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Volumn 10, Issue 8, 2014, Pages 677-685

Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models

(13)  Barmada, Sami J a,b,c   Serio, Andrea d,e,f   Arjun, Arpana a   Bilican, Bilada d,e   Daub, Aaron a   Ando, D Michael a,g   Tsvetkov, Andrey a,h   Pleiss, Michael i   Li, Xingli c   Peisach, Daniel c   Shaw, Christopher j   Chandran, Siddharthan a,e   Finkbeiner, Steven a,b,g,i,k,l,m  


Author keywords

[No Author keywords available]

Indexed keywords

TAR DNA BINDING PROTEIN;

EID: 84904729990     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1563     Document Type: Article
Times cited : (344)

References (50)
  • 1
    • 84875441083 scopus 로고    scopus 로고
    • Te changing scene of amyotrophic lateral sclerosis
    • Robberecht, W. & Philips, T. Te changing scene of amyotrophic lateral sclerosis. Nat. Rev. Neurosci. 14, 248-264 (2013).
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 248-264
    • Robberecht, W.1    Philips, T.2
  • 2
    • 59649086176 scopus 로고    scopus 로고
    • Molecular neuropathology of TDP-43 proteinopathies
    • Neumann, M. Molecular neuropathology of TDP-43 proteinopathies. Int. J. Mol. Sci. 10, 232-246 (2009).
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 232-246
    • Neumann, M.1
  • 3
    • 77954690411 scopus 로고    scopus 로고
    • RNA processing pathways in amyotrophic lateral sclerosis
    • doi:10.1007/s10048-010-0239-4
    • van Blitterswijk, M. & Landers, J.E. RNA processing pathways in amyotrophic lateral sclerosis. Neurogenetics doi:10.1007/s10048-010-0239-4 (2010).
    • (2010) Neurogenetics
    • Van Blitterswijk, M.1    Landers, J.E.2
  • 4
    • 59549094064 scopus 로고    scopus 로고
    • Structural determinants of the cellular localization and shuttling of TDP-43
    • Ayala, Y.M. et al. Structural determinants of the cellular localization and shuttling of TDP-43. J. Cell Sci. 121, 3778-3785 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 3778-3785
    • Ayala, Y.M.1
  • 5
    • 70349292075 scopus 로고    scopus 로고
    • -/- mice: Support for a role for TDP-43 in the physiological response to neuronal injury
    • -/- mice: support for a role for TDP-43 in the physiological response to neuronal injury. Brain Res. 1296, 176-186 (2009).
    • (2009) Brain Res. , vol.1296 , pp. 176-186
    • Moisse, K.1
  • 6
    • 79952268025 scopus 로고    scopus 로고
    • TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor
    • Dewey, C.M. et al. TDP-43 is directed to stress granules by sorbitol, a novel physiological osmotic and oxidative stressor. Mol. Cell. Biol. 31, 1098-1108 (2011).
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1098-1108
    • Dewey, C.M.1
  • 7
    • 82355181107 scopus 로고    scopus 로고
    • TDP-43 pathological changes in early onset familial and sporadic Alzheimer's disease, late onset Alzheimer's disease and Down's Syndrome: Association with age, hippocampal sclerosis and clinical phenotype
    • Davidson, Y.S. et al. TDP-43 pathological changes in early onset familial and sporadic Alzheimer's disease, late onset Alzheimer's disease and Down's Syndrome: association with age, hippocampal sclerosis and clinical phenotype. Acta Neuropathol. 122, 703-713 (2011).
    • (2011) Acta Neuropathol. , vol.122 , pp. 703-713
    • Davidson, Y.S.1
  • 8
    • 78349241067 scopus 로고    scopus 로고
    • Pathogenic TARDBP mutations in amyotrophic lateral sclerosis and frontotemporal dementia: Disease-associated pathways
    • Barmada, S.J. & Finkbeiner, S. Pathogenic TARDBP mutations in amyotrophic lateral sclerosis and frontotemporal dementia: disease-associated pathways. Rev. Neurosci. 21, 251-272 (2010).
    • (2010) Rev. Neurosci. , vol.21 , pp. 251-272
    • Barmada, S.J.1    Finkbeiner, S.2
  • 9
    • 74949135753 scopus 로고    scopus 로고
    • Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis
    • Barmada, S.J. et al. Cytoplasmic mislocalization of TDP-43 is toxic to neurons and enhanced by a mutation associated with familial amyotrophic lateral sclerosis. J. Neurosci. 30, 639-649 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 639-649
    • Barmada, S.J.1
  • 10
    • 84862118369 scopus 로고    scopus 로고
    • Rodent models of TDP-43: Recent advances
    • Tsao, W. et al. Rodent models of TDP-43: recent advances. Brain Res. 1462, 26-39 (2012).
    • (2012) Brain Res. , vol.1462 , pp. 26-39
    • Tsao, W.1
  • 11
    • 84872000265 scopus 로고    scopus 로고
    • Mouse models of frontotemporal dementia
    • Roberson, E.D. Mouse models of frontotemporal dementia. Ann. Neurol. 72, 837-849 (2012).
    • (2012) Ann. Neurol. , vol.72 , pp. 837-849
    • Roberson, E.D.1
  • 12
    • 77955784599 scopus 로고    scopus 로고
    • ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS
    • Ling, S.-C. et al. ALS-associated mutations in TDP-43 increase its stability and promote TDP-43 complexes with FUS/TLS. Proc. Natl. Acad. Sci. USA 107, 13318-13323 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13318-13323
    • Ling, S.-C.1
  • 13
    • 84873314938 scopus 로고    scopus 로고
    • Accelerated disease onset with stabilized familial Amyotrophic Lateral Sclerosis (ALS)-linked TDP-43 mutations
    • Watanabe, S., Kaneko, K. & Yamanaka, K. Accelerated disease onset with stabilized familial Amyotrophic Lateral Sclerosis (ALS)-linked TDP-43 mutations. J. Biol. Chem. 288, 3641-3654 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 3641-3654
    • Watanabe, S.1    Kaneko, K.2    Yamanaka, K.3
  • 14
    • 80053563760 scopus 로고    scopus 로고
    • Induction of autophagy with catalytic mTOR inhibitors reduces huntingtin aggregates in a neuronal cell model
    • Roscic, A., Baldo, B., Crochemore, C., Marcellin, D. & Paganetti, P. Induction of autophagy with catalytic mTOR inhibitors reduces huntingtin aggregates in a neuronal cell model. J. Neurochem. 119, 398-407 (2011).
    • (2011) J. Neurochem. , vol.119 , pp. 398-407
    • Roscic, A.1    Baldo, B.2    Crochemore, C.3    Marcellin, D.4    Paganetti, P.5
  • 15
    • 32644474993 scopus 로고    scopus 로고
    • Regulation of IRF7 through cell type-specifc protein stability
    • Prakash, A. & Levy, D.E. Regulation of IRF7 through cell type-specifc protein stability. Biochem. Biophys. Res. Commun. 342, 50-56 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 50-56
    • Prakash, A.1    Levy, D.E.2
  • 16
    • 72649087184 scopus 로고    scopus 로고
    • Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system
    • Wang, X. et al. Degradation of TDP-43 and its pathogenic form by autophagy and the ubiquitin-proteasome system. Neurosci. Lett. 469, 112-116 (2010).
    • (2010) Neurosci. Lett. , vol.469 , pp. 112-116
    • Wang, X.1
  • 17
    • 76549101965 scopus 로고    scopus 로고
    • Synergistic efect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43
    • Urushitani, M., Sato, T., Bamba, H., Hisa, Y. & Tooyama, I. Synergistic efect between proteasome and autophagosome in the clearance of polyubiquitinated TDP-43. J. Neurosci. Res. 88, 784-797 (2010).
    • (2010) J. Neurosci. Res. , vol.88 , pp. 784-797
    • Urushitani, M.1    Sato, T.2    Bamba, H.3    Hisa, Y.4    Tooyama, I.5
  • 18
    • 79953647105 scopus 로고    scopus 로고
    • G93A mouse model of amyotrophic lateral sclerosis
    • G93A mouse model of amyotrophic lateral sclerosis. Autophagy 7, 412-425 (2011).
    • (2011) Autophagy , vol.7 , pp. 412-425
    • Zhang, X.1
  • 19
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 defciency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz, C. et al. XBP-1 defciency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 23, 2294-2306 (2009).
    • (2009) Genes Dev. , vol.23 , pp. 2294-2306
    • Hetz, C.1
  • 20
    • 84866289381 scopus 로고    scopus 로고
    • Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43
    • Wang, I.-F. et al. Autophagy activators rescue and alleviate pathogenesis of a mouse model with proteinopathies of the TAR DNA-binding protein 43. Proc. Natl. Acad. Sci. USA 109, 15024-15029 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15024-15029
    • Wang, I.-F.1
  • 21
    • 77953665285 scopus 로고    scopus 로고
    • Te mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease
    • Fox, J.H. et al. Te mTOR kinase inhibitor Everolimus decreases S6 kinase phosphorylation but fails to reduce mutant huntingtin levels in brain and is not neuroprotective in the R6/2 mouse model of Huntington's disease. Mol. Neurodegener. 5, 26 (2010).
    • (2010) Mol. Neurodegener. , vol.5 , pp. 26
    • Fox, J.H.1
  • 22
    • 78049231804 scopus 로고    scopus 로고
    • A small-molecule scafold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model
    • Tsvetkov, A.S. et al. A small-molecule scafold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model. Proc. Natl. Acad. Sci. USA 107, 16982-16987 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16982-16987
    • Tsvetkov, A.S.1
  • 23
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante, M. & Sabatini, D.M. mTOR signaling in growth control and disease. Cell 149, 274-293 (2012).
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 24
    • 41949119043 scopus 로고    scopus 로고
    • TDP-43 A315T mutation in familial motor neuron disease
    • Gitcho, M.A. et al. TDP-43 A315T mutation in familial motor neuron disease. Ann. Neurol. 63, 535-538 (2008).
    • (2008) Ann. Neurol. , vol.63 , pp. 535-538
    • Gitcho, M.A.1
  • 25
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E.S., Segal, M.R. & Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810 (2004).
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 26
    • 84880783961 scopus 로고    scopus 로고
    • Te pathological phenotypes of human TDP-43 transgenic mouse models are independent of downregulation of mouse Tdp-43
    • Xu, Y.-F. et al. Te pathological phenotypes of human TDP-43 transgenic mouse models are independent of downregulation of mouse Tdp-43. PLoS ONE 8, e69864 (2013).
    • (2013) PLoS ONE , vol.8
    • Xu, Y.-F.1
  • 27
    • 34548181882 scopus 로고    scopus 로고
    • Tracking intracellular protein movements using photoswitchable fuorescent proteins PS-CFP2 and Dendra2
    • Chudakov, D.M., Lukyanov, S. & Lukyanov, K.A. Tracking intracellular protein movements using photoswitchable fuorescent proteins PS-CFP2 and Dendra2. Nat. Protoc. 2, 2024-2032 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 2024-2032
    • Chudakov, D.M.1    Lukyanov, S.2    Lukyanov, K.A.3
  • 28
    • 79952585579 scopus 로고    scopus 로고
    • Integration of clearance mechanisms: The proteasome and autophagy
    • Wong, E. & Cuervo, A.M. Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb. Perspect. Biol. 2, a006734 (2010).
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Wong, E.1    Cuervo, A.M.2
  • 29
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky, D.J. et al. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy 4, 151-175 (2008).
    • (2008) Autophagy , vol.4 , pp. 151-175
    • Klionsky, D.J.1
  • 30
    • 53549132786 scopus 로고    scopus 로고
    • Beclin 1 bridges autophagy, apoptosis and diferentiation
    • Wang, J. Beclin 1 bridges autophagy, apoptosis and diferentiation. Autophagy 4, 947-948 (2008).
    • (2008) Autophagy , vol.4 , pp. 947-948
    • Wang, J.1
  • 31
    • 0032896760 scopus 로고    scopus 로고
    • Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways
    • Kim, J., Dalton, V.M., Eggerton, K.P., Scott, S.V. & Klionsky, D.J. Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways. Mol. Biol. Cell 10, 1337-1351 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1337-1351
