FUS
    • Mackenzie, I. R. et al. Distinct pathological subtypes of FTLD-FUS. Acta Neuropathol. 121, 207-218 (2011).
    • (2011) Acta Neuropathol , vol.121 , pp. 207-218
    • MacKenzie, I.R.1
  • 11
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie, I. R., Rademakers, R. & Neumann, M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol. 9, 995-1007 (2010).
    • (2010) Lancet Neurol , vol.9 , pp. 995-1007
    • MacKenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 12
    • 84885484879 scopus 로고    scopus 로고
    • Globular glial tauopathies (GGT): Consensus recommendations
    • Ahmed, Z. et al. Globular glial tauopathies (GGT): consensus recommendations. Acta Neuropathol. 126, 537-544 (2013).
    • (2013) Acta Neuropathol , vol.126 , pp. 537-544
    • Ahmed, Z.1
  • 13
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D. R. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62 (1993).
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1
  • 14
    • 0032543684 scopus 로고    scopus 로고
    • Association of missense and 5'-splice-site mutations in tau with the inherited dementia FTDP-17
    • Hutton, M. 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
  • 15
    • 33746919083 scopus 로고    scopus 로고
    • Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17
    • Baker, M. et al. Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17. Nature 442, 916-919 (2006).
    • (2006) Nature , vol.442 , pp. 916-919
    • Baker, M.1
  • 16
    • 33746910649 scopus 로고    scopus 로고
    • Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21
    • Cruts, M. 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
  • 17
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez, M. et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron 72, 245-256 (2011).
    • (2011) Neuron , vol.72 , pp. 245-256
    • Dejesus-Hernandez, M.1
  • 18
    • 80054837386 scopus 로고    scopus 로고
    • A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton, A. E. et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron 72, 257-268 (2011).
    • (2011) Neuron , vol.72 , pp. 257-268
    • Renton, A.E.1
  • 19
    • 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, G. D. et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat. Genet. 36, 377-381 (2004).
    • (2004) Nat. Genet , vol.36 , pp. 377-381
    • Watts, G.D.1
  • 20
    • 65649112431 scopus 로고    scopus 로고
    • TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration
    • Benajiba, L. et al. TARDBP mutations in motoneuron disease with frontotemporal lobar degeneration. Ann. Neurol. 65, 470-473 (2009).
    • (2009) Ann. Neurol , vol.65 , pp. 470-473
    • Benajiba, L.1
  • 21
    • 77649136250 scopus 로고    scopus 로고
    • Common variants at 7p21 are associated with frontotemporal lobar degeneration with TDP-43 inclusions
    • Van Deerlin, V. M. et al. Common variants at 7p21 are associated with frontotemporal lobar degeneration with TDP-43 inclusions. Nat. Genet. 42, 234-239 (2010).
    • (2010) Nat. Genet , vol.42 , pp. 234-239
    • Van Deerlin, V.M.1
  • 22
    • 23044471011 scopus 로고    scopus 로고
    • Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia
    • Skibinski, G. et al. Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in frontotemporal dementia. Nat. Genet. 37, 806-808 (2005).
    • (2005) Nat. Genet , vol.37 , pp. 806-808
    • Skibinski, G.1
  • 23
    • 84865843186 scopus 로고    scopus 로고
    • The genetics and neuropathology of amyotrophic lateral sclerosis
    • Al-Chalabi, A. et al. The genetics and neuropathology of amyotrophic lateral sclerosis. Acta Neuropathol. 124, 339-352 (2012).
    • (2012) Acta Neuropathol , vol.124 , pp. 339-352
    • Al-Chalabi, A.1
  • 24
    • 45749151056 scopus 로고    scopus 로고
    • Animal models of Alzheimer's disease and frontotemporal dementia
    • Gotz, J. & Ittner, L. M. Animal models of Alzheimer's disease and frontotemporal dementia. Nat. Rev. Neurosci. 9, 532-544 (2008).
    • (2008) Nat. Rev. Neurosci , vol.9 , pp. 532-544
    • Gotz, J.1    Ittner, L.M.2
  • 26
    • 84860859564 scopus 로고    scopus 로고
    • Modeling human neurodegenerative diseases in transgenic systems
    • Gama Sosa, M. A., De Gasperi, R. & Elder, G. A. Modeling human neurodegenerative diseases in transgenic systems. Hum. Genet. 131, 535-563 (2012).
    • (2012) Hum. Genet , vol.131 , pp. 535-563
    • Gama Sosa, M.A.1    De Gasperi, R.2    Elder, G.A.3
  • 27
    • 0032560487 scopus 로고    scopus 로고
    • Mutation in the tau gene in familial multiple system tauopathy with presenile dementia
    • Spillantini, M. G. et al. Mutation in the tau gene in familial multiple system tauopathy with presenile dementia. Proc. Natl Acad. Sci. USA 95, 7737-7741 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7737-7741
    • Spillantini, M.G.1
  • 28
    • 14444284106 scopus 로고    scopus 로고
    • Tau is a candidate gene for chromosome 17 frontotemporal dementia
    • Poorkaj, P. et al. Tau is a candidate gene for chromosome 17 frontotemporal dementia. Ann. Neurol. 43, 815-825 (1998).
    • (1998) Ann. Neurol , vol.43 , pp. 815-825
    • Poorkaj, P.1
  • 29
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu Zn superoxide dismutase mutation
    • Gurney, M. E. et al. Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science 264, 1772-1775 (1994).
