메뉴 건너뛰기




Volumn 29, Issue 6, 2011, Pages 468-480

Apoptosis: Why and how does it occur in biology?

Author keywords

Apoptosis; Apoptosis inducing factors (AIFs); Bcl 2 family; Caspase; Inhibitor of apoptosis proteins (IAPs); Necrosis; Programmed cell death

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ANTINEOPLASTIC AGENT; APOPTOSIS INHIBITOR; BAG 1 PROTEIN; BIM PROTEIN; CASPASE; CASPASE INHIBITOR; CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN; CERAMIDE; FAS ANTIBODY; FAS ASSOCIATED DEATH DOMAIN PROTEIN; GRANZYME; HLA DR3 ANTIGEN; HLA DR4 ANTIGEN; HLA DR5 ANTIGEN; NAVITOCLAX; NEURONAL APOPTOSIS INHIBITORY PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; OBATOCLAX; PERFORIN; PROTEIN BAD; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BID; PROTEIN KINASE B INHIBITOR; PROTEIN P53; SURVIVIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; X LINKED INHIBITOR OF APOPTOSIS; X LINKED INHIBITOR OF APOPTOSIS ANTAGONIST;

EID: 80051668693     PISSN: 02636484     EISSN: 10990844     Source Type: Journal    
DOI: 10.1002/cbf.1774     Document Type: Review
Times cited : (190)

References (207)
  • 2
    • 0018411931 scopus 로고
    • Production and life span of cutaneous mast cells in young rats
    • Kiernan JA. Production and life span of cutaneous mast cells in young rats. J Anat 1979; 128: 225-238.
    • (1979) J Anat , vol.128 , pp. 225-238
    • Kiernan, J.A.1
  • 3
    • 23844532724 scopus 로고    scopus 로고
    • Cardiac stem cells and myocardial regeneration
    • discussion 155-147, 204-111.
    • Nadal-Ginard B, Anversa P, Kajstura J, Leri A. Cardiac stem cells and myocardial regeneration. Novartis Found Symp 2005; 265: 142-154; discussion 155-147, 204-111.
    • (2005) Novartis Found Symp , vol.265 , pp. 142-154
    • Nadal-Ginard, B.1    Anversa, P.2    Kajstura, J.3    Leri, A.4
  • 5
    • 0034029953 scopus 로고    scopus 로고
    • Apoptotic and anti-apoptotic synaptic signaling mechanisms
    • Mattson MP. Apoptotic and anti-apoptotic synaptic signaling mechanisms. Brain Pathol 2000; 10: 300-312.
    • (2000) Brain Pathol , vol.10 , pp. 300-312
    • Mattson, M.P.1
  • 6
    • 77952982790 scopus 로고    scopus 로고
    • Apoptosis: a way to maintain healthy individuals
    • Mondello C, Scovassi AI. Apoptosis: a way to maintain healthy individuals. Subcell Biochem 2011; 50: 307-323.
    • (2011) Subcell Biochem , vol.50 , pp. 307-323
    • Mondello, C.1    Scovassi, A.I.2
  • 7
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science 1995; 267: 1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 8
    • 0025012042 scopus 로고
    • Cell death via apoptosis and its relationship to growth, development and differentiation of both tumour and normal cells
    • Cotter TG, Lennon SV, Glynn JG, Martin SJ. Cell death via apoptosis and its relationship to growth, development and differentiation of both tumour and normal cells. Anticancer Res 1990; 10: 1153-1159.
    • (1990) Anticancer Res , vol.10 , pp. 1153-1159
    • Cotter, T.G.1    Lennon, S.V.2    Glynn, J.G.3    Martin, S.J.4
  • 9
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26: 239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 10
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis. An overview of cell death
    • Majno G, Joris I. Apoptosis, oncosis, and necrosis. An overview of cell death. Am J Pathol 1995; 146: 3-15.
    • (1995) Am J Pathol , vol.146 , pp. 3-15
    • Majno, G.1    Joris, I.2
  • 11
    • 0033957359 scopus 로고    scopus 로고
    • Morphologic and biochemical hallmarks of apoptosis
    • Saraste A, Pulkki K. Morphologic and biochemical hallmarks of apoptosis. Cardiovasc Res 2000; 45: 528-537.
    • (2000) Cardiovasc Res , vol.45 , pp. 528-537
    • Saraste, A.1    Pulkki, K.2
  • 12
    • 0034631827 scopus 로고    scopus 로고
    • Sphingomyelin hydrolysis to ceramide during the execution phase of apoptosis results from phospholipid scrambling and alters cell-surface morphology
    • Tepper AD, Ruurs P, Wiedmer T, et al. Sphingomyelin hydrolysis to ceramide during the execution phase of apoptosis results from phospholipid scrambling and alters cell-surface morphology. J Cell Biol 2000; 150: 155-164.
    • (2000) J Cell Biol , vol.150 , pp. 155-164
    • Tepper, A.D.1    Ruurs, P.2    Wiedmer, T.3
  • 13
    • 77950365906 scopus 로고    scopus 로고
    • Nonresolving inflammation
    • Nathan C, Ding A. Nonresolving inflammation. Cell 2011; 140: 871-882.
    • (2011) Cell , vol.140 , pp. 871-882
    • Nathan, C.1    Ding, A.2
  • 14
    • 0029862212 scopus 로고    scopus 로고
    • Cellular catabolism in apoptosis: DNA degradation and endonuclease activation
    • Montague JW, Cidlowski JA. Cellular catabolism in apoptosis: DNA degradation and endonuclease activation. Experientia 1996; 52: 957-962.
    • (1996) Experientia , vol.52 , pp. 957-962
    • Montague, J.W.1    Cidlowski, J.A.2
  • 15
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • Vance JE, Steenbergen R. Metabolism and functions of phosphatidylserine. Prog Lipid Res 2005; 44: 207-234.
    • (2005) Prog Lipid Res , vol.44 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 16
    • 17644363667 scopus 로고    scopus 로고
    • Dynamics of membrane translocation of phosphatidylserine during apoptosis detected by a monoclonal antibody
    • Mourdjeva M, Kyurkchiev D, Mandinova A, et al. Dynamics of membrane translocation of phosphatidylserine during apoptosis detected by a monoclonal antibody. Apoptosis 2005; 10: 209-217.
    • (2005) Apoptosis , vol.10 , pp. 209-217
    • Mourdjeva, M.1    Kyurkchiev, D.2    Mandinova, A.3
  • 17
    • 0033107657 scopus 로고    scopus 로고
    • The apoptosome: heart and soul of the cell death machine
    • Chinnaiyan AM. The apoptosome: heart and soul of the cell death machine. Neoplasia 1999; 1: 5-15.
    • (1999) Neoplasia , vol.1 , pp. 5-15
    • Chinnaiyan, A.M.1
  • 18
    • 0344237127 scopus 로고    scopus 로고
    • Calcium orchestrates apoptosis
    • Mattson MP, Chan SL. Calcium orchestrates apoptosis. Nat Cell Biol 2003; 5: 1041-1043.
    • (2003) Nat Cell Biol , vol.5 , pp. 1041-1043
    • Mattson, M.P.1    Chan, S.L.2
  • 19
    • 0037329351 scopus 로고    scopus 로고
    • The role of various Bcl-2 domains in the anti-proliferative effect and modulation of cellular glutathione levels: a prominent role for the BH4 domain
    • Hoetelmans RW, Vahrmeijer AL, van Vlierberghe RL, et al. The role of various Bcl-2 domains in the anti-proliferative effect and modulation of cellular glutathione levels: a prominent role for the BH4 domain. Cell Prolif 2003; 36: 35-44.
    • (2003) Cell Prolif , vol.36 , pp. 35-44
    • Hoetelmans, R.W.1    Vahrmeijer, A.L.2    van Vlierberghe, R.L.3
  • 20
    • 0033662433 scopus 로고    scopus 로고
    • Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5
    • Kischkel FC, Lawrence DA, Chuntharapai A, et al. Apo2L/TRAIL-dependent recruitment of endogenous FADD and caspase-8 to death receptors 4 and 5. Immunity 2000; 12: 611-620.
    • (2000) Immunity , vol.12 , pp. 611-620
    • Kischkel, F.C.1    Lawrence, D.A.2    Chuntharapai, A.3
  • 21
    • 0026642195 scopus 로고
    • Induction of apoptosis in fibroblasts by c-myc protein
    • Evan GI, Wyllie AH, Gilbert CS, et al. Induction of apoptosis in fibroblasts by c-myc protein. Cell 1992; 69: 119-128.
    • (1992) Cell , vol.69 , pp. 119-128
    • Evan, G.I.1    Wyllie, A.H.2    Gilbert, C.S.3
  • 22
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • LaCasse EC, Baird S, Korneluk RG, MacKenzie AE. The inhibitors of apoptosis (IAPs) and their emerging role in cancer. Oncogene 1998; 17: 3247-3259.
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • LaCasse, E.C.1    Baird, S.2    Korneluk, R.G.3    MacKenzie, A.E.4
  • 24
    • 43549111150 scopus 로고    scopus 로고
    • IAPs: more than just inhibitors of apoptosis proteins
    • Dubrez-Daloz L, Dupoux A, Cartier J. IAPs: more than just inhibitors of apoptosis proteins. Cell Cycle 2008; 7: 1036-1046.
    • (2008) Cell Cycle , vol.7 , pp. 1036-1046
    • Dubrez-Daloz, L.1    Dupoux, A.2    Cartier, J.3
  • 25
    • 0032546795 scopus 로고    scopus 로고
    • Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis
    • Janicke RU, Ng P, Sprengart ML, Porter AG. Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J Biol Chem 1998; 273: 15540-15545.
    • (1998) J Biol Chem , vol.273 , pp. 15540-15545
    • Janicke, R.U.1    Ng, P.2    Sprengart, M.L.3    Porter, A.G.4
  • 26
    • 0037090614 scopus 로고    scopus 로고
    • Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation
    • Ruchaud S, Korfali N, Villa P, et al. Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J 2002; 21: 1967-1977.
