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Volumn 1783, Issue 7, 2008, Pages 1272-1279

Mitochondrial death pathways in yeast and mammalian cells

Author keywords

Caspase; Cytochrome c; Dnm1; Drp1; Fission; Fragmentation; Fusion; Metacaspase">; Mitochondria; Yeast apoptosis

Indexed keywords

APOPTOSIS; CELL ACTIVITY; CELL DEATH; CELL STRUCTURE; FRAGMENTATION REACTION; FUNGAL GENE; MAMMAL CELL; MITOCHONDRION; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; REVIEW; YEAST;

EID: 46549086527     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.04.012     Document Type: Review
Times cited : (59)

References (144)
  • 1
    • 0036536714 scopus 로고    scopus 로고
    • Mitochondrial dynamics and division in budding yeast
    • Shaw J.M., and Nunnari J. Mitochondrial dynamics and division in budding yeast. Trends Cell Biol. 12 (2002) 178-184.
    • (2002) Trends Cell Biol. , vol.12
    • Shaw, J.M.1    Nunnari, J.2
  • 2
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S., Lackner L., and Nunnari J. The machines that divide and fuse mitochondria. Ann. Rev. Biochem. 76 (2007) 751-780
    • (2007) Ann. Rev. Biochem. , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 3
    • 45449111156 scopus 로고    scopus 로고
    • Berman, S.B., Pineda, F.J., and Hardwick, J.M., (in press) Mitochondrial fission and fusion dynamics: the long and short of it. Cell Death Differ. (available online April 25, 2008).
    • Berman, S.B., Pineda, F.J., and Hardwick, J.M., (in press) Mitochondrial fission and fusion dynamics: the long and short of it. Cell Death Differ. (available online April 25, 2008).
  • 5
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • Chen H., and Chan D.C. Emerging functions of mammalian mitochondrial fusion and fission. Hum. Mol. Gen. 14 Spec No. 2 (2005) R283-R289
    • (2005) Hum. Mol. Gen. , vol.14 , Issue.Spec 2
    • Chen, H.1    Chan, D.C.2
  • 6
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • Chen H., McCaffery J.M., and Chan D.C. Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130 (2007) 548-562
    • (2007) Cell , vol.130 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 8
    • 0037174142 scopus 로고    scopus 로고
    • Programmed death in yeast as adaptation?
    • Skulachev V.P. Programmed death in yeast as adaptation?. FEBS Lett. 528 (2002) 23-26
    • (2002) FEBS Lett. , vol.528 , pp. 23-26
    • Skulachev, V.P.1
  • 11
    • 9944222855 scopus 로고    scopus 로고
    • Induction of programmed cell death in lily by the fungal pathogen Botrytis elliptica
    • Van Baarlen P., Staats M., and Van Kan J.A.L. Induction of programmed cell death in lily by the fungal pathogen Botrytis elliptica. Mol. Plant Pathol. 5 (2004) 559-574
    • (2004) Mol. Plant Pathol. , vol.5 , pp. 559-574
    • Van Baarlen, P.1    Staats, M.2    Van Kan, J.A.L.3
  • 12
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren A.G., O'Rourke K., Aravind L.A., Pisabarro M.T., Seshagiri S., Koonin E.V., and Dixit V.M. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol. Cell 6 (2000) 961-967
    • (2000) Mol. Cell , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.A.3    Pisabarro, M.T.4    Seshagiri, S.5    Koonin, E.V.6    Dixit, V.M.7
  • 13
    • 0030667206 scopus 로고    scopus 로고
    • A yeast mutant showing diagnostic markers of early and late apoptosis
    • Madeo F., Frohlich E., and Frohlich K.U. A yeast mutant showing diagnostic markers of early and late apoptosis. J. Cell Biol. 139 (1997) 729-734
    • (1997) J. Cell Biol. , vol.139 , pp. 729-734
    • Madeo, F.1    Frohlich, E.2    Frohlich, K.U.3
  • 15
    • 0034807841 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae commits to a programmed cell death process in response to acetic acid
    • Ludovico P., Sousa M.J., Silva M.T., Leao C., and Corte-Real M. Saccharomyces cerevisiae commits to a programmed cell death process in response to acetic acid. Microbiology, (Reading, England) 147 (2001) 2409-2415
    • (2001) Microbiology, (Reading, England) , vol.147 , pp. 2409-2415
    • Ludovico, P.1    Sousa, M.J.2    Silva, M.T.3    Leao, C.4    Corte-Real, M.5
  • 21
    • 33745377897 scopus 로고    scopus 로고
    • Yeast AMID homologue Ndi1p displays respiration-restricted apoptotic activity and is involved in chronological aging
