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Volumn 5, Issue 10, 2014, Pages

Cystatin C protects neuronal cells against mutant copper-zinc superoxide dismutase-mediated toxicity

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; COPPER ZINC SUPEROXIDE DISMUTASE; CYSTATIN C; MAMMALIAN TARGET OF RAPAMYCIN; ADENYLATE KINASE; CLATHRIN; MUTANT PROTEIN; NEUROPROTECTIVE AGENT; PROTEIN AGGREGATE; SUPEROXIDE DISMUTASE; TARGET OF RAPAMYCIN KINASE;

EID: 84928044063     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.459     Document Type: Article
Times cited : (60)

References (60)
  • 1
    • 0035516124 scopus 로고    scopus 로고
    • From Charcot to Lou Gehrig: Deciphering selective motor neuron death in ALS
    • Cleveland DW, Rothstein JD. From Charcot to Lou Gehrig: deciphering selective motor neuron death in ALS. Nat Rev Neurosci 2001; 2: 806-819.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 806-819
    • Cleveland, D.W.1    Rothstein, J.D.2
  • 2
    • 4043075622 scopus 로고    scopus 로고
    • Lessons from models of SOD1-linked familial ALS
    • Bendotti C, Carri MT. Lessons from models of SOD1-linked familial ALS. Trends Mol Med 2004; 10: 393-400.
    • (2004) Trends Mol Med , vol.10 , pp. 393-400
    • Bendotti, C.1    Carri, M.T.2
  • 3
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn LI, Miller TM, Cleveland DW. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 2004; 27: 723-749.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 4
    • 0035664213 scopus 로고    scopus 로고
    • Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues
    • Watanabe M, Dykes-Hoberg M, Culotta VC, Price DL, Wong PC, Rothstein JD. Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol Dis 2001; 8: 933-941.
    • (2001) Neurobiol Dis , vol.8 , pp. 933-941
    • Watanabe, M.1    Dykes-Hoberg, M.2    Culotta, V.C.3    Price, D.L.4    Wong, P.C.5    Rothstein, J.D.6
  • 5
    • 0037388067 scopus 로고    scopus 로고
    • Misfolded CuZnSOD and amyotrophic lateral sclerosis
    • Valentine JS, Hart PJ. Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2003; 100: 3617-3622.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3617-3622
    • Valentine, J.S.1    Hart, P.J.2
  • 7
    • 84859454704 scopus 로고    scopus 로고
    • An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1
    • Guareschi S, Cova E, Cereda C, Ceroni M, Donetti E, Bosco DA et al. An over-oxidized form of superoxide dismutase found in sporadic amyotrophic lateral sclerosis with bulbar onset shares a toxic mechanism with mutant SOD1. Proc Natl Acad Sci USA 2012; 109: 5074-5079.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 5074-5079
    • Guareschi, S.1    Cova, E.2    Cereda, C.3    Ceroni, M.4    Donetti, E.5    Bosco, D.A.6
  • 8
    • 0023024774 scopus 로고
    • Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids
    • Abrahamson M, Barrett AJ, Salvesen G, Grubb A. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids. J Biol Chem 1986; 261: 11282-11289.
    • (1986) J Biol Chem , vol.261 , pp. 11282-11289
    • Abrahamson, M.1    Barrett, A.J.2    Salvesen, G.3    Grubb, A.4
  • 9
    • 0014061584 scopus 로고
    • Trace proteins in biological fluids. IV. Physicochemical properties and sites of formation of gamma-trace and beta-trace proteins
    • Hochwald GM, Pepe AJ, Thorbecke GJ. Trace proteins in biological fluids. IV. Physicochemical properties and sites of formation of gamma-trace and beta-trace proteins. Proc Soc Exp Biol Med 1967; 124: 961-966.