    • (2002) EMBO J , vol.21 , pp. 1967-1977
    • Ruchaud, S.1    Korfali, N.2    Villa, P.3
  • 27
    • 67650103911 scopus 로고    scopus 로고
    • Mitochondrial bioenergetics as a major motive force of speciation
    • Gershoni M, Templeton AR, Mishmar D. Mitochondrial bioenergetics as a major motive force of speciation. BioEssays 2009; 31: 642-650.
    • (2009) BioEssays , vol.31 , pp. 642-650
    • Gershoni, M.1    Templeton, A.R.2    Mishmar, D.3
  • 29
    • 3242666765 scopus 로고
    • Ca(2+)-dependent mechanisms of cytotoxicity and programmed cell death
    • Spec No: 357-364.
    • Orrenius S, McCabe MJ, Jr., Nicotera P. Ca(2+)-dependent mechanisms of cytotoxicity and programmed cell death. Toxicol Lett 1992; 64-65 Spec No: 357-364.
    • (1992) Toxicol Lett , pp. 64-65
    • Orrenius, S.1    McCabe Jr., M.J.2    Nicotera, P.3
  • 30
    • 0022330157 scopus 로고
    • Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein
    • Hand D, Bungay PJ, Elliott BM, Griffin M. Activation of transglutaminase at calcium levels consistent with a role for this enzyme as a calcium receptor protein. Biosci Rep 1985; 5: 1079-1086.
    • (1985) Biosci Rep , vol.5 , pp. 1079-1086
    • Hand, D.1    Bungay, P.J.2    Elliott, B.M.3    Griffin, M.4
  • 32
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 2000; 150: 887-894.
    • (2000) J Cell Biol , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 33
    • 0020453701 scopus 로고
    • Characterization of a brain calcium-activated protease that degrades neurofilament proteins
    • Zimmerman UJ, Schlaepfer WW. Characterization of a brain calcium-activated protease that degrades neurofilament proteins. Biochemistry 1982; 21: 3977-3982.
    • (1982) Biochemistry , vol.21 , pp. 3977-3982
    • Zimmerman, U.J.1    Schlaepfer, W.W.2
  • 34
    • 0019088749 scopus 로고
    • Calcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations
    • Glenney JR, Jr., Bretscher A, Weber K. Calcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations. Proc Natl Acad Sci USA 1980; 77: 6458-6462.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6458-6462
    • Glenney Jr., J.R.1    Bretscher, A.2    Weber, K.3
  • 35
    • 0028199891 scopus 로고
    • Inhibition of p53 DNA binding by human papillomavirus E6 proteins
    • Lechner MS, Laimins LA. Inhibition of p53 DNA binding by human papillomavirus E6 proteins. J Virol 1994; 68: 4262-4273.
    • (1994) J Virol , vol.68 , pp. 4262-4273
    • Lechner, M.S.1    Laimins, L.A.2
  • 36
    • 62749155744 scopus 로고    scopus 로고
    • MDM2-dependent inhibition of p53 is required for Epstein-Barr virus B-cell growth transformation and infected-cell survival
    • Forte E, Luftig MA. MDM2-dependent inhibition of p53 is required for Epstein-Barr virus B-cell growth transformation and infected-cell survival. J Virol 2009; 83: 2491-2499.
    • (2009) J Virol , vol.83 , pp. 2491-2499
    • Forte, E.1    Luftig, M.A.2
  • 37
    • 0345167026 scopus 로고    scopus 로고
    • Sequestration of p53 in the cytoplasm by adenovirus type 12 E1B 55-kilodalton oncoprotein is required for inhibition of p53-mediated apoptosis
    • Zhao LY, Liao D. Sequestration of p53 in the cytoplasm by adenovirus type 12 E1B 55-kilodalton oncoprotein is required for inhibition of p53-mediated apoptosis. J Virol 2003; 77: 13171-13181.
    • (2003) J Virol , vol.77 , pp. 13171-13181
    • Zhao, L.Y.1    Liao, D.2
  • 38
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. Nature 1997; 387: 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 39
    • 0036247821 scopus 로고    scopus 로고
    • p53-Mdm2--the affair that never ends
    • Alarcon-Vargas D, Ronai Z. p53-Mdm2--the affair that never ends. Carcinogenesis 2002; 23: 541-547.
    • (2002) Carcinogenesis , vol.23 , pp. 541-547
    • Alarcon-Vargas, D.1    Ronai, Z.2
  • 40
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997; 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 41
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death
    • Joza N, Susin SA, Daugas E, et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 2001; 410: 549-554.
    • (2001) Nature , vol.410 , pp. 549-554
    • Joza, N.1    Susin, S.A.2    Daugas, E.3
  • 42
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91: 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 43
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 1998; 391: 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3
  • 44
    • 0035805523 scopus 로고    scopus 로고
    • Apoptosis. Death of a monopoly?
    • Hunot S, Flavell RA. Apoptosis. Death of a monopoly? Science 2001; 292: 865-866.
    • (2001) Science , vol.292 , pp. 865-866
    • Hunot, S.1    Flavell, R.A.2
  • 46
    • 0036022407 scopus 로고    scopus 로고
    • Initiator caspases in apoptosis signaling pathways
    • Chen M, Wang J. Initiator caspases in apoptosis signaling pathways. Apoptosis 2002; 7: 313-319.
    • (2002) Apoptosis , vol.7 , pp. 313-319
    • Chen, M.1    Wang, J.2
  • 47
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee EA, Adrain C, Martin SJ. Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J Biol Chem 2001; 276: 7320-7326.
    • (2001) J Biol Chem , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 48
    • 36148946797 scopus 로고    scopus 로고
    • Role of caspases in cleavage of lamin A/C and PARP during apoptosis in macrophages infected with a periodontopathic bacterium
    • Okinaga T, Kasai H, Tsujisawa T, Nishihara T. Role of caspases in cleavage of lamin A/C and PARP during apoptosis in macrophages infected with a periodontopathic bacterium. J Med Microbiol 2007; 56: 1399-1404.
    • (2007) J Med Microbiol , vol.56 , pp. 1399-1404
    • Okinaga, T.1    Kasai, H.2    Tsujisawa, T.3    Nishihara, T.4
  • 49
    • 0033551699 scopus 로고    scopus 로고
    • Role of poly(ADP-ribose) polymerase (PARP) cleavage in apoptosis. Caspase 3-resistant PARP mutant increases rates of apoptosis in transfected cells
    • Boulares AH, Yakovlev AG, Ivanova V, et al. Role of poly(ADP-ribose) polymerase (PARP) cleavage in apoptosis. Caspase 3-resistant PARP mutant increases rates of apoptosis in transfected cells. J Biol Chem 1999; 274: 22932-22940.
    • (1999) J Biol Chem , vol.274 , pp. 22932-22940
    • Boulares, A.H.1    Yakovlev, A.G.2    Ivanova, V.3
  • 50
    • 20544456147 scopus 로고    scopus 로고
    • PARP cleavage and caspase activity to assess chemosensitivity
    • Bharti AC, Takada Y, Aggarwal BB. PARP cleavage and caspase activity to assess chemosensitivity. Methods Mol Med 2005; 111: 69-78.
    • (2005) Methods Mol Med , vol.111 , pp. 69-78
    • Bharti, A.C.1    Takada, Y.2    Aggarwal, B.B.3
  • 51
    • 0032508505 scopus 로고    scopus 로고
    • Activation of caspase-1 in the nucleus requires nuclear translocation of pro-caspase-1 mediated by its prodomain
    • Mao PL, Jiang Y, Wee BY, Porter AG. Activation of caspase-1 in the nucleus requires nuclear translocation of pro-caspase-1 mediated by its prodomain. J Biol Chem 1998; 273: 23621-23624.
    • (1998) J Biol Chem , vol.273 , pp. 23621-23624
    • Mao, P.L.1    Jiang, Y.2    Wee, B.Y.3    Porter, A.G.4
  • 52
    • 0035650709 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis protein (IAP) survivin participates in regulation of chromosome segregation and mitotic exit
    • Kallio MJ, Nieminen M, Eriksson JE. Human inhibitor of apoptosis protein (IAP) survivin participates in regulation of chromosome segregation and mitotic exit. FASEB J 2001; 15: 2721-2723.
    • (2001) FASEB J , vol.15 , pp. 2721-2723
    • Kallio, M.J.1    Nieminen, M.2    Eriksson, J.E.3
  • 54
    • 0034066405 scopus 로고    scopus 로고
    • Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN
    • Teitz T, Wei T, Valentine MB, et al. Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN. Nat Med 2000; 6: 529-535.
    • (2000) Nat Med , vol.6 , pp. 529-535
    • Teitz, T.1    Wei, T.2    Valentine, M.B.3
  • 55
    • 68049143304 scopus 로고    scopus 로고
    • Apoptosis and cancer: mutations within caspase genes
    • Ghavami S, Hashemi M, Ande SR, et al. Apoptosis and cancer: mutations within caspase genes. J Med Genet 2009; 46: 497-510.
    • (2009) J Med Genet , vol.46 , pp. 497-510
    • Ghavami, S.1    Hashemi, M.2    Ande, S.R.3
  • 56
    • 0031155385 scopus 로고    scopus 로고
    • Perforin, Fas/Fas ligand, and TNF-alpha pathways as specific and bystander killing mechanisms of hepatitis C virus-specific human CTL
    • Ando K, Hiroishi K, Kaneko T, et al. Perforin, Fas/Fas ligand, and TNF-alpha pathways as specific and bystander killing mechanisms of hepatitis C virus-specific human CTL. J Immunol 1997; 158: 5283-5291.
    • (1997) J Immunol , vol.158 , pp. 5283-5291
    • Ando, K.1    Hiroishi, K.2    Kaneko, T.3
  • 57
    • 77949887174 scopus 로고    scopus 로고
    • Perforin activates clathrin- and dynamin-dependent endocytosis, which is required for plasma membrane repair and delivery of granzyme B for granzyme-mediated apoptosis
    • Thiery J, Keefe D, Saffarian S, et al. Perforin activates clathrin- and dynamin-dependent endocytosis, which is required for plasma membrane repair and delivery of granzyme B for granzyme-mediated apoptosis. Blood 2011; 115: 1582-1593.