    • Kim, J.1    Dalton, V.M.2    Eggerton, K.P.3    Scott, S.V.4    Klionsky, D.J.5
  • 32
    • 84859569070 scopus 로고    scopus 로고
    • Mutant induced pluripotent stem cell lines recapitulate aspects of TDP-43 proteinopathies and reveal cell-specifc vulnerability
    • Bilican, B. et al. Mutant induced pluripotent stem cell lines recapitulate aspects of TDP-43 proteinopathies and reveal cell-specifc vulnerability. Proc. Natl. Acad. Sci. USA 109, 5803-5808 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 5803-5808
    • Bilican, B.1
  • 33
    • 27744438009 scopus 로고    scopus 로고
    • Enhancer-specifed GFP-based FACS purifcation of human spinal motor neurons from embryonic stem cells
    • Singh Roy, N. et al. Enhancer-specifed GFP-based FACS purifcation of human spinal motor neurons from embryonic stem cells. Exp. Neurol. 196, 224-234 (2005).
    • (2005) Exp. Neurol. , vol.196 , pp. 224-234
    • Singh Roy, N.1
  • 34
    • 60549117972 scopus 로고    scopus 로고
    • Clinical and pathological continuum of multisystem TDP-43 proteinopathies
    • Geser, F. et al. Clinical and pathological continuum of multisystem TDP-43 proteinopathies. Arch. Neurol. 66, 180-189 (2009).
    • (2009) Arch. Neurol. , vol.66 , pp. 180-189
    • Geser, F.1
  • 35
    • 0023434104 scopus 로고
    • MAP2 and tau segregate into dendritic and axonal domains afer the elaboration of morphologically distinct neurites: An immunocytochemical study of cultured rat cerebrum
    • Kosik, K.S. & Finch, E.A. MAP2 and tau segregate into dendritic and axonal domains afer the elaboration of morphologically distinct neurites: an immunocytochemical study of cultured rat cerebrum. J. Neurosci. 7, 3142-3153 (1987).
    • (1987) J. Neurosci. , vol.7 , pp. 3142-3153
    • Kosik, K.S.1    Finch, E.A.2
  • 36
    • 33749056809 scopus 로고    scopus 로고
    • ALS: A disease of motor neurons and their nonneuronal neighbors
    • Boillée, S., Vande Velde, C. & Cleveland, D.W. ALS: a disease of motor neurons and their nonneuronal neighbors. Neuron 52, 39-59 (2006).
    • (2006) Neuron , vol.52 , pp. 39-59
    • Boillée, S.1    Vande Velde, C.2    Cleveland, D.W.3
  • 37
    • 84875275232 scopus 로고    scopus 로고
    • Astrocyte pathology and the absence of non-cell autonomy in an induced pluripotent stem cell model of TDP-43 proteinopathy
    • doi:10.1073/pnas.1300398110
    • Serio, A. et al. Astrocyte pathology and the absence of non-cell autonomy in an induced pluripotent stem cell model of TDP-43 proteinopathy. Proc. Natl. Acad. Sci. USA doi:10.1073/pnas.1300398110 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA
    • Serio, A.1
  • 38
    • 84864542080 scopus 로고    scopus 로고
    • Drug screening for ALS using patient-specifc induced pluripotent stem cells
    • Egawa, N. et al. Drug screening for ALS using patient-specifc induced pluripotent stem cells. Sci. Transl. Med. 5, 188lr2 (2012).
    • (2012) Sci. Transl. Med. , vol.5
    • Egawa, N.1
  • 39
    • 3242755831 scopus 로고    scopus 로고
    • Clinically approved heterocyclics act on a mitochondrial target and reduce stroke-induced pathology
    • Stavrovskaya, I.G. Clinically approved heterocyclics act on a mitochondrial target and reduce stroke-induced pathology. J. Exp. Med. 200, 211-222 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 211-222
    • Stavrovskaya, I.G.1
  • 40
    • 0032107326 scopus 로고    scopus 로고
    • Assessment of the efcacy of treatment with pimozide in patients with amyotrophic lateral sclerosis. Introductory notes
    • Szczudlik, A., Tomik, B., Słowik, A. & Kasprzyk, K. Assessment of the efcacy of treatment with pimozide in patients with amyotrophic lateral sclerosis. Introductory notes. Neurol. Neurochir. Pol. 32, 821-829 (1998).
    • (1998) Neurol. Neurochir. Pol. , vol.32 , pp. 821-829
    • Szczudlik, A.1    Tomik, B.2    Słowik, A.3    Kasprzyk, K.4
  • 41
