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Volumn 22, Issue 6, 2012, Pages 318-328

Multipolar functions of BCL-2 proteins link energetics to apoptosis

Author keywords

Apoptosis; Bcl 2; Bcl x L; Energetics.; Inner mitochondrial membrane; Mitochondria

Indexed keywords

BH3 PROTEIN; CYTOCHROME C; DIPHTHERIA TOXIN; PROTEIN BCL 2;

EID: 84861777075     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.03.005     Document Type: Review
Times cited : (89)

References (120)
  • 1
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: opposing activities that mediate cell death
    • Youle R.J., Strasser A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 2008, 9:47-59.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 2
    • 0034975774 scopus 로고    scopus 로고
    • Mouse models of cell death
    • Ranger A.M., et al. Mouse models of cell death. Nat. Genet. 2001, 28:113-118.
    • (2001) Nat. Genet. , vol.28 , pp. 113-118
    • Ranger, A.M.1
  • 3
    • 82255192310 scopus 로고    scopus 로고
    • Pretreatment mitochondrial priming correlates with clinical response to cytotoxic chemotherapy
    • Ni Chonghaile T., et al. Pretreatment mitochondrial priming correlates with clinical response to cytotoxic chemotherapy. Science 2011, 334:1129-1133.
    • (2011) Science , vol.334 , pp. 1129-1133
    • Ni Chonghaile, T.1
  • 4
    • 79952291173 scopus 로고    scopus 로고
    • Phase I study of Navitoclax (ABT-263), a novel Bcl-2 family inhibitor, in patients with small-cell lung cancer and other solid tumors
    • Gandhi L., et al. Phase I study of Navitoclax (ABT-263), a novel Bcl-2 family inhibitor, in patients with small-cell lung cancer and other solid tumors. J. Clin. Oncol. 2011, 29:909-916.
    • (2011) J. Clin. Oncol. , vol.29 , pp. 909-916
    • Gandhi, L.1
  • 5
    • 77957141008 scopus 로고    scopus 로고
    • Still embedded together binding to membranes regulates Bcl-2 protein interactions
    • Leber B., et al. Still embedded together binding to membranes regulates Bcl-2 protein interactions. Oncogene 2010, 29:5221-5230.
    • (2010) Oncogene , vol.29 , pp. 5221-5230
    • Leber, B.1
  • 6
    • 0033258120 scopus 로고    scopus 로고
    • Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?
    • Vander Heiden M.G., Thompson C.B. Bcl-2 proteins: regulators of apoptosis or of mitochondrial homeostasis?. Nat. Cell Biol. 1999, 1:E209-E216.
    • (1999) Nat. Cell Biol. , vol.1
    • Vander Heiden, M.G.1    Thompson, C.B.2
  • 7
    • 64749114270 scopus 로고    scopus 로고
    • Bcl-x L increases mitochondrial fission, fusion, and biomass in neurons
    • Berman S.B., et al. Bcl-x L increases mitochondrial fission, fusion, and biomass in neurons. J. Cell Biol. 2009, 184:707-719.
    • (2009) J. Cell Biol. , vol.184 , pp. 707-719
    • Berman, S.B.1
  • 9
    • 80051970600 scopus 로고    scopus 로고
    • Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival
    • Yi C.H., et al. Metabolic regulation of protein N-alpha-acetylation by Bcl-xL promotes cell survival. Cell 2011, 146:607-620.
    • (2011) Cell , vol.146 , pp. 607-620
    • Yi, C.H.1
  • 10
    • 0037418843 scopus 로고    scopus 로고
    • 2+: a control point for apoptosis
    • 2+: a control point for apoptosis. Science 2003, 300:135-139.
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1
  • 11
    • 77958124651 scopus 로고    scopus 로고
    • Homeostatic functions of BCL-2 proteins beyond apoptosis
    • Danial N.N., et al. Homeostatic functions of BCL-2 proteins beyond apoptosis. Adv. Exp. Med. Biol. 2010, 687:1-32.
    • (2010) Adv. Exp. Med. Biol. , vol.687 , pp. 1-32
    • Danial, N.N.1
  • 12
    • 0000906170 scopus 로고    scopus 로고
    • Induction of autophagy and inhibition of tumorigenesis by beclin 1
    • Liang X.H., et al. Induction of autophagy and inhibition of tumorigenesis by beclin 1. Nature 1999, 402:672-676.
    • (1999) Nature , vol.402 , pp. 672-676
    • Liang, X.H.1
  • 13
    • 0347091260 scopus 로고    scopus 로고
    • BAK alters neuronal excitability and can switch from anti- to pro-death function during postnatal development
    • Fannjiang Y., et al. BAK alters neuronal excitability and can switch from anti- to pro-death function during postnatal development. Dev. Cell 2003, 4:575-585.