    • (2011) Blood , vol.115 , pp. 1582-1593
    • Thiery, J.1    Keefe, D.2    Saffarian, S.3
  • 58
    • 0028889656 scopus 로고
    • Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1
    • Brinkmann U, Brinkmann E, Gallo M, Pastan I. Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1. Proc Natl Acad Sci USA 1995; 92: 10427-10431.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10427-10431
    • Brinkmann, U.1    Brinkmann, E.2    Gallo, M.3    Pastan, I.4
  • 59
    • 27644480657 scopus 로고    scopus 로고
    • Molecular cloning of cellular apoptosis susceptibility (CAS) gene in Oreochromis niloticus and its proposed role in regulation of non-specific cytotoxic cell (NCC) functions
    • Praveen K, Leary JH, 3rd, Evans DL, Jaso-Friedmann L. Molecular cloning of cellular apoptosis susceptibility (CAS) gene in Oreochromis niloticus and its proposed role in regulation of non-specific cytotoxic cell (NCC) functions. Fish Shellfish Immunol 2006; 20: 647-655.
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 647-655
    • Praveen, K.1    Leary 3rd, J.H.2    Evans, D.L.3    Jaso-Friedmann, L.4
  • 60
    • 0037249834 scopus 로고    scopus 로고
    • CSE1L/CAS: its role in proliferation and apoptosis
    • Behrens P, Brinkmann U, Wellmann A. CSE1L/CAS: its role in proliferation and apoptosis. Apoptosis 2003; 8: 39-44.
    • (2003) Apoptosis , vol.8 , pp. 39-44
    • Behrens, P.1    Brinkmann, U.2    Wellmann, A.3
  • 61
    • 0031981554 scopus 로고    scopus 로고
    • CAS, the human homologue of the yeast chromosome-segregation gene CSE1, in proliferation, apoptosis, and cancer
    • Brinkmann U. CAS, the human homologue of the yeast chromosome-segregation gene CSE1, in proliferation, apoptosis, and cancer. Am J Hum Genet 1998; 62: 509-513.
    • (1998) Am J Hum Genet , vol.62 , pp. 509-513
    • Brinkmann, U.1
  • 62
    • 0029965390 scopus 로고    scopus 로고
    • The human CAS (cellular apoptosis susceptibility) gene mapping on chromosome 20q13 is amplified in BT474 breast cancer cells and part of aberrant chromosomes in breast and colon cancer cell lines
    • Brinkmann U, Gallo M, Polymeropoulos MH, Pastan I. The human CAS (cellular apoptosis susceptibility) gene mapping on chromosome 20q13 is amplified in BT474 breast cancer cells and part of aberrant chromosomes in breast and colon cancer cell lines. Genome Res 1996; 6: 187-194.
    • (1996) Genome Res , vol.6 , pp. 187-194
    • Brinkmann, U.1    Gallo, M.2    Polymeropoulos, M.H.3    Pastan, I.4
  • 64
    • 0032942436 scopus 로고    scopus 로고
    • To die or not to die--the quest of the TRAIL receptors
    • Degli-Esposti M. To die or not to die--the quest of the TRAIL receptors. J Leukoc Biol 1999; 65: 535-542.
    • (1999) J Leukoc Biol , vol.65 , pp. 535-542
    • Degli-Esposti, M.1
  • 65
    • 0030996297 scopus 로고    scopus 로고
    • The receptor for the cytotoxic ligand TRAIL
    • Pan G, O'Rourke K, Chinnaiyan AM, et al. The receptor for the cytotoxic ligand TRAIL. Science 1997; 276: 111-113.
    • (1997) Science , vol.276 , pp. 111-113
    • Pan, G.1    O'Rourke, K.2    Chinnaiyan, A.M.3
  • 66
    • 0029935682 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/FAS) receptor/ligand system in drug-induced apoptosis in leukemia cells
    • Friesen C, Herr I, Krammer PH, Debatin KM. Involvement of the CD95 (APO-1/FAS) receptor/ligand system in drug-induced apoptosis in leukemia cells. Nat Med 1996; 2: 574-577.
    • (1996) Nat Med , vol.2 , pp. 574-577
    • Friesen, C.1    Herr, I.2    Krammer, P.H.3    Debatin, K.M.4
  • 67
    • 70449491806 scopus 로고    scopus 로고
    • Emerging role of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) as a key regulator of inflammatory responses
    • Collison A, Foster PS, Mattes J. Emerging role of tumour necrosis factor-related apoptosis-inducing ligand (TRAIL) as a key regulator of inflammatory responses. Clin Exp Pharmacol Physiol 2009; 36: 1049-1053.
    • (2009) Clin Exp Pharmacol Physiol , vol.36 , pp. 1049-1053
    • Collison, A.1    Foster, P.S.2    Mattes, J.3
  • 68
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal
    • Martin DA, Siegel RM, Zheng L, Lenardo MJ. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J Biol Chem 1998; 273: 4345-4349.
    • (1998) J Biol Chem , vol.273 , pp. 4345-4349
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.3    Lenardo, M.J.4
  • 69
    • 0033667778 scopus 로고    scopus 로고
    • FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2
    • Sprick MR, Weigand MA, Rieser E, et al. FADD/MORT1 and caspase-8 are recruited to TRAIL receptors 1 and 2 and are essential for apoptosis mediated by TRAIL receptor 2. Immunity 2000; 12: 599-609.
    • (2000) Immunity , vol.12 , pp. 599-609
    • Sprick, M.R.1    Weigand, M.A.2    Rieser, E.3
  • 70
    • 0037099678 scopus 로고    scopus 로고
    • c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis
    • Chang DW, Xing Z, Pan Y, et al. c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis. EMBO J 2002; 21: 3704-3714.
    • (2002) EMBO J , vol.21 , pp. 3704-3714
    • Chang, D.W.1    Xing, Z.2    Pan, Y.3
  • 71
    • 0032538505 scopus 로고    scopus 로고
    • Inhibition of toxic epidermal necrolysis by blockade of CD95 with human intravenous immunoglobulin
    • Viard I, Wehrli P, Bullani R, et al. Inhibition of toxic epidermal necrolysis by blockade of CD95 with human intravenous immunoglobulin. Science 1998; 282: 490-493.
    • (1998) Science , vol.282 , pp. 490-493
    • Viard, I.1    Wehrli, P.2    Bullani, R.3
  • 72
    • 0032103027 scopus 로고    scopus 로고
    • The Fas counterattack in vivo: apoptotic depletion of tumor-infiltrating lymphocytes associated with Fas ligand expression by human esophageal carcinoma
    • Bennett MW, O'Connell J, O'Sullivan GC, et al. The Fas counterattack in vivo: apoptotic depletion of tumor-infiltrating lymphocytes associated with Fas ligand expression by human esophageal carcinoma. J Immunol 1998; 160: 5669-5675.
    • (1998) J Immunol , vol.160 , pp. 5669-5675
    • Bennett, M.W.1    O'Connell, J.2    O'Sullivan, G.C.3
  • 73
    • 35548945336 scopus 로고    scopus 로고
    • Serum soluble Fas ligand (sFasL) in patients with primary squamous cell carcinoma of the esophagus
    • Kozlowski M, Kowalczuk O, Sulewska A, et al. Serum soluble Fas ligand (sFasL) in patients with primary squamous cell carcinoma of the esophagus. Folia Histochem Cytobiol 2007; 45: 199-204.
    • (2007) Folia Histochem Cytobiol , vol.45 , pp. 199-204
    • Kozlowski, M.1    Kowalczuk, O.2    Sulewska, A.3
  • 74
    • 0032982834 scopus 로고    scopus 로고
    • FasL is more frequently expressed in liver metastases of colorectal cancer than in matched primary carcinomas
    • Mann B, Gratchev A, Bohm C, et al. FasL is more frequently expressed in liver metastases of colorectal cancer than in matched primary carcinomas. Br J Cancer 1999; 79: 1262-1269.
    • (1999) Br J Cancer , vol.79 , pp. 1262-1269
    • Mann, B.1    Gratchev, A.2    Bohm, C.3
  • 75
    • 0032783244 scopus 로고    scopus 로고
    • The alteration of Fas receptor and ligand system in hepatocellular carcinomas: how do hepatoma cells escape from the host immune surveillance in vivo?
    • Nagao M, Nakajima Y, Hisanaga M, et al. The alteration of Fas receptor and ligand system in hepatocellular carcinomas: how do hepatoma cells escape from the host immune surveillance in vivo? Hepatology 1999; 30: 413-421.
    • (1999) Hepatology , vol.30 , pp. 413-421
    • Nagao, M.1    Nakajima, Y.2    Hisanaga, M.3
  • 76
    • 0034901557 scopus 로고    scopus 로고
    • Increased soluble CD95 (sFas/CD95) serum level correlates with poor prognosis in melanoma patients
    • Ugurel S, Rappl G, Tilgen W, Reinhold U. Increased soluble CD95 (sFas/CD95) serum level correlates with poor prognosis in melanoma patients. Clin Cancer Res 2001; 7: 1282-1286.
    • (2001) Clin Cancer Res , vol.7 , pp. 1282-1286
    • Ugurel, S.1    Rappl, G.2    Tilgen, W.3    Reinhold, U.4
  • 77
    • 0031740779 scopus 로고    scopus 로고
    • Fas ligand is present in tumors of the Ewing's sarcoma family and is cleaved into a soluble form by a metalloproteinase
    • Mitsiades N, Poulaki V, Kotoula V, Leone A, Tsokos M. Fas ligand is present in tumors of the Ewing's sarcoma family and is cleaved into a soluble form by a metalloproteinase. Am J Pathol 1998; 153: 1947-1956.
    • (1998) Am J Pathol , vol.153 , pp. 1947-1956
    • Mitsiades, N.1    Poulaki, V.2    Kotoula, V.3    Leone, A.4    Tsokos, M.5
  • 78
    • 0032860304 scopus 로고    scopus 로고
    • Increased serum soluble Fas ligand associated with recurrent B-cell non-Hodgkin's lymphoma after autologous peripheral blood stem cell transplantation
    • Kanda Y, Chiba S, Tanaka Y, et al. Increased serum soluble Fas ligand associated with recurrent B-cell non-Hodgkin's lymphoma after autologous peripheral blood stem cell transplantation. Leuk Lymphoma 1999; 34: 625-628.
