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Volumn 10, Issue 6, 2010, Pages 604-613

Multistep and multitask Bax activation

Author keywords

Apoptosis; BH3; Ca2+; Endoplasmic reticulum; Mitochondria; MOMP

Indexed keywords

APOPTOSIS INDUCING FACTOR; BH3 PROTEIN; CALCIUM ION; CALPAIN; CARDIOLIPIN; CASPASE 3; CASPASE 8; CELL PROTEIN; CYTOCHROME C; INHIBITOR OF APOPTOSIS PROTEIN; INOSITOL 3 PHOSPHATE RECEPTOR; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BID; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 78149359658     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mito.2010.08.003     Document Type: Review
Times cited : (73)

References (133)
  • 1
    • 33750619845 scopus 로고    scopus 로고
    • How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?
    • Antignani A., Youle R.J. How do Bax and Bak lead to permeabilization of the outer mitochondrial membrane?. Curr. Opin. Cell Biol. 2006, 18:685-689.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 685-689
    • Antignani, A.1    Youle, R.J.2
  • 2
    • 0042237031 scopus 로고    scopus 로고
    • Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization
    • Arnoult D., Gaume B., Karbowski M., Sharpe J.C., Cecconi F., Youle R.J. Mitochondrial release of AIF and EndoG requires caspase activation downstream of Bax/Bak-mediated permeabilization. EMBO J. 2003, 22:4385-4399.
    • (2003) EMBO J. , vol.22 , pp. 4385-4399
    • Arnoult, D.1    Gaume, B.2    Karbowski, M.3    Sharpe, J.C.4    Cecconi, F.5    Youle, R.J.6
  • 3
    • 63649100705 scopus 로고    scopus 로고
    • Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity
    • Arzoine L., Zilberberg N., Ben-Romano R., Shoshan-Barmatz V. Voltage-dependent anion channel 1-based peptides interact with hexokinase to prevent its anti-apoptotic activity. J. Biol. Chem. 2009, 284:3946-3955.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3946-3955
    • Arzoine, L.1    Zilberberg, N.2    Ben-Romano, R.3    Shoshan-Barmatz, V.4
  • 4
    • 70449107007 scopus 로고    scopus 로고
    • Emerging role for members of the Bcl-2 family in mitochondrial morphogenesis
    • Autret A., Martin S.J. Emerging role for members of the Bcl-2 family in mitochondrial morphogenesis. Mol. Cell 2009, 36:355-363.
    • (2009) Mol. Cell , vol.36 , pp. 355-363
    • Autret, A.1    Martin, S.J.2
  • 5
    • 4444380912 scopus 로고    scopus 로고
    • Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid
    • Banerjee J., Ghosh S. Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid. Biochem. Biophys. Res. Commun. 2004, 323:310-314.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 310-314
    • Banerjee, J.1    Ghosh, S.2
  • 7
    • 0022291796 scopus 로고
    • Porin from bacterial and mitochondrial outer membranes
    • Benz R. Porin from bacterial and mitochondrial outer membranes. CRC Crit. Rev. Biochem. 1985, 19:145-190.
    • (1985) CRC Crit. Rev. Biochem. , vol.19 , pp. 145-190
    • Benz, R.1
  • 8
    • 0026687312 scopus 로고
    • Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations
    • Bernardi P., Vassanelli S., Veronese P., Colonna R., Szabo I., Zoratti M. Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J. Biol. Chem. 1992, 267:2934-2939.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2934-2939
    • Bernardi, P.1    Vassanelli, S.2    Veronese, P.3    Colonna, R.4    Szabo, I.5    Zoratti, M.6
  • 9
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi P., Broekemeier K.M., Pfeiffer D.R. Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J. Bioenerg. Biomembr. 1994, 26:509-517.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 11
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1, 4, 5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D., Patterson R.L., Sedaghat L., Glebova N.O., Kurosaki T., Snyder S.H. Cytochrome c binds to inositol (1, 4, 5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat. Cell Biol. 2003, 5:1051-1061.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 12
    • 47249134609 scopus 로고    scopus 로고
    • C-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis
    • Cao X., Bennett R.L., May W.S. c-Myc and caspase-2 are involved in activating Bax during cytotoxic drug-induced apoptosis. J. Biol. Chem. 2008, 283:14490-14496.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14490-14496
    • Cao, X.1    Bennett, R.L.2    May, W.S.3
  • 13
    • 0037070160 scopus 로고    scopus 로고
    • Involvement of the N-terminus of Bax in its intracellular localization and function
    • Cartron P.F., Moreau C., Oliver L., Mayat E., Meflah K., Vallette F.M. Involvement of the N-terminus of Bax in its intracellular localization and function. FEBS Lett. 2002, 512:95-100.
