메뉴 건너뛰기




Volumn 3, Issue 6, 2008, Pages 765-780

Structural implications of mitochondrial dynamics

Author keywords

Aging; Cytoskeleton; Fission; Fusion; Mitochondria

Indexed keywords

ANION CHANNELS; CYTOCHALASIN D; CYTOSKELETAL ELEMENTS; DYNAMIN; ELECTRON MICROGRAPHS; F ACTIN; FIBRILLAR STRUCTURES; FUNCTIONAL REQUIREMENTS (FR); HUMAN UMBILICAL VEIN ENDOTHELIAL CELL (HUVEC); INTRACELLULAR DISTRIBUTION; LOCAL FLUCTUATIONS; MICROTUBULE (MT); MITOCHONDRIAL PROTEINS; MOLECULAR ORGANIZATIONS; MULTIPLE RING; PERIPHERAL (SPI); RED FLUORESCENT PROTEIN (RFP); SHAPE CHANGES; STRUCTURAL IMPLICATIONS;

EID: 48949119163     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.200800024     Document Type: Review
Times cited : (85)

References (123)
  • 1
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi, V., Chinopoulos, C., Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol. Sci. 2006, 27, 639-645.
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 2
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harmann, D., The biologic clock: The mitochondria? J. Am. Geriatr. Soc. 1972, 20, 145-147.
    • (1972) J. Am. Geriatr. Soc , vol.20 , pp. 145-147
    • Harmann, D.1
  • 3
    • 0034695436 scopus 로고    scopus 로고
    • Accumulation of defective mitochondria through delayed degradation of damaged organelles and its possible role in the ageing of post-mitotic and dividing cells
    • Kowald, A., Kirkwood, T. B. L., Accumulation of defective mitochondria through delayed degradation of damaged organelles and its possible role in the ageing of post-mitotic and dividing cells. J. Theor. Biol. 2000, 202, 145-160.
    • (2000) J. Theor. Biol , vol.202 , pp. 145-160
    • Kowald, A.1    Kirkwood, T.B.L.2
  • 4
    • 27744524523 scopus 로고    scopus 로고
    • On the relevance of mitochondrial fusions for the accumulation of mitochondrial deletion mutants: A modelling study
    • Kowald A., Jendrach M., Pohl S., Bereiter-Hahn J., Hammerstein P., On the relevance of mitochondrial fusions for the accumulation of mitochondrial deletion mutants: A modelling study. Aging Cell 2005, 4, 273-283.
    • (2005) Aging Cell , vol.4 , pp. 273-283
    • Kowald, A.1    Jendrach, M.2    Pohl, S.3    Bereiter-Hahn, J.4    Hammerstein, P.5
  • 5
    • 18844444203 scopus 로고    scopus 로고
    • Morphodynamic changes of mitochondria during ageing of human endothelial cells
    • Jendrach M., Poll S., Vöth M., Kowald A. et al., Morphodynamic changes of mitochondria during ageing of human endothelial cells. Mech. Ageing Dev. 2005, 126, 813-821.
    • (2005) Mech. Ageing Dev , vol.126 , pp. 813-821
    • Jendrach, M.1    Poll, S.2    Vöth, M.3    Kowald, A.4
  • 6
    • 48049111526 scopus 로고    scopus 로고
    • A single short-term dose of hydrogen peroxide causes mitochondrial damage and shorted lifespan in HUVEC
    • in press
    • Jendrach, M., Pohl, S., Mai, S., Vöth, M., Bereiter-Hahn, J. A single short-term dose of hydrogen peroxide causes mitochondrial damage and shorted lifespan in HUVEC. Mitochondrion 2008, in press.
    • (2008) Mitochondrion
    • Jendrach, M.1    Pohl, S.2    Mai, S.3    Vöth, M.4    Bereiter-Hahn, J.5
  • 7
    • 0034694152 scopus 로고    scopus 로고
    • Role of microtubules and actin filaments in the movement of mitochondria in axons and dendrites of cultures hippocampal neurons
    • Ligon, L. A., Steward, O., Role of microtubules and actin filaments in the movement of mitochondria in axons and dendrites of cultures hippocampal neurons. J. Comp. Neurol., 2000, 427, 351-361.
    • (2000) J. Comp. Neurol , vol.427 , pp. 351-361
    • Ligon, L.A.1    Steward, O.2
  • 8
    • 0020830517 scopus 로고
    • Fluorimetry of mitochondria in cells vitally stained with DASP-MI or rhodamine 6GO
    • Bereiter-Hahn, J., Seipel, K. H., Voeth, M., Ploem, J. S., Fluorimetry of mitochondria in cells vitally stained with DASP-MI or rhodamine 6GO. Cell Biochem. Funct. 1983, 1, 147-155.
    • (1983) Cell Biochem. Funct , vol.1 , pp. 147-155
    • Bereiter-Hahn, J.1    Seipel, K.H.2    Voeth, M.3    Ploem, J.S.4
  • 9
    • 0013816904 scopus 로고
    • Lebendnachweis von Einzelelementen des endoplasmatischen Retikulums.
    • Girbardt, M., Lebendnachweis von Einzelelementen des endoplasmatischen Retikulums. J. Cell Biol., 1965, 27, 433-440.
    • (1965) J. Cell Biol , vol.27 , pp. 433-440
    • Girbardt, M.1
  • 10
    • 0033987381 scopus 로고    scopus 로고
    • Mitochondrial movement and morphology depend on an intact actin cytosekeleton in Aspergillus nidulans
    • Suelmann, R., Fischer, R. Mitochondrial movement and morphology depend on an intact actin cytosekeleton in Aspergillus nidulans. Cell Motil. Cytoskeleton 2000, 45, 42-50.
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 42-50
    • Suelmann, R.1    Fischer, R.2
  • 11
    • 33749512938 scopus 로고    scopus 로고
    • Implicatons for developmental potential
    • Mitochondrial distribution and microtubule organization in fertilized and clone porcine embryos
    • Katayama, M., Zhong, Z., Lai, L. Sutovsky, P. et al., Mitochondrial distribution and microtubule organization in fertilized and clone porcine embryos: Implicatons for developmental potential. Dev. Biol. 2006, 299, 206-220.
