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Volumn 14, Issue 7, 2009, Pages 829-848

Caspase-2: Controversial killer or checkpoint controller?

Author keywords

Activation; Apoptosis; Caspase; PIDDosome; Protease; Splicing

Indexed keywords

BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; CASPASE 2; CASPASE INHIBITOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2;

EID: 67649774226     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-009-0365-3     Document Type: Article
Times cited : (39)

References (183)
  • 2
    • 46649096691 scopus 로고    scopus 로고
    • Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire
    • 10.1093/molbev/msn012
    • L Eckhart C Ballaun M Hermann 2008 Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire Mol Biol Evol 25 831 841 10.1093/molbev/msn012
    • (2008) Mol Biol Evol , vol.25 , pp. 831-841
    • Eckhart, L.1    Ballaun, C.2    Hermann, M.3
  • 3
    • 0025255636 scopus 로고
    • The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death
    • 10.1016/0012-1606(90)90174-H
    • JY Yuan HR Horvitz 1990 The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death Dev Biol 138 33 41 10.1016/0012-1606(90)90174-H
    • (1990) Dev Biol , vol.138 , pp. 33-41
    • Yuan, J.Y.1    Horvitz, H.R.2
  • 4
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: A new apoptotic signalling motif
    • 10.1016/S0968-0004(97)01043-8
    • K Hofmann P Bucher J Tschopp 1997 The CARD domain: a new apoptotic signalling motif Trends Biochem Sci 22 155 156 10.1016/S0968-0004(97)01043-8
    • (1997) Trends Biochem Sci , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 6
    • 0030951345 scopus 로고    scopus 로고
    • Direct physical interaction between the Caenorhabditis elegans death proteins CED-3 and CED-4
    • 10.1016/S0014-5793(97)00271-8
    • M Irmler K Hofmann D Vaux J Tschopp 1997 Direct physical interaction between the Caenorhabditis elegans death proteins CED-3 and CED-4 FEBS Lett 406 189 190 10.1016/S0014-5793(97)00271-8
    • (1997) FEBS Lett , vol.406 , pp. 189-190
    • Irmler, M.1    Hofmann, K.2    Vaux, D.3    Tschopp, J.4
  • 7
    • 0031194404 scopus 로고    scopus 로고
    • Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
    • S Seshagiri LK Miller 1997 Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis Curr Biol 7 455 460 10.1016/S0960- 9822(06)00216-8 (Pubitemid 27308968)
    • (1997) Current Biology , vol.7 , Issue.7 , pp. 455-460
    • Seshagiri, S.1    Miller, L.K.2
  • 8
    • 0030826436 scopus 로고    scopus 로고
    • Interaction and regulation of the Caenorhabditis elegans death protease CED-3 by CED-4 and CED-9
    • 10.1074/jbc.272.34.21449
    • D Wu H Wallen N Inohara G Nunez 1997 Interaction and regulation of the Caenorhabditis elegans death protease CED-3 by CED-4 and CED-9 J Biol Chem 272 21449 21454 10.1074/jbc.272.34.21449
    • (1997) J Biol Chem , vol.272 , pp. 21449-21454
    • Wu, D.1    Wallen, H.2    Inohara, N.3    Nunez, G.4
  • 10
    • 37749030247 scopus 로고    scopus 로고
    • A phylogenetic and functional overview of inflammatory caspases and caspase-1-related CARD-only proteins
    • 10.1042/BST0351508
    • K Kersse T Vanden Berghe M Lamkanfi P Vandenabeele 2007 A phylogenetic and functional overview of inflammatory caspases and caspase-1-related CARD-only proteins Biochem Soc Trans 35 1508 1511 10.1042/BST0351508
    • (2007) Biochem Soc Trans , vol.35 , pp. 1508-1511
    • Kersse, K.1    Vanden Berghe, T.2    Lamkanfi, M.3    Vandenabeele, P.4
  • 12
    • 55949099352 scopus 로고    scopus 로고
    • Caspase-2: Vestigial remnant or master regulator?
    • 10.1126/scisignal.138pe42
    • CM Troy EM Ribe 2008 Caspase-2: vestigial remnant or master regulator? Sci Signal 1 pe42 10.1126/scisignal.138pe42
    • (2008) Sci Signal , vol.1 , pp. 42
    • Troy, C.M.1    Ribe, E.M.2
  • 14
    • 0035896511 scopus 로고    scopus 로고
    • Polypyrimidine track-binding protein binding downstream of caspase-2 alternative exon 9 represses its inclusion
    • 10.1074/jbc.M008924200
    • J Cote S Dupuis JY Wu 2001 Polypyrimidine track-binding protein binding downstream of caspase-2 alternative exon 9 represses its inclusion J Biol Chem 276 8535 8543 10.1074/jbc.M008924200
    • (2001) J Biol Chem , vol.276 , pp. 8535-8543
    • Cote, J.1    Dupuis, S.2    Wu, J.Y.3
  • 15
    • 0035970031 scopus 로고    scopus 로고
    • Caspase-2 pre-mRNA alternative splicing: Identification of an intronic element containing a decoy 3acceptor site
    • 10.1073/pnas.031564098
    • J Cote S Dupuis Z Jiang JY Wu 2001 Caspase-2 pre-mRNA alternative splicing: identification of an intronic element containing a decoy 3 acceptor site Proc Natl Acad Sci USA 98 938 943 10.1073/pnas.031564098
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 938-943
    • Cote, J.1    Dupuis, S.2    Jiang, Z.3    Wu, J.Y.4
  • 16
    • 0037434720 scopus 로고    scopus 로고
    • The human caspase-2 gene: Alternative promoters, pre-mRNA splicing and AUG usage direct isoform-specific expression
    • 10.1038/sj.onc.1206172
    • E Logette A Wotawa S Solier L Desoche E Solary L Corcos 2003 The human caspase-2 gene: alternative promoters, pre-mRNA splicing and AUG usage direct isoform-specific expression Oncogene 22 935 946 10.1038/sj.onc.1206172
    • (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
  • 17
    • 0028168593 scopus 로고
    • ICH-1, an ICE/CED-3-related gene, encodes both positive and negative regulators of programmed cell death
    • 10.1016/S0092-8674(94)90422-7
    • L Wang M Miura L Bergeron H Zhu J Yuan 1994 ICH-1, an ICE/CED-3-related gene, encodes both positive and negative regulators of programmed cell death Cell 78 739 750 10.1016/S0092-8674(94)90422-7
    • (1994) Cell , vol.78 , pp. 739-750
    • Wang, L.1    Miura, M.2    Bergeron, L.3    Zhu, H.4    Yuan, J.5
  • 18
    • 0032482968 scopus 로고    scopus 로고
    • Regulation of ICH-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors
    • 10.1073/pnas.95.16.9155
    • ZH Jiang WJ Zhang Y Rao JY Wu 1998 Regulation of ICH-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors Proc Natl Acad Sci USA 95 9155 9160 10.1073/pnas.95.16.9155
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9155-9160
    • Jiang, Z.H.1    Zhang, W.J.2    Rao, Y.3    Wu, J.Y.4
  • 19
    • 0036024020 scopus 로고    scopus 로고
    • Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9
    • 10.1038/sj.cdd.4401033
    • LA O'Reilly P Ekert N Harvey 2002 Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9 Cell Death Differ 9 832 841 10.1038/sj.cdd.4401033
    • (2002) Cell Death Differ , vol.9 , pp. 832-841
    • O'Reilly, L.A.1    Ekert, P.2    Harvey, N.3
  • 20
    • 0034671217 scopus 로고    scopus 로고
    • Identification of a caspase-2 isoform that behaves as an endogenous inhibitor of the caspase cascade
    • N Droin M Beauchemin E Solary R Bertrand 2000 Identification of a caspase-2 isoform that behaves as an endogenous inhibitor of the caspase cascade Cancer Res 60 7039 7047 (Pubitemid 32059182)
    • (2000) Cancer Research , vol.60 , Issue.24 , pp. 7039-7047
    • Droin, N.1    Beauchemin, M.2    Solary, E.3    Bertrand, R.4
  • 21
    • 11144357398 scopus 로고    scopus 로고
    • Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease
    • 10.1038/sj.cdd.4401358
    • E Hermel J Gafni SS Propp 2004 Specific caspase interactions and amplification are involved in selective neuronal vulnerability in Huntington's disease Cell Death Differ 11 424 438 10.1038/sj.cdd.4401358
    • (2004) Cell Death Differ , vol.11 , pp. 424-438
    • Hermel, E.1    Gafni, J.2    Propp, S.S.3
  • 22
    • 27144488677 scopus 로고    scopus 로고
    • Caspase-2, a novel lipid sensor under the control of sterol regulatory element binding protein 2
    • 10.1128/MCB.25.21.9621-9631.2005
    • E Logette C Le Jossic-Corcos D Masson 2005 Caspase-2, a novel lipid sensor under the control of sterol regulatory element binding protein 2 Mol Cell Biol 25 9621 9631 10.1128/MCB.25.21.9621-9631.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 9621-9631
    • Logette, E.1    Le Jossic-Corcos, C.2    Masson, D.3
  • 23
    • 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
    • DOI 10.1016/j.bbalip.2005.11.006, PII S1388198105002751
    • E Logette E Solary L Corcos 2005 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 1738 1 5 (Pubitemid 43122124)
    • (2005) Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids , vol.1738 , Issue.1-3 , pp. 1-5
    • Logette, E.1    Solary, E.2    Corcos, L.3
  • 24
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • 10.1016/j.cell.2006.07.033
    • L Gurcel L Abrami S Girardin J Tschopp FG van der Goot 2006 Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival Cell 126 1135 1145 10.1016/j.cell.2006.07.033
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    Van Der Goot, F.G.5
  • 25
    • 50949133662 scopus 로고    scopus 로고
    • E1A oncogene enhancement of caspase-2-mediated mitochondrial injury sensitizes cells to macrophage nitric oxide-induced apoptosis
    • JR Radke ZK Siddiqui TA Miura JM Routes JL Cook 2008 E1A oncogene enhancement of caspase-2-mediated mitochondrial injury sensitizes cells to macrophage nitric oxide-induced apoptosis J Immunol 180 8272 8279
    • (2008) J Immunol , vol.180 , pp. 8272-8279
    • Radke, J.R.1    Siddiqui, Z.K.2    Miura, T.A.3    Routes, J.M.4    Cook, J.L.5
  • 26
    • 44149110803 scopus 로고    scopus 로고
    • Caspase 2 is both required for p53-mediated apoptosis and downregulated by p53 in a p21-dependent manner