    • (2003) Dev. Cell , vol.4 , pp. 575-585
    • Fannjiang, Y.1
  • 14
    • 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
  • 15
    • 78650679999 scopus 로고    scopus 로고
    • An evolving NGF-Hoxd1 signaling pathway mediates development of divergent neural circuits in vertebrates
    • Guo T., et al. An evolving NGF-Hoxd1 signaling pathway mediates development of divergent neural circuits in vertebrates. Nat. Neurosci. 2011, 14:31-36.
    • (2011) Nat. Neurosci. , vol.14 , pp. 31-36
    • Guo, T.1
  • 16
    • 24144493694 scopus 로고    scopus 로고
    • Actions of BAX on mitochondrial channel activity and on synaptic transmission
    • Jonas E.A., et al. Actions of BAX on mitochondrial channel activity and on synaptic transmission. Antioxid. Redox Signal. 2005, 7:1092-1100.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 1092-1100
    • Jonas, E.A.1
  • 17
    • 84055212651 scopus 로고    scopus 로고
    • Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back?
    • Beverly L.J. Regulation of anti-apoptotic BCL2-proteins by non-canonical interactions: the next step forward or two steps back?. J. Cell. Biochem. 2012, 113:3-12.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 3-12
    • Beverly, L.J.1
  • 18
    • 27944470616 scopus 로고    scopus 로고
    • Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators
    • Aouacheria A., et al. Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators. Mol. Biol. Evol. 2005, 22:2395-2416.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 2395-2416
    • Aouacheria, A.1
  • 19
    • 79952709680 scopus 로고    scopus 로고
    • Molecular biology of Bax and Bak activation and action
    • Westphal D., et al. Molecular biology of Bax and Bak activation and action. Biochim. Biophys. Acta 2011, 1813:521-531.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 521-531
    • Westphal, D.1
  • 20
    • 77955717344 scopus 로고    scopus 로고
    • The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins
    • Lasi M., et al. The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins. Cell Res. 2010, 20:812-825.
    • (2010) Cell Res. , vol.20 , pp. 812-825
    • Lasi, M.1
  • 21
    • 42949148784 scopus 로고    scopus 로고
    • Surprising complexity of the ancestral apoptosis network
    • Zmasek C.M., et al. Surprising complexity of the ancestral apoptosis network. Genome Biol. 2007, 8:R226.
    • (2007) Genome Biol. , vol.8
    • Zmasek, C.M.1
  • 22
    • 32044465724 scopus 로고    scopus 로고
    • A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin
    • Ellermeier C.D., et al. A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin. Cell 2006, 124:549-559.
    • (2006) Cell , vol.124 , pp. 549-559
    • Ellermeier, C.D.1
  • 23
    • 80052313694 scopus 로고    scopus 로고
    • Gene-dependent cell death in yeast
    • Teng X., et al. Gene-dependent cell death in yeast. Cell Death Dis. 2011, 2:e188.
    • (2011) Cell Death Dis. , vol.2
    • Teng, X.1
  • 24
    • 52149113769 scopus 로고    scopus 로고
    • Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands
    • Kvansakul M., et al. Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands. Cell Death Differ. 2008, 15:1564-1571.
    • (2008) Cell Death Differ. , vol.15 , pp. 1564-1571
    • Kvansakul, M.1
  • 25
    • 0036171149 scopus 로고    scopus 로고
    • Epstein-Barr virus BALF1 is a BCL-2-like antagonist of the herpesvirus antiapoptotic BCL-2 proteins
    • Bellows D.S., et al. Epstein-Barr virus BALF1 is a BCL-2-like antagonist of the herpesvirus antiapoptotic BCL-2 proteins. J. Virol. 2002, 76:2469-2479.
    • (2002) J. Virol. , vol.76 , pp. 2469-2479
    • Bellows, D.S.1
  • 26
    • 50849109845 scopus 로고    scopus 로고
    • Vaccinia virus proteins A52 and B14 share a Bcl-2-like fold but have evolved to inhibit NF-kappaB rather than apoptosis
    • Graham S.C., et al. Vaccinia virus proteins A52 and B14 share a Bcl-2-like fold but have evolved to inhibit NF-kappaB rather than apoptosis. PLoS Pathog. 2008, 4:e1000128.
    • (2008) PLoS Pathog. , vol.4
    • Graham, S.C.1
  • 27
    • 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
  • 28
    • 79953236969 scopus 로고    scopus 로고
    • Mechanism of Diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process
    • Murphy J.R. Mechanism of Diphtheria toxin catalytic domain delivery to the eukaryotic cell cytosol and the cellular factors that directly participate in the process. Toxins (Basel) 2011, 3:294-308.
    • (2011) Toxins (Basel) , vol.3 , pp. 294-308
    • Murphy, J.R.1
  • 29
    • 33845486323 scopus 로고    scopus 로고
    • Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets
    • Hinds M.G., et al. Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death Differ. 2007, 14:128-136.
    • (2007) Cell Death Differ. , vol.14 , pp. 128-136
    • Hinds, M.G.1
  • 30
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S., et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005, 122:927-939.