    • (2006) Dev. Biol , vol.299 , pp. 206-220
    • Katayama, M.1    Zhong, Z.2    Lai, L.3    Sutovsky, P.4
  • 12
    • 0028047262 scopus 로고
    • Dynamics of mitochondria in living cell: Shape changes, dislocations, fusion, and fission of mitochondria
    • Bereiter-Hahn, J., Voeth, M., Dynamics of mitochondria in living cell: Shape changes, dislocations, fusion, and fission of mitochondria. Microsc. Res. Tech. 1994, 27, 198-219.
    • (1994) Microsc. Res. Tech , vol.27 , pp. 198-219
    • Bereiter-Hahn, J.1    Voeth, M.2
  • 13
    • 5444236916 scopus 로고    scopus 로고
    • Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1
    • Varadi, A., Johnson-Cadwell, L. I., Cirulli, V., Yoon, Y. et al., Cytoplasmic dynein regulates the subcellular distribution of mitochondria by controlling the recruitment of the fission factor dynamin-related protein-1. J. Cell Sci. 2004, 117, 4389-4400.
    • (2004) J. Cell Sci , vol.117 , pp. 4389-4400
    • Varadi, A.1    Johnson-Cadwell, L.I.2    Cirulli, V.3    Yoon, Y.4
  • 14
    • 0008925445 scopus 로고
    • Metabolic control of shape and structure of mitochondria in situ
    • Bereiter-Hahn, J., Voeth, M., Metabolic control of shape and structure of mitochondria in situ. Biol. Cell 1983, 47, 309-322.
    • (1983) Biol. Cell , vol.47 , pp. 309-322
    • Bereiter-Hahn, J.1    Voeth, M.2
  • 15
    • 0028293260 scopus 로고
    • Changes in mitochondrial shape and distribution induced by ethacrynic acid and the transient formation of a mitochondrial reticulum
    • Soltys, B. J., Gupta, R., Changes in mitochondrial shape and distribution induced by ethacrynic acid and the transient formation of a mitochondrial reticulum. J. Cell Physiol. 1994, 159, 281-294.
    • (1994) J. Cell Physiol , vol.159 , pp. 281-294
    • Soltys, B.J.1    Gupta, R.2
  • 16
    • 35248824214 scopus 로고    scopus 로고
    • Mitochondria-endoplasmic reticulum choreography: Structure and signaling dynamics
    • Pizzo, P., Pozzan, T., Mitochondria-endoplasmic reticulum choreography: Structure and signaling dynamics. Trends Cell Biol. 2007, 17, 511-517.
    • (2007) Trends Cell Biol , vol.17 , pp. 511-517
    • Pizzo, P.1    Pozzan, T.2
  • 17
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey, T. G., Manella, C. A., The internal structure of mitochondria. Trends Biochem. Sci. 2000, 25, 319-324.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 319-324
    • Frey, T.G.1    Manella, C.A.2
  • 18
    • 0023203829 scopus 로고
    • Sequestration of iontophoretically injected calcium by living endothelial cells
    • Stolz, B., Bereiter-Hahn, J., Sequestration of iontophoretically injected calcium by living endothelial cells. Cell Calcium 1987, 8, 103-121.
    • (1987) Cell Calcium , vol.8 , pp. 103-121
    • Stolz, B.1    Bereiter-Hahn, J.2
  • 21
    • 44749086506 scopus 로고    scopus 로고
    • Mitochondrial regulation of store-operated CRAC channels
    • doi:10.1016/j.ceca.2007.12.006
    • Parekh, A. B., Mitochondrial regulation of store-operated CRAC channels. Cell Calcium 2008, doi:10.1016/j.ceca.2007.12.006.
    • (2008) Cell Calcium
    • Parekh, A.B.1
  • 22
    • 44749089373 scopus 로고    scopus 로고
    • High- and low-calcium-dependent mechanisms of mitochondrial calcium signalling
    • doi:10.1016/j.ceca.2007.11.015
    • Spät, A., Szanda, G., Csordás, G., Hajnóczky, G., High- and low-calcium-dependent mechanisms of mitochondrial calcium signalling. Cell Calcium 2008, doi:10.1016/j.ceca.2007.11.015.
    • (2008) Cell Calcium
    • Spät, A.1    Szanda, G.2    Csordás, G.3    Hajnóczky, G.4
  • 23
    • 0037417334 scopus 로고    scopus 로고
    • Caspase cleavage product of BAP31 induces mitochondrial fisson through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol
    • Breckenridge, D. G., Stojanovic, M., Marcellus, R. C., Shore, G. C., Caspase cleavage product of BAP31 induces mitochondrial fisson through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol. J. Cell Biol. 2003, 160, 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
  • 24
    • 0032734577 scopus 로고    scopus 로고
    • The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells
    • Pitts, K. R., Yoon, Y., Krueger, E. W., McNiven, M. A., The dynamin-like protein DLP1 is essential for normal distribution and morphology of the endoplasmic reticulum and mitochondria in mammalian cells. Mol. Biol. Cell 1999, 10, 4403-4417.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4403-4417
    • Pitts, K.R.1    Yoon, Y.2    Krueger, E.W.3    McNiven, M.A.4
  • 25
    • 0025806764 scopus 로고
    • Intracllular heterogeneitiy in mitochondrial membrane potentials revealed by a J-aggregate forming lipophilic cation JC-1
    • Smiley, S. T., Reers, M. Mottola-Hartshorn, C., Lin, M. et al., Intracllular heterogeneitiy in mitochondrial membrane potentials revealed by a J-aggregate forming lipophilic cation JC-1. Proc. Natl. Acad. Sci. USA 1991, 66, 3671-3675.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.66 , pp. 3671-3675
    • Smiley, S.T.1    Reers, M.2    Mottola-Hartshorn, C.3    Lin, M.4
  • 26
    • 0032905925 scopus 로고    scopus 로고
    • Subcellular heterogeneity of mitochondrial membrane potential: Relationship with organelle distribution and intercellular contacts in normal, hypoxic and apoptotic cells
    • Diaz, G., Setzu, M. D., Zucca A., Isola, R. et al., Subcellular heterogeneity of mitochondrial membrane potential: Relationship with organelle distribution and intercellular contacts in normal, hypoxic and apoptotic cells. J. Cell Sci. 1999, 112, 1077-1084.
    • (1999) J. Cell Sci , vol.112 , pp. 1077-1084
    • Diaz, G.1    Setzu, M.D.2    Zucca, A.3    Isola, R.4
  • 27
    • 0842345390 scopus 로고    scopus 로고
    • Subcellular heterogeneity of mitochondrial function and dysfunction: Evidence by confocal imaging
    • Kuznetsov, A. V., Usson, Y., Leverve, X., Margreiter, R., Subcellular heterogeneity of mitochondrial function and dysfunction: Evidence by confocal imaging. Mol. Cell. Biochem. 2004, 256/257, 359-365.