    • (1967) Proc Soc Exp Biol Med , vol.124 , pp. 961-966
    • Hochwald, G.M.1    Pepe, A.J.2    Thorbecke, G.J.3
  • 10
    • 79955958446 scopus 로고    scopus 로고
    • Protective mechanisms by cystatin C in neurodegenerative diseases
    • Gauthier S, Kaur G, Mi W, Tizon B, Levy E. Protective mechanisms by cystatin C in neurodegenerative diseases. Front Biosci 2011; 3: 541-554.
    • (2011) Front Biosci , vol.3 , pp. 541-554
    • Gauthier, S.1    Kaur, G.2    Mi, W.3    Tizon, B.4    Levy, E.5
  • 11
    • 36549043900 scopus 로고    scopus 로고
    • Cystatin C inhibits amyloid-beta deposition in Alzheimer's disease mouse models
    • Mi W, Pawlik M, Sastre M, Jung SS, Radvinsky DS, Klein AM et al. Cystatin C inhibits amyloid-beta deposition in Alzheimer's disease mouse models. Nat Genet 2007; 39: 1440-1442.
    • (2007) Nat Genet , vol.39 , pp. 1440-1442
    • Mi, W.1    Pawlik, M.2    Sastre, M.3    Jung, S.S.4    Radvinsky, D.S.5    Klein, A.M.6
  • 12
    • 19944426120 scopus 로고    scopus 로고
    • Cystatin C prevents degeneration of rat nigral dopaminergic neurons: In vitro and in vivo studies
    • Xu L, Sheng J, Tang Z, Wu X, Yu Y, Guo H et al. Cystatin C prevents degeneration of rat nigral dopaminergic neurons: in vitro and in vivo studies. Neurobiol Dis 2005; 18: 152-165.
    • (2005) Neurobiol Dis , vol.18 , pp. 152-165
    • Xu, L.1    Sheng, J.2    Tang, Z.3    Wu, X.4    Yu, Y.5    Guo, H.6
  • 13
    • 0027444626 scopus 로고
    • Bunina bodies in amyotrophic lateral sclerosis immunostained with rabbit anti-cystatin C serum
    • Okamoto K, Hirai S, Amari M, Watanabe M, Sakurai A. Bunina bodies in amyotrophic lateral sclerosis immunostained with rabbit anti-cystatin C serum. Neurosci Lett 1993; 162: 125-128.
    • (1993) Neurosci Lett , vol.162 , pp. 125-128
    • Okamoto, K.1    Hirai, S.2    Amari, M.3    Watanabe, M.4    Sakurai, A.5
  • 15
    • 78650087291 scopus 로고    scopus 로고
    • Cystatin C: A candidate biomarker for amyotrophic lateral sclerosis
    • Wilson ME, Boumaza I, Lacomis D, Bowser R. Cystatin C: a candidate biomarker for amyotrophic lateral sclerosis. PLoS One 2010; 5: e15133.
    • (2010) PLoS One , vol.5 , pp. e15133
    • Wilson, M.E.1    Boumaza, I.2    Lacomis, D.3    Bowser, R.4
  • 16
    • 77956475769 scopus 로고    scopus 로고
    • Induction of autophagy by cystatin C: A mechanism that protects murine primary cortical neurons and neuronal cell lines
    • Tizon B, Sahoo S, Yu H, Gauthier S, Kumar AR, Mohan P et al. Induction of autophagy by cystatin C: a mechanism that protects murine primary cortical neurons and neuronal cell lines. PLoS One 2010; 5: e9819.
    • (2010) PLoS One , vol.5 , pp. e9819
    • Tizon, B.1    Sahoo, S.2    Yu, H.3    Gauthier, S.4    Kumar, A.R.5    Mohan, P.6
  • 17
    • 0038155130 scopus 로고    scopus 로고
    • Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins
    • Hyun DH, Lee M, Halliwell B, Jenner P. Proteasomal inhibition causes the formation of protein aggregates containing a wide range of proteins, including nitrated proteins. J Neurochem 2003; 86: 363-373.