    • (2002) FEBS Lett. , vol.512 , pp. 95-100
    • Cartron, P.F.1    Moreau, C.2    Oliver, L.3    Mayat, E.4    Meflah, K.5    Vallette, F.M.6
  • 14
    • 9744244990 scopus 로고    scopus 로고
    • The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA
    • Cartron P.F., Gallenne T., Bougras G., Gautier F., Manero F., Vusio P., Meflah K., Vallette F.M., Juin P. The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA. Mol. Cell 2004, 16:807-818.
    • (2004) Mol. Cell , vol.16 , pp. 807-818
    • Cartron, P.F.1    Gallenne, T.2    Bougras, G.3    Gautier, F.4    Manero, F.5    Vusio, P.6    Meflah, K.7    Vallette, F.M.8    Juin, P.9
  • 15
    • 15444364107 scopus 로고    scopus 로고
    • Distinct domains control the addressing and the insertion of Bax into mitochondria
    • Cartron P.F., Arokium H., Oliver L., Meflah K., Manon S., Vallette F.M. Distinct domains control the addressing and the insertion of Bax into mitochondria. J. Biol. Chem. 2005, 280:10587-10598.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10587-10598
    • Cartron, P.F.1    Arokium, H.2    Oliver, L.3    Meflah, K.4    Manon, S.5    Vallette, F.M.6
  • 17
    • 77955973993 scopus 로고    scopus 로고
    • The dual role of calcium as messenger and stressor in cell damage, death, and survival
    • Cerella C., Diederich M., Ghibelli L. The dual role of calcium as messenger and stressor in cell damage, death, and survival. Int. J. Cell Biol. 2010, 2010:546163.
    • (2010) Int. J. Cell Biol. , vol.2010 , pp. 546163
    • Cerella, C.1    Diederich, M.2    Ghibelli, L.3
  • 19
    • 21444443226 scopus 로고    scopus 로고
    • Bax-dependent regulation of Bak by voltage-dependent anion channel 2
    • Chandra D., Choy G., Daniel P.T., Tang D.G. Bax-dependent regulation of Bak by voltage-dependent anion channel 2. J. Biol. Chem. 2005, 280:19051-19061.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19051-19061
    • Chandra, D.1    Choy, G.2    Daniel, P.T.3    Tang, D.G.4
  • 20
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • Chen M., He H., Zhan S., Krajewski S., Reed J.C., Gottlieb R.A. Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J. Biol. Chem. 2001, 276:30724-30728.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30724-30728
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 22
    • 77950510346 scopus 로고    scopus 로고
    • Phosphorylation by Nek1 regulates opening and closing of voltage dependent anion channel 1
    • Chen Y., Gaczynska M., Osmulski P., Polci R., Riley D.J. Phosphorylation by Nek1 regulates opening and closing of voltage dependent anion channel 1. Biochem. Biophys. Res. Commun. 2010, 394:798-803.
    • (2010) Biochem. Biophys. Res. Commun. , vol.394 , pp. 798-803
    • Chen, Y.1    Gaczynska, M.2    Osmulski, P.3    Polci, R.4    Riley, D.J.5
  • 28
    • 14244265108 scopus 로고    scopus 로고
    • Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands
    • Day C.L., Chen L., Richardson S.J., Harrison P.J., Huang D.C., Hinds M.G. Solution structure of prosurvival Mcl-1 and characterization of its binding by proapoptotic BH3-only ligands. J. Biol. Chem. 2005, 280:4738-4744.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4738-4744
    • Day, C.L.1    Chen, L.2    Richardson, S.J.3    Harrison, P.J.4    Huang, D.C.5    Hinds, M.G.6
  • 30
    • 0026519544 scopus 로고
    • Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC)
    • De Pinto V.D., Palmieri F. Transmembrane arrangement of mitochondrial porin or voltage-dependent anion channel (VDAC). J. Bioenerg. Biomembr. 1992, 24:21-26.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 21-26
    • De Pinto, V.D.1    Palmieri, F.2
  • 31
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO
    • Deng Y., Lin Y., Wu X. TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO. Genes Dev. 2002, 16:33-45.
