메뉴 건너뛰기




Volumn 18, Issue 4, 2013, Pages 439-456

Mitochondria in heart failure: The emerging role of mitochondrial dynamics

Author keywords

Autophagy; Cell death; Heart failure; Ischemia reperfusion injury; Mitochondria; Mitochondrial dynamics; Oxidative stress

Indexed keywords

ANTIOXIDANT; CALCIUM ION; DYNAMIN; HYDROXYL RADICAL; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; MITOFUSIN 1; MITOFUSIN 2; REACTIVE OXYGEN METABOLITE; SUPEROXIDE;

EID: 84879076534     PISSN: 13824147     EISSN: 15737322     Source Type: Journal    
DOI: 10.1007/s10741-012-9330-2     Document Type: Review
Times cited : (77)

References (159)
  • 1
    • 78149407069 scopus 로고    scopus 로고
    • Mitochondrial fission and fusion and their roles in the heart
    • 10.1007/s00109-010-0674-6
    • Kane LA, Youle RJ (2010) Mitochondrial fission and fusion and their roles in the heart. J Mol Med (Berl) 88:971-979
    • (2010) J Mol Med (Berl) , vol.88 , pp. 971-979
    • Kane, L.A.1    Youle, R.J.2
  • 2
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species affect mitochondrial electron transport complex i activity through oxidative cardiolipin damage
    • 11943469 1:CAS:528:DC%2BD38XisFyru7c%3D 10.1016/S0378-1119(01)00814-9
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM (2002) Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage. Gene 286:135-141
    • (2002) Gene , vol.286 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 3
    • 0035896205 scopus 로고    scopus 로고
    • Mitochondrial DNA damage and dysfunction associated with oxidative stress in failing hearts after myocardial infarction
    • 11249877 1:CAS:528:DC%2BD3MXit1Cqt7o%3D 10.1161/01.RES.88.5.529
    • Ide T, Tsutsui H, Hayashidani S et al (2001) Mitochondrial DNA damage and dysfunction associated with oxidative stress in failing hearts after myocardial infarction. Circ Res 88:529-535
    • (2001) Circ Res , vol.88 , pp. 529-535
    • Ide, T.1    Tsutsui, H.2    Hayashidani, S.3
  • 4
    • 0033588198 scopus 로고    scopus 로고
    • Mitochondrial electron transport complex i is a potential source of oxygen free radicals in the failing myocardium
    • 10455064 1:CAS:528:DyaK1MXltlehurg%3D 10.1161/01.RES.85.4.357
    • Ide T, Tsutsui H, Kinugawa S et al (1999) Mitochondrial electron transport complex I is a potential source of oxygen free radicals in the failing myocardium. Circ Res 85:357-363
    • (1999) Circ Res , vol.85 , pp. 357-363
    • Ide, T.1    Tsutsui, H.2    Kinugawa, S.3
  • 5
    • 14644442283 scopus 로고    scopus 로고
    • Oxygen, oxidative stress, hypoxia, and heart failure
    • 15765131 1:CAS:528:DC%2BD2MXit1emsL0%3D
    • Giordano FJ (2005) Oxygen, oxidative stress, hypoxia, and heart failure. J Clin Invest 115:500-508
    • (2005) J Clin Invest , vol.115 , pp. 500-508
    • Giordano, F.J.1
  • 6
    • 0035800882 scopus 로고    scopus 로고
    • Oxidative stress-mediated cardiac cell death is a major determinant of ventricular dysfunction and failure in dog dilated cardiomyopathy
    • 11485979 1:CAS:528:DC%2BD3MXmt1ClsbY%3D 10.1161/hh1501.094115
    • Cesselli D, Jakoniuk I, Barlucchi L et al (2001) Oxidative stress-mediated cardiac cell death is a major determinant of ventricular dysfunction and failure in dog dilated cardiomyopathy. Circ Res 89:279-286
    • (2001) Circ Res , vol.89 , pp. 279-286
    • Cesselli, D.1    Jakoniuk, I.2    Barlucchi, L.3
  • 7
    • 0034845541 scopus 로고    scopus 로고
    • Abnormal cardiac and skeletal muscle mitochondrial function in pacing-induced cardiac failure
    • 11557238 1:CAS:528:DC%2BD3MXms1OltL8%3D 10.1016/S0008-6363(01)00368-6
    • Marin-Garcia J, Goldenthal MJ, Moe GW (2001) Abnormal cardiac and skeletal muscle mitochondrial function in pacing-induced cardiac failure. Cardiovasc Res 52:103-110
    • (2001) Cardiovasc Res , vol.52 , pp. 103-110
    • Marin-Garcia, J.1    Goldenthal, M.J.2    Moe, G.W.3
  • 8
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • 11728801 1:CAS:528:DC%2BD3MXos1Knu7w%3D 10.1016/S0891-5849(01)00724-9
    • Nordberg J, Arner ES (2001) Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 31:1287-1312
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.2
  • 9
    • 33845945406 scopus 로고    scopus 로고
    • Oxidative stress causes heart failure with impaired mitochondrial respiration
    • 16959785 1:CAS:528:DC%2BD28XhtFegsbvJ 10.1074/jbc.M602118200
    • Nojiri H, Shimizu T, Funakoshi M et al (2006) Oxidative stress causes heart failure with impaired mitochondrial respiration. J Biol Chem 281:33789-33801
    • (2006) J Biol Chem , vol.281 , pp. 33789-33801
    • Nojiri, H.1    Shimizu, T.2    Funakoshi, M.3
  • 10
    • 0035500460 scopus 로고    scopus 로고
    • Genetic modification of prenatal lethality and dilated cardiomyopathy in Mn superoxide dismutase mutant mice
    • 11677043 1:CAS:528:DC%2BD3MXnslWqu70%3D 10.1016/S0891-5849(01)00694-3
    • Huang TT, Carlson EJ, Kozy HM et al (2001) Genetic modification of prenatal lethality and dilated cardiomyopathy in Mn superoxide dismutase mutant mice. Free Radic Biol Med 31:1101-1110
    • (2001) Free Radic Biol Med , vol.31 , pp. 1101-1110
    • Huang, T.T.1    Carlson, E.J.2    Kozy, H.M.3
  • 11
    • 6344277918 scopus 로고    scopus 로고
    • Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function
    • 15485910 1:CAS:528:DC%2BD2MXltl2jug%3D%3D 10.1128/MCB.24.21.9414-9423. 2004