    • (2004) Mol. Cell. Biochem , vol.256-257 , pp. 359-365
    • Kuznetsov, A.V.1    Usson, Y.2    Leverve, X.3    Margreiter, R.4
  • 28
    • 0038609470 scopus 로고    scopus 로고
    • Mitochondria are morphologically heterogeneous within cells
    • Collins, T. J., Bootmann, M. D., Mitochondria are morphologically heterogeneous within cells. J. Exp. Biol. 2003, 206, 1993-2000.
    • (2003) J. Exp. Biol , vol.206 , pp. 1993-2000
    • Collins, T.J.1    Bootmann, M.D.2
  • 29
    • 33745616352 scopus 로고    scopus 로고
    • Mitochondrial subpopulations and heterogeneity revealed by confocal imaging: Possible physiological role?
    • Kuznetsov, A. V., Troppmair, J., Sucher, R., Hermann, M. et al., Mitochondrial subpopulations and heterogeneity revealed by confocal imaging: Possible physiological role? Biochim. Biophys. Acta 2006, 1757, 686-691.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 686-691
    • Kuznetsov, A.V.1    Troppmair, J.2    Sucher, R.3    Hermann, M.4
  • 30
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris, R. L., Hollenbeck, P. J., Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J. Cell Biol. 1995, 131, 1315-1326.
    • (1995) J. Cell Biol , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 31
    • 0034833558 scopus 로고    scopus 로고
    • Mitochondrial transmembrane potential changes support the concept of mitochondrial heterogeneity during apoptosis
    • Krysko, D. V., Roels, F, Leybaer, L., D'Herde, K., Mitochondrial transmembrane potential changes support the concept of mitochondrial heterogeneity during apoptosis. J. Histochem. Cytochem. 2001, 49, 1277-1284.
    • (2001) J. Histochem. Cytochem , vol.49 , pp. 1277-1284
    • Krysko, D.V.1    Roels, F.2    Leybaer, L.3    D'Herde, K.4
  • 32
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power-transmitting cables
    • Skulachev, V. P., Mitochondrial filaments and clusters as intracellular power-transmitting cables. Trends Biochem. Sci. 2001, 26, 23-29.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 33
    • 0036310959 scopus 로고    scopus 로고
    • Expression of uncoupling protein-3 in subsarcolemmal and intermyofibrillar mitochondria of vaious mouse muscle types and its modulation by fasting
    • Jimenez, M., Yvon, C., Lehr, L., Leger, B. et al., Expression of uncoupling protein-3 in subsarcolemmal and intermyofibrillar mitochondria of vaious mouse muscle types and its modulation by fasting. Eur. J. Biochem. 2002, 269, 2878-2884.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2878-2884
    • Jimenez, M.1    Yvon, C.2    Lehr, L.3    Leger, B.4
  • 34
    • 33751229610 scopus 로고    scopus 로고
    • Structure of cristae in cardiac mitochondria of aged rat
    • Riva, A., Tandler, B., Lesnefsky, E. J., Conti, G. et al. Structure of cristae in cardiac mitochondria of aged rat. Mech. Ageing Dev. 2006, 127, 917-921.
    • (2006) Mech. Ageing Dev , vol.127 , pp. 917-921
    • Riva, A.1    Tandler, B.2    Lesnefsky, E.J.3    Conti, G.4
  • 35
    • 34948890528 scopus 로고    scopus 로고
    • Beta-cell mitochondria exhibit membrane potential heterogeneity that can be altered by stimulatory or toxic fuel levels
    • Wikstrom, J. D., Kathman, S. M., Mohamed, H., Twig, G. et al., Beta-cell mitochondria exhibit membrane potential heterogeneity that can be altered by stimulatory or toxic fuel levels. Diabetes 2007, 56, 2569-2578.
    • (2007) Diabetes , vol.56 , pp. 2569-2578
    • Wikstrom, J.D.1    Kathman, S.M.2    Mohamed, H.3    Twig, G.4
  • 36
    • 0002242836 scopus 로고    scopus 로고
    • Do single mitochondria contain zones with different membrane potential?
    • Bereiter-Hahn, J., Voeth, M., Do single mitochondria contain zones with different membrane potential?. Exp. Biol. Online 1998, 3, 12.
    • (1998) Exp. Biol. Online , vol.3 , pp. 12
    • Bereiter-Hahn, J.1    Voeth, M.2
  • 37
    • 0242290783 scopus 로고    scopus 로고
    • Spontaneous changes in mitochondrial membrane potential in single isolated brain mitochondria
    • Vergun, O., Vatyakova, T. V. and Reynolds I. J., Spontaneous changes in mitochondrial membrane potential in single isolated brain mitochondria. Biophys. J. 2003, 85, 3358-3366.
    • (2003) Biophys. J , vol.85 , pp. 3358-3366
    • Vergun, O.1    Vatyakova, T.V.2    Reynolds, I.J.3
  • 38
    • 0024398871 scopus 로고
    • The specific binding of the microtubule-associated protein2 (MAP2) to the outer membrane of rat brain mitochondria
    • Linden M., Nelson B. D., Leterrrier J.-F., The specific binding of the microtubule-associated protein2 (MAP2) to the outer membrane of rat brain mitochondria. Biochem. J. 1989, 261, 167-173.
    • (1989) Biochem. J , vol.261 , pp. 167-173
    • Linden, M.1    Nelson, B.D.2    Leterrrier, J.-F.3
  • 39
    • 34547670277 scopus 로고    scopus 로고
    • Misgeld, T., Kerschensteiner, M., Bareyre, F. M., Burgess, W. R. et al., Imaging axonal transport of mitochondria in vivo. Nat. Methods 2007 DOI:10.1038/NMeth1055.
    • Misgeld, T., Kerschensteiner, M., Bareyre, F. M., Burgess, W. R. et al., Imaging axonal transport of mitochondria in vivo. Nat. Methods 2007 DOI:10.1038/NMeth1055.
  • 40
    • 3242875557 scopus 로고    scopus 로고
    • Axonal mitochondrial transport and potential are correlated
    • Miller, K. E., Sheetz, M. P., Axonal mitochondrial transport and potential are correlated. J. Cell Sci. 2004, 117, 2791-2804.
