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Volumn 17, Issue 1, 2007, Pages 6-12

Mitochondrial fragmentation in apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; ARTICLE; CELL ACTIVITY; CELL STRUCTURE; CYTOSOL; ENZYME ACTIVATION; FISSION NEUTRON; HUMAN; MITOCHONDRIAL FRAGMENTATION; MITOCHONDRIAL MEMBRANE; MITOCHONDRIAL OUTER MEMBRANE PERMEABILIZATION; MITOCHONDRIAL PERMEABILITY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN SECRETION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION;

EID: 33845885125     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2006.11.001     Document Type: Article
Times cited : (135)

References (59)
  • 1
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 2
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl S.J., and Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5 (2004) 897-907
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 3
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 (2004) 205-219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 4
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 5
    • 0344413426 scopus 로고    scopus 로고
    • Mitochondrial fission in apoptosis, neurodegeneration and aging
    • Bossy-Wetzel E., et al. Mitochondrial fission in apoptosis, neurodegeneration and aging. Curr. Opin. Cell Biol. 15 (2003) 706-716
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 706-716
    • Bossy-Wetzel, E.1
  • 6
    • 0035487808 scopus 로고    scopus 로고
    • The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis
    • Frank S., et al. The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev. Cell 1 (2001) 515-525
    • (2001) Dev. Cell , vol.1 , pp. 515-525
    • Frank, S.1
  • 7
    • 0043166392 scopus 로고    scopus 로고
    • Dynamics of mitochondrial morphology in healthy cells and during apoptosis
    • Karbowski M., and Youle R.J. Dynamics of mitochondrial morphology in healthy cells and during apoptosis. Cell Death Differ. 10 (2003) 870-880
    • (2003) Cell Death Differ. , vol.10 , pp. 870-880
    • Karbowski, M.1    Youle, R.J.2
  • 9
    • 18444400187 scopus 로고    scopus 로고
    • Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis
    • Germain M., et al. Endoplasmic reticulum BIK initiates DRP1-regulated remodelling of mitochondrial cristae during apoptosis. EMBO J. 24 (2005) 1546-1556
    • (2005) EMBO J. , vol.24 , pp. 1546-1556
    • Germain, M.1
  • 10
    • 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
    • Breckenridge D.G., et al. Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J. Cell Biol. 160 (2003) 1115-1127
    • (2003) J. Cell Biol. , vol.160 , pp. 1115-1127
    • Breckenridge, D.G.1
  • 11
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee Y.J., et al. Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol. Biol. Cell 15 (2004) 5001-5011
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1
  • 12
    • 21644455319 scopus 로고    scopus 로고
    • Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization
    • Neuspiel M., et al. Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization. J. Biol. Chem. 280 (2005) 25060-25070
    • (2005) J. Biol. Chem. , vol.280 , pp. 25060-25070
    • Neuspiel, M.1
  • 13
    • 10644296253 scopus 로고    scopus 로고
    • Fzo1, a protein involved in mitochondrial fusion, inhibits apoptosis
    • Sugioka R., et al. Fzo1, a protein involved in mitochondrial fusion, inhibits apoptosis. J. Biol. Chem. 279 (2004) 52726-52734
    • (2004) J. Biol. Chem. , vol.279 , pp. 52726-52734
    • Sugioka, R.1
  • 14
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D., et al. Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J. Biol. Chem. 280 (2005) 35742-35750
    • (2005) J. Biol. Chem. , vol.280 , pp. 35742-35750
    • Arnoult, D.1
  • 15
    • 28444487509 scopus 로고    scopus 로고
    • Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death
    • Arnoult D., et al. Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death. Curr. Biol. 15 (2005) 2112-2118
    • (2005) Curr. Biol. , vol.15 , pp. 2112-2118
    • Arnoult, D.1
  • 16
    • 33749623421 scopus 로고    scopus 로고
    • Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis
    • Parone P.A., et al. Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis. Mol. Cell. Biol. 26 (2006) 7397-7408
