메뉴 건너뛰기




Volumn 443, Issue 7113, 2006, Pages 796-802

Cell death in the nervous system

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; DISEASES; DRUG THERAPY;

EID: 33750292972     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05293     Document Type: Review
Times cited : (533)

References (80)
  • 2
    • 0013982846 scopus 로고
    • The nerve growth factor: Its mode of action on sensory and sympathetic nerve cells
    • Levi-Montalcini, R. The nerve growth factor: its mode of action on sensory and sympathetic nerve cells. Harvey Lect. 60, 217-259 (1966).
    • (1966) Harvey Lect. , vol.60 , pp. 217-259
    • Levi-Montalcini, R.1
  • 3
    • 0000031083 scopus 로고
    • Programmed cell death. II. Endocrine potentiation of the breakdown of the intersegmental muscles of silkmoths
    • Lockshin, R. A. & Williams, C. M. Programmed cell death. II. Endocrine potentiation of the breakdown of the intersegmental muscles of silkmoths. J. Insect Physiol. 10, 643-649 (1964).
    • (1964) J. Insect Physiol. , vol.10 , pp. 643-649
    • Lockshin, R.A.1    Williams, C.M.2
  • 4
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J. F., Wyllie, A. H. & Currie, A. R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257 (1972).
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 5
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke, P. G. Developmental cell death: morphological diversity and multiple mechanisms. Anat. Embryol. 181, 195-213 (1990).
    • (1990) Anat. Embryol. , vol.181 , pp. 195-213
    • Clarke, P.G.1
  • 6
    • 0020004194 scopus 로고
    • Naturally occurring neuron death and its regulation by developing neural pathways
    • Cunningham, T. J. Naturally occurring neuron death and its regulation by developing neural pathways. Int. Rev. Cytol. 74, 163-186 (1982).
    • (1982) Int. Rev. Cytol. , vol.74 , pp. 163-186
    • Cunningham, T.J.1
  • 7
    • 0027946294 scopus 로고
    • Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis
    • Dal Canto, M. C. & Gurney, M. E. Development of central nervous system pathology in a murine transgenic model of human amyotrophic lateral sclerosis. Am. J. Pathol. 145, 1271-1279 (1994).
    • (1994) Am. J. Pathol. , vol.145 , pp. 1271-1279
    • Dal Canto, M.C.1    Gurney, M.E.2
  • 8
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • Schweichel, J. U. & Merker, H. J. The morphology of various types of cell death in prenatal tissues. Teratology 7, 253-266 (1973).
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 9
    • 0034687754 scopus 로고    scopus 로고
    • An alternative, non-apoptotic form of programmed cell death
    • Sperandio, S., de Belle, I. & Bredesen, D. E. An alternative, non-apoptotic form of programmed cell death. Proc. Natl Acad. Sci. USA 97, 14376-14381 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14376-14381
    • Sperandio, S.1    De Belle, I.2    Bredesen, D.E.3
  • 10
    • 0022354769 scopus 로고
    • Naturally occurring cell death during neural development
    • Oppenheim, R. W. Naturally occurring cell death during neural development. Trends Neurosci. 17, 487-493 (1985).
    • (1985) Trends Neurosci. , vol.17 , pp. 487-493
    • Oppenheim, R.W.1
  • 11
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V. A. et al. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148, 2207-2216 (1992).
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1
  • 12
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N. A. & Lazebnik, Y. Caspases: enemies within. Science 281, 1312-1316 (1998).
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 13
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • Yuan, J., Shaham, S., Ledoux, S., Ellis, H. M. & Horvitz, H. R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75, 641-652 (1993).
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 14
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G. S. & Dixit, V. M. Caspases: intracellular signaling by proteolysis. Cell 91, 443-446 (1997).
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 15
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima, N., Nakanishi, K., Takenouchi, H., Shibata, T. & Yasuhiko, Y. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J. Biol. Chem. 277, 34287-34294 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 16
    • 0037077254 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway
    • Rao, R. V. et al. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway. J. Biol. Chem. 277, 21836-21842 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 21836-21842
    • Rao, R.V.1
  • 17
    • 0033145416 scopus 로고    scopus 로고
    • Caspase activity sows the seeds of neuronal death
    • Yuan, J. & Yankner, B. A. Caspase activity sows the seeds of neuronal death. Nature Cell Biol. 1, E44-E45 (1999).
