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Volumn 17, Issue 3, 2007, Pages 135-144

Nonapoptotic functions of caspases: caspases as regulatory molecules for immunity and cell-fate determination

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE;

EID: 33847367323     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2007.01.001     Document Type: Review
Times cited : (169)

References (80)
  • 1
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis H.M., and Horvitz H.R. Genetic control of programmed cell death in the nematode C. elegans. Cell 44 (1986) 817-829
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 2
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J., et al. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 75 (1993) 641-652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1
  • 3
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry N.A., et al. A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356 (1992) 768-774
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1
  • 4
    • 0026517239 scopus 로고
    • Molecular cloning of the interleukin-1 beta converting enzyme
    • Cerretti D.P., et al. Molecular cloning of the interleukin-1 beta converting enzyme. Science 256 (1992) 97-100
    • (1992) Science , vol.256 , pp. 97-100
    • Cerretti, D.P.1
  • 5
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura M., et al. Induction of apoptosis in fibroblasts by IL-1 β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 75 (1993) 653-660
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1
  • 6
    • 33646087420 scopus 로고    scopus 로고
    • The apoptosome: physiological, developmental, and pathological modes of regulation
    • Schafer Z.T., and Kornbluth S. The apoptosome: physiological, developmental, and pathological modes of regulation. Dev. Cell 10 (2006) 549-561
    • (2006) Dev. Cell , vol.10 , pp. 549-561
    • Schafer, Z.T.1    Kornbluth, S.2
  • 7
    • 10644288480 scopus 로고    scopus 로고
    • Drosophila caspase DRONC is required for specific developmental cell death pathways and stress-induced apoptosis
    • Daish T.J., et al. Drosophila caspase DRONC is required for specific developmental cell death pathways and stress-induced apoptosis. Dev. Cell 7 (2004) 909-915
    • (2004) Dev. Cell , vol.7 , pp. 909-915
    • Daish, T.J.1
  • 8
    • 10644290827 scopus 로고    scopus 로고
    • The apical caspase dronc governs programmed and unprogrammed cell death in Drosophila
    • Chew S.K., et al. The apical caspase dronc governs programmed and unprogrammed cell death in Drosophila. Dev. Cell 7 (2004) 897-907
    • (2004) Dev. Cell , vol.7 , pp. 897-907
    • Chew, S.K.1
  • 9
    • 19444366944 scopus 로고    scopus 로고
    • The CARD-carrying caspase Dronc is essential for most, but not all, developmental cell death in Drosophila
    • Xu D., et al. The CARD-carrying caspase Dronc is essential for most, but not all, developmental cell death in Drosophila. Development 132 (2005) 2125-2134
    • (2005) Development , vol.132 , pp. 2125-2134
    • Xu, D.1
  • 10
    • 21844449428 scopus 로고    scopus 로고
    • The Drosophila caspase DRONC is required for metamorphosis and cell death in response to irradiation and developmental signals
    • Waldhuber M., et al. The Drosophila caspase DRONC is required for metamorphosis and cell death in response to irradiation and developmental signals. Mech. Dev. 122 (2005) 914-927
    • (2005) Mech. Dev. , vol.122 , pp. 914-927
    • Waldhuber, M.1
  • 11
    • 33749173274 scopus 로고    scopus 로고
    • DRONC coordinates cell death and compensatory proliferation
    • Kondo S., et al. DRONC coordinates cell death and compensatory proliferation. Mol. Cell. Biol. 26 (2006) 7258-7268
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7258-7268
    • Kondo, S.1
  • 12
    • 33748676654 scopus 로고    scopus 로고