    • N Baptiste-Okoh AM Barsotti C Prives 2008 Caspase 2 is both required for p53-mediated apoptosis and downregulated by p53 in a p21-dependent manner Cell Cycle 7 1133 1138 (Pubitemid 351749262)
    • (2008) Cell Cycle , vol.7 , Issue.9 , pp. 1133-1138
    • Baptiste-Okoh, N.1    Barsotti, A.M.2    Prives, C.3
  • 27
    • 48349083376 scopus 로고    scopus 로고
    • TAp73beta and DNp73beta activate the expression of the pro-survival caspase-2S
    • 10.1093/nar/gkn414
    • WH Toh E Logette L Corcos K Sabapathy 2008 TAp73beta and DNp73beta activate the expression of the pro-survival caspase-2S Nucleic Acids Res 36 4498 4509 10.1093/nar/gkn414
    • (2008) Nucleic Acids Res , vol.36 , pp. 4498-4509
    • Toh, W.H.1    Logette, E.2    Corcos, L.3    Sabapathy, K.4
  • 28
    • 38049086171 scopus 로고    scopus 로고
    • PKC zeta controls DNA topoisomerase-dependent human caspase-2 pre-mRNA splicing
    • 10.1016/j.febslet.2007.12.032
    • S Solier MC De Cian A Bettaieb L Desoche E Solary L Corcos 2008 PKC zeta controls DNA topoisomerase-dependent human caspase-2 pre-mRNA splicing FEBS Lett 582 372 378 10.1016/j.febslet.2007.12.032
    • (2008) FEBS Lett , vol.582 , pp. 372-378
    • Solier, S.1    De Cian, M.C.2    Bettaieb, A.3    Desoche, L.4    Solary, E.5    Corcos, L.6
  • 29
    • 0037191508 scopus 로고    scopus 로고
    • Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells
    • 10.1016/S0304-3835(02)00287-2
    • A Wotawa S Solier E Logette E Solary L Corcos 2002 Differential influence of etoposide on two caspase-2 mRNA isoforms in leukemic cells Cancer Lett 185 181 189 10.1016/S0304-3835(02)00287-2
    • (2002) Cancer Lett , vol.185 , pp. 181-189
    • Wotawa, A.1    Solier, S.2    Logette, E.3    Solary, E.4    Corcos, L.5
  • 30
    • 20044363604 scopus 로고    scopus 로고
    • Regulation of alternative splicing of caspase-2 through an intracellular signaling pathway in response to pro-apoptotic stimuli
    • 10.1016/j.lab.2004.11.020
    • N Iwanaga M Kamachi K Aratake 2005 Regulation of alternative splicing of caspase-2 through an intracellular signaling pathway in response to pro-apoptotic stimuli J Lab Clin Med 145 105 110 10.1016/j.lab.2004.11.020
    • (2005) J Lab Clin Med , vol.145 , pp. 105-110
    • Iwanaga, N.1    Kamachi, M.2    Aratake, K.3
  • 32
    • 0034327412 scopus 로고    scopus 로고
    • The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: Identification and evaluation of the resident candidate tumor suppressor genes. the International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium
    • MI Lerman JD Minna 2000 The 630-kb lung cancer homozygous deletion region on human chromosome 3p21.3: identification and evaluation of the resident candidate tumor suppressor genes. The International Lung Cancer Chromosome 3p21.3 Tumor Suppressor Gene Consortium Cancer Res 60 6116 6133
    • (2000) Cancer Res , vol.60 , pp. 6116-6133
    • Lerman, M.I.1    Minna, J.D.2
  • 33
    • 42349106119 scopus 로고    scopus 로고
    • Down-regulation of caspase-2 by rottlerin via protein kinase C-delta-independent pathway
    • 10.1158/0008-5472.CAN-07-6244
    • A Basu B Adkins C Basu 2008 Down-regulation of caspase-2 by rottlerin via protein kinase C-delta-independent pathway Cancer Res 68 2795 2802 10.1158/0008-5472.CAN-07-6244
    • (2008) Cancer Res , vol.68 , pp. 2795-2802
    • Basu, A.1    Adkins, B.2    Basu, C.3
  • 35
    • 0032544397 scopus 로고    scopus 로고
    • Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor
    • 10.1074/jbc.273.38.24535
    • PA Colussi NL Harvey S Kumar 1998 Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor A novel function for a caspase prodomain. J Biol Chem 273 24535 24542 10.1074/jbc.273.38.24535
    • (1998) A Novel Function for A Caspase Prodomain. J Biol Chem , vol.273 , pp. 24535-24542
    • Colussi, P.A.1    Harvey, N.L.2    Kumar, S.3
  • 36
    • 0037177809 scopus 로고    scopus 로고
    • Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus
    • 10.1074/jbc.M112338200
    • G Paroni C Henderson C Schneider C Brancolini 2002 Caspase-2 can trigger cytochrome c release and apoptosis from the nucleus J Biol Chem 277 15147 15161 10.1074/jbc.M112338200
    • (2002) J Biol Chem , vol.277 , pp. 15147-15161
    • Paroni, G.1    Henderson, C.2    Schneider, C.3    Brancolini, C.4
  • 37
    • 33745242294 scopus 로고    scopus 로고
    • Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: A role for the IAPs
    • DOI 10.1016/j.yexcr.2006.03.027, PII S0014482706001364
    • HH Cheung N Lynn Kelly P Liston RG Korneluk 2006 Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: a role for the IAPs Exp Cell Res 312 12 2347 2357 (Pubitemid 43928950)
    • (2006) Experimental Cell Research , vol.312 , Issue.12 , pp. 2347-2357
    • Cheung, H.H.1    Lynn Kelly, N.2    Liston, P.3    Korneluk, R.G.4
  • 38
    • 65349178993 scopus 로고    scopus 로고
    • Caspase-2 activation in the absence of PIDDosome formation
    • 10.1083/jcb.200811105
    • C Manzl G Krumschnabel F Bock 2009 Caspase-2 activation in the absence of PIDDosome formation J Cell Biol 185 291 303 10.1083/jcb.200811105
    • (2009) J Cell Biol , vol.185 , pp. 291-303
    • Manzl, C.1    Krumschnabel, G.2    Bock, F.3
  • 39
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: Their intracellular localization and translocation during apoptosis
    • B Zhivotovsky A Samali A Gahm S Orrenius 1999 Caspases: their intracellular localization and translocation during apoptosis Cell Death Differ 6 644 651 10.1038/sj.cdd.4400536 (Pubitemid 29366654)
    • (1999) Cell Death and Differentiation , vol.6 , Issue.7 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4
  • 40
    • 18844450183 scopus 로고    scopus 로고
    • Caspase recruitment domain of procaspase-2 could be a target for SUMO-1 modification through Ubc9
    • 10.1016/j.bbrc.2005.04.019
    • H Shirakura N Hayashi S Ogino K Tsuruma T Uehara Y Nomura 2005 Caspase recruitment domain of procaspase-2 could be a target for SUMO-1 modification through Ubc9 Biochem Biophys Res Commun 331 1007 1015 10.1016/j.bbrc.2005.04.019
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 1007-1015
    • Shirakura, H.1    Hayashi, N.2    Ogino, S.3    Tsuruma, K.4    Uehara, T.5    Nomura, Y.6
  • 41
    • 0034194338 scopus 로고    scopus 로고
    • Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis
    • 10.1083/jcb.149.3.603
    • M Mancini CE Machamer S Roy 2000 Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis J Cell Biol 149 603 612 10.1083/jcb.149.3.603
    • (2000) J Cell Biol , vol.149 , pp. 603-612
    • Mancini, M.1    MacHamer, C.E.2    Roy, S.3
  • 42
    • 0035298087 scopus 로고    scopus 로고
    • Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases
    • 10.1006/excr.2000.5153
    • Y Shikama M U T Miyashita M Yamada 2001 Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases Exp Cell Res 264 315 325 10.1006/excr.2000.5153
    • (2001) Exp Cell Res , vol.264 , pp. 315-325
    • Shikama, Y.1    M, U.2    Miyashita, T.3    Yamada, M.4
  • 43
    • 0038136890 scopus 로고    scopus 로고
    • Role of prodomain in importin-mediated nuclear localization and activation of caspase-2
    • 10.1074/jbc.M211512200
    • BC Baliga PA Colussi SH Read MM Dias DA Jans S Kumar 2003 Role of prodomain in importin-mediated nuclear localization and activation of caspase-2 J Biol Chem 278 4899 4905 10.1074/jbc.M211512200
    • (2003) J Biol Chem , vol.278 , pp. 4899-4905
    • Baliga, B.C.1    Colussi, P.A.2    Read, S.H.3    Dias, M.M.4    Jans, D.A.5    Kumar, S.6
  • 44
    • 25444517110 scopus 로고    scopus 로고
    • Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies
    • 10.1158/1535-7163.MCT-05-0041
    • J Tang W Xie X Yang 2005 Association of caspase-2 with the promyelocytic leukemia protein nuclear bodies Cancer Biol Ther 4 645 649 10.1158/1535-7163. MCT-05-0041
    • (2005) Cancer Biol Ther , vol.4 , pp. 645-649
    • Tang, J.1    Xie, W.2    Yang, X.3
  • 45
    • 0034306019 scopus 로고    scopus 로고
    • The function of PML in p53-dependent apoptosis
    • 10.1038/35036365
    • A Guo P Salomoni J Luo 2000 The function of PML in p53-dependent apoptosis Nat Cell Biol 2 730 736 10.1038/35036365
    • (2000) Nat Cell Biol , vol.2 , pp. 730-736
    • Guo, A.1    Salomoni, P.2    Luo, J.3
  • 46
    • 0025633966 scopus 로고
    • Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis
    • C Szostecki HH Guldner HJ Netter H Will 1990 Isolation and characterization of cDNA encoding a human nuclear antigen predominantly recognized by autoantibodies from patients with primary biliary cirrhosis J Immunol 145 4338 4347
    • (1990) J Immunol , vol.145 , pp. 4338-4347
    • Szostecki, C.1    Guldner, H.H.2    Netter, H.J.3    Will, H.4
  • 47
    • 0032721540 scopus 로고    scopus 로고
    • PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1
    • 10.1083/jcb.147.2.221
    • AM Ishov AG Sotnikov D Negorev 1999 PML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1 J Cell Biol 147 221 234 10.1083/jcb.147.2.221
    • (1999) J Cell Biol , vol.147 , pp. 221-234
    • Ishov, A.M.1    Sotnikov, A.G.2    Negorev, D.3
  • 48
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: Dynamic sensors of DNA damage and cellular stress
    • 10.1002/bies.20089
    • G Dellaire DP Bazett-Jones 2004 PML nuclear bodies: dynamic sensors of DNA damage and cellular stress Bioessays 26 963 977 10.1002/bies.20089
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 49
    • 34548501553 scopus 로고    scopus 로고
    • Are promyelocytic leukaemia protein nuclear bodies a scaffold for caspase-2 programmed cell death?
