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Volumn 15, Issue 2, 2009, Pages 420-424

Targeting the apoptosome for cancer therapy

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSOME; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE; CASPASE 3; CYTOCHROME C; FAS LIGAND; PROCASPASE 9; TUMOR NECROSIS FACTOR;

EID: 59449110529     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: 10.1158/1078-0432.CCR-08-1172     Document Type: Review
Times cited : (89)

References (70)
  • 2
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome C - mediated apoptosis
    • Jiang X, Wang X. Cytochrome C - mediated apoptosis. Annu Rev Biochem 2004;73:87-106.
    • (2004) Annu Rev Biochem , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 4
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996; 86:147-57.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 5
    • 0032478659 scopus 로고    scopus 로고
    • Death by dozens of cuts
    • Barinaga M. Death by dozens of cuts. Science 1998; 280:32-4.
    • (1998) Science , vol.280 , pp. 32-34
    • Barinaga, M.1
  • 6
    • 27544471076 scopus 로고    scopus 로고
    • The mitochondrial death squad: Hardened killers or innocent bystanders?
    • Ekert PG, Vaux DL. The mitochondrial death squad: hardened killers or innocent bystanders? Curr Opin Cell Biol 2005;17:626-30.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 626-630
    • Ekert, P.G.1    Vaux, D.L.2
  • 7
    • 0345731420 scopus 로고    scopus 로고
    • Chemical-induced apoptosis: Formation of the Apaf-1 apoptosome
    • Cain K. Chemical-induced apoptosis: formation of the Apaf-1 apoptosome. Drug Metab Rev 2003:35: 337-63.
    • (2003) Drug Metab Rev , vol.35 , pp. 337-363
    • Cain, K.1
  • 8
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • Riedl SJ, Salvesen GS. The apoptosome: signalling platform of cell death. Nat Rev Mol Cell Biol 2007;8: 405-13.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 9
    • 33845501864 scopus 로고    scopus 로고
    • Apoptosome: A platform for the activation of initiator caspases
    • Bao Q, Shi Y. Apoptosome: a platform for the activation of initiator caspases. Cell Death Differ 2007;14: 56-65
    • (2007) Cell Death Differ , vol.14 , pp. 56-65
    • Bao, Q.1    Shi, Y.2
  • 10
    • 0034708504 scopus 로고    scopus 로고
    • Expression and functional analysis of Apaf-1 isoforms
    • Benedict MA, HuY, Inohara N, Nún̊tez G. Expression and functional analysis of Apaf-1 isoforms. J Biol Chem 2000:275:8461 -8.
    • (2000) J Biol Chem , vol.275 , pp. 8461-8468
    • Benedict, M.A.1    Hu, Y.2    Inohara, N.3    Nún̊tez, G.4
  • 11
    • 27644483812 scopus 로고    scopus 로고
    • A structure of the human apoptosome at 12.8 Å resolution provides insights into this cell death platform
    • Yu X, Acehan D, Menetret JF, et al. A structure of the human apoptosome at 12.8 Å resolution provides insights into this cell death platform. Structure 2005; 13:1725-35.
    • (2005) Structure , vol.13 , pp. 1725-1735
    • Yu, X.1    Acehan, D.2    Menetret, J.F.3
  • 12
    • 0033581154 scopus 로고    scopus 로고
    • Stoichiometry, free energy, and kinetic aspects of cytochrome c: Apaf-1 binding in apoptosis
    • Purring C, Zou H, Wang X, McLendon G. Stoichiometry, free energy, and kinetic aspects of cytochrome c: Apaf-1 binding in apoptosis. J Am Chem Soc 1999; 121:7435.
    • (1999) J Am Chem Soc , vol.121 , pp. 7435
    • Purring, C.1    Zou, H.2    Wang, X.3    McLendon, G.4
  • 13
    • 0037086663 scopus 로고    scopus 로고
    • A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect
    • Abdullaev Z, Bodrova ME, Chernyak BV, et al. A cytochrome c mutant with high electron transfer and antioxidant activities but devoid of apoptogenic effect. Biochem J 2002;362:749-54.