    • (2004) J. Cell Sci , vol.117 , pp. 2791-2804
    • Miller, K.E.1    Sheetz, M.P.2
  • 41
    • 0027146417 scopus 로고
    • Imaging in five dimensions: Time-dependent membrane potentials in individual mitochondria
    • Loew, L. M., Tuft, R. A., Carrington W., Fay F. S. Imaging in five dimensions: Time-dependent membrane potentials in individual mitochondria. Biophys. J. 1993, 65, 2396-2407.
    • (1993) Biophys. J , vol.65 , pp. 2396-2407
    • Loew, L.M.1    Tuft, R.A.2    Carrington, W.3    Fay, F.S.4
  • 42
    • 35248842739 scopus 로고    scopus 로고
    • Mitochondria on the move
    • Boldogh, I. R., Pon, L. A., Mitochondria on the move. Trends Cell Biol. 2007, 17, 502-510.
    • (2007) Trends Cell Biol , vol.17 , pp. 502-510
    • Boldogh, I.R.1    Pon, L.A.2
  • 43
    • 0028800221 scopus 로고
    • Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain
    • Kolodney, M. S., Elson, E. L., Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain. Proc. Natl. Acad. Sci. USA 1995, 92, 10252-10256.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10252-10256
    • Kolodney, M.S.1    Elson, E.L.2
  • 44
    • 0034609764 scopus 로고    scopus 로고
    • Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC
    • Kusano, H., Shimizu, S., Koya, R. C., Fujita, H. et al., Human gelsolin prevents apoptosis by inhibiting apoptotic mitochondrial changes via closing VDAC. Oncogene 2000, 19, 4807-4814.
    • (2000) Oncogene , vol.19 , pp. 4807-4814
    • Kusano, H.1    Shimizu, S.2    Koya, R.C.3    Fujita, H.4
  • 45
    • 21744445111 scopus 로고    scopus 로고
    • The actin cytoskeleton: A key regulator of apoptosis and ageing?
    • Gourlay, C. W., Ayscough, K. R., The actin cytoskeleton: A key regulator of apoptosis and ageing? Nat. Rev. Mol. Cell Biol. 2005, 6, 583-589.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 583-589
    • Gourlay, C.W.1    Ayscough, K.R.2
  • 46
    • 33646761645 scopus 로고    scopus 로고
    • The increase in mitochondrial association with actin prescedes Bax translocation in apoptosis
    • Tang, H. L., Le, A. H., Lung, H. L., The increase in mitochondrial association with actin prescedes Bax translocation in apoptosis. Biochem. J. 2006, 396, 1-5.
    • (2006) Biochem. J , vol.396 , pp. 1-5
    • Tang, H.L.1    Le, A.H.2    Lung, H.L.3
  • 47
    • 3343021928 scopus 로고    scopus 로고
    • Nerve growth factor signaling regulates motility and docking of axonal mitochondria
    • Chada, S. R., Hollenbeck, P. J., Nerve growth factor signaling regulates motility and docking of axonal mitochondria. Curr. Biol. 2004, 14, 1272-1276.
    • (2004) Curr. Biol , vol.14 , pp. 1272-1276
    • Chada, S.R.1    Hollenbeck, P.J.2
  • 48
    • 17144429793 scopus 로고    scopus 로고
    • Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission
    • De Vos, K. J., Allan, V. J., Grierson, A. J., Sheetz, M. P., Mitochondrial function and actin regulate dynamin-related protein 1-dependent mitochondrial fission. Curr. Biol. 2005, 15, 678-683.
    • (2005) Curr. Biol , vol.15 , pp. 678-683
    • De Vos, K.J.1    Allan, V.J.2    Grierson, A.J.3    Sheetz, M.P.4
  • 49
    • 0032246159 scopus 로고    scopus 로고
    • Cell contraction caused by microtubule disruption is accompanied by shape changes and an increased elasticity measured by scanning acoustic microscopy
    • Karl, I., Bereiter-Hahn J., Cell contraction caused by microtubule disruption is accompanied by shape changes and an increased elasticity measured by scanning acoustic microscopy. Cell Biochem. Biophys. 1998, 29, 225-241.
    • (1998) Cell Biochem. Biophys , vol.29 , pp. 225-241
    • Karl, I.1    Bereiter-Hahn, J.2
  • 50
    • 38949125860 scopus 로고
    • Stoffwechselabhängige mitochondriale Bewegungen in epithelialen Kaulquappenherzzellen in Gewebekulturen
    • Bereiter-Hahn, J., Morawe, G., Stoffwechselabhängige mitochondriale Bewegungen in epithelialen Kaulquappenherzzellen in Gewebekulturen. Cytobiology 1972, 6, 447-467.
    • (1972) Cytobiology , vol.6 , pp. 447-467
    • Bereiter-Hahn, J.1    Morawe, G.2
  • 51
    • 0021070504 scopus 로고
    • The pathway of ATP hydrolysis by dynein kinetics of a presteady state phosphate burst
    • Johnson, K. A., The pathway of ATP hydrolysis by dynein kinetics of a presteady state phosphate burst. J. Biol. Chem. 1983, 258, 1325-13832.
    • (1983) J. Biol. Chem , vol.258 , pp. 1325-13832
    • Johnson, K.A.1
  • 52
    • 33750305666 scopus 로고    scopus 로고
    • Dynamic subcompartmentalization of the mitochondrial inner membrane
    • Vogel, F., Bornhovd, C., Neupert, W., Reichert, A. S., Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 2006, 175, 237-247.
    • (2006) J. Cell Biol , vol.175 , pp. 237-247
    • Vogel, F.1    Bornhovd, C.2    Neupert, W.3    Reichert, A.S.4
  • 53
    • 0014347959 scopus 로고
    • Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states
    • Hackenbrock, C. R. Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states. Proc. Natl. Acad. Sci. USA 1968, 61, 598-605.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 598-605
    • Hackenbrock, C.R.1
  • 54
    • 20244381365 scopus 로고    scopus 로고
    • Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
    • Delettre, C., Lenaers, G., Griffoin, J-M., Gigarel, N. et al., Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat. Genet. 2000, 26, 207-210.
    • (2000) Nat. Genet , vol.26 , pp. 207-210
    • Delettre, C.1    Lenaers, G.2    Griffoin, J.-M.3    Gigarel, N.4
  • 55
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • doi:10.1083/jcb.200704110
    • Song, Z., Chen, H., Fiket, M., Alexander, C. et al., OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J. Cell Biol. 2007, doi:10.1083/jcb.200704110.
