메뉴 건너뛰기




Volumn 16, Issue 2, 2009, Pages 195-207

The enigma of caspase-2: The laymen's view

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CASPASE 2; CASPASE 8; CASPASE RECRUITMENT DOMAIN SIGNALING PROTEIN; CRADD PROTEIN; CYCLIN D2; DNA; PROTEIN BCL 2; PROTEIN BCL XL; PROTEIN P53; PROTEIN UBC9; SUMO PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED DEATH DOMAIN PROTEIN;

EID: 58249101029     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2008.170     Document Type: Review
Times cited : (111)

References (119)
  • 2
    • 0032555716 scopus 로고    scopus 로고
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-490.
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-490.
  • 3
    • 3142581992 scopus 로고    scopus 로고
    • Requirement for aspartate-cleaved bid in apoptosis signaling by DNA-damaging anti-cancer regimens
    • Werner AB, Tait SW, de Vries E, Eldering E, Borst J. Requirement for aspartate-cleaved bid in apoptosis signaling by DNA-damaging anti-cancer regimens. J Biol Chem 2004; 279: 28771-28780.
    • (2004) J Biol Chem , vol.279 , pp. 28771-28780
    • Werner, A.B.1    Tait, S.W.2    de Vries, E.3    Eldering, E.4    Borst, J.5
  • 4
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 1993; 75: 641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 5
    • 0028168593 scopus 로고
    • Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death
    • Wang L, Miura M, Bergeron L, Zhu H, Yuan J. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 1994; 78: 739-750.
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 6
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme
    • Kumar S, Kinoshita M, Noda M, Copeland NG, Jenkins NA. Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme. Genes Dev 1994; 8: 1613-1626.
    • (1994) Genes Dev , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 7
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry NA, Rano TA, Peterson EP, Rasper DM, Timkey T, Garcia-Calvo M et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 1997; 272: 17907-17911.
    • (1997) J Biol Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5    Garcia-Calvo, M.6
  • 8
    • 0032549652 scopus 로고    scopus 로고
    • Dimerization and autoprocessing of the Nedd2 (caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions
    • Butt AJ, Harvey NL, Parasivam G, Kumar S. Dimerization and autoprocessing of the Nedd2 (caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions. J Biol Chem 1998; 273: 6763-6768.
    • (1998) J Biol Chem , vol.273 , pp. 6763-6768
    • Butt, A.J.1    Harvey, N.L.2    Parasivam, G.3    Kumar, S.4
  • 9
    • 8844224859 scopus 로고    scopus 로고
    • The biochemical mechanism of caspase-2 activation
    • Baliga BC, Read SH, Kumar S. The biochemical mechanism of caspase-2 activation. Cell Death Differ 2004; 11: 1234-1241.
    • (2004) Cell Death Differ , vol.11 , pp. 1234-1241
    • Baliga, B.C.1    Read, S.H.2    Kumar, S.3
  • 10
    • 0142242170 scopus 로고    scopus 로고
    • Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway
    • Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem 2003; 278: 42441-42447.
    • (2003) J Biol Chem , vol.278 , pp. 42441-42447
    • Schweizer, A.1    Briand, C.2    Grutter, M.G.3
  • 11
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • Riedl SJ, Salvesen GS. The apoptosome: Signalling platform of cell death. Nat Rev Mol Cell Biol 2007; 8: 405-413.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 12
    • 37849033506 scopus 로고    scopus 로고
    • Biochemical analysis of the native TRAIL death-inducing signaling complex
    • Walczak H, Haas TL. Biochemical analysis of the native TRAIL death-inducing signaling complex. Methods Mol Biol 2008; 414 221-239.
    • (2008) Methods Mol Biol , vol.414 , pp. 221-239
    • Walczak, H.1    Haas, T.L.2
  • 13
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • Stennicke HR, Salvesen GS. Biochemical characteristics of caspases-3, -6, -7, and -8. J Biol Chem 1997; 272: 25719-25723.
    • (1997) J Biol Chem , vol.272 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 14
    • 0032500552 scopus 로고    scopus 로고
    • Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain
    • Colussi PA, Harvey NL, Shearwin-Whyatt LM, Kumar S. Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain. J Biol Chem 1998; 273: 26566-26570.
    • (1998) J Biol Chem , vol.273 , pp. 26566-26570
    • Colussi, P.A.1    Harvey, N.L.2    Shearwin-Whyatt, L.M.3    Kumar, S.4
  • 15
    • 0032785022 scopus 로고    scopus 로고
    • Van de Craen M, Declercq W, Van den brande I, Fiers W, Vandenabeele P. The proteolytic procaspase activation network: An in vitro analysis. Cell Death Differ 1999; 6: 1117-1124.
    • Van de Craen M, Declercq W, Van den brande I, Fiers W, Vandenabeele P. The proteolytic procaspase activation network: An in vitro analysis. Cell Death Differ 1999; 6: 1117-1124.
  • 17
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • Henderson C, Mizzau M, Paroni G, Maestro R, Schneider C, Brancolini C. Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J Biol Chem 2003; 278: 12579-12589.
    • (2003) J Biol Chem , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 18
    • 8844254088 scopus 로고    scopus 로고
    • Regulation of procaspase-2 by glucocorticoid modulatory element-binding protein 1 through the interaction with caspase recruitment domain
    • Tsuruma K, Nakagawa T, Shirakura H, Hayashi N, Uehara T, Nomura Y. Regulation of procaspase-2 by glucocorticoid modulatory element-binding protein 1 through the interaction with caspase recruitment domain. Biochem Biophys Res Commun 2004; 325: 1246-1251.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 1246-1251
    • Tsuruma, K.1    Nakagawa, T.2    Shirakura, H.3    Hayashi, N.4    Uehara, T.5    Nomura, Y.6
  • 19
    • 0035800827 scopus 로고    scopus 로고
    • Characterization of a novel proapoptotic caspase-2- and caspase-9-binding protein
    • Bonfoco E, Li E, Kolbinger F, Cooper NR. Characterization of a novel proapoptotic caspase-2- and caspase-9-binding protein. J Biol Chem 2001; 276: 29242-29250.