    • The effector caspases drICE and dcp-1 have partially overlapping functions in the apoptotic pathway in Drosophila
    • Xu D., et al. The effector caspases drICE and dcp-1 have partially overlapping functions in the apoptotic pathway in Drosophila. Cell Death Differ. 13 (2006) 1697-1706
    • (2006) Cell Death Differ. , vol.13 , pp. 1697-1706
    • Xu, D.1
  • 13
    • 33749392341 scopus 로고    scopus 로고
    • The Drosophila caspase Ice is important for many apoptotic cell deaths and for spermatid individualization, a nonapoptotic process
    • Muro I., et al. The Drosophila caspase Ice is important for many apoptotic cell deaths and for spermatid individualization, a nonapoptotic process. Development 133 (2006) 3305-3315
    • (2006) Development , vol.133 , pp. 3305-3315
    • Muro, I.1
  • 14
    • 0033193863 scopus 로고    scopus 로고
    • Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway
    • Rodriguez A., et al. Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway. Nat. Cell Biol. 1 (1999) 272-279
    • (1999) Nat. Cell Biol. , vol.1 , pp. 272-279
    • Rodriguez, A.1
  • 15
    • 0033231548 scopus 로고    scopus 로고
    • HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis
    • Zhou L., et al. HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis. Mol. Cell 4 (1999) 745-755
    • (1999) Mol. Cell , vol.4 , pp. 745-755
    • Zhou, L.1
  • 16
    • 0033231614 scopus 로고    scopus 로고
    • Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator
    • Kanuka H., et al. Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator. Mol. Cell 4 (1999) 757-769
    • (1999) Mol. Cell , vol.4 , pp. 757-769
    • Kanuka, H.1
  • 17
    • 33646696937 scopus 로고    scopus 로고
    • Autophagy occurs upstream or parallel to the apoptosome during histolytic cell death
    • Akdemir F., et al. Autophagy occurs upstream or parallel to the apoptosome during histolytic cell death. Development 133 (2006) 1457-1465
    • (2006) Development , vol.133 , pp. 1457-1465
    • Akdemir, F.1
  • 18
    • 33845510345 scopus 로고    scopus 로고
    • ARK, the Apaf-1 related killer in Drosophila, requires diverse domains for its apoptotic activity
    • Srivastava M., et al. ARK, the Apaf-1 related killer in Drosophila, requires diverse domains for its apoptotic activity. Cell Death Differ 14 (2006) 92-102
    • (2006) Cell Death Differ , vol.14 , pp. 92-102
    • Srivastava, M.1
  • 19
    • 33845483887 scopus 로고    scopus 로고
    • Caspases in cell survival, proliferation and differentiation
    • Lamkanfi M., et al. Caspases in cell survival, proliferation and differentiation. Cell Death Differ 14 (2006) 44-55
    • (2006) Cell Death Differ , vol.14 , pp. 44-55
    • Lamkanfi, M.1
  • 20
    • 33749131042 scopus 로고    scopus 로고
    • The inflammatory caspases: key players in the host response to pathogenic invasion and sepsis
    • Nadiri A., et al. The inflammatory caspases: key players in the host response to pathogenic invasion and sepsis. J. Immunol. 177 (2006) 4239-4245
    • (2006) J. Immunol. , vol.177 , pp. 4239-4245
    • Nadiri, A.1
  • 21
    • 3142654767 scopus 로고    scopus 로고
    • Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf
    • Mariathasan S., et al. Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf. Nature 430 (2004) 213-218
    • (2004) Nature , vol.430 , pp. 213-218
    • Mariathasan, S.1
  • 22
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon F., et al. Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440 (2006) 237-241
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1
  • 23
    • 32944470765 scopus 로고    scopus 로고
    • Cryopyrin activates the inflammasome in response to toxins and ATP
    • Mariathasan S., et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 440 (2006) 228-232
    • (2006) Nature , vol.440 , pp. 228-232
    • Mariathasan, S.1
  • 24
    • 33644985564 scopus 로고    scopus 로고
    • Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1
    • Sutterwala F.S., et al. Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive immunity through its regulation of caspase-1. Immunity 24 (2006) 317-327
    • (2006) Immunity , vol.24 , pp. 317-327
    • Sutterwala, F.S.1
  • 25
    • 33747191203 scopus 로고    scopus 로고
    • The inflammasome: first line of the immune response to cell stress
    • Ogura Y., et al. The inflammasome: first line of the immune response to cell stress. Cell 126 (2006) 659-662
    • (2006) Cell , vol.126 , pp. 659-662
    • Ogura, Y.1
  • 26
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L., et al. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126 (2006) 1135-1145
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1
  • 27
    • 0035956931 scopus 로고    scopus 로고
    • Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing
    • Aballay A., and Ausubel F.M. Programmed cell death mediated by ced-3 and ced-4 protects Caenorhabditis elegans from Salmonella typhimurium-mediated killing. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 2735-2739
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2735-2739
    • Aballay, A.1    Ausubel, F.M.2
  • 28
    • 33645239254 scopus 로고    scopus 로고
    • Restriction of vaccinia virus replication by a ced-3 and ced-4-dependent pathway in Caenorhabditis elegans
    • Liu W.H., et al. Restriction of vaccinia virus replication by a ced-3 and ced-4-dependent pathway in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4174-4179
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 4174-4179
    • Liu, W.H.1
  • 29
    • 20044396975 scopus 로고    scopus 로고
    • Regulators of the Toll and Imd pathways in the Drosophila innate immune response
    • Tanji T., and Ip Y.T. Regulators of the Toll and Imd pathways in the Drosophila innate immune response. Trends Immunol. 26 (2005) 193-198
    • (2005) Trends Immunol. , vol.26 , pp. 193-198
    • Tanji, T.1    Ip, Y.T.2
  • 30
    • 0038284956 scopus 로고    scopus 로고
    • Caspase-mediated processing of the Drosophila NF-kappaB factor Relish
    • Stoven S., et al. Caspase-mediated processing of the Drosophila NF-kappaB factor Relish. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5991-5996
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5991-5996
    • Stoven, S.1
  • 31
    • 27344453240 scopus 로고    scopus 로고
    • An RNA interference screen identifies Inhibitor of Apoptosis Protein 2 as a regulator of innate immune signalling in Drosophila
    • Gesellchen V., et al. An RNA interference screen identifies Inhibitor of Apoptosis Protein 2 as a regulator of innate immune signalling in Drosophila. EMBO Rep. 6 (2005) 979-984
    • (2005) EMBO Rep. , vol.6 , pp. 979-984
    • Gesellchen, V.1
  • 32
    • 27144475536 scopus 로고    scopus 로고
    • Inhibitor of apoptosis 2 and TAK1-binding protein are components of the Drosophila Imd pathway
    • Kleino A., et al. Inhibitor of apoptosis 2 and TAK1-binding protein are components of the Drosophila Imd pathway. EMBO J. 24 (2005) 3423-3434
    • (2005) EMBO J. , vol.24 , pp. 3423-3434
    • Kleino, A.1
  • 33
    • 18544383460 scopus 로고    scopus 로고
    • Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency
    • Chun H.J., et al. Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency. Nature 419 (2002) 395-399
    • (2002) Nature , vol.419 , pp. 395-399
    • Chun, H.J.1
  • 34
    • 0037380628 scopus 로고    scopus 로고
    • Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity
    • Salmena L., et al. Essential role for caspase 8 in T-cell homeostasis and T-cell-mediated immunity. Genes Dev. 17 (2003) 883-895
    • (2003) Genes Dev. , vol.17 , pp. 883-895
    • Salmena, L.1
  • 35
    • 25144480009 scopus 로고    scopus 로고
    • Caspase-8 deficiency in T cells leads to a lethal lymphoinfiltrative immune disorder