    • Li W., Sun L., Liang Q., Wang J., Mo W., and Zhou B. Yeast AMID homologue Ndi1p displays respiration-restricted apoptotic activity and is involved in chronological aging. Mol. Biol. Cell 17 (2006) 1802-1811
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1802-1811
    • Li, W.1    Sun, L.2    Liang, Q.3    Wang, J.4    Mo, W.5    Zhou, B.6
  • 22
    • 28744436967 scopus 로고    scopus 로고
    • A possible cooperation of SOD1 and cytochrome c in mitochondria-dependent apoptosis
    • Li Q., Sato E.F., Kira Y., Nishikawa M., Utsumi K., and Inoue M. A possible cooperation of SOD1 and cytochrome c in mitochondria-dependent apoptosis. Free Radic. Biol. Med. 40 (2006) 173-181
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 173-181
    • Li, Q.1    Sato, E.F.2    Kira, Y.3    Nishikawa, M.4    Utsumi, K.5    Inoue, M.6
  • 24
    • 0347917233 scopus 로고    scopus 로고
    • The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis
    • Fahrenkrog B., Sauder U., and Aebi U. The S. cerevisiae HtrA-like protein Nma111p is a nuclear serine protease that mediates yeast apoptosis. J. Cell Sci. 117 (2004) 115-126
    • (2004) J. Cell Sci. , vol.117 , pp. 115-126
    • Fahrenkrog, B.1    Sauder, U.2    Aebi, U.3
  • 29
    • 33845408268 scopus 로고    scopus 로고
    • YCA1 participates in the acetic acid induced yeast programmed cell death also in a manner unrelated to its caspase-like activity
    • Guaragnella N., Pereira C., Sousa M.J., Antonacci L., Passarella S., Corte-Real M., Marra E., and Giannattasio S. YCA1 participates in the acetic acid induced yeast programmed cell death also in a manner unrelated to its caspase-like activity. FEBS Lett. 580 (2006) 6880-6884
    • (2006) FEBS Lett. , vol.580 , pp. 6880-6884
    • Guaragnella, N.1    Pereira, C.2    Sousa, M.J.3    Antonacci, L.4    Passarella, S.5    Corte-Real, M.6    Marra, E.7    Giannattasio, S.8
  • 30
    • 23744458531 scopus 로고    scopus 로고
    • Viruses activate a genetically conserved cell death pathway in a unicellular organism
    • Ivanovska I., and Hardwick J.M. Viruses activate a genetically conserved cell death pathway in a unicellular organism. J. Cell Biol. 170 (2005) 391-399
    • (2005) J. Cell Biol. , vol.170 , pp. 391-399
    • Ivanovska, I.1    Hardwick, J.M.2
  • 34
    • 0038012805 scopus 로고    scopus 로고
    • Inactivation of Cdc13p triggers MEC1-dependent apoptotic signals in yeast
    • Qi H., Li T.K., Kuo D., Nur E.K.A., and Liu L.F. Inactivation of Cdc13p triggers MEC1-dependent apoptotic signals in yeast. J. Biol. Chem. 278 (2003) 15136-15141
    • (2003) J. Biol. Chem. , vol.278 , pp. 15136-15141
    • Qi, H.1    Li, T.K.2    Kuo, D.3    Nur, E.K.A.4    Liu, L.F.5
  • 35
    • 13444266047 scopus 로고    scopus 로고
    • Viral killer toxins induce caspase-mediated apoptosis in yeast
    • Reiter J., Herker E., Madeo F., and Schmitt M.J. Viral killer toxins induce caspase-mediated apoptosis in yeast. J. Cell Biol. 168 (2005) 353-358
    • (2005) J. Cell Biol. , vol.168 , pp. 353-358
    • Reiter, J.1    Herker, E.2    Madeo, F.3    Schmitt, M.J.4
  • 37
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A., and Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391 (1998) 43-50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 38
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara S., Aoto M., Eguchi Y., Imamoto N., Yoneda Y., and Tsujimoto Y. Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature 401 (1999) 168-173
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 39
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H., Zhu H., Xu C.J., and Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 40
    • 0037235145 scopus 로고    scopus 로고
    • Multiple mediators of plant programmed cell death: interplay of conserved cell death mechanisms and plant-specific regulators
    • Hoeberichts F.A., and Woltering E.J. Multiple mediators of plant programmed cell death: interplay of conserved cell death mechanisms and plant-specific regulators. BioEssays 25 (2003) 47-57
    • (2003) BioEssays , vol.25 , pp. 47-57
    • Hoeberichts, F.A.1    Woltering, E.J.2
  • 41
    • 46549090137 scopus 로고    scopus 로고
    • Cleavage of Mcd1 by caspase-like protease Esp1 promotes apoptosis in budding yeast
    • Yang H., Ren Q., and Zhang Z. Cleavage of Mcd1 by caspase-like protease Esp1 promotes apoptosis in budding yeast. Mol. Biol. Cell. 19 (2008) 2127-2134
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2127-2134