    • 84874607780 scopus 로고    scopus 로고
    • Translation of HTT mRNA with expanded CAG repeats is regulated by the MID1-PP2A protein complex
    • Krauss, S. et al. Translation of HTT mRNA with expanded CAG repeats is regulated by the MID1-PP2A protein complex. Nat. Commun. 4, 1511 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1511
    • Krauss, S.1
  • 42
    • 77955359169 scopus 로고    scopus 로고
    • Quantitative relationships between Huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis
    • Miller, J. et al. Quantitative relationships between Huntingtin levels, polyglutamine length, inclusion body formation, and neuronal death provide novel insight into huntington's disease molecular pathogenesis. J. Neurosci. 30, 10541-10550 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 10541-10550
    • Miller, J.1
  • 43
    • 78149324557 scopus 로고    scopus 로고
    • Bridging the Valley of Death of therapeutics for neurodegeneration
    • Finkbeiner, S. Bridging the Valley of Death of therapeutics for neurodegeneration. Nat. Med. 16, 1227-1232 (2010).
    • (2010) Nat. Med. , vol.16 , pp. 1227-1232
    • Finkbeiner, S.1
  • 44
    • 79958260092 scopus 로고    scopus 로고
    • Te Human brain in a dish: The promise of iPSC-derived neurons
    • Dolmetsch, R. & Geschwind, D.H. Te 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
  • 45
    • 66149091121 scopus 로고    scopus 로고
    • Astrocytic protection of spinal motor neurons but not cortical neurons against loss of Als2/alsin function
    • Jacquier, A., Bellouze, S., Blanchard, S., Bohl, D. & Haase, G. Astrocytic protection of spinal motor neurons but not cortical neurons against loss of Als2/alsin function. Hum. Mol. Genet. 18, 2127-2139 (2009).
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2127-2139
    • Jacquier, A.1    Bellouze, S.2    Blanchard, S.3    Bohl, D.4    Haase, G.5
  • 46
    • 80052783545 scopus 로고    scopus 로고
    • Astrocytes from familial and sporadic ALS patients are toxic to motor neurons
    • Haidet-Phillips, A.M. et al. Astrocytes from familial and sporadic ALS patients are toxic to motor neurons. Nat. Biotechnol. 29, 824-828 (2011).
    • (2011) Nat. Biotechnol. , vol.29 , pp. 824-828
    • Haidet-Phillips, A.M.1
  • 47
    • 58149234447 scopus 로고    scopus 로고
    • Aggregates assembled from overexpression of wild-type α-synuclein are not toxic to human neuronal cells
    • Ko, L.-W., Ko, H.-H.C., Lin, W.-L., Kulathingal, J.G. & Yen, S.-H.C. Aggregates assembled from overexpression of wild-type α-synuclein are not toxic to human neuronal cells. J. Neuropathol. Exp. Neurol. 67, 1084-1096 (2008).
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 1084-1096
    • Ko, L.-W.1    Ko, H.-H.C.2    Lin, W.-L.3    Kulathingal, J.G.4    Yen, S.-H.C.5
  • 48
    • 0034213718 scopus 로고    scopus 로고
    • High-level neuronal expression of aβ 1-42 in wild-type human amyloid protein precursor transgenic mice: Synaptotoxicity without plaque formation
    • Mucke, L. et al. High-level neuronal expression of aβ 1-42 in wild-type human amyloid protein precursor transgenic mice: synaptotoxicity without plaque formation. J. Neurosci. 20, 4050-4058 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 4050-4058
    • Mucke, L.1
  • 49
    • 84883204078 scopus 로고    scopus 로고
    • Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration
    • Tsvetkov, A.S. et al. Proteostasis of polyglutamine varies among neurons and predicts neurodegeneration. Nat. Chem. Biol. 9, 586-592 (2013).
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 586-592
    • Tsvetkov, A.S.1
  • 50
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou, F., Finkbeiner, S., Devys, D. & Greenberg, M.E. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95, 55-66 (1998).
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4


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