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Volumn 181, Issue , 2014, Pages 62-75

Mitochondrial alterations in apoptosis

Author keywords

Apoptosis; Bcl 2 family proteins; Cardiolipin; Cristae remodeling; Mitochondrial fission; Mitochondrial outer membrane permeabilization

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARDIOLIPIN; CYTOCHROME C; LIPID; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PROTEIN BAK; PROTEIN BAX; PROTEIN BCL 2;

EID: 84899510806     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2014.04.001     Document Type: Review
Times cited : (157)

References (174)
  • 2
    • 33750526651 scopus 로고    scopus 로고
    • The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis
    • E. Alirol, D. James, D. Huber, A. Marchetto, L. Vergani, J.-C. Martinou, and L. Scorrano The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce apoptosis Mol. Biol. Cell 17 11 2006 4593 4605
    • (2006) Mol. Biol. Cell , vol.17 , Issue.11 , pp. 4593-4605
    • Alirol, E.1    James, D.2    Huber, D.3    Marchetto, A.4    Vergani, L.5    Martinou, J.-C.6    Scorrano, L.7
  • 3
    • 84893480044 scopus 로고    scopus 로고
    • Organization of the mitochondrial apoptotic BAK pore: Oligomerization of the BAK homodimers
    • 10.1074/jbc.M113.526806
    • S. Aluvila, T. Mandal, E. Hustedt, P. Fajer, J.Y. Choe, and K.J. Oh Organization of the mitochondrial apoptotic BAK pore: oligomerization of the BAK homodimers J. Biol. Chem. 2013 10.1074/jbc.M113.526806
    • (2013) J. Biol. Chem.
    • Aluvila, S.1    Mandal, T.2    Hustedt, E.3    Fajer, P.4    Choe, J.Y.5    Oh, K.J.6
  • 4
    • 84859056673 scopus 로고    scopus 로고
    • Differences in the mechanisms of proapoptotic BH3 proteins binding to Bcl-XL and Bcl-2 quantified in live MCF-7 cells
    • A. Aranovich, Q. Liu, T. Collins, F. Geng, S. Dixit, B. Leber and David, and W. Andrews Differences in the mechanisms of proapoptotic BH3 proteins binding to Bcl-XL and Bcl-2 quantified in live MCF-7 cells Mol. Cell 45 6 2012 754 763
    • (2012) Mol. Cell , vol.45 , Issue.6 , pp. 754-763
    • Aranovich, A.1    Liu, Q.2    Collins, T.3    Geng, F.4    Dixit, S.5
  • 6
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • D. Arnoult, A. Grodet, Y.-J. Lee, J. Estaquier, and C. Blackstone Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation J. Biol. Chem. 280 42 2005 35742 35750
    • (2005) J. Biol. Chem. , vol.280 , Issue.42 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.-J.3    Estaquier, J.4    Blackstone, C.5
  • 7
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • G. Basanez Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature J. Biol. Chem. 277 51 2002 49360 49365
    • (2002) J. Biol. Chem. , vol.277 , Issue.51 , pp. 49360-49365
    • Basanez, G.1
  • 9
    • 57649215874 scopus 로고    scopus 로고
    • GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission
    • P.V. Bashkirov, S.A. Akimov, A.I. Evseev, S.L. Schmid, J. Zimmerberg, and V.A. Frolov GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission Cell 135 7 2008 1276 1286
    • (2008) Cell , vol.135 , Issue.7 , pp. 1276-1286
    • Bashkirov, P.V.1    Akimov, S.A.2    Evseev, A.I.3    Schmid, S.L.4    Zimmerberg, J.5    Frolov, V.A.6
  • 10
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • E. Basso, L. Fante, J. Fowlkes, V. Petronilli, M.A. Forte, and P. Bernardi Properties of the permeability transition pore in mitochondria devoid of cyclophilin D J. Biol. Chem. 280 19 2005 18558 18561
    • (2005) J. Biol. Chem. , vol.280 , Issue.19 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 11
    • 84878749325 scopus 로고    scopus 로고
    • Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins
    • T. Becker, S.E. Horvath, L. Bottinger, N. Gebert, G. Daum, and N. Pfanner Role of phosphatidylethanolamine in the biogenesis of mitochondrial outer membrane proteins J. Biol. Chem. 288 23 2013 16451 16459
    • (2013) J. Biol. Chem. , vol.288 , Issue.23 , pp. 16451-16459
    • Becker, T.1    Horvath, S.E.2    Bottinger, L.3    Gebert, N.4    Daum, G.5    Pfanner, N.6
  • 14
    • 84887840021 scopus 로고    scopus 로고
    • Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size
    • S. Bleicken, O. Landeta, A. Landajuela, G. Basanez, and A.J. Garcia-Saez Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size J. Biol. Chem. 288 46 2013 33241 33252
    • (2013) J. Biol. Chem. , vol.288 , Issue.46 , pp. 33241-33252
    • Bleicken, S.1    Landeta, O.2    Landajuela, A.3    Basanez, G.4    Garcia-Saez, A.J.5
  • 15
    • 84872816605 scopus 로고    scopus 로고
    • Mechanistic differences in the membrane activity of Bax and Bcl-xL correlate with their opposing roles in apoptosis
    • S. Bleicken, C. Wagner, J. Ana, and García-Sáez Mechanistic differences in the membrane activity of Bax and Bcl-xL correlate with their opposing roles in apoptosis Biophys. J. 104 2 2013 421 431
    • (2013) Biophys. J. , vol.104 , Issue.2 , pp. 421-431
    • Bleicken, S.1    Wagner, C.2    Ana, J.3    García-Sáez4
  • 17
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • R. Bose, M. Verheij, A. Haimovitz-Friedman, K. Scotto, Z. Fuks, and R. Kolesnick Ceramide synthase mediates daunorubicin-induced apoptosis: an alternative mechanism for generating death signals Cell 82 3 1995 405 414
    • (1995) Cell , vol.82 , Issue.3 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-Friedman, A.3    Scotto, K.4    Fuks, Z.5    Kolesnick, R.6
  • 18
    • 49349100454 scopus 로고    scopus 로고
    • Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution pathways downstream of ced-3 and independent of ced-9
    • D.G. Breckenridge, B.-H. Kang, D. Kokel, S. Mitani, L.A. Staehelin, and D. Xue Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution pathways downstream of ced-3 and independent of ced-9 Mol. cell 31 4 2008 586 597
    • (2008) Mol. Cell , vol.31 , Issue.4 , pp. 586-597
    • Breckenridge, D.G.1    Kang, B.-H.2    Kokel, D.3    Mitani, S.4    Staehelin, L.A.5    Xue, D.6
  • 19
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • D.G. Breckenridge, M. Stojanovic, R.C. Marcellus, and G.C. Shore Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol J. Cell Biol. 160 7 2003 1115 1127