    • (2002) Genes Dev. , vol.16 , pp. 33-45
    • Deng, Y.1    Lin, Y.2    Wu, X.3
  • 32
    • 0141953270 scopus 로고    scopus 로고
    • A JNK-dependent pathway is required for TNFalpha-induced apoptosis
    • Deng Y., Ren X., Yang L., Lin Y., Wu X. A JNK-dependent pathway is required for TNFalpha-induced apoptosis. Cell 2003, 115:61-70.
    • (2003) Cell , vol.115 , pp. 61-70
    • Deng, Y.1    Ren, X.2    Yang, L.3    Lin, Y.4    Wu, X.5
  • 34
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Deveraux Q.L., Reed J.C. IAP family proteins-suppressors of apoptosis. Genes Dev. 1999, 13:239-252.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 35
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C., Fang M., Li Y., Li L., Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000, 102:33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 37
    • 33746886979 scopus 로고    scopus 로고
    • Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
    • Fulda S., Debatin K.M. Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene 2006, 25:4798-4811.
    • (2006) Oncogene , vol.25 , pp. 4798-4811
    • Fulda, S.1    Debatin, K.M.2
  • 38
    • 0033758751 scopus 로고    scopus 로고
    • N-terminal cleavage of bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes bcl-2-independent cytochrome C release and apoptotic cell death
    • Gao G., Dou Q.P. N-terminal cleavage of bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes bcl-2-independent cytochrome C release and apoptotic cell death. J. Cell. Biochem. 2000, 80:53-72.
    • (2000) J. Cell. Biochem. , vol.80 , pp. 53-72
    • Gao, G.1    Dou, Q.P.2
  • 39
    • 0027346546 scopus 로고
    • The c-myc oncogene in tumor progression
    • Garte S.J. The c-myc oncogene in tumor progression. Crit. Rev. Oncog. 1993, 4:435-449.
    • (1993) Crit. Rev. Oncog. , vol.4 , pp. 435-449
    • Garte, S.J.1
  • 40
    • 34547629939 scopus 로고    scopus 로고
    • A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax
    • George N.M., Evans J.J., Luo X. A three-helix homo-oligomerization domain containing BH3 and BH1 is responsible for the apoptotic activity of Bax. Genes Dev. 2007, 21:1937-1948.
    • (2007) Genes Dev. , vol.21 , pp. 1937-1948
    • George, N.M.1    Evans, J.J.2    Luo, X.3
  • 41
  • 42
    • 68149154728 scopus 로고    scopus 로고
    • BH3-only proteins and their roles in programmed cell death
    • Giam M., Huang D.C., Bouillet P. BH3-only proteins and their roles in programmed cell death. Oncogene 2008, 27(Suppl 1):S128-S136.
    • (2008) Oncogene , vol.27 , Issue.SUPPL. 1
    • Giam, M.1    Huang, D.C.2    Bouillet, P.3
  • 43
    • 0034678367 scopus 로고    scopus 로고
    • Integrin-mediated survival signals regulate the apoptotic function of Bax through its conformation and subcellular localization
    • Gilmore A.P., Metcalfe A.D., Romer L.H., Streuli C.H. Integrin-mediated survival signals regulate the apoptotic function of Bax through its conformation and subcellular localization. J. Cell Biol. 2000, 149:431-446.
    • (2000) J. Cell Biol. , vol.149 , pp. 431-446
    • Gilmore, A.P.1    Metcalfe, A.D.2    Romer, L.H.3    Streuli, C.H.4
  • 44
    • 0035881510 scopus 로고    scopus 로고
    • Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function
    • Gincel D., Zaid H., Shoshan-Barmatz V. Calcium binding and translocation by the voltage-dependent anion channel: a possible regulatory mechanism in mitochondrial function. Biochem. J. 2001, 358:147-155.
