메뉴 건너뛰기




Volumn 9, Issue 1, 2014, Pages 16-24

Autophagic induction of amyotrophic lateral sclerosislinked Cu/Zn superoxide dismutase 1 G93A mutant in NSC34 cells

Author keywords

Aggregates; Amyotrophic lateral sclerosis; Autophagy; Beclin 1; Beclin 1 interacting proteins; Nerve regeneration; Neural regeneration; Neurodegeneration; NSC34 cells; Oversea Study Fellowship from the China Scholarship Council; SOD1 G93A mutant

Indexed keywords

ALPHA SYNUCLEIN; BECLIN 1; BETA ACTIN; COPPER ZINC SUPEROXIDE DISMUTASE; MAMMALIAN TARGET OF RAPAMYCIN; MICROTUBULE ASSOCIATED PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE;

EID: 84896260510     PISSN: 16735374     EISSN: 18767958     Source Type: Journal    
DOI: 10.4103/1673-5374.125325     Document Type: Article
Times cited : (12)

References (56)
  • 1
    • 64649086140 scopus 로고    scopus 로고
    • Recent advances in the genetics of amyotrophic lateral sclerosis
    • Valdmanis PN, Daoud H, Dion PA, et al. Recent advances in the genetics of amyotrophic lateral sclerosis. Curr Neurol Neurosci Rep. 2009;9(3):198-205.
    • (2009) Curr Neurol Neurosci Rep , vol.9 , Issue.3 , pp. 198-205
    • Valdmanis, P.N.1    Daoud, H.2    Dion, P.A.3
  • 2
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR, Siddique T, Patterson D, et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993;362(6415):59-62.
    • (1993) Nature , vol.362 , Issue.6415 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3
  • 3
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor JP, Hardy J, Fischbeck KH. Toxic proteins in neurodegenerative disease. Science. 2002;296(5575):1991-1995.
    • (2002) Science , vol.296 , Issue.5575 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 4
    • 56449094841 scopus 로고    scopus 로고
    • Autophagy and the ubiquitin- proteasome system: Collaborators in neuroprotection
    • Nedelsky NB, Todd PK, Taylor JP. Autophagy and the ubiquitin- proteasome system: collaborators in neuroprotection. Biochim Biophys Acta. 2008;1782(12):691-699.
    • (2008) Biochim Biophys Acta , vol.1782 , Issue.12 , pp. 691-699
    • Nedelsky, N.B.1    Todd, P.K.2    Taylor, J.P.3
  • 5
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin- proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin- proteasome system by protein aggregation. Science. 2001;292(5521):1552-1555.
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 6
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin
    • Iwata A, Riley BE, Johnston JA, et al. HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem. 2005;280(48):40282-40292.
    • (2005) J Biol Chem , vol.280 , Issue.48 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3
  • 7
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • Mizushima N. Autophagy: process and function. Genes Dev. 2007;21(22):2861-2873.
    • (2007) Genes Dev , vol.21 , Issue.22 , pp. 2861-2873
    • Mizushima, N.1
  • 8
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein DC. The roles of intracellular protein-degradation pathways in neurodegeneration. Nature. 2006;443(7113):780-786.
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 9
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature. 2006;441(7095):885-889.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3
  • 10
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature. 2006;441(7095):880-884.
    • (2006) Nature , vol.441 , Issue.7095 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3
  • 11
    • 33751034682 scopus 로고    scopus 로고
    • Aggregate-prone proteins are cleared from the cytosol by autophagy: Therapeutic implications
    • Williams A, Jahreiss L, Sarkar S, et al. Aggregate-prone proteins are cleared from the cytosol by autophagy: therapeutic implications. Curr Top Dev Biol. 2006;76:89-101.
    • (2006) Curr Top Dev Biol , vol.76 , pp. 89-101
    • Williams, A.1    Jahreiss, L.2    Sarkar, S.3
  • 12
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • Kegel KB, Kim M, Sapp E, et al. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J Neurosci. 2000;20(19):7268-7278.