    • (2007) J. Cell Biol
    • Song, Z.1    Chen, H.2    Fiket, M.3    Alexander, C.4
  • 56
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza, C., Cipolat S., deBrito, O. M., Micaroni, M. et al., OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 2006, 126, 177-189.
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1    Cipolat, S.2    deBrito, O.M.3    Micaroni, M.4
  • 57
    • 34547611925 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology
    • Chang, C. R., Blackstone, C., Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J. Biol. Chem. 2007, 282, 21583-21587.
    • (2007) J. Biol. Chem , vol.282 , pp. 21583-21587
    • Chang, C.R.1    Blackstone, C.2
  • 58
    • 33947434544 scopus 로고    scopus 로고
    • OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis
    • Olichon, A., ElAchouri, G., Baricault, L., Delettre, C. et al., OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis. Cell Death Differ. 2007, 14, 682-692.
    • (2007) Cell Death Differ , vol.14 , pp. 682-692
    • Olichon, A.1    ElAchouri, G.2    Baricault, L.3    Delettre, C.4
  • 59
    • 38849190029 scopus 로고    scopus 로고
    • OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion
    • Zanna, C., Ghelli, A., Porcelli, A-M., Karbowski, M., Youle, R. J. et al., OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion. Brain 2008, 131, 352-367.
    • (2008) Brain , vol.131 , pp. 352-367
    • Zanna, C.1    Ghelli, A.2    Porcelli, A.-M.3    Karbowski, M.4    Youle, R.J.5
  • 60
    • 34548313686 scopus 로고    scopus 로고
    • Regulation of the mitochondrial dynamin-like protein Opa-1 by proteolytic cleavage
    • Griparic, L., Kanazawa, T., van der Bliek, A. M., Regulation of the mitochondrial dynamin-like protein Opa-1 by proteolytic cleavage. J. Cell Biol. 2007, 178, 757-764.
    • (2007) J. Cell Biol , vol.178 , pp. 757-764
    • Griparic, L.1    Kanazawa, T.2    van der Bliek, A.M.3
  • 61
    • 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., L. Baricault, N. Gas, E. Guillou, A. et al., Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 2003, 278, 7743-7746.
    • (2003) J. Biol. Chem , vol.278 , pp. 7743-7746
    • Olichon, A.L.1    Baricault, N.2    Gas, E.3    Guillou, A.4
  • 62
    • 2442421118 scopus 로고    scopus 로고
    • Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria
    • Griparic, L., van der Wel, N. N., Orozco, I. J., Peters, P. J. et al., Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria. J. Biol. Chem. 2004, 279, 18792-18798.
    • (2004) J. Biol. Chem , vol.279 , pp. 18792-18798
    • Griparic, L.1    van der Wel, N.N.2    Orozco, I.J.3    Peters, P.J.4
  • 63
    • 0037415638 scopus 로고    scopus 로고
    • A Cassidy-Stone, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion
    • Wong, E. D., Wagner, S. V., Okreglak, V., Holewinske, T. J. et al., A Cassidy-Stone, Mgm1p, is a component of a protein complex that mediates mitochondrial fusion. J. Cell Biol. 2003, 160, 303-311.
    • (2003) J. Cell Biol , vol.160 , pp. 303-311
    • Wong, E.D.1    Wagner, S.V.2    Okreglak, V.3    Holewinske, T.J.4
  • 64
    • 8644270474 scopus 로고    scopus 로고
    • Cipolat, S., Martins de Brito, O, Dal Zilia, B., Scorrano, L., OPA1 requires mitofusin1 to promote mitochondrial fusion. Proc. Nat. Acad. Sci. USA 2004, 101, 15927-15932.
    • Cipolat, S., Martins de Brito, O,, Dal Zilia, B., Scorrano, L., OPA1 requires mitofusin1 to promote mitochondrial fusion. Proc. Nat. Acad. Sci. USA 2004, 101, 15927-15932.
  • 65
    • 33745872237 scopus 로고    scopus 로고
    • Get the balance right: Mitofusins roles in health and disease
    • Santel, A., Get the balance right: Mitofusins roles in health and disease. Biochim. Biophys. Acta 2006, 1763, 490-499.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 490-499
    • Santel, A.1
  • 66
    • 0017961478 scopus 로고
    • Intracellular motility of mitochondria: Role of the inner compartment in migration and shape changes of mitochondria in XTH-cells
    • Bereiter-Hahn, J. Intracellular motility of mitochondria: Role of the inner compartment in migration and shape changes of mitochondria in XTH-cells. J. Cell Sci. 1978, 39, 99-115.
    • (1978) J. Cell Sci , vol.39 , pp. 99-115
    • Bereiter-Hahn, J.1
  • 67
    • 0025036216 scopus 로고
    • Behavior of mitochondria in the living cell
    • Bereiter-Hahn, J., Behavior of mitochondria in the living cell. Int. Rev. Cytol. 1990, 122, 1-63.
    • (1990) Int. Rev. Cytol , vol.122 , pp. 1-63
    • Bereiter-Hahn, J.1
  • 68
    • 0242264074 scopus 로고    scopus 로고
    • Distribution and dynamics of mitochondrial nucleoids in animal cells in culture
    • Bereiter-Hahn, J., Voeth, M., Distribution and dynamics of mitochondrial nucleoids in animal cells in culture. Exp. Biol. Online 1996, 1, 4.
    • (1996) Exp. Biol. Online , vol.1 , pp. 4
    • Bereiter-Hahn, J.1    Voeth, M.2
  • 69
    • 2442687998 scopus 로고    scopus 로고
    • Frequent fusion and fission of plant mitochondria with unequal nucleoid distribution
    • Arimura S-I., Yamamoto, J., Aida, G. P. Nakazono, M. et al., Frequent fusion and fission of plant mitochondria with unequal nucleoid distribution. Proc. Natl. Acad. Sci. USA 2004, 101, 7805-7808.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7805-7808
    • Arimura, S.-I.1    Yamamoto, J.2    Aida, G.P.3    Nakazono, M.4
  • 70
    • 0036242518 scopus 로고    scopus 로고
    • Cell cycle dependent morphology changes and associated mitochondrial DNA redistribution in mitochondria of human cell lines
    • Margineantu, D. H., Cox, W. G., Sundell, L., Sherwood, S. W., Cell cycle dependent morphology changes and associated mitochondrial DNA redistribution in mitochondria of human cell lines. Mitochondrion 2002, 1, 425-435.