    • (2002) Biochem J , vol.362 , pp. 749-754
    • Abdullaev, Z.1    Bodrova, M.E.2    Chernyak, B.V.3
  • 14
    • 0035918306 scopus 로고    scopus 로고
    • A mutational epitope for cytochrome c binding to the apoptosis protease activation factor-1
    • Yu T. Wang X, Purring-Koch C. Wei Y, McLendon GL. A mutational epitope for cytochrome c binding to the apoptosis protease activation factor-1. J Biol Chem 2001;276:13034-8.
    • (2001) J Biol Chem , vol.276 , pp. 13034-13038
    • Yu, T.1    Wang, X.2    Purring-Koch, C.3    Wei, Y.4    McLendon, G.L.5
  • 15
    • 0034717037 scopus 로고    scopus 로고
    • Determinants of cytochrome c pro-apoptotic activity
    • Kluck RM, Ellerby LM, Ellerby HM, et al. Determinants of cytochrome c pro-apoptotic activity. J Biol Chem 2000;275:16127-33.
    • (2000) J Biol Chem , vol.275 , pp. 16127-16133
    • Kluck, R.M.1    Ellerby, L.M.2    Ellerby, H.M.3
  • 16
    • 33745246534 scopus 로고    scopus 로고
    • Intracellular nucleotides act as critical prosurvival factors by binding to cytochrome c and inhibiting apoptosome
    • Chandra D, Bratton SB, Person MD, et al. Intracellular nucleotides act as critical prosurvival factors by binding to cytochrome c and inhibiting apoptosome. Cell 2006;125:1333-46.
    • (2006) Cell , vol.125 , pp. 1333-1346
    • Chandra, D.1    Bratton, S.B.2    Person, M.D.3
  • 17
    • 41349097770 scopus 로고    scopus 로고
    • A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia
    • Morison IM, Cramer-Bordé EM, Cheesman EJ, et al. A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia. Nat Genet 2008;40:387-9.
    • (2008) Nat Genet , vol.40 , pp. 387-389
    • Morison, I.M.1    Cramer-Bordé, E.M.2    Cheesman, E.J.3
  • 18
    • 0033596909 scopus 로고    scopus 로고
    • A conformational change incytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles
    • Jemmerson R, Liu J, Hausauer D, Lam K-P, Mondino A, Nelson RD. A conformational change incytochrome c of apoptotic and necrotic cells is detected by monoclonal antibody binding and mimicked by association of the native antigen with synthetic phospholipid vesicles. Biochemistry 1999;38: 3599-609.
    • (1999) Biochemistry , vol.38 , pp. 3599-3609
    • Jemmerson, R.1    Liu, J.2    Hausauer, D.3    Lam, K.-P.4    Mondino, A.5    Nelson, R.D.6
  • 19
    • 15244362527 scopus 로고    scopus 로고
    • ATP specifically drives refolding of non-native conformations of cytochrome c
    • Sinibaldi F, Mei G, Polticelli F, et al. ATP specifically drives refolding of non-native conformations of cytochrome c. Protein Sci 2005;14:1049-58.
    • (2005) Protein Sci , vol.14 , pp. 1049-1058
    • Sinibaldi, F.1    Mei, G.2    Polticelli, F.3
  • 20
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat regulates Apaf-1 self-association and procaspase-9 activation
    • Hu Y, Ding L, Spencer DM, Nún̄ez G. WD-40 repeat regulates Apaf-1 self-association and procaspase-9 activation. J Biol Chem 1998;273:33489-94.
    • (1998) J Biol Chem , vol.273 , pp. 33489-33494
    • Hu, Y.1    Ding, L.2    Spencer, D.M.3    Nún̄ez, G.4
  • 21
    • 27644505459 scopus 로고    scopus 로고
    • Kim HE, Du F, Fang M.Wang X. Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc Natl Acad Sci U S A 2005;102:17545-50.
    • Kim HE, Du F, Fang M.Wang X. Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc Natl Acad Sci U S A 2005;102:17545-50.