    • (2000) J Neurosci , vol.20 , Issue.19 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    Sapp, E.3
  • 13
    • 0033890821 scopus 로고    scopus 로고
    • Alpha-synuclein promotes mitochondrial deficit and oxidative stress
    • Hsu LJ, Sagara Y, Arroyo A, et al. Alpha-synuclein promotes mitochondrial deficit and oxidative stress. Am J Pathol. 2000; 157(2):401-410.
    • (2000) Am J Pathol , vol.157 , Issue.2 , pp. 401-410
    • Hsu, L.J.1    Sagara, Y.2    Arroyo, A.3
  • 14
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • Ravikumar B, Duden R, Rubinsztein DC. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet. 2002;11(9):1107-1117.
    • (2002) Hum Mol Genet , vol.11 , Issue.9 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 15
    • 0041589248 scopus 로고    scopus 로고
    • Alpha-synuclein is degraded by both autophagy and the proteasome
    • Webb JL, Ravikumar B, Atkins J, et al. Alpha-synuclein is degraded by both autophagy and the proteasome. J Biol Chem. 2003; 278(27):25009-25013.
    • (2003) J Biol Chem , vol.278 , Issue.27 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3
  • 16
    • 33750089740 scopus 로고    scopus 로고
    • Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Zn-superoxide dismutase proteins by macroautophagy and the proteasome
    • Kabuta T, Suzuki Y, Wada K. Degradation of amyotrophic lateral sclerosis-linked mutant Cu, Zn-superoxide dismutase proteins by macroautophagy and the proteasome. J Biol Chem. 2006; 281(41):30524-30533.
    • (2006) J Biol Chem , vol.281 , Issue.41 , pp. 30524-30533
    • Kabuta, T.1    Suzuki, Y.2    Wada, K.3
  • 17
    • 0036892683 scopus 로고    scopus 로고
    • Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis
    • Urushitani M, Kurisu J, Tsukita K, et al. Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis. J Neurochem. 2002;83(5):1030-1042.
    • (2002) J Neurochem , vol.83 , Issue.5 , pp. 1030-1042
    • Urushitani, M.1    Kurisu, J.2    Tsukita, K.3
  • 18
    • 83455243339 scopus 로고    scopus 로고
    • Autophagy dysregulation in amyotrophic lateral sclerosis
    • Chen S, Zhang X, Song L, et al. Autophagy dysregulation in amyotrophic lateral sclerosis. Brain Pathol. 2012;22(1):110-116.
    • (2012) Brain Pathol , vol.22 , Issue.1 , pp. 110-116
    • Chen, S.1    Zhang, X.2    Song, L.3
  • 19
    • 33751233260 scopus 로고    scopus 로고
    • Altered distribution and levels of cathepsinD and cystatins in amyotrophic lateral sclerosis transgenic mice: Possible roles in motor neuron survival
    • Wootz H, Weber E, Korhonen L, et al. Altered distribution and levels of cathepsinD and cystatins in amyotrophic lateral sclerosis transgenic mice: possible roles in motor neuron survival. Neuroscience. 2006;143(2):419-430.
    • (2006) Neuroscience , vol.143 , Issue.2 , pp. 419-430
    • Wootz, H.1    Weber, E.2    Korhonen, L.3
  • 20
    • 79955522014 scopus 로고    scopus 로고
    • Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis
    • Sasaki S. Autophagy in spinal cord motor neurons in sporadic amyotrophic lateral sclerosis. J Neuropathol Exp Neurol. 2011;70(5):349-359.
    • (2011) J Neuropathol Exp Neurol , vol.70 , Issue.5 , pp. 349-359
    • Sasaki, S.1
  • 21
    • 34249679116 scopus 로고    scopus 로고
    • p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis
    • Gal J, Strom AL, Kilty R, et al. p62 accumulates and enhances aggregate formation in model systems of familial amyotrophic lateral sclerosis. J Biol Chem. 2007;282(15):11068-11077.