    • (1999) Nature Cell Biol. , vol.1
    • Yuan, J.1    Yankner, B.A.2
  • 18
    • 26444434342 scopus 로고    scopus 로고
    • Pharmacological manipulation of cell death: Clinical applications in sight?
    • Green, D. R. & Kroemer, G. Pharmacological manipulation of cell death: clinical applications in sight? J. Clin. Invest. 115, 2610-2617 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 2610-2617
    • Green, D.R.1    Kroemer, G.2
  • 19
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior, P. & Salvesen, G. S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384, 201-232 (2004).
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 21
    • 0037077040 scopus 로고    scopus 로고
    • Toxic proteins in neurodegenerative disease
    • Taylor, J. P., Hardy, J. & Fischbeck, K. H. Toxic proteins in neurodegenerative disease. Science 296, 1991-1995 (2002).
    • (2002) Science , vol.296 , pp. 1991-1995
    • Taylor, J.P.1    Hardy, J.2    Fischbeck, K.H.3
  • 22
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia, R. & Braakman, I. Quality control in the endoplasmic reticulum protein factory. Nature 426, 891-894 (2003).
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 23
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman, M. Y. & Goldberg, A. L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 29, 15-32 (2001).
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 24
    • 7744232493 scopus 로고    scopus 로고
    • Misfolded proteins, endoplasmic reticulum stress and neurodegeneration
    • Rao, R. V. & Bredesen, D. E. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration. Curr. Opin. Cell Biol. 16, 653-662 (2004).
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 653-662
    • Rao, R.V.1    Bredesen, D.E.2
  • 25
    • 0037418843 scopus 로고    scopus 로고
    • 2+: A control point for apoptosis
    • 2+: a control point for apoptosis. Science 300, 135-139 (2003).
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1
  • 26
    • 17644371025 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK control multiple initiator caspases
    • Ruiz-Vela, A., Opferman, J. T., Cheng, E. H. & Korsmeyer, S. J. Proapoptotic BAX and BAK control multiple initiator caspases. EMBO Rep. 6, 379-385 (2005).
    • (2005) EMBO Rep. , vol.6 , pp. 379-385
    • Ruiz-Vela, A.1    Opferman, J.T.2    Cheng, E.H.3    Korsmeyer, S.J.4
  • 27
    • 4143087106 scopus 로고    scopus 로고
    • BI-1 regulates an apoptosis pathway linked to endoplasmic reticulum stress
    • Chae, H. J. et al. BI-1 regulates an apoptosis pathway linked to endoplasmic reticulum stress. Mol. Cell 15, 355-366 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 355-366
    • Chae, H.J.1
  • 28
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: Multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • Li, J., Lee, B. & Lee, A. S. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J. Biol. Chem. 281, 7260-7270 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 29
    • 0032488777 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein in neurodegenerative disease
    • Hegde, R. S. et al. A transmembrane form of the prion protein in neurodegenerative disease. Science 279, 827-834 (1998).
    • (1998) Science , vol.279 , pp. 827-834
    • Hegde, R.S.1
  • 30
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: An innocent convict?
    • Levine, B. & Yuan, J. Autophagy in cell death: an innocent convict? J. Clin. Invest. 115, 2679-2688 (2005).
    • (2005) J. Clin. Invest. , vol.115 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 31
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice
    • Komatsu, M. et al. Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J. Cell Biol. 169, 425-434 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 425-434
    • Komatsu, M.1
  • 32
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • Yue, Z., Jin, S., Yang, C., Levine, A. J. & Heintz, N. Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc. Natl Acad. Sci. USA 100, 15077-15082 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 33
    • 10344262564 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
    • Shimizu, S. et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nature Cell Biol. 6, 1221-1228 (2004).
    • (2004) Nature Cell Biol. , vol.6 , pp. 1221-1228
    • Shimizu, S.1
  • 34
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • Yu, L. et al. Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science 304, 1500-1502 (2004).
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1
  • 35
    • 33645521571 scopus 로고    scopus 로고
    • Autophagic programmed cell death by selective catalase degradation
    • Yu, L. et al. Autophagic programmed cell death by selective catalase degradation. Proc. Natl Acad. Sci. USA 103, 4952-4957 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4952-4957
    • Yu, L.1
  • 36
    • 0043173825 scopus 로고    scopus 로고
    • Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY5Y cells
    • Gomez-Santos, C. et al. Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY5Y cells. J. Neurosci. Res. 73, 341-350 (2003).