    • (2001) J Biol Chem , vol.276 , pp. 29242-29250
    • Bonfoco, E.1    Li, E.2    Kolbinger, F.3    Cooper, N.R.4
  • 20
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new 'death' adaptor molecule
    • Duan H, Dixit VM. RAIDD is a new 'death' adaptor molecule. Nature 1997; 385: 86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 21
    • 0031045588 scopus 로고    scopus 로고
    • CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP
    • Ahmad M, Srinivasula SM, Wang L, Talanian RV, Litwack G, Fernandes-Alnemri T et al. CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. Cancer Res 1997; 57: 615-619.
    • (1997) Cancer Res , vol.57 , pp. 615-619
    • Ahmad, M.1    Srinivasula, S.M.2    Wang, L.3    Talanian, R.V.4    Litwack, G.5    Fernandes-Alnemri, T.6
  • 23
    • 0347986652 scopus 로고    scopus 로고
    • HOXA5-induced apoptosis in breast cancer cells is mediated by caspases 2 and 8
    • Chen H, Chung S, Sukumar S. HOXA5-induced apoptosis in breast cancer cells is mediated by caspases 2 and 8. Mol Cell Biol 2004; 24 924-935.
    • (2004) Mol Cell Biol , vol.24 , pp. 924-935
    • Chen, H.1    Chung, S.2    Sukumar, S.3
  • 24
    • 22344435528 scopus 로고    scopus 로고
    • Bid is upstream of lysosome-mediated caspase 2 activation in tumor necrosis factor alpha-induced hepatocyte apoptosis
    • Guicciardi ME, Bronk SF, Werneburg NW, Yin XM, Gores GJ. Bid is upstream of lysosome-mediated caspase 2 activation in tumor necrosis factor alpha-induced hepatocyte apoptosis. Gastroenterology 2005; 129 269-284.
    • (2005) Gastroenterology , vol.129 , pp. 269-284
    • Guicciardi, M.E.1    Bronk, S.F.2    Werneburg, N.W.3    Yin, X.M.4    Gores, G.J.5
  • 25
    • 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. Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis. Blood 2006; 108: 559-565.
    • (2006) Blood , vol.108 , pp. 559-565
    • Lavrik, I.N.1    Golks, A.2    Baumann, S.3    Krammer, P.H.4
  • 26
    • 0035869463 scopus 로고    scopus 로고
    • Involvement of caspase-2 long isoform in Fas-mediated cell death of human leukemic cells
    • Droin N, Bichat F, Rebe C, Wotawa A, Sordet O, Hammann A et al. Involvement of caspase-2 long isoform in Fas-mediated cell death of human leukemic cells. Blood 2001; 97: 1835-1844.
    • (2001) Blood , vol.97 , pp. 1835-1844
    • Droin, N.1    Bichat, F.2    Rebe, C.3    Wotawa, A.4    Sordet, O.5    Hammann, A.6
  • 27
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114: 181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 28
    • 0034254689 scopus 로고    scopus 로고
    • Fas ligand-induced c-Jun kinase activation in lymphoid cells requires extensive receptor aggregation but is independent of DAXX, and Fas-mediated cell death does not involve DAXX, RIP, or RAIDD
    • Villunger A, Huang DC, Holler N, Tschopp J, Strasser A. Fas ligand-induced c-Jun kinase activation in lymphoid cells requires extensive receptor aggregation but is independent of DAXX, and Fas-mediated cell death does not involve DAXX, RIP, or RAIDD. J Immunol 2000; 165: 1337-1343.
    • (2000) J Immunol , vol.165 , pp. 1337-1343
    • Villunger, A.1    Huang, D.C.2    Holler, N.3    Tschopp, J.4    Strasser, A.5
  • 29
    • 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. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 2004; 304: 843-846.
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 30
    • 30344459150 scopus 로고    scopus 로고
    • In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
    • Tu S, McStay GP, Boucher LM, Mak T, Beere HM, Green DR. In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis. Nat Cell Biol 2006; 8: 72-77.
    • (2006) Nat Cell Biol , vol.8 , pp. 72-77
    • Tu, S.1    McStay, G.P.2    Boucher, L.M.3    Mak, T.4    Beere, H.M.5    Green, D.R.6
  • 31
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • Park HH, Logette E, Raunser S, Cuenin S, Walz T, Tschopp J et al. Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex. Cell 2007; 128: 533-546.
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3    Cuenin, S.4    Walz, T.5    Tschopp, J.6
  • 32
    • 0037049549 scopus 로고    scopus 로고
    • A novel Apaf-1-independent putative caspase-2 activation complex
    • Read SH, Baliga BC, Ekert PG, Vaux DL, Kumar S. A novel Apaf-1-independent putative caspase-2 activation complex. J Cell Biol 2002; 159: 739-745.
    • (2002) J Cell Biol , vol.159 , pp. 739-745
    • Read, S.H.1    Baliga, B.C.2    Ekert, P.G.3    Vaux, D.L.4    Kumar, S.5
  • 33
    • 26444433872 scopus 로고    scopus 로고
    • Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD
    • Berube C, Boucher LM, Ma W, Wakeham A, Salmena L, Hakem R et al. Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD. Proc Natl Acad Sci USA 2005; 102: 14314-14320.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14314-14320
    • Berube, C.1    Boucher, L.M.2    Ma, W.3    Wakeham, A.4    Salmena, L.5    Hakem, R.6
  • 34
    • 0035937775 scopus 로고    scopus 로고
    • Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins
    • Hlaing T, Guo RF, Dilley KA, Loussia JM, Morrish TA, Shi MM et al. Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins. J Biol Chem 2001; 276: 9230-9238.
