메뉴 건너뛰기




Volumn 17, Issue 7, 2010, Pages 1104-1114

Neuronal caspase-3 signaling: Not only cell death

Author keywords

Apoptosis; Neurodegeneration; Neurodevelopment; Neuron differentiation; Synaptic plasticity

Indexed keywords

ADAPTOR PROTEIN; AMYLOID BETA PROTEIN; APOPTOSOME; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; BETA SECRETASE; CASPASE 3; CASPASE 6; CASPASE 9; COPPER ZINC SUPEROXIDE DISMUTASE; CULLIN; CULLIN 3; CYTOCHROME C; DEATH RECEPTOR; DEATH RECEPTOR 6; HUNTINGTIN; PARKIN; POLYGLUTAMINE; PRESENILIN; PROTEIN BCL 2; PROTEIN GGA3; TAR DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 77953613803     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2009.180     Document Type: Review
Times cited : (390)

References (87)
  • 1
    • 0037428232 scopus 로고    scopus 로고
    • Apoptosis. Life and death decisions
    • Nicholson DW, Thornberry NA. Apoptosis. Life and death decisions. Science 2003; 299: 214-215.
    • (2003) Science , vol.299 , pp. 214-215
    • Nicholson, D.W.1    Thornberry, N.A.2
  • 2
    • 0035213498 scopus 로고    scopus 로고
    • Caspases: Cellular demolition experts
    • Creagh EM, Martin SJ. Caspases: cellular demolition experts. Biochem Soc Trans 2001; 29: 696-702.
    • (2001) Biochem Soc Trans , vol.29 , pp. 696-702
    • Creagh, E.M.1    Martin, S.J.2
  • 3
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw WC, Martins LM, Kaufmann SH. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 1999; 68: 383-424.
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 4
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green DR, Kroemer G. The pathophysiology of mitochondrial cell death. Science 2004; 305: 626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 7
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • DOI 10.1152/physrev.00013.2006
    • Kroemer G, Galluzzi L, Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol Rev 2007; 87: 99-163. (Pubitemid 46209992)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 8
    • 33745962416 scopus 로고    scopus 로고
    • BH3-only proteins in cell death initiation, malignant disease and anticancer therapy
    • Labi V, Erlacher M, Kiessling S, Villunger A. BH3-only proteins in cell death initiation, malignant disease and anticancer therapy. Cell Death Differ 2006; 13: 1325-1338.
    • (2006) Cell Death Differ , vol.13 , pp. 1325-1338
    • Labi, V.1    Erlacher, M.2    Kiessling, S.3    Villunger, A.4
  • 9
    • 0034676089 scopus 로고    scopus 로고
    • Cross-talk in cell death signaling
    • Roy S, Nicholson DW. Cross-talk in cell death signaling. J Exp Med 2000; 192: F21-F25.
    • (2000) J Exp Med , vol.192
    • Roy, S.1    Nicholson, D.W.2
  • 10
    • 42449123761 scopus 로고    scopus 로고
    • Expansion and evolution of cell death programmes
    • Degterev A, Yuan J. Expansion and evolution of cell death programmes. Nat Rev Mol Cell Biol 2008; 9: 378-390.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 378-390
    • Degterev, A.1    Yuan, J.2
  • 11
    • 33244471589 scopus 로고    scopus 로고
    • Developmental apoptosis in C. elegans: A complex CEDnario
    • Lettre G, Hengartner MO. Developmental apoptosis in C. elegans: a complex CEDnario. Nat Rev Mol Cell Biol 2006; 7: 97-108.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 97-108
    • Lettre, G.1    Hengartner, M.O.2
  • 12
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia R, Grote P, Westermann B, Conradt B. DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans. Nature 2005; 433: 754-760.
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 13
    • 28944443033 scopus 로고    scopus 로고
    • Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer
    • Yu X, Wang L, Acehan D, Wang X, Akey CW. Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer. J Mol Biol 2006; 355: 577-589.
    • (2006) J Mol Biol , vol.355 , pp. 577-589
    • Yu, X.1    Wang, L.2    Acehan, D.3    Wang, X.4    Akey, C.W.5
  • 14
    • 23944456417 scopus 로고    scopus 로고
    • IAPs-the ubiquitin connection
    • Vaux DL, Silke J. IAPs-the ubiquitin connection. Cell Death Differ 2005; 12: 1205-1207.