    • (2003) J Neurochem , vol.86 , pp. 363-373
    • Hyun, D.H.1    Lee, M.2    Halliwell, B.3    Jenner, P.4
  • 18
    • 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, Takahashi R. Proteasomal inhibition by misfolded mutant superoxide dismutase 1 induces selective motor neuron death in familial amyotrophic lateral sclerosis. J Neurochem 2002; 83: 1030-1042.
    • (2002) J Neurochem , vol.83 , pp. 1030-1042
    • Urushitani, M.1    Kurisu, J.2    Tsukita, K.3    Takahashi, R.4
  • 19
    • 84873314938 scopus 로고    scopus 로고
    • Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins
    • Watanabe S, Kaneko K, Yamanaka K. Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins. J Biol Chem 2013; 288: 3641-3654.
    • (2013) J Biol Chem , vol.288 , pp. 3641-3654
    • Watanabe, S.1    Kaneko, K.2    Yamanaka, K.3
  • 20
    • 84871150225 scopus 로고    scopus 로고
    • Motor neuronspecific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis
    • Tashiro Y, Urushitani M, Inoue H, Koike M, Uchiyama Y, Komatsu M et al. Motor neuronspecific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis. J Biol Chem 2012; 287: 42984-42994.
    • (2012) J Biol Chem , vol.287 , pp. 42984-42994
    • Tashiro, Y.1    Urushitani, M.2    Inoue, H.3    Koike, M.4    Uchiyama, Y.5    Komatsu, M.6
  • 21
    • 84881638591 scopus 로고    scopus 로고
    • Autophagy activation and neuroprotection by progesterone in the G93A-SOD1 transgenic mouse model of amyotrophic lateral sclerosis
    • Kim J, Kim TY, Cho KS, Kim HN, Koh JY. Autophagy activation and neuroprotection by progesterone in the G93A-SOD1 transgenic mouse model of amyotrophic lateral sclerosis. Neurobiol Dis 2013; 59: 80-85.
    • (2013) Neurobiol Dis , vol.59 , pp. 80-85
    • Kim, J.1    Kim, T.Y.2    Cho, K.S.3    Kim, H.N.4    Koh, J.Y.5
  • 22
    • 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 USA 2012; 109: 15024-15029.
    • (2012) Proc Natl Acad Sci USA , vol.109 , 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
  • 23
    • 0038388993 scopus 로고    scopus 로고
    • Involvement of cathepsin B in the motor neuron degeneration of amyotrophic lateral sclerosis
    • Kikuchi H, Yamada T, Furuya H, Doh-ura K, Ohyagi Y, Iwaki T et al. Involvement of cathepsin B in the motor neuron degeneration of amyotrophic lateral sclerosis. Acta Neuropathol 2003; 105: 462-468.
    • (2003) Acta Neuropathol , vol.105 , pp. 462-468
    • Kikuchi, H.1    Yamada, T.2    Furuya, H.3    Doh-ura, K.4    Ohyagi, Y.5    Iwaki, T.6
  • 24
    • 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, Lindholm D. Altered distribution and levels of cathepsinD and cystatins in amyotrophic lateral sclerosis transgenic mice: possible roles in motor neuron survival. Neuroscience 2006; 143: 419-430.
    • (2006) Neuroscience , vol.143 , pp. 419-430
    • Wootz, H.1    Weber, E.2    Korhonen, L.3    Lindholm, D.4
  • 26
    • 0029838035 scopus 로고    scopus 로고
    • Neuropathology of ALS: An overview
    • Hirano A. Neuropathology of ALS: an overview. Neurology 1996; 47(4 Suppl 2): S63-S66.