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1
  • 31
    • 83455225635 scopus 로고    scopus 로고
    • The autophagy protein Atg12 associates with antiapoptotic Bcl-2 family members to promote mitochondrial apoptosis
    • Rubinstein A.D., et al. The autophagy protein Atg12 associates with antiapoptotic Bcl-2 family members to promote mitochondrial apoptosis. Mol. Cell 2011, 44:698-709.
    • (2011) Mol. Cell , vol.44 , pp. 698-709
    • Rubinstein, A.D.1
  • 32
    • 84862777560 scopus 로고    scopus 로고
    • Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein
    • Huang W., et al. Crystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein. Cell Res. 2012, 22:473-489.
    • (2012) Cell Res. , vol.22 , pp. 473-489
    • Huang, W.1
  • 33
    • 80355146535 scopus 로고    scopus 로고
    • Bcl-xL regulates mitochondrial energetics by stabilizing the inner membrane potential
    • Chen Y.B., et al. Bcl-xL regulates mitochondrial energetics by stabilizing the inner membrane potential. J. Cell Biol. 2011, 195:263-276.
    • (2011) J. Cell Biol. , vol.195 , pp. 263-276
    • Chen, Y.B.1
  • 34
    • 80053560844 scopus 로고    scopus 로고
    • Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase
    • Alavian K.N., et al. Bcl-xL regulates metabolic efficiency of neurons through interaction with the mitochondrial F1FO ATP synthase. Nat. Cell Biol. 2011, 13:1224-1233.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1224-1233
    • Alavian, K.N.1
  • 35
    • 73349128117 scopus 로고    scopus 로고
    • Genetic control of programmed cell death during animal development
    • Conradt B. Genetic control of programmed cell death during animal development. Annu. Rev. Genet. 2009, 43:493-523.
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 493-523
    • Conradt, B.1
  • 36
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan N., et al. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 2005, 437:831-837.
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1
  • 37
    • 4644249309 scopus 로고    scopus 로고
    • Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4
    • Yan N., et al. Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4. Mol. Cell 2004, 15:999-1006.
    • (2004) Mol. Cell , vol.15 , pp. 999-1006
    • Yan, N.1
  • 38
    • 0033635266 scopus 로고    scopus 로고
    • Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1
    • Chau B.N., et al. Aven, a novel inhibitor of caspase activation, binds Bcl-xL and Apaf-1. Mol. Cell 2000, 6:31-40.
    • (2000) Mol. Cell , vol.6 , pp. 31-40
    • Chau, B.N.1
  • 39
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia R., et al. DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans. Nature 2005, 433:754-760.
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1
  • 40
    • 69449104405 scopus 로고    scopus 로고
    • The BCL-2-like protein CED-9 of C. elegans promotes FZO-1/Mfn1,2- and EAT-3/Opa1-dependent mitochondrial fusion
    • Rolland S.G., et al. The BCL-2-like protein CED-9 of C. elegans promotes FZO-1/Mfn1,2- and EAT-3/Opa1-dependent mitochondrial fusion. J. Cell Biol. 2009, 186:525-540.
    • (2009) J. Cell Biol. , vol.186 , pp. 525-540
    • Rolland, S.G.1
  • 41
    • 80054765894 scopus 로고    scopus 로고
    • A molecular switch that governs mitochondrial fusion and fission mediated by the BCL2-like protein CED-9 of Caenorhabditis elegans
    • Lu Y., et al. A molecular switch that governs mitochondrial fusion and fission mediated by the BCL2-like protein CED-9 of Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:E813-E822.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Lu, Y.1
  • 42
    • 41149111891 scopus 로고    scopus 로고
    • Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal neurons
    • Li H., et al. Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal neurons. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:2169-2174.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2169-2174
    • Li, H.1
  • 43
    • 78651468702 scopus 로고    scopus 로고
    • The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes
    • Hoppins S., et al. The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes. Mol. Cell 2011, 41:150-160.
    • (2011) Mol. Cell , vol.41 , pp. 150-160
    • Hoppins, S.1
  • 44
    • 33749846225 scopus 로고    scopus 로고
    • Role of Bax and Bak in mitochondrial morphogenesis
    • Karbowski M., et al. Role of Bax and Bak in mitochondrial morphogenesis. Nature 2006, 443:658-662.
    • (2006) Nature , vol.443 , pp. 658-662
    • Karbowski, M.1
  • 45
    • 79960621726 scopus 로고    scopus 로고
    • Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission
    • Zhao J., et al. Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission. EMBO J. 2011, 30:2762-2778.
    • (2011) EMBO J. , vol.30 , pp. 2762-2778
    • Zhao, J.1
  • 46
    • 34447323097 scopus 로고    scopus 로고
    • Drosophila Omi, a mitochondrial-localized IAP antagonist and proapoptotic serine protease
    • Challa M., et al. Drosophila Omi, a mitochondrial-localized IAP antagonist and proapoptotic serine protease. EMBO J. 2007, 26:3144-3156.