    • Yang, H.1    Ren, Q.2    Zhang, Z.3
  • 44
    • 0029032660 scopus 로고
    • Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax
    • Hanada M., Aime-Sempe C., Sato T., and Reed J.C. Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax. J. Biol. Chem. 270 (1995) 11962-11969
    • (1995) J. Biol. Chem. , vol.270 , pp. 11962-11969
    • Hanada, M.1    Aime-Sempe, C.2    Sato, T.3    Reed, J.C.4
  • 45
    • 33846024762 scopus 로고    scopus 로고
    • Evaluation of the roles of apoptosis, autophagy, and mitophagy in the loss of plating efficiency induced by Bax expression in yeast
    • Kissova I., Plamondon L.T., Brisson L., Priault M., Renouf V., Schaeffer J., Camougrand N., and Manon S. Evaluation of the roles of apoptosis, autophagy, and mitophagy in the loss of plating efficiency induced by Bax expression in yeast. J. Biol. Chem. 281 (2006) 36187-36197
    • (2006) J. Biol. Chem. , vol.281 , pp. 36187-36197
    • Kissova, I.1    Plamondon, L.T.2    Brisson, L.3    Priault, M.4    Renouf, V.5    Schaeffer, J.6    Camougrand, N.7    Manon, S.8
  • 47
    • 0034666388 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe Rad9 contains a BH3-like region and interacts with the anti-apoptotic protein Bcl-2
    • Komatsu K., Hopkins K.M., Lieberman H.B., and Wang H. Schizosaccharomyces pombe Rad9 contains a BH3-like region and interacts with the anti-apoptotic protein Bcl-2. FEBS Lett. 481 (2000) 122-126
    • (2000) FEBS Lett. , vol.481 , pp. 122-126
    • Komatsu, K.1    Hopkins, K.M.2    Lieberman, H.B.3    Wang, H.4
  • 48
    • 33947727119 scopus 로고    scopus 로고
    • Structure of M11L: a myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2
    • Douglas A.E., Corbett K.D., Berger J.M., McFadden G., and Handel T.M. Structure of M11L: a myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2. Protein Sci. 16 (2007) 695-703
    • (2007) Protein Sci. , vol.16 , pp. 695-703
    • Douglas, A.E.1    Corbett, K.D.2    Berger, J.M.3    McFadden, G.4    Handel, T.M.5
  • 49
    • 33947304650 scopus 로고    scopus 로고
    • A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak
    • Kvansakul M., van Delft M.F., Lee E.F., Gulbis J.M., Fairlie W.D., Huang D.C., and Colman P.M. A structural viral mimic of prosurvival Bcl-2: a pivotal role for sequestering proapoptotic Bax and Bak. Mol. Cell 25 (2007) 933-942
    • (2007) Mol. Cell , vol.25 , pp. 933-942
    • Kvansakul, M.1    van Delft, M.F.2    Lee, E.F.3    Gulbis, J.M.4    Fairlie, W.D.5    Huang, D.C.6    Colman, P.M.7
  • 51
    • 0037007151 scopus 로고    scopus 로고
    • Pheromone induces programmed cell death in S. cerevisiae
    • Severin F.F., and Hyman A.A. Pheromone induces programmed cell death in S. cerevisiae. Curr. Biol. 12 (2002) R233-R235
    • (2002) Curr. Biol. , vol.12
    • Severin, F.F.1    Hyman, A.A.2
  • 53
    • 1642491749 scopus 로고    scopus 로고
    • Chronological aging-independent replicative life span regulation by Msn2/Msn4 and Sod2 in Saccharomyces cerevisiae
    • Fabrizio P., Pletcher S.D., Minois N., Vaupel J.W., and Longo V.D. Chronological aging-independent replicative life span regulation by Msn2/Msn4 and Sod2 in Saccharomyces cerevisiae. FEBS Lett. 557 (2004) 136-142
    • (2004) FEBS Lett. , vol.557 , pp. 136-142
    • Fabrizio, P.1    Pletcher, S.D.2    Minois, N.3    Vaupel, J.W.4    Longo, V.D.5
  • 55
    • 7744246084 scopus 로고    scopus 로고
    • Mitochondrial programmed cell death pathways in yeast
    • Hardwick J.M., and Cheng W.C. Mitochondrial programmed cell death pathways in yeast. Dev. Cell 7 (2004) 630-632
    • (2004) Dev. Cell , vol.7 , pp. 630-632
    • Hardwick, J.M.1    Cheng, W.C.2
  • 57
  • 59
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., and Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112 (2003) 481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 60
    • 0036863609 scopus 로고    scopus 로고
    • Bax, along with lipid conspirators, allows cytochrome c to escape mitochondria
    • Hardwick J.M., and Polster B.M. Bax, along with lipid conspirators, allows cytochrome c to escape mitochondria. Mol. Cell 10 (2002) 963-965
    • (2002) Mol. Cell , vol.10 , pp. 963-965
    • Hardwick, J.M.1    Polster, B.M.2
  • 62
    • 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., Stojanovic M., Marcellus R.C., and Shore G.C. 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    Stojanovic, M.2    Marcellus, R.C.3    Shore, G.C.4