    • Conrad M, Jakupoglu C, Moreno SG et al (2004) Essential role for mitochondrial thioredoxin reductase in hematopoiesis, heart development, and heart function. Mol Cell Biol 24:9414-9423
    • (2004) Mol Cell Biol , vol.24 , pp. 9414-9423
    • Conrad, M.1    Jakupoglu, C.2    Moreno, S.G.3
  • 12
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • 7493016 1:CAS:528:DyaK2MXpvVCksL8%3D 10.1038/ng1295-376
    • Li Y, Huang TT, Carlson EJ et al (1995) Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat Genet 11:376-381
    • (1995) Nat Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3
  • 13
    • 10744225549 scopus 로고    scopus 로고
    • Overexpression of glutathione peroxidase prevents left ventricular remodeling and failure after myocardial infarction in mice
    • 14744974 1:CAS:528:DC%2BD2cXms1ahtw%3D%3D 10.1161/01.CIR.0000109701. 77059.E9
    • Shiomi T, Tsutsui H, Matsusaka H et al (2004) Overexpression of glutathione peroxidase prevents left ventricular remodeling and failure after myocardial infarction in mice. Circulation 109:544-549
    • (2004) Circulation , vol.109 , pp. 544-549
    • Shiomi, T.1    Tsutsui, H.2    Matsusaka, H.3
  • 14
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine life span by overexpression of catalase targeted to mitochondria
    • 15879174 1:CAS:528:DC%2BD2MXlsVWmtbs%3D 10.1126/science.1106653
    • Schriner SE, Linford NJ, Martin GM et al (2005) Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 308:1909-1911
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1    Linford, N.J.2    Martin, G.M.3
  • 15
    • 0035680903 scopus 로고    scopus 로고
    • The oxidative stress hypothesis of congestive heart failure: Radical thoughts
    • 11742938 1:CAS:528:DC%2BD38XlvFeruw%3D%3D 10.1378/chest.120.6.2035
    • Mak S, Newton GE (2001) The oxidative stress hypothesis of congestive heart failure: radical thoughts. Chest 120:2035-2046
    • (2001) Chest , vol.120 , pp. 2035-2046
    • Mak, S.1    Newton, G.E.2
  • 16
    • 33644585112 scopus 로고    scopus 로고
    • Increased reactive oxygen species production and functional alterations in antioxidant enzymes in human failing myocardium
    • 16105639 1:CAS:528:DC%2BD2MXosVahsrk%3D 10.1016/j.cardfail.2005.01.007
    • Sam F, Kerstetter DL, Pimental DR et al (2005) Increased reactive oxygen species production and functional alterations in antioxidant enzymes in human failing myocardium. J Card Fail 11:473-480
    • (2005) J Card Fail , vol.11 , pp. 473-480
    • Sam, F.1    Kerstetter, D.L.2    Pimental, D.R.3
  • 17
    • 10244254975 scopus 로고    scopus 로고
    • Apoptosis in myocytes in end-stage heart failure
    • 8815940 1:STN:280:DyaK28zpvFShtw%3D%3D 10.1056/NEJM199610173351603
    • Narula J, Haider N, Virmani R et al (1996) Apoptosis in myocytes in end-stage heart failure. N Engl J Med 335:1182-1189
    • (1996) N Engl J Med , vol.335 , pp. 1182-1189
    • Narula, J.1    Haider, N.2    Virmani, R.3
  • 18
    • 0030766192 scopus 로고    scopus 로고
    • Apoptosis in the failing human heart
    • 9099657 1:STN:280:DyaK2s3jvVOmtg%3D%3D 10.1056/NEJM199704173361603
    • Olivetti G, Abbi R, Quaini F et al (1997) Apoptosis in the failing human heart. N Engl J Med 336:1131-1141
    • (1997) N Engl J Med , vol.336 , pp. 1131-1141
    • Olivetti, G.1    Abbi, R.2    Quaini, F.3
  • 19
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • 14744432 1:CAS:528:DC%2BD2cXhtValsrY%3D 10.1016/S0092-8674(04)00046-7
    • Danial NN, Korsmeyer SJ (2004) Cell death: critical control points. Cell 116:205-219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 20
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • 11452314 1:CAS:528:DC%2BD3MXlt1Cqsr0%3D 10.1038/35083620
    • Li LY, Luo X, Wang X (2001) Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412:95-99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 21
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • 9989411 1:CAS:528:DyaK1MXhtFOhu78%3D 10.1038/17135
    • Susin SA, Lorenzo HK, Zamzami N et al (1999) Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 397:441-446
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 22
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • 8689682 1:CAS:528:DyaK28XktlGnsbY%3D 10.1016/S0092-8674(00)80085-9
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147-157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 23
    • 0037427479 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: An introduction
    • 12729576 1:CAS:528:DC%2BD3sXjt1Kisr8%3D 10.1016/S0006-291X(03)00614-4
    • Kroemer G (2003) Mitochondrial control of apoptosis: an introduction. Biochem Biophys Res Commun 304:433-435
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 433-435
    • Kroemer, G.1
  • 24
    • 0032550363 scopus 로고    scopus 로고
    • The permeability transition pore complex: A target for apoptosis regulation by caspases and bcl-2-related proteins
    • 9547337 1:CAS:528:DyaK1cXis1Cru7c%3D 10.1084/jem.187.8.1261
    • Marzo I, Brenner C, Zamzami N et al (1998) The permeability transition pore complex: a target for apoptosis regulation by caspases and bcl-2-related proteins. J Exp Med 187:1261-1271
    • (1998) J Exp Med , vol.187 , pp. 1261-1271
    • Marzo, I.1    Brenner, C.2    Zamzami, N.3
  • 25