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1
  • 30
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis, J. et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat. Genet. 25, 402-405 (2000).
    • (2000) Nat. Genet , vol.25 , pp. 402-405
    • Lewis, J.1
  • 31
    • 73249152831 scopus 로고    scopus 로고
    • TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration
    • Wegorzewska, I., Bell, S., Cairns, N. J., Miller, T. M. & Baloh, R. H. TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 106, 18809-18814 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18809-18814
    • Wegorzewska, I.1    Bell, S.2    Cairns, N.J.3    Miller, T.M.4    Baloh, R.H.5
  • 32
    • 77649269011 scopus 로고    scopus 로고
    • TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration
    • Wils, H. et al. TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration. Proc. Natl Acad. Sci. USA 107, 3858-3863 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3858-3863
    • Wils, H.1
  • 33
    • 77956199371 scopus 로고    scopus 로고
    • Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice
    • Xu, Y. F. et al. Wild-type human TDP-43 expression causes TDP-43 phosphorylation, mitochondrial aggregation, motor deficits, and early mortality in transgenic mice. J. Neurosci. 30, 10851-10859 (2010).
    • (2010) J. Neurosci , vol.30 , pp. 10851-10859
    • Xu, Y.F.1
  • 34
    • 79551523377 scopus 로고    scopus 로고
    • Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice
    • Igaz, L. M. et al. Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice. J. Clin. Invest. 121, 726-738 (2011).
    • (2011) J. Clin. Invest , vol.121 , pp. 726-738
    • Igaz, L.M.1
  • 36
    • 80052936462 scopus 로고    scopus 로고
    • Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
    • Swarup, V. et al. Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain 134, 2610-2626 (2011).
    • (2011) Brain , vol.134 , pp. 2610-2626
    • Swarup, V.1
  • 37
    • 84880919532 scopus 로고    scopus 로고
    • Overexpression of ALS-associated p.M337V human TDP-43 in mice worsens disease features compared to wild-type human TDP-43 mice
    • Janssens, J. et al. Overexpression of ALS-associated p.M337V human TDP-43 in mice worsens disease features compared to wild-type human TDP-43 mice. Mol. Neurobiol. 48, 22-35 (2013).
    • (2013) Mol. Neurobiol , vol.48 , pp. 22-35
    • Janssens, J.1
  • 38
    • 84861636497 scopus 로고    scopus 로고
    • HO-1 induction in motor cortex and intestinal dysfunction in TDP-43 A315T transgenic mice
    • Guo, Y. et al. HO-1 induction in motor cortex and intestinal dysfunction in TDP-43 A315T transgenic mice. Brain Res. 1460, 88-95 (2012).
    • (2012) Brain Res , vol.1460 , pp. 88-95
    • Guo, Y.1
  • 39
    • 84872465426 scopus 로고    scopus 로고
    • Premature death of TDP-43 (A315T) transgenic mice due to gastrointestinal complications prior to development of full neurological symptoms of amyotrophic lateral sclerosis
    • Esmaeili, M. A., Panahi, M., Yadav, S., Hennings, L. & Kiaei, M. Premature death of TDP-43 (A315T) transgenic mice due to gastrointestinal complications prior to development of full neurological symptoms of amyotrophic lateral sclerosis. Int. J. Exp. Pathol. 94, 56-64 (2013).
    • (2013) Int. J. Exp. Pathol , vol.94 , pp. 56-64
    • Esmaeili, M.A.1    Panahi, M.2    Yadav, S.3    Hennings, L.4    Kiaei, M.5
  • 40
    • 84907687330 scopus 로고    scopus 로고
    • C57BL/6J congenic Prp-TDP43A315T mice develop progressive neurodegeneration in the myenteric plexus of the colon without exhibiting key features of ALS
    • Hatzipetros, T. et al. C57BL/6J congenic Prp-TDP43A315T mice develop progressive neurodegeneration in the myenteric plexus of the colon without exhibiting key features of ALS. Brain Res. 1584, 59-72 (2014).
    • (2014) Brain Res , vol.1584 , pp. 59-72
    • Hatzipetros, T.1
  • 41
    • 84902300616 scopus 로고    scopus 로고
    • Prevention of intestinal obstruction reveals progressive neurodegeneration in mutant TDP-43 (A315T) mice
    • Herdewyn, S. et al. Prevention of intestinal obstruction reveals progressive neurodegeneration in mutant TDP-43 (A315T) mice. Mol. Neurodegener 9, 24 (2014).
    • (2014) Mol. Neurodegener , vol.9 , pp. 24
    • Herdewyn, S.1
  • 42
    • 76149118401 scopus 로고    scopus 로고
    • Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice
    • Yin, F. et al. Exaggerated inflammation, impaired host defense, and neuropathology in progranulin-deficient mice. J. Exp. Med. 207, 117-128 (2010).
    • (2010) J. Exp. Med , vol.207 , pp. 117-128
    • Yin, F.1
  • 43
    • 84864744790 scopus 로고    scopus 로고
    • Cellular ageing, increased mortality and FTLD-TDP-associated neuropathology in progranulin knockout mice
    • Wils, H. et al. Cellular ageing, increased mortality and FTLD-TDP-associated neuropathology in progranulin knockout mice. J. Pathol. 228, 67-76 (2012).