    • (2007) J Biol Chem , vol.282 , Issue.15 , pp. 11068-11077
    • Gal, J.1    Strom, A.L.2    Kilty, R.3
  • 22
    • 66749133370 scopus 로고    scopus 로고
    • Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS
    • Chattopadhyay M, Valentine JS. Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS. Antioxid Redox Signal. 2009;11(7):1603-1614.
    • (2009) Antioxid Redox Signal , vol.11 , Issue.7 , pp. 1603-1614
    • Chattopadhyay, M.1    Valentine, J.S.2
  • 23
    • 34247398719 scopus 로고    scopus 로고
    • Constitutive autophagy: Vital role in clearance of unfavorable proteins in neurons
    • Tanaka K, Komatsu M, Ueno T, et al. Constitutive autophagy: vital role in clearance of unfavorable proteins in neurons. Cell Death Differ. 2007;14(5):887-894.
    • (2007) Cell Death Differ , vol.14 , Issue.5 , pp. 887-894
    • Tanaka, K.1    Komatsu, M.2    Ueno, T.3
  • 24
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EFC, et al. Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem. 2000;275(2):992-998.
    • (2000) J Biol Chem , vol.275 , Issue.2 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.C.3
  • 25
    • 0028284779 scopus 로고
    • Motor-neuron degeneration in mice that express a human Cu, Zn superoxide-dismutase mutation
    • Gurney ME, Pu HF, Chiu AY, et al. Motor-neuron degeneration in mice that express a human Cu, Zn superoxide-dismutase mutation. Science. 1994;264(5166):1772-1775.
    • (1994) Science , vol.264 , Issue.5166 , pp. 1772-1775
    • Gurney, M.E.1    Pu, H.F.2    Chiu, A.Y.3
  • 26
    • 42249102078 scopus 로고    scopus 로고
    • Transgenics, toxicity and therapeutics in rodent models of mutant Cu/Zn superoxide dismutase 1-mediated familial ALS
    • Turner BJ, Talbot K. Transgenics, toxicity and therapeutics in rodent models of mutant Cu/Zn superoxide dismutase 1-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
  • 27
    • 34248583762 scopus 로고    scopus 로고
    • Methods for monitoring autophagy from yeast to human
    • Klionsky DJ, Cuervo AM, Seglen PO. Methods for monitoring autophagy from yeast to human. Autophagy. 2007;3(3):181-206.
    • (2007) Autophagy , vol.3 , Issue.3 , pp. 181-206
    • Klionsky, D.J.1    Cuervo, A.M.2    Seglen, P.O.3
  • 28
    • 0034329418 scopus 로고    scopus 로고
    • LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing
    • Kabeya Y, Mizushima N, Uero T, et al. LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing. EMBO J. 2000;19(21):5720-5728.
    • (2000) EMBO J , vol.19 , Issue.21 , pp. 5720-5728
    • Kabeya, Y.1    Mizushima, N.2    Uero, T.3
  • 29
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida I, Minematsu-Ikeguchi N, Ueno T, et al. Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy. 2005;1(2):84-91.
    • (2005) Autophagy , vol.1 , Issue.2 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3
  • 30
    • 35848967804 scopus 로고    scopus 로고
    • How to interpret LC3 immunoblotting
    • Mizushima N, Yoshimori T. How to interpret LC3 immunoblotting. Autophagy. 2007;3(6):542-545.
    • (2007) Autophagy , vol.3 , Issue.6 , pp. 542-545
    • Mizushima, N.1    Yoshimori, T.2
  • 31
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A(1) prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A, Tagawa Y, Yoshimori T, et al. Bafilomycin A(1) prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct. 1998;23(1):33-42.