    • 10.1016/j.tibs.2007.08.001
    • L Sanchez-Pulido A Valencia AM Rojas 2007 Are promyelocytic leukaemia protein nuclear bodies a scaffold for caspase-2 programmed cell death? Trends Biochem Sci 32 400 406 10.1016/j.tibs.2007.08.001
    • (2007) Trends Biochem Sci , vol.32 , pp. 400-406
    • Sanchez-Pulido, L.1    Valencia, A.2    Rojas, A.M.3
  • 50
    • 0033579810 scopus 로고    scopus 로고
    • Mitochondrial release of caspase-2 and -9 during the apoptotic process
    • 10.1084/jem.189.2.381
    • SA Susin HK Lorenzo N Zamzami 1999 Mitochondrial release of caspase-2 and -9 during the apoptotic process J Exp Med 189 381 394 10.1084/jem.189.2.381
    • (1999) J Exp Med , vol.189 , pp. 381-394
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 51
    • 0036848165 scopus 로고    scopus 로고
    • Caspases are not localized in mitochondria during life or death
    • 10.1038/sj.cdd.4401101
    • G van Loo X Saelens F Matthijssens 2002 Caspases are not localized in mitochondria during life or death Cell Death Differ 9 1207 1211 10.1038/sj.cdd.4401101
    • (2002) Cell Death Differ , vol.9 , pp. 1207-1211
    • Van Loo, G.1    Saelens, X.2    Matthijssens, F.3
  • 52
    • 0035960537 scopus 로고    scopus 로고
    • Differential subcellular localization of caspase family proteins in the adult rat brain
    • 10.1016/S0304-3940(01)02336-9
    • S Shimohama H Tanino S Fujimoto 2001 Differential subcellular localization of caspase family proteins in the adult rat brain Neurosci Lett 315 125 128 10.1016/S0304-3940(01)02336-9
    • (2001) Neurosci Lett , vol.315 , pp. 125-128
    • Shimohama, S.1    Tanino, H.2    Fujimoto, S.3
  • 53
    • 0031018396 scopus 로고    scopus 로고
    • Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) downregulation, in sympathetic neurons and PC12 cells
    • CM Troy L Stefanis LA Greene ML Shelanski 1997 Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) downregulation, in sympathetic neurons and pc12 cells J Neurosci 17 1911 1918 (Pubitemid 27106750)
    • (1997) Journal of Neuroscience , vol.17 , Issue.6 , pp. 1911-1918
    • Troy, C.M.1    Stefanis, L.2    Greene, L.A.3    Shelanski, M.L.4
  • 54
    • 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-1β-converting enzyme
    • S Kumar M Kinoshita M Noda NG Copeland NA Jenkins 1994 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 8 1613 1626 10.1101/gad.8.14.1613 (Pubitemid 24236241)
    • (1994) Genes and Development , vol.8 , Issue.14 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 56
    • 0034954981 scopus 로고    scopus 로고
    • Caspase-2 deficiency prevents programmed germ cell death resulting from cytokine insufficiency but not meiotic defects caused by loss of ataxia telangiectasia-mutated (ATM) gene function
    • 10.1038/sj.cdd.4400845
    • Y Morita DV Maravei L Bergeron 2001 Caspase-2 deficiency prevents programmed germ cell death resulting from cytokine insufficiency but not meiotic defects caused by loss of ataxia telangiectasia-mutated (ATM) gene function Cell Death Differ 8 614 620 10.1038/sj.cdd.4400845
    • (2001) Cell Death Differ , vol.8 , pp. 614-620
    • Morita, Y.1    Maravei, D.V.2    Bergeron, L.3
  • 57
    • 33846202919 scopus 로고    scopus 로고
    • Caspase-2 deficiency enhances aging-related traits in mice
    • 10.1016/j.mad.2006.11.030
    • Y Zhang SS Padalecki AR Chaudhuri 2006 Caspase-2 deficiency enhances aging-related traits in mice Mech Ageing Dev 128 2 213 221 10.1016/j.mad.2006. 11.030
    • (2006) Mech Ageing Dev , vol.128 , Issue.2 , pp. 213-221
    • Zhang, Y.1    Padalecki, S.S.2    Chaudhuri, A.R.3
  • 59
    • 0029062524 scopus 로고
    • Apoptosis regulatory gene NEDD2 maps to human chromosome segment 7q34-35, a region frequently affected in haematological neoplasms
    • 10.1007/BF00209480
    • S Kumar DL White S Takai S Turczynowicz CA Juttner TP Hughes 1995 Apoptosis regulatory gene NEDD2 maps to human chromosome segment 7q34-35, a region frequently affected in haematological neoplasms Hum Genet 95 641 644 10.1007/BF00209480
    • (1995) Hum Genet , vol.95 , pp. 641-644
    • Kumar, S.1    White, D.L.2    Takai, S.3    Turczynowicz, S.4    Juttner, C.A.5    Hughes, T.P.6
  • 60
    • 23944464465 scopus 로고    scopus 로고
    • Decreased PARP and procaspase-2 protein levels are associated with cellular drug resistance in childhood acute lymphoblastic leukemia
    • 10.1182/blood-2004-11-4296
    • A Holleman ML den Boer KM Kazemier 2005 Decreased PARP and procaspase-2 protein levels are associated with cellular drug resistance in childhood acute lymphoblastic leukemia Blood 106 1817 1823 10.1182/blood-2004-11-4296
    • (2005) Blood , vol.106 , pp. 1817-1823
    • Holleman, A.1    Den Boer, M.L.2    Kazemier, K.M.3
  • 61
    • 0035437143 scopus 로고    scopus 로고
    • Altered apoptosis pathways in mantle cell lymphoma detected by oligonucleotide microarray
    • 10.1182/blood.V98.3.787
    • WK Hofmann S de Vos K Tsukasaki 2001 Altered apoptosis pathways in mantle cell lymphoma detected by oligonucleotide microarray Blood 98 787 794 10.1182/blood.V98.3.787
    • (2001) Blood , vol.98 , pp. 787-794
    • Hofmann, W.K.1    De Vos, S.2    Tsukasaki, K.3
  • 64
    • 0037076326 scopus 로고    scopus 로고
    • Cyclin D3 activates caspase 2, connecting cell proliferation with cell death
    • 10.1073/pnas.072290599
    • AR Mendelsohn JD Hamer ZB Wang R Brent 2002 Cyclin D3 activates caspase 2, connecting cell proliferation with cell death Proc Natl Acad Sci USA 99 6871 6876 10.1073/pnas.072290599
    • (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
  • 65
    • 3042592579 scopus 로고    scopus 로고
    • Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9
    • 10.1083/jcb.200312030
    • VS Marsden PG Ekert M Van Delft DL Vaux JM Adams A Strasser 2004 Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9 J Cell Biol 165 775 780 10.1083/jcb.200312030
    • (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
  • 66
    • 59049093349 scopus 로고    scopus 로고
    • DNA-PKcs-PIDDosome: A nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance
    • 10.1016/j.cell.2008.12.021
    • M Shi CJ Vivian KJ Lee 2009 DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance Cell 136 508 520 10.1016/j.cell.2008.12.021
    • (2009) Cell , vol.136 , pp. 508-520
    • Shi, M.1    Vivian, C.J.2    Lee, K.J.3
  • 67
    • 33748685227 scopus 로고    scopus 로고
    • Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage
    • 10.1038/sj.onc.1209569
    • H Vakifahmetoglu M Olsson S Orrenius B Zhivotovsky 2006 Functional connection between p53 and caspase-2 is essential for apoptosis induced by DNA damage Oncogene 25 5683 5692 10.1038/sj.onc.1209569
    • (2006) Oncogene , vol.25 , pp. 5683-5692
    • Vakifahmetoglu, H.1    Olsson, M.2    Orrenius, S.3    Zhivotovsky, B.4
  • 68
    • 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
    • 10.1091/mbc.E04-10-0862
    • T Panaretakis E Laane K Pokrovskaja 2005 Doxorubicin requires the sequential activation of caspase-2, protein kinase Cdelta, and c-Jun NH2-terminal kinase to induce apoptosis Mol Biol Cell 16 3821 3831 10.1091/mbc.E04-10-0862
    • (2005) Mol Biol Cell , vol.16 , pp. 3821-3831
    • Panaretakis, T.1    Laane, E.2    Pokrovskaja, K.3
  • 69
    • 47249134609 scopus 로고    scopus 로고
    • C-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis
    • 10.1074/jbc.M801107200
    • X Cao RL Bennett WS May 2008 c-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis J Biol Chem 283 14490 14496 10.1074/jbc.M801107200
    • (2008) J Biol Chem , vol.283 , pp. 14490-14496
    • Cao, X.1    Bennett, R.L.2    May, W.S.3
  • 70
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • 10.1126/science.1074721
    • P Lassus X Opitz-Araya Y Lazebnik 2002 Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization Science 297 1352 1354 10.1126/science.1074721
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 72
    • 0037119491 scopus 로고    scopus 로고
    • Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis
    • 10.1074/jbc.M204185200
    • JD Robertson M Enoksson M Suomela B Zhivotovsky S Orrenius 2002 Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis J Biol Chem 277 29803 29809 10.1074/jbc.M204185200
    • (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
  • 73
    • 4544274785 scopus 로고    scopus 로고