    • Salmena L., and Hakem R. Caspase-8 deficiency in T cells leads to a lethal lymphoinfiltrative immune disorder. J. Exp. Med. 202 (2005) 727-732
    • (2005) J. Exp. Med. , vol.202 , pp. 727-732
    • Salmena, L.1    Hakem, R.2
  • 36
    • 0035901969 scopus 로고    scopus 로고
    • Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27(KIP1) in transformed lymphoid cells
    • Frost V., et al. Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27(KIP1) in transformed lymphoid cells. Oncogene 20 (2001) 2737-2748
    • (2001) Oncogene , vol.20 , pp. 2737-2748
    • Frost, V.1
  • 37
    • 0142092617 scopus 로고    scopus 로고
    • Caspase-3 regulates cell cycle in B cells: a consequence of substrate specificity
    • Woo M., et al. Caspase-3 regulates cell cycle in B cells: a consequence of substrate specificity. Nat. Immunol. 4 (2003) 1016-1022
    • (2003) Nat. Immunol. , vol.4 , pp. 1016-1022
    • Woo, M.1
  • 38
    • 0030995511 scopus 로고    scopus 로고
    • Developmental parameters of cell death in the wing disc of Drosophila
    • Milan M., et al. Developmental parameters of cell death in the wing disc of Drosophila. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 5691-5696
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5691-5696
    • Milan, M.1
  • 39
    • 3342881896 scopus 로고    scopus 로고
    • Compensatory proliferation induced by cell death in the Drosophila wing disc requires activity of the apical cell death caspase Dronc in a nonapoptotic role
    • Huh J.R., et al. Compensatory proliferation induced by cell death in the Drosophila wing disc requires activity of the apical cell death caspase Dronc in a nonapoptotic role. Curr. Biol. 14 (2004) 1262-1266
    • (2004) Curr. Biol. , vol.14 , pp. 1262-1266
    • Huh, J.R.1
  • 40
    • 33747176844 scopus 로고    scopus 로고
    • Compensatory proliferation in Drosophila imaginal discs requires Dronc-dependent p53 activity
    • Wells B.S., et al. Compensatory proliferation in Drosophila imaginal discs requires Dronc-dependent p53 activity. Curr. Biol. 16 (2006) 1606-1615
    • (2006) Curr. Biol. , vol.16 , pp. 1606-1615
    • Wells, B.S.1
  • 41
    • 5044248528 scopus 로고    scopus 로고
    • Apoptotic cells can induce compensatory cell proliferation through the JNK and the Wingless signaling pathways
    • Ryoo H.D., et al. Apoptotic cells can induce compensatory cell proliferation through the JNK and the Wingless signaling pathways. Dev. Cell 7 (2004) 491-501
    • (2004) Dev. Cell , vol.7 , pp. 491-501
    • Ryoo, H.D.1
  • 42
    • 10344258000 scopus 로고    scopus 로고
    • Caspase inhibition during apoptosis causes abnormal signalling and developmental aberrations in Drosophila
    • Perez-Garijo A., et al. Caspase inhibition during apoptosis causes abnormal signalling and developmental aberrations in Drosophila. Development 131 (2004) 5591-5598
    • (2004) Development , vol.131 , pp. 5591-5598
    • Perez-Garijo, A.1
  • 43
    • 29144453339 scopus 로고    scopus 로고
    • Dpp signaling and the induction of neoplastic tumors by caspase-inhibited apoptotic cells in Drosophila
    • Perez-Garijo A., et al. Dpp signaling and the induction of neoplastic tumors by caspase-inhibited apoptotic cells in Drosophila. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17664-17669
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17664-17669
    • Perez-Garijo, A.1
  • 44
    • 0037114624 scopus 로고    scopus 로고
    • Specific involvement of caspases in the differentiation of monocytes into macrophages
    • Sordet O., et al. Specific involvement of caspases in the differentiation of monocytes into macrophages. Blood 100 (2002) 4446-4453
    • (2002) Blood , vol.100 , pp. 4446-4453
    • Sordet, O.1
  • 45
    • 4344560197 scopus 로고    scopus 로고
    • Caspase-8 serves both apoptotic and nonapoptotic roles