    • (2003) J. Neurosci. Res. , vol.73 , pp. 341-350
    • Gomez-Santos, C.1
  • 37
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M. O. The biochemistry of apoptosis. Nature 407, 770-776 (2000).
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 38
    • 5044249067 scopus 로고    scopus 로고
    • Paraptosis: Mediation by MAP kinases and inhibition by AIP-1/Alix
    • Sperandio, S. et al. Paraptosis: mediation by MAP kinases and inhibition by AIP-1/Alix. Cell Death Differ. 11, 1066-1075 (2004).
    • (2004) Cell Death Differ. , vol.11 , pp. 1066-1075
    • Sperandio, S.1
  • 39
    • 0029065517 scopus 로고
    • Potentiated necrosis of cultured cortical neurons by neurotrophins
    • Koh, J. Y., Gwag, B. J., Lobner, D. & Choi, D. W. Potentiated necrosis of cultured cortical neurons by neurotrophins. Science 268, 573-575 (1995).
    • (1995) Science , vol.268 , pp. 573-575
    • Koh, J.Y.1    Gwag, B.J.2    Lobner, D.3    Choi, D.W.4
  • 40
    • 0033988744 scopus 로고    scopus 로고
    • Aponecrosis: Morphological and biochemical exploration of a syncretic process of cell death sharing apoptosis and necrosis
    • Formigli, L. et al. Aponecrosis: morphological and biochemical exploration of a syncretic process of cell death sharing apoptosis and necrosis. J. Cell Physiol. 182, 41-49 (2000).
    • (2000) J. Cell Physiol. , vol.182 , pp. 41-49
    • Formigli, L.1
  • 41
    • 0028793257 scopus 로고
    • Glutamate-induced neuronal death: A succession of necrosis or apoptosis depending on mitochondrial function
    • Ankarcrona, M. et al. Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function. Neuron 15, 961-973 (1995).
    • (1995) Neuron , vol.15 , pp. 961-973
    • Ankarcrona, M.1
  • 42
    • 0037206901 scopus 로고    scopus 로고
    • Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
    • Syntichaki, P., Xu, K., Driscoll, M. & Tavernarakis, N. Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans. Nature 419, 939-944 (2002).
    • (2002) Nature , vol.419 , pp. 939-944
    • Syntichaki, P.1    Xu, K.2    Driscoll, M.3    Tavernarakis, N.4
  • 43
    • 0037067317 scopus 로고    scopus 로고
    • Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor
    • Yu, S. W. et al. Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science 297, 259-263 (2002).
    • (2002) Science , vol.297 , pp. 259-263
    • Yu, S.W.1
  • 44
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin, S. A. et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 397, 441-446 (1999).
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 46
    • 33646480747 scopus 로고    scopus 로고
    • Reversal of Alzheimer's-like pathology and behavior in human APP transgenic mice by mutation of Asp664
    • Galvan, V. et al. Reversal of Alzheimer's-like pathology and behavior in human APP transgenic mice by mutation of Asp664. Proc. Natl Acad. Sci. USA 103, 7130-7135 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7130-7135
    • Galvan, V.1
  • 47
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham, R. K. et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 125, 1179-1191 (2006).
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1
  • 48
    • 0031930313 scopus 로고    scopus 로고
    • Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease
    • Yang, F. et al. Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease. Am. J. Pathol. 152, 379-389 (1998).
    • (1998) Am. J. Pathol. , vol.152 , pp. 379-389
    • Yang, F.1
  • 50
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • Ona, V. O. et al. Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature 399, 263-267 (1999).
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1
  • 51
    • 0030756459 scopus 로고    scopus 로고
    • Bcl-2: Prolonging life in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • 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 277, 559-562 (1997).
    • (1997) Science , vol.277 , pp. 559-562
    • Kostic, V.1    Jackson-Lewis, V.2    De Bilbao, F.3    Dubois-Dauphin, M.4    Przedborski, S.5
  • 52
    • 0037417220 scopus 로고    scopus 로고
    • Apoptosis and caspases in neurodegenerative diseases
    • Friedlander, R. M. Apoptosis and caspases in neurodegenerative diseases. N. Engl. J. Med. 348, 1365-1375 (2003).