    • (2001) J Biol Chem , vol.276 , pp. 9230-9238
    • Hlaing, T.1    Guo, R.F.2    Dilley, K.A.3    Loussia, J.M.4    Morrish, T.A.5    Shi, M.M.6
  • 35
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J. The inflammasome: A molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 2002; 10: 417-426.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 36
    • 0034596826 scopus 로고    scopus 로고
    • Salmonella-induced caspase-2 activation in macrophages: A novel mechanism in pathogen-mediated apoptosis
    • Jesenberger V, Procyk KJ, Yuan J, Reipert S, Baccarini M. Salmonella-induced caspase-2 activation in macrophages: A novel mechanism in pathogen-mediated apoptosis. J Exp Med 2000; 192 1035-1046.
    • (2000) J Exp Med , vol.192 , pp. 1035-1046
    • Jesenberger, V.1    Procyk, K.J.2    Yuan, J.3    Reipert, S.4    Baccarini, M.5
  • 37
    • 40149084641 scopus 로고    scopus 로고
    • Caspase-12 modulates NOD signaling and regulates antimicrobial peptide production and mucosal immunity
    • LeBlanc PM, Yeretssian G, Rutherford N, Doiron K, Nadiri A, Zhu L et al. Caspase-12 modulates NOD signaling and regulates antimicrobial peptide production and mucosal immunity. Cell Host Microbe 2008; 3: 146-157.
    • (2008) Cell Host Microbe , vol.3 , pp. 146-157
    • LeBlanc, P.M.1    Yeretssian, G.2    Rutherford, N.3    Doiron, K.4    Nadiri, A.5    Zhu, L.6
  • 39
    • 0037076326 scopus 로고    scopus 로고
    • Cyclin D3 activates caspase 2, connecting cell proliferation with cell death
    • Mendelsohn AR, Hamer JD, Wang ZB, Brent R. Cyclin D3 activates caspase 2, connecting cell proliferation with cell death. Proc Natl Acad Sci USA 2002; 99: 6871-6876.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6871-6876
    • Mendelsohn, A.R.1    Hamer, J.D.2    Wang, Z.B.3    Brent, R.4
  • 40
  • 41
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-kappaB activation in response to DNA damage
    • Janssens S, Tinel A, Lippens S, Tschopp J. PIDD mediates NF-kappaB activation in response to DNA damage. Cell 2005; 123: 1079-1092.
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 42
    • 33846219997 scopus 로고    scopus 로고
    • Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway
    • Tinel A, Janssens S, Lippens S, Cuenin S, Logette E, Jaccard B et al Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway. EMBO J 2007; 26 197-208.
    • (2007) EMBO J , vol.26 , pp. 197-208
    • Tinel, A.1    Janssens, S.2    Lippens, S.3    Cuenin, S.4    Logette, E.5    Jaccard, B.6
  • 43
    • 38049143949 scopus 로고    scopus 로고
    • p53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress
    • Cuenin S, Tinel A, Janssens S, Tschopp J. p53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress. Oncogene 2008; 27: 387-396.
    • (2008) Oncogene , vol.27 , pp. 387-396
    • Cuenin, S.1    Tinel, A.2    Janssens, S.3    Tschopp, J.4
  • 44
    • 27144512715 scopus 로고    scopus 로고
    • Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8
    • Shin S, Lee Y, Kim W, Ko H, Choi H, Kim K. Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO J 2005; 24: 3532-3542.
    • (2005) EMBO J , vol.24 , pp. 3532-3542
    • Shin, S.1    Lee, Y.2    Kim, W.3    Ko, H.4    Choi, H.5    Kim, K.6
  • 45
    • 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. Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2. Cell 2005; 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
  • 46
    • 31044440029 scopus 로고    scopus 로고
    • Identification of a functional DNA binding site for the SREBP-1c transcription factor in the first intron of the human caspase-2 gene
    • Logette E, Solary E, Corcos L. Identification of a functional DNA binding site for the SREBP-1c transcription factor in the first intron of the human caspase-2 gene. Biochim Biophys Acta 2005; 1738 1-5.
    • (2005) Biochim Biophys Acta , vol.1738 , pp. 1-5
    • Logette, E.1    Solary, E.2    Corcos, L.3
  • 47
    • 44149110803 scopus 로고    scopus 로고
    • Caspase 2 is both required for p53-mediated apoptosis and downregulated by p53 in a p21-dependent manner
    • Baptiste-Okoh N, Barsotti AM, Prives C. Caspase 2 is both required for p53-mediated apoptosis and downregulated by p53 in a p21-dependent manner. Cell Cycle 2008; 7: 1133-1138.
    • (2008) Cell Cycle , vol.7 , pp. 1133-1138
    • Baptiste-Okoh, N.1    Barsotti, A.M.2    Prives, C.3
  • 48
    • 0002323493 scopus 로고    scopus 로고
    • Origin, expression and possible functions of the two alternatively spliced forms of the mouse Nedd2mRNA
    • Kumar S, Kinoshita M, Dorstyn L, Noda M. Origin, expression and possible functions of the two alternatively spliced forms of the mouse Nedd2mRNA. Cell Death Differ 1997; 4: 378-387.
    • (1997) Cell Death Differ , vol.4 , pp. 378-387
    • Kumar, S.1    Kinoshita, M.2    Dorstyn, L.3    Noda, M.4
  • 49
    • 0035843138 scopus 로고    scopus 로고
    • Modulation of apoptosis by procaspase-2 short isoform: Selective inhibition of chromatin condensation, apoptotic body formation and phosphatidylserine externalization
    • Droin N, Rebe C, Bichat F, Hammann A, Bertrand R, Solary E. Modulation of apoptosis by procaspase-2 short isoform: Selective inhibition of chromatin condensation, apoptotic body formation and phosphatidylserine externalization. Oncogene 2001; 20: 260-269.
    • (2001) Oncogene , vol.20 , pp. 260-269
    • Droin, N.1    Rebe, C.2    Bichat, F.3    Hammann, A.4    Bertrand, R.5    Solary, E.6
  • 50
    • 0037191508 scopus 로고    scopus 로고
    • Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells
    • Wotawa A, Solier S, Logette E, Solary E, Corcos L. Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells. Cancer Lett 2002; 185: 181-189.