    • Kang T.B., et al. Caspase-8 serves both apoptotic and nonapoptotic roles. J. Immunol. 173 (2004) 2976-2984
    • (2004) J. Immunol. , vol.173 , pp. 2976-2984
    • Kang, T.B.1
  • 46
    • 33846922252 scopus 로고    scopus 로고
    • Caspase-8 prevents sustained activation of NF-{kappa}B in monocytes undergoing macrophagic differentiation
    • Rebe C., et al. Caspase-8 prevents sustained activation of NF-{kappa}B in monocytes undergoing macrophagic differentiation. Blood 109 (2007) 1442-1450
    • (2007) Blood , vol.109 , pp. 1442-1450
    • Rebe, C.1
  • 47
    • 0037143626 scopus 로고    scopus 로고
    • Caspase 3 activity is required for skeletal muscle differentiation
    • Fernando P., et al. Caspase 3 activity is required for skeletal muscle differentiation. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 11025-11030
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11025-11030
    • Fernando, P.1
  • 48
    • 1642433091 scopus 로고    scopus 로고
    • Syncytial fusion of human trophoblast depends on caspase 8
    • Black S., et al. Syncytial fusion of human trophoblast depends on caspase 8. Cell Death Differ. 11 (2004) 90-98
    • (2004) Cell Death Differ. , vol.11 , pp. 90-98
    • Black, S.1
  • 49
    • 85047689672 scopus 로고    scopus 로고
    • A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells
    • Miura M., et al. A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells. J. Clin. Invest. 114 (2004) 1704-1713
    • (2004) J. Clin. Invest. , vol.114 , pp. 1704-1713
    • Miura, M.1
  • 50
    • 11144356373 scopus 로고    scopus 로고
    • High commitment of embryonic keratinocytes to terminal differentiation through a Notch1-caspase 3 regulatory mechanism
    • Okuyama R., et al. High commitment of embryonic keratinocytes to terminal differentiation through a Notch1-caspase 3 regulatory mechanism. Dev. Cell 6 (2004) 551-562
    • (2004) Dev. Cell , vol.6 , pp. 551-562
    • Okuyama, R.1
  • 51
    • 33645847531 scopus 로고    scopus 로고
    • Bergmann glia utilize active caspase-3 for differentiation.
    • Oomman S., et al. Bergmann glia utilize active caspase-3 for differentiation. Brain Res. 1078 (2006) 19-34
    • (2006) Brain Res. , vol.1078 , pp. 19-34
    • Oomman, S.1
  • 52
    • 26444537963 scopus 로고    scopus 로고
    • Neural stem cell differentiation is dependent upon endogenous caspase 3 activity
    • Fernando P., et al. Neural stem cell differentiation is dependent upon endogenous caspase 3 activity. FASEB J. 19 (2005) 1671-1673
    • (2005) FASEB J. , vol.19 , pp. 1671-1673
    • Fernando, P.1
  • 53
    • 1642461401 scopus 로고    scopus 로고
    • Caspase activation independent of cell death is required for proper cell dispersal and correct morphology in PC12 cells
    • Rohn T.T., et al. Caspase activation independent of cell death is required for proper cell dispersal and correct morphology in PC12 cells. Exp. Cell Res. 295 (2004) 215-225
    • (2004) Exp. Cell Res. , vol.295 , pp. 215-225
    • Rohn, T.T.1
  • 54
    • 17444406677 scopus 로고    scopus 로고
    • Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems
    • Vaisid T., et al. Caspase-1 activity is required for neuronal differentiation of PC12 cells: cross-talk between the caspase and calpain systems. Biochim. Biophys. Acta 1743 (2005) 223-230
    • (2005) Biochim. Biophys. Acta , vol.1743 , pp. 223-230
    • Vaisid, T.1
  • 55
    • 27744511564 scopus 로고    scopus 로고
    • Drosophila caspase transduces Shaggy/GSK-3beta kinase activity in neural precursor development
    • Kanuka H., et al. Drosophila caspase transduces Shaggy/GSK-3beta kinase activity in neural precursor development. EMBO J. 24 (2005) 3793-3806
    • (2005) EMBO J. , vol.24 , pp. 3793-3806
    • Kanuka, H.1
  • 56
    • 33746570157 scopus 로고    scopus 로고
    • Drosophila IKK-related kinase regulates nonapoptotic function of caspases via degradation of IAPs