    • Caspase-2 can function upstream of Bid cleavage in the TRAIL apoptosis pathway
    • 10.1074/jbc.M400708200
    • KW Wagner IH Engels QL Deveraux 2004 Caspase-2 can function upstream of Bid cleavage in the TRAIL apoptosis pathway J Biol Chem 279 35047 35052 10.1074/jbc.M400708200
    • (2004) J Biol Chem , vol.279 , pp. 35047-35052
    • Wagner, K.W.1    Engels, I.H.2    Deveraux, Q.L.3
  • 74
    • 44149090307 scopus 로고    scopus 로고
    • Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3
    • 10.1016/j.cell.2008.03.037
    • S Sidi T Sanda RD Kennedy 2008 Chk1 suppresses a caspase-2 apoptotic response to DNA damage that bypasses p53, Bcl-2, and caspase-3 Cell 133 864 877 10.1016/j.cell.2008.03.037
    • (2008) Cell , vol.133 , pp. 864-877
    • Sidi, S.1    Sanda, T.2    Kennedy, R.D.3
  • 75
    • 3042537050 scopus 로고    scopus 로고
    • Mitotic catastrophe constitutes a special case of apoptosis whose suppression entails aneuploidy
    • 10.1038/sj.onc.1207572
    • M Castedo JL Perfettini T Roumier 2004 Mitotic catastrophe constitutes a special case of apoptosis whose suppression entails aneuploidy Oncogene 23 4362 4370 10.1038/sj.onc.1207572
    • (2004) Oncogene , vol.23 , pp. 4362-4370
    • Castedo, M.1    Perfettini, J.L.2    Roumier, T.3
  • 76
    • 33847368592 scopus 로고    scopus 로고
    • Docetaxel-induced apoptosis in melanoma cells is dependent on activation of caspase-2
    • 10.1158/1535-7163.MCT-06-0564
    • NM Mhaidat Y Wang KA Kiejda XD Zhang P Hersey 2007 Docetaxel-induced apoptosis in melanoma cells is dependent on activation of caspase-2 Mol Cancer Ther 6 752 761 10.1158/1535-7163.MCT-06-0564
    • (2007) Mol Cancer Ther , vol.6 , pp. 752-761
    • Mhaidat, N.M.1    Wang, Y.2    Kiejda, K.A.3    Zhang, X.D.4    Hersey, P.5
  • 77
    • 44149087374 scopus 로고    scopus 로고
    • Caspase-2 is required for cell death induced by cytoskeletal disruption
    • 10.1038/sj.onc.1211005
    • LH Ho SH Read L Dorstyn L Lambrusco S Kumar 2008 Caspase-2 is required for cell death induced by cytoskeletal disruption Oncogene 27 3393 3404 10.1038/sj.onc.1211005
    • (2008) Oncogene , vol.27 , pp. 3393-3404
    • Ho, L.H.1    Read, S.H.2    Dorstyn, L.3    Lambrusco, L.4    Kumar, S.5
  • 78
    • 30344459150 scopus 로고    scopus 로고
    • In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis
    • 10.1038/ncb1340
    • S Tu GP McStay LM Boucher T Mak HM Beere DR Green 2005 In situ trapping of activated initiator caspases reveals a role for caspase-2 in heat shock-induced apoptosis Nat Cell Biol 8 72 77 10.1038/ncb1340
    • (2005) 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
  • 79
    • 33745223497 scopus 로고    scopus 로고
    • Heat shock induces apoptosis independently of any known initiator caspase-activating complex
    • 10.1074/jbc.M512754200
    • RS Milleron SB Bratton 2006 Heat shock induces apoptosis independently of any known initiator caspase-activating complex J Biol Chem 281 16991 17000 10.1074/jbc.M512754200
    • (2006) J Biol Chem , vol.281 , pp. 16991-17000
    • Milleron, R.S.1    Bratton, S.B.2
  • 80
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts-requirement for datp and cytochrome c
    • 10.1016/S0092-8674(00)80085-9
    • XS Liu CN Kim J Yang R Jemmerson XD Wang 1996 Induction of apoptotic program in cell-free extracts-requirement for datp and cytochrome c Cell 86 147 157 10.1016/S0092-8674(00)80085-9
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.S.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.D.5
  • 81
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues
    • 10.1016/S1097-2765(00)00136-2
    • T Lindsten AJ Ross A King 2000 The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues Mol Cell 6 1389 1399 10.1016/S1097-2765(00)00136-2
    • (2000) Mol Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1    Ross, A.J.2    King, A.3
  • 82
    • 44949233264 scopus 로고    scopus 로고
    • Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress
    • 10.1128/MCB.00013-08
    • JP Upton K Austgen M Nishino 2008 Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress Mol Cell Biol 28 3943 3951 10.1128/MCB.00013-08
    • (2008) Mol Cell Biol , vol.28 , pp. 3943-3951
    • Upton, J.P.1    Austgen, K.2    Nishino, M.3
  • 83
    • 53349101501 scopus 로고    scopus 로고
    • Caspase-2 functions upstream of mitochondria in endoplasmic reticulum stress-induced apoptosis by bortezomib in human myeloma cells
    • 10.1158/1535-7163.MCT-08-0186
    • H Gu X Chen G Gao H Dong 2008 Caspase-2 functions upstream of mitochondria in endoplasmic reticulum stress-induced apoptosis by bortezomib in human myeloma cells Mol Cancer Ther 7 2298 2307 10.1158/1535-7163.MCT-08-0186
    • (2008) Mol Cancer Ther , vol.7 , pp. 2298-2307
    • Gu, H.1    Chen, X.2    Gao, G.3    Dong, H.4
  • 84
    • 0035869463 scopus 로고    scopus 로고
    • Involvement of caspase-2 long isoform in Fas-mediated cell death of human leukemic cells
    • 10.1182/blood.V97.6.1835
    • N Droin F Bichat C Rebe 2001 Involvement of caspase-2 long isoform in Fas-mediated cell death of human leukemic cells Blood 97 1835 1844 10.1182/blood.V97.6.1835
    • (2001) Blood , vol.97 , pp. 1835-1844
    • Droin, N.1    Bichat, F.2    Rebe, C.3
  • 85
    • 3142581992 scopus 로고    scopus 로고
    • Requirement for aspartate-cleaved bid in apoptosis signaling by DNA-damaging anti-cancer regimens
    • 10.1074/jbc.M400268200
    • AB Werner SW Tait E de Vries E Eldering J Borst 2004 Requirement for aspartate-cleaved bid in apoptosis signaling by DNA-damaging anti-cancer regimens J Biol Chem 279 28771 28780 10.1074/jbc.M400268200
    • (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
  • 86
    • 27144512715 scopus 로고    scopus 로고
    • Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8
    • 10.1038/sj.emboj.7600827
    • S Shin Y Lee W Kim H Ko H Choi K Kim 2005 Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8 EMBO J 24 3532 3542 10.1038/sj.emboj.7600827
    • (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
  • 87
    • 22344435528 scopus 로고    scopus 로고
    • Bid is upstream of lysosome-mediated caspase 2 activation in tumor necrosis factor alpha-induced hepatocyte apoptosis
    • 10.1053/j.gastro.2005.05.022
    • ME Guicciardi SF Bronk NW Werneburg XM Yin GJ Gores 2005 Bid is upstream of lysosome-mediated caspase 2 activation in tumor necrosis factor alpha-induced hepatocyte apoptosis Gastroenterology 129 269 284 10.1053/j.gastro.2005.05.022
    • (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
  • 89
    • 0035879074 scopus 로고    scopus 로고
    • Death in the balance: Alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation
    • CM Troy SA Rabacchi JB Hohl JM Angelastro LA Greene ML Shelanski 2001 Death in the balance: alternative participation of the caspase-2 and -9 pathways in neuronal death induced by nerve growth factor deprivation J Neurosci 21 5007 5016 (Pubitemid 32622926)
    • (2001) Journal of Neuroscience , vol.21 , Issue.14 , pp. 5007-5016
    • Troy, C.M.1    Rabacchi, S.A.2    Hohl, J.B.3    Angelastro, J.M.4    Greene, L.A.5    Shelanski, M.L.6
  • 91
    • 26244453715 scopus 로고    scopus 로고
    • Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2
    • 10.1016/j.cell.2005.07.032
    • LK Nutt SS Margolis M Jensen 2005 Metabolic regulation of oocyte cell death through the CaMKII-mediated phosphorylation of caspase-2 Cell 123 89 103 10.1016/j.cell.2005.07.032
    • (2005) Cell , vol.123 , pp. 89-103
    • Nutt, L.K.1    Margolis, S.S.2    Jensen, M.3
  • 92
    • 0030948457 scopus 로고    scopus 로고
    • Substrate specificities of caspase family proteases
    • 10.1074/jbc.272.15.9677
    • RV Talanian C Quinlan S Trautz 1997 Substrate specificities of caspase family proteases J Biol Chem 272 9677 9682 10.1074/jbc.272.15.9677
    • (1997) J Biol Chem , vol.272 , pp. 9677-9682
    • Talanian, R.V.1    Quinlan, C.2    Trautz, S.3
  • 93
    • 38049119903 scopus 로고    scopus 로고
    • Overlapping cleavage motif selectivity of caspases: Implications for analysis of apoptotic pathways
    • 10.1038/sj.cdd.4402260
    • GP McStay GS Salvesen DR Green 2007 Overlapping cleavage motif selectivity of caspases: implications for analysis of apoptotic pathways Cell Death Differ 15 322 331 10.1038/sj.cdd.4402260
    • (2007) Cell Death Differ , vol.15 , pp. 322-331
    • McStay, G.P.1    Salvesen, G.S.2    Green, D.R.3