    • (2002) Cancer Lett , vol.185 , pp. 181-189
    • Wotawa, A.1    Solier, S.2    Logette, E.3    Solary, E.4    Corcos, L.5
  • 51
    • 0037434720 scopus 로고    scopus 로고
    • The human caspase-2 gene: Alternative promoters, pre-mRNA splicing and AUG usage direct isoform-specific expression
    • Logette E, Wotawa A, Solier S, Desoche L, Solary E, Corcos L. The human caspase-2 gene: Alternative promoters, pre-mRNA splicing and AUG usage direct isoform-specific expression. Oncogene 2003; 22: 935-946.
    • (2003) Oncogene , vol.22 , pp. 935-946
    • Logette, E.1    Wotawa, A.2    Solier, S.3    Desoche, L.4    Solary, E.5    Corcos, L.6
  • 52
    • 0842304139 scopus 로고    scopus 로고
    • Topoisomerase I and II inhibitors control caspase-2 pre-messenger RNA splicing in human cells
    • Solier S, Lansiaux A, Logette E, Wu J, Soret J, Tazi J et al. Topoisomerase I and II inhibitors control caspase-2 pre-messenger RNA splicing in human cells. Mol Cancer Res 2004; 2: 53-61.
    • (2004) Mol Cancer Res , vol.2 , pp. 53-61
    • Solier, S.1    Lansiaux, A.2    Logette, E.3    Wu, J.4    Soret, J.5    Tazi, J.6
  • 53
    • 38049119903 scopus 로고    scopus 로고
    • Overlapping cleavage motif selectivity of caspases: Implications for analysis of apoptotic pathways
    • McStay GP, Salvesen GS, Green DR. Overlapping cleavage motif selectivity of caspases: Implications for analysis of apoptotic pathways. Cell Death Differ 2008; 15: 322-331.
    • (2008) Cell Death Differ , vol.15 , pp. 322-331
    • McStay, G.P.1    Salvesen, G.S.2    Green, D.R.3
  • 57
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • Sakahira H, Enari M, Nagata S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 1998; 391: 96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 58
    • 36049042702 scopus 로고    scopus 로고
    • Caspase-2 cleaves DNA fragmentation factor (DFF45)/inhibitor of caspase-activated DNase (ICAD)
    • Dahal GR, Karki P, Thapa A, Shahnawaz M, Shin SY, Lee JS et al. Caspase-2 cleaves DNA fragmentation factor (DFF45)/inhibitor of caspase-activated DNase (ICAD). Arch Biochem Biophys 2007; 468 134-139.
    • (2007) Arch Biochem Biophys , vol.468 , pp. 134-139
    • Dahal, G.R.1    Karki, P.2    Thapa, A.3    Shahnawaz, M.4    Shin, S.Y.5    Lee, J.S.6
  • 59
    • 23044473622 scopus 로고    scopus 로고
    • Doxorubicin requires the sequential activation of caspase-2, protein kinase Cdelta, and c-Jun NH2-terminal kinase to induce apoptosis
    • Panaretakis T, Laane E, Pokrovskaja K, Bjorklund AC, Moustakas A, Zhivotovsky B et al. Doxorubicin requires the sequential activation of caspase-2, protein kinase Cdelta, and c-Jun NH2-terminal kinase to induce apoptosis. Mol Biol Cell 2005; 16: 3821-3831.
    • (2005) Mol Biol Cell , vol.16 , pp. 3821-3831
    • Panaretakis, T.1    Laane, E.2    Pokrovskaja, K.3    Bjorklund, A.C.4    Moustakas, A.5    Zhivotovsky, B.6
  • 60
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease
    • Hermel E, Gafni J, Propp SS, Leavitt BR, Wellington CL, Young JE et al. Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease. Cell Death Differ 2004; 11: 424-438.
    • (2004) Cell Death Differ , vol.11 , pp. 424-438
    • Hermel, E.1    Gafni, J.2    Propp, S.S.3    Leavitt, B.R.4    Wellington, C.L.5    Young, J.E.6
  • 61
    • 0029166984 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by interleukin-1 beta converting enzyme and its homologs TX and Nedd-2
    • Gu Y, Sarnecki C, Aldape RA, Livingston DJ, Su MS. Cleavage of poly(ADP-ribose) polymerase by interleukin-1 beta converting enzyme and its homologs TX and Nedd-2. J Biol Chem 1995; 270: 18715-18718.
    • (1995) J Biol Chem , vol.270 , pp. 18715-18718
    • Gu, Y.1    Sarnecki, C.2    Aldape, R.A.3    Livingston, D.J.4    Su, M.S.5
  • 62
    • 1542374647 scopus 로고    scopus 로고
    • AlphaII-spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding
    • Rotter B, Kroviarski Y, Nicolas G, Dhermy D, Lecomte MC. AlphaII-spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding. Biochem J 2004; 378: 161-168.
    • (2004) Biochem J , vol.378 , pp. 161-168
    • Rotter, B.1    Kroviarski, Y.2    Nicolas, G.3    Dhermy, D.4    Lecomte, M.C.5
  • 63
    • 8344221944 scopus 로고    scopus 로고
    • Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases
    • Aho S. Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases. Exp Dermatol 2004; 13: 700-707.
    • (2004) Exp Dermatol , vol.13 , pp. 700-707
    • Aho, S.1
  • 64
    • 2542431137 scopus 로고    scopus 로고
    • Caspase-dependent regulation of histone deacetylase 4 nuclear-cytoplasmic shuttling promotes apoptosis
    • Paroni G, Mizzau M, Henderson C, Del Sal G, Schneider C, Brancolini C. Caspase-dependent regulation of histone deacetylase 4 nuclear-cytoplasmic shuttling promotes apoptosis. Mol Biol Cell 2004; 15: 2804-2818.