    • Kuranaga E., et al. Drosophila IKK-related kinase regulates nonapoptotic function of caspases via degradation of IAPs. Cell 126 (2006) 583-596
    • (2006) Cell , vol.126 , pp. 583-596
    • Kuranaga, E.1
  • 57
    • 33746363831 scopus 로고    scopus 로고
    • Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning
    • Kuo C.T., et al. Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning. Neuron 51 (2006) 283-290
    • (2006) Neuron , vol.51 , pp. 283-290
    • Kuo, C.T.1
  • 58
    • 0036300083 scopus 로고    scopus 로고
    • Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1
    • Ryoo H.D., et al. Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1. Nat. Cell Biol. 4 (2002) 432-438
    • (2002) Nat. Cell Biol. , vol.4 , pp. 432-438
    • Ryoo, H.D.1
  • 59
    • 33749000311 scopus 로고    scopus 로고
    • Local caspase activity directs engulfment of dendrites during pruning
    • Williams D.W., et al. Local caspase activity directs engulfment of dendrites during pruning. Nat Neurosci 9 (2006) 1234-1236
    • (2006) Nat Neurosci , vol.9 , pp. 1234-1236
    • Williams, D.W.1
  • 60
    • 19344368275 scopus 로고    scopus 로고
    • Multiple apoptotic caspase cascades are required in nonapoptotic roles for Drosophila spermatid individualization
    • Huh J.R., et al. Multiple apoptotic caspase cascades are required in nonapoptotic roles for Drosophila spermatid individualization. PLoS Biol. 2 (2004) E15
    • (2004) PLoS Biol. , vol.2
    • Huh, J.R.1
  • 61
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • Arama E., et al. Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev. Cell 4 (2003) 687-697
    • (2003) Dev. Cell , vol.4 , pp. 687-697
    • Arama, E.1
  • 62
    • 30444448684 scopus 로고    scopus 로고
    • The two Drosophila cytochrome C proteins can function in both respiration and caspase activation
    • Arama E., et al. The two Drosophila cytochrome C proteins can function in both respiration and caspase activation. EMBO J. 25 (2006) 232-243
    • (2006) EMBO J. , vol.25 , pp. 232-243
    • Arama, E.1
  • 63
    • 8444227809 scopus 로고    scopus 로고
    • The two cytochrome c species, DC3 and DC4, are not required for caspase activation and apoptosis in Drosophila cells
    • Dorstyn L., et al. The two cytochrome c species, DC3 and DC4, are not required for caspase activation and apoptosis in Drosophila cells. J. Cell Biol. 167 (2004) 405-410
    • (2004) J. Cell Biol. , vol.167 , pp. 405-410
    • Dorstyn, L.1
  • 64
    • 0037128923 scopus 로고    scopus 로고
    • The role of ARK in stress-induced apoptosis in Drosophila cells
    • Zimmermann K.C., et al. The role of ARK in stress-induced apoptosis in Drosophila cells. J. Cell Biol. 156 (2002) 1077-1087
    • (2002) J. Cell Biol. , vol.156 , pp. 1077-1087
    • Zimmermann, K.C.1
  • 65
    • 33749521656 scopus 로고    scopus 로고
    • Cytochrome c-d regulates developmental apoptosis in the Drosophila retina
    • Mendes C.S., et al. Cytochrome c-d regulates developmental apoptosis in the Drosophila retina. EMBO Rep. 7 (2006) 933-939
    • (2006) EMBO Rep. , vol.7 , pp. 933-939
    • Mendes, C.S.1
  • 66
    • 33749233824 scopus 로고    scopus 로고
    • Activation of Rho-associated coiled-coil protein kinase 1 (ROCK-1) by caspase-3 cleavage plays an essential role in cardiac myocyte apoptosis
    • Chang J., et al. Activation of Rho-associated coiled-coil protein kinase 1 (ROCK-1) by caspase-3 cleavage plays an essential role in cardiac myocyte apoptosis. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 14495-14500
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14495-14500
    • Chang, J.1
  • 67
    • 33646264300 scopus 로고    scopus 로고
    • Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions
    • Helfer B., et al. Caspase-8 promotes cell motility and calpain activity under nonapoptotic conditions. Cancer Res. 66 (2006) 4273-4278