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • 11782314 1:CAS:528:DC%2BD38Xos1ShtQ%3D%3D 10.1016/S1534-5807(01)00116-2
    • Scorrano L, Ashiya M, Buttle K et al (2002) A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev Cell 2:55-67
    • (2002) Dev Cell , vol.2 , pp. 55-67
    • Scorrano, L.1    Ashiya, M.2    Buttle, K.3
  • 26
    • 0037418843 scopus 로고    scopus 로고
    • BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis
    • 12624178 1:CAS:528:DC%2BD3sXis1Cgt7Y%3D 10.1126/science.1081208
    • Scorrano L, Oakes SA, Opferman JT et al (2003) BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis. Science 300:135-139
    • (2003) Science , vol.300 , pp. 135-139
    • Scorrano, L.1    Oakes, S.A.2    Opferman, J.T.3
  • 27
    • 9644295726 scopus 로고    scopus 로고
    • Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis
    • 15452118 1:CAS:528:DC%2BD2cXhtVWjs7bF 10.1074/jbc.M408493200
    • Morishima N, Nakanishi K, Tsuchiya K, Shibata T, Seiwa E (2004) Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis. J Biol Chem 279:50375-50381
    • (2004) J Biol Chem , vol.279 , pp. 50375-50381
    • Morishima, N.1    Nakanishi, K.2    Tsuchiya, K.3    Shibata, T.4    Seiwa, E.5
  • 28
    • 0035823571 scopus 로고    scopus 로고
    • The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function
    • 11438535 1:CAS:528:DC%2BD3MXmslyltL0%3D 10.1074/jbc.M104080200
    • Neuss M, Monticone R, Lundberg MS, Chesley AT, Fleck E, Crow MT (2001) The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function. J Biol Chem 276:33915-33922
    • (2001) J Biol Chem , vol.276 , pp. 33915-33922
    • Neuss, M.1    Monticone, R.2    Lundberg, M.S.3    Chesley, A.T.4    Fleck, E.5    Crow, M.T.6
  • 29
    • 34250222466 scopus 로고    scopus 로고
    • Mitochondrial involvement in IGF-1 induced protection of cardiomyocytes against hypoxia/reoxygenation injury
    • 17264981 1:CAS:528:DC%2BD2sXmtFens74%3D 10.1007/s11010-007-9410-0
    • Pi Y, Goldenthal MJ, Marin-Garcia J (2007) Mitochondrial involvement in IGF-1 induced protection of cardiomyocytes against hypoxia/reoxygenation injury. Mol Cell Biochem 301:181-189
    • (2007) Mol Cell Biochem , vol.301 , pp. 181-189
    • Pi, Y.1    Goldenthal, M.J.2    Marin-Garcia, J.3
  • 30
    • 41249086364 scopus 로고    scopus 로고
    • Mitochondrial centrality in heart failure
    • 18185992 10.1007/s10741-007-9079-1
    • Marín-García J, Goldenthal MJ (2008) Mitochondrial centrality in heart failure. Heart Fail Rev 13:137-150
    • (2008) Heart Fail Rev , vol.13 , pp. 137-150
    • Marín-García, J.1    Goldenthal, M.J.2
  • 31
    • 0030870555 scopus 로고    scopus 로고
    • The bcl-2 gene product prevents programmed cell death of ventricular myocytes
    • 9315550 1:CAS:528:DyaK2sXmtFeisL0%3D 10.1161/01.CIR.96.5.1580
    • Kirshenbaum LA, de Moissac D (1997) The bcl-2 gene product prevents programmed cell death of ventricular myocytes. Circulation 96:1580-1585
    • (1997) Circulation , vol.96 , pp. 1580-1585
    • Kirshenbaum, L.A.1    De Moissac, D.2
  • 32
    • 0035695645 scopus 로고    scopus 로고
    • Regulation of sodium-calcium exchange and mitochondrial energetics by Bcl-2 in the heart of transgenic mice
    • 11735260 1:CAS:528:DC%2BD3MXovV2msLs%3D 10.1006/jmcc.2001.1476
    • Zhu L, Yu Y, Chua BH, Ho YS, Kuo TH (2001) Regulation of sodium-calcium exchange and mitochondrial energetics by Bcl-2 in the heart of transgenic mice. J Mol Cell Cardiol 33:2135-2144
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 2135-2144
    • Zhu, L.1    Yu, Y.2    Chua, B.H.3    Ho, Y.S.4    Kuo, T.H.5
  • 33
    • 0034698118 scopus 로고    scopus 로고
    • Morphological and molecular characterization of adult cardiomyocyte apoptosis during hypoxia and reoxygenation
    • 10903995 1:CAS:528:DC%2BD3cXlt1aitbk%3D 10.1161/01.RES.87.2.118
    • Kang PM, Haunstetter A, Aoki H, Usheva A, Izumo S (2000) Morphological and molecular characterization of adult cardiomyocyte apoptosis during hypoxia and reoxygenation. Circ Res 87:118-125
    • (2000) Circ Res , vol.87 , pp. 118-125
    • Kang, P.M.1    Haunstetter, A.2    Aoki, H.3    Usheva, A.4    Izumo, S.5
  • 34
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • 10995435 1:CAS:528:DC%2BD3cXmslGmur8%3D 10.1083/jcb.150.6.1283
    • Milner DJ, Mavroidis M, Weisleder N, Capetanaki Y (2000) Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J Cell Biol 150:1283-1298
    • (2000) J Cell Biol , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanaki, Y.4
  • 35
    • 0034750422 scopus 로고    scopus 로고
    • Effects of desmin gene knockout on mice heart mitochondria
    • 11710808 1:CAS:528:DC%2BD3MXnvF2ntro%3D 10.1023/A:1010611408007
    • Linden M, Li Z, Paulin D, Gotow T, Leterrier JF (2001) Effects of desmin gene knockout on mice heart mitochondria. J Bioenerg Biomembr 33:333-341
    • (2001) J Bioenerg Biomembr , vol.33 , pp. 333-341
    • Linden, M.1    Li, Z.2    Paulin, D.3    Gotow, T.4    Leterrier, J.F.5
  • 36
    • 1642433232 scopus 로고    scopus 로고
    • Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy
    • 14715896 1:CAS:528:DC%2BD2cXhsVWhurk%3D 10.1073/pnas.0303202101
    • Weisleder N, Taffet GE, Capetanaki Y (2004) Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy. Proc Natl Acad Sci USA 101:769-774
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 769-774
