메뉴 건너뛰기




Volumn , Issue , 2015, Pages 63-78

Dual role of autophagy in neurodegenerative diseases: The case of amyotrophic lateral sclerosis

Author keywords

Aggregation; ALS; Apamycin; Autophagy; Beclin 1; MTOR; Neurodegenerative disease

Indexed keywords


EID: 84943764562     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-3-319-13939-5_4     Document Type: Chapter
Times cited : (3)

References (103)
  • 1
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz C, Mollereau B. Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat Rev Neurosci. 2014;15(4):233-49.
    • (2014) Nat Rev Neurosci , vol.15 , Issue.4 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 2
    • 79954425809 scopus 로고    scopus 로고
    • Protein folding stress in neurodegenerative diseases: A glimpse into the ER
    • Matus S, Glimcher LH, Hetz C. Protein folding stress in neurodegenerative diseases: a glimpse into the ER. Curr Opin Cell Biol. 2011;23(2):239-52.
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 239-252
    • Matus, S.1    Glimcher, L.H.2    Hetz, C.3
  • 3
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C. Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci. 2003;4(1):49-60.
    • (2003) Nat Rev Neurosci , vol.4 , Issue.1 , pp. 49-60
    • Soto, C.1
  • 5
    • 84884634690 scopus 로고    scopus 로고
    • Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: Autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers
    • Sarkar S. Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers. Biochem Soc Trans. 2013;41(5):1103-30.
    • (2013) Biochem Soc Trans , vol.41 , Issue.5 , pp. 1103-1130
    • Sarkar, S.1
  • 6
    • 57649227693 scopus 로고    scopus 로고
    • Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies
    • Sarkar S, Ravikumar B, Floto RA, Rubinsztein DC. Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ. 2009;16(1):46-56.
    • (2009) Cell Death Differ , vol.16 , Issue.1 , pp. 46-56
    • Sarkar, S.1    Ravikumar, B.2    Floto, R.A.3    Rubinsztein, D.C.4
  • 7
    • 84874529071 scopus 로고    scopus 로고
    • mTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy
    • Ching JK, Elizabeth SV, Ju JS, Lusk C, Pittman SK, Weihl CC. mTOR dysfunction contributes to vacuolar pathology and weakness in valosin-containing protein associated inclusion body myopathy. Hum Mol Genet. 2013;22(6):1167-79.
    • (2013) Hum Mol Genet , vol.22 , Issue.6 , pp. 1167-1179
    • Ching, J.K.1    Elizabeth, S.V.2    Ju, J.S.3    Lusk, C.4    Pittman, S.K.5    Weihl, C.C.6
  • 8
    • 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 IF, Guo BS, Liu YC, Wu CC, Yang CH, Tsai KJ, 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 U S A. 2012;109(37):15024-9.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.37 , pp. 15024-15029
    • Wang, I.F.1    Guo, B.S.2    Liu, Y.C.3    Wu, C.C.4    Yang, C.H.5    Tsai, K.J.6
  • 9
    • 79953647105 scopus 로고    scopus 로고
    • Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis
    • Zhang X, Li L, Chen S, Yang D, Wang Y, Wang Z, et al. Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Autophagy. 2011;7(4):412-25.
    • (2011) Autophagy , vol.7 , Issue.4 , pp. 412-425
    • Zhang, X.1    Li, L.2    Chen, S.3    Yang, D.4    Wang, Y.5    Wang, Z.6
  • 10
    • 84884294596 scopus 로고    scopus 로고
    • Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons
    • Castillo K, Nassif M, Valenzuela V, Rojas F, Matus S, Mercado G, et al. Trehalose delays the progression of amyotrophic lateral sclerosis by enhancing autophagy in motoneurons. Autophagy. 2013;9(9):1308-20.
    • (2013) Autophagy , vol.9 , Issue.9 , pp. 1308-1320
    • Castillo, K.1    Nassif, M.2    Valenzuela, V.3    Rojas, F.4    Matus, S.5    Mercado, G.6
  • 11
    • 84898465382 scopus 로고    scopus 로고
    • MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis
    • Zhang X, Chen S, Song L, Tang Y, Shen Y, Jia L, et al. MTOR-independent, autophagic enhancer trehalose prolongs motor neuron survival and ameliorates the autophagic flux defect in a mouse model of amyotrophic lateral sclerosis. Autophagy. 2014;10(4):588-602.
    • (2014) Autophagy , vol.10 , Issue.4 , pp. 588-602
    • Zhang, X.1    Chen, S.2    Song, L.3    Tang, Y.4    Shen, Y.5    Jia, L.6
  • 12
    • 84904729990 scopus 로고    scopus 로고
    • Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models
    • Barmada SJ, Serio A, Arjun A, Bilican B, Daub A, Ando DM, et al. Autophagy induction enhances TDP43 turnover and survival in neuronal ALS models. Nat Chem Biol. 2014;10(8):677-85.
    • (2014) Nat Chem Biol , vol.10 , Issue.8 , pp. 677-685
    • Barmada, S.J.1    Serio, A.2    Arjun, A.3    Bilican, B.4    Daub, A.5    Ando, D.M.6
  • 13
    • 79954417611 scopus 로고    scopus 로고
    • Autophagy for tissue homeostasis and neuroprotection
    • Marino G, Madeo F, Kroemer G. Autophagy for tissue homeostasis and neuroprotection. Curr Opin Cell Biol. 2011;23(2):198-206.