    • (2007) EMBO J. , vol.26 , pp. 3144-3156
    • Challa, M.1
  • 47
    • 34247564610 scopus 로고    scopus 로고
    • Mitochondrial disruption in Drosophila apoptosis
    • Abdelwahid E., et al. Mitochondrial disruption in Drosophila apoptosis. Dev. Cell 2007, 12:793-806.
    • (2007) Dev. Cell , vol.12 , pp. 793-806
    • Abdelwahid, E.1
  • 48
    • 79952740220 scopus 로고    scopus 로고
    • Mitochondrial involvement in cell death of non-mammalian eukaryotes
    • Abdelwahid E., et al. Mitochondrial involvement in cell death of non-mammalian eukaryotes. Biochim. Biophys. Acta 2011, 1813:597-607.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 597-607
    • Abdelwahid, E.1
  • 49
    • 67249131118 scopus 로고    scopus 로고
    • A lepidopteran orthologue of reaper reveals functional conservation and evolution of IAP antagonists
    • Bryant B., et al. A lepidopteran orthologue of reaper reveals functional conservation and evolution of IAP antagonists. Insect Mol. Biol. 2009, 18:341-351.
    • (2009) Insect Mol. Biol. , vol.18 , pp. 341-351
    • Bryant, B.1
  • 50
    • 33749521656 scopus 로고    scopus 로고
    • Cytochrome c-d regulates developmental apoptosis in the Drosophila retina
    • Mendes C.S., et al. Cytochrome c-d regulates developmental apoptosis in the Drosophila retina. EMBO Rep. 2006, 7:933-939.
    • (2006) EMBO Rep. , vol.7 , pp. 933-939
    • Mendes, C.S.1
  • 51
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • Arama E., et al. Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev. Cell 2003, 4:687-697.
    • (2003) Dev. Cell , vol.4 , pp. 687-697
    • Arama, E.1
  • 52
    • 30444448684 scopus 로고    scopus 로고
    • The two Drosophila cytochrome C proteins can function in both respiration and caspase activation
    • Arama E., et al. The two Drosophila cytochrome C proteins can function in both respiration and caspase activation. EMBO J. 2006, 25:232-243.
    • (2006) EMBO J. , vol.25 , pp. 232-243
    • Arama, E.1
  • 53
    • 21144451097 scopus 로고    scopus 로고
    • Specific ablation of the apoptotic functions of cytochrome C reveals a differential requirement for cytochrome C and Apaf-1 in apoptosis
    • Hao Z., et al. Specific ablation of the apoptotic functions of cytochrome C reveals a differential requirement for cytochrome C and Apaf-1 in apoptosis. Cell 2005, 121:579-591.
    • (2005) Cell , vol.121 , pp. 579-591
    • Hao, Z.1
  • 54
    • 0041813273 scopus 로고    scopus 로고
    • Buffy, a Drosophila Bcl-2 protein, has anti-apoptotic and cell cycle inhibitory functions
    • Quinn L., et al. Buffy, a Drosophila Bcl-2 protein, has anti-apoptotic and cell cycle inhibitory functions. EMBO J. 2003, 22:3568-3579.
    • (2003) EMBO J. , vol.22 , pp. 3568-3579
    • Quinn, L.1
  • 55
    • 0028922885 scopus 로고
    • Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice
    • Motoyama N., et al. Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice. Science 1995, 267:1506-1510.
    • (1995) Science , vol.267 , pp. 1506-1510
    • Motoyama, N.1
  • 56
    • 0033954132 scopus 로고    scopus 로고
    • Mcl-1 deficiency results in peri-implantation embryonic lethality
    • Rinkenberger J.L., et al. Mcl-1 deficiency results in peri-implantation embryonic lethality. Genes Dev. 2000, 14:23-27.
    • (2000) Genes Dev. , vol.14 , pp. 23-27
    • Rinkenberger, J.L.1
  • 57
    • 0026582702 scopus 로고
    • Caenorhabditis elegans gene ced-9 protects cells from programmed cell death
    • Hengartner M.O., et al. Caenorhabditis elegans gene ced-9 protects cells from programmed cell death. Nature 1992, 356:494-499.
    • (1992) Nature , vol.356 , pp. 494-499
    • Hengartner, M.O.1
  • 58
    • 34247599253 scopus 로고    scopus 로고
    • Drosophila Bcl-2 proteins participate in stress-induced apoptosis, but are not required for normal development
    • Sevrioukov E.A., et al. Drosophila Bcl-2 proteins participate in stress-induced apoptosis, but are not required for normal development. Genesis 2007, 45:184-193.
    • (2007) Genesis , vol.45 , pp. 184-193
    • Sevrioukov, E.A.1
  • 59
    • 62349085960 scopus 로고    scopus 로고
    • The Bax/Bak ortholog in Drosophila, Debcl, exerts limited control over programmed cell death
    • Galindo K.A., et al. The Bax/Bak ortholog in Drosophila, Debcl, exerts limited control over programmed cell death. Development (Cambridge, England) 2009, 136:275-283.