    • (2012) J. Pathol , vol.228 , pp. 67-76
    • Wils, H.1
  • 44
    • 78149296002 scopus 로고    scopus 로고
    • Behavioral deficits and progressive neuropathology in progranulin-deficient mice: A mouse model of frontotemporal dementia
    • Yin, F. et al. Behavioral deficits and progressive neuropathology in progranulin-deficient mice: a mouse model of frontotemporal dementia. FASEB J. 24, 4639-4647 (2010).
    • (2010) FASEB J , vol.24 , pp. 4639-4647
    • Yin, F.1
  • 45
    • 84855791444 scopus 로고    scopus 로고
    • Synaptic dysfunction in progranulin-deficient mice
    • Petkau, T. L. et al. Synaptic dysfunction in progranulin-deficient mice. Neurobiol. Dis. 45, 711-722 (2012).
    • (2012) Neurobiol. Dis , vol.45 , pp. 711-722
    • Petkau, T.L.1
  • 46
    • 81955160693 scopus 로고    scopus 로고
    • Core features of frontotemporal dementia recapitulated in progranulin knockout mice
    • Ghoshal, N., Dearborn, J. T., Wozniak, D. F. & Cairns, N. J. Core features of frontotemporal dementia recapitulated in progranulin knockout mice. Neurobiol. Dis. 45, 395-408 (2012).
    • (2012) Neurobiol. Dis , vol.45 , pp. 395-408
    • Ghoshal, N.1    Dearborn, J.T.2    Wozniak, D.F.3    Cairns, N.J.4
  • 47
    • 84880579253 scopus 로고    scopus 로고
    • Neuronal-specific overexpression of a mutant valosin-containing protein associated with IBMPFD promotes aberrant ubiquitin and TDP-43 accumulation and cognitive dysfunction in transgenic mice
    • Rodriguez-Ortiz, C. J. et al. Neuronal-specific overexpression of a mutant valosin-containing protein associated with IBMPFD promotes aberrant ubiquitin and TDP-43 accumulation and cognitive dysfunction in transgenic mice. Am. J. Pathol. 183, 504-515 (2013).
    • (2013) Am. J. Pathol , vol.183 , pp. 504-515
    • Rodriguez-Ortiz, C.J.1
  • 48
    • 34447093377 scopus 로고    scopus 로고
    • Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice
    • Weihl, C. C., Miller, S. E., Hanson, P. I. & Pestronk, A. Transgenic expression of inclusion body myopathy associated mutant p97/VCP causes weakness and ubiquitinated protein inclusions in mice. Hum. Mol. Genet. 16, 919-928 (2007).
    • (2007) Hum. Mol. Genet , vol.16 , pp. 919-928
    • Weihl, C.C.1    Miller, S.E.2    Hanson, P.I.3    Pestronk, A.4
  • 49
    • 77952486387 scopus 로고    scopus 로고
    • Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone
    • Custer, S. K., Neumann, M., Lu, H., Wright, A. C. & Taylor, J. P. Transgenic mice expressing mutant forms VCP/p97 recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone. Hum. Mol. Genet. 19, 1741-1755 (2010).
    • (2010) Hum. Mol. Genet , vol.19 , pp. 1741-1755
    • Custer, S.K.1    Neumann, M.2    Lu, H.3    Wright, A.C.4    Taylor, J.P.5
  • 50
    • 78049244477 scopus 로고    scopus 로고
    • VCP associated inclusion body myopathy and Paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease
    • Badadani, M. et al. VCP associated inclusion body myopathy and Paget disease of bone knock-in mouse model exhibits tissue pathology typical of human disease. PLoS ONE 5, e13183 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e13183
    • Badadani, M.1
  • 51
    • 84873029243 scopus 로고    scopus 로고
    • A progressive translational mouse model of human valosin-containing protein disease: The VCPR155H/+ mouse
    • Nalbandian, A. et al. A progressive translational mouse model of human valosin-containing protein disease: the VCPR155H/+ mouse. Muscle Nerve 47, 260-270 (2013).
    • (2013) Muscle Nerve , vol.47 , pp. 260-270
    • Nalbandian, A.1
  • 52
    • 84865752018 scopus 로고    scopus 로고
    • Slow development of ALS-like spinal cord pathology in mutant valosin-containing protein gene knock-in mice
    • Yin, H. Z. et al. Slow development of ALS-like spinal cord pathology in mutant valosin-containing protein gene knock-in mice. Cell Death Dis. 3, e374 (2012).
    • (2012) Cell Death Dis , vol.3 , pp. e374
    • Yin, H.Z.1
  • 53
    • 84875427900 scopus 로고    scopus 로고
    • Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age-and dose-dependent fashion
    • Mitchell, J. C. et al. Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age-and dose-dependent fashion. Acta Neuropathol. 125, 273-288 (2013).
    • (2013) Acta Neuropathol , vol.125 , pp. 273-288
    • Mitchell, J.C.1
  • 54
    • 84857568926 scopus 로고    scopus 로고
    • Progressive neuronal inclusion formation and axonal degeneration in CHMP2B mutant transgenic mice
    • Ghazi-Noori, S. et al. Progressive neuronal inclusion formation and axonal degeneration in CHMP2B mutant transgenic mice. Brain 135, 819-832 (2012).