    • (2003) J. Cell Biol. , vol.160 , Issue.7 , pp. 1115-1127
    • Breckenridge, D.G.1    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 20
    • 79952172319 scopus 로고    scopus 로고
    • Fragmented mitochondria are sensitized to Bax insertion and activation during apoptosis
    • C. Brooks, S.-G. Cho, C.-Y. Wang, T. Yang, and Z. Dong Fragmented mitochondria are sensitized to Bax insertion and activation during apoptosis Am. J. Physiol. Cell Physiol. 300 3 2011 C447 C455
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300 , Issue.3
    • Brooks, C.1    Cho, S.-G.2    Wang, C.-Y.3    Yang, T.4    Dong, Z.5
  • 22
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • H. Chen, S.A. Detmer, A.J. Ewald, E.E. Griffin, S.E. Fraser, and D.C. Chan Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development J. Cell Biol. 160 2 2003 189 200
    • (2003) J. Cell Biol. , vol.160 , Issue.2 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 23
    • 70350374353 scopus 로고    scopus 로고
    • Suppression of mitochondrial function by oxidatively truncated phospholipids is reversible, aided by Bid, and suppressed by Bcl-XL
    • R. Chen, A.E. Feldstein, and T.M. McIntyre Suppression of mitochondrial function by oxidatively truncated phospholipids is reversible, aided by Bid, and suppressed by Bcl-XL J. Biol. Chem. 284 39 2009 26297 26308
    • (2009) J. Biol. Chem. , vol.284 , Issue.39 , pp. 26297-26308
    • Chen, R.1    Feldstein, A.E.2    McIntyre, T.M.3
  • 25
    • 84857873334 scopus 로고    scopus 로고
    • Sphingolipid metabolism cooperates with BAK and BAX to promote the mitochondrial pathway of apoptosis
    • J.E. Chipuk, G.P. McStay, A. Bharti, T. Kuwana, C.J. Clarke, L.J. Siskind, L.M. Obeid, and D.R. Green Sphingolipid metabolism cooperates with BAK and BAX to promote the mitochondrial pathway of apoptosis Cell 148 5 2012 988 1000
    • (2012) Cell , vol.148 , Issue.5 , pp. 988-1000
    • Chipuk, J.E.1    McStay, G.P.2    Bharti, A.3    Kuwana, T.4    Clarke, C.J.5    Siskind, L.J.6    Obeid, L.M.7    Green, D.R.8
  • 28
    • 84855581252 scopus 로고    scopus 로고
    • The complexity of cardiolipin in health and disease
    • S.M. Claypool, and C.M. Koehler The complexity of cardiolipin in health and disease Trends Biochem. Sci. 37 1 2012 32 41
    • (2012) Trends Biochem. Sci. , vol.37 , Issue.1 , pp. 32-41
    • Claypool, S.M.1    Koehler, C.M.2
  • 29
    • 0015209679 scopus 로고
    • Enzymac characterization and lipid composition of rat liver subcellular membranes
    • A. Colbeau, J. Nachbaur, and P.M. Vignais Enzymac characterization and lipid composition of rat liver subcellular membranes Biochim. Biophys. Acta (BBA) - Biomembr. 249 2 1971 462 492
    • (1971) Biochim. Biophys. Acta (BBA) - Biomembr. , vol.249 , Issue.2 , pp. 462-492
    • Colbeau, A.1    Nachbaur, J.2    Vignais, P.M.3
  • 30
    • 0018775962 scopus 로고
    • A candidate for the permeability pathway of the outer mitochondrial membrane
    • M. Colombini A candidate for the permeability pathway of the outer mitochondrial membrane Nature 279 5714 1979 643 645
    • (1979) Nature , vol.279 , Issue.5714 , pp. 643-645
    • Colombini, M.1
  • 31
    • 77953811195 scopus 로고    scopus 로고
    • Ceramide channels and their role in mitochondria-mediated apoptosis
    • M. Colombini Ceramide channels and their role in mitochondria-mediated apoptosis Biochim. Biophys. Acta (BBA) - Bioenerg. 1797 6 2010 1239 1244
    • (2010) Biochim. Biophys. Acta (BBA) - Bioenerg. , vol.1797 , Issue.6 , pp. 1239-1244
    • Colombini, M.1
  • 32
    • 84868596965 scopus 로고    scopus 로고
    • Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein
    • M. Connerth, T. Tatsuta, M. Haag, T. Klecker, B. Westermann, and T. Langer Intramitochondrial transport of phosphatidic acid in yeast by a lipid transfer protein Science 338 6108 2012 815 818
    • (2012) Science , vol.338 , Issue.6108 , pp. 815-818
    • Connerth, M.1    Tatsuta, T.2    Haag, M.3    Klecker, T.4    Westermann, B.5    Langer, T.6
  • 34
    • 1842680755 scopus 로고    scopus 로고
    • Membrane lipids and cell death: An overview
    • I.M. Cristea, and M. Degli Esposti Membrane lipids and cell death: an overview Chem. Phys. Lipids 129 2 2004 133 160
    • (2004) Chem. Phys. Lipids , vol.129 , Issue.2 , pp. 133-160
    • Cristea, I.M.1    Degli Esposti, M.2
  • 36
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • P.R. Cullis, and B. De Kruijff Lipid polymorphism and the functional roles of lipids in biological membranes Biochim. Biophys. Acta (BBA) - Rev. Biomembr. 559 4 1979 399 420
    • (1979) Biochim. Biophys. Acta (BBA) - Rev. Biomembr. , vol.559 , Issue.4 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 37
    • 84890909335 scopus 로고    scopus 로고
    • Control of apoptosis by the BCL-2 protein family: Implications for physiology and therapy
    • P.E. Czabotar, G. Lessene, A. Strasser, and J.M. Adams Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy Nat. Rev. Mol. Cell. Biol. 15 1 2014 49 63
    • (2014) Nat. Rev. Mol. Cell. Biol. , vol.15 , Issue.1 , pp. 49-63
    • Czabotar, P.E.1    Lessene, G.2    Strasser, A.3    Adams, J.M.4
  • 38
    • 2442711625 scopus 로고    scopus 로고
    • Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin
    • Q. Dai, J. Liu, J. Chen, D. Durrant, T.M. McIntyre, and R.M. Lee Mitochondrial ceramide increases in UV-irradiated HeLa cells and is mainly derived from hydrolysis of sphingomyelin Oncogene 23 20 2004 3650 3658
    • (2004) Oncogene , vol.23 , Issue.20 , pp. 3650-3658
    • Dai, Q.1    Liu, J.2    Chen, J.3    Durrant, D.4    McIntyre, T.M.5    Lee, R.M.6
  • 39
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • O.M. de Brito, and L. Scorrano Mitofusin 2 tethers endoplasmic reticulum to mitochondria Nature 456 7222 2008 605 610
    • (2008) Nature , vol.456 , Issue.7222 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 40
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa is cardiolipin present in the mitochondrial outer membrane?