    • Weisleder, N.1    Taffet, G.E.2    Capetanaki, Y.3
  • 37
    • 4944265466 scopus 로고    scopus 로고
    • Transgenic expression of Bcl-2 modulates energy metabolism, prevents cytosolic acidification during ischemia, and reduces ischemia/reperfusion injury
    • 15345651 1:CAS:528:DC%2BD2cXnvVekurw%3D 10.1161/01.RES.0000143898.67182. 4c
    • Imahashi K, Schneider MD, Steenbergen C, Murphy E (2004) Transgenic expression of Bcl-2 modulates energy metabolism, prevents cytosolic acidification during ischemia, and reduces ischemia/reperfusion injury. Circ Res 95:734-741
    • (2004) Circ Res , vol.95 , pp. 734-741
    • Imahashi, K.1    Schneider, M.D.2    Steenbergen, C.3    Murphy, E.4
  • 38
    • 10644244369 scopus 로고    scopus 로고
    • AIF deficiency compromises oxidative phosphorylation
    • 15526035 1:CAS:528:DC%2BD2cXhtVWisr3N 10.1038/sj.emboj.7600461
    • Vahsen N, Cande C, Briere JJ et al (2004) AIF deficiency compromises oxidative phosphorylation. EMBO J 23:4679-4689
    • (2004) EMBO J , vol.23 , pp. 4679-4689
    • Vahsen, N.1    Cande, C.2    Briere, J.J.3
  • 39
    • 27944475065 scopus 로고    scopus 로고
    • Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy
    • 16287843 1:CAS:528:DC%2BD2MXht1OnsL7M 10.1128/MCB.25.23.10261-10272.2005
    • Joza N, Oudit GY, Brown D et al (2005) Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy. Mol Cell Biol 25:10261-10272
    • (2005) Mol Cell Biol , vol.25 , pp. 10261-10272
    • Joza, N.1    Oudit, G.Y.2    Brown, D.3
  • 40
    • 0030031983 scopus 로고    scopus 로고
    • Apoptotic and necrotic myocyte cell deaths are independent contributing variables of infarct size in rats
    • 8569201 1:STN:280:DyaK287lsVWmsQ%3D%3D
    • Kajstura J, Cheng W, Reiss K et al (1996) Apoptotic and necrotic myocyte cell deaths are independent contributing variables of infarct size in rats. Lab Invest 74:86-107
    • (1996) Lab Invest , vol.74 , pp. 86-107
    • Kajstura, J.1    Cheng, W.2    Reiss, K.3
  • 41
    • 0033058929 scopus 로고    scopus 로고
    • Myocyte loss in chronic heart failure
    • 10398167 1:STN:280:DyaK1MzlvFGqug%3D%3D 10.1002/(SICI)1096-9896(199906) 188:2<213: AID-PATH348>3.0.CO;2-5
    • Rayment NB, Haven AJ, Madden B et al (1999) Myocyte loss in chronic heart failure. J Pathol 188:213-219
    • (1999) J Pathol , vol.188 , pp. 213-219
    • Rayment, N.B.1    Haven, A.J.2    Madden, B.3
  • 42
    • 0036156875 scopus 로고    scopus 로고
    • Losing heart: The role of apoptosis in heart disease - A novel therapeutic target?
    • 11818361 1:CAS:528:DC%2BD38XhsVCitr4%3D 10.1096/fj.01-0629com
    • Gill C, Mestril R, Samali A (2002) Losing heart: the role of apoptosis in heart disease - a novel therapeutic target? Faseb J 16:135-146
    • (2002) Faseb J , vol.16 , pp. 135-146
    • Gill, C.1    Mestril, R.2    Samali, A.3
  • 43
    • 0034133036 scopus 로고    scopus 로고
    • Assessment of secondary necrosis of Jurkat cells using a new microscopic system and double staining method with annexin v and propidium iodide
    • 10639571 1:CAS:528:DC%2BD3cXnvF2mtg%3D%3D
    • Honda O, Kuroda M, Joja I et al (2000) Assessment of secondary necrosis of Jurkat cells using a new microscopic system and double staining method with annexin V and propidium iodide. Int J Oncol 16:283-288
    • (2000) Int J Oncol , vol.16 , pp. 283-288
    • Honda, O.1    Kuroda, M.2    Joja, I.3
  • 44
    • 33644524120 scopus 로고    scopus 로고
    • Apoptosis and necrosis in the liver: A tale of two deaths?
    • 16447272 1:CAS:528:DC%2BD28XhvVSkt78%3D 10.1002/hep.21062
    • Malhi H, Gores GJ, Lemasters JJ (2006) Apoptosis and necrosis in the liver: a tale of two deaths? Hepatology 43:S31-S44
    • (2006) Hepatology , vol.43
    • Malhi, H.1    Gores, G.J.2    Lemasters, J.J.3
  • 45
    • 0037427440 scopus 로고    scopus 로고
    • Mitochondrial permeability transition: A common pathway to necrosis and apoptosis
    • 12729580 1:CAS:528:DC%2BD3sXjt1Kisrs%3D 10.1016/S0006-291X(03)00618-1
    • Kim JS, He L, Lemasters JJ (2003) Mitochondrial permeability transition: a common pathway to necrosis and apoptosis. Biochem Biophys Res Commun 304:463-470
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 463-470
    • Kim, J.S.1    He, L.2    Lemasters, J.J.3
  • 46
    • 0032504568 scopus 로고    scopus 로고
    • The mitochondrial permeability transition in cell death: A common mechanism in necrosis, apoptosis and autophagy
    • 9714796 1:CAS:528:DyaK1cXltFWksb4%3D 10.1016/S0005-2728(98)00112-1
    • Lemasters JJ, Nieminen AL, Qian T et al (1998) The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochim Biophys Acta 1366:177-196
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 177-196
    • Lemasters, J.J.1    Nieminen, A.L.2    Qian, T.3
  • 47
    • 0030848374 scopus 로고    scopus 로고
    • Mitochondrial implication in accidental and programmed cell death: Apoptosis and necrosis
    • 9239543 1:CAS:528:DyaK2sXksFahtb4%3D 10.1023/A:1022694131572
    • Zamzami N, Hirsch T, Dallaporta B, Petit PX, Kroemer G (1997) Mitochondrial implication in accidental and programmed cell death: apoptosis and necrosis. J Bioenerg Biomembr 29:185-193
    • (1997) J Bioenerg Biomembr , vol.29 , pp. 185-193
    • Zamzami, N.1    Hirsch, T.2    Dallaporta, B.3    Petit, P.X.4    Kroemer, G.5
  • 48
    • 34848902937 scopus 로고    scopus 로고