  • 22
    • 0034710942 scopus 로고    scopus 로고
    • Cytochrome c binding to Apaf-1: The effects of dATP and ionic strength
    • Purring-Koch C, McLendon G. Cytochrome c binding to Apaf-1: the effects of dATP and ionic strength. Proc Natl Acad Sci U S A 2000;97:11928-31.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11928-11931
    • Purring-Koch, C.1    McLendon, G.2
  • 23
    • 0035834691 scopus 로고    scopus 로고
    • Physiological concentrations of K+ inhibit cytochrome c - dependent formation of the apoptosome
    • Cain K, Langlais C, Sun X-M, Brown DG, Cohen GM. Physiological concentrations of K+ inhibit cytochrome c - dependent formation of the apoptosome. J Biol Chem 2001;276:41985-90.
    • (2001) J Biol Chem , vol.276 , pp. 41985-41990
    • Cain, K.1    Langlais, C.2    Sun, X.-M.3    Brown, D.G.4    Cohen, G.M.5
  • 24
    • 0034796446 scopus 로고    scopus 로고
    • Effect of pH, ionic charge, and osmolality of cytochrome c - mediated caspase activation
    • Segal M, Beem E. Effect of pH, ionic charge, and osmolality of cytochrome c - mediated caspase activation. Am J Physiol 2001;281:C1196-204.
    • (2001) Am J Physiol , vol.281
    • Segal, M.1    Beem, E.2
  • 25
    • 0031973203 scopus 로고    scopus 로고
    • Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts
    • Hampton MB, Zhivotovsky B, Slater AFG, Burgess DH, Orrenius S. Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts. Biochem J 1998;329:95-9.
    • (1998) Biochem J , vol.329 , pp. 95-99
    • Hampton, M.B.1    Zhivotovsky, B.2    Slater, A.F.G.3    Burgess, D.H.4    Orrenius, S.5
  • 26
    • 33846236461 scopus 로고    scopus 로고
    • Bao Q, Lu W. Rabinowitz JD, Shi Y Calcium blocks formation of apoptosome by preventing nucleotide exchange in Apaf-1. Mol Cell 2007;25:181 -92.
    • Bao Q, Lu W. Rabinowitz JD, Shi Y Calcium blocks formation of apoptosome by preventing nucleotide exchange in Apaf-1. Mol Cell 2007;25:181 -92.
  • 27
    • 15644374609 scopus 로고    scopus 로고
    • Intracellular K+ supresses the activation of apoptosis in lymphocytes
    • Hughes FM, Jr., Bortner CD, Purdy GD, Cidlowski JA. Intracellular K+ supresses the activation of apoptosis in lymphocytes. J Biol Chem 1997;272:30567-76.
    • (1997) J Biol Chem , vol.272 , pp. 30567-30576
    • Hughes Jr., F.M.1    Bortner, C.D.2    Purdy, G.D.3    Cidlowski, J.A.4
  • 28
    • 0031451872 scopus 로고    scopus 로고
    • A primary role for K+ and Na+ efflux in the activation of apoptosis
    • Bortner CD, Hughes FM, Jr., Cidlowski JA. A primary role for K+ and Na+ efflux in the activation of apoptosis. J Biol Chem 1997;272:32436-42.
    • (1997) J Biol Chem , vol.272 , pp. 32436-32442
    • Bortner, C.D.1    Hughes Jr., F.M.2    Cidlowski, J.A.3
  • 29
    • 0032489390 scopus 로고    scopus 로고
    • Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
    • Pan G, O'Rourke K, Dixit VM. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J Biol Chem 1998:273:5841 -5.
    • (1998) J Biol Chem , vol.273 , pp. 5841-5845
    • Pan, G.1    O'Rourke, K.2    Dixit, V.M.3
  • 30
    • 0032515874 scopus 로고    scopus 로고
    • Bcl-XL interacts with Apaf-1 and inhibits Apaf- 1-dependent caspase-9 activation
    • Hu Y, Benedict MA. Wu D, Inohara N, Nún̊ez G. Bcl-XL interacts with Apaf-1 and inhibits Apaf- 1-dependent caspase-9 activation. Proc Natl Acad Sci USA1998;95:4386-91.