    • (2012) Brain , vol.135 , pp. 819-832
    • Ghazi-Noori, S.1
  • 55
    • 84876319986 scopus 로고    scopus 로고
    • Controversies and priorities in amyotrophic lateral sclerosis
    • Turner, M. R. et al. Controversies and priorities in amyotrophic lateral sclerosis. Lancet Neurol. 12, 310-322 (2013).
    • (2013) Lancet Neurol , vol.12 , pp. 310-322
    • Turner, M.R.1
  • 56
    • 79952486262 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Kiernan, M. C. et al. Amyotrophic lateral sclerosis. Lancet 377, 942-955 (2011).
    • (2011) Lancet , vol.377 , pp. 942-955
    • Kiernan, M.C.1
  • 57
    • 0036406903 scopus 로고    scopus 로고
    • Minocycline slows disease progression in a mouse model of amyotrophic lateral sclerosis
    • Kriz, J., Nguyen, M. D. & Julien, J. P. Minocycline slows disease progression in a mouse model of amyotrophic lateral sclerosis. Neurobiol. Dis. 10, 268-278 (2002).
    • (2002) Neurobiol. Dis , vol.10 , pp. 268-278
    • Kriz, J.1    Nguyen, M.D.2    Julien, J.P.3
  • 58
    • 36148960127 scopus 로고    scopus 로고
    • Efficacy of minocycline in patients with amyotrophic lateral sclerosis: A phase III randomised trial
    • Gordon, P. H. et al. Efficacy of minocycline in patients with amyotrophic lateral sclerosis: a phase III randomised trial. Lancet Neurol. 6, 1045-1053 (2007).
    • (2007) Lancet Neurol , vol.6 , pp. 1045-1053
    • Gordon, P.H.1
  • 59
    • 79851513221 scopus 로고    scopus 로고
    • Treatment with minocycline after disease onset alters astrocyte reactivity and increases microgliosis in SOD1 mutant mice
    • Keller, A. F., Gravel, M. & Kriz, J. Treatment with minocycline after disease onset alters astrocyte reactivity and increases microgliosis in SOD1 mutant mice. Exp. Neurol. 228, 69-79 (2011).
    • (2011) Exp. Neurol , vol.228 , pp. 69-79
    • Keller, A.F.1    Gravel, M.2    Kriz, J.3
  • 60
    • 19944428649 scopus 로고    scopus 로고
    • Beta-lactam antibiotics offer neuroprotection by increasing glutamate transporter expression
    • Rothstein, J. D. et al. Beta-lactam antibiotics offer neuroprotection by increasing glutamate transporter expression. Nature 433, 73-77 (2005).
    • (2005) Nature , vol.433 , pp. 73-77
    • Rothstein, J.D.1
  • 61
    • 84865794601 scopus 로고    scopus 로고
    • The importance of preclinical trial timing-A potential reason for the disconnect between mouse studies and human clinical trials in ALS
    • Kong, Q., Carothers, S., Chang, Y. & Glenn Lin, C. L. The importance of preclinical trial timing-a potential reason for the disconnect between mouse studies and human clinical trials in ALS. CNS Neurosci. Ther. 18, 791-793 (2012).
    • (2012) CNS Neurosci. Ther , vol.18 , pp. 791-793
    • Kong, Q.1    Carothers, S.2    Chang, Y.3    Glenn Lin, C.L.4
  • 62
    • 84907978186 scopus 로고    scopus 로고
    • Safety and efficacy of ceftriaxone for amyotrophic lateral sclerosis: A multi-stage, randomised, double-blind, placebo-controlled trial
    • Cudkowicz, M. E. et al. Safety and efficacy of ceftriaxone for amyotrophic lateral sclerosis: a multi-stage, randomised, double-blind, placebo-controlled trial. Lancet Neurol. 13, 1083-1091 (2014).
    • (2014) Lancet Neurol , vol.13 , pp. 1083-1091
    • Cudkowicz, M.E.1
  • 63
    • 39349107014 scopus 로고    scopus 로고
    • Design, power, and interpretation of studies in the standard murine model of ALS
    • Scott, S. et al. Design, power, and interpretation of studies in the standard murine model of ALS. Amyotroph. Lateral Scler. 9, 4-15 (2008).
    • (2008) Amyotroph. Lateral Scler , vol.9 , pp. 4-15
    • Scott, S.1
  • 64
    • 84893493940 scopus 로고    scopus 로고
    • Characterization of early pathogenesis in the SOD1G93A mouse model of ALS: Part II, results and discussion
    • Vinsant, S. et al. Characterization of early pathogenesis in the SOD1G93A mouse model of ALS: part II, results and discussion. Brain Behav. 3, 431-457 (2013).
    • (2013) Brain Behav , vol.3 , pp. 431-457
    • Vinsant, S.1
  • 65
    • 77449107448 scopus 로고    scopus 로고
    • Improving toxicity screening and drug development by using genetically defined strains
    • Festing, M. F. Improving toxicity screening and drug development by using genetically defined strains. Methods Mol. Biol. 602, 1-21 (2010).
    • (2010) Methods Mol. Biol , vol.602 , pp. 1-21
    • Festing, M.F.1
  • 66
    • 84866423602 scopus 로고    scopus 로고
    • Neuronal sensitivity to TDP-43 overexpression is dependent on timing of induction
    • Cannon, A. et al. Neuronal sensitivity to TDP-43 overexpression is dependent on timing of induction. Acta Neuropathol. 123, 807-823 (2012).
