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Volumn 28, Issue 35, 2009, Pages 3093-3096

Caspase-2: Killer, savior and safeguardemerging versatile roles for an ill-defined caspase

Author keywords

Apoptosis; Caspase; DNA repair; Tumor suppression

Indexed keywords

CASPASE 2;

EID: 69849101403     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2009.173     Document Type: Review
Times cited : (38)

References (24)
  • 1
    • 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. (2003). Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev Cell 4: 687-697.
    • (2003) Dev Cell , vol.4 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 3
    • 44149119740 scopus 로고    scopus 로고
    • Involvement of oxidative stress and caspase 2-mediated intrinsic pathway signaling in age-related increase in muscle cell apoptosis in mice
    • Braga M, Sinha Hikim AP, Datta S, Ferrini MG, Brown D, Kovacheva EL et al. (2008). Involvement of oxidative stress and caspase 2-mediated intrinsic pathway signaling in age-related increase in muscle cell apoptosis in mice. Apoptosis 13: 822-832.
    • (2008) Apoptosis , vol.13 , pp. 822-832
    • Braga, M.1    Sinha Hikim, A.P.2    Datta, S.3    Ferrini, M.G.4    Brown, D.5    Kovacheva, E.L.6
  • 4
    • 0037103295 scopus 로고    scopus 로고
    • Platelet formation is the consequence of caspase activation within megakaryocytes
    • De Botton S, Sabri S, Daugas E, Zermati Y, Guidotti JE, Hermine O et al. (2002). Platelet formation is the consequence of caspase activation within megakaryocytes. Blood 100: 1310-1317.
    • (2002) Blood , vol.100 , pp. 1310-1317
    • De Botton, S.1    Sabri, S.2    Daugas, E.3    Zermati, Y.4    Guidotti, J.E.5    Hermine, O.6
  • 5
    • 55949118522 scopus 로고    scopus 로고
    • Inactivation of effector caspases through nondegradative polyubiquitylation
    • Ditzel M, Broemer M, Tenev T, Bolduc C, Lee TV, Rigbolt KT et al. (2008). Inactivation of effector caspases through nondegradative polyubiquitylation. Mol Cell 32: 540-553.
    • (2008) Mol Cell , vol.32 , pp. 540-553
    • Ditzel, M.1    Broemer, M.2    Tenev, T.3    Bolduc, C.4    Lee, T.V.5    Rigbolt, K.T.6
  • 6
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H, Dixit VM. (1997). RAIDD is a new 'death' adaptor molecule. Nature 385: 86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 10
    • 0026763128 scopus 로고
    • Identification of a set of genes with developmentally down-regulated expression in the mouse brain
    • Kumar S, Tomooka Y, Noda M. (1992). Identification of a set of genes with developmentally down-regulated expression in the mouse brain. Biochem Biophys Res Commun 185: 1155-1161.
    • (1992) Biochem Biophys Res Commun , vol.185 , pp. 1155-1161
    • Kumar, S.1    Tomooka, Y.2    Noda, M.3
  • 12
    • 33745932874 scopus 로고    scopus 로고
    • Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis
    • Lavrik IN, Golks A, Baumann S, Krammer PH. (2006). Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis. Blood 108: 559-565.
    • (2006) Blood , vol.108 , pp. 559-565
    • Lavrik, I.N.1    Golks, A.2    Baumann, S.3    Krammer, P.H.4
  • 13
    • 54249096028 scopus 로고    scopus 로고
    • Caspases in apoptosis and beyond
    • Li J, Yuan J. (2008). Caspases in apoptosis and beyond. Oncogene 27: 6194-6206.
    • (2008) Oncogene , vol.27 , pp. 6194-6206
    • Li, J.1    Yuan, J.2
  • 15
    • 26244453715 scopus 로고    scopus 로고
    • Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2
    • Nutt LK, Margolis SS, Jensen M, Herman CE, Dunphy WG, Rathmell JC et al. (2005). Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2. Cell 123: 89-103.
    • (2005) Cell , vol.123 , pp. 89-103
    • Nutt, L.K.1    Margolis, S.S.2    Jensen, M.3    Herman, C.E.4    Dunphy, W.G.5    Rathmell, J.C.6
  • 17
    • 33846053961 scopus 로고    scopus 로고
    • Loss of caspase-9 reveals its essential role for caspase-2 activation and mitochondrial membrane depolarization
    • Samraj AK, Sohn D, Schulze-Osthoff K, Schmitz I. (2007). Loss of caspase-9 reveals its essential role for caspase-2 activation and mitochondrial membrane depolarization. Mol Biol Cell 18: 84-93.
    • (2007) Mol Biol Cell , vol.18 , pp. 84-93
    • Samraj, A.K.1    Sohn, D.2    Schulze-Osthoff, K.3    Schmitz, I.4
  • 18
    • 0346492579 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 do not act as tumor suppressors in myc-induced lymphomagenesis or mouse embryo fibroblast transformation
    • Scott CL, Schuler M, Marsden VS, Egle A, Pellegrini M, Nesic D et al. (2004). Apaf-1 and caspase-9 do not act as tumor suppressors in myc-induced lymphomagenesis or mouse embryo fibroblast transformation. J Cell Biol 164: 89-96.
    • (2004) J Cell Biol , vol.164 , pp. 89-96
    • Scott, C.L.1    Schuler, M.2    Marsden, V.S.3    Egle, A.4    Pellegrini, M.5    Nesic, D.6
  • 19
    • 59049093349 scopus 로고    scopus 로고
    • DNA-PKcs-PIDDosome: A nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance
    • Shi M, Vivian CJ, Lee KJ, Ge C, Morotomi-Yano K, Manzl C et al. (2009). DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance. Cell 136: 508-520.
    • (2009) Cell , vol.136 , pp. 508-520
    • Shi, M.1    Vivian, C.J.2    Lee, K.J.3    Ge, C.4    Morotomi-Yano, K.5    Manzl, C.6
  • 20
    • 44149090307 scopus 로고    scopus 로고
    • Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3
    • Sidi S, Sanda T, Kennedy RD, Hagen AT, Jette CA, Hoffmans R et al. (2008). Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3. Cell 133: 864-877.
    • (2008) Cell , vol.133 , pp. 864-877
    • Sidi, S.1    Sanda, T.2    Kennedy, R.D.3    Hagen, A.T.4    Jette, C.A.5    Hoffmans, R.6
  • 21
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A, Tschopp J. (2004). The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304: 843-846.
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 22
    • 58149464289 scopus 로고    scopus 로고
    • The Jekyll and Hyde functions of caspases
    • Yi CH, Yuan J. (2009). The Jekyll and Hyde functions of caspases. Dev Cell 16: 21-34.
    • (2009) Dev Cell , vol.16 , pp. 21-34
    • Yi, C.H.1    Yuan, J.2
  • 24
    • 33749572210 scopus 로고    scopus 로고
    • Carcinogenesis and apoptosis: Paradigms and paradoxes
    • Zhivotovsky B, Orrenius S. (2006). Carcinogenesis and apoptosis: paradigms and paradoxes. Carcinogenesis 27: 939-1945.
    • (2006) Carcinogenesis , vol.27 , pp. 939-1945
    • Zhivotovsky, B.1    Orrenius, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.