    • Ca2+- and mitochondrial-dependent cardiomyocyte necrosis as a primary mediator of heart failure
    • 17694179 1:CAS:528:DC%2BD2sXhtVCms7vO 10.1172/JCI31060
    • Nakayama H, Chen X, Baines CP et al (2007) Ca2+- and mitochondrial- dependent cardiomyocyte necrosis as a primary mediator of heart failure. J Clin Invest 117:2431-2444
    • (2007) J Clin Invest , vol.117 , pp. 2431-2444
    • Nakayama, H.1    Chen, X.2    Baines, C.P.3
  • 49
    • 0025104163 scopus 로고
    • Proteolysis of myosin and troponin in human myocardium of elderly subjects
    • 2273558 1:CAS:528:DyaK3MXhsVSnsLc%3D 10.1536/ihj.31.683
    • Yoshida K, Hanafusa T, Matoba R, Wakasugi C (1990) Proteolysis of myosin and troponin in human myocardium of elderly subjects. Jpn Heart J 31:683-691
    • (1990) Jpn Heart J , vol.31 , pp. 683-691
    • Yoshida, K.1    Hanafusa, T.2    Matoba, R.3    Wakasugi, C.4
  • 50
    • 0034613294 scopus 로고    scopus 로고
    • Age-related decline in chaperone-mediated autophagy
    • 10806201 1:CAS:528:DC%2BD3cXntlCitLY%3D 10.1074/jbc.M002102200
    • Cuervo AM, Dice JF (2000) Age-related decline in chaperone-mediated autophagy. J Biol Chem 275:31505-31513
    • (2000) J Biol Chem , vol.275 , pp. 31505-31513
    • Cuervo, A.M.1    Dice, J.F.2
  • 51
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • 15524167 1:CAS:528:DC%2BD2cXotlCrtr4%3D 10.1023/B:MCBI.0000041848.57020. 57
    • Cuervo AM (2004) Autophagy: many paths to the same end. Mol Cell Biochem 263(1-2):55-72
    • (2004) Mol Cell Biochem , vol.263 , Issue.1-2 , pp. 55-72
    • Cuervo, A.M.1
  • 52
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • 15068787 1:CAS:528:DC%2BD2cXjsFeqsbs%3D 10.1016/S1534-5807(04)00099-1
    • Levine B, Klionsky DJ (2004) Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 6:463-477
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 53
    • 1342321743 scopus 로고    scopus 로고
    • Two ubiquitin-like conjugation systems essential for autophagy
    • 15209383 1:CAS:528:DC%2BD2cXhsFWksrg%3D 10.1016/j.semcdb.2003.12.004
    • Ohsumi Y, Mizushima N (2004) Two ubiquitin-like conjugation systems essential for autophagy. Semin Cell Dev Biol 15:231-236
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 231-236
    • Ohsumi, Y.1    Mizushima, N.2
  • 54
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • 15247238 1:CAS:528:DC%2BD2cXnt1yjsbY%3D 10.1074/jbc.M406960200
    • Kissova I, Deffieu M, Manon S, Camougrand N (2004) Uth1p is involved in the autophagic degradation of mitochondria. J Biol Chem 279:39068-39074
    • (2004) J Biol Chem , vol.279 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 55
    • 16844366524 scopus 로고    scopus 로고
    • Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging
    • 15798367 1:CAS:528:DC%2BD2MXislagtbc%3D 10.1089/rej.2005.8.3
    • Lemasters JJ (2005) Selective mitochondrial autophagy, or mitophagy, as a targeted defense against oxidative stress, mitochondrial dysfunction, and aging. Rejuvenation Res 8:3-5
    • (2005) Rejuvenation Res , vol.8 , pp. 3-5
    • Lemasters, J.J.1
  • 56
    • 34447133404 scopus 로고    scopus 로고
    • Cardiac autophagy is a maladaptive response to hemodynamic stress
    • 17607355 1:CAS:528:DC%2BD2sXnvVagur4%3D 10.1172/JCI27523
    • Zhu H, Tannous P, Johnstone JL et al (2007) Cardiac autophagy is a maladaptive response to hemodynamic stress. J Clin Invest 117:1782-1793
    • (2007) J Clin Invest , vol.117 , pp. 1782-1793
    • Zhu, H.1    Tannous, P.2    Johnstone, J.L.3
  • 57
    • 25444473426 scopus 로고    scopus 로고
    • Autophagy in chronically ischemic myocardium
    • 16174725 1:CAS:528:DC%2BD2MXhtVOqsbrP 10.1073/pnas.0506843102
    • Yan L, Vatner DE, Kim SJ et al (2005) Autophagy in chronically ischemic myocardium. Proc Natl Acad Sci USA 102:13807-13812
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13807-13812
    • Yan, L.1    Vatner, D.E.2    Kim, S.J.3
  • 58
    • 33745816360 scopus 로고    scopus 로고
    • Autophagic degeneration and death of cardiomyocytes in heart failure
    • 16874110 1:CAS:528:DC%2BD28XnsVWjsbs%3D
    • Takemura G, Miyata S, Kawase Y, Okada H, Maruyama R, Fujiwara H (2006) Autophagic degeneration and death of cardiomyocytes in heart failure. Autophagy 2:212-214
    • (2006) Autophagy , vol.2 , pp. 212-214
    • Takemura, G.1    Miyata, S.2    Kawase, Y.3    Okada, H.4    Maruyama, R.5    Fujiwara, H.6
  • 59
    • 0032579473 scopus 로고    scopus 로고
    • On the degradability and exocytosis of ceroid/lipofuscin in cultured rat cardiac myocytes
    • 9541135 1:CAS:528:DyaK1cXhsFenu7Y%3D 10.1016/S0047-6374(97)00129-2
    • Terman A, Brunk UT (1998) On the degradability and exocytosis of ceroid/lipofuscin in cultured rat cardiac myocytes. Mech Ageing Dev 100:145-156
    • (1998) Mech Ageing Dev , vol.100 , pp. 145-156
    • Terman, A.1    Brunk, U.T.2
  • 60
    • 26044482960 scopus 로고    scopus 로고
    • Protein oxidation and degradation during postmitotic senescence
    • 16214036 1:CAS:528:DC%2BD2MXhtVymsrbF 10.1016/j.freeradbiomed.2005.06.009
    • Grune T, Merker K, Jung T, Sitte N, Davies KJ (2005) Protein oxidation and degradation during postmitotic senescence. Free Radic Biol Med 39:1208-1215
    • (2005) Free Radic Biol Med , vol.39 , pp. 1208-1215
    • Grune, T.1    Merker, K.2    Jung, T.3    Sitte, N.4    Davies, K.J.5
  • 61
    • 0030451773 scopus 로고    scopus 로고