    • (1996) Neurology , vol.47 , Issue.4 , pp. S63-S66
    • Hirano, A.1
  • 27
    • 0014063240 scopus 로고
    • Familial amyotrophic lateral sclerosis. A subgroup characterized by posterior and spinocerebellar tract involvement and hyaline inclusions in the anterior horn cells
    • Hirano A, Kurland LT, Sayre GP. Familial amyotrophic lateral sclerosis. A subgroup characterized by posterior and spinocerebellar tract involvement and hyaline inclusions in the anterior horn cells. Arch Neurol 1967; 16: 232-243.
    • (1967) Arch Neurol , vol.16 , pp. 232-243
    • Hirano, A.1    Kurland, L.T.2    Sayre, G.P.3
  • 28
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011; 13: 132-141.
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 29
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave BT, Ouwens M, Withers DJ, Alessi DR, Shepherd PR. Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation. Biochem J 1999; 344(Pt 2): 427-431.
    • (1999) Biochem J , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 30
    • 11844306671 scopus 로고    scopus 로고
    • Aberrant deltaPKC activation in the spinal cord of Wobbler mouse: A model of motor neuron disease
    • Dave KR, Raval AP, Purroy J, Kirkinezos IG, Moraes CT, Bradley WG et al. Aberrant deltaPKC activation in the spinal cord of Wobbler mouse: a model of motor neuron disease. Neurobiol Dis 2005; 18: 126-133.
    • (2005) Neurobiol Dis , vol.18 , pp. 126-133
    • Dave, K.R.1    Raval, A.P.2    Purroy, J.3    Kirkinezos, I.G.4    Moraes, C.T.5    Bradley, W.G.6
  • 31
    • 34548073361 scopus 로고    scopus 로고
    • PKC delta and tissue transglutaminase are novel inhibitors of autophagy in pancreatic cancer cells
    • Ozpolat B, Akar U, Mehta K, Lopez-Berestein G. PKC delta and tissue transglutaminase are novel inhibitors of autophagy in pancreatic cancer cells. Autophagy 2007; 3: 480-483.
    • (2007) Autophagy , vol.3 , pp. 480-483
    • Ozpolat, B.1    Akar, U.2    Mehta, K.3    Lopez-Berestein, G.4
  • 33
    • 84878759123 scopus 로고    scopus 로고
    • Cystatin C properties crucial for uptake and inhibition of intracellular target enzymes
    • Wallin H, Abrahamson M, Ekstrom U. Cystatin C properties crucial for uptake and inhibition of intracellular target enzymes. J Biol Chem 2013; 288: 17019-17029.
    • (2013) J Biol Chem , vol.288 , pp. 17019-17029
    • Wallin, H.1    Abrahamson, M.2    Ekstrom, U.3
  • 34
    • 79952743365 scopus 로고    scopus 로고
    • Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells
    • Munch C, O'Brien J, Bertolotti A. Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells. Proc Natl Acad Sci USA 2011; 108: 3548-3553.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3548-3553
    • Munch, C.1    O'Brien, J.2    Bertolotti, A.3
  • 36
    • 79956326016 scopus 로고    scopus 로고
    • Syntaxin 1B suppresses macropinocytosis and semaphorin 3A-induced growth cone collapse
    • Kabayama H, Takeuchi M, Taniguchi M, Tokushige N, Kozaki S, Mizutani A et al. Syntaxin 1B suppresses macropinocytosis and semaphorin 3A-induced growth cone collapse. J Neurosci 2011; 31: 7357-7364.
    • (2011) J Neurosci , vol.31 , pp. 7357-7364
    • Kabayama, H.1    Takeuchi, M.2    Taniguchi, M.3    Tokushige, N.4    Kozaki, S.5    Mizutani, A.6
  • 38
    • 70450222302 scopus 로고    scopus 로고
    • The role of lysosomal rupture in neuronal death
    • Yamashima T, Oikawa S. The role of lysosomal rupture in neuronal death. Prog Neurobiol 2009; 89: 343-358.