    • (2002) Mitochondrion , vol.1 , pp. 425-435
    • Margineantu, D.H.1    Cox, W.G.2    Sundell, L.3    Sherwood, S.W.4
  • 71
    • 0036164351 scopus 로고    scopus 로고
    • Solute and macromolecular diffusion in cellular aqueous compartments
    • Verkman, A. S., Solute and macromolecular diffusion in cellular aqueous compartments. Trends Biochem. Sci. 2002, 27, 27-33.
    • (2002) Trends Biochem. Sci , vol.27 , pp. 27-33
    • Verkman, A.S.1
  • 72
    • 33745737928 scopus 로고    scopus 로고
    • Structure and dynamics of the mitochondrial inner membrane cristae
    • Manella, C. Structure and dynamics of the mitochondrial inner membrane cristae. Biochim. Biophys. Acta 2006, 1763, 542-548.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 542-548
    • Manella, C.1
  • 73
    • 70449184252 scopus 로고
    • Recherche cytologiques sur le chondriome normal ou soumis à l'expérimentation dans des cellules vivantes cultivées in vitro.
    • Frederic, J., Recherche cytologiques sur le chondriome normal ou soumis à l'expérimentation dans des cellules vivantes cultivées in vitro. Arch. Biol. (Liège), 1958, 69, 167-349.
    • (1958) Arch. Biol. (Liège) , vol.69 , pp. 167-349
    • Frederic, J.1
  • 74
    • 37749043369 scopus 로고    scopus 로고
    • Mitochondrial dynamics and peripheral neuropathy
    • Baloh, R. H., Mitochondrial dynamics and peripheral neuropathy. Neuroscientist 2008, 14, 12-18.
    • (2008) Neuroscientist , vol.14 , pp. 12-18
    • Baloh, R.H.1
  • 75
    • 33644552417 scopus 로고    scopus 로고
    • Increased production of reactive oxgen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology
    • Yu, T., Robotham, J. L., Yoon, A., Increased production of reactive oxgen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology. Proc. Natl. Acad. Sci. USA 2006, 103, 2653-2658.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2653-2658
    • Yu, T.1    Robotham, J.L.2    Yoon, A.3
  • 77
    • 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., Yoon, Y., Regulation of mitochondrial fission and apoptosis by the mitochondrial outer membrane protein hFis1. J. Cell Sci. 2005, 118, 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
  • 78
    • 0031440879 scopus 로고    scopus 로고
    • Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase
    • Hales, K. G., Fuller, M. T., Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 1997, 90, 121-129
    • (1997) Cell , vol.90 , pp. 121-129
    • Hales, K.G.1    Fuller, M.T.2
  • 79
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari, J., Marshall, W. F., Straigth, A., Murray, A. et al., Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 1997, 8, 1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straigth, A.3    Murray, A.4
  • 80
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharamoyces cerevisiae
    • Rapaport, D., Brunner, M. Neupert, W, Westermann, B., Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharamoyces cerevisiae. J. Biol. Chem. 1998, 273, 20150-20155.
    • (1998) J. Biol. Chem , vol.273 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 82
    • 0036906665 scopus 로고    scopus 로고
    • Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins
    • Legros, F., Lombés, A., Frachon, P., Rojo M., Mitochondrial fusion in human cells is efficient, requires the inner membrane potential, and is mediated by mitofusins. Mol. Biol. Cell 2002, 13, 4343-4354.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4343-4354
    • Legros, F.1    Lombés, A.2    Frachon, P.3    Rojo, M.4
  • 83
    • 0034128803 scopus 로고    scopus 로고
    • Rearrangements of human mitochondrial DNA (mtDNA): New insights into the regulation of mtDNA copy number and gene expression
    • Tang, Y,, Schon, E. A., Wililchowski, E., Vazquez-Memije, M. E. et al., Rearrangements of human mitochondrial DNA (mtDNA): New insights into the regulation of mtDNA copy number and gene expression. Mol. Biol. Cell 2000, 11, 1471-1485.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1471-1485
    • Tang, Y.1    Schon, E.A.2    Wililchowski, E.3    Vazquez-Memije, M.E.4
  • 84
    • 36549002757 scopus 로고    scopus 로고
    • Giant mitochondria do not fuse and exchange their contents with normal mitochondria
    • Navratil, M., Terman, A., Arriaga, E. A., Giant mitochondria do not fuse and exchange their contents with normal mitochondria. Exp. Cell Res. 2008, 314, 164-172.
    • (2008) Exp. Cell Res , vol.314 , pp. 164-172
    • Navratil, M.1    Terman, A.2    Arriaga, E.A.3
  • 85
    • 36048945306 scopus 로고    scopus 로고
    • Regulation of mitochondrial fusion and division
    • Cerveny, K. L., Tamura, Y., Zhang, Z., Jensen, R. et al., Regulation of mitochondrial fusion and division. Trends Cell Biol. 2007, 17, 563-569.
    • (2007) Trends Cell Biol , vol.17 , pp. 563-569
    • Cerveny, K.L.1    Tamura, Y.2    Zhang, Z.3    Jensen, R.4
  • 86
    • 0017816161 scopus 로고
    • Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy
    • Pfeifer, U., Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy. J. Cell Biol. 1978, 78, 152-167.
    • (1978) J. Cell Biol , vol.78 , pp. 152-167
    • Pfeifer, U.1
  • 87
    • 33747389446 scopus 로고    scopus 로고
    • Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1
    • Escobar-Henriques M., Westermann, B., Langer, T., Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1. J. Cell Biol. 2006, 173, 645-650.
    • (2006) J. Cell Biol , vol.173 , pp. 645-650
    • Escobar-Henriques, M.1    Westermann, B.2    Langer, T.3
  • 88
    • 0015239454 scopus 로고
    • The turnover of mitochondria in a variety of tissues of young and aged rats
    • Menzies, R. A., Gold, P. H., The turnover of mitochondria in a variety of tissues of young and aged rats. J. Biol. Chem. 1971, 246, 2425-2429.
    • (1971) J. Biol. Chem , vol.246 , pp. 2425-2429
    • Menzies, R.A.1    Gold, P.H.2
  • 89
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function?