    • (2001) Biochem. J. , vol.358 , pp. 147-155
    • Gincel, D.1    Zaid, H.2    Shoshan-Barmatz, V.3
  • 45
    • 9244260553 scopus 로고    scopus 로고
    • Kinetics of Smac/DIABLO release from mitochondria during apoptosis of MCF-7 breast cancer cells
    • Gorka M., Godlewski M.M., Gajkowska B., Wojewodzka U., Motyl T. Kinetics of Smac/DIABLO release from mitochondria during apoptosis of MCF-7 breast cancer cells. Cell Biol. Int. 2004, 28:741-754.
    • (2004) Cell Biol. Int. , vol.28 , pp. 741-754
    • Gorka, M.1    Godlewski, M.M.2    Gajkowska, B.3    Wojewodzka, U.4    Motyl, T.5
  • 46
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., Kroemer G. The pathophysiology of mitochondrial cell death. Science 2004, 305:626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 50
    • 0031008145 scopus 로고    scopus 로고
    • Role of the mitochondrial permeability transition pore in apoptosis
    • Hirsch T., Marzo I., Kroemer G. Role of the mitochondrial permeability transition pore in apoptosis. Biosci. Rep. 1997, 17:67-76.
    • (1997) Biosci. Rep. , vol.17 , pp. 67-76
    • Hirsch, T.1    Marzo, I.2    Kroemer, G.3
  • 54
    • 0037379739 scopus 로고    scopus 로고
    • Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: differential regulation of cytochrome c and Smac/DIABLO release
    • Kandasamy K., Srinivasula S.M., Alnemri E.S., Thompson C.B., Korsmeyer S.J., Bryant J.L., Srivastava R.K. Involvement of proapoptotic molecules Bax and Bak in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced mitochondrial disruption and apoptosis: differential regulation of cytochrome c and Smac/DIABLO release. Cancer Res. 2003, 63:1712-1721.
    • (2003) Cancer Res. , vol.63 , pp. 1712-1721
    • Kandasamy, K.1    Srinivasula, S.M.2    Alnemri, E.S.3    Thompson, C.B.4    Korsmeyer, S.J.5    Bryant, J.L.6    Srivastava, R.K.7
  • 56
    • 0032146987 scopus 로고    scopus 로고
    • Bcl-2-family proteins: the role of the BH3 domain in apoptosis
    • Kelekar A., Thompson C.B. 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
  • 57
    • 33746379603 scopus 로고    scopus 로고
    • JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells
    • Kim B.J., Ryu S.W., Song B.J. JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells. J. Biol. Chem. 2006, 281:21256-21265.
    • (2006) J. Biol. Chem. , vol.281 , pp. 21256-21265
    • Kim, B.J.1    Ryu, S.W.2    Song, B.J.3
  • 60
    • 60249089101 scopus 로고    scopus 로고
    • Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them?
    • Kumarswamy R., Chandna S. Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them?. Mitochondrion 2009, 9:1-8.
    • (2009) Mitochondrion , vol.9 , pp. 1-8
    • Kumarswamy, R.1    Chandna, S.2
  • 64
    • 0032493935 scopus 로고    scopus 로고
    • 2+ homeostasis in the agonist-sensitive internal store: functional interactions between mitochondria and the ER measured In situ in intact cells
    • 2+ homeostasis in the agonist-sensitive internal store: functional interactions between mitochondria and the ER measured In situ in intact cells. J. Cell Biol. 1998, 142:1235-1243.
    • (1998) J. Cell Biol. , vol.142 , pp. 1235-1243
    • Landolfi, B.1    Curci, S.2    Debellis, L.3    Pozzan, T.4    Hofer, A.M.5
  • 65
    • 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 C.J., 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
  • 66
    • 33645220247 scopus 로고    scopus 로고
    • Relative timing of redistribution of cytochrome c and Smac/DIABLO from mitochondria during apoptosis assessed by double immunocytochemistry on mammalian cells
    • Lim M.L., Chen B., Beart P.M., Nagley P. Relative timing of redistribution of cytochrome c and Smac/DIABLO from mitochondria during apoptosis assessed by double immunocytochemistry on mammalian cells. Exp. Cell Res. 2006, 312:1174-1184.