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 7397-7408
    • Parone, P.A.1
  • 17
    • 33644859410 scopus 로고    scopus 로고
    • Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics
    • Delivani P., et al. Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics. Mol. Cell 21 (2006) 761-773
    • (2006) Mol. Cell , vol.21 , pp. 761-773
    • Delivani, P.1
  • 18
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza C., et al. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126 (2006) 177-189
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1
  • 19
    • 0034870228 scopus 로고    scopus 로고
    • Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells
    • Gao W., et al. Temporal relationship between cytochrome c release and mitochondrial swelling during UV-induced apoptosis in living HeLa cells. J. Cell Sci. 114 (2001) 2855-2862
    • (2001) J. Cell Sci. , vol.114 , pp. 2855-2862
    • Gao, W.1
  • 20
    • 0031795088 scopus 로고    scopus 로고
    • Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential
    • Zhuang J., et al. Apoptosis, in human monocytic THP.1 cells, results in the release of cytochrome c from mitochondria prior to their ultracondensation, formation of outer membrane discontinuities and reduction in inner membrane potential. Cell Death Differ. 5 (1998) 953-962
    • (1998) Cell Death Differ. , vol.5 , pp. 953-962
    • Zhuang, J.1
  • 21
    • 0032778902 scopus 로고    scopus 로고
    • Redistribution of cytochrome c precedes the caspase-dependent formation of ultracondensed mitochondria, with a reduced inner membrane potential, in apoptotic monocytes
    • Dinsdale D., et al. Redistribution of cytochrome c precedes the caspase-dependent formation of ultracondensed mitochondria, with a reduced inner membrane potential, in apoptotic monocytes. Am. J. Pathol. 155 (1999) 607-618
    • (1999) Am. J. Pathol. , vol.155 , pp. 607-618
    • Dinsdale, D.1
  • 22
    • 16544365664 scopus 로고    scopus 로고
    • Temporal dissection of Bax-induced events leading to fission of the single mitochondrion in Trypanosoma brucei
    • Esseiva A.C., et al. Temporal dissection of Bax-induced events leading to fission of the single mitochondrion in Trypanosoma brucei. EMBO Rep. 5 (2004) 268-273
    • (2004) EMBO Rep. , vol.5 , pp. 268-273
    • Esseiva, A.C.1
  • 23
    • 0037164813 scopus 로고    scopus 로고
    • Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis
    • Karbowski M., et al. Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J. Cell Biol. 159 (2002) 931-938
    • (2002) J. Cell Biol. , vol.159 , pp. 931-938
    • Karbowski, M.1
  • 24
    • 0030792850 scopus 로고    scopus 로고
    • Mitochondrial proliferation and paradoxical membrane depolarization during terminal differentiation and apoptosis in a human colon carcinoma cell line
    • Mancini M., et al. Mitochondrial proliferation and paradoxical membrane depolarization during terminal differentiation and apoptosis in a human colon carcinoma cell line. J. Cell Biol. 138 (1997) 449-469
    • (1997) J. Cell Biol. , vol.138 , pp. 449-469
    • Mancini, M.1
  • 25
    • 0035355341 scopus 로고    scopus 로고
    • The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action
    • Pinton P., et al. The Ca2+ concentration of the endoplasmic reticulum is a key determinant of ceramide-induced apoptosis: significance for the molecular mechanism of Bcl-2 action. EMBO J. 20 (2001) 2690-2701
    • (2001) EMBO J. , vol.20 , pp. 2690-2701
    • Pinton, P.1
  • 26
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E., et al. Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 12 (2001) 2245-2256
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1
  • 27
    • 4944222095 scopus 로고    scopus 로고
    • Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+-mediated apoptosis
    • Szabadkai G., et al. Drp-1-dependent division of the mitochondrial network blocks intraorganellar Ca2+ waves and protects against Ca2+-mediated apoptosis. Mol. Cell 16 (2004) 59-68
    • (2004) Mol. Cell , vol.16 , pp. 59-68
    • Szabadkai, G.1
  • 28
    • 0032547754 scopus 로고    scopus 로고
    • A human dynamin-related protein controls the distribution of mitochondria