    • (1999) Leuk Lymphoma , vol.34 , pp. 625-628
    • Kanda, Y.1    Chiba, S.2    Tanaka, Y.3
  • 79
    • 0031593748 scopus 로고    scopus 로고
    • The relationship between BcI2, Bax and p53: consequences for cell cycle progression and cell death
    • Basu A, Haldar S. The relationship between BcI2, Bax and p53: consequences for cell cycle progression and cell death. Mol Hum Reprod 1998; 4: 1099-1109.
    • (1998) Mol Hum Reprod , vol.4 , pp. 1099-1109
    • Basu, A.1    Haldar, S.2
  • 81
    • 23944445368 scopus 로고    scopus 로고
    • A role for proapoptotic BID in the DNA-damage response
    • Zinkel SS, Hurov KE, Ong C, et al. A role for proapoptotic BID in the DNA-damage response. Cell 2005; 122: 579-591.
    • (2005) Cell , vol.122 , pp. 579-591
    • Zinkel, S.S.1    Hurov, K.E.2    Ong, C.3
  • 82
    • 33645283870 scopus 로고    scopus 로고
    • BID as a double agent in cell life and death
    • Gross A. BID as a double agent in cell life and death. Cell Cycle 2006; 5: 582-584.
    • (2006) Cell Cycle , vol.5 , pp. 582-584
    • Gross, A.1
  • 83
    • 0033805442 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis
    • Kannan K, Jain SK. Oxidative stress and apoptosis. Pathophysiology 2000; 7: 153-163.
    • (2000) Pathophysiology , vol.7 , pp. 153-163
    • Kannan, K.1    Jain, S.K.2
  • 84
    • 0032933179 scopus 로고    scopus 로고
    • Effect of serum starvation on expression and phosphorylation of PKC-alpha and p53 in V79 cells: implications for cell death
    • Hasan NM, Adams GE, Joiner MC. Effect of serum starvation on expression and phosphorylation of PKC-alpha and p53 in V79 cells: implications for cell death. Int J Cancer 1999; 80: 400-405.
    • (1999) Int J Cancer , vol.80 , pp. 400-405
    • Hasan, N.M.1    Adams, G.E.2    Joiner, M.C.3
  • 85
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR, Dudek H, Tao X, et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997; 91: 231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1    Dudek, H.2    Tao, X.3
  • 86
    • 0034721646 scopus 로고    scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced apoptosis
    • Motyka B, Korbutt G, Pinkoski MJ, et al. Mannose 6-phosphate/insulin-like growth factor II receptor is a death receptor for granzyme B during cytotoxic T cell-induced apoptosis. Cell 2000; 103: 491-500.
    • (2000) Cell , vol.103 , pp. 491-500
    • Motyka, B.1    Korbutt, G.2    Pinkoski, M.J.3
  • 87
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon AJ, Nicholson DW, Bleackley RC. Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 1995; 377: 446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 88
    • 0037203342 scopus 로고    scopus 로고
    • Ceramide in apoptosis: an overview and current perspectives
    • Pettus BJ, Chalfant CE, Hannun YA. Ceramide in apoptosis: an overview and current perspectives. Biochim Biophys Acta 2002; 1585: 114-125.
    • (2002) Biochim Biophys Acta , vol.1585 , pp. 114-125
    • Pettus, B.J.1    Chalfant, C.E.2    Hannun, Y.A.3
  • 89
    • 0028287960 scopus 로고
    • Ionizing radiation acts on cellular membranes to generate ceramide and initiate apoptosis
    • Haimovitz-Friedman A, Kan CC, Ehleiter D, et al. Ionizing radiation acts on cellular membranes to generate ceramide and initiate apoptosis. J Exp Med 1994; 180: 525-535.
    • (1994) J Exp Med , vol.180 , pp. 525-535
    • Haimovitz-Friedman, A.1    Kan, C.C.2    Ehleiter, D.3
  • 90
    • 34547135165 scopus 로고    scopus 로고
    • Potential roles of membrane fluidity and ceramide in hyperthermia and alcohol stimulation of TRAIL apoptosis
    • Moulin M, Carpentier S, Levade T, Arrigo AP. Potential roles of membrane fluidity and ceramide in hyperthermia and alcohol stimulation of TRAIL apoptosis. Apoptosis 2007; 12: 1703-1720.
    • (2007) Apoptosis , vol.12 , pp. 1703-1720
    • Moulin, M.1    Carpentier, S.2    Levade, T.3    Arrigo, A.P.4
  • 91
    • 1842375100 scopus 로고    scopus 로고
    • Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis
    • Quillet-Mary A, Jaffrezou JP, Mansat V, et al. Implication of mitochondrial hydrogen peroxide generation in ceramide-induced apoptosis. J Biol Chem 1997; 272: 21388-21395.
    • (1997) J Biol Chem , vol.272 , pp. 21388-21395
    • Quillet-Mary, A.1    Jaffrezou, J.P.2    Mansat, V.3
  • 92
    • 0034488193 scopus 로고    scopus 로고
    • Pivotal role for acidic sphingomyelinase in cerebral ischemia-induced ceramide and cytokine production, and neuronal apoptosis
    • Yu ZF, Nikolova-Karakashian M, Zhou D, et al. Pivotal role for acidic sphingomyelinase in cerebral ischemia-induced ceramide and cytokine production, and neuronal apoptosis. J Mol Neurosci 2000; 15: 85-97.
    • (2000) J Mol Neurosci , vol.15 , pp. 85-97
    • Yu, Z.F.1    Nikolova-Karakashian, M.2    Zhou, D.3
  • 93
    • 0036310233 scopus 로고    scopus 로고
    • Ultraviolet B radiation induces activation of neutral and acidic sphingomyelinases and ceramide generation in cultured normal human keratinocytes
    • Magnoni C, Euclidi E, Benassi L, et al. Ultraviolet B radiation induces activation of neutral and acidic sphingomyelinases and ceramide generation in cultured normal human keratinocytes. Toxicol In Vitro 2002; 16: 349-355.
    • (2002) Toxicol In Vitro , vol.16 , pp. 349-355
    • Magnoni, C.1    Euclidi, E.2    Benassi, L.3
  • 94
    • 0034902215 scopus 로고    scopus 로고
    • Choline deficiency induces apoptosis in primary cultures of fetal neurons
    • Yen CL, Mar MH, Meeker RB, Fernandes A, Zeisel SH. Choline deficiency induces apoptosis in primary cultures of fetal neurons. FASEB J 2001; 15: 1704-1710.
    • (2001) FASEB J , vol.15 , pp. 1704-1710
    • Yen, C.L.1    Mar, M.H.2    Meeker, R.B.3    Fernandes, A.4    Zeisel, S.H.5
  • 95
    • 0033178928 scopus 로고    scopus 로고
    • Doxorubicin induces slow ceramide accumulation and late apoptosis in cultured adult rat ventricular myocytes
    • Delpy E, Hatem SN, Andrieu N, et al. Doxorubicin induces slow ceramide accumulation and late apoptosis in cultured adult rat ventricular myocytes. Cardiovasc Res 1999; 43: 398-407.
    • (1999) Cardiovasc Res , vol.43 , pp. 398-407
    • Delpy, E.1    Hatem, S.N.2    Andrieu, N.3
  • 96
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis*
    • Wang C, Youle RJ. The role of mitochondria in apoptosis*. Annu Rev Genet 2009; 43: 95-118.
    • (2009) Annu Rev Genet , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 97
    • 39049149816 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • Jeong SY, Seol DW. The role of mitochondria in apoptosis. BMB Rep 2008; 41: 11-22.
    • (2008) BMB Rep , vol.41 , pp. 11-22
    • Jeong, S.Y.1    Seol, D.W.2
  • 98
    • 0032418092 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?
    • Tsujimoto Y. Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria? Genes Cells 1998; 3: 697-707.
    • (1998) Genes Cells , vol.3 , pp. 697-707
    • Tsujimoto, Y.1
  • 99
    • 33745966804 scopus 로고    scopus 로고
    • BH3-only proteins: orchestrating cell death
    • Fletcher JI, Huang DC. BH3-only proteins: orchestrating cell death. Cell Death Differ 2006; 13: 1268-1271.
    • (2006) Cell Death Differ , vol.13 , pp. 1268-1271
    • Fletcher, J.I.1    Huang, D.C.2
  • 100
    • 0242522206 scopus 로고    scopus 로고
    • Regulation of apoptosis by Bcl-2 family proteins
    • Burlacu A. Regulation of apoptosis by Bcl-2 family proteins. J Cell Mol Med 2003; 7: 249-257.
    • (2003) J Cell Mol Med , vol.7 , pp. 249-257
    • Burlacu, A.1
  • 101
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: the role of the BH3 domain in apoptosis
    • Kelekar A, Thompson CB. Bcl-2-family proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol 1998; 8: 324-330.
    • (1998) Trends Cell Biol , vol.8 , pp. 324-330
    • Kelekar, A.1    Thompson, C.B.2
  • 102
    • 0030614915 scopus 로고    scopus 로고
    • Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis
    • Sattler M, Liang H, Nettesheim D, et al. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 1997; 275: 983-986.
    • (1997) Science , vol.275 , pp. 983-986
    • Sattler, M.1    Liang, H.2    Nettesheim, D.3
  • 103
    • 0346753589 scopus 로고    scopus 로고
    • BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo
    • Sugioka R, Shimizu S, Funatsu T, et al. BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo. Oncogene 2003; 22: 8432-8440.
    • (2003) Oncogene , vol.22 , pp. 8432-8440
    • Sugioka, R.1    Shimizu, S.2    Funatsu, T.3
  • 104
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, et al. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2002; 2: 183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3
  • 105
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana T, Bouchier-Hayes L, Chipuk JE, et al. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol Cell 2005; 17: 525-535.
    • (2005) Mol Cell , vol.17 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3
  • 106
    • 68549089038 scopus 로고    scopus 로고
    • The role of BH3-only protein Bim extends beyond inhibiting Bcl-2-like prosurvival proteins
    • Merino D, Giam M, Hughes PD, et al. The role of BH3-only protein Bim extends beyond inhibiting Bcl-2-like prosurvival proteins. J Cell Biol 2009; 186: 355-362.