    • (2005) Cell Death Differ , vol.12 , pp. 1205-1207
    • Vaux, D.L.1    Silke, J.2
  • 15
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • Arama E, Agapite J, Steller H. Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev Cell 2003; 4: 687-697.
    • (2003) Dev Cell , vol.4 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 16
    • 30444448684 scopus 로고    scopus 로고
    • The two Drosophila cytochrome C proteins can function in both respiration and caspase activation
    • Arama E, Bader M, Srivastava M, Bergmann A, Steller H. The two Drosophila cytochrome C proteins can function in both respiration and caspase activation. EMBO J 2006; 25: 232-243.
    • (2006) EMBO J , vol.25 , pp. 232-243
    • Arama, E.1    Bader, M.2    Srivastava, M.3    Bergmann, A.4    Steller, H.5
  • 17
    • 0002171705 scopus 로고    scopus 로고
    • Cellular interactions that regulate programmed cell death in the developing vertebrate nervous system
    • Koliatsos V Ratan R (eds) Humana: Totowa
    • Burek M, Oppenheim R. Cellular interactions that regulate programmed cell death in the developing vertebrate nervous system. In: Koliatsos V, Ratan R (eds). Cell Death and Disease of the Nervous System. Humana: Totowa, 1999, pp 145-180.
    • (1999) Cell Death and Disease of the Nervous System , pp. 145-180
    • Burek, M.1    Oppenheim, R.2
  • 19
    • 0033615957 scopus 로고    scopus 로고
    • Programmed cell death of embryonic motoneurons triggered through the Fas death receptor
    • Raoul C, Henderson CE, Pettmann B. Programmed cell death of embryonic motoneurons triggered through the Fas death receptor. J Cell Biol 1999; 147: 1049-1062.
    • (1999) J Cell Biol , vol.147 , pp. 1049-1062
    • Raoul, C.1    Henderson, C.E.2    Pettmann, B.3
  • 20
    • 0033562658 scopus 로고    scopus 로고
    • CD95 ligand (Fas-L/APO-1L) and tumor necrosis factor-related apoptosis-inducingligand mediate ischemia-induced apoptosis in neurons
    • Martin-Villalba A, Herr I, Jeremias I, Hahne M, Brandt R, Vogel J et al. CD95 ligand (Fas-L/APO-1L) and tumor necrosis factor-related apoptosis-inducingligand mediate ischemia-induced apoptosis in neurons. J Neurosci 1999; 19: 3809-3817.
    • (1999) J Neurosci , vol.19 , pp. 3809-3817
    • Martin-Villalba, A.1    Herr, I.2    Jeremias, I.3    Hahne, M.4    Brandt, R.5    Vogel, J.6
  • 21
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • Kuida K, Zheng TS, Na S, Kuan C, Yang D, Karasuyama H et al. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 1996; 384: 368-372.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1    Zheng, T.S.2    Na, S.3    Kuan, C.4    Yang, D.5    Karasuyama, H.6
  • 23
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem R, Hakem A, Duncan GS, Henderson JT, Woo M, Soengas MS et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 1998; 94: 339-352.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3    Henderson, J.T.4    Woo, M.5    Soengas, M.S.6
  • 24
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • Kuida K, Haydar TF, Kuan CY, Gu Y, Taya C, Karasuyama H et al. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 1998; 94: 325-337.
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1    Haydar, T.F.2    Kuan, C.Y.3    Gu, Y.4    Taya, C.5    Karasuyama, H.6
  • 25
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Gruss P. Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 1998; 94: 727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 26
    • 21144451097 scopus 로고    scopus 로고
    • Specific ablation of the apoptotic functions of cytochrome C reveals a differential requirement for cytochrome C and Apaf-1 in apoptosis
    • Hao Z, Duncan GS, Chang CC, Elia A, Fang M, Wakeham A et al. Specific ablation of the apoptotic functions of cytochrome C reveals a differential requirement for cytochrome C and Apaf-1 in apoptosis. Cell 2005; 121: 579-591.
    • (2005) Cell , vol.121 , pp. 579-591
    • Hao, Z.1    Duncan, G.S.2    Chang, C.C.3    Elia, A.4    Fang, M.5    Wakeham, A.6
  • 28
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke PG. Developmental cell death: morphological diversity and multiple mechanisms. Anat Embryol (Berl) 1990; 181: 195-213.