    • Proc Natl Acad Sci , vol.USA1998 , Issue.95 , pp. 4386-4391
    • Hu, Y.1    Benedict, M.A.2    Wu, D.3    Inohara, N.4    Nún̊ez, G.5
  • 31
    • 0033578303 scopus 로고    scopus 로고
    • Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1
    • Moriishi K, Huang DCS, Cory S, Adams JM. Bcl-2 family members do not inhibit apoptosis by binding the caspase activator Apaf-1. Proc Natl Acad Sci U S A 1999;96:9683-8.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9683-9688
    • Moriishi, K.1    Huang, D.C.S.2    Cory, S.3    Adams, J.M.4
  • 32
    • 2442540299 scopus 로고    scopus 로고
    • Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/caspase-9 apoptosome complex
    • Twiddy D, Brown DG, Adrain C, et al. Pro-apoptotic proteins released from the mitochondria regulate the protein composition and caspase-processing activity of the native Apaf-1/caspase-9 apoptosome complex. J Biol Chem 2004;279:19665-82.
    • (2004) J Biol Chem , vol.279 , pp. 19665-19682
    • Twiddy, D.1    Brown, D.G.2    Adrain, C.3
  • 33
    • 2942532135 scopus 로고    scopus 로고
    • Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes
    • Hill MM, Adrain C, Duriez PJ, Creagh EM, Martin SJ. Analysis of the composition, assembly kinetics and activity of native Apaf-1 apoptosomes. EMBO J 2004;23:2134-45.
    • (2004) EMBO J , vol.23 , pp. 2134-2145
    • Hill, M.M.1    Adrain, C.2    Duriez, P.J.3    Creagh, E.M.4    Martin, S.J.5
  • 35
    • 0034253533 scopus 로고    scopus 로고
    • Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
    • Beere HM, Wolf BA, Cain K, et al. Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nat Cell Biol 2000;2:469-75.
    • (2000) Nat Cell Biol , vol.2 , pp. 469-475
    • Beere, H.M.1    Wolf, B.A.2    Cain, K.3
  • 36
    • 10944266160 scopus 로고    scopus 로고
    • Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1
    • Steel R, Doherty JP, Buzzard K, Clemons N, Hawkins CJ, Anderson RL. Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1. J Biol Chem 2004;279: 51490-9.
    • (2004) J Biol Chem , vol.279 , pp. 51490-51499
    • Steel, R.1    Doherty, J.P.2    Buzzard, K.3    Clemons, N.4    Hawkins, C.J.5    Anderson, R.L.6
  • 37
    • 0034282104 scopus 로고    scopus 로고
    • Hsp27 negatively regulates cell death by interacting with cytochrome c
    • Bruey J-M, Ducasse C, Bonniaud P, et al. Hsp27 negatively regulates cell death by interacting with cytochrome c. Nat Cell Biol 2000, 2:645-52.
    • (2000) Nat Cell Biol , vol.2 , pp. 645-652
    • Bruey, J.-M.1    Ducasse, C.2    Bonniaud, P.3
  • 38
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c - mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P, Saleh A, Nakazawa A, et al. Negative regulation of cytochrome c - mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 2000;19:4310-22.
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3
  • 39
    • 50249168335 scopus 로고    scopus 로고
    • Inhibition of apoptosome formation by suppression of Hsp90β phosphorylation in tyrosine kinase-induced leukemias
    • Kurokawa M, Zhao C, Reya T, Kornbluth S. Inhibition of apoptosome formation by suppression of Hsp90β phosphorylation in tyrosine kinase-induced leukemias. Mol Cell Biol 2008;28:5494-506.
    • (2008) Mol Cell Biol , vol.28 , pp. 5494-5506
    • Kurokawa, M.1    Zhao, C.2    Reya, T.3    Kornbluth, S.4
  • 40
    • 0037428217 scopus 로고    scopus 로고
    • Distinctive roles of PHAP proteins and prothymosin-α in a death regulatory pathway
    • Jiang X, Kim H-E, Shu H-B, et al. Distinctive roles of PHAP proteins and prothymosin-α in a death regulatory pathway. Science 2003;299:223-6.
    • (2003) Science , vol.299 , pp. 223-226
    • Jiang, X.1    Kim, H.-E.2    Shu, H.-B.3
  • 41
    • 43049147998 scopus 로고    scopus 로고
    • PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1
    • Kim HE, Jiang X, Du F, Wang X. PHAPI, CAS, and Hsp70 promote apoptosome formation by preventing Apaf-1 aggregation and enhancing nucleotide exchange on Apaf-1. Mol Cell 2008;30:239-47.