    • (2009) Prog Neurobiol , vol.89 , pp. 343-358
    • Yamashima T1    Oikawa, S.2
  • 39
    • 0032032227 scopus 로고    scopus 로고
    • Amino acid substitutions in the N-terminal segment of cystatin C create selective protein inhibitors of lysosomal cysteine proteinases
    • Mason RW, Sol-Church K, Abrahamson M. Amino acid substitutions in the N-terminal segment of cystatin C create selective protein inhibitors of lysosomal cysteine proteinases. Biochem J 1998; 330(Pt 2): 833-838.
    • (1998) Biochem J , vol.330 , pp. 833-838
    • Mason, R.W.1    Sol-Church, K.2    Abrahamson, M.3
  • 40
    • 0037047320 scopus 로고    scopus 로고
    • Directed differentiation of embryonic stem cells into motor neurons
    • Wichterle H, Lieberam I, Porter JA, Jessell TM. Directed differentiation of embryonic stem cells into motor neurons. Cell 2002; 110: 385-397.
    • (2002) Cell , vol.110 , pp. 385-397
    • Wichterle, H.1    Lieberam, I.2    Porter, J.A.3    Jessell, T.M.4
  • 41
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • Klionsky DJ, Emr SD. Autophagy as a regulated pathway of cellular degradation. Science 2000; 290: 1717-1721.
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 42
    • 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: 880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 43
    • 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: 885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 44
    • 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: 1308-1320.
    • (2013) Autophagy , vol.9 , pp. 1308-1320
    • Castillo, K.1    Nassif, M.2    Valenzuela, V.3    Rojas, F.4    Matus, S.5    Mercado, G.6
  • 45
    • 68149100027 scopus 로고    scopus 로고
    • Treatment with lithium carbonate does not improve disease progression in two different strains of SOD1 mutant mice
    • Pizzasegola C, Caron I, Daleno C, Ronchi A, Minoia C, Carri MT et al. Treatment with lithium carbonate does not improve disease progression in two different strains of SOD1 mutant mice. Amyotroph Lateral Scler 2009; 10: 221-228.
    • (2009) Amyotroph Lateral Scler , vol.10 , pp. 221-228
    • Pizzasegola, C.1    Caron, I.2    Daleno, C.3    Ronchi, A.4    Minoia, C.5    Carri, M.T.6
  • 46
    • 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, Zhang X et al. Rapamycin treatment augments motor neuron degeneration in SOD1(G93A) mouse model of amyotrophic lateral sclerosis. Autophagy 2011; 7: 412-425.
    • (2011) Autophagy , vol.7 , pp. 412-425
    • Zhang, X.1    Li, L.2    Chen, S.3    Yang, D.4    Wang, Y.5    Zhang, X.6
  • 48
    • 84855993170 scopus 로고    scopus 로고
    • Reduced activity of AMP-activated protein kinase protects against genetic models of motor neuron disease
    • Lim MA, Selak MA, Xiang Z, Krainc D, Neve RL, Kraemer BC et al. Reduced activity of AMP-activated protein kinase protects against genetic models of motor neuron disease. J Neurosci 2012; 32: 1123-1141.
    • (2012) J Neurosci , vol.32 , pp. 1123-1141
    • Lim, M.A.1    Selak, M.A.2    Xiang, Z.3    Krainc, D.4    Neve, R.L.5    Kraemer, B.C.6
  • 49
    • 0030052426 scopus 로고    scopus 로고
    • Folding-related dimerization of human cystatin C
    • Ekiel I, Abrahamson M. Folding-related dimerization of human cystatin C. J Biol Chem 1996; 271: 1314-1321.
    • (1996) J Biol Chem , vol.271 , pp. 1314-1321
    • Ekiel, I.1    Abrahamson, M.2
  • 50
    • 0030613747 scopus 로고    scopus 로고
    • Human cystatin C forms an inactive dimer during intracellular trafficking in transfected CHO cells
    • Merz GS, Benedikz E, Schwenk V, Johansen TE, Vogel LK, Rushbrook JI et al. Human cystatin C forms an inactive dimer during intracellular trafficking in transfected CHO cells. J Cell Physiol 1997; 173: 423-432.