    • (1990) Anat Embryol (Berl) , vol.181 , pp. 195-213
    • Clarke, P.G.1
  • 30
    • 26444537963 scopus 로고    scopus 로고
    • Neural stem cell differentiation is dependent upon endogenous caspase 3 activity
    • Fernando P, Brunette S, Megeney LA. Neural stem cell differentiation is dependent upon endogenous caspase 3 activity. FASEB J 2005; 19: 1671-1673.
    • (2005) FASEB J , vol.19 , pp. 1671-1673
    • Fernando, P.1    Brunette, S.2    Megeney, L.A.3
  • 31
    • 23244436227 scopus 로고    scopus 로고
    • Axon retraction and degeneration in development and disease
    • Luo L, O'Leary DD. Axon retraction and degeneration in development and disease. Annu Rev Neurosci 2005; 28: 127-156.
    • (2005) Annu Rev Neurosci , vol.28 , pp. 127-156
    • Luo, L.1    O'Leary, D.D.2
  • 32
    • 0025009264 scopus 로고
    • Metamorphosis of the central nervous system of Drosophila
    • Truman JW. Metamorphosis of the central nervous system of Drosophila. J Neurobiol 1990; 21: 1072-1084.
    • (1990) J Neurobiol , vol.21 , pp. 1072-1084
    • Truman, J.W.1
  • 34
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A, McLaughlin T, O'Leary DD, Tessier-Lavigne M. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 2009; 457: 981-989.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 35
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: Roles in synaptic plasticity and cell death
    • Chan SL, Mattson MP. Caspase and calpain substrates: roles in synaptic plasticity and cell death. J Neurosci Res 1999; 58: 167-190.
    • (1999) J Neurosci Res , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.P.2
  • 36
    • 0034699033 scopus 로고    scopus 로고
    • Caspase activity plays an essential role in long-term memory
    • Dash PK, Blum S, Moore AN. Caspase activity plays an essential role in long-term memory. Neuroreport 2000; 11: 2811-2816.
    • (2000) Neuroreport , vol.11 , pp. 2811-2816
    • Dash, P.K.1    Blum, S.2    Moore, A.N.3
  • 39
    • 33845439096 scopus 로고    scopus 로고
    • Dynamic role of postsynaptic caspase-3 and BIRC4 in zebra finch song-response habituation
    • Huesmann GR, Clayton DF. Dynamic role of postsynaptic caspase-3 and BIRC4 in zebra finch song-response habituation. Neuron 2006; 52: 1061-1072.
    • (2006) Neuron , vol.52 , pp. 1061-1072
    • Huesmann, G.R.1    Clayton, D.F.2
  • 42
    • 0002639306 scopus 로고    scopus 로고
    • Neurotrophic factors protect cortical synaptic terminals against amyloid and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function
    • Guo ZH, Mattson MP. Neurotrophic factors protect cortical synaptic terminals against amyloid and oxidative stress-induced impairment of glucose transport, glutamate transport and mitochondrial function. Cereb Cortex 2000; 10: 50-57.
    • (2000) Cereb Cortex , vol.10 , pp. 50-57
    • Guo, Z.H.1    Mattson, M.P.2
  • 43
    • 35649007879 scopus 로고    scopus 로고
    • A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila
    • Arama E, Bader M, Rieckhof GE, Steller H. A ubiquitin ligase complex regulates caspase activation during sperm differentiation in Drosophila. PLoS Biol 2007; 5: e251.
    • (2007) PLoS Biol , vol.5
    • Arama, E.1    Bader, M.2    Rieckhof, G.E.3    Steller, H.4
  • 44
    • 0028642274 scopus 로고
    • Calcium and excitotoxic neuronal injury
    • Choi DW. Calcium and excitotoxic neuronal injury. Ann N Y Acad Sci 1994; 747: 162-171.
    • (1994) Ann N y Acad Sci , vol.747 , pp. 162-171
    • Choi, D.W.1
  • 45
    • 0020067965 scopus 로고
    • Temporal profile of neuronal damage in a model of transient forebrain ischemia
    • Pulsinelli WA, Brierley JB, Plum F. Temporal profile of neuronal damage in a model of transient forebrain ischemia. Ann Neurol 1982; 11: 491-498.