  • 63
    • 34347386472 scopus 로고    scopus 로고
    • Thapsigargin induces biphasic fragmentation of mitochondria through calcium-mediated mitochondrial fission and apoptosis
    • Hom J.R., Gewandter J.S., Michael L., Sheu S.S., and Yoon Y. Thapsigargin induces biphasic fragmentation of mitochondria through calcium-mediated mitochondrial fission and apoptosis. J. Cell. Physiol. 212 (2007) 498-508
    • (2007) J. Cell. Physiol. , vol.212 , pp. 498-508
    • Hom, J.R.1    Gewandter, J.S.2    Michael, L.3    Sheu, S.S.4    Yoon, Y.5
  • 64
    • 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., Smith V.L., Chow D., and Mocarski E.S. 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    Smith, V.L.2    Chow, D.3    Mocarski, E.S.4
  • 65
    • 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., Ferrari D., Rapizzi E., Di Virgilio F., Pozzan T., and Rizzuto R. 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    Ferrari, D.2    Rapizzi, E.3    Di Virgilio, F.4    Pozzan, T.5    Rizzuto, R.6
  • 67
    • 34250198994 scopus 로고    scopus 로고
    • Ethanol-induced death in yeast exhibits features of apoptosis mediated by mitochondrial fission pathway
    • Kitagaki H., Araki Y., Funato K., and Shimoi H. Ethanol-induced death in yeast exhibits features of apoptosis mediated by mitochondrial fission pathway. FEBS Lett. 581 (2007) 2935-2942
    • (2007) FEBS Lett. , vol.581 , pp. 2935-2942
    • Kitagaki, H.1    Araki, Y.2    Funato, K.3    Shimoi, H.4
  • 68
    • 10744222249 scopus 로고    scopus 로고
    • V.P., Skulachev, L.E., Bakeeva, B.V., Chernyak, L.V., Domnina, A.A., Minin, O.Y., Pletjushkina, V.B., Saprunova, I.V., Skulachev, V.G., Tsyplenkova, J.M., Vasiliev, L.S., Yaguzhinsky, D.B., Zorov, Thread-grain transition of mitochondrial reticulum as a step of mitoptosis and apoptosis. Mol. Cell. Biochem. 256-257, (2004), 341-358.
    • V.P., Skulachev, L.E., Bakeeva, B.V., Chernyak, L.V., Domnina, A.A., Minin, O.Y., Pletjushkina, V.B., Saprunova, I.V., Skulachev, V.G., Tsyplenkova, J.M., Vasiliev, L.S., Yaguzhinsky, D.B., Zorov, Thread-grain transition of mitochondrial reticulum as a step of mitoptosis and apoptosis. Mol. Cell. Biochem. 256-257, (2004), 341-358.
  • 70
    • 34247603036 scopus 로고    scopus 로고
    • Role of mitochondrial remodeling in programmed cell death in Drosophila melanogaster
    • Goyal G., Fell B., Sarin A., Youle R.J., and Sriram V. Role of mitochondrial remodeling in programmed cell death in Drosophila melanogaster. Dev. Cell 12 (2007) 807-816
    • (2007) Dev. Cell , vol.12 , pp. 807-816
    • Goyal, G.1    Fell, B.2    Sarin, A.3    Youle, R.J.4    Sriram, V.5
  • 71
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia R., Grote P., Westermann B., and Conradt B. 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    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 72
    • 19444386896 scopus 로고    scopus 로고
    • Apoptosis in Drosophila: neither fish nor fowl, (nor man, nor worm)
    • Kornbluth S., and White K. Apoptosis in Drosophila: neither fish nor fowl, (nor man, nor worm). J. Cell Sci. 118 (2005) 1779-1787
    • (2005) J. Cell Sci. , vol.118 , pp. 1779-1787
    • Kornbluth, S.1    White, K.2
  • 73
    • 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., Simoni A.M., Chami M., Wieckowski M.R., Youle R.J., and Rizzuto R. 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    Simoni, A.M.2    Chami, M.3    Wieckowski, M.R.4    Youle, R.J.5    Rizzuto, R.6
  • 74
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • Arama E., Agapite J., and Steller H. Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila. Dev. Cell 4 (2003) 687-697
    • (2003) Dev. Cell , vol.4 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 75
    • 0036678040 scopus 로고    scopus 로고
    • Cytochrome c release and mitochondria involvement in programmed cell death induced by acetic acid in Saccharomyces cerevisiae
    • Ludovico P., Rodrigues F., Almeida A., Silva M.T., Barrientos A., and Corte-Real M. Cytochrome c release and mitochondria involvement in programmed cell death induced by acetic acid in Saccharomyces cerevisiae. Mol. Biol. Cell 13 (2002) 2598-2606
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2598-2606
    • Ludovico, P.1    Rodrigues, F.2    Almeida, A.3    Silva, M.T.4    Barrientos, A.5    Corte-Real, M.6
  • 77