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1365-1375
    • Friedlander, R.M.1
  • 53
    • 29144517660 scopus 로고    scopus 로고
    • FGF-2 promotes neurogenesis and neuroprotection and prolongs survival in a transgenic mouse model of Huntington's disease
    • Jin, K. et al. FGF-2 promotes neurogenesis and neuroprotection and prolongs survival in a transgenic mouse model of Huntington's disease. Proc. Natl Acad. Sci. USA 102, 18189-18194 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18189-18194
    • Jin, K.1
  • 54
    • 21044458854 scopus 로고    scopus 로고
    • A phase 1 clinical trial of nerve growth factor gene therapy for Alzheimer disease
    • Tuszynski, M. H. et al. A phase 1 clinical trial of nerve growth factor gene therapy for Alzheimer disease. Nature Med. 11, 551-555 (2005).
    • (2005) Nature Med. , vol.11 , pp. 551-555
    • Tuszynski, M.H.1
  • 55
    • 33644833272 scopus 로고    scopus 로고
    • Randomized controlled trial of intraputamenal glial cell line-derived neurotrophic factor infusion in Parkinson disease
    • Lang, A. E. et al. Randomized controlled trial of intraputamenal glial cell line-derived neurotrophic factor infusion in Parkinson disease. Ann. Neurol. 59, 459-466 (2006).
    • (2006) Ann. Neurol. , vol.59 , pp. 459-466
    • Lang, A.E.1
  • 56
    • 0032826920 scopus 로고    scopus 로고
    • Cellular delivery of trophic factors for the treatment of Huntington's disease: Is neuroprotection possible?
    • Kordower, J. H., Isacson, O. & Emerich, D. F. Cellular delivery of trophic factors for the treatment of Huntington's disease: is neuroprotection possible? Exp. Neurol. 159, 4-20 (1999).
    • (1999) Exp. Neurol. , vol.159 , pp. 4-20
    • Kordower, J.H.1    Isacson, O.2    Emerich, D.F.3
  • 57
    • 33646421164 scopus 로고    scopus 로고
    • Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase
    • Borrell-Pages, M. et al. Cystamine and cysteamine increase brain levels of BDNF in Huntington disease via HSJ1b and transglutaminase. J. Clin. Invest. 116, 1410-1424 (2006).
    • (2006) J. Clin. Invest. , vol.116 , pp. 1410-1424
    • Borrell-Pages, M.1
  • 58
    • 0004137722 scopus 로고
    • (eds Tomei, L. D. & Cope, F. O.) (Cold Spring Harbor Laboratory Press, Plainview, New York)
    • Kerr, J. F. R. & Harmon, B. V. in Apoptosis: The Molecular Basis of Cell Death (eds Tomei, L. D. & Cope, F. O.) 321 (Cold Spring Harbor Laboratory Press, Plainview, New York, 1991).
    • (1991) Apoptosis: The Molecular Basis of Cell Death , pp. 321
    • Kerr, J.F.R.1    Harmon, B.V.2
  • 59
    • 0034012322 scopus 로고    scopus 로고
    • Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments
    • Bursch, W. et al. Autophagic and apoptotic types of programmed cell death exhibit different fates of cytoskeletal filaments. J. Cell Sci. 113, 1189-1198 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 1189-1198
    • Bursch, W.1
  • 60
    • 0030893167 scopus 로고    scopus 로고
    • The cytotoxicity of 1-(phenylmethyl)-4,7,10-tris-[(4′methylphenyl) sulfonyl]-1,4,7,10-tetraazacyclododecane in human Tmolt3 T leukemic cells
    • Hall, I. H., Elkins, A. L., Karthikeyan, S. & Spielvogel, B. F. The cytotoxicity of 1-(phenylmethyl)-4,7,10-tris-[(4′methylphenyl) sulfonyl]-1,4,7,10-tetraazacyclododecane in human Tmolt3 T leukemic cells. Anticancer Res. 17, 1195-1198 (1997).
    • (1997) Anticancer Res. , vol.17 , pp. 1195-1198
    • Hall, I.H.1    Elkins, A.L.2    Karthikeyan, S.3    Spielvogel, B.F.4
  • 61
    • 0034698733 scopus 로고    scopus 로고
    • Two distinct pathways leading to nuclear apoptosis
    • Susin, S. A. et al. Two distinct pathways leading to nuclear apoptosis. J. Exp. Med. 192, 571-580 (2000).