    • He, L., Lemasters, J. J., Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function? FEBS Lett. 2002, 512, 1-7.
    • (2002) FEBS Lett , vol.512 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 90
    • 0032504568 scopus 로고    scopus 로고
    • The mitochondrial permeability transition in cell death: A common mechanism in necrosis
    • Lemasters, J. J., Nieminen, A.-L., Qian, T., Grost, L. C. et al., The mitochondrial permeability transition in cell death: A common mechanism in necrosis. Biochim. Biophys. Acta 1998, 1366, 177-196.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 177-196
    • Lemasters, J.J.1    Nieminen, A.-L.2    Qian, T.3    Grost, L.C.4
  • 91
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig, G., Elorza, A., Molina, A. J. A., Mohamed, H. et al., Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J. 2008, 27, 433-446.
    • (2008) EMBO J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.A.3    Mohamed, H.4
  • 92
    • 2442589922 scopus 로고    scopus 로고
    • Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neurophathy type 2A
    • Zuchner, S., Mersyanova, I. V., Muglia, M., Bissar-Tadmouri, N. et al., Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neurophathy type 2A. Nat. Genet. 2004, 36, 449-451.
    • (2004) Nat. Genet , vol.36 , pp. 449-451
    • Zuchner, S.1    Mersyanova, I.V.2    Muglia, M.3    Bissar-Tadmouri, N.4
  • 93
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • Detmer, S. A., Chan, D. C., Functions and dysfunctions of mitochondrial dynamics. Nat. Rev. 2007, 8, 870-878.
    • (2007) Nat. Rev , vol.8 , pp. 870-878
    • Detmer, S.A.1    Chan, D.C.2
  • 95
    • 34447314190 scopus 로고    scopus 로고
    • Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function
    • Davies, V. J., Hollins, A. J., Piechota, M. J., Yip, W. et al. Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function. Hum. Mol. Genet. 2007, 16, 1307-1318.
    • (2007) Hum. Mol. Genet , vol.16 , pp. 1307-1318
    • Davies, V.J.1    Hollins, A.J.2    Piechota, M.J.3    Yip, W.4
  • 97
    • 33845876643 scopus 로고    scopus 로고
    • Reducing mitochondrial fission results in increased lifespan and fitness of two fungal ageing models
    • Scheckhuber, C. Q., Erjavec, N., Tinazil, A., Hamann, A. et al., Reducing mitochondrial fission results in increased lifespan and fitness of two fungal ageing models. Nat. Cell Biol. 2007, 9, 99-105.
    • (2007) Nat. Cell Biol , vol.9 , pp. 99-105
    • Scheckhuber, C.Q.1    Erjavec, N.2    Tinazil, A.3    Hamann, A.4
  • 98
    • 24144462451 scopus 로고    scopus 로고
    • Expression of Mfn2, the Charcot-Marie-Tooth neuropathy type 2A gene, in human sekeletal muscle: Effects of Type 2 diabetes, obesity, weight loss, and the regulatory role of tumor necrosis factor (alpha) and Interleukin-6
    • Bach, D., Naon, D., Pich, S., Soriano, F. X. et al., Expression of Mfn2, the Charcot-Marie-Tooth neuropathy type 2A gene, in human sekeletal muscle: Effects of Type 2 diabetes, obesity, weight loss, and the regulatory role of tumor necrosis factor (alpha) and Interleukin-6. Diabetes 2005, 54, 2685-2693.
    • (2005) Diabetes , vol.54 , pp. 2685-2693
    • Bach, D.1    Naon, D.2    Pich, S.3    Soriano, F.X.4
  • 99
    • 20444461625 scopus 로고    scopus 로고
    • The Charcot-Marie-Tooth type 2A gene product, Mfn2, upregulates fuel oxidation through expression of OXPHOS system
    • Pich, S., Bach, D., Briones, P., Liesa, M. et al., The Charcot-Marie-Tooth type 2A gene product, Mfn2, upregulates fuel oxidation through expression of OXPHOS system. Hum. Mol. Genet. 2005, 14, 1405-1415.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1405-1415
    • Pich, S.1    Bach, D.2    Briones, P.3    Liesa, M.4
  • 100
    • 0034938453 scopus 로고    scopus 로고
    • Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria
    • Ono, T, Isobe, K., Nakada, K., Hayashi, J. I., Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria. Nat. Genet. 2001, 28, 272-275.
    • (2001) Nat. Genet , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 101
    • 4644343220 scopus 로고    scopus 로고
    • In vivo interaction between mitochondria carrying mtDNAs from different mouse species
    • Sato, A., Nakada, K., Shitara, H., Yonekawa, H. et al., In vivo interaction between mitochondria carrying mtDNAs from different mouse species. Genetics 2004, 167, 1855-1861.
    • (2004) Genetics , vol.167 , pp. 1855-1861
    • Sato, A.1    Nakada, K.2    Shitara, H.3    Yonekawa, H.4
  • 102
    • 33751544005 scopus 로고    scopus 로고
    • Mitochondrial dynamics generate equal distribution but patchwork localization of respiratory complex I
    • Busch K., Bereiter-Hahn J., Wittig I., Schägger H., Jendrach M., Mitochondrial dynamics generate equal distribution but patchwork localization of respiratory complex I. Mol. Membr. Biol. 2006, 23, 509-520.
    • (2006) Mol. Membr. Biol , vol.23 , pp. 509-520
    • Busch, K.1    Bereiter-Hahn, J.2    Wittig, I.3    Schägger, H.4    Jendrach, M.5
  • 103
    • 48049092565 scopus 로고    scopus 로고
    • Dujon, B., Mitochondrial genetics and functions, In: Strathern, J. N., Jones, E. W., Braoch, J. R. (Eds.), The Molecular Biology of the Yeast Saccharomyces. 1., Life Cycle and Inheritance, Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1981, pp. 505-635.
    • Dujon, B., Mitochondrial genetics and functions, In: Strathern, J. N., Jones, E. W., Braoch, J. R. (Eds.), The Molecular Biology of the Yeast Saccharomyces. vol. 1., Life Cycle and Inheritance, Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1981, pp. 505-635.
  • 104
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation, mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • Nakada, K., Inoue, K., Ono, T., Isobe, K. et al., Inter-mitochondrial complementation, mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat. Med. 2001, 7, 934-940.
    • (2001) Nat. Med , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3    Isobe, K.4
  • 105
    • 0024448458 scopus 로고
    • Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation
    • King, M. P., Attardi, G., Human cells lacking mtDNA: Repopulation with exogenous mitochondria by complementation. Science 1993, 246, 500-503.