    • (2012) Acta Neuropathol , vol.123 , pp. 807-823
    • Cannon, A.1
  • 67
    • 22344438508 scopus 로고    scopus 로고
    • Tau suppression in a neurodegenerative mouse model improves memory function
    • Santacruz, K. et al. Tau suppression in a neurodegenerative mouse model improves memory function. Science 309, 476-481 (2005).
    • (2005) Science , vol.309 , pp. 476-481
    • Santacruz, K.1
  • 68
    • 79951818085 scopus 로고    scopus 로고
    • Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic tau mutant
    • Sydow, A. et al. Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic tau mutant. J. Neurosci. 31, 2511-2525 (2011).
    • (2011) J. Neurosci , vol.31 , pp. 2511-2525
    • Sydow, A.1
  • 69
    • 84899536781 scopus 로고    scopus 로고
    • Divergent phenotypes in mutant TDP-43 transgenic mice highlight potential confounds in TDP-43 transgenic modeling
    • D'Alton, S. et al. Divergent phenotypes in mutant TDP-43 transgenic mice highlight potential confounds in TDP-43 transgenic modeling. PLoS ONE 9, e86513 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e86513
    • D'Alton, S.1
  • 70
    • 84908494841 scopus 로고    scopus 로고
    • Inducible tightly regulated and non-leaky neuronal gene expression in mice
    • Delerue, F., White, M. & Ittner, L. M. Inducible, tightly regulated and non-leaky neuronal gene expression in mice. Transgenic Res. 23, 225-233 (2014).
    • (2014) Transgenic Res , vol.23 , pp. 225-233
    • Delerue, F.1    White, M.2    Ittner, L.M.3
  • 71
    • 80155157847 scopus 로고    scopus 로고
    • The seeds of neurodegeneration: Prion-like spreading in ALS
    • Polymenidou, M. & Cleveland, D. W. The seeds of neurodegeneration: prion-like spreading in ALS. Cell 147, 498-508 (2011).
    • (2011) Cell , vol.147 , pp. 498-508
    • Polymenidou, M.1    Cleveland, D.W.2
  • 72
    • 84861841901 scopus 로고    scopus 로고
    • Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation?
    • Kanouchi, T., Ohkubo, T. & Yokota, T. Can regional spreading of amyotrophic lateral sclerosis motor symptoms be explained by prion-like propagation? J. Neurol. Neurosurg. Psychiatry 83, 739-745 (2012).
    • (2012) J. Neurol. Neurosurg. Psychiatry , vol.83 , pp. 739-745
    • Kanouchi, T.1    Ohkubo, T.2    Yokota, T.3
  • 73
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost, B. & Diamond, M. I. Prion-like mechanisms in neurodegenerative diseases. Nat. Rev. Neurosci. 11, 155-159 (2010).
    • (2010) Nat. Rev. Neurosci , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 74
    • 84902486430 scopus 로고    scopus 로고
    • Distinct tau prion strains propagate in cells and mice and define different tauopathies
    • Sanders, D. W. et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 82, 1271-1288 (2014).
    • (2014) Neuron , vol.82 , pp. 1271-1288
    • Sanders, D.W.1
  • 75
    • 67650077008 scopus 로고    scopus 로고
    • Transmission and spreading of tauopathy in transgenic mouse brain
    • Clavaguera, F. et al. Transmission and spreading of tauopathy in transgenic mouse brain. Nat. Cell Biol. 11, 909-913 (2009).
    • (2009) Nat. Cell Biol , vol.11 , pp. 909-913
    • Clavaguera, F.1
  • 76
    • 84878723720 scopus 로고    scopus 로고
    • Brain homogenates from human tauopathies induce tau inclusions in mouse brain
    • Clavaguera, F. et al. Brain homogenates from human tauopathies induce tau inclusions in mouse brain. Proc. Natl Acad. Sci. USA 110, 9535-9540 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9535-9540
    • Clavaguera, F.1
  • 77
    • 84885783467 scopus 로고    scopus 로고
    • Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo
    • Yanamandra, K. et al. Anti-tau antibodies that block tau aggregate seeding in vitro markedly decrease pathology and improve cognition in vivo. Neuron 80, 402-414 (2013).
    • (2013) Neuron , vol.80 , pp. 402-414
    • Yanamandra, K.1
  • 78
    • 84899944338 scopus 로고    scopus 로고
    • A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: The pattern of spread is determined by connectivity, not proximity
    • Ahmed, Z. et al. A novel in vivo model of tau propagation with rapid and progressive neurofibrillary tangle pathology: the pattern of spread is determined by connectivity, not proximity. Acta Neuropathol. 127, 667-683 (2014).
    • (2014) Acta Neuropathol , vol.127 , pp. 667-683
    • Ahmed, Z.1
  • 79
    • 84872346089 scopus 로고    scopus 로고
    • Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy
    • Iba, M. et al. Synthetic tau fibrils mediate transmission of neurofibrillary tangles in a transgenic mouse model of Alzheimer's-like tauopathy. J. Neurosci. 33, 1024-1037 (2013).