    • (1982) Ann Neurol , vol.11 , pp. 491-498
    • Pulsinelli, W.A.1    Brierley, J.B.2    Plum, F.3
  • 46
    • 0029773397 scopus 로고    scopus 로고
    • An ICE inhibitor, z-VAD-DCB attenuates ischaemic brain damage in the rat
    • Loddick SA, MacKenzie A, Rothwell NJ. An ICE inhibitor, z-VAD-DCB attenuates ischaemic brain damage in the rat. Neuroreport 1996; 7: 1465-1468.
    • (1996) Neuroreport , vol.7 , pp. 1465-1468
    • Loddick, S.A.1    MacKenzie, A.2    Rothwell, N.J.3
  • 47
    • 0030614952 scopus 로고    scopus 로고
    • Inhibition of interleukin 1beta converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage
    • Hara H, Friedlander RM, Gagliardini V, Ayata C, Fink K, Huang Z et al. Inhibition of interleukin 1beta converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage. Proc Natl Acad Sci USA 1997; 94: 2007-2012.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2007-2012
    • Hara, H.1    Friedlander, R.M.2    Gagliardini, V.3    Ayata, C.4    Fink, K.5    Huang, Z.6
  • 48
    • 0031894316 scopus 로고    scopus 로고
    • Reduced ischemic brain injury in interleukin-1 beta converting enzyme-deficient mice
    • Schielke GP, Yang GY, Shivers BD, Betz AL. Reduced ischemic brain injury in interleukin-1 beta converting enzyme-deficient mice. J Cereb Blood Flow Metab 1998; 18: 180-185.
    • (1998) J Cereb Blood Flow Metab , vol.18 , pp. 180-185
    • Schielke, G.P.1    Yang, G.Y.2    Shivers, B.D.3    Betz, A.L.4
  • 49
    • 0032124903 scopus 로고    scopus 로고
    • Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia
    • Chen J, Nagayama T, Jin K, Stetler RA, Zhu RL, Graham SH et al. Induction of caspase-3-like protease may mediate delayed neuronal death in the hippocampus after transient cerebral ischemia. J Neurosci 1998; 18: 4914-4928.
    • (1998) J Neurosci , vol.18 , pp. 4914-4928
    • Chen, J.1    Nagayama, T.2    Jin, K.3    Stetler, R.A.4    Zhu, R.L.5    Graham, S.H.6
  • 50
    • 0031841171 scopus 로고    scopus 로고
    • A caspase inhibitor blocks ischaemia-induced delayed neuronal death in the gerbil
    • Himi T, Ishizaki Y, Murota S. A caspase inhibitor blocks ischaemia-induced delayed neuronal death in the gerbil. Eur J Neurosci 1998; 10: 777-781.
    • (1998) Eur J Neurosci , vol.10 , pp. 777-781
    • Himi, T.1    Ishizaki, Y.2    Murota, S.3
  • 51
    • 0032080673 scopus 로고    scopus 로고
    • Caspase inhibitor affords neuroprotection with delayed administration in a rat model of neonatal hypoxic-ischemic brain injury
    • Cheng Y, Deshmukh M, D'Costa A, Demaro JA, Gidday JM, Shah A et al. Caspase inhibitor affords neuroprotection with delayed administration in a rat model of neonatal hypoxic-ischemic brain injury. J Clin Invest 1998; 101: 1992-1999.
    • (1998) J Clin Invest , vol.101 , pp. 1992-1999
    • Cheng, Y.1    Deshmukh, M.2    D'Costa, A.3    Demaro, J.A.4    Gidday, J.M.5    Shah, A.6
  • 52
    • 0042888669 scopus 로고    scopus 로고
    • Clinical practice. Early Alzheimer's disease
    • Kawas CH. Clinical practice. Early Alzheimer's disease. N Engl J Med 2003; 349: 1056-1063.
    • (2003) N Engl J Med , vol.349 , pp. 1056-1063
    • Kawas, C.H.1
  • 53
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001; 81: 741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 55
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su JH, Anderson AJ, Cummings BJ, Cotman CW. Immunohistochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 1994; 5: 2529-2533.
    • (1994) Neuroreport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 57
    • 0030868903 scopus 로고    scopus 로고
    • Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease
    • Kim TW, Pettingell WH, Jung YK, Kovacs DM, Tanzi RE. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. Science 1997; 277: 373-376.