    • (2004) Mol Biol Cell , vol.15 , pp. 2804-2818
    • Paroni, G.1    Mizzau, M.2    Henderson, C.3    Del Sal, G.4    Schneider, C.5    Brancolini, C.6
  • 65
    • 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
  • 66
    • 0037119491 scopus 로고    scopus 로고
    • Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis
    • Robertson JD, Enoksson M, Suomela M, Zhivotovsky B, Orrenius S. Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis. J Biol Chem 2002; 277: 29803-29809.
    • (2002) J Biol Chem , vol.277 , pp. 29803-29809
    • Robertson, J.D.1    Enoksson, M.2    Suomela, M.3    Zhivotovsky, B.4    Orrenius, S.5
  • 67
    • 9644307904 scopus 로고    scopus 로고
    • Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids
    • Enoksson M, Robertson JD, Gogvadze V, Bu P, Kropotov A, Zhivotovsky B et al. Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids. J Biol Chem 2004; 279: 49575-49578.
    • (2004) J Biol Chem , vol.279 , pp. 49575-49578
    • Enoksson, M.1    Robertson, J.D.2    Gogvadze, V.3    Bu, P.4    Kropotov, A.5    Zhivotovsky, B.6
  • 68
    • 33644663668 scopus 로고    scopus 로고
    • Essential roles of the Bcl-2 family of proteins in caspase-2-induced apoptosis
    • Gao Z, Shao Y, Jiang X. Essential roles of the Bcl-2 family of proteins in caspase-2-induced apoptosis. J Biol Chem 2005; 280: 38271-38275.
    • (2005) J Biol Chem , vol.280 , pp. 38271-38275
    • Gao, Z.1    Shao, Y.2    Jiang, X.3
  • 69
    • 33745739717 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis requires bid cleavage: A physiological role for bid in heat shock-induced death
    • Bonzon C, Bouchier-Hayes L, Pagliari LJ, Green DR, Newmeyer DD. Caspase-2-induced apoptosis requires bid cleavage: A physiological role for bid in heat shock-induced death. Mol Biol Cell 2006; 17: 2150-2157.
    • (2006) Mol Biol Cell , vol.17 , pp. 2150-2157
    • Bonzon, C.1    Bouchier-Hayes, L.2    Pagliari, L.J.3    Green, D.R.4    Newmeyer, D.D.5
  • 71
    • 15944379869 scopus 로고    scopus 로고
    • Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7
    • Ho PK, Jabbour AM, Ekert PG, Hawkins CJ. Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7. FEBS J 2005; 272: 1401-1414.
    • (2005) FEBS J , vol.272 , pp. 1401-1414
    • Ho, P.K.1    Jabbour, A.M.2    Ekert, P.G.3    Hawkins, C.J.4
  • 72
    • 19644394499 scopus 로고    scopus 로고
    • Caspase-resistant Golgin-160 disrupts apoptosis induced by secretory pathway stress and ligation of death receptors
    • Maag RS, Mancini M, Rosen A, Machamer CE. Caspase-resistant Golgin-160 disrupts apoptosis induced by secretory pathway stress and ligation of death receptors. Mol Biol Cell 2005; 16: 3019-3027.
    • (2005) Mol Biol Cell , vol.16 , pp. 3019-3027
    • Maag, R.S.1    Mancini, M.2    Rosen, A.3    Machamer, C.E.4
  • 73
    • 0030916417 scopus 로고    scopus 로고
    • Liu X, Zou H, Slaughter C, Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 1997; 89: 175-184.
    • Liu X, Zou H, Slaughter C, Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 1997; 89: 175-184.
  • 74
    • 0032582539 scopus 로고    scopus 로고
    • Cleavage of DFF-45/ICAD by multiple caspases is essential for its function during apoptosis
    • Tang D, Kidd VJ. Cleavage of DFF-45/ICAD by multiple caspases is essential for its function during apoptosis. J Biol Chem 1998; 273: 28549-28552.
    • (1998) J Biol Chem , vol.273 , pp. 28549-28552
    • Tang, D.1    Kidd, V.J.2
  • 75
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Janicke RU, Sprengart ML, Wati MR, Porter AG. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J Biol Chem 1998; 273: 9357-9360.
    • (1998) J Biol Chem , vol.273 , pp. 9357-9360
    • Janicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 76
    • 10344262595 scopus 로고    scopus 로고
    • Contrasting nuclear dynamics of the caspase-activated DNase (CAD) in dividing and apoptotic cells
    • Lechardeur D, Xu M, Lukacs GL. Contrasting nuclear dynamics of the caspase-activated DNase (CAD) in dividing and apoptotic cells. J Cell Biol 2004; 167: 851-862.
    • (2004) J Cell Biol , vol.167 , pp. 851-862
    • Lechardeur, D.1    Xu, M.2    Lukacs, G.L.3
  • 77
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • Graham RK, Deng Y, Slow EJ, Haigh B, Bissada N, Lu G et al. Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin. Cell 2006; 125: 1179-1191.
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3    Haigh, B.4    Bissada, N.5    Lu, G.6
  • 78
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P, Opitz-Araya X, Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 2002; 297: 1352-1354.
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 79
    • 4644314416 scopus 로고    scopus 로고
    • Sequential caspase-2 and caspase-8 activation upstream of mitochondria during ceramide and etoposide-induced apoptosis
    • Lin CF, Chen CL, Chang WT, Jan MS, Hsu LJ, Wu RH et al. Sequential caspase-2 and caspase-8 activation upstream of mitochondria during ceramide and etoposide-induced apoptosis. J Biol Chem 2004; 279 40755-40761.
    • (2004) J Biol Chem , vol.279 , pp. 40755-40761
    • Lin, C.F.1    Chen, C.L.2    Chang, W.T.3    Jan, M.S.4    Hsu, L.J.5    Wu, R.H.6
  • 80
    • 21244441600 scopus 로고    scopus 로고
    • Bcl-2 rescues ceramide- and etoposide-induced mitochondrial apoptosis through blockage of caspase-2 activation
    • Lin CF, Chen CL, Chang WT, Jan MS, Hsu LJ, Wu RH et al. Bcl-2 rescues ceramide- and etoposide-induced mitochondrial apoptosis through blockage of caspase-2 activation. J Biol Chem 2005; 280: 23758-23765.