    • (2013) J. Neurosci , vol.33 , pp. 1024-1037
    • Iba, M.1
  • 80
    • 84883292041 scopus 로고    scopus 로고
    • Stages of pTDP-43 pathology in amyotrophic lateral sclerosis
    • Brettschneider, J. et al. Stages of pTDP-43 pathology in amyotrophic lateral sclerosis. Ann. Neurol. 74, 20-38 (2013).
    • (2013) Ann. Neurol , vol.74 , pp. 20-38
    • Brettschneider, J.1
  • 81
    • 84921935837 scopus 로고    scopus 로고
    • Experimental transmissibility of mutant SOD1 motor neuron disease
    • Ayers, J. I. et al. Experimental transmissibility of mutant SOD1 motor neuron disease. Acta Neuropathol. 128, 791-803 (2014).
    • (2014) Acta Neuropathol , vol.128 , pp. 791-803
    • Ayers, J.I.1
  • 82
    • 84856454190 scopus 로고    scopus 로고
    • Trans-synaptic spread of tau pathology in vivo
    • Liu, L. et al. Trans-synaptic spread of tau pathology in vivo. PLoS ONE 7, e31302 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e31302
    • Liu, L.1
  • 83
    • 84857275902 scopus 로고    scopus 로고
    • Propagation of tau pathology in a model of early Alzheimer's disease
    • De Calignon, A. et al. Propagation of tau pathology in a model of early Alzheimer's disease. Neuron 73, 685-697 (2012).
    • (2012) Neuron , vol.73 , pp. 685-697
    • De Calignon, A.1
  • 84
    • 84903541550 scopus 로고    scopus 로고
    • Neuron-to-neuron wild-type tau protein transfer through a trans-synaptic mechanism: Relevance to sporadic tauopathies
    • Dujardin, S. et al. Neuron-to-neuron wild-type tau protein transfer through a trans-synaptic mechanism: relevance to sporadic tauopathies. Acta Neuropathol. Commun. 2, 14 (2014).
    • (2014) Acta Neuropathol. Commun , vol.2 , pp. 14
    • Dujardin, S.1
  • 85
    • 85027906921 scopus 로고    scopus 로고
    • Tau-targeting passive immunization modulates aspects of pathology in tau transgenic mice
    • Ittner, A. et al. Tau-targeting passive immunization modulates aspects of pathology in tau transgenic mice. J. Neurochem. (2014).
    • (2014) J. Neurochem.
    • Ittner, A.1
  • 86
    • 84891945085 scopus 로고    scopus 로고
    • Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo
    • Kuchibhotla, K. V. et al. Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo. Proc. Natl Acad. Sci. USA 111, 510-514 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 510-514
    • Kuchibhotla, K.V.1
  • 87
    • 84871712720 scopus 로고    scopus 로고
    • Synaptic scaffold evolution generated components of vertebrate cognitive complexity
    • Nithianantharajah, J. et al. Synaptic scaffold evolution generated components of vertebrate cognitive complexity. Nat. Neurosci. 16, 16-24 (2013).
    • (2013) Nat. Neurosci , vol.16 , pp. 16-24
    • Nithianantharajah, J.1
  • 88
    • 84860334015 scopus 로고    scopus 로고
    • Inhibitory interneuron deficit links altered network activity and cognitive dysfunction in Alzheimer model
    • Verret, L. et al. Inhibitory interneuron deficit links altered network activity and cognitive dysfunction in Alzheimer model. Cell 149, 708-721 (2012).
    • (2012) Cell , vol.149 , pp. 708-721
    • Verret, L.1
  • 89
    • 84964697116 scopus 로고    scopus 로고
    • P38 MAP kinase-mediated NMDA receptor-dependent suppression of hippocampal hypersynchronicity in a mouse model of Alzheimer inverted question marks disease
    • Ittner, A. A., Gladbach, A., Bertz, J., Suh, L. S. & Ittner, L. M. p38 MAP kinase-mediated NMDA receptor-dependent suppression of hippocampal hypersynchronicity in a mouse model of Alzheimer inverted question marks disease. Acta Neuropathol. Commun. 2, 149 (2014).
    • (2014) Acta Neuropathol. Commun , vol.2 , pp. 149
    • Ittner, A.A.1    Gladbach, A.2    Bertz, J.3    Suh, L.S.4    Ittner, L.M.5
  • 90
    • 84874835620 scopus 로고    scopus 로고
    • Distinct clinical characteristics of C9orf72 expansion carriers compared with GRN MAPT and nonmutation carriers in a Flanders-Belgian FTLD cohort
    • Van Langenhove, T. et al. Distinct clinical characteristics of C9orf72 expansion carriers compared with GRN, MAPT, and nonmutation carriers in a Flanders-Belgian FTLD cohort. JAMA Neurol. 70, 365-373 (2013).
    • (2013) JAMA Neurol , vol.70 , pp. 365-373
    • Van Langenhove, T.1
  • 91
    • 84896781404 scopus 로고    scopus 로고
    • Frontotemporal dementia associated with the C9ORF72 mutation: A unique clinical profile
    • Devenney, E. et al. Frontotemporal dementia associated with the C9ORF72 mutation: a unique clinical profile. JAMA Neurol. 71, 331-339 (2014).
    • (2014) JAMA Neurol , vol.71 , pp. 331-339
    • Devenney, E.1
  • 92
    • 84874272095 scopus 로고    scopus 로고
    • Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS
    • Ash, P. E. et al. Unconventional translation of C9ORF72 GGGGCC expansion generates insoluble polypeptides specific to c9FTD/ALS. Neuron 77, 639-646 (2013).