    • 0035206962 scopus 로고    scopus 로고
    • Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1
    • Yamaki M., Umehara T., Chimura T., and Horikoshi M. Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1. Genes Cells 6 (2001) 1043-1054
    • (2001) Genes Cells , vol.6 , pp. 1043-1054
    • Yamaki, M.1    Umehara, T.2    Chimura, T.3    Horikoshi, M.4
  • 79
    • 35449002545 scopus 로고    scopus 로고
    • Another piece of the puzzle of apoptotic cytochrome c release
    • Lawen A. Another piece of the puzzle of apoptotic cytochrome c release. Mol. Microbiol. 66 (2007) 553-556
    • (2007) Mol. Microbiol. , vol.66 , pp. 553-556
    • Lawen, A.1
  • 80
    • 35448982828 scopus 로고    scopus 로고
    • ADP/ATP carrier is required for mitochondrial outer membrane permeabilization and cytochrome c release in yeast apoptosis
    • Pereira C., Camougrand N., Manon S., Sousa M.J., and Corte-Real M. ADP/ATP carrier is required for mitochondrial outer membrane permeabilization and cytochrome c release in yeast apoptosis. Mol. Microbiol. 66 (2007) 571-582
    • (2007) Mol. Microbiol. , vol.66 , pp. 571-582
    • Pereira, C.1    Camougrand, N.2    Manon, S.3    Sousa, M.J.4    Corte-Real, M.5
  • 82
    • 33745934410 scopus 로고    scopus 로고
    • Which came first, the cytochrome c release or the mitochondrial fission?
    • Martinou J.C., and Youle R.J. Which came first, the cytochrome c release or the mitochondrial fission?. Cell Death Differ. 13 (2006) 1291-1295
    • (2006) Cell Death Differ. , vol.13 , pp. 1291-1295
    • Martinou, J.C.1    Youle, R.J.2
  • 83
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A., Smith C.L., Lamensdorf I., Yoon S.H., and Youle R.J. 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    Smith, C.L.2    Lamensdorf, I.3    Yoon, S.H.4    Youle, R.J.5
  • 85
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee Y.J., Jeong S.Y., Karbowski M., Smith C.L., and Youle R.J. 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    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 86
    • 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., Baricault L., Gas N., Guillou E., Valette A., Belenguer P., and Lenaers G. 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    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 87
    • 10644296253 scopus 로고    scopus 로고
    • Fzo1, a protein involved in mitochondrial fusion, inhibits apoptosis
    • Sugioka R., Shimizu S., and Tsujimoto Y. 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    Shimizu, S.2    Tsujimoto, Y.3
  • 88
    • 21644455319 scopus 로고    scopus 로고
    • Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization
    • Neuspiel M., Zunino R., Gangaraju S., Rippstein P., and McBride H. 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    Zunino, R.2    Gangaraju, S.3    Rippstein, P.4    McBride, H.5
  • 89
    • 33746933765 scopus 로고    scopus 로고
    • The many shapes of mitochondrial death
    • Cereghetti G.M., and Scorrano L. The many shapes of mitochondrial death. Oncogene 25 (2006) 4717-4724
    • (2006) Oncogene , vol.25 , pp. 4717-4724
    • Cereghetti, G.M.1    Scorrano, L.2
  • 92
    • 42049092501 scopus 로고    scopus 로고
    • Mitochondrial dynamics: to be in good shape to survive
    • Herzig S., and Martinou J.C. Mitochondrial dynamics: to be in good shape to survive. Curr. Mol. Med. 8 (2008) 131-137
    • (2008) Curr. Mol. Med. , vol.8 , pp. 131-137
    • Herzig, S.1    Martinou, J.C.2
  • 93
    • 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., Arnoult D., Chen H., Chan D.C., Smith C.L., and Youle R.J. 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    Arnoult, D.2    Chen, H.3    Chan, D.C.4    Smith, C.L.5    Youle, R.J.6
  • 94
    • 0034676062 scopus 로고    scopus 로고
    • Gag3p, an outer membrane protein required for fission of mitochondrial tubules
    • Fekkes P., Shepard K.A., and Yaffe M.P. Gag3p, an outer membrane protein required for fission of mitochondrial tubules. J. Cell Biol. 151 (2000) 333-340
    • (2000) J. Cell Biol. , vol.151 , pp. 333-340
    • Fekkes, P.1    Shepard, K.A.2    Yaffe, M.P.3
  • 95
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy A.D., McCaffery J.M., and Shaw J.M. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151 (2000) 367-380
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 96
    • 0035149539 scopus 로고    scopus 로고