    • Smirnova E., et al. A human dynamin-related protein controls the distribution of mitochondria. J. Cell Biol. 143 (1998) 351-358
    • (1998) J. Cell Biol. , vol.143 , pp. 351-358
    • Smirnova, E.1
  • 29
    • 0141592470 scopus 로고    scopus 로고
    • hFis1, a novel component of the mammalian mitochondrial fission machinery
    • James D.I., et al. hFis1, a novel component of the mammalian mitochondrial fission machinery. J. Biol. Chem. 278 (2003) 36373-36379
    • (2003) J. Biol. Chem. , vol.278 , pp. 36373-36379
    • James, D.I.1
  • 30
    • 33750526651 scopus 로고    scopus 로고
    • The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce Apoptosis
    • Alirol E., et al. The mitochondrial fission protein hFis1 requires the endoplasmic reticulum gateway to induce Apoptosis. Mol. Biol. Cell 17 (2006) 4593-4605
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4593-4605
    • Alirol, E.1
  • 31
    • 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 433 (2005) 754-760
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1
  • 32
    • 27544446991 scopus 로고    scopus 로고
    • Life in the balance: how BH3-only proteins induce apoptosis
    • Willis S.N., and Adams J.M. Life in the balance: how BH3-only proteins induce apoptosis. Curr. Opin. Cell Biol. 17 (2005) 617-625
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 617-625
    • Willis, S.N.1    Adams, J.M.2
  • 33
    • 0033781027 scopus 로고    scopus 로고
    • The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant
    • Goldstein J.C., et al. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nat. Cell Biol. 2 (2000) 156-162
    • (2000) Nat. Cell Biol. , vol.2 , pp. 156-162
    • Goldstein, J.C.1
  • 34
    • 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 2 (2002) 55-67
    • (2002) Dev. Cell , vol.2 , pp. 55-67
    • Scorrano, L.1
  • 35
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat S., et al. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 126 (2006) 163-175
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1
  • 36
    • 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. 139 (1997) 1281-1292
    • (1997) J. Cell Biol. , vol.139 , pp. 1281-1292
    • Wolter, K.G.1
  • 37
    • 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. 153 (2001) 1265-1276
    • (2001) J. Cell Biol. , vol.153 , pp. 1265-1276
    • Nechushtan, A.1
  • 38
    • 0001777212 scopus 로고    scopus 로고
    • Protein translocation into mitochondria: the role of TIM complexes
    • Bauer M.F., et al. Protein translocation into mitochondria: the role of TIM complexes. Trends Cell Biol. 10 (2000) 25-31
    • (2000) Trends Cell Biol. , vol.10 , pp. 25-31
    • Bauer, M.F.1
  • 39
    • 1242307475 scopus 로고    scopus 로고
    • Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis
    • Karbowski M., et al. Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J. Cell Biol. 164 (2004) 493-499
    • (2004) J. Cell Biol. , vol.164 , pp. 493-499
    • Karbowski, M.1
  • 40
    • 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 443 (2006) 658-662
    • (2006) Nature , vol.443 , pp. 658-662
    • Karbowski, M.1
  • 41
    • 3843125367 scopus 로고    scopus 로고
    • Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent protein, affects mitochondrial morphology and induces apoptosis
    • Tondera D., et al. Knockdown of MTP18, a novel phosphatidylinositol 3-kinase-dependent protein, affects mitochondrial morphology and induces apoptosis. J. Biol. Chem. 279 (2004) 31544-31555
    • (2004) J. Biol. Chem. , vol.279 , pp. 31544-31555
    • Tondera, D.1
  • 42
    • 2542629734 scopus 로고    scopus 로고
    • Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria
    • Arnoult D., et al. Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 7988-7993
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 7988-7993
    • Arnoult, D.1
  • 43
    • 0037213306 scopus 로고    scopus 로고
    • Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis
    • McCormick A.L., et al. Disruption of mitochondrial networks by the human cytomegalovirus UL37 gene product viral mitochondrion-localized inhibitor of apoptosis. J. Virol. 77 (2003) 631-641
    • (2003) J. Virol. , vol.77 , pp. 631-641
    • McCormick, A.L.1
  • 44