    • (2000) J. Exp. Med. , vol.192 , pp. 571-580
    • Susin, S.A.1
  • 62
    • 0032491172 scopus 로고    scopus 로고
    • 'Apoptotic' myocytes in infarct area in rabbit hearts may be oncotic myocytes with DNA fragmentation: Analysis by immunogold electron microscopy combined with in situ nick end-labeling
    • Ohno, M. et al. 'Apoptotic' myocytes in infarct area in rabbit hearts may be oncotic myocytes with DNA fragmentation: analysis by immunogold electron microscopy combined with in situ nick end-labeling. Circulation 98, 1422-1430 (1998).
    • (1998) Circulation , vol.98 , pp. 1422-1430
    • Ohno, M.1
  • 63
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio, M. et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 85, 817-827 (1996).
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 64
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana, T. et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 111, 331-342 (2002).
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1
  • 65
    • 0038485614 scopus 로고    scopus 로고
    • Humanin peptide suppresses apoptosis by interfering with Bax activation
    • Guo, B. et al. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature 423, 456-461 (2003).
    • (2003) Nature , vol.423 , pp. 456-461
    • Guo, B.1
  • 66
    • 0034629291 scopus 로고    scopus 로고
    • p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Schuler, M., Bossy-Wetzel, E., Goldstein, J. C., Fitzgerald, P. & Green, D. R. p53 induces apoptosis by caspase activation through mitochondrial cytochrome c release. J. Biol. Chem. 275, 7337-7342 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 7337-7342
    • Schuler, M.1    Bossy-Wetzel, E.2    Goldstein, J.C.3    Fitzgerald, P.4    Green, D.R.5
  • 67
    • 1342306819 scopus 로고    scopus 로고
    • Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3
    • Lin, B. et al. Conversion of Bcl-2 from protector to killer by interaction with nuclear orphan receptor Nur77/TR3. Cell 116, 527-540 (2004).
    • (2004) Cell , vol.116 , pp. 527-540
    • Lin, B.1
  • 68
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux, Q. L., Takahashi, R., Salvesen, G. S. & Reed, J. C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388, 300-304 (1997).
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 69
    • 0036303143 scopus 로고    scopus 로고
    • Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition
    • Holley, C. L., Olson, M. R., Colon-Ramos, D. A. & Kornbluth, S. Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition. Nature Cell Biol. 4, 439-444 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 439-444
    • Holley, C.L.1    Olson, M.R.2    Colon-Ramos, D.A.3    Kornbluth, S.4
  • 70
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L. & Wang, X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42 (2000).
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 71
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen, A. M. et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102, 43-53 (2000).
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1
  • 72
    • 0037016707 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif
    • Martins, L. M. et al. The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif. J. Biol. Chem. 277, 439-444 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 439-444
    • Martins, L.M.1
  • 74
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee, Y. J., Jeong, S. Y., Karbowski, M., Smith, C. L. & Youle, R. J. Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol. Biol. Cell. 15, 5001-5011 (2004).
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 75
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza, C. et al. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126, 177-189 (2006).
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1
  • 76
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat, S. et al. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 126, 163-175 (2006).
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1
  • 77
    • 0030705234 scopus 로고    scopus 로고
    • p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
    • Ng, F. W. et al. p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum. J. Cell Biol. 139, 327-338 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 327-338
    • Ng, F.W.1
  • 78
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge, D. G., Stojanovic, M., Marcellus, R. C. & Shore, G. C. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J. Cell Biol. 160, 1115-1127 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 79
    • 0141893377 scopus 로고    scopus 로고
    • Bifunctional apoptosis inhibitor (BAR) protects neurons from diverse cell death pathways
    • Roth, W. et al. Bifunctional apoptosis inhibitor (BAR) protects neurons from diverse cell death pathways. Cell Death Differ. 10, 1178-1187 (2003).
    • (2003) Cell Death Differ. , vol.10 , pp. 1178-1187
    • Roth, W.1
  • 80
    • 32544461105 scopus 로고    scopus 로고
    • Alix, making a link between apoptosis-linked gene-2, the endosomal sorting complexes required for transport, and neuronal death in vivo
    • Mahul-Mellier, A. L., Hemming, F. J., Blot, B., Fraboulet, S. & Sadoul, R. Alix, making a link between apoptosis-linked gene-2, the endosomal sorting complexes required for transport, and neuronal death in vivo. J. Neurosci. 26, 542-549 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 542-549
    • Mahul-Mellier, A.L.1    Hemming, F.J.2    Blot, B.3    Fraboulet, S.4    Sadoul, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.