    • Division of mitochondria requires a novel DMN1-interacting protein, Net2p
    • Cerveny K.L., McCaffery J.M., and Jensen R.E. Division of mitochondria requires a novel DMN1-interacting protein, Net2p. Mol. Biol. Cell 12 (2001) 309-321
    • (2001) Mol. Biol. Cell , vol.12 , pp. 309-321
    • Cerveny, K.L.1    McCaffery, J.M.2    Jensen, R.E.3
  • 97
    • 0141541721 scopus 로고    scopus 로고
    • The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria
    • Cerveny K.L., and Jensen R.E. The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria. Mol. Biol. Cell 14 (2003) 4126-4139
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4126-4139
    • Cerveny, K.L.1    Jensen, R.E.2
  • 98
    • 0036322806 scopus 로고    scopus 로고
    • The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission
    • Tieu Q., Okreglak V., Naylor K., and Nunnari J. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J. Cell Biol. 158 (2002) 445-452
    • (2002) J. Cell Biol. , vol.158 , pp. 445-452
    • Tieu, Q.1    Okreglak, V.2    Naylor, K.3    Nunnari, J.4
  • 99
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division
    • Tieu Q., and Nunnari J. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J. Cell Biol. 151 (2000) 353-366
    • (2000) J. Cell Biol. , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 100
    • 22944440071 scopus 로고    scopus 로고
    • The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria
    • Griffin E.E., Graumann J., and Chan D.C. The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. J. Cell Biol. 170 (2005) 237-248
    • (2005) J. Cell Biol. , vol.170 , pp. 237-248
    • Griffin, E.E.1    Graumann, J.2    Chan, D.C.3
  • 103
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K., and Shaw J.M. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Ann. Rev. Genet. 39 (2005) 503-536
    • (2005) Ann. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 104
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • Smirnova E., Griparic L., Shurland D.L., and van der Bliek A.M. 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    Griparic, L.2    Shurland, D.L.3    van der Bliek, A.M.4
  • 105
    • 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., Krueger E.W., Oswald B.J., and McNiven M.A. 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    Krueger, E.W.2    Oswald, B.J.3    McNiven, M.A.4
  • 106
    • 0033571410 scopus 로고    scopus 로고
    • Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape
    • Sesaki H., and Jensen R.E. Division versus fusion: Dnm1p and Fzo1p antagonistically regulate mitochondrial shape. J. Cell Biol. 147 (1999) 699-706
    • (1999) J. Cell Biol. , vol.147 , pp. 699-706
    • Sesaki, H.1    Jensen, R.E.2
  • 107
    • 34249019899 scopus 로고    scopus 로고
    • Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis
    • Estaquier J., and Arnoult D. Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis. Cell Death Differ. 14 (2007) 1086-1094
    • (2007) Cell Death Differ. , vol.14 , pp. 1086-1094
    • Estaquier, J.1    Arnoult, D.2
  • 109
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li Z., Okamoto K., Hayashi Y., and Sheng M. The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 119 (2004) 873-887
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 114
    • 40949143555 scopus 로고    scopus 로고
    • Bcl-xL inhibitor ABT-737 reveals a dual role for Bcl-xL in synaptic transmission
    • Hickman J.A., Hardwick J.M., Kaczmarek L.K., and Jonas E.A. Bcl-xL inhibitor ABT-737 reveals a dual role for Bcl-xL in synaptic transmission. J. Neurophysiol. 99 (2008) 1515-1522
    • (2008) J. Neurophysiol. , vol.99 , pp. 1515-1522
    • Hickman, J.A.1    Hardwick, J.M.2    Kaczmarek, L.K.3    Jonas, E.A.4
  • 115
    • 33745221197 scopus 로고    scopus 로고
    • Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1
    • Bhar D., Karren M.A., Babst M., and Shaw J.M. Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. J. Biol. Chem. 281 (2006) 17312-17320
    • (2006) J. Biol. Chem. , vol.281 , pp. 17312-17320
    • Bhar, D.1    Karren, M.A.2    Babst, M.3    Shaw, J.M.4
  • 116
    • 33748291455 scopus 로고    scopus 로고
    • Fis1p and Caf4p, but not Mdv1p, determine the polar localization of Dnm1p clusters on the mitochondrial surface
    • Schauss A.C., Bewersdorf J., and Jakobs S. Fis1p and Caf4p, but not Mdv1p, determine the polar localization of Dnm1p clusters on the mitochondrial surface. J. Cell Sci. 119 (2006) 3098-3106