    • (1997) Science , vol.277 , pp. 373-376
    • Kim, T.W.1    Pettingell, W.H.2    Jung, Y.K.3    Kovacs, D.M.4    Tanzi, R.E.5
  • 59
    • 0032507667 scopus 로고    scopus 로고
    • Caspase-mediated cleavage is not required for the activity of presenilins in amyloidogenesis and NOTCH signaling
    • Brockhaus M, Grünberg J, Röhrig S, Loetscher H, Wittenburg N, Baumeister R et al. Caspase-mediated cleavage is not required for the activity of presenilins in amyloidogenesis and NOTCH signaling. Neuroreport 1998; 9: 1481-1486.
    • (1998) Neuroreport , vol.9 , pp. 1481-1486
    • Brockhaus, M.1    Grünberg, J.2    Röhrig, S.3    Loetscher, H.4    Wittenburg, N.5    Baumeister, R.6
  • 60
    • 34249734831 scopus 로고    scopus 로고
    • Depletion of GGA3 stabilizes BACE and enhances beta-secretase activity
    • Tesco G, Koh YH, Kang EL, Cameron AN, Das S, Sena-Esteves M et al. Depletion of GGA3 stabilizes BACE and enhances beta-secretase activity. Neuron 2007; 54: 721-737.
    • (2007) Neuron , vol.54 , pp. 721-737
    • Tesco, G.1    Koh, Y.H.2    Kang, E.L.3    Cameron, A.N.4    Das, S.5    Sena-Esteves, M.6
  • 61
    • 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: 130-133.
    • (2006) Science , vol.314 , 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
  • 62
    • 2442676753 scopus 로고    scopus 로고
    • Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: A functional link with disease penetrance
    • Buratti E, Brindisi A, Pagani F, Baralle FE. Nuclear factor TDP-43 binds to the polymorphic TG repeats in CFTR intron 8 and causes skipping of exon 9: a functional link with disease penetrance. Am J Hum Genet 2004; 74: 1322-1325.
    • (2004) Am J Hum Genet , vol.74 , pp. 1322-1325
    • Buratti, E.1    Brindisi, A.2    Pagani, F.3    Baralle, F.E.4
  • 63
    • 49349104833 scopus 로고    scopus 로고
    • Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease
    • Rohn TT. Caspase-cleaved TAR DNA-binding protein-43 is a major pathological finding in Alzheimer's disease. Brain Res 2008; 1228: 189-198.
    • (2008) Brain Res , vol.1228 , pp. 189-198
    • Rohn, T.T.1
  • 64
    • 55349115428 scopus 로고    scopus 로고
    • Caspase-3 is enriched in postsynaptic densities and increased in Alzheimer's disease
    • Louneva N, Cohen JW, Han LY, Talbot K, Wilson RS, Bennett DA et al. Caspase-3 is enriched in postsynaptic densities and increased in Alzheimer's disease. Am J Pathol 2008; 173: 1488-1495.
    • (2008) Am J Pathol , vol.173 , pp. 1488-1495
    • Louneva, N.1    Cohen, J.W.2    Han, L.Y.3    Talbot, K.4    Wilson, R.S.5    Bennett, D.A.6
  • 65
    • 34247611481 scopus 로고    scopus 로고
    • Synaptic alterations in CA1 in mild Alzheimer's disease and mild cognitive impairment
    • Scheff SW, Price DA, Schmitt FA, DeKosky ST, Mufson EJ. Synaptic alterations in CA1 in mild Alzheimer's disease and mild cognitive impairment. Neurology 2007; 68: 1501-1508.
    • (2007) Neurology , vol.68 , pp. 1501-1508
    • Scheff, S.W.1    Price, D.A.2    Schmitt, F.A.3    Dekosky, S.T.4    Mufson, E.J.5
  • 66
    • 41149163183 scopus 로고    scopus 로고
    • Parkinson's disease: Clinical features and diagnosis
    • Jankovic J. Parkinson's disease: clinical features and diagnosis. J Neurol Neurosurg Psychiatry 2008; 79: 368-376.