    • (2006) Exp. Cell Res. , vol.312 , pp. 1174-1184
    • Lim, M.L.1    Chen, B.2    Beart, P.M.3    Nagley, P.4
  • 67
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c
    • Liu X., Kim C.N., Yang J., Jemmerson R., Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996, 86:147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 68
    • 77954516857 scopus 로고    scopus 로고
    • Dominant-negative VDAC1 mutants reveal oligomeric VDAC1 to be the active unit in mitochondria-mediated apoptosis
    • Mader A., Abu-Hamad S., Arbel N., Gutierr-Asuilar M., Shoshan-Barmatz V. Dominant-negative VDAC1 mutants reveal oligomeric VDAC1 to be the active unit in mitochondria-mediated apoptosis. Biochem. J. 2010, 429:147-155.
    • (2010) Biochem. J. , vol.429 , pp. 147-155
    • Mader, A.1    Abu-Hamad, S.2    Arbel, N.3    Gutierr-Asuilar, M.4    Shoshan-Barmatz, V.5
  • 69
    • 33748037685 scopus 로고    scopus 로고
    • Molecular dynamics simulation and automated docking of the pro-apoptotic Bax protein and its complex with a peptide designed from the Bax-binding domain of anti-apoptotic Ku70
    • Mancinelli F., Caraglia M., Budillon A., Abbruzzese A., Bismuto E. Molecular dynamics simulation and automated docking of the pro-apoptotic Bax protein and its complex with a peptide designed from the Bax-binding domain of anti-apoptotic Ku70. J. Cell. Biochem. 2006, 99:305-318.
    • (2006) J. Cell. Biochem. , vol.99 , pp. 305-318
    • Mancinelli, F.1    Caraglia, M.2    Budillon, A.3    Abbruzzese, A.4    Bismuto, E.5
  • 70
    • 0036236471 scopus 로고    scopus 로고
    • Calpain-mediated Bid cleavage and calpain-independent Bak modulation: two separate pathways in cisplatin-induced apoptosis
    • Mandic A., Viktorsson K., Strandberg L., Heiden T., Hansson J., Linder S., Shoshan M.C. Calpain-mediated Bid cleavage and calpain-independent Bak modulation: two separate pathways in cisplatin-induced apoptosis. Mol. Cell. Biol. 2002, 22:3003-3013.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3003-3013
    • Mandic, A.1    Viktorsson, K.2    Strandberg, L.3    Heiden, T.4    Hansson, J.5    Linder, S.6    Shoshan, M.C.7
  • 74
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M., Shimizu S., Ito T., Chittenden T., Lutz R.J., Matsuda H., Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc. Natl. Acad. Sci. USA 1998, 95:14681-14686.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 75
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A., Smith C.L., Hsu Y.T., Youle R.J. 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
  • 76
    • 47249135572 scopus 로고    scopus 로고
    • Cysteine 62 of Bax is critical for its conformational activation and its proapoptotic activity in response to H2O2-induced apoptosis
    • Nie C., Tian C., Zhao L., Petit P.X., Mehrpour M., Chen Q. Cysteine 62 of Bax is critical for its conformational activation and its proapoptotic activity in response to H2O2-induced apoptosis. J. Biol. Chem. 2008, 283:15359-15369.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15359-15369
    • Nie, C.1    Tian, C.2    Zhao, L.3    Petit, P.X.4    Mehrpour, M.5    Chen, Q.6
  • 78
    • 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. 2010, 396:95-100.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 95-100
    • Norberg, E.1    Orrenius, S.2    Zhivotovsky, B.3
  • 82
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai Z.N., Milliman C.L., Korsmeyer S.J. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 1993, 74:609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 85
    • 0033615649 scopus 로고    scopus 로고
    • Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore
    • Pastorino J.G., Tafani M., Rothman R.J., Marcinkeviciute A., Hoek J.B., Farber J.L. Functional consequences of the sustained or transient activation by Bax of the mitochondrial permeability transition pore. J. Biol. Chem. 1999, 274:31734-31739.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31734-31739
    • Pastorino, J.G.1    Tafani, M.2    Rothman, R.J.3    Marcinkeviciute, A.4    Hoek, J.B.5    Farber, J.L.6
  • 86
    • 34250768073 scopus 로고    scopus 로고
    • A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis
    • Pellegrini L., Scorrano L. A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis. Cell Death Differ. 2007, 14:1275-1284.