  • 94
    • 56049116880 scopus 로고    scopus 로고
    • Some commonly used caspase substrates and inhibitors lack the specificity required to monitor individual caspase activity
    • 10.1016/j.bbrc.2008.10.101
    • NA Pereira Z Song 2008 Some commonly used caspase substrates and inhibitors lack the specificity required to monitor individual caspase activity Biochem Biophys Res Commun 377 873 877 10.1016/j.bbrc.2008.10.101
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 873-877
    • Pereira, N.A.1    Song, Z.2
  • 96
    • 50349089817 scopus 로고    scopus 로고
    • Caspase assays: Identifying caspase activity and substrates in vitro and in vivo
    • 10.1016/S0076-6879(08)01621-2
    • C Pop GS Salvesen FL Scott 2008 Caspase assays: identifying caspase activity and substrates in vitro and in vivo Methods Enzymol 446 351 367 10.1016/S0076-6879(08)01621-2
    • (2008) Methods Enzymol , vol.446 , pp. 351-367
    • Pop, C.1    Salvesen, G.S.2    Scott, F.L.3
  • 97
    • 0037804642 scopus 로고    scopus 로고
    • Wither RNAi
    • Editorial
    • Editorial 2008 Wither RNAi Nat Cell Biol 5 489 490
    • (2008) Nat Cell Biol , vol.5 , pp. 489-490
  • 98
    • 34247853389 scopus 로고    scopus 로고
    • Inhibition of caspase-2 by a designed ankyrin repeat protein: Specificity, structure, and inhibition mechanism
    • 10.1016/j.str.2007.03.014
    • A Schweizer H Roschitzki-Voser P Amstutz 2007 Inhibition of caspase-2 by a designed ankyrin repeat protein: specificity, structure, and inhibition mechanism Structure 15 625 636 10.1016/j.str.2007.03.014
    • (2007) Structure , vol.15 , pp. 625-636
    • Schweizer, A.1    Roschitzki-Voser, H.2    Amstutz, P.3
  • 99
    • 27744477444 scopus 로고    scopus 로고
    • Mammalian initiator apoptotic caspases
    • 10.1111/j.1742-4658.2005.04966.x
    • PK Ho CJ Hawkins 2005 Mammalian initiator apoptotic caspases FEBS J 272 5436 5453 10.1111/j.1742-4658.2005.04966.x
    • (2005) FEBS J , vol.272 , pp. 5436-5453
    • Ho, P.K.1    Hawkins, C.J.2
  • 100
    • 33845501864 scopus 로고    scopus 로고
    • Apoptosome: A platform for the activation of initiator caspases
    • 10.1038/sj.cdd.4402028
    • Q Bao Y Shi 2007 Apoptosome: a platform for the activation of initiator caspases Cell Death Differ 14 56 65 10.1038/sj.cdd.4402028
    • (2007) Cell Death Differ , vol.14 , pp. 56-65
    • Bao, Q.1    Shi, Y.2
  • 101
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • 10.1038/nrm2153
    • SJ Riedl GS Salvesen 2007 The apoptosome: signalling platform of cell death Nat Rev Mol Cell Biol 8 405 413 10.1038/nrm2153
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 102
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • 10.1038/sj.onc.1207102
    • S Cory DC Huang JM Adams 2003 The Bcl-2 family: roles in cell survival and oncogenesis Oncogene 22 8590 8607 10.1038/sj.onc.1207102
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 103
    • 0030881653 scopus 로고    scopus 로고
    • Activation of caspase-2 in apoptosis
    • 10.1074/jbc.272.34.21010
    • H Li L Bergeron V Cryns 1997 Activation of caspase-2 in apoptosis J Biol Chem 272 21010 21017 10.1074/jbc.272.34.21010
    • (1997) J Biol Chem , vol.272 , pp. 21010-21017
    • Li, H.1    Bergeron, L.2    Cryns, V.3
  • 104
    • 17244368276 scopus 로고    scopus 로고
    • Structure of the apoptotic protease-activating factor 1 bound to ADP
    • 10.1038/nature03465
    • SJ Riedl W Li Y Chao R Schwarzenbacher Y Shi 2005 Structure of the apoptotic protease-activating factor 1 bound to ADP Nature 434 926 933 10.1038/nature03465
    • (2005) Nature , vol.434 , pp. 926-933
    • Riedl, S.J.1    Li, W.2    Chao, Y.3    Schwarzenbacher, R.4    Shi, Y.5
  • 105
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • 10.1016/S1097-2765(02)00442-2
    • D Acehan X Jiang DG Morgan JE Heuser X Wang CW Akey 2002 Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation Mol Cell 9 423 432 10.1016/S1097-2765(02) 00442-2
    • (2002) Mol Cell , vol.9 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 106
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • 10.1101/gad.13.24.3179
    • J Rodriguez Y Lazebnik 1999 Caspase-9 and APAF-1 form an active holoenzyme Genes Dev 15 3179 3184 10.1101/gad.13.24.3179
    • (1999) Genes Dev , vol.15 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 107
    • 0033605722 scopus 로고    scopus 로고
    • Caspase-9 can be activated without proteolytic processing
    • 10.1074/jbc.274.13.8359
    • H Stennicke Q Deveraux E Humke J Reed V Dixit G Salvesen 1999 Caspase-9 can be activated without proteolytic processing J Biol Chem 274 8359 8362 10.1074/jbc.274.13.8359
    • (1999) J Biol Chem , vol.274 , pp. 8359-8362
    • Stennicke, H.1    Deveraux, Q.2    Humke, E.3    Reed, J.4    Dixit, V.5    Salvesen, G.6
  • 108
    • 22744436580 scopus 로고    scopus 로고
    • Engineering a dimeric caspase-9: A re-evaluation of the induced proximity model for caspase activation
    • 10.1371/journal.pbio.0030183
    • Y Chao EN Shiozaki SM Srinivasula DJ Rigotti R Fairman Y Shi 2005 Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation PLoS Biol 3 e183 10.1371/journal.pbio.0030183
    • (2005) PLoS Biol , vol.3 , pp. 183
    • Chao, Y.1    Shiozaki, E.N.2    Srinivasula, S.M.3    Rigotti, D.J.4    Fairman, R.5    Shi, Y.6
  • 109
    • 0032549652 scopus 로고    scopus 로고
    • Dimerization and autoprocessing of the Nedd2 (Caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions
    • 10.1074/jbc.273.12.6763
    • AJ Butt NL Harvey G Parasivam S Kumar 1998 Dimerization and autoprocessing of the Nedd2 (Caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions J Biol Chem 273 6763 6768 10.1074/jbc.273.12. 6763
    • (1998) J Biol Chem , vol.273 , pp. 6763-6768
    • Butt, A.J.1    Harvey, N.L.2    Parasivam, G.3    Kumar, S.4
  • 110
    • 0032500552 scopus 로고    scopus 로고
    • Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain
    • 10.1074/jbc.273.41.26566
    • PA Colussi NL Harvey LM Shearwin-Whyatt S Kumar 1998 Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain J Biol Chem 273 26566 26570 10.1074/jbc.273.41.26566
    • (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
  • 111
    • 0031021356 scopus 로고    scopus 로고
    • RAIDDis a new death adaptor molecule
    • 10.1038/385086a0
    • H Duan VM Dixit 1997 RAIDDis a new death adaptor molecule Nature 385 86 89 10.1038/385086a0
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 113
    • 0029054725 scopus 로고
    • RIP-a novel protein containing a death domain that interacts with Fas/Apo-1 (CD95) in yeast and causes cell death
    • 10.1016/0092-8674(95)90072-1
    • BZ Stanger P Leder TH Lee E Kim B Seed 1995 RIP-a novel protein containing a death domain that interacts with Fas/Apo-1 (CD95) in yeast and causes cell death Cell 81 513 523 10.1016/0092-8674(95)90072-1
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 114
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • 10.1016/S1074-7613(00)80252-6
    • HL Hsu JN Huang HB Shu V Baichwal DV Goeddel 1996 TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex Immunity 4 387 396 10.1016/S1074-7613(00)80252-6
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.L.1    Huang, J.N.2    Shu, H.B.3    Baichwal, V.4    Goeddel, D.V.5
  • 115
    • 0037049549 scopus 로고    scopus 로고
    • A novel Apaf-1-independent putative caspase-2 activation complex
    • 10.1083/jcb.200209004
    • SH Read BC Baliga PG Ekert DL Vaux S Kumar 2002 A novel Apaf-1-independent putative caspase-2 activation complex J Cell Biol 159 739 745 10.1083/jcb.200209004
    • (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
  • 116
    • 0032574745 scopus 로고    scopus 로고
    • ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases
    • 10.1073/pnas.95.9.5156
    • T Koseki N Inohara S Chen G Nunez 1998 ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases Proc Natl Acad Sci USA 95 5156 5160 10.1073/pnas.95.9.5156
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5156-5160
    • Koseki, T.1    Inohara, N.2    Chen, S.3    Nunez, G.4
  • 117
    • 0035800827 scopus 로고    scopus 로고
    • Characterization of a novel pro-apoptotic caspase-2 and -9 binding protein
    • 10.1074/jbc.M100684200
    • E Bonfoco E Li F Kolbinger NR Cooper 2001 Characterization of a novel pro-apoptotic caspase-2 and -9 binding protein J Biol Chem 276 29242 29250 10.1074/jbc.M100684200