    • (2013) Neuron , vol.77 , pp. 639-646
    • Ash, P.E.1
  • 93
    • 84874962380 scopus 로고    scopus 로고
    • The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS
    • Mori, K. et al. The C9orf72 GGGGCC repeat is translated into aggregating dipeptide-repeat proteins in FTLD/ALS. Science 339, 1335-1338 (2013).
    • (2013) Science , vol.339 , pp. 1335-1338
    • Mori, K.1
  • 94
    • 83555166183 scopus 로고    scopus 로고
    • A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: A gene identification study
    • Gijselinck, I. et al. A C9orf72 promoter repeat expansion in a Flanders-Belgian cohort with disorders of the frontotemporal lobar degeneration-amyotrophic lateral sclerosis spectrum: a gene identification study. Lancet Neurol. 11, 54-65 (2012).
    • (2012) Lancet Neurol , vol.11 , pp. 54-65
    • Gijselinck, I.1
  • 96
    • 84964697584 scopus 로고    scopus 로고
    • A new inducible transgenic mouse model for C9orf72-associated GGGGCC repeat expansion supports a gain-of-function mechanism in C9orf72 associated ALS and FTD
    • Hukema, R. K. et al. A new inducible transgenic mouse model for C9orf72-associated GGGGCC repeat expansion supports a gain-of-function mechanism in C9orf72 associated ALS and FTD. Acta Neuropathol. Commun. 2, 166 (2014).
    • (2014) Acta Neuropathol. Commun , vol.2 , pp. 166
    • Hukema, R.K.1
  • 97
    • 84887061001 scopus 로고    scopus 로고
    • Highly efficient targeted mutagenesis in mice using TALENs
    • Panda, S. K. et al. Highly efficient targeted mutagenesis in mice using TALENs. Genetics 195, 703-713 (2013).
    • (2013) Genetics , vol.195 , pp. 703-713
    • Panda, S.K.1
  • 98
    • 84907188956 scopus 로고    scopus 로고
    • C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins
    • Mizielinska, S. et al. C9orf72 repeat expansions cause neurodegeneration in Drosophila through arginine-rich proteins. Science 345, 1192-1194 (2014).
    • (2014) Science , vol.345 , pp. 1192-1194
    • Mizielinska, S.1
  • 99
    • 84987781385 scopus 로고    scopus 로고
    • Systems-level G Protein-coupled receptor therapy across a neurodegenerative continuum by the GLP-1 receptor system
    • Janssens, J. et al. Systems-level G Protein-coupled receptor therapy across a neurodegenerative continuum by the GLP-1 receptor system. Front. Endocrinol. (Lausanne) 5, 142 (2014).
    • (2014) Front. Endocrinol. (Lausanne) , vol.5 , pp. 142
    • Janssens, J.1
  • 100
    • 84925283253 scopus 로고    scopus 로고
    • Systemic metabolism in frontotemporal dementia
    • Ahmed, R. M. et al. Systemic metabolism in frontotemporal dementia Neurology 83, 1812-1818 (2014).
    • (2014) Neurology , vol.83 , pp. 1812-1818
    • Ahmed, R.M.1
  • 101
    • 79958260092 scopus 로고    scopus 로고
    • The human brain in a dish: The promise of iPSC-derived neurons
    • Dolmetsch, R. & Geschwind, D. H. The human brain in a dish: the promise of iPSC-derived neurons. Cell 145, 831-834 (2011).
    • (2011) Cell , vol.145 , pp. 831-834
    • Dolmetsch, R.1    Geschwind, D.H.2
  • 102
    • 84885808774 scopus 로고    scopus 로고
    • RNA Toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention
    • Donnelly, C. J. et al. RNA Toxicity from the ALS/FTD C9ORF72 expansion is mitigated by antisense intervention. Neuron 80, 415-428 (2013).
    • (2013) Neuron , vol.80 , pp. 415-428
    • Donnelly, C.J.1
  • 103
    • 84886389563 scopus 로고    scopus 로고
    • Targeting RNA foci in iPSC-derived motor neurons from ALS patients with a C9ORF72 repeat expansion.
    • Sareen, D. et al. Targeting RNA foci in iPSC-derived motor neurons from ALS patients with a C9ORF72 repeat expansion. Sci. Transl. Med. 5, 208ra149 (2013).
    • (2013) Sci. Transl. Med , vol.5 , pp. 208-149
    • Sareen, D.1
  • 104
    • 84888098632 scopus 로고    scopus 로고
    • Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration
    • Lagier-Tourenne, C. et al. Targeted degradation of sense and antisense C9orf72 RNA foci as therapy for ALS and frontotemporal degeneration. Proc. Natl Acad. Sci. USA 110, E4530-E4539 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E4530-E4539
    • Lagier-Tourenne, C.1
  • 105
    • 84882687005 scopus 로고    scopus 로고
    • C9RAN translation: A potential therapeutic target for the treatment of amyotrophic lateral sclerosis and frontotemporal dementia
    • Gendron, T. F., Cosio, D. M. & Petrucelli, L. c9RAN translation: a potential therapeutic target for the treatment of amyotrophic lateral sclerosis and frontotemporal dementia. Expert Opin. Ther. Targets. 17, 991-995 (2013).