    • (2009) Development (Cambridge, England) , vol.136 , pp. 275-283
    • Galindo, K.A.1
  • 60
    • 79955526702 scopus 로고    scopus 로고
    • Increasing adult hippocampal neurogenesis is sufficient to improve pattern separation
    • Sahay A., et al. Increasing adult hippocampal neurogenesis is sufficient to improve pattern separation. Nature 2011, 472:466-470.
    • (2011) Nature , vol.472 , pp. 466-470
    • Sahay, A.1
  • 61
    • 0034508217 scopus 로고    scopus 로고
    • The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues
    • Lindsten T., et al. The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. Mol. Cell 2000, 6:1389-1399.
    • (2000) Mol. Cell , vol.6 , pp. 1389-1399
    • Lindsten, T.1
  • 62
    • 77958121925 scopus 로고    scopus 로고
    • Noncanonical functions of BCL-2 proteins in the nervous system
    • Lamb H.M., Hardwick M. Noncanonical functions of BCL-2 proteins in the nervous system. Adv. Exp. Med. Biol. 2010, 687:115-129.
    • (2010) Adv. Exp. Med. Biol. , vol.687 , pp. 115-129
    • Lamb, H.M.1    Hardwick, M.2
  • 63
    • 77957201030 scopus 로고    scopus 로고
    • Grim promotes programmed cell death of Drosophila microchaete glial cells
    • Wu J.N., et al. grim promotes programmed cell death of Drosophila microchaete glial cells. Mech. Dev. 2010, 127:407-417.
    • (2010) Mech. Dev. , vol.127 , pp. 407-417
    • Wu, J.N.1
  • 64
    • 78751482244 scopus 로고    scopus 로고
    • Bcl-2 proteins and autophagy regulate mitochondrial dynamics during programmed cell death in the Drosophila ovary
    • Tanner E.A., et al. Bcl-2 proteins and autophagy regulate mitochondrial dynamics during programmed cell death in the Drosophila ovary. Development (Cambridge, England) 2011, 138:327-338.
    • (2011) Development (Cambridge, England) , vol.138 , pp. 327-338
    • Tanner, E.A.1
  • 65
    • 84859464590 scopus 로고    scopus 로고
    • Mitochondrial pathway of apoptosis is ancestral in metazoans
    • Bender C.E., et al. Mitochondrial pathway of apoptosis is ancestral in metazoans. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:4904-4909.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4904-4909
    • Bender, C.E.1
  • 67
    • 75749098116 scopus 로고    scopus 로고
    • The micro-architecture of mitochondria at active zones: electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism
    • Perkins G.A., et al. The micro-architecture of mitochondria at active zones: electron tomography reveals novel anchoring scaffolds and cristae structured for high-rate metabolism. J. Neurosci. 2010, 30:1015-1026.
    • (2010) J. Neurosci. , vol.30 , pp. 1015-1026
    • Perkins, G.A.1
  • 68
    • 0032563736 scopus 로고    scopus 로고
    • Ultrastructure of neurons and large synaptic terminals in the lateral nucleus of the trapezoid body of the cat
    • Spirou G.A., et al. Ultrastructure of neurons and large synaptic terminals in the lateral nucleus of the trapezoid body of the cat. J. Comp. Neurol. 1998, 398:257-272.
    • (1998) J. Comp. Neurol. , vol.398 , pp. 257-272
    • Spirou, G.A.1
  • 69
    • 77953271477 scopus 로고    scopus 로고
    • Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization
    • Li Z., et al. Caspase-3 activation via mitochondria is required for long-term depression and AMPA receptor internalization. Cell 2010, 141:859-871.
    • (2010) Cell , vol.141 , pp. 859-871
    • Li, Z.1
  • 70
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev A., et al. APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 2009, 457:981-989.
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1
  • 71
    • 79959929850 scopus 로고    scopus 로고
    • Mitochondrial regulation of cell death in the Drosophila ovary
    • Tanner E.A., McCall K. Mitochondrial regulation of cell death in the Drosophila ovary. Autophagy 2011, 7:793-794.
    • (2011) Autophagy , vol.7 , pp. 793-794
    • Tanner, E.A.1    McCall, K.2
  • 72
    • 0037421190 scopus 로고    scopus 로고
    • Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane
    • Kaufmann T., et al. Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane. J. Cell Biol. 2003, 160:53-64.
    • (2003) J. Cell Biol. , vol.160 , pp. 53-64
    • Kaufmann, T.1
  • 73
    • 0029760303 scopus 로고    scopus 로고
    • Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types
    • Zhu W., et al. Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types. EMBO J. 1996, 15:4130-4141.
    • (1996) EMBO J. , vol.15 , pp. 4130-4141
    • Zhu, W.1
  • 74
    • 0033535347 scopus 로고    scopus 로고
    • Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis
    • Griffiths G.J., et al. Cell damage-induced conformational changes of the pro-apoptotic protein Bak in vivo precede the onset of apoptosis. J. Cell Biol. 1999, 144:903-914.