    • (2007) Cell Death Differ. , vol.14 , pp. 1275-1284
    • Pellegrini, L.1    Scorrano, L.2
  • 87
    • 77955291571 scopus 로고    scopus 로고
    • Oxidative stress caused by mitochondrial calcium overload
    • Peng T.I., Jou M.J. Oxidative stress caused by mitochondrial calcium overload. Ann. NY Acad. Sci. 2010, 1201:183-188.
    • (2010) Ann. NY Acad. Sci. , vol.1201 , pp. 183-188
    • Peng, T.I.1    Jou, M.J.2
  • 91
    • 0141768255 scopus 로고    scopus 로고
    • Real-time single cell analysis of Smac/DIABLO release during apoptosis
    • Rehm M., Dussmann H., Prehn J.H. Real-time single cell analysis of Smac/DIABLO release during apoptosis. J. Cell Biol. 2003, 162:1031-1043.
    • (2003) J. Cell Biol. , vol.162 , pp. 1031-1043
    • Rehm, M.1    Dussmann, H.2    Prehn, J.H.3
  • 93
    • 67349156098 scopus 로고    scopus 로고
    • Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1, 4, 5-trisphosphate receptor
    • Rong Y.P., Barr P., Yee V.C., Distelhorst C.W. Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1, 4, 5-trisphosphate receptor. Biochim. Biophys. Acta 2009, 1793:971-978.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 971-978
    • Rong, Y.P.1    Barr, P.2    Yee, V.C.3    Distelhorst, C.W.4
  • 94
    • 33747884339 scopus 로고    scopus 로고
    • DNA damage-induced cell death by apoptosis
    • Roos W.P., Kaina B. DNA damage-induced cell death by apoptosis. Trends Mol. Med. 2006, 12:440-450.
    • (2006) Trends Mol. Med. , vol.12 , pp. 440-450
    • Roos, W.P.1    Kaina, B.2
  • 99
    • 0030724539 scopus 로고    scopus 로고
    • Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition
    • Scarlett J.L., Murphy M.P. Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition. FEBS Lett. 1997, 418:282-286.
    • (1997) FEBS Lett. , vol.418 , pp. 282-286
    • Scarlett, J.L.1    Murphy, M.P.2
  • 100
    • 69249114710 scopus 로고    scopus 로고
    • Involvement of VDAC, Bax and ceramides in the efflux of AIF from mitochondria during curcumin-induced apoptosis
    • Scharstuhl A., Mutsaers H.A., Pennings S.W., Russel F.G., Wagener F.A. Involvement of VDAC, Bax and ceramides in the efflux of AIF from mitochondria during curcumin-induced apoptosis. PLoS ONE 2009, 4:e6688.
    • (2009) PLoS ONE , vol.4
    • Scharstuhl, A.1    Mutsaers, H.A.2    Pennings, S.W.3    Russel, F.G.4    Wagener, F.A.5
  • 103
    • 78149360191 scopus 로고    scopus 로고
    • Mitochondrial fission and fusion
    • Scott I., Youle R.J. Mitochondrial fission and fusion. Essays Biochem. 2010, 47:85-98.
    • (2010) Essays Biochem. , vol.47 , pp. 85-98
    • Scott, I.1    Youle, R.J.2
  • 104
    • 49349105966 scopus 로고    scopus 로고
    • Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release
    • Sheridan C., Delivani P., Cullen S.P., Martin S.J. Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release. Mol. Cell 2008, 31:570-585.