    • (2013) Expert Opin. Ther. Targets , vol.17 , pp. 991-995
    • Gendron, T.F.1    Cosio, D.M.2    Petrucelli, L.3
  • 106
    • 84873729095 scopus 로고    scopus 로고
    • Multiplex genome engineering using CRISPR/Cas systems
    • Cong, L. et al. Multiplex genome engineering using CRISPR/Cas systems. Science 339, 819-823 (2013).
    • (2013) Science , vol.339 , pp. 819-823
    • Cong, L.1
  • 107
    • 84873734105 scopus 로고    scopus 로고
    • RNA-guided human genome engineering via Cas9
    • Mali, P. et al. RNA-guided human genome engineering via Cas9. Science 339, 823-826 (2013).
    • (2013) Science , vol.339 , pp. 823-826
    • Mali, P.1
  • 108
    • 84884289608 scopus 로고    scopus 로고
    • One-step generation of mice carrying reporter and conditional alleles by CRISPR/Cas-mediated genome engineering
    • Yang, H. et al. One-step generation of mice carrying reporter and conditional alleles by CRISPR/Cas-mediated genome engineering. Cell 154, 1370-1379 (2013).
    • (2013) Cell , vol.154 , pp. 1370-1379
    • Yang, H.1
  • 109
    • 84877707375 scopus 로고    scopus 로고
    • One-step generation of mice carrying mutations in multiple genes by CRISPR/Cas-mediated genome engineering
    • Wang, H. et al. One-step generation of mice carrying mutations in multiple genes by CRISPR/Cas-mediated genome engineering. Cell 153, 910-918 (2013).
    • (2013) Cell , vol.153 , pp. 910-918
    • Wang, H.1
  • 110
    • 77956385203 scopus 로고    scopus 로고
    • Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models
    • van Eersel, J. et al. Sodium selenate mitigates tau pathology, neurodegeneration, and functional deficits in Alzheimer's disease models. Proc. Natl Acad. Sci. USA 107, 13888-13893 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13888-13893
    • Van Eersel, J.1
  • 111
    • 0029053881 scopus 로고
    • An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria
    • Wong, P. C. et al. An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105-1116 (1995).
    • (1995) Neuron , vol.14 , pp. 1105-1116
    • Wong, P.C.1
  • 112
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn, L. I. et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 18, 327-338 (1997).
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1
  • 114
    • 0030050727 scopus 로고    scopus 로고
    • Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis
    • Gurney, M. E. et al. Benefit of vitamin E, riluzole, and gabapentin in a transgenic model of familial amyotrophic lateral sclerosis. Ann. Neurol. 39, 147-157 (1996).
    • (1996) Ann. Neurol , vol.39 , pp. 147-157
    • Gurney, M.E.1
  • 115
    • 57349172663 scopus 로고    scopus 로고
    • Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia
    • Ittner, L. M. et al. Parkinsonism and impaired axonal transport in a mouse model of frontotemporal dementia. Proc. Natl Acad. Sci. USA 105, 15597-16002 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 15597-16002
    • Ittner, L.M.1
  • 116
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • Asuni, A. A., Boutajangout, A., Quartermain, D. & Sigurdsson, E. M. Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J. Neurosci. 27, 9115-9129 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 117
    • 82955194797 scopus 로고    scopus 로고
    • Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice
    • Bi, M., Ittner, A., Ke, Y. D., Gotz, J. & Ittner, L. M. Tau-targeted immunization impedes progression of neurofibrillary histopathology in aged P301L tau transgenic mice. PLoS ONE 6, e26860 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e26860
    • Bi, M.1    Ittner, A.2    Ke, Y.D.3    Gotz, J.4    Ittner, L.M.5
  • 118
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • Boimel, M. et al. Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp. Neurol. 224, 472-485 (2010).
    • (2010) Exp. Neurol , vol.224 , pp. 472-485
    • Boimel, M.1
  • 119
    • 80053202160 scopus 로고    scopus 로고
    • Passive immunization with anti-Tau antibodies in two transgenic models: Reduction of Tau pathology and delay of disease progression
    • Chai, X. et al. Passive immunization with anti-Tau antibodies in two transgenic models: reduction of Tau pathology and delay of disease progression. J. Biol. Chem. 286, 34457-34467 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 34457-34467
    • Chai, X.1
  • 120
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: Molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee, E. B., Lee, V. M. & Trojanowski, J. Q. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat. Rev. Neurosci. 13, 38-50 (2012).
    • (2012) Nat. Rev. Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 121
    • 84885383793 scopus 로고    scopus 로고
    • The murky path to drug discovery in ALS becomes clearer
    • Gordon, P. H. The murky path to drug discovery in ALS becomes clearer. Lancet Neurol. 12, 1037-1038 (2013).
    • (2013) Lancet Neurol , vol.12 , pp. 1037-1038
    • Gordon, P.H.1
  • 122
    • 80755146087 scopus 로고    scopus 로고
    • Biomarkers in amyotrophic lateral sclerosis: Opportunities and limitations
    • Bowser, R., Turner, M. R. & Shefner, J. Biomarkers in amyotrophic lateral sclerosis: opportunities and limitations. Nat. Rev. Neurol. 7, 631-638 (2011).
    • (2011) Nat. Rev. Neurol , vol.7 , pp. 631-638
    • Bowser, R.1    Turner, M.R.2    Shefner, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.