    • (1999) J. Cell Biol. , vol.144 , pp. 903-914
    • Griffiths, G.J.1
  • 75
    • 0033522391 scopus 로고    scopus 로고
    • Conformation of the Bax C-terminus regulates subcellular location and cell death
    • Nechushtan A., et al. 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
  • 76
    • 0030780106 scopus 로고    scopus 로고
    • Movement of Bax from the cytosol to mitochondria during apoptosis
    • Wolter K.G., et al. Movement of Bax from the cytosol to mitochondria during apoptosis. J. Cell Biol. 1997, 139:1281-1292.
    • (1997) J. Cell Biol. , vol.139 , pp. 1281-1292
    • Wolter, K.G.1
  • 77
    • 70449091753 scopus 로고    scopus 로고
    • Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis
    • Kim H., 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
  • 78
    • 34247533289 scopus 로고    scopus 로고
    • Bax activation and mitochondrial insertion during apoptosis
    • Lalier L., et al. Bax activation and mitochondrial insertion during apoptosis. Apoptosis 2007, 12:887-896.
    • (2007) Apoptosis , vol.12 , pp. 887-896
    • Lalier, L.1
  • 79
    • 8844235617 scopus 로고    scopus 로고
    • The mitochondrial death pathway and cardiac myocyte apoptosis
    • Crow M.T., et al. The mitochondrial death pathway and cardiac myocyte apoptosis. Circ. Res. 2004, 95:957-970.
    • (2004) Circ. Res. , vol.95 , pp. 957-970
    • Crow, M.T.1
  • 80
    • 34247506768 scopus 로고    scopus 로고
    • A tale of two mitochondrial channels, MAC and PTP, in apoptosis
    • Kinnally K.W., Antonsson B. A tale of two mitochondrial channels, MAC and PTP, in apoptosis. Apoptosis 2007, 12:857-868.
    • (2007) Apoptosis , vol.12 , pp. 857-868
    • Kinnally, K.W.1    Antonsson, B.2
  • 81
    • 79952708659 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeabilization during apoptosis: the role of mitochondrial fission
    • Landes T., Martinou J.C. Mitochondrial outer membrane permeabilization during apoptosis: the role of mitochondrial fission. Biochim. Biophys. Acta 2011, 1813:540-545.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 540-545
    • Landes, T.1    Martinou, J.C.2
  • 82
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery D., et al. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 1990, 348:334-336.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1
  • 83
    • 0030610962 scopus 로고    scopus 로고
    • Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis
    • Kharbanda S., et al. Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:6939-6942.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6939-6942
    • Kharbanda, S.1
  • 84
    • 0032575606 scopus 로고    scopus 로고
    • Bcl-2 is located predominantly in the inner membrane and crista of mitochondria in rat liver
    • Motoyama S., et al. Bcl-2 is located predominantly in the inner membrane and crista of mitochondria in rat liver. Biochem. Biophys. Res. Commun. 1998, 249:628-636.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 628-636
    • Motoyama, S.1
  • 85
    • 0033939697 scopus 로고    scopus 로고
    • Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells
    • Gotow T., et al. Selective localization of Bcl-2 to the inner mitochondrial and smooth endoplasmic reticulum membranes in mammalian cells. Cell Death Differ. 2000, 7:666-674.
    • (2000) Cell Death Differ. , vol.7 , pp. 666-674
    • Gotow, T.1
  • 86
    • 0037439801 scopus 로고    scopus 로고
    • Bcl-2 and Bax modulate adenine nucleotide translocase activity
    • Belzacq A.S., et al. Bcl-2 and Bax modulate adenine nucleotide translocase activity. Cancer Res. 2003, 63:541-546.
    • (2003) Cancer Res. , vol.63 , pp. 541-546
    • Belzacq, A.S.1
  • 87
    • 0027453852 scopus 로고
    • The bcl-2 protein is inserted into the outer membrane but not into the inner membrane of rat liver mitochondria in vitro
    • Nakai M., et al. The bcl-2 protein is inserted into the outer membrane but not into the inner membrane of rat liver mitochondria in vitro. Biochem. Biophys. Res. Commun. 1993, 196:233-239.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 233-239
    • Nakai, M.1
  • 88
    • 0027525536 scopus 로고
    • Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence
    • Nguyen M., et al. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 1993, 268:25265-25268.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25265-25268
    • Nguyen, M.1
  • 89
    • 0028289951 scopus 로고
    • Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus
    • Nguyen M., et al. Role of membrane anchor domain of Bcl-2 in suppression of apoptosis caused by E1B-defective adenovirus. J. Biol. Chem. 1994, 269:16521-16524.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16521-16524
    • Nguyen, M.1
  • 90
    • 0032487582 scopus 로고    scopus 로고
    • Regulated targeting of BAX to mitochondria
    • Goping I.S., et al. Regulated targeting of BAX to mitochondria. J. Cell Biol. 1998, 143:207-215.