    • Effect of age on in vivo rates of mitochondrial protein synthesis in human skeletal muscle
    • 8986817 1:CAS:528:DyaK2sXnsV2j 10.1073/pnas.93.26.15364
    • Rooyackers OE, Adey DB, Ades PA, Nair KS (1996) Effect of age on in vivo rates of mitochondrial protein synthesis in human skeletal muscle. Proc Natl Acad Sci USA 93:15364-15369
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15364-15369
    • Rooyackers, O.E.1    Adey, D.B.2    Ades, P.A.3    Nair, K.S.4
  • 62
    • 0036236006 scopus 로고    scopus 로고
    • The mitochondrial-lysosomal axis theory of aging: Accumulation of damaged mitochondria as a result of imperfect autophagocytosis
    • 11985575 1:CAS:528:DC%2BD38XjsFWlt7w%3D 10.1046/j.1432-1033.2002.02869.x
    • Brunk UT, Terman A (2002) The mitochondrial-lysosomal axis theory of aging: accumulation of damaged mitochondria as a result of imperfect autophagocytosis. Eur J Biochem 269:1996-2002
    • (2002) Eur J Biochem , vol.269 , pp. 1996-2002
    • Brunk, U.T.1    Terman, A.2
  • 63
    • 27644467802 scopus 로고    scopus 로고
    • Autophagy in cardiac myocyte homeostasis, aging, and pathology
    • 16213475 1:CAS:528:DC%2BD2MXht1Sqsr3O 10.1016/j.cardiores.2005.08.014
    • Terman A, Brunk UT (2005) Autophagy in cardiac myocyte homeostasis, aging, and pathology. Cardiovasc Res 68(3):355-365
    • (2005) Cardiovasc Res , vol.68 , Issue.3 , pp. 355-365
    • Terman, A.1    Brunk, U.T.2
  • 64
    • 80255137555 scopus 로고    scopus 로고
    • The role of lysosomes in iron metabolism and recycling
    • 21907822 1:CAS:528:DC%2BC3MXhtl2gsrjM 10.1016/j.biocel.2011.08.016
    • Kurz T, Eaton JW, Brunk UT (2011) The role of lysosomes in iron metabolism and recycling. Int J Biochem Cell Biol 43:1686-1697
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1686-1697
    • Kurz, T.1    Eaton, J.W.2    Brunk, U.T.3
  • 65
    • 0034983544 scopus 로고    scopus 로고
    • Lysosomal involvement in apoptosis
    • 11450988 1:CAS:528:DC%2BD3MXlt12gtbk%3D 10.1179/135100001101536094
    • Brunk UT, Neuzil J, Eaton JW (2001) Lysosomal involvement in apoptosis. Redox Rep 6:91-97
    • (2001) Redox Rep , vol.6 , pp. 91-97
    • Brunk, U.T.1    Neuzil, J.2    Eaton, J.W.3
  • 66
    • 33749656530 scopus 로고    scopus 로고
    • The lysosomal-mitochondrial axis theory of postmitotic aging and cell death
    • 16737690 1:CAS:528:DC%2BD28XhtFSksbzO 10.1016/j.cbi.2006.04.013
    • Terman A, Gustafsson B, Brunk UT (2006) The lysosomal-mitochondrial axis theory of postmitotic aging and cell death. Chem Biol Interact 163:29-37
    • (2006) Chem Biol Interact , vol.163 , pp. 29-37
    • Terman, A.1    Gustafsson, B.2    Brunk, U.T.3
  • 67
    • 33744905803 scopus 로고    scopus 로고
    • Autophagy: A novel protective mechanism in chronic ischemia
    • 16760663 1:CAS:528:DC%2BD28XnvFWqtLo%3D 10.4161/cc.5.11.2787
    • Yan L, Sadoshima J, Vatner DE, Vatner SF (2006) Autophagy: a novel protective mechanism in chronic ischemia. Cell Cycle 5:1175-1177
    • (2006) Cell Cycle , vol.5 , pp. 1175-1177
    • Yan, L.1    Sadoshima, J.2    Vatner, D.E.3    Vatner, S.F.4
  • 68
    • 33744525885 scopus 로고    scopus 로고
    • How do cardiomyocytes die?" apoptosis and autophagic cell death in cardiac myocytes
    • 16762802 1:CAS:528:DC%2BD28Xltleltr4%3D 10.1016/j.cardfail.2006.02.002
    • Kunapuli S, Rosanio S, Schwarz ER (2006) "How do cardiomyocytes die?" apoptosis and autophagic cell death in cardiac myocytes. J Card Fail 12:381-391
    • (2006) J Card Fail , vol.12 , pp. 381-391
    • Kunapuli, S.1    Rosanio, S.2    Schwarz, E.R.3
  • 69
    • 78649906421 scopus 로고    scopus 로고
    • Mitochondrial fission and autophagy in the normal and diseased heart
    • 20865352 10.1007/s11906-010-0147-x
    • Iglewski M, Hill JA, Lavandero S, Rothermel BA (2010) Mitochondrial fission and autophagy in the normal and diseased heart. Curr Hypertens Rep 12:418-425
    • (2010) Curr Hypertens Rep , vol.12 , pp. 418-425
    • Iglewski, M.1    Hill, J.A.2    Lavandero, S.3    Rothermel, B.A.4
  • 70
    • 77955342581 scopus 로고    scopus 로고
    • Inhibition of autophagy in the heart induces age-related cardiomyopathy
    • 20431347 1:CAS:528:DC%2BC3cXhtVGlsL7K 10.4161/auto.6.5.11947
    • Taneike M, Yamaguchi O, Nakai A et al. (2010) Inhibition of autophagy in the heart induces age-related cardiomyopathy. Autophagy 6(5):600-606
    • (2010) Autophagy , vol.6 , Issue.5 , pp. 600-606
    • Taneike, M.1    Yamaguchi, O.2    Nakai, A.3
  • 71
    • 52949136220 scopus 로고    scopus 로고
    • Cell death in heart failure
    • Nishida K, Otsu K (2008) Cell death in heart failure. Circ J 72(Suppl A):A17-A21
    • (2008) Circ J , vol.72 , Issue.SUPPL. A
    • Nishida, K.1    Otsu, K.2
  • 72
    • 34249714158 scopus 로고    scopus 로고
    • The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
    • 17450150 1:CAS:528:DC%2BD2sXkvVOgsr4%3D 10.1038/nm1574
    • Nakai A, Yamaguchi O, Takeda T et al (2007) The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress. Nat Med 13:619-624
    • (2007) Nat Med , vol.13 , pp. 619-624
    • Nakai, A.1    Yamaguchi, O.2    Takeda, T.3
  • 73
    • 77951096150 scopus 로고    scopus 로고
    • Mitochondrial dynamics-fusion, fission, movement, and mitophagy - In neurodegenerative diseases
    • Chen H, Chan DC (2009) Mitochondrial dynamics-fusion, fission, movement, and mitophagy - in neurodegenerative diseases. Hum Mol Genet 18(R2):R169-R176