    • (2008) Mol Cell , vol.30 , pp. 239-247
    • Kim, H.E.1    Jiang, X.2    Du, F.3    Wang, X.4
  • 42
    • 33644515959 scopus 로고    scopus 로고
    • Malicet C, Giroux V. Vasseur S, Dagorn JC, Neira JL, lovanna JL. Regulation of apoptosis by the p8/prothymosin α complex. Proc Natl Acad Sci U S A 2006; 103:2617-76.
    • Malicet C, Giroux V. Vasseur S, Dagorn JC, Neira JL, lovanna JL. Regulation of apoptosis by the p8/prothymosin α complex. Proc Natl Acad Sci U S A 2006; 103:2617-76.
  • 43
    • 0037422415 scopus 로고    scopus 로고
    • Cytochrome c is transformed from ami- to pro-oxidant when interacting with truncated oncoprotein prothymosin α
    • Markova OV, Evstafieva AG, Mansurova SE, et al. Cytochrome c is transformed from ami- to pro-oxidant when interacting with truncated oncoprotein prothymosin α. Biochim Biophys Acta 2003;1557: 109-17.
    • (2003) Biochim Biophys Acta , vol.1557 , pp. 109-117
    • Markova, O.V.1    Evstafieva, A.G.2    Mansurova, S.E.3
  • 44
    • 33646087420 scopus 로고    scopus 로고
    • The apoptosome: Physiological, developmental, and pathological modes of regulation
    • Schafer ZT, Kornbluth S. The apoptosome: physiological, developmental, and pathological modes of regulation. Dev Cell 2006;10:549-61.
    • (2006) Dev Cell , vol.10 , pp. 549-561
    • Schafer, Z.T.1    Kornbluth, S.2
  • 45
    • 0038381423 scopus 로고    scopus 로고
    • Nitrosylation of cytochrome c during apoptosis
    • Schonhoff C, Gaston B, Mannick JB. Nitrosylation of cytochrome c during apoptosis. J Biol Chem 2003;278:18265-70.
    • (2003) J Biol Chem , vol.278 , pp. 18265-18270
    • Schonhoff, C.1    Gaston, B.2    Mannick, J.B.3
  • 46
    • 29144432723 scopus 로고    scopus 로고
    • Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanism
    • Suto D, Sato K, Ohba Y, Yoshimura T, Fujii J. Suppression of the pro-apoptotic function of cytochrome c by singlet oxygen via a haem redox state-independent mechanism. Biochem J 2005;392:399-406.
    • (2005) Biochem J , vol.392 , pp. 399-406
    • Suto, D.1    Sato, K.2    Ohba, Y.3    Yoshimura, T.4    Fujii, J.5
  • 47
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, EWeinberg RA. The hallmarks of cancer. Cell 2000;100:57 - 70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    EWeinberg, R.A.2
  • 49
    • 43349088699 scopus 로고    scopus 로고
    • The apoptosome: Emerging insights and new potential targets for drug design
    • D'Amelio M, Tino E, Cecconi F. The apoptosome: emerging insights and new potential targets for drug design. Pharm Res 2008;25:740 - 51.
    • (2008) Pharm Res , vol.25 , pp. 740-751
    • D'Amelio, M.1    Tino, E.2    Cecconi, F.3
  • 50
    • 39449127365 scopus 로고    scopus 로고
    • Big wheel keeps on turning: Apoptosome regulation and its role in chemoresistance
    • Fadeel B, Ottosson A, Pervaiz S. Big wheel keeps on turning: apoptosome regulation and its role in chemoresistance. Cell Death Differ 2008;15:443-52.
    • (2008) Cell Death Differ , vol.15 , pp. 443-452
    • Fadeel, B.1    Ottosson, A.2    Pervaiz, S.3
  • 51
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • Johnstone RW, Ruefli AA, Lowe SW. Apoptosis: a link between cancer genetics and chemotherapy. Cell 2002;108:153-64.
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 52
    • 17444383660 scopus 로고    scopus 로고
    • Apoptosome dysfunction in human cancer
    • Hajra KM, Liu JR. Apoptosome dysfunction in human cancer. Apoptosis 2004;9:691 -704.