    • (2009) J Cell Biol , vol.186 , pp. 355-362
    • Merino, D.1    Giam, M.2    Hughes, P.D.3
  • 108
    • 77957141008 scopus 로고    scopus 로고
    • Still embedded together binding to membranes regulates Bcl-2 protein interactions
    • Leber B, Lin J, Andrews DW. Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene 2011; 29: 5221-5230.
    • (2011) Oncogene , vol.29 , pp. 5221-5230
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 111
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A, Smith CL, Hsu YT, Youle RJ. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J 1999; 18: 2330-2341.
    • (1999) EMBO J , vol.18 , pp. 2330-2341
    • Nechushtan, A.1    Smith, C.L.2    Hsu, Y.T.3    Youle, R.J.4
  • 112
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 1999; 399: 483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 113
    • 0034697365 scopus 로고    scopus 로고
    • Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c
    • Shimizu S, Ide T, Yanagida T, Tsujimoto Y. Electrophysiological study of a novel large pore formed by Bax and the voltage-dependent anion channel that is permeable to cytochrome c. J Biol Chem 2000; 275: 12321-12325.
    • (2000) J Biol Chem , vol.275 , pp. 12321-12325
    • Shimizu, S.1    Ide, T.2    Yanagida, T.3    Tsujimoto, Y.4
  • 114
    • 2442429306 scopus 로고    scopus 로고
    • JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins
    • Tsuruta F, Sunayama J, Mori Y, et al. JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. EMBO J 2004; 23: 1889-1899.
    • (2004) EMBO J , vol.23 , pp. 1889-1899
    • Tsuruta, F.1    Sunayama, J.2    Mori, Y.3
  • 115
    • 1642633791 scopus 로고    scopus 로고
    • ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway
    • Ohtsuka T, Ryu H, Minamishima YA, et al. ASC is a Bax adaptor and regulates the p53-Bax mitochondrial apoptosis pathway. Nat Cell Biol 2004; 6: 121-128.
    • (2004) Nat Cell Biol , vol.6 , pp. 121-128
    • Ohtsuka, T.1    Ryu, H.2    Minamishima, Y.A.3
  • 116
    • 79958698544 scopus 로고    scopus 로고
    • Synergistic induction of cell death in liver tumor cells by TRAIL and chemotherapeutic drugs via the BH3-only proteins Bim and Bid
    • DOI:10.1038/cddis.2010.1066.
    • Schneider-Jakob S, Corazza N, Badmann A, et al. Synergistic induction of cell death in liver tumor cells by TRAIL and chemotherapeutic drugs via the BH3-only proteins Bim and Bid. Cell Death Disease 2010; 1: e86. DOI:10.1038/cddis.2010.1066.
    • (2010) Cell Death Disease , vol.1
    • Schneider-Jakob, S.1    Corazza, N.2    Badmann, A.3
  • 117
    • 78650361485 scopus 로고    scopus 로고
    • Bid Stands at the Crossroad of Stress-response Pathways
    • Song G, Chen GG, Hu T, Lai PB. Bid Stands at the Crossroad of Stress-response Pathways. Curr Cancer Drug Targets 2010; 10: 584-592.
    • (2010) Curr Cancer Drug Targets , vol.10 , pp. 584-592
    • Song, G.1    Chen, G.G.2    Hu, T.3    Lai, P.B.4
  • 118
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998; 94: 491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 119
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: paper wraps stone blunts scissors
    • Green DR. Apoptotic pathways: paper wraps stone blunts scissors. Cell 2000; 102: 1-4.
    • (2000) Cell , vol.102 , pp. 1-4
    • Green, D.R.1
  • 120
    • 11144294667 scopus 로고    scopus 로고
    • Mechanism of hepatocytes apoptosis induced by the proapoptosis protein Bid
    • Bai L, Cao CP, Mao GP. Mechanism of hepatocytes apoptosis induced by the proapoptosis protein Bid. Chin J Dig Dis 2004; 5: 175-180.
    • (2004) Chin J Dig Dis , vol.5 , pp. 175-180
    • Bai, L.1    Cao, C.P.2    Mao, G.P.3
  • 121
    • 0034663829 scopus 로고    scopus 로고
    • tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei MC, Lindsten T, Mootha VK, et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev 2000; 14: 2060-2071.
    • (2000) Genes Dev , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 122
    • 23944498161 scopus 로고    scopus 로고
    • Proapoptotic BID is an ATM effector in the DNA-damage response
    • Kamer I, Sarig R, Zaltsman Y, et al. Proapoptotic BID is an ATM effector in the DNA-damage response. Cell 2005; 122: 593-603.
    • (2005) Cell , vol.122 , pp. 593-603
    • Kamer, I.1    Sarig, R.2    Zaltsman, Y.3
  • 123
    • 0041338049 scopus 로고    scopus 로고
    • Inhibition of the phosphatidylinositol 3'-kinase-AKT pathway induces apoptosis in pancreatic carcinoma cells in vitro and in vivo
    • Bondar VM, Sweeney-Gotsch B, Andreeff M, Mills GB, McConkey DJ. Inhibition of the phosphatidylinositol 3'-kinase-AKT pathway induces apoptosis in pancreatic carcinoma cells in vitro and in vivo. Mol Cancer Ther 2002; 1: 989-997.
    • (2002) Mol Cancer Ther , vol.1 , pp. 989-997
    • Bondar, V.M.1    Sweeney-Gotsch, B.2    Andreeff, M.3    Mills, G.B.4    McConkey, D.J.5
  • 124
    • 24944441858 scopus 로고    scopus 로고
    • PKB/AKT and ERK regulation of caspase-mediated apoptosis by methylseleninic acid in LNCaP prostate cancer cells
    • Hu H, Jiang C, Li G, Lu J. PKB/AKT and ERK regulation of caspase-mediated apoptosis by methylseleninic acid in LNCaP prostate cancer cells. Carcinogenesis 2005; 26: 1374-1381.
    • (2005) Carcinogenesis , vol.26 , pp. 1374-1381
    • Hu, H.1    Jiang, C.2    Li, G.3    Lu, J.4
  • 125
    • 1242285048 scopus 로고    scopus 로고
    • Inhibition of phosphatidylinositol 3-kinase dephosphorylates BAD and promotes apoptosis in myeloid leukemias
    • Zhao S, Konopleva M, Cabreira-Hansen M, et al. Inhibition of phosphatidylinositol 3-kinase dephosphorylates BAD and promotes apoptosis in myeloid leukemias. Leukemia 2004; 18: 267-275.
    • (2004) Leukemia , vol.18 , pp. 267-275
    • Zhao, S.1    Konopleva, M.2    Cabreira-Hansen, M.3
  • 126
    • 0141996464 scopus 로고    scopus 로고
    • Microtubules, microtubule-interfering agents and apoptosis
    • Mollinedo F, Gajate C. Microtubules, microtubule-interfering agents and apoptosis. Apoptosis 2003; 8: 413-450.
    • (2003) Apoptosis , vol.8 , pp. 413-450
    • Mollinedo, F.1    Gajate, C.2
  • 127
    • 70449091753 scopus 로고    scopus 로고
    • Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis
    • Kim H, Tu HC, Ren D, et al. Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis. Mol Cell 2009; 36: 487-499.
    • (2009) Mol Cell , vol.36 , pp. 487-499
    • Kim, H.1    Tu, H.C.2    Ren, D.3
  • 128
    • 54249096028 scopus 로고    scopus 로고
    • Caspases in apoptosis and beyond
    • Li J, Yuan J. Caspases in apoptosis and beyond. Oncogene 2008; 27: 6194-6206.
    • (2008) Oncogene , vol.27 , pp. 6194-6206
    • Li, J.1    Yuan, J.2
  • 131
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • Rodriguez J, Lazebnik Y. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 1999; 13: 3179-3184.
    • (1999) Genes Dev , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 132
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • Kuida K, Haydar TF, Kuan CY, et al. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 1998; 94: 325-337.
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1    Haydar, T.F.2    Kuan, C.Y.3
  • 133
    • 0036479012 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria
    • Cande C, Cohen I, Daugas E, et al. Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria. Biochimie 2002; 84: 215-222.
    • (2002) Biochimie , vol.84 , pp. 215-222
    • Cande, C.1    Cohen, I.2    Daugas, E.3
  • 134
    • 0033026172 scopus 로고    scopus 로고
    • Targeted disruption of caspase genes in mice: what they tell us about the functions of individual caspases in apoptosis
    • Colussi PA, Kumar S. Targeted disruption of caspase genes in mice: what they tell us about the functions of individual caspases in apoptosis. Immunol Cell Biol 1999; 77: 58-63.
    • (1999) Immunol Cell Biol , vol.77 , pp. 58-63
    • Colussi, P.A.1    Kumar, S.2
  • 135
    • 80051666118 scopus 로고    scopus 로고
    • The execution complex of apoptosis
    • Mak T. The execution complex of apoptosis. Biochemica 2000; 1: 39-41.
    • (2000) Biochemica , vol.1 , pp. 39-41
    • Mak, T.1
  • 136
    • 0031659755 scopus 로고    scopus 로고
    • The role of caspases in T cell development and the control of immune responses
    • Denis F, Rheaume E, Aouad SM, et al. The role of caspases in T cell development and the control of immune responses. Cell Mol Life Sci 1998; 54: 1005-1019.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 1005-1019
    • Denis, F.1    Rheaume, E.2    Aouad, S.M.3
  • 137
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: structure, activation, substrates, and functions during apoptosis
    • Earnshaw WC, Martins LM, Kaufmann SH. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 1999; 68: 383-424.
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 138
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998; 281: 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 139
    • 0036403886 scopus 로고    scopus 로고
    • Expression of inhibitor of apoptosis proteins in small- and non-small-cell lung carcinoma cells
    • Ekedahl J, Joseph B, Grigoriev MY, et al. Expression of inhibitor of apoptosis proteins in small- and non-small-cell lung carcinoma cells. Exp Cell Res 2002; 279: 277-290.