    • 0035814933 scopus 로고    scopus 로고
    • Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis
    • Xue L., et al. Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis. Curr. Biol. 11 (2001) 361-365
    • (2001) Curr. Biol. , vol.11 , pp. 361-365
    • Xue, L.1
  • 45
    • 33748028841 scopus 로고    scopus 로고
    • Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons
    • Barsoum M.J., et al. Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons. EMBO J. 25 (2006) 3900-3911
    • (2006) EMBO J. , vol.25 , pp. 3900-3911
    • Barsoum, M.J.1
  • 46
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: a double-edged sword
    • Shintani T., and Klionsky D.J. Autophagy in health and disease: a double-edged sword. Science 306 (2004) 990-995
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 47
    • 0032870475 scopus 로고    scopus 로고
    • Autophagy is activated by apoptotic signalling in sympathetic neurons: an alternative mechanism of death execution
    • Xue L., et al. Autophagy is activated by apoptotic signalling in sympathetic neurons: an alternative mechanism of death execution. Mol. Cell. Neurosci. 14 (1999) 180-198
    • (1999) Mol. Cell. Neurosci. , vol.14 , pp. 180-198
    • Xue, L.1
  • 48
    • 0036634059 scopus 로고    scopus 로고
    • Tantalizing Thanatos: unexpected links in death pathways
    • Cohen I., et al. Tantalizing Thanatos: unexpected links in death pathways. Trends Cell Biol. 12 (2002) 293-295
    • (2002) Trends Cell Biol. , vol.12 , pp. 293-295
    • Cohen, I.1
  • 49
    • 8644284924 scopus 로고    scopus 로고
    • Mitochondrial fission proteins regulate programmed cell death in yeast
    • Fannjiang Y., et al. Mitochondrial fission proteins regulate programmed cell death in yeast. Genes Dev. 18 (2004) 2785-2797
    • (2004) Genes Dev. , vol.18 , pp. 2785-2797
    • Fannjiang, Y.1
  • 50
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A., et al. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13 (1999) 1899-1911
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1
  • 51
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: how Pandora's box opens
    • Zamzami N., and Kroemer G. The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell Biol. 2 (2001) 67-71
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 53
    • 4143088384 scopus 로고    scopus 로고
    • Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1
    • Zhu P.P., et al. Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1. J. Biol. Chem. 279 (2004) 35967-35974
    • (2004) J. Biol. Chem. , vol.279 , pp. 35967-35974
    • Zhu, P.P.1
  • 54
    • 0043092647 scopus 로고    scopus 로고
    • The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1
    • Yoon Y., et al. The mitochondrial protein hFis1 regulates mitochondrial fission in mammalian cells through an interaction with the dynamin-like protein DLP1. Mol. Cell. Biol. 23 (2003) 5409-5420
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5409-5420
    • Yoon, Y.1
  • 55
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H., et al. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160 (2003) 189-200
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1
  • 56
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A., et al. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 278 (2003) 7743-7746
    • (2003) J. Biol. Chem. , vol.278 , pp. 7743-7746
    • Olichon, A.1
  • 57
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo M., et al. Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115 (2002) 1663-1674
    • (2002) J. Cell Sci. , vol.115 , pp. 1663-1674
    • Rojo, M.1
  • 58
    • 0035683581 scopus 로고    scopus 로고
    • Mutation spectrum and splicing variants in the OPA1 gene
    • Delettre C., et al. Mutation spectrum and splicing variants in the OPA1 gene. Hum. Genet. 109 (2001) 584-591
    • (2001) Hum. Genet. , vol.109 , pp. 584-591
    • Delettre, C.1
  • 59
    • 8644270474 scopus 로고    scopus 로고
    • OPA1 requires mitofusin 1 to promote mitochondrial fusion
    • Cipolat S., et al. OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 15927-15932
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15927-15932
    • Cipolat, S.1


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