    • (1993) Science , vol.246 , pp. 500-503
    • King, M.P.1    Attardi, G.2
  • 106
    • 33749265862 scopus 로고    scopus 로고
    • Involvement of enhanced fusion process through modulation of Fis1
    • Formation of elongated giant mitochondria in DFO-induced cellular senescence
    • Yoon, Y-S., Yoon, D-S., Lim, I. K., Yoon, S-H., Chung, H-Y. et al., Formation of elongated giant mitochondria in DFO-induced cellular senescence: Involvement of enhanced fusion process through modulation of Fis1. J. Cell Physiol. 2006, 209, 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
  • 107
    • 0041911531 scopus 로고
    • Variety of mitochondrial shapes, sizes and volumes in Chlamydomonas reinhardii
    • Blank, R., Arnold, C. G., Variety of mitochondrial shapes, sizes and volumes in Chlamydomonas reinhardii. Protoplasma 1980, 104, 287-291.
    • (1980) Protoplasma , vol.104 , pp. 287-291
    • Blank, R.1    Arnold, C.G.2
  • 108
    • 34249689057 scopus 로고    scopus 로고
    • Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fusion
    • Taguchi, N., Ishihara. N., Jofuku, A., Oka, T. et al., Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fusion. J. Biol. Chem. 2007, 282, 11521-11529.
    • (2007) J. Biol. Chem , vol.282 , pp. 11521-11529
    • Taguchi, N.1    Ishihara, N.2    Jofuku, A.3    Oka, T.4
  • 109
    • 48049104519 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. 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. 2003, 160, 1115-1127.
    • (2003) J. Cell Biol , vol.160 , pp. 1115-1127
    • Karbowski, M.1    Arnoult, D.2    Chen, H.3    Chan, D.C.4
  • 110
    • 33745742159 scopus 로고    scopus 로고
    • Mitochondrial fission and apoptosis: An ongoing trial
    • Parone, P. A., Martinou, J.-C., Mitochondrial fission and apoptosis: An ongoing trial. Biochim. Biophys. Acta 2006, 1763, 522-530.
    • (2006) Biochim. Biophys. Acta , vol.1763 , pp. 522-530
    • Parone, P.A.1    Martinou, J.-C.2
  • 112
    • 1542380494 scopus 로고    scopus 로고
    • Sumo1 conjgates mitochondrial substrates and participates in mitochondrial fission
    • Harder, Z., Zunino, R., McBride, H., Sumo1 conjgates mitochondrial substrates and participates in mitochondrial fission. Curr. Biol. 2004, 14, 340-345.
    • (2004) Curr. Biol , vol.14 , pp. 340-345
    • Harder, Z.1    Zunino, R.2    McBride, H.3
  • 113
    • 34248225298 scopus 로고    scopus 로고
    • The SUMO protease SENP5 is required to maintain mitochondrial morphology and function
    • Zunino, R., Schauss, A., Rippstein, P., Andrade-Navarro, M. et al., The SUMO protease SENP5 is required to maintain mitochondrial morphology and function. J. Cell Sci. 2007, 120, 1178-1188.
    • (2007) J. Cell Sci , vol.120 , pp. 1178-1188
    • Zunino, R.1    Schauss, A.2    Rippstein, P.3    Andrade-Navarro, M.4
  • 114
    • 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., Grodet, A., Lee. Y. J., Estagquier, C. et al., Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J. Biol. Chem. 2005, 280, 35742-35750.
    • (2005) J. Biol. Chem , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estagquier, C.4
  • 115
    • 38849190029 scopus 로고    scopus 로고
    • OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion
    • Zanna, C., Ghelli, A., Porcelli, A-M., Karbowski, M., Youle, R. J. et al., OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion. Brain 2008, 131, 352-367.
    • (2008) Brain , vol.131 , pp. 352-367
    • Zanna, C.1    Ghelli, A.2    Porcelli, A.-M.3    Karbowski, M.4    Youle, R.J.5
  • 117
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 ccordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E. et al., Mitofusins Mfn1 and Mfn2 ccordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 2003, 160, 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
  • 118
    • 0036479010 scopus 로고    scopus 로고
    • vMIA, viral inhibitor of apoptosis targeting mitochondria
    • Goldmacher, V. S., vMIA, viral inhibitor of apoptosis targeting mitochondria. Biochimie 2002, 84, 177-185.
    • (2002) Biochimie , vol.84 , pp. 177-185
    • Goldmacher, V.S.1
  • 119
    • 0035487808 scopus 로고    scopus 로고
    • The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis
    • Frank, S., Gaume, B., Bergmann-Leitner, E. S., Leitner, W. W. et al., The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis. Dev. Cell 2001, 1, 515-525.
    • (2001) Dev. Cell , vol.1 , pp. 515-525
    • Frank, S.1    Gaume, B.2    Bergmann-Leitner, E.S.3    Leitner, W.W.4
  • 120
    • 10644296253 scopus 로고    scopus 로고
    • Fzo1, a protein involved in mitochondria fusion, inhibits apoptosis
    • Sugioka, R., Shimizu, S., Tsujimoto, Y., Fzo1, a protein involved in mitochondria fusion, inhibits apoptosis. J. Biol. Chem. 2004, 279, 5276-52734.
    • (2004) J. Biol. Chem , vol.279 , pp. 5276-52734
    • Sugioka, R.1    Shimizu, S.2    Tsujimoto, Y.3
  • 121
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondria fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • Lee, Y. J., Jeong, S. Y., Karbowski, C. L., Smith, C. L. et al., Roles of the mammalian mitochondria fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol. Biol. Cell 2004, 15, 5001-5011.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, C.L.3    Smith, C.L.4
  • 122
    • 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., Conradt, B., DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans. Nature 2005, 433, 754-760.
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 123
    • 0019904757 scopus 로고
    • Ultrastructural observations on the regeneration of adrenocortical autotransplants in the rat spleen
    • Belloni, A. S., Vassanelli, P., Robba, C., Rebuffat, P. et al., Ultrastructural observations on the regeneration of adrenocortical autotransplants in the rat spleen. J. Anat. 1982, 135, 245-253.
    • (1982) J. Anat , vol.135 , pp. 245-253
    • Belloni, A.S.1    Vassanelli, P.2    Robba, C.3    Rebuffat, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.