    • (2002) Exp Cell Res , vol.279 , pp. 277-290
    • Ekedahl, J.1    Joseph, B.2    Grigoriev, M.Y.3
  • 140
    • 67650727602 scopus 로고    scopus 로고
    • Effects of cIAP-1, cIAP-2 and XIAP triple knockdown on prostate cancer cell susceptibility to apoptosis, cell survival and proliferation
    • Gill C, Dowling C, O'Neill AJ, Watson RW. Effects of cIAP-1, cIAP-2 and XIAP triple knockdown on prostate cancer cell susceptibility to apoptosis, cell survival and proliferation. Mol Cancer 2009; 8: 39.
    • (2009) Mol Cancer , vol.8 , pp. 39
    • Gill, C.1    Dowling, C.2    O'Neill, A.J.3    Watson, R.W.4
  • 141
    • 0032478717 scopus 로고    scopus 로고
    • A single BIR domain of XIAP sufficient for inhibiting caspases
    • Takahashi R, Deveraux Q, Tamm I, et al. A single BIR domain of XIAP sufficient for inhibiting caspases. J Biol Chem 1998; 273: 7787-7790.
    • (1998) J Biol Chem , vol.273 , pp. 7787-7790
    • Takahashi, R.1    Deveraux, Q.2    Tamm, I.3
  • 142
    • 69749094996 scopus 로고    scopus 로고
    • Survivin as a global target of intrinsic tumor suppression networks
    • Guha M, Altieri DC. Survivin as a global target of intrinsic tumor suppression networks. Cell Cycle 2009; 8: 2708-2710.
    • (2009) Cell Cycle , vol.8 , pp. 2708-2710
    • Guha, M.1    Altieri, D.C.2
  • 143
    • 0032506524 scopus 로고    scopus 로고
    • Control of apoptosis and mitotic spindle checkpoint by survivin
    • Li F, Ambrosini G, Chu EY, et al. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature 1998; 396: 580-584.
    • (1998) Nature , vol.396 , pp. 580-584
    • Li, F.1    Ambrosini, G.2    Chu, E.Y.3
  • 144
    • 10744232728 scopus 로고    scopus 로고
    • Elevated expression of inhibitor of apoptosis proteins in prostate cancer
    • Krajewska M, Krajewski S, Banares S, et al. Elevated expression of inhibitor of apoptosis proteins in prostate cancer. Clin Cancer Res 2003; 9: 4914-4925.
    • (2003) Clin Cancer Res , vol.9 , pp. 4914-4925
    • Krajewska, M.1    Krajewski, S.2    Banares, S.3
  • 145
    • 0037444287 scopus 로고    scopus 로고
    • Functional blocks in caspase activation pathways are common in leukemia and predict patient response to induction chemotherapy
    • Schimmer AD, Pedersen IM, Kitada S, et al. Functional blocks in caspase activation pathways are common in leukemia and predict patient response to induction chemotherapy. Cancer Res 2003; 63: 1242-1248.
    • (2003) Cancer Res , vol.63 , pp. 1242-1248
    • Schimmer, A.D.1    Pedersen, I.M.2    Kitada, S.3
  • 146
    • 17144438370 scopus 로고    scopus 로고
    • Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias
    • Tamm I, Kornblau SM, Segall H, et al. Expression and prognostic significance of IAP-family genes in human cancers and myeloid leukemias. Clin Cancer Res 2000; 6: 1796-1803.
    • (2000) Clin Cancer Res , vol.6 , pp. 1796-1803
    • Tamm, I.1    Kornblau, S.M.2    Segall, H.3
  • 147
    • 70350741406 scopus 로고    scopus 로고
    • Overexpression of X-linked inhibitor of apoptosis protein (XIAP) is an independent unfavorable prognostic factor in childhood de novo acute myeloid leukemia
    • Sung KW, Choi J, Hwang YK, et al. Overexpression of X-linked inhibitor of apoptosis protein (XIAP) is an independent unfavorable prognostic factor in childhood de novo acute myeloid leukemia. J Korean Med Sci 2009; 24: 605-613.
    • (2009) J Korean Med Sci , vol.24 , pp. 605-613
    • Sung, K.W.1    Choi, J.2    Hwang, Y.K.3
  • 148
    • 0036464611 scopus 로고    scopus 로고
    • The mechanism of tumor cell clearance by rituximab in vivo in patients with B-cell chronic lymphocytic leukemia: evidence of caspase activation and apoptosis induction
    • Byrd JC, Kitada S, Flinn IW, et al. The mechanism of tumor cell clearance by rituximab in vivo in patients with B-cell chronic lymphocytic leukemia: evidence of caspase activation and apoptosis induction. Blood 2002; 99: 1038-1043.
    • (2002) Blood , vol.99 , pp. 1038-1043
    • Byrd, J.C.1    Kitada, S.2    Flinn, I.W.3
  • 149
    • 0034954219 scopus 로고    scopus 로고
    • Assessment of IAP (inhibitor of apoptosis) proteins as predictors of response to chemotherapy in advanced non-small-cell lung cancer patients
    • Ferreira CG, van der Valk P, Span SW, et al. Assessment of IAP (inhibitor of apoptosis) proteins as predictors of response to chemotherapy in advanced non-small-cell lung cancer patients. Ann Oncol 2001; 12: 799-805.
    • (2001) Ann Oncol , vol.12 , pp. 799-805
    • Ferreira, C.G.1    van der Valk, P.2    Span, S.W.3
  • 150
    • 0036032266 scopus 로고    scopus 로고
    • Expression of inhibitors of apoptosis (IAP) proteins in non-small cell human lung cancer
    • Hofmann HS, Simm A, Hammer A, Silber RE, Bartling B. Expression of inhibitors of apoptosis (IAP) proteins in non-small cell human lung cancer. J Cancer Res Clin Oncol 2002; 128: 554-560.
    • (2002) J Cancer Res Clin Oncol , vol.128 , pp. 554-560
    • Hofmann, H.S.1    Simm, A.2    Hammer, A.3    Silber, R.E.4    Bartling, B.5
  • 151
    • 9144234685 scopus 로고    scopus 로고
    • Small-molecule antagonists of apoptosis suppressor XIAP exhibit broad antitumor activity
    • Schimmer AD, Welsh K, Pinilla C, et al. Small-molecule antagonists of apoptosis suppressor XIAP exhibit broad antitumor activity. Cancer Cell 2004; 5: 25-35.
    • (2004) Cancer Cell , vol.5 , pp. 25-35
    • Schimmer, A.D.1    Welsh, K.2    Pinilla, C.3
  • 152
    • 33745283242 scopus 로고    scopus 로고
    • Targeting the IAP family of caspase inhibitors as an emerging therapeutic strategy
    • Schimmer AD, Dalili S. Targeting the IAP family of caspase inhibitors as an emerging therapeutic strategy. Hematology Am Soc Hematol Educ Program 2005: 215-219.
    • (2005) Hematology Am Soc Hematol Educ Program , pp. 215-219
    • Schimmer, A.D.1    Dalili, S.2
  • 153
    • 0037478904 scopus 로고    scopus 로고
    • Antisense oligonucleotides targeting XIAP induce apoptosis and enhance chemotherapeutic activity against human lung cancer cells in vitro and in vivo
    • Hu Y, Cherton-Horvat G, Dragowska V, et al. Antisense oligonucleotides targeting XIAP induce apoptosis and enhance chemotherapeutic activity against human lung cancer cells in vitro and in vivo. Clin Cancer Res 2003; 9: 2826-2836.
    • (2003) Clin Cancer Res , vol.9 , pp. 2826-2836
    • Hu, Y.1    Cherton-Horvat, G.2    Dragowska, V.3
  • 154
    • 0035920126 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes
    • Suzuki Y, Nakabayashi Y, Nakata K, Reed JC, Takahashi R. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes. J Biol Chem 2001; 276: 27058-27063.
    • (2001) J Biol Chem , vol.276 , pp. 27058-27063
    • Suzuki, Y.1    Nakabayashi, Y.2    Nakata, K.3    Reed, J.C.4    Takahashi, R.5
  • 155
    • 0037291737 scopus 로고    scopus 로고
    • Mechanism of XIAP-mediated inhibition of caspase-9
    • Shiozaki EN, Chai J, Rigotti DJ, et al. Mechanism of XIAP-mediated inhibition of caspase-9. Mol Cell 2003; 11: 519-527.
    • (2003) Mol Cell , vol.11 , pp. 519-527
    • Shiozaki, E.N.1    Chai, J.2    Rigotti, D.J.3
  • 156
    • 33645640920 scopus 로고    scopus 로고
    • The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases
    • Eckelman BP, Salvesen GS. The human anti-apoptotic proteins cIAP1 and cIAP2 bind but do not inhibit caspases. J Biol Chem 2006; 281: 3254-3260.
    • (2006) J Biol Chem , vol.281 , pp. 3254-3260
    • Eckelman, B.P.1    Salvesen, G.S.2
  • 157
    • 61449134122 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of apoptosis
    • Broemer M, Meier P. Ubiquitin-mediated regulation of apoptosis. Trends Cell Biol 2009; 19: 130-140.
    • (2009) Trends Cell Biol , vol.19 , pp. 130-140
    • Broemer, M.1    Meier, P.2
  • 158
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Suzuki Y, Nakabayashi Y, Takahashi R. Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death. Proc Natl Acad Sci USA 2001; 98: 8662-8667.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 159
    • 44949240664 scopus 로고    scopus 로고
    • cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination
    • Bertrand MJ, Milutinovic S, Dickson KM, et al. cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. Mol Cell 2008; 30: 689-700.
    • (2008) Mol Cell , vol.30 , pp. 689-700
    • Bertrand, M.J.1    Milutinovic, S.2    Dickson, K.M.3
  • 160
    • 50049110244 scopus 로고    scopus 로고
    • Regulation of apoptosis by XIAP ubiquitin-ligase activity
    • Schile AJ, Garcia-Fernandez M, Steller H. Regulation of apoptosis by XIAP ubiquitin-ligase activity. Genes Dev 2008; 22: 2256-2266.