    • (1998) J. Cell Biol. , vol.143 , pp. 207-215
    • Goping, I.S.1
  • 91
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A., et al. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 2001, 153:1265-1276.
    • (2001) J. Cell Biol. , vol.153 , pp. 1265-1276
    • Nechushtan, A.1
  • 92
    • 0026480579 scopus 로고
    • Ultrastructural localization of bcl-2 protein
    • Monaghan P., et al. Ultrastructural localization of bcl-2 protein. J. Histochem. Cytochem. 1992, 40:1819-1825.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1819-1825
    • Monaghan, P.1
  • 93
    • 0028793279 scopus 로고
    • Localization of the Bcl-2 protein to the outer mitochondrial membrane by electron microscopy
    • Riparbelli M.G., et al. Localization of the Bcl-2 protein to the outer mitochondrial membrane by electron microscopy. Exp. Cell Res. 1995, 221:363-369.
    • (1995) Exp. Cell Res. , vol.221 , pp. 363-369
    • Riparbelli, M.G.1
  • 94
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • Lithgow T., et al. The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ. 1994, 5:411-417.
    • (1994) Cell Growth Differ. , vol.5 , pp. 411-417
    • Lithgow, T.1
  • 95
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter M., et al. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat. Cell Biol. 2000, 2:754-761.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 754-761
    • Lutter, M.1
  • 96
    • 20044370709 scopus 로고    scopus 로고
    • TBid interaction with cardiolipin primarily orchestrates mitochondrial dysfunctions and subsequently activates Bax and Bak
    • Gonzalvez F., et al. tBid interaction with cardiolipin primarily orchestrates mitochondrial dysfunctions and subsequently activates Bax and Bak. Cell Death Differ. 2005, 12:614-626.
    • (2005) Cell Death Differ. , vol.12 , pp. 614-626
    • Gonzalvez, F.1
  • 97
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana T., et al. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell 2002, 111:331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1
  • 98
    • 77956634444 scopus 로고    scopus 로고
    • Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization
    • Montessuit S., et al. Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization. Cell 2010, 142:889-901.
    • (2010) Cell , vol.142 , pp. 889-901
    • Montessuit, S.1
  • 99
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • Scorrano L., et al. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev. Cell 2002, 2:55-67.
    • (2002) Dev. Cell , vol.2 , pp. 55-67
    • Scorrano, L.1
  • 100
    • 0025013378 scopus 로고
    • Mitochondrial contact sites. Lipid composition and dynamics
    • Ardail D., et al. Mitochondrial contact sites. Lipid composition and dynamics. J. Biol. Chem. 1990, 265:18797-18802.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18797-18802
    • Ardail, D.1
  • 101
    • 77955271289 scopus 로고    scopus 로고
    • The fast-mobility isoform of mouse Mcl-1 is a mitochondrial matrix-localized protein with attenuated anti-apoptotic activity
    • Huang C.R., Yang-Yen H.F. The fast-mobility isoform of mouse Mcl-1 is a mitochondrial matrix-localized protein with attenuated anti-apoptotic activity. FEBS Lett. 2010, 584:3323-3330.
    • (2010) FEBS Lett. , vol.584 , pp. 3323-3330
    • Huang, C.R.1    Yang-Yen, H.F.2
  • 102
    • 79960148142 scopus 로고    scopus 로고
    • Mitochondrion-dependent N-terminal processing of outer membrane Mcl-1 protein removes an essential Mule/Lasu1 protein-binding site
    • Warr M.R., et al. Mitochondrion-dependent N-terminal processing of outer membrane Mcl-1 protein removes an essential Mule/Lasu1 protein-binding site. J. Biol. Chem. 2011, 286:25098-25107.
    • (2011) J. Biol. Chem. , vol.286 , pp. 25098-25107
    • Warr, M.R.1
  • 103
    • 0033021064 scopus 로고    scopus 로고
    • Inhibition of virus-induced neuronal apoptosis by Bax
    • Lewis J., et al. Inhibition of virus-induced neuronal apoptosis by Bax. Nat. Med. 1999, 5:832-835.
    • (1999) Nat. Med. , vol.5 , pp. 832-835
    • Lewis, J.1
  • 104
    • 4744362784 scopus 로고    scopus 로고
    • BAD is a pro-survival factor prior to activation of its pro-apoptotic function
    • Seo S.Y., et al. BAD is a pro-survival factor prior to activation of its pro-apoptotic function. J. Biol. Chem. 2004, 279:42240-42249.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42240-42249
    • Seo, S.Y.1
  • 105
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng E.H., et al. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science 1997, 278:1966-1968.