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.2 , pp. 198-206
    • Marino, G.1    Madeo, F.2    Kroemer, G.3
  • 14
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • Hetz C, Thielen P, Matus S, Nassif M, Court F, Kiffin R, et al. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 2009;23(19):2294-306.
    • (2009) Genes Dev , vol.23 , Issue.19 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3    Nassif, M.4    Court, F.5    Kiffin, R.6
  • 15
    • 84898463603 scopus 로고    scopus 로고
    • Pathogenic role of BECN1/Beclin 1 in the development of amyotrophic lateral sclerosis
    • Nassif M, Valenzuela V, Rojas-Rivera D, Vidal R, Matus S, Castillo K, et al. Pathogenic role of BECN1/Beclin 1 in the development of amyotrophic lateral sclerosis. Autophagy. 2014;10(7):1256-71.
    • (2014) Autophagy , vol.10 , Issue.7 , pp. 1256-1271
    • Nassif, M.1    Valenzuela, V.2    Rojas-Rivera, D.3    Vidal, R.4    Matus, S.5    Castillo, K.6
  • 16
    • 0020391968 scopus 로고
    • Clinical limits of amyotrophic lateral sclerosis
    • Mulder DW. Clinical limits of amyotrophic lateral sclerosis. Adv Neurol. 1982;36:15-22.
    • (1982) Adv Neurol , vol.36 , pp. 15-22
    • Mulder, D.W.1
  • 17
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • Pasinelli P, Brown RH. Molecular biology of amyotrophic lateral sclerosis: insights from genetics. Nat Rev Neurosci. 2006;7(9):710-23.
    • (2006) Nat Rev Neurosci , vol.7 , Issue.9 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 18
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Rowland LP, Shneider NA. Amyotrophic lateral sclerosis. N Engl J Med. 2001;344(22):1688-700.
    • (2001) N Engl J Med , vol.344 , Issue.22 , pp. 1688-1700
    • Rowland, L.P.1    Shneider, N.A.2
  • 19
    • 80054832080 scopus 로고    scopus 로고
    • Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS
    • DeJesus-Hernandez M, Mackenzie IR, Boeve BF, Boxer AL, Baker M, Rutherford NJ, et al. Expanded GGGGCC hexanucleotide repeat in noncoding region of C9ORF72 causes chromosome 9p-linked FTD and ALS. Neuron. 2011;72(2):245-56.
    • (2011) Neuron , vol.72 , Issue.2 , pp. 245-256
    • DeJesus-Hernandez, M.1    Mackenzie, I.R.2    Boeve, B.F.3    Boxer, A.L.4    Baker, M.5    Rutherford, N.J.6
  • 20
    • 80054837386 scopus 로고    scopus 로고
    • A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD
    • Renton AE, Majounie E, Waite A, Simon-Sanchez J, Rollinson S, Gibbs JR, et al. A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD. Neuron. 2011;72(2):257-68.
    • (2011) Neuron , vol.72 , Issue.2 , pp. 257-268
    • Renton, A.E.1    Majounie, E.2    Waite, A.3    Simon-Sanchez, J.4    Rollinson, S.5    Gibbs, J.R.6
  • 21
    • 80755133370 scopus 로고    scopus 로고
    • Clinical genetics of amyotrophic lateral sclerosis: What do we really know
    • Andersen PM, Al-Chalabi A. Clinical genetics of amyotrophic lateral sclerosis: what do we really know Nat Rev Neurol. 2011;7(11):603-15.
    • (2011) Nat Rev Neurol , vol.7 , Issue.11 , pp. 603-615
    • Andersen, P.M.1    Al-Chalabi, A.2
  • 22
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, Truax AC, Micsenyi MC, Chou TT, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science. 2006;314(5796):130-3.
    • (2006) Science , vol.314 , Issue.5796 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.C.4    Micsenyi, M.C.5    Chou, T.T.6
  • 23
    • 0002815190 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Brown RHJ, Meininger K, Swash M, Editors, London: Martin Dunitz;
    • Ince PG. Amyotrophic lateral sclerosis. In: Brown RHJ, Meininger K, Swash M, Editors. Neuropathology. London: Martin Dunitz; 2000. pp. 83-112.
    • (2000) Neuropathology , pp. 83-112
    • Ince, P.G.1
  • 24
    • 0025868659 scopus 로고
    • Reactive astrogliosis is widespread in the subcortical white matter of amyotrophic lateral sclerosis brain
    • Kushner PD, Stephenson DT, Wright S. Reactive astrogliosis is widespread in the subcortical white matter of amyotrophic lateral sclerosis brain. J Neuropathol Exp Neurol. 1991;50(3):263-77.
    • (1991) J Neuropathol Exp Neurol , vol.50 , Issue.3 , pp. 263-277
    • Kushner, P.D.1    Stephenson, D.T.2    Wright, S.3
  • 25
    • 0026005516 scopus 로고
    • A unique pattern of astrocytosis in the primary motor area in amyotrophic lateral sclerosis
    • Murayama S, Inoue K, Kawakami H, Bouldin TW, Suzuki K. A unique pattern of astrocytosis in the primary motor area in amyotrophic lateral sclerosis. Acta Neuropathol. 1991;82(6):456-61.