    • (2006) J. Cell Sci. , vol.119 , pp. 3098-3106
    • Schauss, A.C.1    Bewersdorf, J.2    Jakobs, S.3
  • 117
    • 36749075083 scopus 로고    scopus 로고
    • Structural basis for recruitment of mitochondrial fission complexes by Fis1
    • Zhang Y., and Chan D.C. Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 18526-18530
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 18526-18530
    • Zhang, Y.1    Chan, D.C.2
  • 118
    • 36348930592 scopus 로고    scopus 로고
    • Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm
    • Wells R.C., Picton L.K., Williams S.C., Tan F.J., and Hill R.B. Direct binding of the dynamin-like GTPase, Dnm1, to mitochondrial dynamics protein Fis1 is negatively regulated by the Fis1 N-terminal arm. J. Biol. Chem. 282 (2007) 33769-33775
    • (2007) J. Biol. Chem. , vol.282 , pp. 33769-33775
    • Wells, R.C.1    Picton, L.K.2    Williams, S.C.3    Tan, F.J.4    Hill, R.B.5
  • 119
    • 33645747175 scopus 로고    scopus 로고
    • BIGYIN, an orthologue of human and yeast FIS1 genes functions in the control of mitochondrial size and number in Arabidopsis thaliana
    • Scott I., Tobin A.K., and Logan D.C. BIGYIN, an orthologue of human and yeast FIS1 genes functions in the control of mitochondrial size and number in Arabidopsis thaliana. J. Exp. Bot. 57 (2006) 1275-1280
    • (2006) J. Exp. Bot. , vol.57 , pp. 1275-1280
    • Scott, I.1    Tobin, A.K.2    Logan, D.C.3
  • 120
    • 27144477744 scopus 로고    scopus 로고
    • Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1
    • Yu T., Fox R.J., Burwell L.S., and Yoon Y. Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1. J. Cell Sci. 118 (2005) 4141-4151
    • (2005) J. Cell Sci. , vol.118 , pp. 4141-4151
    • Yu, T.1    Fox, R.J.2    Burwell, L.S.3    Yoon, Y.4
  • 121
    • 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., Schlipf S., Sanz J., Neubert K., Stein R., and Borner C. Characterization of the signal that directs Bcl-x(L), but not Bcl-2, to the mitochondrial outer membrane. J. Cell Biol. 160 (2003) 53-64
    • (2003) J. Cell Biol. , vol.160 , pp. 53-64
    • Kaufmann, T.1    Schlipf, S.2    Sanz, J.3    Neubert, K.4    Stein, R.5    Borner, C.6
  • 123
    • 1842479419 scopus 로고    scopus 로고
    • Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology
    • Stojanovski D., Koutsopoulos O.S., Okamoto K., and Ryan M.T. Levels of human Fis1 at the mitochondrial outer membrane regulate mitochondrial morphology. J. Cell Sci. 117 (2004) 1201-1210
    • (2004) J. Cell Sci. , vol.117 , pp. 1201-1210
    • Stojanovski, D.1    Koutsopoulos, O.S.2    Okamoto, K.3    Ryan, M.T.4
  • 125
    • 33644859410 scopus 로고    scopus 로고
    • Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics
    • Delivani P., Adrain C., Taylor R.C., Duriez P.J., and Martin S.J. 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    Adrain, C.2    Taylor, R.C.3    Duriez, P.J.4    Martin, S.J.5
  • 126
    • 0141592470 scopus 로고    scopus 로고
    • hFis1, a novel component of the mammalian mitochondrial fission machinery
    • James D.I., Parone P.A., Mattenberger Y., and Martinou J.C. 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    Parone, P.A.2    Mattenberger, Y.3    Martinou, J.C.4
  • 128
    • 2542487188 scopus 로고    scopus 로고
    • Ca(2+) homeostasis during mitochondrial fragmentation and perinuclear clustering induced by hFis1
    • Frieden M., James D., Castelbou C., Danckaert A., Martinou J.C., and Demaurex N. Ca(2+) homeostasis during mitochondrial fragmentation and perinuclear clustering induced by hFis1. J. Biol. Chem. 279 (2004) 22704-22714
    • (2004) J. Biol. Chem. , vol.279 , pp. 22704-22714
    • Frieden, M.1    James, D.2    Castelbou, C.3    Danckaert, A.4    Martinou, J.C.5    Demaurex, N.6
  • 129
    • 33749265862 scopus 로고    scopus 로고
    • Formation of elongated giant mitochondria in DFO-induced cellular senescence: involvement of enhanced fusion process through modulation of Fis1
    • Yoon Y.S., Yoon D.S., Lim I.K., Yoon S.H., Chung H.Y., Rojo M., Malka F., Jou M.J., Martinou J.C., and Yoon G. Formation of elongated giant mitochondria in DFO-induced cellular senescence: involvement of enhanced fusion process through modulation of Fis1. J. Cell. Physiol. 209 (2006) 468-480
    • (2006) J. Cell. Physiol. , vol.209 , pp. 468-480