    • (2001) J Biol Chem , vol.276 , pp. 29242-29250
    • Bonfoco, E.1    Li, E.2    Kolbinger, F.3    Cooper, N.R.4
  • 118
    • 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
    • 10.1074/jbc.M009853200
    • T Hlaing RF Guo KA Dilley 2001 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 276 9230 9238 10.1074/jbc.M009853200
    • (2001) J Biol Chem , vol.276 , pp. 9230-9238
    • Hlaing, T.1    Guo, R.F.2    Dilley, K.A.3
  • 119
    • 8844254088 scopus 로고    scopus 로고
    • Regulation of procaspase-2 by glucocorticoid modulatory element-binding protein 1 through the interaction with caspase recruitment domain
    • 10.1016/j.bbrc.2004.10.145
    • K Tsuruma T Nakagawa H Shirakura N Hayashi T Uehara Y Nomura 2004 Regulation of procaspase-2 by glucocorticoid modulatory element-binding protein 1 through the interaction with caspase recruitment domain Biochem Biophys Res Commun 325 1246 1251 10.1016/j.bbrc.2004.10.145
    • (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
  • 120
    • 20044367651 scopus 로고    scopus 로고
    • A novel caspase-2 complex containing TRAF2 and RIP1
    • 10.1074/jbc.M411180200
    • M Lamkanfi K D'Hondt L Vande Walle 2005 A novel caspase-2 complex containing TRAF2 and RIP1 J Biol Chem 280 6923 6932 10.1074/jbc.M411180200
    • (2005) J Biol Chem , vol.280 , pp. 6923-6932
    • Lamkanfi, M.1    D'Hondt, K.2    Vande Walle, L.3
  • 121
    • 0033812557 scopus 로고    scopus 로고
    • PIDD, a new death-domain-containing protein, is induced by p53 and promotes apoptosis
    • 10.1038/79102
    • Y Lin W Ma S Benchimol 2000 PIDD, a new death-domain-containing protein, is induced by p53 and promotes apoptosis Nat Genet 26 122 127 10.1038/79102
    • (2000) Nat Genet , vol.26 , pp. 122-127
    • Lin, Y.1    Ma, W.2    Benchimol, S.3
  • 122
    • 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
    • S Cuenin A Tinel S Janssens J Tschopp 2007 p53-induced protein with a death domain (PIDD) isoforms differentially activate nuclear factor-kappaB and caspase-2 in response to genotoxic stress Oncogene 27 3 387 396
    • (2007) Oncogene , vol.27 , Issue.3 , pp. 387-396
    • Cuenin, S.1    Tinel, A.2    Janssens, S.3    Tschopp, J.4
  • 123
    • 33846219997 scopus 로고    scopus 로고
    • Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway
    • 10.1038/sj.emboj.7601473
    • A Tinel S Janssens S Lippens 2007 Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway EMBO J 26 197 208 10.1038/sj.emboj.7601473
    • (2007) EMBO J , vol.26 , pp. 197-208
    • Tinel, A.1    Janssens, S.2    Lippens, S.3
  • 124
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • 10.1126/science.1095432
    • A Tinel J Tschopp 2004 The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress Science 304 843 846 10.1126/science.1095432
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 125
    • 28944447430 scopus 로고    scopus 로고
    • PIDD mediates NF-kappaB activation in response to DNA damage
    • 10.1016/j.cell.2005.09.036
    • S Janssens A Tinel S Lippens J Tschopp 2005 PIDD mediates NF-kappaB activation in response to DNA damage Cell 123 1079 1092 10.1016/j.cell.2005.09. 036
    • (2005) Cell , vol.123 , pp. 1079-1092
    • Janssens, S.1    Tinel, A.2    Lippens, S.3    Tschopp, J.4
  • 126
    • 33846702221 scopus 로고    scopus 로고
    • Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex
    • 10.1016/j.cell.2007.01.019
    • HH Park E Logette S Raunser 2007 Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex Cell 128 533 546 10.1016/j.cell.2007.01.019
    • (2007) Cell , vol.128 , pp. 533-546
    • Park, H.H.1    Logette, E.2    Raunser, S.3
  • 127
    • 33751100367 scopus 로고    scopus 로고
    • TSA-induced cell death in prostate cancer cell lines is caspase-2 dependent and involves the PIDDosome
    • AF Taghiyev NV Guseva RA Glover OW Rokhlin MB Cohen 2006 TSA-induced cell death in prostate cancer cell lines is caspase-2 dependent and involves the PIDDosome Cancer Biol Ther 5 1199 1205 (Pubitemid 44772238)
    • (2006) Cancer Biology and Therapy , vol.5 , Issue.9 , pp. 1199-1205
    • Taghiyev, A.F.1    Guseva, N.V.2    Glover, R.A.3    Rokhlin, O.W.4    Cohen, M.B.5
  • 128
    • 26444433872 scopus 로고    scopus 로고
    • Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD
    • 10.1073/pnas.0506475102
    • C Berube LM Boucher W Ma 2005 Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD Proc Natl Acad Sci USA 102 14314 14320 10.1073/pnas.0506475102
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14314-14320
    • Berube, C.1    Boucher, L.M.2    Ma, W.3
  • 129
    • 33745932874 scopus 로고    scopus 로고
    • Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis
    • 10.1182/blood-2005-07-007096
    • IN Lavrik A Golks S Baumann PH Krammer 2006 Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis Blood 108 559 565 10.1182/blood-2005-07-007096
    • (2006) Blood , vol.108 , pp. 559-565
    • Lavrik, I.N.1    Golks, A.2    Baumann, S.3    Krammer, P.H.4
  • 131
    • 15944379869 scopus 로고    scopus 로고
    • Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7
    • 10.1111/j.1742-4658.2005.04573.x
    • PK Ho AM Jabbour PG Ekert CJ Hawkins 2005 Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7 FEBS J 272 1401 1414 10.1111/j.1742-4658.2005.04573.x
    • (2005) FEBS J , vol.272 , pp. 1401-1414
    • Ho, P.K.1    Jabbour, A.M.2    Ekert, P.G.3    Hawkins, C.J.4
  • 132
    • 8844224859 scopus 로고    scopus 로고
    • The biochemical mechanism of caspase-2 activation
    • 10.1038/sj.cdd.4401492
    • BC Baliga SH Read S Kumar 2004 The biochemical mechanism of caspase-2 activation Cell Death Differ 11 1234 1241 10.1038/sj.cdd.4401492
    • (2004) Cell Death Differ , vol.11 , pp. 1234-1241
    • Baliga, B.C.1    Read, S.H.2    Kumar, S.3
  • 133
    • 0029862249 scopus 로고    scopus 로고
    • Dissecting processing and apoptotic activity of a cysteine protease by mutant analysis
    • 10.1083/jcb.135.2.479
    • B Allet A Hochmann I Martinou 1996 Dissecting processing and apoptotic activity of a cysteine protease by mutant analysis J Cell Biol 135 479 486 10.1083/jcb.135.2.479
    • (1996) J Cell Biol , vol.135 , pp. 479-486
    • Allet, B.1    Hochmann, A.2    Martinou, I.3
  • 134
    • 0142242170 scopus 로고    scopus 로고
    • Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway
    • 10.1074/jbc.M304895200
    • A Schweizer C Briand MG Grutter 2003 Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway J Biol Chem 278 42441 42447 10.1074/jbc.M304895200
    • (2003) J Biol Chem , vol.278 , pp. 42441-42447
    • Schweizer, A.1    Briand, C.2    Grutter, M.G.3
  • 136
    • 0009530192 scopus 로고    scopus 로고
    • Human ICE/CED-3 protease nomenclature
    • 10.1016/S0092-8674(00)81334-3
    • ES Alnemri DJ Livingston DW Nicholson 1996 Human ICE/CED-3 protease nomenclature Cell 87 171 10.1016/S0092-8674(00)81334-3
    • (1996) Cell , vol.87 , pp. 171
    • Alnemri, E.S.1    Livingston, D.J.2    Nicholson, D.W.3
  • 137
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • 10.1042/0264-6021:3500563
    • HR Stennicke M Renatus M Meldal GS Salvesen 2000 Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8 Biochem J 350 Pt 2 563 568 10.1042/0264-6021:3500563
    • (2000) Biochem J , vol.350 , Issue.PT 2 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 138
    • 16644392080 scopus 로고    scopus 로고
    • A substrate-phage approach for investigating caspase specificity
    • 10.1023/B:JOPC.0000039555.92058.51
    • S Lien R Pastor D Sutherlin HB Lowman 2004 A substrate-phage approach for investigating caspase specificity Protein J 23 413 425 10.1023/B:JOPC. 0000039555.92058.51
    • (2004) Protein J , vol.23 , pp. 413-425
    • Lien, S.1    Pastor, R.2    Sutherlin, D.3    Lowman, H.B.4
  • 139
    • 0034282666 scopus 로고    scopus 로고
    • The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM
    • DOI 10.1074/jbc.M000869200
    • CJ Hawkins SJ Yoo EP Petersen SL Wang SY Vernooy BA Hay 2000 The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM J Biol Chem 275 27084 27093 (Pubitemid 30688061)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.35 , pp. 27084-27093
    • Hawkins, C.J.1    Yoo, S.J.2    Peterson, E.P.3    Wang, S.L.4    Vernooy, S.Y.5    Hay, B.A.6
  • 140
    • 21444436375 scopus 로고    scopus 로고
    • Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells
    • 10.1074/jbc.M501206200
    • I Muro JC Means RJ Clem 2005 Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells J Biol Chem 280 18683 18688 10.1074/jbc.M501206200
    • (2005) J Biol Chem , vol.280 , pp. 18683-18688
    • Muro, I.1    Means, J.C.2    Clem, R.J.3
  • 141
    • 0035884195 scopus 로고    scopus 로고
    • Targeting of the transcription factor Max during apoptosis: Phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1
    • 10.1042/0264-6021:3580705
    • A Krippner-Heidenreich RV Talanian R Sekul 2001 Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1 Biochem J 358 705 715 10.1042/0264-6021:3580705
    • (2001) Biochem J , vol.358 , pp. 705-715
    • Krippner-Heidenreich, A.1    Talanian, R.V.2    Sekul, R.3
  • 142
    • 0035915457 scopus 로고    scopus 로고
    • Caspase 7 can cleave tumor necrosis factor receptor-I (p60) at a non-consensus motif, in vitro
    • 10.1016/S0167-4889(01)00159-8
    • DW Ethell E Bossy-Wetzel DE Bredesen 2001 Caspase 7 can cleave tumor necrosis factor receptor-I (p60) at a non-consensus motif, in vitro Biochim Biophys Acta 1541 231 238 10.1016/S0167-4889(01)00159-8
    • (2001) Biochim Biophys Acta , vol.1541 , pp. 231-238
    • Ethell, D.W.1    Bossy-Wetzel, E.2    Bredesen, D.E.3
  • 143
    • 0035282570 scopus 로고    scopus 로고
    • A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis
    • 10.1038/35065125
    • SM Srinivasula R Hegde A Saleh 2001 A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis Nature 410 112 116 10.1038/35065125
    • (2001) Nature , vol.410 , pp. 112-116
    • Srinivasula, S.M.1    Hegde, R.2    Saleh, A.3
  • 144
    • 33845480311 scopus 로고    scopus 로고
    • Caspase substrates
    • 10.1038/sj.cdd.4402059
    • JC Timmer GS Salvesen 2007 Caspase substrates Cell Death Differ 14 66 72 10.1038/sj.cdd.4402059
    • (2007) Cell Death Differ , vol.14 , pp. 66-72
    • Timmer, J.C.1    Salvesen, G.S.2
  • 145
    • 54249147029 scopus 로고    scopus 로고
    • Efficient cleavage of Bid and procaspase-7 by caspase-2 at lower pH
    • 10.2174/092986608786071193
    • P Karki GR Dahal SY Shin JS Lee B Cho IS Park 2008 Efficient cleavage of Bid and procaspase-7 by caspase-2 at lower pH Protein Pept Lett 15 1044 1049 10.2174/092986608786071193
    • (2008) Protein Pept Lett , vol.15 , pp. 1044-1049
    • Karki, P.1    Dahal, G.R.2    Shin, S.Y.3    Lee, J.S.4    Cho, B.5    Park, I.S.6
  • 147
    • 35648963733 scopus 로고    scopus 로고
    • Carboxyl-terminal proteolytic processing of CUX1 by a caspase enables transcriptional activation in proliferating cells
    • 10.1074/jbc.M702328200
    • M Truscott JB Denault B Goulet L Leduy GS Salvesen A Nepveu 2007 Carboxyl-terminal proteolytic processing of CUX1 by a caspase enables transcriptional activation in proliferating cells J Biol Chem 282 30216 30226 10.1074/jbc.M702328200
    • (2007) J Biol Chem , vol.282 , pp. 30216-30226
    • Truscott, M.1    Denault, J.B.2    Goulet, B.3    Leduy, L.4    Salvesen, G.S.5    Nepveu, A.6
  • 148
    • 33644657517 scopus 로고    scopus 로고
    • Bid, a BH3-only multi-functional molecule, is at the cross road of life and death
    • XM Yin 2006 Bid, a BH3-only multi-functional molecule, is at the cross road of life and death Gene 369 7 19
    • (2006) Gene , vol.369 , pp. 7-19
    • Yin, X.M.1
  • 149
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • H Li H Zhu C Xu J Yuan 1998 Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis Cell 94 491 501 10.1016/S0092-8674(00)81590-1 (Pubitemid 28391865)
    • (1998) Cell , vol.94 , Issue.4 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.-J.3    Yuan, J.4
  • 150
    • 0037134495 scopus 로고    scopus 로고
    • Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria
    • 10.1074/jbc.M108029200
    • Y Guo SM Srinivasula A Druilhe T Fernandes-Alnemri ES Alnemri 2002 Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria J Biol Chem 277 13430 13437 10.1074/jbc.M108029200
    • (2002) J Biol Chem , vol.277 , pp. 13430-13437
    • Guo, Y.1    Srinivasula, S.M.2    Druilhe, A.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5
  • 151
    • 33745739717 scopus 로고    scopus 로고
    • Caspase-2-induced apoptosis requires Bid cleavage: A physiological role for bid in heat shock-induced death
    • 10.1091/mbc.E05-12-1107
    • C Bonzon L Bouchier-Hayes LJ Pagliari DR Green DD Newmeyer 2006 Caspase-2-induced apoptosis requires Bid cleavage: a physiological role for bid in heat shock-induced death Mol Biol Cell 17 2150 2157 10.1091/mbc.E05-12-1107
    • (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
  • 152
    • 0034534795 scopus 로고    scopus 로고
    • Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis
    • 10.1126/science.290.5497.1761
    • J Zha S Weiler KJ Oh MC Wei SJ Korsmeyer 2000 Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis Science 290 1761 1765 10.1126/science.290.5497.1761
    • (2000) Science , vol.290 , pp. 1761-1765
    • Zha, J.1    Weiler, S.2    Oh, K.J.3    Wei, M.C.4    Korsmeyer, S.J.5
  • 153
    • 33644663668 scopus 로고    scopus 로고
    • Essential roles of the Bcl-2 family of proteins in caspase-2-induced apoptosis
    • 10.1074/jbc.M506488200
    • Z Gao Y Shao X Jiang 2005 Essential roles of the Bcl-2 family of proteins in caspase-2-induced apoptosis J Biol Chem 280 38271 38275 10.1074/jbc. M506488200
    • (2005) J Biol Chem , vol.280 , pp. 38271-38275
    • Gao, Z.1    Shao, Y.2    Jiang, X.3
  • 154
    • 47749133767 scopus 로고    scopus 로고
    • Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1
    • 10.1074/jbc.C800051200
    • JW Upton WJ Kaiser ES Mocarski 2008 Cytomegalovirus M45 cell death suppression requires receptor-interacting protein (RIP) homotypic interaction motif (RHIM)-dependent interaction with RIP1 J Biol Chem 283 16966 16970 10.1074/jbc.C800051200
    • (2008) J Biol Chem , vol.283 , pp. 16966-16970
    • Upton, J.W.1    Kaiser, W.J.2    Mocarski, E.S.3
  • 155
    • 9644307904 scopus 로고    scopus 로고
    • Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids
    • 10.1074/jbc.C400374200
    • M Enoksson JD Robertson V Gogvadze 2004 Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids J Biol Chem 279 49575 49578 10.1074/jbc.C400374200
    • (2004) J Biol Chem , vol.279 , pp. 49575-49578
    • Enoksson, M.1    Robertson, J.D.2    Gogvadze, V.3
  • 156
    • 4344663051 scopus 로고    scopus 로고
    • Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity
    • 10.1038/sj.embor.7400153
    • JD Robertson V Gogvadze A Kropotov H Vakifahmetoglu B Zhivotovsky S Orrenius 2004 Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity EMBO Rep 5 643 648 10.1038/sj.embor. 7400153
    • (2004) EMBO Rep , vol.5 , pp. 643-648
    • Robertson, J.D.1    Gogvadze, V.2    Kropotov, A.3    Vakifahmetoglu, H.4    Zhivotovsky, B.5    Orrenius, S.6
  • 159
    • 19644375921 scopus 로고    scopus 로고
    • Discovery, regulation, and action of the major apoptotic nucleases DFF40/CAD and endonuclease G
    • 10.1002/jcb.20409
    • P Widlak WT Garrard 2005 Discovery, regulation, and action of the major apoptotic nucleases DFF40/CAD and endonuclease G J Cell Biochem 94 1078 1087 10.1002/jcb.20409
    • (2005) J Cell Biochem , vol.94 , pp. 1078-1087
    • Widlak, P.1    Garrard, W.T.2
  • 160
    • 36049042702 scopus 로고    scopus 로고
    • Caspase-2 cleaves DNA fragmentation factor (DFF45)/inhibitor of caspase-activated DNase (ICAD)
    • 10.1016/j.abb.2007.09.007
    • GR Dahal P Karki A Thapa 2007 Caspase-2 cleaves DNA fragmentation factor (DFF45)/inhibitor of caspase-activated DNase (ICAD) Arch Biochem Biophys 468 134 139 10.1016/j.abb.2007.09.007
    • (2007) Arch Biochem Biophys , vol.468 , pp. 134-139
    • Dahal, G.R.1    Karki, P.2    Thapa, A.3
  • 162
    • 44449131447 scopus 로고    scopus 로고
    • Huntington's disease: From pathology and genetics to potential therapies
    • 10.1042/BJ20071619
    • S Imarisio J Carmichael V Korolchuk 2008 Huntington's disease: from pathology and genetics to potential therapies Biochem J 412 191 209 10.1042/BJ20071619
    • (2008) Biochem J , vol.412 , pp. 191-209
    • Imarisio, S.1    Carmichael, J.2    Korolchuk, V.3
  • 163
    • 48049092846 scopus 로고    scopus 로고
    • Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus
    • 10.1093/hmg/ddn139