    • (1991) Acta Neuropathol , vol.82 , Issue.6 , pp. 456-461
    • Murayama, S.1    Inoue, K.2    Kawakami, H.3    Bouldin, T.W.4    Suzuki, K.5
  • 26
    • 0028264346 scopus 로고
    • Reactive astrocytes are widespread in the cortical gray matter of amyotrophic lateral sclerosis
    • Nagy D, Kato T, Kushner PD. Reactive astrocytes are widespread in the cortical gray matter of amyotrophic lateral sclerosis. J Neurosci Res. 1994;38(3):336-47.
    • (1994) J Neurosci Res , vol.38 , Issue.3 , pp. 336-347
    • Nagy, D.1    Kato, T.2    Kushner, P.D.3
  • 28
    • 42249102078 scopus 로고    scopus 로고
    • Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS
    • Turner BJ, Talbot K. Transgenics, toxicity and therapeutics in rodent models of mutant SOD1-mediated familial ALS. Prog Neurobiol. 2008;85(1):94-134.
    • (2008) Prog Neurobiol , vol.85 , Issue.1 , pp. 94-134
    • Turner, B.J.1    Talbot, K.2
  • 29
    • 0028097839 scopus 로고
    • A controlled trial of riluzole in amyotrophic lateral sclerosis. ALS/Riluzole Study Group
    • Bensimon G, Lacomblez L, Meininger V. A controlled trial of riluzole in amyotrophic lateral sclerosis. ALS/Riluzole Study Group. N Engl J Med. 1994;330(9):585-91.
    • (1994) N Engl J Med , vol.330 , Issue.9 , pp. 585-591
    • Bensimon, G.1    Lacomblez, L.2    Meininger, V.3
  • 30
    • 0442323561 scopus 로고    scopus 로고
    • Autophagy: In sickness and in health
    • Cuervo AM. Autophagy: in sickness and in health. Trends Cell Biol. 2004;14(2):70-7.
    • (2004) Trends Cell Biol , vol.14 , Issue.2 , pp. 70-77
    • Cuervo, A.M.1
  • 31
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: Unanswered questions
    • Klionsky DJ. The molecular machinery of autophagy: unanswered questions. J Cell Sci. 2005;118(Pt 1):7-18.
    • (2005) J Cell Sci , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 32
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ. Autophagy fights disease through cellular self-digestion. Nature. 2008;451(7182):1069-75.
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 33
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C, Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet. 2009;43:67-93.
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 34
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • He C, Levine B. The Beclin 1 interactome. Curr Opin Cell Biol. 2010;22(2):140-9.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 140-149
    • He, C.1    Levine, B.2
  • 35
    • 0035032723 scopus 로고    scopus 로고
    • Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
    • Kihara A, Kabeya Y, Ohsumi Y, Yoshimori T. Beclin-phosphatidylinositol 3-kinase complex functions at the trans-Golgi network. EMBO Rep. 2001;2(4):330-5.
    • (2001) EMBO Rep , vol.2 , Issue.4 , pp. 330-335
    • Kihara, A.1    Kabeya, Y.2    Ohsumi, Y.3    Yoshimori, T.4
  • 36
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, Mizushima N, et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell. 2005;122(6):927-39.
    • (2005) Cell , vol.122 , Issue.6 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3    Garuti, R.4    Liang, X.H.5    Mizushima, N.6
  • 37
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • Maiuri MC, Zalckvar E, Kimchi A, Kroemer G. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol. 2007;8(9):741-52.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.9 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 39
    • 84875753542 scopus 로고    scopus 로고
    • Chemical screening platforms for autophagy drug discovery to identify therapeutic candidates for Huntington’s disease and other neurodegenerative disorders
    • Sarkar S. Chemical screening platforms for autophagy drug discovery to identify therapeutic candidates for Huntington’s disease and other neurodegenerative disorders. Drug Discover Today Technol. 2013;10(1):e137-44.
    • (2013) Drug Discover Today Technol , vol.10 , Issue.1 , pp. e137-e144
    • Sarkar, S.1
  • 40
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTORindependent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S, Davies JE, Huang Z, Tunnacliffe A, Rubinsztein DC. Trehalose, a novel mTORindependent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem. 2007;282(8):5641-52.
    • (2007) J Biol Chem , vol.282 , Issue.8 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 41
    • 42249106042 scopus 로고    scopus 로고
    • Novel targets for Huntington’s disease in an mTOR-independent autophagy pathway
    • Williams A, Sarkar S, Cuddon P, Ttofi EK, Saiki S, Siddiqi FH, et al. Novel targets for Huntington’s disease in an mTOR-independent autophagy pathway. Nat Chem Biol. 2008;4(5):295-305.
    • (2008) Nat Chem Biol , vol.4 , Issue.5 , pp. 295-305
    • Williams, A.1    Sarkar, S.2    Cuddon, P.3    Ttofi, E.K.4    Saiki, S.5    Siddiqi, F.H.6
  • 42
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer G, Marino G, Levine B. Autophagy and the integrated stress response. Mol Cell. 2010;40(2):280-93.