    • (2005) J Biol Chem , vol.280 , pp. 23758-23765
    • Lin, C.F.1    Chen, C.L.2    Chang, W.T.3    Jan, M.S.4    Hsu, L.J.5    Wu, R.H.6
  • 81
    • 47249134609 scopus 로고    scopus 로고
    • c-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis
    • Cao X, Bennett RL, May WS. c-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis. J Biol Chem 2008; 283: 14490-14496.
    • (2008) J Biol Chem , vol.283 , pp. 14490-14496
    • Cao, X.1    Bennett, R.L.2    May, W.S.3
  • 83
    • 24744451822 scopus 로고    scopus 로고
    • p53-dependent caspase-2 activation in mitochondrial release of apoptosis-inducing factor and its role in renal tubular epithelial cell injury
    • Seth R, Yang C, Kaushal V, Shah SV, Kaushal GP. p53-dependent caspase-2 activation in mitochondrial release of apoptosis-inducing factor and its role in renal tubular epithelial cell injury. J Biol Chem 2005; 280: 31230-31239.
    • (2005) J Biol Chem , vol.280 , pp. 31230-31239
    • Seth, R.1    Yang, C.2    Kaushal, V.3    Shah, S.V.4    Kaushal, G.P.5
  • 84
    • 41149087212 scopus 로고    scopus 로고
    • A role for caspase 2 and PIDD in the process of p53-mediated apoptosis
    • Baptiste-Okoh N, Barsotti AM, Prives C. A role for caspase 2 and PIDD in the process of p53-mediated apoptosis. Proc Natl Acad Sci USA 2008; 105: 1937-1942.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1937-1942
    • Baptiste-Okoh, N.1    Barsotti, A.M.2    Prives, C.3
  • 85
    • 33751100367 scopus 로고    scopus 로고
    • TSA-induced cell death in prostate cancer cell lines is caspase-2 dependent and involves the PIDDosome
    • Taghiyev AF, Guseva NV, Glover RA, Rokhlin OW, Cohen MB. TSA-induced cell death in prostate cancer cell lines is caspase-2 dependent and involves the PIDDosome. Cancer Biol Ther 2006; 5: 1199-1205.
    • (2006) Cancer Biol Ther , vol.5 , pp. 1199-1205
    • Taghiyev, A.F.1    Guseva, N.V.2    Glover, R.A.3    Rokhlin, O.W.4    Cohen, M.B.5
  • 87
    • 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. Loss of caspase-9 reveals its essential role for caspase-2 activation and mitochondrial membrane depolarization. Mol Biol Cell 2007; 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
  • 88
    • 1442351992 scopus 로고    scopus 로고
    • Bax deficiency affects caspase-2 activation during ultraviolet radiation-induced apoptosis
    • He Q, Huang Y, Sheikh MS. Bax deficiency affects caspase-2 activation during ultraviolet radiation-induced apoptosis. Oncogene 2004; 23: 1321-1325.
    • (2004) Oncogene , vol.23 , pp. 1321-1325
    • He, Q.1    Huang, Y.2    Sheikh, M.S.3
  • 89
    • 3042592579 scopus 로고    scopus 로고
    • Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9
    • Marsden VS, Ekert PG, Van Delft M, Vaux DL, Adams JM, Strasser A. Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9. J Cell Biol 2004; 165: 775-780.
    • (2004) J Cell Biol , vol.165 , pp. 775-780
    • Marsden, V.S.1    Ekert, P.G.2    Van Delft, M.3    Vaux, D.L.4    Adams, J.M.5    Strasser, A.6
  • 90
    • 0033709907 scopus 로고    scopus 로고
    • Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation
    • Zheng TS, Hunot S, Kuida K, Momoi T, Srinivasan A, Nicholson DW et al Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation. Nat Med 2000; 6: 1241-1247.
    • (2000) Nat Med , vol.6 , pp. 1241-1247
    • Zheng, T.S.1    Hunot, S.2    Kuida, K.3    Momoi, T.4    Srinivasan, A.5    Nicholson, D.W.6
  • 91
    • 3042687605 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die
    • Ekert PG, Read SH, Silke J, Marsden VS, Kaufmann H, Hawkins CJ et al Apaf-1 and caspase-9 accelerate apoptosis, but do not determine whether factor-deprived or drug-treated cells die. J Cell Biol 2004; 165: 835-842.
    • (2004) J Cell Biol , vol.165 , pp. 835-842
    • Ekert, P.G.1    Read, S.H.2    Silke, J.3    Marsden, V.S.4    Kaufmann, H.5    Hawkins, C.J.6
  • 92
    • 0033593038 scopus 로고    scopus 로고
    • Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival
    • Ogilvy S, Metcalf D, Print CG, Bath ML, Harris AW, Adams JM. Constitutive Bcl-2 expression throughout the hematopoietic compartment affects multiple lineages and enhances progenitor cell survival. Proc Natl Acad Sci USA 1999; 96: 14943-14948.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 14943-14948
    • Ogilvy, S.1    Metcalf, D.2    Print, C.G.3    Bath, M.L.4    Harris, A.W.5    Adams, J.M.6
  • 93
    • 0033555707 scopus 로고    scopus 로고
    • Inhibition of apoptosis and clonogenic survival of cells expressing crmA variants: Optimal caspase substrates are not necessarily optimal inhibitors
    • Ekert PG, Silke J, Vaux DL. Inhibition of apoptosis and clonogenic survival of cells expressing crmA variants: Optimal caspase substrates are not necessarily optimal inhibitors. EMBO J 1999; 18: 330-338.