    • A.I.P.M. de Kroon, D. Dolis, A. Mayer, R. Lill, and B. de Kruijff Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa is cardiolipin present in the mitochondrial outer membrane? Biochim. Biophys. Acta (BBA) - Biomembr. 1325 1 1997 108 116
    • (1997) Biochim. Biophys. Acta (BBA) - Biomembr. , vol.1325 , Issue.1 , pp. 108-116
    • De Kroon, A.I.P.M.1    Dolis, D.2    Mayer, A.3    Lill, R.4    De Kruijff, B.5
  • 41
    • 0036791637 scopus 로고    scopus 로고
    • The roles of Bid
    • M. Degli Esposti The roles of Bid Apoptosis 7 5 2002 433 440
    • (2002) Apoptosis , vol.7 , Issue.5 , pp. 433-440
    • Degli Esposti, M.1
  • 42
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • M. Degli Esposti, J.T. Erler, J.A. Hickman, and C. Dive Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity Mol. Cell. Biol. 21 21 2001 7268 7276
    • (2001) Mol. Cell. Biol. , vol.21 , Issue.21 , pp. 7268-7276
    • Degli Esposti, M.1    Erler, J.T.2    Hickman, J.A.3    Dive, C.4
  • 45
    • 0032875663 scopus 로고    scopus 로고
    • Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids
    • M. Dolder, K. Zeth, P. Tittmann, H. Gross, W. Welte, and T. Wallimann Crystallization of the human, mitochondrial voltage-dependent anion-selective channel in the presence of phospholipids J. Struct. Biol. 127 1 1999 64 71
    • (1999) J. Struct. Biol. , vol.127 , Issue.1 , pp. 64-71
    • Dolder, M.1    Zeth, K.2    Tittmann, P.3    Gross, H.4    Welte, W.5    Wallimann, T.6
  • 49
    • 33748448681 scopus 로고    scopus 로고
    • Sphingosine, a product of ceramide hydrolysis, influences the formation of ceramide channels
    • M.J. Elrick, S. Fluss, and M. Colombini Sphingosine, a product of ceramide hydrolysis, influences the formation of ceramide channels Biophys. J. 91 5 2006 1749 1756
    • (2006) Biophys. J. , vol.91 , Issue.5 , pp. 1749-1756
    • Elrick, M.J.1    Fluss, S.2    Colombini, M.3
  • 51
    • 0348038751 scopus 로고    scopus 로고
    • Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death
    • M.D. Esposti, I.M. Cristea, S.J. Gaskell, Y. Nakao, and C. Dive Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death Cell Death Differ. 10 12 2003 1300 1309
    • (2003) Cell Death Differ. , vol.10 , Issue.12 , pp. 1300-1309
    • Esposti, M.D.1    Cristea, I.M.2    Gaskell, S.J.3    Nakao, Y.4    Dive, C.5
  • 52
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • M.D. Esposti, J.T. Erler, J.A. Hickman, and C. Dive Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity Mol. Cell. Biol. 21 21 2001 7268 7276
    • (2001) Mol. Cell. Biol. , vol.21 , Issue.21 , pp. 7268-7276
    • Esposti, M.D.1    Erler, J.T.2    Hickman, J.A.3    Dive, C.4
  • 53
    • 34249019899 scopus 로고    scopus 로고
    • Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis
    • J. Estaquier, and D. Arnoult Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis Cell Death Differ. 14 6 2007 1086 1094
    • (2007) Cell Death Differ. , vol.14 , Issue.6 , pp. 1086-1094
    • Estaquier, J.1    Arnoult, D.2
  • 54
    • 0034003692 scopus 로고    scopus 로고
    • Opening of the mitochondrial permeability transition pore causes matrix expansion and outer membrane rupture in fas-mediated hepatic apoptosis in mice
    • G. Feldmann, D. Haouzi, A. Moreau, A.-M. Durand-Schneider, A. Bringuier, A. Berson, A. Mansouri, D. Fau, and D. Pessayre Opening of the mitochondrial permeability transition pore causes matrix expansion and outer membrane rupture in fas-mediated hepatic apoptosis in mice Hepatology 31 3 2000 674 683
    • (2000) Hepatology , vol.31 , Issue.3 , pp. 674-683
    • Feldmann, G.1    Haouzi, D.2    Moreau, A.3    Durand-Schneider, A.-M.4    Bringuier, A.5    Berson, A.6    Mansouri, A.7    Fau, D.8    Pessayre, D.9
  • 59
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • S. Gandre-Babbe, and A.M. van der Bliek The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells Mol. Biol. Cell 19 6 2008 2402 2412
    • (2008) Mol. Biol. Cell , vol.19 , Issue.6 , pp. 2402-2412
    • Gandre-Babbe, S.1    Van Der Bliek, A.M.2
  • 60
    • 77951665317 scopus 로고    scopus 로고
    • Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane
    • V. Ganesan, M.N. Perera, D. Colombini, D. Datskovskiy, K. Chadha, and M. Colombini Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane Apoptosis 15 5 2010 553 562
    • (2010) Apoptosis , vol.15 , Issue.5 , pp. 553-562
    • Ganesan, V.1    Perera, M.N.2    Colombini, D.3    Datskovskiy, D.4    Chadha, K.5    Colombini, M.6
  • 61
    • 84864710153 scopus 로고    scopus 로고
    • The dynamics of Bax channel formation: Influence of ionic strength
    • V. Ganesan, T. Walsh, K.-T. Chang, and M. Colombini The dynamics of Bax channel formation: influence of ionic strength Biophys. J. 103 3 2012 483 491
    • (2012) Biophys. J. , vol.103 , Issue.3 , pp. 483-491
    • Ganesan, V.1    Walsh, T.2    Chang, K.-T.3    Colombini, M.4
  • 63
    • 84870990121 scopus 로고    scopus 로고
    • The secrets of the Bcl-2 family
    • A.J. García-Sáez The secrets of the Bcl-2 family Cell Death Differ. 19 11 2012 1733 1740