    • (2010) Mol Cell , vol.40 , Issue.2 , pp. 280-293
    • Kroemer, G.1    Marino, G.2    Levine, B.3
  • 44
    • 33845459165 scopus 로고    scopus 로고
    • Autophagy is activated for cell survival after endoplasmic reticulum stress
    • Ogata M, Hino S, Saito A, Morikawa K, Kondo S, Kanemoto S, et al. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol. 2006;26(24):9220-31.
    • (2006) Mol Cell Biol , vol.26 , Issue.24 , pp. 9220-9231
    • Ogata, M.1    Hino, S.2    Saito, A.3    Morikawa, K.4    Kondo, S.5    Kanemoto, S.6
  • 45
    • 80455173839 scopus 로고    scopus 로고
    • BAX inhibitor-1 regulates autophagy by controlling the IRE1alpha branch of the unfolded protein response
    • Castillo K, Rojas-Rivera D, Lisbona F, Caballero B, Nassif M, Court FA, et al. BAX inhibitor-1 regulates autophagy by controlling the IRE1alpha branch of the unfolded protein response. EMBO J. 2011;30(21):4465-78.
    • (2011) EMBO J , vol.30 , Issue.21 , pp. 4465-4478
    • Castillo, K.1    Rojas-Rivera, D.2    Lisbona, F.3    Caballero, B.4    Nassif, M.5    Court, F.A.6
  • 46
    • 84876410429 scopus 로고    scopus 로고
    • Unspliced XBP1 controls autophagy through FoxO1
    • Vidal RL, Hetz C. Unspliced XBP1 controls autophagy through FoxO1. Cell Res. 2013;23(4):463-4.
    • (2013) Cell Res , vol.23 , Issue.4 , pp. 463-464
    • Vidal, R.L.1    Hetz, C.2
  • 47
    • 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. 2006;441(7095):885-9.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 48
    • 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. 2006;441(7095):880-4.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 49
    • 79953665568 scopus 로고    scopus 로고
    • Targeting autophagy in ALS: A complex mission
    • Nassif M, Hetz C. Targeting autophagy in ALS: a complex mission. Autophagy. 2011;7(4):450-3.
    • (2011) Autophagy , vol.7 , Issue.4 , pp. 450-453
    • Nassif, M.1    Hetz, C.2
  • 50
    • 82755161734 scopus 로고    scopus 로고
    • Autophagy and disease: Always two sides to a problem
    • Sridhar S, Botbol Y, Macian F, Cuervo AM. Autophagy and disease: always two sides to a problem. J Pathol. 2012;226(2):255-73.
    • (2012) J Pathol , vol.226 , Issue.2 , pp. 255-273
    • Sridhar, S.1    Botbol, Y.2    Macian, F.3    Cuervo, A.M.4
  • 51
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong E, Cuervo AM. Autophagy gone awry in neurodegenerative diseases. Nat Neurosci. 2010;13(7):805-11.
    • (2010) Nat Neurosci , vol.13 , Issue.7 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 52
    • 36549041882 scopus 로고    scopus 로고
    • Focal cerebral ischemia induces upregulation of Beclin 1 and autophagy-like cell death
    • Rami A, Langhagen A, Steiger S. Focal cerebral ischemia induces upregulation of Beclin 1 and autophagy-like cell death. Neurobiol Dis. 2008;29(1):132-41.
    • (2008) Neurobiol Dis , vol.29 , Issue.1 , pp. 132-141
    • Rami, A.1    Langhagen, A.2    Steiger, S.3
  • 53
    • 84862547657 scopus 로고    scopus 로고
    • The regulation of N-terminal Huntingtin (Htt552) accumulation by Beclin1
    • Wu JC, Qi L, Wang Y, Kegel KB, Yoder J, Difiglia M, et al. The regulation of N-terminal Huntingtin (Htt552) accumulation by Beclin1. Acta Pharmacol Sin. 2012;33(6):743-51.
    • (2012) Acta Pharmacol Sin , vol.33 , Issue.6 , pp. 743-751
    • Wu, J.C.1    Qi, L.2    Wang, Y.3    Kegel, K.B.4    Yoder, J.5    Difiglia, M.6
  • 54
    • 22244491605 scopus 로고    scopus 로고
    • Closed head injury induces upregulation of Beclin 1 at the cortical site of injury
    • Diskin T, Tal-Or P, Erlich S, Mizrachy L, Alexandrovich A, Shohami E, et al. Closed head injury induces upregulation of Beclin 1 at the cortical site of injury. J Neurotrauma. 2005;22(7):750-62.
    • (2005) J Neurotrauma , vol.22 , Issue.7 , pp. 750-762
    • Diskin, T.1    Tal-Or, P.2    Erlich, S.3    Mizrachy, L.4    Alexandrovich, A.5    Shohami, E.6
  • 55
    • 84856189081 scopus 로고    scopus 로고
    • Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways
    • Wills J, Credle J, Oaks AW, Duka V, Lee JH, Jones J, et al. Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways. PLoS ONE. 2012;7(1):e30745.