    • (1999) EMBO J , vol.18 , pp. 330-338
    • Ekert, P.G.1    Silke, J.2    Vaux, D.L.3
  • 94
    • 23944514831 scopus 로고    scopus 로고
    • FADD and caspase-8 are required for cytokine-induced proliferation of hematopoietic progenitor cells
    • Pellegrini M, Bath S, Marsden VS, Huang DC, Metcalf D, Harris AW et al. FADD and caspase-8 are required for cytokine-induced proliferation of hematopoietic progenitor cells. Blood 2005; 106: 1581-1589.
    • (2005) Blood , vol.106 , pp. 1581-1589
    • Pellegrini, M.1    Bath, S.2    Marsden, V.S.3    Huang, D.C.4    Metcalf, D.5    Harris, A.W.6
  • 95
    • 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. Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3. Cell 2008; 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
  • 96
    • 0027336298 scopus 로고
    • Go 6976, a selective inhibitor of protein kinase C, is a potent antagonist of human immunodeficiency virus 1 induction from latent/low-level-producing reservoir cells in vitro
    • Qatsha KA, Rudolph C, Marme D, Schachtele C, May WS. Go 6976, a selective inhibitor of protein kinase C, is a potent antagonist of human immunodeficiency virus 1 induction from latent/low-level-producing reservoir cells in vitro. Proc Natl Acad Sci USA 1993; 90: 4674-4678.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4674-4678
    • Qatsha, K.A.1    Rudolph, C.2    Marme, D.3    Schachtele, C.4    May, W.S.5
  • 97
    • 33747432604 scopus 로고    scopus 로고
    • Disruption of the endoplasmic reticulum and increases in cytoplasmic calcium are early events in cell death induced by the natural triterpenoid asiatic acid
    • Gurfinkel DM, Chow S, Hurren R, Gronda M, Henderson C, Berube C et al Disruption of the endoplasmic reticulum and increases in cytoplasmic calcium are early events in cell death induced by the natural triterpenoid asiatic acid. Apoptosis 2006; 11: 1463-1471.
    • (2006) Apoptosis , vol.11 , pp. 1463-1471
    • Gurfinkel, D.M.1    Chow, S.2    Hurren, R.3    Gronda, M.4    Henderson, C.5    Berube, C.6
  • 98
    • 38049097948 scopus 로고    scopus 로고
    • Deletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS mice
    • Kieran D, Woods I, Villunger A, Strasser A, Prehn JH. Deletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS mice. Proc Natl Acad Sci USA 2007; 104: 20606-20611.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20606-20611
    • Kieran, D.1    Woods, I.2    Villunger, A.3    Strasser, A.4    Prehn, J.H.5
  • 99
    • 34248641140 scopus 로고    scopus 로고
    • Suppression of endoplasmic reticulum stress-induced caspase activation and cell death by the overexpression of Bcl-xL or Bcl-2
    • Murakami Y, Aizu-Yokota E, Sonoda Y, Ohta S, Kasahara T. Suppression of endoplasmic reticulum stress-induced caspase activation and cell death by the overexpression of Bcl-xL or Bcl-2. J Biochem 2007; 141 401-410.
    • (2007) J Biochem , vol.141 , pp. 401-410
    • Murakami, Y.1    Aizu-Yokota, E.2    Sonoda, Y.3    Ohta, S.4    Kasahara, T.5
  • 100
    • 33646176558 scopus 로고    scopus 로고
    • ER stress and UPR in familial amyotrophic lateral sclerosis
    • Turner BJ, Atkin JD. ER stress and UPR in familial amyotrophic lateral sclerosis. Curr Mol Med 2006; 6: 79-86.
    • (2006) Curr Mol Med , vol.6 , pp. 79-86
    • Turner, B.J.1    Atkin, J.D.2
  • 101
    • 4544274785 scopus 로고    scopus 로고
    • Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway
    • Wagner KW, Engels IH, Deveraux QL. Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway. J Biol Chem 2004; 279: 35047-35052.
    • (2004) J Biol Chem , vol.279 , pp. 35047-35052
    • Wagner, K.W.1    Engels, I.H.2    Deveraux, Q.L.3
  • 102
    • 53149102493 scopus 로고    scopus 로고
    • Caspases activation in hyperthermia-induced stimulation of TRAIL apoptosis
    • Moulin M, Arrigo AP. Caspases activation in hyperthermia-induced stimulation of TRAIL apoptosis. Cell Stress Chaperones 2008; 13 313-326.
    • (2008) Cell Stress Chaperones , vol.13 , pp. 313-326
    • Moulin, M.1    Arrigo, A.P.2
  • 103
    • 3543096349 scopus 로고    scopus 로고
    • NFkappaB activation by Fas is mediated through FADD, caspase-8, and RIP and is inhibited by FLIP
    • Kreuz S, Siegmund D, Rumpf JJ, Samel D, Leverkus M, Janssen O et al NFkappaB activation by Fas is mediated through FADD, caspase-8, and RIP and is inhibited by FLIP. J Cell Biol 2004; 166: 369-380.
    • (2004) J Cell Biol , vol.166 , pp. 369-380
    • Kreuz, S.1    Siegmund, D.2    Rumpf, J.J.3    Samel, D.4    Leverkus, M.5    Janssen, O.6
  • 104
    • 29244440885 scopus 로고    scopus 로고
    • Activation or suppression of NFkappaB by HPK1 determines sensitivity to activation-induced cell death
    • Brenner D, Golks A, Kiefer F, Krammer PH, Arnold R. Activation or suppression of NFkappaB by HPK1 determines sensitivity to activation-induced cell death. EMBO J 2005; 24: 4279-4290.
    • (2005) EMBO J , vol.24 , pp. 4279-4290
    • Brenner, D.1    Golks, A.2    Kiefer, F.3    Krammer, P.H.4    Arnold, R.5
  • 105
    • 33745223497 scopus 로고    scopus 로고
    • Heat shock induces apoptosis independently of any known initiator caspase-activating complex
    • Milleron RS, Bratton SB. Heat shock induces apoptosis independently of any known initiator caspase-activating complex. J Biol Chem 2006; 281: 16991-17000.