    • (2012) Cell Death Differ. , vol.19 , Issue.11 , pp. 1733-1740
    • García-Sáez, A.J.1
  • 64
    • 34447255173 scopus 로고    scopus 로고
    • Pore formation by a Bax-derived peptide: Effect on the line tension of the membrane probed by AFM
    • A.J. García-Sáez, S. Chiantia, J. Salgado, and P. Schwille Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM Biophys. J. 93 1 2007 103 112
    • (2007) Biophys. J. , vol.93 , Issue.1 , pp. 103-112
    • García-Sáez, A.J.1    Chiantia, S.2    Salgado, J.3    Schwille, P.4
  • 65
    • 22244493864 scopus 로고    scopus 로고
    • Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
    • A.J. García-Sáez, M. Coraiola, M. Dalla Serra, I. Mingarro, G. Menestrina, and J. Salgado Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins Biophys. J. 88 6 2005 3976 3990
    • (2005) Biophys. J. , vol.88 , Issue.6 , pp. 3976-3990
    • García-Sáez, A.J.1    Coraiola, M.2    Dalla Serra, M.3    Mingarro, I.4    Menestrina, G.5    Salgado, J.6
  • 66
    • 33644946679 scopus 로고    scopus 로고
    • Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
    • A.J. García-Sáez, M. Coraiola, M.D. Serra, I. Mingarro, P. Müller, and J. Salgado Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores FEBS J. 273 5 2006 971 981
    • (2006) FEBS J. , vol.273 , Issue.5 , pp. 971-981
    • García-Sáez, A.J.1    Coraiola, M.2    Serra, M.D.3    Mingarro, I.4    Müller, P.5    Salgado, J.6
  • 73
    • 0037636369 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis
    • E. Gottlieb, S.M. Armour, M.H. Harris, and C.B. Thompson Mitochondrial membrane potential regulates matrix configuration and cytochrome c release during apoptosis Cell Death Differ. 10 6 2003 709 717
    • (2003) Cell Death Differ. , vol.10 , Issue.6 , pp. 709-717
    • Gottlieb, E.1    Armour, S.M.2    Harris, M.H.3    Thompson, C.B.4
  • 74
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • D.R. Green The pathophysiology of mitochondrial cell death Science 305 5684 2004 626 629
    • (2004) Science , vol.305 , Issue.5684 , pp. 626-629
    • Green, D.R.1
  • 75
    • 0032589515 scopus 로고    scopus 로고
    • Ca2+-induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of Ca2+-stimulated generation of reactive oxygen species by the respiratory chain
    • M.T. Grijalba, A.E. Vercesi, and S. Schreier Ca2+-induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of Ca2+-stimulated generation of reactive oxygen species by the respiratory chain Biochemistry 38 40 1999 13279 13287
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 13279-13287
    • Grijalba, M.T.1    Vercesi, A.E.2    Schreier, S.3
  • 76
    • 36348989007 scopus 로고    scopus 로고
    • Mitofusin 2 triggers vascular smooth muscle cell apoptosis via mitochondrial death pathway
    • X. Guo, K.-H. Chen, Y. Guo, H. Liao, J. Tang, and R.-P. Xiao Mitofusin 2 triggers vascular smooth muscle cell apoptosis via mitochondrial death pathway Circ. Res. 101 11 2007 1113 1122
    • (2007) Circ. Res. , vol.101 , Issue.11 , pp. 1113-1122
    • Guo, X.1    Chen, K.-H.2    Guo, Y.3    Liao, H.4    Tang, J.5    Xiao, R.-P.6
  • 79
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • S. Hoppins, L. Lackner, and J. Nunnari The machines that divide and fuse mitochondria Annu. Rev. Biochem. 76 1 2007 751 780
    • (2007) Annu. Rev. Biochem. , vol.76 , Issue.1 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 80
    • 84865547276 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis - The ER connection
    • S. Hoppins, and J. Nunnari Mitochondrial dynamics and apoptosis - the ER connection Science 337 6098 2012 1052 1054
    • (2012) Science , vol.337 , Issue.6098 , pp. 1052-1054
    • Hoppins, S.1    Nunnari, J.2
  • 81
    • 84884965580 scopus 로고    scopus 로고
    • Lipids of mitochondria
    • S.E. Horvath, and G. Daum Lipids of mitochondria Prog. Lipid Res. 52 4 2013 590 614
    • (2013) Prog. Lipid Res. , vol.52 , Issue.4 , pp. 590-614
    • Horvath, S.E.1    Daum, G.2
  • 82
    • 0027208289 scopus 로고
    • Phospholipid asymmetry of the outer membrane of rat liver mitochondria: Evidence for the presence of cardiolipin on the outside of the outer membrane
    • R. Hovius, J. Thijssen, P. van der Linden, K. Nicolay, and B. de Kruijff Phospholipid asymmetry of the outer membrane of rat liver mitochondria: evidence for the presence of cardiolipin on the outside of the outer membrane FEBS Lett. 330 1 1993 71 76
    • (1993) FEBS Lett. , vol.330 , Issue.1 , pp. 71-76
    • Hovius, R.1    Thijssen, J.2    Van Der Linden, P.3    Nicolay, K.4    De Kruijff, B.5
  • 83
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of peptide-induced pores in membranes
    • H.W. Huang, F.-Y. Chen, and M.-T. Lee Molecular mechanism of peptide-induced pores in membranes Phys. Rev. Lett. 92 19 2004 198304
    • (2004) Phys. Rev. Lett. , vol.92 , Issue.19 , pp. 198304
    • Huang, H.W.1    Chen, F.-Y.2    Lee, M.-T.3
  • 86
    • 84881091005 scopus 로고    scopus 로고
    • Decoding and unlocking the BCL-2 dependency of cancer cells