    • (2009) Hum Mol Genet , vol.18 , Issue.R2
    • Chen, H.1    Chan, D.C.2
  • 74
    • 67650868959 scopus 로고    scopus 로고
    • Mitochondrial dynamics in mammalian health and disease
    • Liesa M, Palacin M, Zorzano A (2009) Mitochondrial dynamics in mammalian health and disease. Physiol Rev 89:799-845
    • (2009) Physiol Rev , vol.89 , pp. 799-845
    • Liesa, M.1    Palacin, M.2    Zorzano, A.3
  • 75
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • 17928812 1:CAS:528:DC%2BD2sXhtF2qsLzE 10.1038/nrm2275
    • Detmer SA, Chan DC (2007) Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 8:870-879
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 870-879
    • Detmer, S.A.1    Chan, D.C.2
  • 76
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • 16285870 1:CAS:528:DC%2BD28Xlt1Wqsg%3D%3D 10.1146/annurev.genet.38. 072902.093019
    • Okamoto K, Shaw JM (2005) Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu Rev Genet 39:503-536
    • (2005) Annu Rev Genet , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 77
    • 49349102894 scopus 로고    scopus 로고
    • Mitochondrial fusion, fission and autophagy as a quality control axis: The bioenergetic view
    • 18519024 1:CAS:528:DC%2BD1cXpvF2qt7g%3D 10.1016/j.bbabio.2008.05.001
    • Twig G, Hyde B, Shirihai OS (2008) Mitochondrial fusion, fission and autophagy as a quality control axis: the bioenergetic view. Biochim Biophys Acta 1777:1092-1097
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 1092-1097
    • Twig, G.1    Hyde, B.2    Shirihai, O.S.3
  • 78
    • 77955287381 scopus 로고    scopus 로고
    • Physiological functions of mitochondrial fusion
    • 20649534 1:CAS:528:DC%2BC3cXhtFegsL3E 10.1111/j.1749-6632.2010.05615.x
    • Chen H, Chen DC (2010) Physiological functions of mitochondrial fusion. Ann NY Acad Sci 1201:21-25
    • (2010) Ann NY Acad Sci , vol.1201 , pp. 21-25
    • Chen, H.1    Chen, D.C.2
  • 79
    • 77954536442 scopus 로고    scopus 로고
    • Mitochondrial fission controls DNA fragmentation by regulating endonuclease G
    • 20594982 1:CAS:528:DC%2BC3cXoslWrsLg%3D 10.1016/j.freeradbiomed.2010.05. 021
    • Li J, Zhou J, Li Y, Qin D, Li P (2010) Mitochondrial fission controls DNA fragmentation by regulating endonuclease G. Free Radic Biol Med 49:622-631
    • (2010) Free Radic Biol Med , vol.49 , pp. 622-631
    • Li, J.1    Zhou, J.2    Li, Y.3    Qin, D.4    Li, P.5
  • 80
    • 79961021186 scopus 로고    scopus 로고
    • Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus
    • 21747057 1:CAS:528:DC%2BC3MXptlyktbg%3D 10.1161/CIRCULATIONAHA.110.014506
    • Shenouda SM, Widlansky ME, Chen K et al (2011) Altered mitochondrial dynamics contributes to endothelial dysfunction in diabetes mellitus. Circulation 124:444-453
    • (2011) Circulation , vol.124 , pp. 444-453
    • Shenouda, S.M.1    Widlansky, M.E.2    Chen, K.3
  • 81
    • 33749991592 scopus 로고    scopus 로고
    • Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1
    • 17055438 1:CAS:528:DC%2BD28XhtFOkt73F 10.1016/j.cell.2006.09.021
    • Meeusen S, DeVay R, Block J et al (2006) Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1. Cell 127:383-395
    • (2006) Cell , vol.127 , pp. 383-395
    • Meeusen, S.1    Devay, R.2    Block, J.3
  • 82
    • 68149103297 scopus 로고    scopus 로고
    • Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion
    • 19477917 1:CAS:528:DC%2BD1MXhsVClt7zI 10.1091/mbc.E09-03-0252
    • Song Z, Ghochani M, McCaffery JM, Frey TG, Chan DC (2009) Mitofusins and OPA1 mediate sequential steps in mitochondrial membrane fusion. Mol Biol Cell 20:3525-3532
    • (2009) Mol Biol Cell , vol.20 , pp. 3525-3532
    • Song, Z.1    Ghochani, M.2    McCaffery, J.M.3    Frey, T.G.4    Chan, D.C.5
  • 83
    • 34249693479 scopus 로고    scopus 로고
    • A splice site mutation in the murine Opa1 gene features pathology of autosomal dominant optic atrophy
    • 17314202 10.1093/brain/awm005
    • Alavi MV, Bette S, Schimpf S et al (2007) A splice site mutation in the murine Opa1 gene features pathology of autosomal dominant optic atrophy. Brain 130:1029-1042
    • (2007) Brain , vol.130 , pp. 1029-1042
    • Alavi, M.V.1    Bette, S.2    Schimpf, S.3
  • 84
    • 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
    • 17428816 1:CAS:528:DC%2BD2sXnsl2jtb4%3D 10.1093/hmg/ddm079
    • Davies VJ, Hollins AJ, Piechota MJ et al (2007) Opa1 deficiency in a mouse model of autosomal dominant optic atrophy impairs mitochondrial morphology, optic nerve structure and visual function. Hum Mol Genet 16:1307-1318
    • (2007) Hum Mol Genet , vol.16 , pp. 1307-1318
    • Davies, V.J.1    Hollins, A.J.2    Piechota, M.J.3
  • 85
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo M, Legros F, Chateau D, Lombes A (2002) Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J Cell Sci 15:1663-1674
    • (2002) J Cell Sci , vol.15 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 86
    • 0035911963 scopus 로고    scopus 로고
    • UGO1 encodes an outer membrane protein required for mitochondrial fusion
    • 11257114 1:CAS:528:DC%2BD3MXit1egtrs%3D 10.1083/jcb.152.6.1123
    • Sesaki H, Jensen RE (2001) UGO1 encodes an outer membrane protein required for mitochondrial fusion. J Cell Biol 152:1123-1134