    • Yoon, Y.S.1    Yoon, D.S.2    Lim, I.K.3    Yoon, S.H.4    Chung, H.Y.5    Rojo, M.6    Malka, F.7    Jou, M.J.8    Martinou, J.C.9    Yoon, G.10
  • 130
    • 34547958816 scopus 로고    scopus 로고
    • Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence
    • Lee S., Jeong S.Y., Lim W.C., Kim S., Park Y.Y., Sun X., Youle R.J., and Cho H. Mitochondrial fission and fusion mediators, hFis1 and OPA1, modulate cellular senescence. J. Biol. Chem. 282 (2007) 22977-22983
    • (2007) J. Biol. Chem. , vol.282 , pp. 22977-22983
    • Lee, S.1    Jeong, S.Y.2    Lim, W.C.3    Kim, S.4    Park, Y.Y.5    Sun, X.6    Youle, R.J.7    Cho, H.8
  • 133
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E., and Chan D.C. 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    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 134
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen H., Chomyn A., and Chan D.C. Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J. Biol. Chem. 280 (2005) 26185-26192
    • (2005) J. Biol. Chem. , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 135
    • 0036479010 scopus 로고    scopus 로고
    • vMIA, a viral inhibitor of apoptosis targeting mitochondria
    • Goldmacher V.S. vMIA, a viral inhibitor of apoptosis targeting mitochondria. Biochimie 84 (2002) 177-185
    • (2002) Biochimie , vol.84 , pp. 177-185
    • Goldmacher, V.S.1
  • 137
    • 46549089432 scopus 로고    scopus 로고
    • K.L. Noris, R.J. Youle, Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins, J. of Virol. (available online on April 16)
    • K.L. Noris, R.J. Youle, Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins, J. of Virol. (available online on April 16)
  • 138
    • 33745268197 scopus 로고    scopus 로고
    • Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease
    • Niemann A., Berger P., and Suter U. Pathomechanisms of mutant proteins in Charcot-Marie-Tooth disease. Neuromol. Med. 8 (2006) 217-242
    • (2006) Neuromol. Med. , vol.8 , pp. 217-242
    • Niemann, A.1    Berger, P.2    Suter, U.3
  • 139
    • 4644229005 scopus 로고    scopus 로고
    • Importance of mitochondrial dynamics during meiosis and sporulation
    • Gorsich S.W., and Shaw J.M. Importance of mitochondrial dynamics during meiosis and sporulation. Mol. Biol. Cell 15 (2004) 4369-4381
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4369-4381
    • Gorsich, S.W.1    Shaw, J.M.2
  • 140
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • Kissova I., Deffieu M., Manon S., and Camougrand N. Uth1p is involved in the autophagic degradation of mitochondria. J. Biol. Chem. 279 (2004) 39068-39074
    • (2004) J. Biol. Chem. , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 141
    • 0032870475 scopus 로고    scopus 로고
    • Autophagy is activated by apoptotic signalling in sympathetic neurons: an alternative mechanism of death execution
    • Xue L., Fletcher G.C., and Tolkovsky A.M. 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    Fletcher, G.C.2    Tolkovsky, A.M.3
  • 142
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern segregation and elimination by autophagy
    • Twig G., Elorza A., Molina A.J., Mohamed H., Wikstrom J.D., Walzer G., et al. Fission and selective fusion govern segregation and elimination by autophagy. EMBO J. 27 (2008) 433-446
    • (2008) EMBO J. , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3    Mohamed, H.4    Wikstrom, J.D.5    Walzer, G.6
  • 143
    • 27944487902 scopus 로고    scopus 로고
    • Logic of the yeast metabolic cycle: temporal compartmentalization of cellular processes
    • Tu B.P., Kudlicki A., Rowicka M., and McKnight S.L. Logic of the yeast metabolic cycle: temporal compartmentalization of cellular processes. Science 310 (2005) 1152-1158
    • (2005) Science , vol.310 , pp. 1152-1158
    • Tu, B.P.1    Kudlicki, A.2    Rowicka, M.3    McKnight, S.L.4
  • 144
    • 34347387832 scopus 로고    scopus 로고
    • Restriction of DNA replication to the reductive phase of the metabolic cycle protects genome integrity
    • Chen Z., Odstrcil E.A., Tu B.P., and McKnight S.L. Restriction of DNA replication to the reductive phase of the metabolic cycle protects genome integrity. Science 316 (2007) 1916-1919
    • (2007) Science , vol.316 , pp. 1916-1919
    • Chen, Z.1    Odstrcil, E.A.2    Tu, B.P.3    McKnight, S.L.4


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