    • (2012) PLoS ONE , vol.7 , Issue.1 , pp. e30745
    • Wills, J.1    Credle, J.2    Oaks, A.W.3    Duka, V.4    Lee, J.H.5    Jones, J.6
  • 56
    • 34548068588 scopus 로고    scopus 로고
    • Lipid trafficking defects increase Beclin-1 and activate autophagy in Niemann-Pick type C disease
    • Pacheco CD, Lieberman AP. Lipid trafficking defects increase Beclin-1 and activate autophagy in Niemann-Pick type C disease. Autophagy. 2007;3(5):487-9.
    • (2007) Autophagy , vol.3 , Issue.5 , pp. 487-489
    • Pacheco, C.D.1    Lieberman, A.P.2
  • 58
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature. 2004;431(7010):805-10.
    • (2004) Nature , vol.431 , Issue.7010 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 59
    • 84866481222 scopus 로고    scopus 로고
    • Cellular toxicity of mutant SOD1 protein is linked to an easily soluble, non-aggregated form in vitro
    • Brotherton TE, Li Y, Glass JD. Cellular toxicity of mutant SOD1 protein is linked to an easily soluble, non-aggregated form in vitro. Neurobiol Dis. 2013;49:c49-56.
    • (2013) Neurobiol Dis , vol.49 , pp. c49-c56
    • Brotherton, T.E.1    Li, Y.2    Glass, J.D.3
  • 60
    • 33744916798 scopus 로고    scopus 로고
    • Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1
    • Shibata M, Lu T, Furuya T, Degterev A, Mizushima N, Yoshimori T, et al. Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1. J Biol Chem. 2006;281(20):14474-85.
    • (2006) J Biol Chem , vol.281 , Issue.20 , pp. 14474-14485
    • Shibata, M.1    Lu, T.2    Furuya, T.3    Degterev, A.4    Mizushima, N.5    Yoshimori, T.6
  • 61
    • 80052580969 scopus 로고    scopus 로고
    • Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset alS and ALS/dementia
    • Deng HX, Chen W, Hong ST, Boycott KM, Gorrie GH, Siddique N, et al. Mutations in UBQLN2 cause dominant X-linked juvenile and adult-onset alS and ALS/dementia. Nature. 2011;477(7363):211-5.
    • (2011) Nature , vol.477 , Issue.7363 , pp. 211-215
    • Deng, H.X.1    Chen, W.2    Hong, S.T.3    Boycott, K.M.4    Gorrie, G.H.5    Siddique, N.6
  • 62
    • 84872676800 scopus 로고    scopus 로고
    • Ubiquilin 2 mutations in Italian patients with amyotrophic lateral sclerosis and frontotemporal dementia
    • Gellera C, Tiloca C, Del Bo R, Corrado L, Pensato V, Agostini J, et al. Ubiquilin 2 mutations in Italian patients with amyotrophic lateral sclerosis and frontotemporal dementia. J Neurol Neurosurg Psychiatry. 2013;84(2):183-7.
    • (2013) J Neurol Neurosurg Psychiatry , vol.84 , Issue.2 , pp. 183-187
    • Gellera, C.1    Tiloca, C.2    Del Bo, R.3    Corrado, L.4    Pensato, V.5    Agostini, J.6
  • 63
    • 84864380051 scopus 로고    scopus 로고
    • UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis
    • Williams KL, Warraich ST, Yang S, Solski JA, Fernando R, Rouleau GA, et al. UBQLN2/ubiquilin 2 mutation and pathology in familial amyotrophic lateral sclerosis. Neurobiol Aging. 2012;33(10):2527 e3-10.
    • (2012) Neurobiol Aging , vol.33 , Issue.10 , pp. 2527.e3-2527.e10
    • Williams, K.L.1    Warraich, S.T.2    Yang, S.3    Solski, J.A.4    Fernando, R.5    Rouleau, G.A.6
  • 64
    • 80855150639 scopus 로고    scopus 로고
    • SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Fecto F, Yan J, Vemula SP, Liu E, Yang Y, Chen W, et al. SQSTM1 mutations in familial and sporadic amyotrophic lateral sclerosis. Arch Neurol. 2011;68(11):1440-6.
    • (2011) Arch Neurol , vol.68 , Issue.11 , pp. 1440-1446
    • Fecto, F.1    Yan, J.2    Vemula, S.P.3    Liu, E.4    Yang, Y.5    Chen, W.6
  • 65
    • 84867543551 scopus 로고    scopus 로고
    • SQSTM1 mutations in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Rubino E, Rainero I, Chio A, Rogaeva E, Galimberti D, Fenoglio P, et al. SQSTM1 mutations in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Neurology. 2012;79(15):1556-62.
    • (2012) Neurology , vol.79 , Issue.15 , pp. 1556-1562
    • Rubino, E.1    Rainero, I.2    Chio, A.3    Rogaeva, E.4    Galimberti, D.5    Fenoglio, P.6
  • 66
    • 84876533723 scopus 로고    scopus 로고
    • Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: Genetics and neuropathology
    • Teyssou E, Takeda T, Lebon V, Boillee S, Doukoure B, Bataillon G, et al. Mutations in SQSTM1 encoding p62 in amyotrophic lateral sclerosis: genetics and neuropathology. Acta Neuropathol. 2013;125(4):511-22.