    • (1997) J Cell Physiol , vol.173 , pp. 423-432
    • Merz, G.S.1    Benedikz, E.2    Schwenk, V.3    Johansen, T.E.4    Vogel, L.K.5    Rushbrook, J.I.6
  • 51
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn LI, Becher MW, Lee MK, Anderson KL, Jenkins NA, Copeland NG et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997; 18: 327-338.
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1    Becher, M.W.2    Lee, M.K.3    Anderson, K.L.4    Jenkins, N.A.5    Copeland, N.G.6
  • 52
    • 34547893834 scopus 로고    scopus 로고
    • Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: Clues to a possible strategy for treating ALS
    • Yamashita H, Kawamata J, Okawa K, Kanki R, Nakamizo T, Hatayama T et al. Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS. J Neurochem 2007; 102: 1497-1505.
    • (2007) J Neurochem , vol.102 , pp. 1497-1505
    • Yamashita, H.1    Kawamata, J.2    Okawa, K.3    Kanki, R.4    Nakamizo, T.5    Hatayama, T.6
  • 53
    • 0023684074 scopus 로고
    • Efficient production of native, biologically active human cystatin C by Escherichia coli
    • Abrahamson M, Dalboge H, Olafsson I, Carlsen S, Grubb A. Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett 1988; 236: 14-18.
    • (1988) FEBS Lett , vol.236 , pp. 14-18
    • Abrahamson, M.1    Dalboge, H.2    Olafsson, I.3    Carlsen, S.4    Grubb, A.5
  • 55
    • 0024997246 scopus 로고
    • Removal of endotoxin from protein solutions by phase separation using Triton X-114
    • Aida Y, Pabst MJ. Removal of endotoxin from protein solutions by phase separation using Triton X-114. J Immunol Methods 1990; 132: 191-195.
    • (1990) J Immunol Methods , vol.132 , pp. 191-195
    • Aida, Y.1    Pabst, M.J.2
  • 57
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem 1989; 182: 319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 58
    • 51549106105 scopus 로고    scopus 로고
    • Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species
    • Sevlever D, Jiang P, Yen SH. Cathepsin D is the main lysosomal enzyme involved in the degradation of alpha-synuclein and generation of its carboxy-terminally truncated species. Biochemistry 2008; 47: 9678-9687.
    • (2008) Biochemistry , vol.47 , pp. 9678-9687
    • Sevlever, D.1    Jiang, P.2    Yen, S.H.3
  • 59
    • 65649146849 scopus 로고    scopus 로고
    • Protective role of endogenous gangliosides for lysosomal pathology in a cellular model of synucleinopathies
    • Wei J, Fujita M, Nakai M, Waragai M, Sekigawa A, Sugama S et al. Protective role of endogenous gangliosides for lysosomal pathology in a cellular model of synucleinopathies. Am J Pathol 2009; 174: 1891-1909.
    • (2009) Am J Pathol , vol.174 , pp. 1891-1909
    • Wei, J.1    Fujita, M.2    Nakai, M.3    Waragai, M.4    Sekigawa, A.5    Sugama, S.6
  • 60
    • 34948850962 scopus 로고    scopus 로고
    • Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosislinked mutant SOD1
    • Niwa J, Yamada S, Ishigaki S, Sone J, Takahashi M, Katsuno M et al. Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosislinked mutant SOD1. J Biol Chem 2007; 282: 28087-28095.
    • (2007) J Biol Chem , vol.282 , pp. 28087-28095
    • Niwa, J.1    Yamada, S.2    Ishigaki, S.3    Sone, J.4    Takahashi, M.5    Katsuno, M.6


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