    • (2008) Mol. Cell , vol.31 , pp. 570-585
    • Sheridan, C.1    Delivani, P.2    Cullen, S.P.3    Martin, S.J.4
  • 105
    • 0031550232 scopus 로고    scopus 로고
    • Rapid loss in the mitochondrial membrane potential during geranylgeranoic acid-induced apoptosis
    • Shidoji Y., Nakamura N., Moriwaki H., Muto Y. Rapid loss in the mitochondrial membrane potential during geranylgeranoic acid-induced apoptosis. Biochem. Biophys. Res. Commun. 1997, 230:58-63.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 58-63
    • Shidoji, Y.1    Nakamura, N.2    Moriwaki, H.3    Muto, Y.4
  • 106
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S., Konishi A., Kodama T., Tsujimoto Y. BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc. Natl. Acad. Sci. USA 2000, 97:3100-3105.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 107
    • 77953812826 scopus 로고    scopus 로고
    • Apoptosis is regulated by the VDAC1 N-terminal region and by VDAC oligomerization: release of cytochrome c, AIF and Smac/Diablo
    • Shoshan-Barmatz V., Keinan N., Abu-Hamad S., Tyomkin D., Aram L. Apoptosis is regulated by the VDAC1 N-terminal region and by VDAC oligomerization: release of cytochrome c, AIF and Smac/Diablo. Biochim. Biophys. Acta 2010, 1797:1281-1291.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1281-1291
    • Shoshan-Barmatz, V.1    Keinan, N.2    Abu-Hamad, S.3    Tyomkin, D.4    Aram, L.5
  • 109
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • Suen D.F., Norris K.L., Youle R.J. Mitochondrial dynamics and apoptosis. Genes Dev. 2008, 22:1577-1590.
    • (2008) Genes Dev. , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 110
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: coregulation of dimer formation and intracellular localization
    • Suzuki M., Youle R.J., Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 2000, 103:645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 111
    • 0026550587 scopus 로고
    • The mitochondrial megachannel is the permeability transition pore
    • Szabo I., Zoratti M. The mitochondrial megachannel is the permeability transition pore. J. Bioenerg. Biomembr. 1992, 24:111-117.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 111-117
    • Szabo, I.1    Zoratti, M.2
  • 112
    • 0037469097 scopus 로고    scopus 로고
    • Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax
    • Toyota H., Yanase N., Yoshimoto T., Moriyama M., Sudo T., Mizuguchi J. Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax. Cancer Lett. 2003, 189:221-230.
    • (2003) Cancer Lett. , vol.189 , pp. 221-230
    • Toyota, H.1    Yanase, N.2    Yoshimoto, T.3    Moriyama, M.4    Sudo, T.5    Mizuguchi, J.6
  • 114
    • 34247354978 scopus 로고    scopus 로고
    • The N-terminal conformation of Bax regulates cell commitment to apoptosis
    • Upton J.P., Valentijn A.J., Zhang L., Gilmore A.P. The N-terminal conformation of Bax regulates cell commitment to apoptosis. Cell Death Differ. 2007, 14:932-942.
    • (2007) Cell Death Differ. , vol.14 , pp. 932-942
    • Upton, J.P.1    Valentijn, A.J.2    Zhang, L.3    Gilmore, A.P.4
  • 115
    • 0036676976 scopus 로고    scopus 로고
    • Promotion of photodynamic therapy-induced apoptosis by the mitochondrial protein Smac/DIABLO: dependence on Bax
    • Usuda J., Chiu S.M., Azizuddin K., Xue L.Y., Lam M., Nieminen A.L., Oleinick N.L. Promotion of photodynamic therapy-induced apoptosis by the mitochondrial protein Smac/DIABLO: dependence on Bax. Photochem. Photobiol. 2002, 76:217-223.
    • (2002) Photochem. Photobiol. , vol.76 , pp. 217-223
    • Usuda, J.1    Chiu, S.M.2    Azizuddin, K.3    Xue, L.Y.4    Lam, M.5    Nieminen, A.L.6    Oleinick, N.L.7
  • 116
    • 3543038162 scopus 로고    scopus 로고
    • Translocation of full-length Bid to mitochondria during anoikis
    • Valentijn A.J., Gilmore A.P. Translocation of full-length Bid to mitochondria during anoikis. J. Biol. Chem. 2004, 279:32848-32857.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32848-32857
    • Valentijn, A.J.1    Gilmore, A.P.2
  • 119
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signaling pathway: more than a paradigm
    • Wajant H. The Fas signaling pathway: more than a paradigm. Science 2002, 296:1635-1636.