    • P. Juin, O. Geneste, F. Gautier, S. Depil, and M. Campone Decoding and unlocking the BCL-2 dependency of cancer cells Nat. Rev. Cancer 13 7 2013 455 465
    • (2013) Nat. Rev. Cancer , vol.13 , Issue.7 , pp. 455-465
    • Juin, P.1    Geneste, O.2    Gautier, F.3    Depil, S.4    Campone, M.5
  • 88
    • 4644242944 scopus 로고    scopus 로고
    • Endophilin B1 is required for the maintenance of mitochondrial morphology
    • M. Karbowski, S.-Y. Jeong, and R.J. Youle Endophilin B1 is required for the maintenance of mitochondrial morphology J. Cell Biol. 166 7 2004 1027 1039
    • (2004) J. Cell Biol. , vol.166 , Issue.7 , pp. 1027-1039
    • Karbowski, M.1    Jeong, S.-Y.2    Youle, R.J.3
  • 91
    • 27544450920 scopus 로고    scopus 로고
    • The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly
    • M.A. Karren, E.M. Coonrod, T.K. Anderson, and J.M. Shaw The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly J. Cell Biol. 171 2 2005 291 301
    • (2005) J. Cell Biol. , vol.171 , Issue.2 , pp. 291-301
    • Karren, M.A.1    Coonrod, E.M.2    Anderson, T.K.3    Shaw, J.M.4
  • 93
    • 3042723249 scopus 로고    scopus 로고
    • Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome c release
    • T.H. Kim Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome c release Mol. Biol. Cell 15 7 2004 3061 3072
    • (2004) Mol. Biol. Cell , vol.15 , Issue.7 , pp. 3061-3072
    • Kim, T.H.1
  • 97
    • 0035957921 scopus 로고    scopus 로고
    • Induction of apoptosis through B-cell receptor cross-linking occurs via de Novo generated C16-ceramide and involves mitochondria
    • B.-J. Kroesen, B. Pettus, C. Luberto, M. Busman, H. Sietsma, L. de Leij, and Y.A. Hannun Induction of apoptosis through B-cell receptor cross-linking occurs via de Novo generated C16-ceramide and involves mitochondria J. Biol. Chem. 276 17 2001 13606 13614
    • (2001) J. Biol. Chem. , vol.276 , Issue.17 , pp. 13606-13614
    • Kroesen, B.-J.1    Pettus, B.2    Luberto, C.3    Busman, M.4    Sietsma, H.5    De Leij, L.6    Hannun, Y.A.7
  • 98
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • T. Kuwana, L. Bouchier-Hayes, J.E. Chipuk, C. Bonzon, B.A. Sullivan, D.R. Green, and D.D. Newmeyer BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly Mol. Cell 17 4 2005 525 535
    • (2005) Mol. Cell , vol.17 , Issue.4 , pp. 525-535
    • Kuwana, T.1    Bouchier-Hayes, L.2    Chipuk, J.E.3    Bonzon, C.4    Sullivan, B.A.5    Green, D.R.6    Newmeyer, D.D.7
  • 100
    • 34247497716 scopus 로고    scopus 로고
    • Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes
    • B. Leber, J. Lin, and D. Andrews Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes Apoptosis 12 5 2007 897 911
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 897-911
    • Leber, B.1    Lin, J.2    Andrews, D.3
  • 101
    • 77957141008 scopus 로고    scopus 로고
    • Still embedded together binding to membranes regulates Bcl-2 protein interactions
    • B. Leber, J. Lin, and D.W. Andrews Still embedded together binding to membranes regulates Bcl-2 protein interactions Oncogene 29 38 2010
    • (2010) Oncogene , vol.29 , Issue.38
    • Leber, B.1    Lin, J.2    Andrews, D.W.3
  • 103
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • A. Letai, M.C. Bassik, L.D. Walensky, M.D. Sorcinelli, S. Weiler, and S.J. Korsmeyer Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics Cancer Cell 2 3 2002 183 192
    • (2002) Cancer Cell , vol.2 , Issue.3 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 104
    • 84867619217 scopus 로고    scopus 로고
    • Nonvesicular lipid transfer from the endoplasmic reticulum
    • S. Lev Nonvesicular lipid transfer from the endoplasmic reticulum Cold Spring Harb. Perspect. Biol. 4. 10 2012
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , Issue.10
    • Lev, S.1
  • 108
    • 57149135309 scopus 로고    scopus 로고
    • Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax
    • J.F. Lovell, L.P. Billen, S. Bindner, A. Shamas-Din, C. Fradin, B. Leber, and D.W. Andrews Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax Cell 135 6 2008 1074 1084
    • (2008) Cell , vol.135 , Issue.6 , pp. 1074-1084
    • Lovell, J.F.1    Billen, L.P.2    Bindner, S.3    Shamas-Din, A.4    Fradin, C.5    Leber, B.6    Andrews, D.W.7
  • 110
    • 18744374204 scopus 로고    scopus 로고
    • The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites
    • M. Lutter, G. Perkins, and X. Wang The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites BMC Cell Biol. 2 1 2001 1 9
    • (2001) BMC Cell Biol. , vol.2 , Issue.1 , pp. 1-9
    • Lutter, M.1    Perkins, G.2    Wang, X.3
  • 111
    • 0037879052 scopus 로고    scopus 로고
    • The mitochondrial membrane potential (Δψm) in apoptosis; An update
    • J.D. Ly, D.R. Grubb, and A. Lawen The mitochondrial membrane potential (Δψm) in apoptosis; an update Apoptosis 8 2 2003 115 128
    • (2003) Apoptosis , vol.8 , Issue.2 , pp. 115-128
    • Ly, J.D.1    Grubb, D.R.2    Lawen, A.3
  • 112
    • 33846207499 scopus 로고    scopus 로고
    • NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL
    • T.J. Malia, and G. Wagner NMR structural investigation of the mitochondrial outer membrane protein VDAC and its interaction with antiapoptotic Bcl-xL Biochemistry 46 2 2006 514 525
    • (2006) Biochemistry , vol.46 , Issue.2 , pp. 514-525
    • Malia, T.J.1    Wagner, G.2
  • 113
    • 66149106292 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation
    • O. Maniti, M.-F. Lecompte, O. Marcillat, B. Desbat, R. Buchet, C. Vial, and T. Granjon Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation Biophys. J. 96 6 2009 2428 2438
    • (2009) Biophys. J. , vol.96 , Issue.6 , pp. 2428-2438
    • Maniti, O.1    Lecompte, M.-F.2    Marcillat, O.3    Desbat, B.4    Buchet, R.5    Vial, C.6    Granjon, T.7
  • 114
    • 79960230433 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics
    • J.-C. Martinou, and Richard J. Youle Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics Dev. Cell 21 1 2011 92 101
    • (2011) Dev. Cell , vol.21 , Issue.1 , pp. 92-101
    • Martinou, J.-C.1    Youle, R.J.2
  • 118
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • A. Olichon, L. Baricault, N. Gas, E. Guillou, A. Valette, P. Belenguer, and G. Lenaers Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis J. Biol. Chem. 278 10 2003 7743 7746
    • (2003) J. Biol. Chem. , vol.278 , Issue.10 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 120
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • H. Otera, C. Wang, M.M. Cleland, K. Setoguchi, S. Yokota, R.J. Youle, and K. Mihara Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells J. Cell Biol. 191 6 2010 1141 1158
    • (2010) J. Cell Biol. , vol.191 , Issue.6 , pp. 1141-1158
    • Otera, H.1    Wang, C.2    Cleland, M.M.3    Setoguchi, K.4    Yokota, S.5    Youle, R.J.6    Mihara, K.7
  • 123
    • 79960729178 scopus 로고    scopus 로고
    • The regulation of mitochondrial morphology: Intricate mechanisms and dynamic machinery
    • C.S. Palmer, L.D. Osellame, D. Stojanovski, and M.T. Ryan The regulation of mitochondrial morphology: intricate mechanisms and dynamic machinery Cell. Signal. 23 10 2011 1534 1545
    • (2011) Cell. Signal. , vol.23 , Issue.10 , pp. 1534-1545
    • Palmer, C.S.1    Osellame, L.D.2    Stojanovski, D.3    Ryan, M.T.4
  • 126
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
    • T.J. Pucadyil, and S.L. Schmid Real-time visualization of dynamin-catalyzed membrane fission and vesicle release Cell 135 7 2008 1263 1275
    • (2008) Cell , vol.135 , Issue.7 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 127
    • 56249132688 scopus 로고    scopus 로고
    • Structure of transmembrane pore induced by Bax-derived peptide: Evidence for lipidic pores
    • S. Qian, W. Wang, L. Yang, and H.W. Huang Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores Proc. Natl. Acad. Sci. U S A 105 45 2008 17379 17383
    • (2008) Proc. Natl. Acad. Sci. U S A , vol.105 , Issue.45 , pp. 17379-17383
    • Qian, S.1    Wang, W.2    Yang, L.3    Huang, H.W.4
  • 128
    • 0037009088 scopus 로고    scopus 로고
    • Contact sites between the outer and inner membrane of mitochondria - Role in protein transport
    • A.S. Reichert, and W. Neupert Contact sites between the outer and inner membrane of mitochondria - role in protein transport Biochim. Biophys. Acta (BBA) - Mol. Cell Res. 1592 1 2002 41 49
    • (2002) Biochim. Biophys. Acta (BBA) - Mol. Cell Res. , vol.1592 , Issue.1 , pp. 41-49
    • Reichert, A.S.1    Neupert, W.2
  • 129
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • J.-E. Ricci, R.A. Gottlieb, and D.R. Green Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis J. Cell Biol. 160 1 2003 65 75
    • (2003) J. Cell Biol. , vol.160 , Issue.1 , pp. 65-75
    • Ricci, J.-E.1    Gottlieb, R.A.2    Green, D.R.3
  • 130
    • 2942581328 scopus 로고    scopus 로고
    • Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex i of the electron transport chain
    • J.-E. Ricci, C. Muñoz-Pinedo, P. Fitzgerald, B. Bailly-Maitre, G.A. Perkins, N. Yadava, I.E. Scheffler, M.H. Ellisman, and D.R. Green Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain Cell 117 6 2004 773 786
    • (2004) Cell , vol.117 , Issue.6 , pp. 773-786
    • Ricci, J.-E.1    Muñoz-Pinedo, C.2    Fitzgerald, P.3    Bailly-Maitre, B.4    Perkins, G.A.5    Yadava, N.6    Scheffler, I.E.7    Ellisman, M.H.8    Green, D.R.9
  • 131
    • 0037421221 scopus 로고    scopus 로고
    • Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis
    • J.E. Ricci Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis J. Cell Biol. 160 1 2003 65 75
    • (2003) J. Cell Biol. , vol.160 , Issue.1 , pp. 65-75
    • Ricci, J.E.1
  • 132
    • 0037115740 scopus 로고    scopus 로고
    • Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein
    • X. Roucou, S. Montessuit, B. Antonsson, and J.C. Martinou Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein Biochem. J. 368 2002 915 921
    • (2002) Biochem. J. , vol.368 , pp. 915-921
    • Roucou, X.1    Montessuit, S.2    Antonsson, B.3    Martinou, J.C.4
  • 136
    • 70349524664 scopus 로고    scopus 로고
    • Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
    • Z.T. Schug, and E. Gottlieb Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis Biochim. Biophys. Acta (BBA) - Biomembr. 1788 10 2009 2022 2031
    • (2009) Biochim. Biophys. Acta (BBA) - Biomembr. , vol.1788 , Issue.10 , pp. 2022-2031
    • Schug, Z.T.1    Gottlieb, E.2
  • 137
  • 141
    • 49349105966 scopus 로고    scopus 로고
    • Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome c release
    • C. Sheridan, P. Delivani, S.P. Cullen, and S.J. Martin Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome c release Mol. Cell 31 4 2008 570 585
    • (2008) Mol. Cell , vol.31 , Issue.4 , pp. 570-585
    • Sheridan, C.1    Delivani, P.2    Cullen, S.P.3    Martin, S.J.4
  • 142
    • 0034623715 scopus 로고    scopus 로고
    • The lipids C2-and C16-ceramide form large stable channels. Implications for apoptosis
    • L.J. Siskind, and M. Colombini The lipids C2-and C16-ceramide form large stable channels. Implications for apoptosis J. Biol. Chem. 275 49 2000 38640 38644
    • (2000) J. Biol. Chem. , vol.275 , Issue.49 , pp. 38640-38644
    • Siskind, L.J.1    Colombini, M.2
  • 144
    • 0037178790 scopus 로고    scopus 로고
    • Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins
    • L.J. Siskind, R.N. Kolesnick, and M. Colombini Ceramide channels increase the permeability of the mitochondrial outer membrane to small proteins J. Biol. Chem. 277 30 2002 26796 26803
    • (2002) J. Biol. Chem. , vol.277 , Issue.30 , pp. 26796-26803
    • Siskind, L.J.1    Kolesnick, R.N.2    Colombini, M.3
  • 145
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • D.F. Suen, K.L. Norris, and R.J. Youle Mitochondrial dynamics and apoptosis Genes Dev. 22 12 2008 1577 1590
    • (2008) Genes Dev. , vol.22 , Issue.12 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 150
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p is a Wd repeat protein that interacts with the dynamin-related Gtpase Dnm1p, to trigger mitochondrial division
    • Q. Tieu, and J. Nunnari Mdv1p is a Wd repeat protein that interacts with the dynamin-related Gtpase Dnm1p, to trigger mitochondrial division J. Cell Biol. 151 2 2000 353 366
    • (2000) J. Cell Biol. , vol.151 , Issue.2 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 151
    • 84872432559 scopus 로고    scopus 로고
    • Sphingolipids in apoptosis
    • T. Tirodkar, and C. Voelkel-Johnson Sphingolipids in apoptosis Exp. Oncol. 34 3 2012 231 242
    • (2012) Exp. Oncol. , vol.34 , Issue.3 , pp. 231-242
    • Tirodkar, T.1    Voelkel-Johnson, C.2
  • 152
    • 84872298568 scopus 로고    scopus 로고
    • The C-terminal helix of Bcl-xL mediates Bax retrotranslocation from the mitochondria
    • F. Todt, Z. Cakir, F. Reichenbach, R.J. Youle, and F. Edlich The C-terminal helix of Bcl-xL mediates Bax retrotranslocation from the mitochondria Cell Death Differ. 20 2 2013 333 342
    • (2013) Cell Death Differ. , vol.20 , Issue.2 , pp. 333-342
    • Todt, F.1    Cakir, Z.2    Reichenbach, F.3    Youle, R.J.4    Edlich, F.5
  • 153
    • 3843125367 scopus 로고    scopus 로고
    • Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent protein, affects mitochondrial morphology and induces apoptosis
    • D. Tondera, A. Santel, R. Schwarzer, S. Dames, K. Giese, A. Klippel, and J. Kaufmann Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent protein, affects mitochondrial morphology and induces apoptosis J. Biol. Chem. 279 30 2004 31544 31555
    • (2004) J. Biol. Chem. , vol.279 , Issue.30 , pp. 31544-31555
    • Tondera, D.1    Santel, A.2    Schwarzer, R.3    Dames, S.4    Giese, K.5    Klippel, A.6    Kaufmann, J.7
  • 156
    • 84899512199 scopus 로고    scopus 로고
    • Membranes in motion: Mitochondrial dynamics and their role in apoptosis
    • B. Ugarte-Uribe, and A.J. Garcia-Saez Membranes in motion: mitochondrial dynamics and their role in apoptosis Biol. Chem. 395 3 2013 297 311
    • (2013) Biol. Chem. , vol.395 , Issue.3 , pp. 297-311
    • Ugarte-Uribe, B.1    Garcia-Saez, A.J.2
  • 157
    • 84896513685 scopus 로고    scopus 로고
    • Cardiolipin effects on membrane structure and dynamics
    • J.D. Unsay, K. Cosentino, Y. Subburaj, and A.J. García-Sáez Cardiolipin effects on membrane structure and dynamics Langmuir 29 51 2013 15878 15887
    • (2013) Langmuir , vol.29 , Issue.51 , pp. 15878-15887
    • Unsay, J.D.1    Cosentino, K.2    Subburaj, Y.3    García-Sáez, A.J.4
  • 158
    • 0020489067 scopus 로고
    • Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study
    • R. van Venetië, and A.J. Verkleij Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study Biochim. Biophys. Acta (BBA) - Biomembr. 692 3 1982 397 405
    • (1982) Biochim. Biophys. Acta (BBA) - Biomembr. , vol.692 , Issue.3 , pp. 397-405
    • Van Venetië, R.1    Verkleij, A.J.2
  • 159
    • 0032587982 scopus 로고    scopus 로고
    • Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange
    • M.G. Vander Heiden, N.S. Chandel, P.T. Schumacker, and C.B. Thompson Bcl-xL prevents cell death following growth factor withdrawal by facilitating mitochondrial ATP/ADP exchange Mol. Cell 3 2 1999 159 167