    • (1998) Cell Struct Funct , vol.23 , Issue.1 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3
  • 32
    • 11144357460 scopus 로고    scopus 로고
    • Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants
    • Hough MA, Grossmann JG, Antonyuk SV, et al. Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants. Proc Natl Acad Sci U S A. 2004;101(16):5976-5981.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.16 , pp. 5976-5981
    • Hough, M.A.1    Grossmann, J.G.2    Antonyuk, S.V.3
  • 33
    • 50249137038 scopus 로고    scopus 로고
    • Induction of macroautophagy by exogenously introduced calcium
    • Gao W, Ding WX, Stolz DB, et al. Induction of macroautophagy by exogenously introduced calcium. Autophagy. 2008;4(6):754-761.
    • (2008) Autophagy , vol.4 , Issue.6 , pp. 754-761
    • Gao, W.1    Ding, W.X.2    Stolz, D.B.3
  • 34
    • 66349120877 scopus 로고    scopus 로고
    • Autophagy protects neuron from Abeta-induced cytotoxicity
    • Hung SY, Huang WP, Liou HC, et al. Autophagy protects neuron from Abeta-induced cytotoxicity. Autophagy. 2009;5(4):502-510.
    • (2009) Autophagy , vol.5 , Issue.4 , pp. 502-510
    • Hung, S.Y.1    Huang, W.P.2    Liou, H.C.3
  • 35
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang XH, Jackson S, Seaman M, et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature. 1999;402(6762):672-676.
    • (1999) Nature , vol.402 , Issue.6762 , pp. 672-676
    • Liang, X.H.1    Jackson, S.2    Seaman, M.3
  • 36
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang Z, Klionsky DJ. Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol. 2010;22(2):124-131.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 37
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol- 3-kinase complex
    • Zhong Y, Wang QJ, Li X, et al. Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol- 3-kinase complex. Nat Cell Biol. 2009;11(4):468-476.
    • (2009) Nat Cell Biol , vol.11 , Issue.4 , pp. 468-476
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3
  • 38
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
    • Liang C, Feng P, Ku B, et al. Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG. Nat Cell Biol. 2006;8(7):688-699.
    • (2006) Nat Cell Biol , vol.8 , Issue.7 , pp. 688-699
    • Liang, C.1    Feng, P.2    Ku, B.3
  • 39
    • 41549114279 scopus 로고    scopus 로고
    • The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease
    • Pan T, Kondo S, Le W, et al. The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease. Brain. 2008;131(Pt 8):1969-1978.
    • (2008) Brain , vol.131 , Issue.PART 8 , pp. 1969-1978
    • Pan, T.1    Kondo, S.2    Le, W.3
  • 40
    • 26444515364 scopus 로고    scopus 로고
    • Autophagy and its possible roles in nervous system diseases, damage and repair
    • Rubinsztein DC, DiFiglia M, Heintz N, et al. Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy. 2005;1(1):11-22.
    • (2005) Autophagy , vol.1 , Issue.1 , pp. 11-22
    • Rubinsztein, D.C.1    Difiglia, M.2    Heintz, N.3
  • 41
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima N, Yoshimori T, Levine B. Methods in mammalian autophagy research. Cell. 2010;140(3):313-326.
    • (2010) Cell , vol.140 , Issue.3 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 42
    • 78149471570 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative disorders: Pathogenic roles and therapeutic implications
    • Banerjee R, Beal MF, Thomas B. Autophagy in neurodegenerative disorders: pathogenic roles and therapeutic implications. Trends Neurosci. 2010;33(12):541-549.
    • (2010) Trends Neurosci , vol.33 , Issue.12 , pp. 541-549
    • Banerjee, R.1    Beal, M.F.2    Thomas, B.3
  • 43
    • 0033366384 scopus 로고    scopus 로고
    • Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons
    • Williamson TL, Cleveland DW. Slowing of axonal transport is a very early event in the toxicity of ALS-linked SOD1 mutants to motor neurons. Nat Neurosci. 1999;2(1):50-56.
    • (1999) Nat Neurosci , vol.2 , Issue.1 , pp. 50-56
    • Williamson, T.L.1    Cleveland, D.W.2
  • 44
    • 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, 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):585-595.