    • (2008) Genes Dev , vol.22 , pp. 2256-2266
    • Schile, A.J.1    Garcia-Fernandez, M.2    Steller, H.3
  • 161
    • 77449136104 scopus 로고    scopus 로고
    • XIAP as a ubiquitin ligase in cellular signaling
    • Galban S, Duckett CS. XIAP as a ubiquitin ligase in cellular signaling. Cell Death Differ 2011; 17: 54-60.
    • (2011) Cell Death Differ , vol.17 , pp. 54-60
    • Galban, S.1    Duckett, C.S.2
  • 162
    • 77952298503 scopus 로고    scopus 로고
    • Mitochondrial regulation of cell death: processing of apoptosis-inducing factor (AIF)
    • Norberg E, Orrenius S, Zhivotovsky B. Mitochondrial regulation of cell death: processing of apoptosis-inducing factor (AIF). Biochem Biophys Res Commun 2011; 396: 95-100.
    • (2011) Biochem Biophys Res Commun , vol.396 , pp. 95-100
    • Norberg, E.1    Orrenius, S.2    Zhivotovsky, B.3
  • 163
    • 0038335334 scopus 로고    scopus 로고
    • PI3K/PTEN/AKT pathway. A critical mediator of oncogenic signaling
    • Paez J, Sellers WR. PI3K/PTEN/AKT pathway. A critical mediator of oncogenic signaling. Cancer Treat Res 2003; 115: 145-167.
    • (2003) Cancer Treat Res , vol.115 , pp. 145-167
    • Paez, J.1    Sellers, W.R.2
  • 164
    • 32544448056 scopus 로고    scopus 로고
    • Role of mitochondria as the gardens of cell death
    • Kim R, Emi M, Tanabe K. Role of mitochondria as the gardens of cell death. Cancer Chemother Pharmacol 2006; 57: 545-553.
    • (2006) Cancer Chemother Pharmacol , vol.57 , pp. 545-553
    • Kim, R.1    Emi, M.2    Tanabe, K.3
  • 165
    • 24744459035 scopus 로고    scopus 로고
    • Ch'en IL, Kolla RV, Hoffmann A, Hedrick SM. Cutting edge: innate immunity conferred by B cells is regulated by caspase-8
    • Beisner DR, Ch'en IL, Kolla RV, Hoffmann A, Hedrick SM. Cutting edge: innate immunity conferred by B cells is regulated by caspase-8. J Immunol 2005; 175: 3469-3473.
    • (2005) J Immunol , vol.175 , pp. 3469-3473
    • Beisner, D.R.1
  • 166
    • 23844464209 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis in human vascular endothelium is regulated by phosphatidylinositol 3-kinase/Akt through the short form of cellular FLIP and Bcl-2
    • Alladina SJ, Song JH, Davidge ST, Hao C, Easton AS. TRAIL-induced apoptosis in human vascular endothelium is regulated by phosphatidylinositol 3-kinase/Akt through the short form of cellular FLIP and Bcl-2. J Vasc Res 2005; 42: 337-347.
    • (2005) J Vasc Res , vol.42 , pp. 337-347
    • Alladina, S.J.1    Song, J.H.2    Davidge, S.T.3    Hao, C.4    Easton, A.S.5
  • 167
    • 0031034574 scopus 로고    scopus 로고
    • Antiapoptotic signalling by the insulin-like growth factor I receptor, phosphatidylinositol 3-kinase, and Akt
    • Kulik G, Klippel A, Weber MJ. Antiapoptotic signalling by the insulin-like growth factor I receptor, phosphatidylinositol 3-kinase, and Akt. Mol Cell Biol 1997; 17: 1595-1606.
    • (1997) Mol Cell Biol , vol.17 , pp. 1595-1606
    • Kulik, G.1    Klippel, A.2    Weber, M.J.3
  • 168
    • 78751513089 scopus 로고    scopus 로고
    • PI-103 and sorafenib inhibit hepatocellular carcinoma cell proliferation by blocking Ras/Raf/MAPK and PI3K/AKT/mTOR pathways
    • Gedaly R, Angulo P, Hundley J, et al. PI-103 and sorafenib inhibit hepatocellular carcinoma cell proliferation by blocking Ras/Raf/MAPK and PI3K/AKT/mTOR pathways. Anticancer Res 2010; 30: 4951-4958.
    • (2010) Anticancer Res , vol.30 , pp. 4951-4958
    • Gedaly, R.1    Angulo, P.2    Hundley, J.3
  • 169
    • 77952828838 scopus 로고    scopus 로고
    • Targeting fibroblast growth factor receptors blocks PI3K/AKT signaling, induces apoptosis, and impairs mammary tumor outgrowth and metastasis
    • Dey JH, Bianchi F, Voshol J, et al. Targeting fibroblast growth factor receptors blocks PI3K/AKT signaling, induces apoptosis, and impairs mammary tumor outgrowth and metastasis. Cancer Res 2010; 70: 4151-4162.
    • (2010) Cancer Res , vol.70 , pp. 4151-4162
    • Dey, J.H.1    Bianchi, F.2    Voshol, J.3
  • 170
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell JE, Jr. STATs and gene regulation. Science 1997; 277: 1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell Jr., J.E.1
  • 171
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang L, Du F, Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 2008; 133: 693-703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 172
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl SJ, Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat Rev Mol Cell Biol 2004; 5: 897-907.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 173
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control
    • Chu ZL, McKinsey TA, Liu L, et al. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kappaB control. Proc Natl Acad Sci USA 1997; 94: 10057-10062.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3
  • 175
    • 0041568189 scopus 로고    scopus 로고
    • The role of apoptosis in human epidermal keratinocytes
    • Weisfelner ME, Gottlieb AB. The role of apoptosis in human epidermal keratinocytes. J Drugs Dermatol 2003; 2: 385-391.
    • (2003) J Drugs Dermatol , vol.2 , pp. 385-391
    • Weisfelner, M.E.1    Gottlieb, A.B.2
  • 176
    • 0033007321 scopus 로고    scopus 로고
    • Mature T lymphocyte apoptosis--immune regulation in a dynamic and unpredictable antigenic environment
    • Lenardo M, Chan KM, Hornung F, et al. Mature T lymphocyte apoptosis--immune regulation in a dynamic and unpredictable antigenic environment. Annu Rev Immunol 1999; 17: 221-253.
    • (1999) Annu Rev Immunol , vol.17 , pp. 221-253
    • Lenardo, M.1    Chan, K.M.2    Hornung, F.3
  • 177
    • 0031774633 scopus 로고    scopus 로고
    • Localization of apoptotic cells within the human endometrium and correlation between apoptosis and p21 expression
    • Toki T, Mori A, Shimizu M, Nikaido T, Fujii S. Localization of apoptotic cells within the human endometrium and correlation between apoptosis and p21 expression. Mol Hum Reprod 1998; 4: 1157-1164.
    • (1998) Mol Hum Reprod , vol.4 , pp. 1157-1164
    • Toki, T.1    Mori, A.2    Shimizu, M.3    Nikaido, T.4    Fujii, S.5
  • 178
    • 77955793357 scopus 로고    scopus 로고
    • Maturation of the olfactory sensory neurons by Apaf-1/caspase-9-mediated caspase activity
    • Ohsawa S, Hamada S, Kuida K, et al. Maturation of the olfactory sensory neurons by Apaf-1/caspase-9-mediated caspase activity. Proc Natl Acad Sci USA 2011; 107: 13366-13371.
    • (2011) Proc Natl Acad Sci USA , vol.107 , pp. 13366-13371
    • Ohsawa, S.1    Hamada, S.2    Kuida, K.3
  • 179
    • 33744493941 scopus 로고    scopus 로고
    • Apoptosis in lens development and pathology
    • Yan Q, Liu JP, Li DW. Apoptosis in lens development and pathology. Differentiation 2006; 74: 195-211.
    • (2006) Differentiation , vol.74 , pp. 195-211
    • Yan, Q.1    Liu, J.P.2    Li, D.W.3
  • 180
    • 0035837040 scopus 로고    scopus 로고
    • Hepatitis C virus core protein enhances FADD-mediated apoptosis and suppresses TRADD signaling of tumor necrosis factor receptor
    • Zhu N, Ware CF, Lai MM. Hepatitis C virus core protein enhances FADD-mediated apoptosis and suppresses TRADD signaling of tumor necrosis factor receptor. Virology 2001; 283: 178-187.
    • (2001) Virology , vol.283 , pp. 178-187
    • Zhu, N.1    Ware, C.F.2    Lai, M.M.3
  • 181
    • 0025772343 scopus 로고
    • Induction of bcl-2 expression by Epstein-Barr virus latent membrane protein 1 protects infected B cells from programmed cell death
    • Henderson S, Rowe M, Gregory C, et al. Induction of bcl-2 expression by Epstein-Barr virus latent membrane protein 1 protects infected B cells from programmed cell death. Cell 1991; 65: 1107-1115.
    • (1991) Cell , vol.65 , pp. 1107-1115
    • Henderson, S.1    Rowe, M.2    Gregory, C.3
  • 182
    • 0030952369 scopus 로고    scopus 로고
    • Perturbation of the p53 response by human papillomavirus type 16 E7
    • Hickman ES, Bates S, Vousden KH. Perturbation of the p53 response by human papillomavirus type 16 E7. J Virol 1997; 71: 3710-3718.
    • (1997) J Virol , vol.71 , pp. 3710-3718
    • Hickman, E.S.1    Bates, S.2    Vousden, K.H.3
  • 184
    • 34250016055 scopus 로고    scopus 로고
    • Apoptotic neuronal death in Parkinson's disease: involvement of nitric oxide
    • Singh S, Dikshit M. Apoptotic neuronal death in Parkinson's disease: involvement of nitric oxide. Brain Res Rev 2007; 54: 233-250.
    • (2007) Brain Res Rev , vol.54 , pp. 233-250
    • Singh, S.1    Dikshit, M.2
  • 186
    • 77549084450 scopus 로고    scopus 로고
    • Mitochondrial-dependent apoptosis in Huntington's disease human cybrids
    • Ferreira IL, Nascimento MV, Ribeiro M, et al. Mitochondrial-dependent apoptosis in Huntington's disease human cybrids. Exp Neurol 2010; 222: 243-255.