    • (2006) J Biol Chem , vol.281 , pp. 16991-17000
    • Milleron, R.S.1    Bratton, S.B.2
  • 107
    • 44149087374 scopus 로고    scopus 로고
    • Caspase-2 is required for cell death induced by cytoskeletal disruption
    • Ho LH, Read SH, Dorstyn L, Lambrusco L, Kumar S. Caspase-2 is required for cell death induced by cytoskeletal disruption. Oncogene 2008; 27: 3393-3404.
    • (2008) Oncogene , vol.27 , pp. 3393-3404
    • Ho, L.H.1    Read, S.H.2    Dorstyn, L.3    Lambrusco, L.4    Kumar, S.5
  • 110
    • 33745849139 scopus 로고    scopus 로고
    • Caspase-2 triggers Bax-Bak-dependent and -independent cell death in colon cancer cells treated with resveratrol
    • Mohan J, Gandhi AA, Bhavya BC, Rashmi R, Karunagaran D, Indu R et al Caspase-2 triggers Bax-Bak-dependent and -independent cell death in colon cancer cells treated with resveratrol. J Biol Chem 2006; 281: 17599-17611.
    • (2006) J Biol Chem , vol.281 , pp. 17599-17611
    • Mohan, J.1    Gandhi, A.A.2    Bhavya, B.C.3    Rashmi, R.4    Karunagaran, D.5    Indu, R.6
  • 112
    • 1542426652 scopus 로고    scopus 로고
    • Apoptosis signaling triggered by the marine alkaloid ascididemin is routed via caspase-2 and JNK to mitochondria
    • Dirsch VM, Kirschke SO, Estermeier M, Steffan B, Vollmar AM. Apoptosis signaling triggered by the marine alkaloid ascididemin is routed via caspase-2 and JNK to mitochondria. Oncogene 2004; 23: 1586-1593.
    • (2004) Oncogene , vol.23 , pp. 1586-1593
    • Dirsch, V.M.1    Kirschke, S.O.2    Estermeier, M.3    Steffan, B.4    Vollmar, A.M.5
  • 113
    • 2442492707 scopus 로고    scopus 로고
    • Norepinephrine induces apoptosis in neonatal rat cardiomyocytes through a reactive oxygen species-TNF alpha-caspase signaling pathway
    • Fu YC, Chi CS, Yin SC, Hwang B, Chiu YT, Hsu SL. Norepinephrine induces apoptosis in neonatal rat cardiomyocytes through a reactive oxygen species-TNF alpha-caspase signaling pathway. Cardiovasc Res 2004; 62: 558-567.
    • (2004) Cardiovasc Res , vol.62 , pp. 558-567
    • Fu, Y.C.1    Chi, C.S.2    Yin, S.C.3    Hwang, B.4    Chiu, Y.T.5    Hsu, S.L.6
  • 114
    • 33744959426 scopus 로고    scopus 로고
    • PS-341 (bortezomib) induces lysosomal cathepsin B release and a caspase-2-dependent mitochondrial permeabilization and apoptosis in human pancreatic cancer cells
    • Yeung BH, Huang DC, Sinicrope FA. PS-341 (bortezomib) induces lysosomal cathepsin B release and a caspase-2-dependent mitochondrial permeabilization and apoptosis in human pancreatic cancer cells. J Biol Chem 2006; 281: 11923-11932.
    • (2006) J Biol Chem , vol.281 , pp. 11923-11932
    • Yeung, B.H.1    Huang, D.C.2    Sinicrope, F.A.3
  • 115
    • 33745818640 scopus 로고    scopus 로고
    • ROS-triggered caspase 2 activation and feedback amplification loop in beta-carotene-induced apoptosis
    • Prasad V, Chandele A, Jagtap JC, Sudheer KP, Shastry P. ROS-triggered caspase 2 activation and feedback amplification loop in beta-carotene-induced apoptosis. Free Radic Biol Med 2006; 41 431-442.
    • (2006) Free Radic Biol Med , vol.41 , pp. 431-442
    • Prasad, V.1    Chandele, A.2    Jagtap, J.C.3    Sudheer, K.P.4    Shastry, P.5
  • 116
    • 40049088310 scopus 로고    scopus 로고
    • Caspase-2 activation in neural stem cells undergoing oxidative stress-induced apoptosis
    • Tamm C, Zhivotovsky B, Ceccatelli S. Caspase-2 activation in neural stem cells undergoing oxidative stress-induced apoptosis. Apoptosis 2008; 13: 354-363.
    • (2008) Apoptosis , vol.13 , pp. 354-363
    • Tamm, C.1    Zhivotovsky, B.2    Ceccatelli, S.3
  • 117
    • 44349130527 scopus 로고    scopus 로고
    • Induction of apoptosis by Vitamin D2, ergocalciferol, via reactive oxygen species generation, glutathione depletion, and caspase activation in human leukemia cells
    • Chen WJ, Huang YT, Wu ML, Huang TC, Ho CT, Pan MH. Induction of apoptosis by Vitamin D2, ergocalciferol, via reactive oxygen species generation, glutathione depletion, and caspase activation in human leukemia cells. J Agric Food Chem 2008; 56: 2996-3005.
    • (2008) J Agric Food Chem , vol.56 , pp. 2996-3005
    • Chen, W.J.1    Huang, Y.T.2    Wu, M.L.3    Huang, T.C.4    Ho, C.T.5    Pan, M.H.6
  • 119
    • 0037362863 scopus 로고    scopus 로고
    • Lifelong caloric restriction increases expression of apoptosis repressor with a caspase recruitment domain (ARC) in the brain
    • Shelke RR, Leeuwenburgh C. Lifelong caloric restriction increases expression of apoptosis repressor with a caspase recruitment domain (ARC) in the brain. FASEB J 2003; 17: 494-496.
    • (2003) FASEB J , vol.17 , pp. 494-496
    • Shelke, R.R.1    Leeuwenburgh, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.