    • (2013) Acta Neuropathol , vol.125 , Issue.4 , pp. 511-522
    • Teyssou, E.1    Takeda, T.2    Lebon, V.3    Boillee, S.4    Doukoure, B.5    Bataillon, G.6
  • 67
    • 80053629733 scopus 로고    scopus 로고
    • Novel optineurin mutations in patients with familial and sporadic amyotrophic lateral sclerosis
    • Del Bo R, Tiloca C, Pensato V, Corrado L, Ratti A, Ticozzi N, et al. Novel optineurin mutations in patients with familial and sporadic amyotrophic lateral sclerosis. J Neurol Neurosurg Psychiatry. 2011;82(11):1239-43.
    • (2011) J Neurol Neurosurg Psychiatry , vol.82 , Issue.11 , pp. 1239-1243
    • Del Bo, R.1    Tiloca, C.2    Pensato, V.3    Corrado, L.4    Ratti, A.5    Ticozzi, N.6
  • 69
    • 77952419246 scopus 로고    scopus 로고
    • Mutations of optineurin in amyotrophic lateral sclerosis
    • Maruyama H, Morino H, Ito H, Izumi Y, Kato H, Watanabe Y, et al. Mutations of optineurin in amyotrophic lateral sclerosis. Nature. 2010;465(7295):223-6.
    • (2010) Nature , vol.465 , Issue.7295 , pp. 223-226
    • Maruyama, H.1    Morino, H.2    Ito, H.3    Izumi, Y.4    Kato, H.5    Watanabe, Y.6
  • 72
    • 77956392186 scopus 로고    scopus 로고
    • Mutations in CHMP2B in lower motor neuron predominant amyotrophic lateral sclerosis (ALS)
    • Cox LE, Ferraiuolo L, Goodall EF, Heath PR, Higginbottom A, Mortiboys H, et al. Mutations in CHMP2B in lower motor neuron predominant amyotrophic lateral sclerosis (ALS). PLoS ONE. 2010;5(3):e9872.
    • (2010) PLoS ONE , vol.5 , Issue.3 , pp. e9872
    • Cox, L.E.1    Ferraiuolo, L.2    Goodall, E.F.3    Heath, P.R.4    Higginbottom, A.5    Mortiboys, H.6
  • 73
    • 33749006845 scopus 로고    scopus 로고
    • ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B)
    • Parkinson N, Ince PG, Smith MO, Highley R, Skibinski G, Andersen PM, et al. ALS phenotypes with mutations in CHMP2B (charged multivesicular body protein 2B). Neurology. 2006;67(6):1074-7.
    • (2006) Neurology , vol.67 , Issue.6 , pp. 1074-1077
    • Parkinson, N.1    Ince, P.G.2    Smith, M.O.3    Highley, R.4    Skibinski, G.5    Andersen, P.M.6
  • 75
    • 70350131893 scopus 로고    scopus 로고
    • Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism
    • Gal J, Strom AL, Kwinter DM, Kilty R, Zhang J, Shi P, et al. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism. J Neurochem. 2009;111(4):1062-73.
    • (2009) J Neurochem , vol.111 , Issue.4 , pp. 1062-1073
    • Gal, J.1    Strom, A.L.2    Kwinter, D.M.3    Kilty, R.4    Zhang, J.5    Shi, P.6
  • 76
    • 78650680776 scopus 로고    scopus 로고
    • Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1
    • Brady OA, Meng P, Zheng Y, Mao Y, Hu F. Regulation of TDP-43 aggregation by phosphorylation and p62/SQSTM1. J Neurochem. 2011;116(2):248-59.
    • (2011) J Neurochem , vol.116 , Issue.2 , pp. 248-259
    • Brady, O.A.1    Meng, P.2    Zheng, Y.3    Mao, Y.4    Hu, F.5
  • 77
    • 79960804104 scopus 로고    scopus 로고
    • Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth
    • Wild P, Farhan H, McEwan DG, Wagner S, Rogov VV, Brady NR, et al. Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science. 2011;333(6039):228-33.
    • (2011) Science , vol.333 , Issue.6039 , pp. 228-233
    • Wild, P.1    Farhan, H.2    McEwan, D.G.3    Wagner, S.4    Rogov, V.V.5    Brady, N.R.6
  • 78
    • 84907059487 scopus 로고    scopus 로고
    • The VCP/p97 system at a glance: Connecting cellular function to disease pathogenesis
    • Meyer H, Weihl CC. The VCP/p97 system at a glance: connecting cellular function to disease pathogenesis. J Cell Sci. 2014;127:3877-83.
    • (2014) J Cell Sci , vol.127 , pp. 3877-3883
    • Meyer, H.1    Weihl, C.C.2
  • 79
    • 74049124412 scopus 로고    scopus 로고
    • Valosincontaining protein (VCP) is required for autophagy and is disrupted in VCP disease
    • Ju JS, Fuentealba RA, Miller SE, Jackson E, Piwnica-Worms D, Baloh RH, et al. Valosincontaining protein (VCP) is required for autophagy and is disrupted in VCP disease. J Cell Biol. 2009;187(6):875-88.
    • (2009) J Cell Biol , vol.187 , Issue.6 , pp. 875-888
    • Ju, J.S.1    Fuentealba, R.A.2    Miller, S.E.3    Jackson, E.4    Piwnica-Worms, D.5    Baloh, R.H.6
  • 80
    • 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, Mehta SG, Mumm S, Darvish D, 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(4):377-81.