    • (1999) Mol. Cell , vol.3 , Issue.2 , pp. 159-167
    • Vander Heiden, M.G.1    Chandel, N.S.2    Schumacker, P.T.3    Thompson, C.B.4
  • 160
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • X. Wang The expanding role of mitochondria in apoptosis Genes Dev. 15 22 2001 2922 2933
    • (2001) Genes Dev. , vol.15 , Issue.22 , pp. 2922-2933
    • Wang, X.1
  • 161
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • S. Wasiak, R. Zunino, and H.M. McBride Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death J. Cell Biol. 177 3 2007 439 450
    • (2007) J. Cell Biol. , vol.177 , Issue.3 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 162
    • 68149100711 scopus 로고    scopus 로고
    • The changing shape of mitochondrial apoptosis
    • M. Wasilewski, and L. Scorrano The changing shape of mitochondrial apoptosis Trends Endocrinol. Metab. 20 6 2009 287 294
    • (2009) Trends Endocrinol. Metab. , vol.20 , Issue.6 , pp. 287-294
    • Wasilewski, M.1    Scorrano, L.2
  • 163
    • 84887024453 scopus 로고    scopus 로고
    • BIM-mediated membrane insertion of the BAK pore domain is an essential requirement for apoptosis
    • K. Weber, N. Harper, J. Schwabe, Gerald, and M. Cohen BIM-mediated
    • (2013) Cell Rep. , vol.5 , Issue.2 , pp. 409-420
    • Weber, K.1    Harper, N.2    Schwabe, J.3    Gerald4    Cohen, M.5
  • 164
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • M.C. Wei Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death Science 292 5517 2001 727 730
    • (2001) Science , vol.292 , Issue.5517 , pp. 727-730
    • Wei, M.C.1
  • 165
    • 84892412571 scopus 로고    scopus 로고
    • Building blocks of the apoptotic pore: How Bax and Bak are activated and oligomerize during apoptosis
    • D. Westphal, R.M. Kluck, and G. Dewson Building blocks of the apoptotic pore: how Bax and Bak are activated and oligomerize during apoptosis Cell Death Differ. 21 2 2013 196 205
    • (2013) Cell Death Differ. , vol.21 , Issue.2 , pp. 196-205
    • Westphal, D.1    Kluck, R.M.2    Dewson, G.3
  • 166
    • 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
    • S.N. Willis, L. Chen, G. Dewson, A. Wei, E. Naik, J.I. Fletcher, J.M. Adams, and D.C.S. Huang Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins Genes Dev. 19 11 2005 1294 1305
    • (2005) Genes Dev. , vol.19 , Issue.11 , 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.S.8
  • 168
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-Stave model or Toroidal model? A case study on melittin pores
    • L. Yang, T.A. Harroun, T.M. Weiss, L. Ding, and H.W. Huang Barrel-Stave model or Toroidal model? A case study on melittin pores Biophys. J. 81 3 2001 1475 1485
    • (2001) Biophys. J. , vol.81 , Issue.3 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 169
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Y. Yoon, E.W. Krueger, B.J. Oswald, and M.A. McNiven The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1 Mol. Cell. Biol. 23 15 2003 5409 5420
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.15 , pp. 5409-5420
    • Yoon, Y.1    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 170
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • R.J. Youle, and A. Strasser The BCL-2 protein family: opposing activities that mediate cell death Nat. Rev. Mol. Cell Biol. 9 1 2008 47 59
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , Issue.1 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 171
    • 84865544952 scopus 로고    scopus 로고
    • Mitochondrial fission, fusion, and stress
    • R.J. Youle, and A.M. van der Bliek Mitochondrial fission, fusion, and stress Science 337 6098 2012 1062 1065
    • (2012) Science , vol.337 , Issue.6098 , pp. 1062-1065
    • Youle, R.J.1    Van Der Bliek, A.M.2
  • 172
    • 77956511129 scopus 로고    scopus 로고
    • Different pathways lead to mitochondrial fragmentation during apoptotic and excitotoxic cell death in primary neurons
    • K.W. Young, L.G.P. Piñon, E.T.W. Bampton, and P. Nicotera Different pathways lead to mitochondrial fragmentation during apoptotic and excitotoxic cell death in primary neurons J. Biochem. Mol. Toxicol. 24 5 2010 335 341
    • (2010) J. Biochem. Mol. Toxicol. , vol.24 , Issue.5 , pp. 335-341
    • Young, K.W.1    Piñon, L.G.P.2    Bampton, E.T.W.3    Nicotera, P.4
  • 173
    • 33847012075 scopus 로고    scopus 로고
    • Mitochondrial fission is an upstream and required event for bax foci formation in response to nitric oxide in cortical neurons
    • H. Yuan, A.A. Gerencser, G. Liot, S.A. Lipton, M. Ellisman, G.A. Perkins, and E. Bossy-Wetzel Mitochondrial fission is an upstream and required event for bax foci formation in response to nitric oxide in cortical neurons Cell Death Differ. 14 3 2007 462 471
    • (2007) Cell Death Differ. , vol.14 , Issue.3 , pp. 462-471
    • Yuan, H.1    Gerencser, A.A.2    Liot, G.3    Lipton, S.A.4    Ellisman, M.5    Perkins, G.A.6    Bossy-Wetzel, E.7


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