    • SC Warby CN Doty RK Graham 2008 Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus Hum Mol Genet 17 2390 2404 10.1093/hmg/ddn139
    • (2008) Hum Mol Genet , vol.17 , pp. 2390-2404
    • Warby, S.C.1    Doty, C.N.2    Graham, R.K.3
  • 164
    • 33745003424 scopus 로고    scopus 로고
    • Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin
    • 10.1016/j.cell.2006.04.026
    • RK Graham Y Deng EJ Slow 2006 Cleavage at the caspase-6 site is required for neuronal dysfunction and degeneration due to mutant huntingtin Cell 125 1179 1191 10.1016/j.cell.2006.04.026
    • (2006) Cell , vol.125 , pp. 1179-1191
    • Graham, R.K.1    Deng, Y.2    Slow, E.J.3
  • 165
    • 8344221944 scopus 로고    scopus 로고
    • Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases
    • 10.1111/j.0906-6705.2004.00217.x
    • S Aho 2004 Plakin proteins are coordinately cleaved during apoptosis but preferentially through the action of different caspases Exp Dermatol 13 700 707 10.1111/j.0906-6705.2004.00217.x
    • (2004) Exp Dermatol , vol.13 , pp. 700-707
    • Aho, S.1
  • 166
    • 0029166984 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by interleukin-1-beta converting enzyme and its homologs TX and NEDD-2
    • 10.1074/jbc.270.19.11238
    • Y Gu C Sarnecki RA Aldape DJ Livingston M Su 1995 Cleavage of poly(ADP-ribose) polymerase by interleukin-1-beta converting enzyme and its homologs TX and NEDD-2 J Biol Chem 270 18715 18718 10.1074/jbc.270.19.11238
    • (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.5
  • 167
    • 0035047712 scopus 로고    scopus 로고
    • Caspase cleavage enhances the apoptosis-inducing effects of BAD
    • 10.1128/MCB.21.9.3025-3036.2001
    • F Condorelli P Salomoni S Cotteret 2001 Caspase cleavage enhances the apoptosis-inducing effects of BAD Mol Cell Biol 21 3025 3036 10.1128/MCB.21.9.3025-3036.2001
    • (2001) Mol Cell Biol , vol.21 , pp. 3025-3036
    • Condorelli, F.1    Salomoni, P.2    Cotteret, S.3
  • 168
    • 2542431137 scopus 로고    scopus 로고
    • Caspase-dependent regulation of histone deacetylase 4 nuclear-cytoplasmic shuttling promotes apoptosis
    • 10.1091/mbc.E03-08-0624
    • G Paroni M Mizzau C Henderson G Del Sal C Schneider C Brancolini 2004 Caspase-dependent regulation of histone deacetylase 4 nuclear-cytoplasmic shuttling promotes apoptosis Mol Biol Cell 15 2804 2818 10.1091/mbc.E03-08-0624
    • (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
  • 169
    • 1542374647 scopus 로고    scopus 로고
    • AlphaII-spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding
    • 10.1042/BJ20030955
    • B Rotter Y Kroviarski G Nicolas D Dhermy MC Lecomte 2004 AlphaII-spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding Biochem J 378 161 168 10.1042/BJ20030955
    • (2004) Biochem J , vol.378 , pp. 161-168
    • Rotter, B.1    Kroviarski, Y.2    Nicolas, G.3    Dhermy, D.4    Lecomte, M.C.5
  • 170
    • 0032575377 scopus 로고    scopus 로고
    • Simultaneous degradation of alphaII- and betaII-spectrin by caspase 3 (CPP32) in apoptotic cells
    • 10.1074/jbc.273.35.22490
    • KK Wang R Posmantur R Nath 1998 Simultaneous degradation of alphaII- and betaII-spectrin by caspase 3 (CPP32) in apoptotic cells J Biol Chem 273 22490 22497 10.1074/jbc.273.35.22490
    • (1998) J Biol Chem , vol.273 , pp. 22490-22497
    • Wang, K.K.1    Posmantur, R.2    Nath, R.3
  • 171
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • N Roy QL Deveraux R Takahashi GS Salvesen JC Reed 1997 The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases EMBO J 16 6914 6925 10.1093/emboj/16.23.6914 (Pubitemid 27520792)
    • (1997) EMBO Journal , vol.16 , Issue.23 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.L.2    Takahashi, R.3    Salvesen, G.S.4    Reed, J.C.5
  • 172
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • 10.1038/40901
    • Q Deveraux R Takahashi G Salvesen J Reed 1997 X-linked IAP is a direct inhibitor of cell-death proteases Nature 388 300 304 10.1038/40901
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.1    Takahashi, R.2    Salvesen, G.3    Reed, J.4
  • 173
    • 33749252583 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis proteins: Why XIAP is the black sheep of the family
    • 10.1038/sj.embor.7400795
    • BP Eckelman GS Salvesen FL Scott 2006 Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family EMBO Rep 7 988 994 10.1038/sj.embor.7400795
    • (2006) EMBO Rep , vol.7 , pp. 988-994
    • Eckelman, B.P.1    Salvesen, G.S.2    Scott, F.L.3
  • 174
    • 14844323968 scopus 로고    scopus 로고
    • XIAP inhibits caspase-3 and -7 using two binding sites: Evolutionarily conserved mechanism of IAPs
    • 10.1038/sj.emboj.7600544
    • FL Scott JB Denault SJ Riedl H Shin M Renatus GS Salvesen 2005 XIAP inhibits caspase-3 and -7 using two binding sites: evolutionarily conserved mechanism of IAPs EMBO J 24 645 655 10.1038/sj.emboj.7600544
    • (2005) EMBO J , vol.24 , pp. 645-655
    • Scott, F.L.1    Denault, J.B.2    Riedl, S.J.3    Shin, H.4    Renatus, M.5    Salvesen, G.S.6
  • 175
    • 0028817947 scopus 로고
    • Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35
    • 10.1126/science.7569933
    • NJ Bump M Hackett M Hugunin 1995 Inhibition of ICE family proteases by baculovirus antiapoptotic protein p35 Science 269 1885 1888 10.1126/science. 7569933
    • (1995) Science , vol.269 , pp. 1885-1888
    • Bump, N.J.1    Hackett, M.2    Hugunin, M.3
  • 176
    • 12244288291 scopus 로고    scopus 로고
    • The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects against apoptosis
    • 10.1038/sj.cdd.4401135
    • AM Jabbour PG Ekert EJ Coulson MJ Knight DM Ashley CJ Hawkins 2002 The p35 relative, p49, inhibits mammalian and Drosophila caspases including DRONC and protects against apoptosis Cell Death Differ 9 1311 1320 10.1038/sj.cdd.4401135
    • (2002) Cell Death Differ , vol.9 , pp. 1311-1320
    • Jabbour, A.M.1    Ekert, P.G.2    Coulson, E.J.3    Knight, M.J.4    Ashley, D.M.5    Hawkins, C.J.6
  • 177
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • 10.1016/0092-8674(93)90486-A
    • M Miura H Zhu R Rotello EA Hartweig J Yuan 1993 Induction of apoptosis in fibroblasts by IL-1β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3 Cell 75 653 660 10.1016/0092-8674(93)90486-A
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartweig, E.A.4    Yuan, J.5
  • 178
    • 0025949006 scopus 로고
    • IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha
    • AD Howard MJ Kostura N Thornberry 1991 IL-1-converting enzyme requires aspartic acid residues for processing of the IL-1 beta precursor at two distinct sites and does not cleave 31-kDa IL-1 alpha J Immunol 147 2964 2969
    • (1991) J Immunol , vol.147 , pp. 2964-2969
    • Howard, A.D.1    Kostura, M.J.2    Thornberry, N.3
  • 179
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • 10.1111/j.1742-4658.2005.04945.x
    • SF Altschul JC Wootton EM Gertz 2005 Protein database searches using compositionally adjusted substitution matrices FEBS J 272 5101 5109 10.1111/j.1742-4658.2005.04945.x
    • (2005) FEBS J , vol.272 , pp. 5101-5109
    • Altschul, S.F.1    Wootton, J.C.2    Gertz, E.M.3
  • 180
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • 10.1093/nar/25.17.3389
    • SF Altschul TL Madden AA Schaffer 1997 Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucleic Acids Res 25 3389 3402 10.1093/nar/25.17.3389
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 181
    • 0029880987 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
    • D Xue S Shaham HR Horvitz 1996 The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease Genes Dev 10 1073 1083 10.1101/gad.10.9.1073 (Pubitemid 26152849)
    • (1996) Genes and Development , vol.10 , Issue.9 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 182
    • 36749025313 scopus 로고    scopus 로고
    • Protein kinase C delta and apoptosis
    • 10.1042/BST0351001
    • ME Reyland 2007 Protein kinase C delta and apoptosis Biochem Soc Trans 35 1001 1004 10.1042/BST0351001
    • (2007) Biochem Soc Trans , vol.35 , pp. 1001-1004
    • Reyland, M.E.1
  • 183
    • 0026763128 scopus 로고
    • Identification of a set of genes with developmentally down-regulated expression in the mouse brain
    • S Kumar Y Tomooka M Noda 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


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