    • (2004) Nat Genet , vol.36 , Issue.4 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3    Mehta, S.G.4    Mumm, S.5    Darvish, D.6
  • 81
    • 63649086486 scopus 로고    scopus 로고
    • The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins
    • Raiborg C, Stenmark H. The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins. Nature. 2009;458(7237):445-52.
    • (2009) Nature , vol.458 , Issue.7237 , pp. 445-452
    • Raiborg, C.1    Stenmark, H.2
  • 82
    • 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. 2010;19(11):2228-38.
    • (2010) Hum Mol Genet , vol.19 , Issue.11 , pp. 2228-2238
    • Urwin, H.1    Authier, A.2    Nielsen, J.E.3    Metcalf, D.4    Powell, C.5    Froud, K.6
  • 83
    • 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. 2008;17(2):313-22.
    • (2008) Hum Mol Genet , vol.17 , Issue.2 , pp. 313-322
    • van der Zee, J.1    Urwin, H.2    Engelborghs, S.3    Bruyland, M.4    Vandenberghe, R.5    Dermaut, B.6
  • 85
    • 84857568926 scopus 로고    scopus 로고
    • Progressive neuronal inclusion formation and axonal degeneration in CHMP2B mutant transgenic mice
    • Ghazi-Noori S, Froud KE, Mizielinska S, Powell C, Smidak M, Fernandez de Marco M, et al. Progressive neuronal inclusion formation and axonal degeneration in CHMP2B mutant transgenic mice. Brain. 2012;135(Pt 3):819-32.
    • (2012) Brain , vol.135 , pp. 819-832
    • Ghazi-Noori, S.1    Froud, K.E.2    Mizielinska, S.3    Powell, C.4    Smidak, M.5    Fernandez de Marco, M.6
  • 86
    • 84892802771 scopus 로고    scopus 로고
    • ALS-associated protein FIG4 is localized in Pick and Lewy bodies, and also neuronal nuclear inclusions, in polyglutamine and intranuclear inclusion body diseases
    • Kon T, Mori F, Tanji K, Miki Y, Toyoshima Y, Yoshida M, et al. ALS-associated protein FIG4 is localized in Pick and Lewy bodies, and also neuronal nuclear inclusions, in polyglutamine and intranuclear inclusion body diseases. Neuropathology. 2014;34(1):19-26.
    • (2014) Neuropathology , vol.34 , Issue.1 , pp. 19-26
    • Kon, T.1    Mori, F.2    Tanji, K.3    Miki, Y.4    Toyoshima, Y.5    Yoshida, M.6
  • 87
    • 34447133038 scopus 로고    scopus 로고
    • Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J
    • Chow CY, Zhang Y, Dowling JJ, Jin N, Adamska M, Shiga K, et al. Mutation of FIG4 causes neurodegeneration in the pale tremor mouse and patients with CMT4J. Nature. 2007;448(7149):68-72.
    • (2007) Nature , vol.448 , Issue.7149 , pp. 68-72
    • Chow, C.Y.1    Zhang, Y.2    Dowling, J.J.3    Jin, N.4    Adamska, M.5    Shiga, K.6
  • 88
    • 49449098975 scopus 로고    scopus 로고
    • Mutation of FIG4 causes a rapidly progressive, asymmetric neuronal degeneration
    • Zhang X, Chow CY, Sahenk Z, Shy ME, Meisler MH, Li J. Mutation of FIG4 causes a rapidly progressive, asymmetric neuronal degeneration. Brain. 2008;131(Pt 8):1990-2001.
    • (2008) Brain , vol.131 , pp. 1990-2001
    • Zhang, X.1    Chow, C.Y.2    Sahenk, Z.3    Shy, M.E.4    Meisler, M.H.5    Li, J.6
  • 89
    • 78650448754 scopus 로고    scopus 로고
    • Chemical modulators of autophagy as biological probes and potential therapeutics
    • Fleming A, Noda T, Yoshimori T, Rubinsztein DC. Chemical modulators of autophagy as biological probes and potential therapeutics. Nat Chem Biol. 2011;7(1):9-17.
    • (2011) Nat Chem Biol , vol.7 , Issue.1 , pp. 9-17
    • Fleming, A.1    Noda, T.2    Yoshimori, T.3    Rubinsztein, D.C.4
  • 90
    • 84866122688 scopus 로고    scopus 로고
    • Autophagy modulation as a potential therapeutic target for diverse diseases
    • Rubinsztein DC, Codogno P, Levine B. Autophagy modulation as a potential therapeutic target for diverse diseases. Nat Rev Drug Discov. 2012;11(9):709-30.
    • (2012) Nat Rev Drug Discov , vol.11 , Issue.9 , pp. 709-730
    • Rubinsztein, D.C.1    Codogno, P.2    Levine, B.3
  • 91
    • 2642586352 scopus 로고    scopus 로고
    • Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
    • Ravikumar B, Vacher C, Berger Z, Davies JE, Luo S, Oroz LG, et al. Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet. 2004;36(6):585-95.