    • (2004) Apoptosis , vol.9 , pp. 691-704
    • Hajra, K.M.1    Liu, J.R.2
  • 53
    • 0035843169 scopus 로고    scopus 로고
    • Inactivation of the apoptosis effector Apaf-1 in malignant melanoma
    • Soengas MS, Capodieci P, Polsky D, et al. Inactivation of the apoptosis effector Apaf-1 in malignant melanoma. Nature 2001;409:207-11.
    • (2001) Nature , vol.409 , pp. 207-211
    • Soengas, M.S.1    Capodieci, P.2    Polsky, D.3
  • 54
    • 1542510618 scopus 로고    scopus 로고
    • Allelic imbalance of 12q22-23 associated with APAF-1 locus correlates with poor disease outcome in cutaneous melanoma
    • Fujimoto A, Takeuchi H, Taback B, et al. Allelic imbalance of 12q22-23 associated with APAF-1 locus correlates with poor disease outcome in cutaneous melanoma. Cancer Res 2004;64:2245-50.
    • (2004) Cancer Res , vol.64 , pp. 2245-2250
    • Fujimoto, A.1    Takeuchi, H.2    Taback, B.3
  • 55
    • 10744220426 scopus 로고    scopus 로고
    • Analysis of APAF- 1 expression in human cutaneous melanoma progression
    • Baldi A, Santini D, Russo P, et al. Analysis of APAF- 1 expression in human cutaneous melanoma progression. Exp Dermatol 2004;13:93-7.
    • (2004) Exp Dermatol , vol.13 , pp. 93-97
    • Baldi, A.1    Santini, D.2    Russo, P.3
  • 58
    • 0035880232 scopus 로고    scopus 로고
    • Apaf-1 protein deficiency confers resistance to cytochrome c -dependent apoptosis in human leukemic cells
    • Jia L, Srinivasula SM, Liu F-T, et al. Apaf-1 protein deficiency confers resistance to cytochrome c -dependent apoptosis in human leukemic cells. Blood 2001;98:414-21.
    • (2001) Blood , vol.98 , pp. 414-421
    • Jia, L.1    Srinivasula, S.M.2    Liu, F.-T.3
  • 59
    • 0035823503 scopus 로고    scopus 로고
    • Defective cytochrome c - dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity
    • Wolf BB, Schuler M, Li W-G, et al. Defective cytochrome c - dependent caspase activation in ovarian cancer cell lines due to diminished or absent apoptotic protease activating factor-1 activity. J Biol Chem 2001; 276:34244-51.
    • (2001) J Biol Chem , vol.276 , pp. 34244-34251
    • Wolf, B.B.1    Schuler, M.2    Li, W.-G.3
  • 60
    • 0242667892 scopus 로고    scopus 로고
    • Frequent LOH at chromosome 12q22-23 and Apaf-1 inactivation in glioblastoma
    • WatanabeT, HirotaY, ArakawaY, et al. Frequent LOH at chromosome 12q22-23 and Apaf-1 inactivation in glioblastoma. Brain Pathol 2003;13:431 -9.
    • (2003) Brain Pathol , vol.13 , pp. 431-439
    • Watanabe, T.1    Hirota, Y.2    Arakawa, Y.3
  • 61
    • 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: 1242-8.
    • (2003) Cancer Res , vol.63 , pp. 1242-1248
    • Schimmer, A.D.1    Pedersen, I.M.2    Kitada, S.3
  • 62
    • 18544385191 scopus 로고    scopus 로고
    • Plasma membrane sequestration of apoptotic protease- activating factor-1 in human B-lymphoma cells: A novel mechanism of chemoresistance
    • Sun Y Orrenius S, Pervaiz S, Fadeel B. Plasma membrane sequestration of apoptotic protease- activating factor-1 in human B-lymphoma cells: a novel mechanism of chemoresistance. Blood 2005; 105:4070-7.
    • (2005) Blood , vol.105 , pp. 4070-4077
    • Sun, Y.1    Orrenius, S.2    Pervaiz, S.3    Fadeel, B.4
  • 63
    • 37349001106 scopus 로고    scopus 로고
    • pp32/PHAPI determines the apoptosis response of non-small-cell lung cancer
    • Hoffarth S, Zitzer A. Wiewrodt R, et al. pp32/PHAPI determines the apoptosis response of non-small-cell lung cancer. Cell Death Differ 2008;15:161 -70.