    • (1997) Science , vol.278 , pp. 1966-1968
    • Cheng, E.H.1
  • 106
    • 0031930688 scopus 로고    scopus 로고
    • Modulation of cell death by Bcl-XL through caspase interaction
    • Clem R.J., et al. Modulation of cell death by Bcl-XL through caspase interaction. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:554-559.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 554-559
    • Clem, R.J.1
  • 107
    • 0033597785 scopus 로고    scopus 로고
    • Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c
    • Kirsch D.G., et al. Caspase-3-dependent cleavage of Bcl-2 promotes release of cytochrome c. J. Biol. Chem. 1999, 274:21155-21161.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21155-21161
    • Kirsch, D.G.1
  • 108
    • 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
  • 109
    • 84862777042 scopus 로고    scopus 로고
    • N-terminally cleaved Bcl-x(L) mediates ischemia-induced neuronal death
    • Ofengeim D., et al. N-terminally cleaved Bcl-x(L) mediates ischemia-induced neuronal death. Nat. Neurosci. 2012, 15:574-580.
    • (2012) Nat. Neurosci. , vol.15 , pp. 574-580
    • Ofengeim, D.1
  • 110
    • 0035478279 scopus 로고    scopus 로고
    • Global ischemia-induced increases in the gap junctional proteins connexin 32 (Cx32) and Cx36 in hippocampus and enhanced vulnerability of Cx32 knock-out mice
    • Oguro K., et al. Global ischemia-induced increases in the gap junctional proteins connexin 32 (Cx32) and Cx36 in hippocampus and enhanced vulnerability of Cx32 knock-out mice. J. Neurosci. 2001, 21:7534-7542.
    • (2001) J. Neurosci. , vol.21 , pp. 7534-7542
    • Oguro, K.1
  • 111
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • Basanez G., et al. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J. Biol. Chem. 2002, 277:49360-49365.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49360-49365
    • Basanez, G.1
  • 112
    • 4544359229 scopus 로고    scopus 로고
    • Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals
    • Jonas E.A., et al. Proapoptotic N-truncated BCL-xL protein activates endogenous mitochondrial channels in living synaptic terminals. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:13590-13595.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13590-13595
    • Jonas, E.A.1
  • 113
    • 84867416957 scopus 로고    scopus 로고
    • Integration of apoptosis and metabolism
    • Yi C.H., et al. Integration of apoptosis and metabolism. Cold Spring Harb. Symp. Quant. Biol. 2011, http://dx.doi.org/10.1101/sqb.2011.76.010777.
    • (2011) Cold Spring Harb. Symp. Quant. Biol.
    • Yi, C.H.1
  • 114
    • 78650874294 scopus 로고    scopus 로고
    • Praf2 is a novel Bcl-xL/Bcl-2 interacting protein with the ability to modulate survival of cancer cells
    • Vento M.T., et al. Praf2 is a novel Bcl-xL/Bcl-2 interacting protein with the ability to modulate survival of cancer cells. PLoS ONE 2010, 5:e15636.
    • (2010) PLoS ONE , vol.5
    • Vento, M.T.1
  • 115
    • 0034688175 scopus 로고    scopus 로고
    • Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator
    • Brenner C., et al. Bcl-2 and Bax regulate the channel activity of the mitochondrial adenine nucleotide translocator. Oncogene 2000, 19:329-336.
    • (2000) Oncogene , vol.19 , pp. 329-336
    • Brenner, C.1
  • 116
    • 79952282995 scopus 로고    scopus 로고
    • Modular assembly of yeast mitochondrial ATP synthase
    • Rak M., et al. Modular assembly of yeast mitochondrial ATP synthase. EMBO J. 2011, 30:920-930.
    • (2011) EMBO J. , vol.30 , pp. 920-930
    • Rak, M.1
  • 117
    • 67649760168 scopus 로고    scopus 로고
    • Mitochondrial dynamics in Parkinson's disease
    • Van Laar V.S., Berman S.B. Mitochondrial dynamics in Parkinson's disease. Exp. Neurol. 2009, 218:247-256.
    • (2009) Exp. Neurol. , vol.218 , pp. 247-256
    • Van Laar, V.S.1    Berman, S.B.2
  • 118
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin S.M., et al. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 2010, 191:933-942.
    • (2010) J. Cell Biol. , vol.191 , pp. 933-942
    • Jin, S.M.1
  • 119
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 Binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
    • Lazarou M., et al. Role of PINK1 Binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev. Cell 2012, 22:320-333.
    • (2012) Dev. Cell , vol.22 , pp. 320-333
    • Lazarou, M.1
  • 120
    • 84857059879 scopus 로고    scopus 로고
    • Evidence that CED-9/Bcl2 and CED-4/Apaf-1 localization is not consistent with the current model for C. elegans apoptosis induction
    • Pourkarimi E., et al. Evidence that CED-9/Bcl2 and CED-4/Apaf-1 localization is not consistent with the current model for C. elegans apoptosis induction. Cell Death Differ. 2012, 19:406-415.
    • (2012) Cell Death Differ. , vol.19 , pp. 406-415
    • Pourkarimi, E.1


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