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 120
    • 78650169392 scopus 로고    scopus 로고
    • Bcl-2 proteins regulate ER membrane permeability to luminal proteins during ER stress-induced apoptosis
    • doi:10.1038/cdd.2010.68
    • Wang X., Olberding K.E., White C., Li C. Bcl-2 proteins regulate ER membrane permeability to luminal proteins during ER stress-induced apoptosis. Cell Death Differ. 2010, doi:10.1038/cdd.2010.68.
    • (2010) Cell Death Differ.
    • Wang, X.1    Olberding, K.E.2    White, C.3    Li, C.4
  • 121
    • 22244464818 scopus 로고    scopus 로고
    • Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins
    • Willis S.N., Chen L., Dewson G., Wei A., Naik E., Fletcher J.I., Adams J.M., Huang D.C. Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 2005, 19:1294-1305.
    • (2005) Genes Dev. , vol.19 , pp. 1294-1305
    • Willis, S.N.1    Chen, L.2    Dewson, G.3    Wei, A.4    Naik, E.5    Fletcher, J.I.6    Adams, J.M.7    Huang, D.C.8
  • 122
    • 74549206782 scopus 로고    scopus 로고
    • Degradation of phospholipids by oxidative stress-exceptional significance of cardiolipin
    • Wiswedel I., Gardemann A., Storch A., Peter D., Schild L. Degradation of phospholipids by oxidative stress-exceptional significance of cardiolipin. Free Radic. Res. 2010, 44:135-145.
    • (2010) Free Radic. Res. , vol.44 , pp. 135-145
    • Wiswedel, I.1    Gardemann, A.2    Storch, A.3    Peter, D.4    Schild, L.5
  • 124
    • 15444371092 scopus 로고    scopus 로고
    • Nicotine inactivation of the proapoptotic function of Bax through phosphorylation
    • Xin M., Deng X. Nicotine inactivation of the proapoptotic function of Bax through phosphorylation. J. Biol. Chem. 2005, 280:10781-10789.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10781-10789
    • Xin, M.1    Deng, X.2
  • 125
    • 33745812349 scopus 로고    scopus 로고
    • Protein phosphatase 2A enhances the proapoptotic function of Bax through dephosphorylation
    • Xin M., Deng X. Protein phosphatase 2A enhances the proapoptotic function of Bax through dephosphorylation. J. Biol. Chem. 2006, 281:18859-18867.
    • (2006) J. Biol. Chem. , vol.281 , pp. 18859-18867
    • Xin, M.1    Deng, X.2
  • 126
    • 34547101741 scopus 로고    scopus 로고
    • Protein kinase Czeta abrogates the proapoptotic function of Bax through phosphorylation
    • Xin M., Gao F., May W.S., Flagg T., Deng X. Protein kinase Czeta abrogates the proapoptotic function of Bax through phosphorylation. J. Biol. Chem. 2007, 282:21268-21277.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21268-21277
    • Xin, M.1    Gao, F.2    May, W.S.3    Flagg, T.4    Deng, X.5
  • 127
    • 67649389595 scopus 로고    scopus 로고
    • Dynamics of mitochondrial structure during apoptosis and the enigma of Opa1
    • Yamaguchi R., Perkins G. Dynamics of mitochondrial structure during apoptosis and the enigma of Opa1. Biochim. Biophys. Acta 2009, 1787:963-972.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 963-972
    • Yamaguchi, R.1    Perkins, G.2
  • 129
    • 0034278085 scopus 로고    scopus 로고
    • The IAP family: endogenous caspase inhibitors with multiple biological activities
    • Yang Y.L., Li X.M. The IAP family: endogenous caspase inhibitors with multiple biological activities. Cell Res. 2000, 10:169-177.
    • (2000) Cell Res. , vol.10 , pp. 169-177
    • Yang, Y.L.1    Li, X.M.2
  • 133
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H., Henzel W.J., Liu X., Lutschg A., Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997, 90:405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


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