    • (2008) Cell Death Differ , vol.15 , pp. 161-170
    • Hoffarth, S.1    Zitzer, A.2    Wiewrodt, R.3
  • 64
    • 34548036056 scopus 로고    scopus 로고
    • Modification of gene products involved in resistance to apoptosis in metastatic colon cancer cells: Roles of Fas, Apaf-1, NF-κB, IAPs, Smac/Diablo, and AIF
    • Huerta S, Heinzerling JH, Anguiano-Hernandez Y-M, et al. Modification of gene products involved in resistance to apoptosis in metastatic colon cancer cells: roles of Fas, Apaf-1, NF-κB, IAPs, Smac/Diablo, and AIF J Surg Res 2007;142: 184-94.
    • (2007) J Surg Res , vol.142 , pp. 184-194
    • Huerta, S.1    Heinzerling, J.H.2    Anguiano-Hernandez, Y.-M.3
  • 65
    • 20544432048 scopus 로고    scopus 로고
    • p53-defective tumors with a functional apoptosome-mediated pathway: A new therapeutic target
    • Mashima T, Oh-hara T, Sato S, et al. p53-defective tumors with a functional apoptosome-mediated pathway: a new therapeutic target. J Natl Cancer Inst 2005;97:765-77.
    • (2005) J Natl Cancer Inst , vol.97 , pp. 765-777
    • Mashima, T.1    Oh-hara, T.2    Sato, S.3
  • 66
    • 33644531879 scopus 로고    scopus 로고
    • Enhanced sensitivity to cytochrome c - induced apoptosis mediated by PHAP1 in breast cancer cells
    • Schafer ZT, Parrish AB, Wright KM, et al. Enhanced sensitivity to cytochrome c - induced apoptosis mediated by PHAP1 in breast cancer cells. Cancer Res 2006;66:2210-8.
    • (2006) Cancer Res , vol.66 , pp. 2210-2218
    • Schafer, Z.T.1    Parrish, A.B.2    Wright, K.M.3
  • 67
    • 38049136542 scopus 로고    scopus 로고
    • Differential Apaf-1 levels allow cytochrome c to induce apoptosis in brain tumors but not in normal neural tissues
    • Johnson CE, Huang YY, Parrish AB, et al. Differential Apaf-1 levels allow cytochrome c to induce apoptosis in brain tumors but not in normal neural tissues. Proc Natl Acad Sci U S A 2007;104:20820-5.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 20820-20825
    • Johnson, C.E.1    Huang, Y.Y.2    Parrish, A.B.3
  • 68
    • 7244245454 scopus 로고    scopus 로고
    • Decreased apoptosome activity with neuronal differentiation sets the threshold for strict IAP regulation of apoptosis
    • Wright KM, Linhoff MW, Potts PR. Deshmukh M. Decreased apoptosome activity with neuronal differentiation sets the threshold for strict IAP regulation of apoptosis. J Cell Biol 2004;167:303-13.
    • (2004) J Cell Biol , vol.167 , pp. 303-313
    • Wright, K.M.1    Linhoff, M.W.2    Potts, P.R.3    Deshmukh, M.4
  • 69
    • 0038610951 scopus 로고    scopus 로고
    • Direct activation of the apoptosis machinery as a mechanism to target cancer cells
    • Nguyen JT, Wells JA. Direct activation of the apoptosis machinery as a mechanism to target cancer cells. Proc Natl Acad Sci U S A 2003; 100:7533-8.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7533-7538
    • Nguyen, J.T.1    Wells, J.A.2
  • 70
    • 33747836834 scopus 로고    scopus 로고
    • Activation of mitochondrial pathway is crucial for tumor selective induction of apoptosis by LAQ824
    • Wang S, Yan-Neale Y, Cai R, Alimov I, Cohen D. Activation of mitochondrial pathway is crucial for tumor selective induction of apoptosis by LAQ824. Cell Cycle 2006;5:1662-8.
    • (2006) Cell Cycle , vol.5 , pp. 1662-1668
    • Wang, S.1    Yan-Neale, Y.2    Cai, R.3    Alimov, I.4    Cohen, D.5


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