    • (2006) Cancer Res. , vol.66 , pp. 4273-4278
    • Helfer, B.1
  • 68
    • 30144434107 scopus 로고    scopus 로고
    • Potentiation of neuroblastoma metastasis by loss of caspase-8
    • Stupack D.G., et al. Potentiation of neuroblastoma metastasis by loss of caspase-8. Nature 439 (2006) 95-99
    • (2006) Nature , vol.439 , pp. 95-99
    • Stupack, D.G.1
  • 69
    • 3142598843 scopus 로고    scopus 로고
    • A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration
    • Geisbrecht E.R., and Montell D.J. A role for Drosophila IAP1-mediated caspase inhibition in Rac-dependent cell migration. Cell 118 (2004) 111-125
    • (2004) Cell , vol.118 , pp. 111-125
    • Geisbrecht, E.R.1    Montell, D.J.2
  • 70
    • 33746574519 scopus 로고    scopus 로고
    • IKK epsilon regulates F actin assembly and interacts with Drosophila IAP1 in cellular morphogenesis
    • Oshima K., et al. IKK epsilon regulates F actin assembly and interacts with Drosophila IAP1 in cellular morphogenesis. Curr. Biol. 16 (2006) 1531-1537
    • (2006) Curr. Biol. , vol.16 , pp. 1531-1537
    • Oshima, K.1
  • 71
    • 4644350173 scopus 로고    scopus 로고
    • Role of programmed cell death in patterning the Drosophila antennal arista
    • Cullen K., and McCall K. Role of programmed cell death in patterning the Drosophila antennal arista. Dev. Biol. 275 (2004) 82-92
    • (2004) Dev. Biol. , vol.275 , pp. 82-92
    • Cullen, K.1    McCall, K.2
  • 72
    • 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 (2006) 1179-1191
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1
  • 73
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation
    • Gervais F.G., et al. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation. Cell 97 (1999) 395-406
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1
  • 74
    • 0036166263 scopus 로고    scopus 로고
    • Cell death induced by a caspase-cleaved transmembrane fragment of the Alzheimer amyloid precursor protein
    • Nishimura I., et al. Cell death induced by a caspase-cleaved transmembrane fragment of the Alzheimer amyloid precursor protein. Cell Death Differ. 9 (2002) 199-208
    • (2002) Cell Death Differ. , vol.9 , pp. 199-208
    • Nishimura, I.1
  • 75
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin T.C., et al. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 10032-10037
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1
  • 76
    • 0037192850 scopus 로고    scopus 로고
    • Nicotine preconditioning antagonizes activity-dependent caspase proteolysis of a glutamate receptor
    • Meyer E.L., et al. Nicotine preconditioning antagonizes activity-dependent caspase proteolysis of a glutamate receptor. J. Biol. Chem. 277 (2002) 10869-10875
    • (2002) J. Biol. Chem. , vol.277 , pp. 10869-10875
    • Meyer, E.L.1
  • 77
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β
    • Martinon F., et al. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-β. Mol. Cell 10 (2002) 417-426
    • (2002) Mol. Cell , vol.10 , pp. 417-426
    • Martinon, F.1
  • 78
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T., and Akira S. Innate immune recognition of viral infection. Nat. Immunol. 7 (2006) 131-137
    • (2006) Nat. Immunol. , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 79
    • 0034280126 scopus 로고    scopus 로고
    • Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer
    • Tyas L., et al. Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer. EMBO Rep. 1 (2000) 266-270
    • (2000) EMBO Rep. , vol.1 , pp. 266-270
    • Tyas, L.1
  • 80
    • 0037455553 scopus 로고    scopus 로고
    • Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects
    • Takemoto K., et al. Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects. J. Cell Biol. 160 (2003) 235-243
    • (2003) J. Cell Biol. , vol.160 , pp. 235-243
    • Takemoto, K.1


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