    • (2008) J Neurol Neurosurg Psychiatry , vol.79 , pp. 368-376
    • Jankovic, J.1
  • 67
    • 0029942337 scopus 로고    scopus 로고
    • Histochemical detection of apoptosis in Parkinson's disease
    • Mochizuki H, Goto K, Mori H, Mizuno Y. Histochemical detection of apoptosis in Parkinson's disease. J Neurol Sci 1996; 137: 120-123.
    • (1996) J Neurol Sci , vol.137 , pp. 120-123
    • Mochizuki, H.1    Goto, K.2    Mori, H.3    Mizuno, Y.4
  • 69
    • 0031930771 scopus 로고    scopus 로고
    • Glial pathology but absence of apoptotic nigral neurons in long-standing Parkinson's disease
    • Banati RB, Daniel SE, Blunt SB. Glial pathology but absence of apoptotic nigral neurons in long-standing Parkinson's disease. Mov Disord 1998; 13: 221-227.
    • (1998) Mov Disord , vol.13 , pp. 221-227
    • Banati, R.B.1    Daniel, S.E.2    Blunt, S.B.3
  • 70
    • 12944250987 scopus 로고    scopus 로고
    • Caspase-3: A vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease
    • Hartmann A, Hunot S, Michel PP, Muriel MP, Vyas S, Faucheux BA et al. Caspase-3: a vulnerability factor and final effector in apoptotic death of dopaminergic neurons in Parkinson's disease. Proc Natl Acad Sci USA 2000; 97: 2875-2880.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2875-2880
    • Hartmann, A.1    Hunot, S.2    Michel, P.P.3    Muriel, M.P.4    Vyas, S.5    Faucheux, B.A.6
  • 72
    • 33846225133 scopus 로고    scopus 로고
    • Huntington's disease
    • Walker FO. Huntington's disease. Lancet 2007; 369: 218-228.
    • (2007) Lancet , vol.369 , pp. 218-228
    • Walker, F.O.1
  • 73
    • 0029040355 scopus 로고
    • In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes
    • Dragunow M, Faull RL, Lawlor P, Beilharz EJ, Singleton K, Walker EB et al. In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. Neuroreport 1995; 6: 1053-1057.
    • (1995) Neuroreport , vol.6 , pp. 1053-1057
    • Dragunow, M.1    Faull, R.L.2    Lawlor, P.3    Beilharz, E.J.4    Singleton, K.5
  • 74
    • 18544392423 scopus 로고    scopus 로고
    • Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila
    • Warrick JM, Paulson HL, Gray-Board GL, Bui QT, Fischbeck KH, Pittman RN et al. Expanded polyglutamine protein forms nuclear inclusions and causes neural degeneration in Drosophila. Cell 1998; 93: 939-949.
    • (1998) Cell , vol.93 , pp. 939-949
    • Warrick, J.M.1    Paulson, H.L.2    Gray-Board, G.L.3    Bui, Q.T.4    Fischbeck, K.H.5    Pittman, R.N.6
  • 75
    • 4544234691 scopus 로고    scopus 로고
    • Neuroprotective effects of M826, a reversible caspase-3 inhibitor, in the rat malonate model of Huntington's disease
    • Toulmond S, Tang K, Bureau Y, Ashdown H, Degen S, O'Donnell R et al. Neuroprotective effects of M826, a reversible caspase-3 inhibitor, in the rat malonate model of Huntington's disease. Br J Pharmacol 2004; 141: 689-697.
    • (2004) Br J Pharmacol , vol.141 , pp. 689-697
    • Toulmond, S.1    Tang, K.2    Bureau, Y.3    Ashdown, H.4    Degen, S.5    O'Donnell, R.6
  • 76
    • 0035978743 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis
    • Rowland LP, Shneider NA. Amyotrophic lateral sclerosis. N Engl J Med 2001; 344: 1688-1700.
    • (2001) N Engl J Med , vol.344 , pp. 1688-1700
    • Rowland, L.P.1    Shneider, N.A.2
  • 77
    • 0034647003 scopus 로고    scopus 로고
    • Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model
    • Li M, Ona VO, Guégan C, Chen M, Jackson-Lewis V, Andrews LJ et al. Functional role of caspase-1 and caspase-3 in an ALS transgenic mouse model. Science 2000; 288: 335-339.