    • (2004) Nat Genet , vol.36 , Issue.6 , pp. 585-595
    • Ravikumar, B.1    Vacher, C.2    Berger, Z.3
  • 45
    • 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, et al. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Gen Dev. 2009;23(19):2294-2306.
    • (2009) Gen Dev , vol.23 , Issue.19 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3
  • 46
    • 77955365630 scopus 로고    scopus 로고
    • The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS)
    • Crippa V, Sau D, Rusmini P, et al. The small heat shock protein B8 (HspB8) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). Hum Mol Genet. 2010;19(17):3440-3456.
    • (2010) Hum Mol Genet , vol.19 , Issue.17 , pp. 3440-3456
    • Crippa, V.1    Sau, D.2    Rusmini, P.3
  • 47
    • 57849136841 scopus 로고    scopus 로고
    • Autophagy: Principles and significance in health and disease
    • Todde V, Veenhuis M, van der Klei IJ. Autophagy: principles and significance in health and disease. Biochim Biophys Acta. 2009;1792(1):3-13.
    • (2009) Biochim Biophys Acta , vol.1792 , Issue.1 , pp. 3-13
    • Todde, V.1    Veenhuis, M.2    van der Klei, I.J.3
  • 48
    • 27644514227 scopus 로고    scopus 로고
    • Another way to die: Autophagic programmed cell death
    • Tsujimoto Y, Shimizu S. Another way to die: autophagic programmed cell death. Cell Death Differ. 2005;12 Suppl 2:1528-1534.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1528-1534
    • Tsujimoto, Y.1    Shimizu, S.2
  • 49
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • Kroemer G, Maiuri MC, Zalckvar E, et al. Self-eating and self-killing: crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol. 2007;8(9):741-752.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.9 , pp. 741-752
    • Kroemer, G.1    Maiuri, M.C.2    Zalckvar, E.3
  • 50
    • 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, et al. Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Autophagy. 2011;7(4):412-425.
    • (2011) Autophagy , vol.7 , Issue.4 , pp. 412-425
    • Zhang, X.1    Li, L.2    Chen, S.3
  • 51
    • 68149139456 scopus 로고    scopus 로고
    • The autophagy effector Beclin 1: A novel BH3-only protein
    • Sinha S, Levine B. The autophagy effector Beclin 1: a novel BH3-only protein. Oncogene. 2008;27 Suppl 1:S137-48.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Sinha, S.1    Levine, B.2
  • 52
    • 77951237303 scopus 로고    scopus 로고
    • The Beclin 1 interactome
    • He CC, Levine B. The Beclin 1 interactome. Curr Opin Cell Biol. 2010;22(2):140-149.
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 140-149
    • He, C.C.1    Levine, B.2
  • 53
    • 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
  • 54
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy-a novel beta-amyloid peptide-generating pathway activated in Alzheimer's disease
    • Yu WH, Cuervo AM, Kumar A, et al. Macroautophagy-a novel beta-amyloid peptide-generating pathway activated in Alzheimer's disease. J Cell Biol. 2005;171(1):87-98.
    • (2005) J Cell Biol , vol.171 , Issue.1 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3
  • 55
    • 33644899679 scopus 로고    scopus 로고
    • Intracellular conformational alterations of mutant SOD1 and the implications for fALS-associated SOD1 mutant induced motor neuron cell death
    • Zhang F, Zhu H. Intracellular conformational alterations of mutant SOD1 and the implications for fALS-associated SOD1 mutant induced motor neuron cell death. Biochim Biophys Acta. 2006;1760(3):404-414.
    • (2006) Biochim Biophys Acta , vol.1760 , Issue.3 , pp. 404-414
    • Zhang, F.1    Zhu, H.2
  • 56
    • 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, et al. Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin-independent mechanism. J Neurochem. 2009;111(4):1062-1073.
    • (2009) J Neurochem , vol.111 , Issue.4 , pp. 1062-1073
    • Gal, J.1    Strom, A.L.2    Kwinter, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.