    • (2010) Exp Neurol , vol.222 , pp. 243-255
    • Ferreira, I.L.1    Nascimento, M.V.2    Ribeiro, M.3
  • 187
    • 0031558778 scopus 로고    scopus 로고
    • Upregulation of the anti-apoptotic protein Bcl-2 may be an early event in neurodegeneration: studies on Parkinson's and incidental Lewy body disease
    • Marshall KA, Daniel SE, Cairns N, Jenner P, Halliwell B. Upregulation of the anti-apoptotic protein Bcl-2 may be an early event in neurodegeneration: studies on Parkinson's and incidental Lewy body disease. Biochem Biophys Res Commun 1997; 240: 84-87.
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 84-87
    • Marshall, K.A.1    Daniel, S.E.2    Cairns, N.3    Jenner, P.4    Halliwell, B.5
  • 188
    • 0029960673 scopus 로고    scopus 로고
    • Involvement of the CD95 (APO-1/Fas) receptor/ligand system in multiple sclerosis brain
    • Dowling P, Shang G, Raval S, et al. Involvement of the CD95 (APO-1/Fas) receptor/ligand system in multiple sclerosis brain. J Exp Med 1996; 184: 1513-1518.
    • (1996) J Exp Med , vol.184 , pp. 1513-1518
    • Dowling, P.1    Shang, G.2    Raval, S.3
  • 189
    • 0030738366 scopus 로고    scopus 로고
    • Multiple sclerosis: oligodendrocytes display cell death-related molecules in situ but do not undergo apoptosis
    • Bonetti B, Raine CS. Multiple sclerosis: oligodendrocytes display cell death-related molecules in situ but do not undergo apoptosis. Ann Neurol 1997; 42: 74-84.
    • (1997) Ann Neurol , vol.42 , pp. 74-84
    • Bonetti, B.1    Raine, C.S.2
  • 190
  • 191
    • 0030731917 scopus 로고    scopus 로고
    • Nitric oxide primes pancreatic beta cells for Fas-mediated destruction in insulin-dependent diabetes mellitus
    • Stassi G, De Maria R, Trucco G, et al. Nitric oxide primes pancreatic beta cells for Fas-mediated destruction in insulin-dependent diabetes mellitus. J Exp Med 1997; 186: 1193-1200.
    • (1997) J Exp Med , vol.186 , pp. 1193-1200
    • Stassi, G.1    De Maria, R.2    Trucco, G.3
  • 192
    • 77953936771 scopus 로고    scopus 로고
    • Mechanisms of pancreatic beta-cell apoptosis in diabetes and its therapies
    • Johnson JD, Luciani DS. Mechanisms of pancreatic beta-cell apoptosis in diabetes and its therapies. Adv Exp Med Biol 2011; 654: 447-462.
    • (2011) Adv Exp Med Biol , vol.654 , pp. 447-462
    • Johnson, J.D.1    Luciani, D.S.2
  • 193
    • 0029029058 scopus 로고
    • Sensitization of T cells to CD95-mediated apoptosis by HIV-1 Tat and gp120
    • Westendorp MO, Frank R, Ochsenbauer C, et al. Sensitization of T cells to CD95-mediated apoptosis by HIV-1 Tat and gp120. Nature 1995; 375: 497-500.
    • (1995) Nature , vol.375 , pp. 497-500
    • Westendorp, M.O.1    Frank, R.2    Ochsenbauer, C.3
  • 194
    • 0021821903 scopus 로고
    • Involvement of the bcl-2 gene in human follicular lymphoma
    • Tsujimoto Y, Cossman J, Jaffe E, Croce CM. Involvement of the bcl-2 gene in human follicular lymphoma. Science 1985; 228: 1440-1443.
    • (1985) Science , vol.228 , pp. 1440-1443
    • Tsujimoto, Y.1    Cossman, J.2    Jaffe, E.3    Croce, C.M.4
  • 195
    • 0035192977 scopus 로고    scopus 로고
    • bcl-2/bax ratio as a predictive marker for therapeutic response to radiotherapy in patients with rectal cancer
    • Scopa CD, Vagianos C, Kardamakis D, et al. bcl-2/bax ratio as a predictive marker for therapeutic response to radiotherapy in patients with rectal cancer. Appl Immunohistochem Mol Morphol 2001; 9: 329-334.
    • (2001) Appl Immunohistochem Mol Morphol , vol.9 , pp. 329-334
    • Scopa, C.D.1    Vagianos, C.2    Kardamakis, D.3
  • 196
    • 0035678781 scopus 로고    scopus 로고
    • A phase I dose-finding study of combined treatment with an antisense Bcl-2 oligonucleotide (Genasense) and mitoxantrone in patients with metastatic hormone-refractory prostate cancer
    • Chi KN, Gleave ME, Klasa R, et al. A phase I dose-finding study of combined treatment with an antisense Bcl-2 oligonucleotide (Genasense) and mitoxantrone in patients with metastatic hormone-refractory prostate cancer. Clin Cancer Res 2001; 7: 3920-3927.
    • (2001) Clin Cancer Res , vol.7 , pp. 3920-3927
    • Chi, K.N.1    Gleave, M.E.2    Klasa, R.3
  • 198
    • 0242721540 scopus 로고    scopus 로고
    • Bcl-2 antisense oligonucleotides: a potential novel strategy for the treatment of breast cancer
    • Nahta R, Esteva FJ. Bcl-2 antisense oligonucleotides: a potential novel strategy for the treatment of breast cancer. Semin Oncol 2003; 30: 143-149.
    • (2003) Semin Oncol , vol.30 , pp. 143-149
    • Nahta, R.1    Esteva, F.J.2
  • 199
    • 79952112980 scopus 로고    scopus 로고
    • Drugs targeting Bcl-2 family members as an emerging strategy in cancer
    • Leber B, Geng F, Kale J, Andrews DW. Drugs targeting Bcl-2 family members as an emerging strategy in cancer. Expert Rev Mol Med 2011; 12: e28.
    • (2011) Expert Rev Mol Med , vol.12
    • Leber, B.1    Geng, F.2    Kale, J.3    Andrews, D.W.4
  • 200
    • 34948871492 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins as targets for anticancer therapy
    • Fulda S. Inhibitor of apoptosis proteins as targets for anticancer therapy. Expert Rev Anticancer Ther 2007; 7: 1255-1264.
    • (2007) Expert Rev Anticancer Ther , vol.7 , pp. 1255-1264
    • Fulda, S.1
  • 201
    • 0036021196 scopus 로고    scopus 로고
    • A novel high-through-put assay for screening of pro-apoptotic drugs
    • Hagg M, Biven K, Ueno T, et al. A novel high-through-put assay for screening of pro-apoptotic drugs. Invest New Drugs 2002; 20: 253-259.
    • (2002) Invest New Drugs , vol.20 , pp. 253-259
    • Hagg, M.1    Biven, K.2    Ueno, T.3
  • 202
    • 12444342652 scopus 로고    scopus 로고
    • A novel assay for discovery and characterization of pro-apoptotic drugs and for monitoring apoptosis in patient sera
    • Biven K, Erdal H, Hagg M, et al. A novel assay for discovery and characterization of pro-apoptotic drugs and for monitoring apoptosis in patient sera. Apoptosis 2003; 8: 263-268.
    • (2003) Apoptosis , vol.8 , pp. 263-268
    • Biven, K.1    Erdal, H.2    Hagg, M.3
  • 203
    • 33751538939 scopus 로고    scopus 로고
    • Response to neoadjuvant chemotherapy in breast cancer could be predictable by measuring a novel serum apoptosis product, caspase-cleaved cytokeratin 18: a prospective pilot study
    • Demiray M, Ulukaya EE, Arslan M, et al. Response to neoadjuvant chemotherapy in breast cancer could be predictable by measuring a novel serum apoptosis product, caspase-cleaved cytokeratin 18: a prospective pilot study. Cancer Invest 2006; 24: 669-676.
    • (2006) Cancer Invest , vol.24 , pp. 669-676
    • Demiray, M.1    Ulukaya, E.E.2    Arslan, M.3
  • 204
    • 16644375439 scopus 로고    scopus 로고
    • A close association between alteration in growth kinetics by neoadjuvant chemotherapy and survival outcome in primary breast cancer
    • Takada M, Kataoka A, Toi M, et al. A close association between alteration in growth kinetics by neoadjuvant chemotherapy and survival outcome in primary breast cancer. Int J Oncol 2004; 25: 397-405.
    • (2004) Int J Oncol , vol.25 , pp. 397-405
    • Takada, M.1    Kataoka, A.2    Toi, M.3
  • 205
    • 34247642617 scopus 로고    scopus 로고
    • The levels of caspase-cleaved cytokeratin 18 are elevated in serum from patients with lung cancer and helpful to predict the survival
    • Ulukaya E, Yilmaztepe A, Akgoz S, Linder S, Karadag M. The levels of caspase-cleaved cytokeratin 18 are elevated in serum from patients with lung cancer and helpful to predict the survival. Lung Cancer 2007; 56: 399-404.
    • (2007) Lung Cancer , vol.56 , pp. 399-404
    • Ulukaya, E.1    Yilmaztepe, A.2    Akgoz, S.3    Linder, S.4    Karadag, M.5
  • 206
    • 70349972775 scopus 로고    scopus 로고
    • Apoptosis and cytokines in non-alcoholic steatohepatitis
    • Syn WK, Choi SS, Diehl AM. Apoptosis and cytokines in non-alcoholic steatohepatitis. Clin Liver Dis 2009; 13: 565-580.
    • (2009) Clin Liver Dis , vol.13 , pp. 565-580
    • Syn, W.K.1    Choi, S.S.2    Diehl, A.M.3
  • 207
    • 33947528311 scopus 로고    scopus 로고
    • Soluble forms of extracellular cytokeratin 18 may differentiate simple steatosis from nonalcoholic steatohepatitis
    • Yilmaz Y, Dolar E, Ulukaya E, et al. Soluble forms of extracellular cytokeratin 18 may differentiate simple steatosis from nonalcoholic steatohepatitis. World J Gastroenterol 2007; 13: 837-844.
    • (2007) World J Gastroenterol , vol.13 , pp. 837-844
    • Yilmaz, Y.1    Dolar, E.2    Ulukaya, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.