    • (2004) Nat Genet , vol.36 , Issue.6 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3    Davies, J.E.4    Luo, S.5    Oroz, L.G.6
  • 92
    • 84861898911 scopus 로고    scopus 로고
    • Dietary restriction but not rapamycin extends disease onset and survival of the H46R/H48Q mouse model of ALS
    • Bhattacharya A, Bokov A, Muller FL, Jernigan AL, Maslin K, Diaz V, et al. Dietary restriction but not rapamycin extends disease onset and survival of the H46R/H48Q mouse model of ALS. Neurobiol Aging. 2012;33(8):1829-32.
    • (2012) Neurobiol Aging , vol.33 , Issue.8 , pp. 1829-1832
    • Bhattacharya, A.1    Bokov, A.2    Muller, F.L.3    Jernigan, A.L.4    Maslin, K.5    Diaz, V.6
  • 94
    • 1642633757 scopus 로고    scopus 로고
    • Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease
    • Tanaka M, Machida Y, Niu S, Ikeda T, Jana NR, Doi H, et al. Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease. Nat Med. 2004;10(2):148-54.
    • (2004) Nat Med , vol.10 , Issue.2 , pp. 148-154
    • Tanaka, M.1    Machida, Y.2    Niu, S.3    Ikeda, T.4    Jana, N.R.5    Doi, H.6
  • 95
    • 84860296702 scopus 로고    scopus 로고
    • Trehalose protects from aggravation of amyloid pathology induced by isoflurane anesthesia in APP(swe) mutant mice
    • Perucho J, Casarejos MJ, Gomez A, Solano RM, de Yebenes JG, Mena MA. Trehalose protects from aggravation of amyloid pathology induced by isoflurane anesthesia in APP(swe) mutant mice. Curr Alzheimer Res. 2012;9(3):334-43.
    • (2012) Curr Alzheimer Res , vol.9 , Issue.3 , pp. 334-343
    • Perucho, J.1    Casarejos, M.J.2    Gomez, A.3    Solano, R.M.4    de Yebenes, J.G.5    Mena, M.A.6
  • 96
    • 77954955573 scopus 로고    scopus 로고
    • Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation
    • Rodriguez-Navarro JA, Rodriguez L, Casarejos MJ, Solano RM, Gomez A, Perucho J, et al. Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation. Neurobiol Dis. 2010;39(3):423-38.
    • (2010) Neurobiol Dis , vol.39 , Issue.3 , pp. 423-438
    • Rodriguez-Navarro, J.A.1    Rodriguez, L.2    Casarejos, M.J.3    Solano, R.M.4    Gomez, A.5    Perucho, J.6
  • 97
    • 29644437591 scopus 로고    scopus 로고
    • Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy
    • Davies JE, Sarkar S, Rubinsztein DC. Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy. Hum Mol Genet. 2006;15(1):23-31.
    • (2006) Hum Mol Genet , vol.15 , Issue.1 , pp. 23-31
    • Davies, J.E.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 98
    • 84863210676 scopus 로고    scopus 로고
    • Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy
    • Schaeffer V, Lavenir I, Ozcelik S, Tolnay M, Winkler DT, Goedert M. Stimulation of autophagy reduces neurodegeneration in a mouse model of human tauopathy. Brain. 2012;135(Pt 7):2169-77.
    • (2012) Brain , vol.135 , pp. 2169-2177
    • Schaeffer, V.1    Lavenir, I.2    Ozcelik, S.3    Tolnay, M.4    Winkler, D.T.5    Goedert, M.6
  • 100
    • 84898486403 scopus 로고    scopus 로고
    • A new method to measure autophagy flux in the nervous system
    • Matus S, Valenzuela V, Hetz C. A new method to measure autophagy flux in the nervous system. Autophagy. 2014;10(4):710-4.
    • (2014) Autophagy , vol.10 , Issue.4 , pp. 710-714
    • Matus, S.1    Valenzuela, V.2    Hetz, C.3
  • 101
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch WE, Morimoto RI, Dillin A, Kelly JW. Adapting proteostasis for disease intervention. Science. 2008;319(5865):916-9.
    • (2008) Science , vol.319 , Issue.5865 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 102
    • 84860471873 scopus 로고    scopus 로고
    • Targeting the UPR transcription factor XBP1 protects against Huntington’s disease through the regulation of FoxO1 and autophagy
    • Vidal RL, Figueroa A, Court FA, Thielen P, Molina C, Wirth C, et al. Targeting the UPR transcription factor XBP1 protects against Huntington’s disease through the regulation of FoxO1 and autophagy. Hum Mol Genet. 2012;21(10):2245-62.
    • (2012) Hum Mol Genet , vol.21 , Issue.10 , pp. 2245-2262
    • Vidal, R.L.1    Figueroa, A.2    Court, F.A.3    Thielen, P.4    Molina, C.5    Wirth, C.6
  • 103
    • 84902204258 scopus 로고    scopus 로고
    • Common ground: Stem cell approaches find shared pathways underlying ALS
    • Matus S, Medinas DB, Hetz C. Common ground: stem cell approaches find shared pathways underlying ALS. Cell Stem Cell. 2014;14(6):697-9.
    • (2014) Cell Stem Cell , vol.14 , Issue.6 , pp. 697-699
    • Matus, S.1    Medinas, D.B.2    Hetz, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.