    • (2000) Science , vol.288 , pp. 335-339
    • Li, M.1    Ona, V.O.2    Guégan, C.3    Chen, M.4    Jackson-Lewis, V.5    Andrews, L.J.6
  • 78
    • 0034610328 scopus 로고    scopus 로고
    • Caspase-1 and-3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis
    • Pasinelli P, Houseweart MK, Brown Jr RH, Cleveland DW. Caspase-1 and-3 are sequentially activated in motor neuron death in Cu,Zn superoxide dismutase-mediated familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 2000; 97: 13901-13906.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13901-13906
    • Pasinelli, P.1    Houseweart, M.K.2    Brown Jr., R.H.3    Cleveland, D.W.4
  • 79
    • 0035437866 scopus 로고    scopus 로고
    • Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis
    • Guégan C, Vila M, Rosoklija G, Hays AP, Przedborski S. Recruitment of the mitochondrial-dependent apoptotic pathway in amyotrophic lateral sclerosis. J Neurosci 2001; 21: 6569-6576.
    • (2001) J Neurosci , vol.21 , pp. 6569-6576
    • Guégan, C.1    Vila, M.2    Rosoklija, G.3    Hays, A.P.4    Przedborski, S.5
  • 80
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • DOI 10.1126/science.277.5325.559
    • Kostic V, Jackson-Lewis V, de Bilbao F, Dubois-Dauphin M, Przedborski S. Bcl-2: prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis. Science 1997; 277: 559-562. (Pubitemid 27369003)
    • (1997) Science , vol.277 , Issue.5325 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3    Dubois-Dauphin, M.4    Przedborski, S.5
  • 81
    • 0037007645 scopus 로고    scopus 로고
    • Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice
    • Zhu S, Stavrovskaya IG, Drozda M, Kim BY, Ona V, Li M et al. Minocycline inhibits cytochrome c release and delays progression of amyotrophic lateral sclerosis in mice. Nature 2002; 417: 74-78.
    • (2002) Nature , vol.417 , pp. 74-78
    • Zhu, S.1    Stavrovskaya, I.G.2    Drozda, M.3    Kim, B.Y.4    Ona, V.5    Li, M.6
  • 82
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 1998; 391: 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 83
    • 0035072953 scopus 로고    scopus 로고
    • Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK i
    • Coleman ML, Sahai EA, Yeo M, Bosch M, Dewar A, Olson MF. Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat Cell Biol 2001; 3: 339-345.
    • (2001) Nat Cell Biol , vol.3 , pp. 339-345
    • Coleman, M.L.1    Sahai, E.A.2    Yeo, M.3    Bosch, M.4    Dewar, A.5    Olson, M.F.6
  • 84
    • 0035964190 scopus 로고    scopus 로고
    • Caspase cleavage of MST1 promotes nuclear translocation and chromatin condensation
    • Ura S, Masuyama N, Graves JD, Gotoh Y. Caspase cleavage of MST1 promotes nuclear translocation and chromatin condensation. Proc Natl Acad Sci USA 2001; 98: 10148-10153.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10148-10153
    • Ura, S.1    Masuyama, N.2    Graves, J.D.3    Gotoh, Y.4
  • 85
    • 0031042902 scopus 로고    scopus 로고
    • Macromolecular substrates for the ICE-like proteases during apoptosis
    • Rosen A, Casciola-Rosen L. Macromolecular substrates for the ICE-like proteases during apoptosis. J Cell Biochem 1997; 64: 50-54.
    • (1997) J Cell Biochem , vol.64 , pp. 50-54
    • Rosen, A.1    Casciola-Rosen, L.2
  • 86
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: A searchable database of caspase substrates
    • Lüthi AU, Martin SJ. The CASBAH: a searchable database of caspase substrates. Cell Death Differ 2007; 14: 641-650.
    • (2007) Cell Death Differ , vol.14 , pp. 641-650
    • Lüthi, A.U.1    Martin, S.J.2
  • 87
    • 45449116322 scopus 로고    scopus 로고
    • The involvement of cell death and survival in neural tube defects: A distinct role for apoptosis and autophagy?
    • Cecconi F, Piacentini M, Fimia GM. The involvement of cell death and survival in neural tube defects: a distinct role for apoptosis and autophagy? Cell Death Differ 2008; 15: 1170-1177.
    • (2008) Cell Death Differ , vol.15 , pp. 1170-1177
    • Cecconi, F.1    Piacentini, M.2    Fimia, G.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.