    • (2001) J Cell Biol , vol.152 , pp. 1123-1134
    • Sesaki, H.1    Jensen, R.E.2
  • 87
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • 15899901 1:CAS:528:DC%2BD2MXlvFymt7s%3D 10.1074/jbc.M503062200
    • Chen H, Chomyn A, Chan DC (2005) Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 280:26185-26192
    • (2005) J Biol Chem , vol.280 , pp. 26185-26192
    • Chen, H.1    Chomyn, A.2    Chan, D.C.3
  • 88
    • 38849192448 scopus 로고    scopus 로고
    • OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes
    • 18158317 10.1093/brain/awm298
    • Amati-Bonneau P, Valentino ML, Reynier P et al (2008) OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes. Brain 131:338-351
    • (2008) Brain , vol.131 , pp. 338-351
    • Amati-Bonneau, P.1    Valentino, M.L.2    Reynier, P.3
  • 89
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • 19052620 10.1038/nature07534 1:CAS:528:DC%2BD1cXhsVGlur7J
    • de Brito OM, Scorrano L (2008) Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456:605-610
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 90
    • 38849151612 scopus 로고    scopus 로고
    • Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: A novel disorder of mtDNA maintenance
    • 18065439 10.1093/brain/awm272
    • Hudson G, Amati-Bonneau P, Blakely EL et al (2008) Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance. Brain 131:329-337
    • (2008) Brain , vol.131 , pp. 329-337
    • Hudson, G.1    Amati-Bonneau, P.2    Blakely, E.L.3
  • 91
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • 1:CAS:528:DC%2BD2cXpslKns7c%3D
    • Lee YJ, Jeong SY, Karbowski M, Smith CL, Youle RJ (2004) Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol Biol 15:5001-5011
    • (2004) Mol Biol , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 92
    • 44649129342 scopus 로고    scopus 로고
    • The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells
    • 18353969 1:CAS:528:DC%2BD1cXntV2rtrg%3D 10.1091/mbc.E07-12-1287
    • Gandre-Babbe S, van der Bliek AM (2008) The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells. Mol Biol Cell 19:2402-2412
    • (2008) Mol Biol Cell , vol.19 , pp. 2402-2412
    • Gandre-Babbe, S.1    Van Der Bliek, A.M.2
  • 93
    • 78650167618 scopus 로고    scopus 로고
    • Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
    • 21149567 1:CAS:528:DC%2BC3cXhs1SmurfL 10.1083/jcb.201007152
    • Otera H, Wang C, Cleland MM et al (2010) Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells. J Cell Biol 191:1141-1158
    • (2010) J Cell Biol , vol.191 , pp. 1141-1158
    • Otera, H.1    Wang, C.2    Cleland, M.M.3
  • 94
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • 21102612 1:CAS:528:DC%2BC3cXhsVGrurnN 10.1038/nrm3013
    • Westermann B (2010) Mitochondrial fusion and fission in cell life and death. Nat Rev Mol Cell Biol 11:872-884
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 872-884
    • Westermann, B.1
  • 95
    • 45349094984 scopus 로고    scopus 로고
    • Mitochondrial dynamics and apoptosis
    • 18559474 1:CAS:528:DC%2BD1cXnvVWmsb4%3D 10.1101/gad.1658508
    • Suen DF, Norris KL, Youle RJ (2008) Mitochondrial dynamics and apoptosis. Genes Dev 22:1577-1590
    • (2008) Genes Dev , vol.22 , pp. 1577-1590
    • Suen, D.F.1    Norris, K.L.2    Youle, R.J.3
  • 96
    • 0036242518 scopus 로고    scopus 로고
    • Cell cycle dependent morphology changes and associated mitochondrial DNA redistribution in mitochondria of human cell lines
    • 16120295 1:CAS:528:DC%2BD38XktVKntL8%3D 10.1016/S1567-7249(02)00006-5
    • Margineantu DH, Gregory CW, Sundell L, Sherwood SW, Beechem JM, Capaldi RA (2002) Cell cycle dependent morphology changes and associated mitochondrial DNA redistribution in mitochondria of human cell lines. Mitochondrion 1:425-435
    • (2002) Mitochondrion , vol.1 , pp. 425-435
    • Margineantu, D.H.1    Gregory, C.W.2    Sundell, L.3    Sherwood, S.W.4    Beechem, J.M.5    Capaldi, R.A.6
  • 97
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • 20403324 1:CAS:528:DC%2BC3cXmtVWnsLg%3D 10.1016/j.cell.2010.02.026
    • Chen H, Vermulst M, Wang YE et al (2010) Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell 141:280-289
    • (2010) Cell , vol.141 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3
  • 98
    • 78651480831 scopus 로고    scopus 로고
    • OPA1 links human mitochondrial genome maintenance to mtDNA replication and distribution
    • 20974897 1:CAS:528:DC%2BC3MXps12nug%3D%3D 10.1101/gr.108696.110
    • Elachouri G, Vidoni S, Zanna C et al (2011) OPA1 links human mitochondrial genome maintenance to mtDNA replication and distribution. Genome Res 21:12-20
    • (2011) Genome Res , vol.21 , pp. 12-20
    • Elachouri, G.1    Vidoni, S.2    Zanna, C.3
  • 99
    • 38849190029 scopus 로고    scopus 로고
    • OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion
    • 18222991 10.1093/brain/awm335
    • Zanna C, Ghelli A, Porcelli AM et al (2008) OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion. Brain 131:352-367
    • (2008) Brain , vol.131 , pp. 352-367
    • Zanna, C.1    Ghelli, A.2    Porcelli, A.M.3
  • 100
    • 20444461625 scopus 로고    scopus 로고
    • The charcot-marie-tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system
    • 15829499 1:CAS:528:DC%2BD2MXktlKqtro%3D 10.1093/hmg/ddi149
    • Pich S, Bach D, Briones P et al (2005) The charcot-marie-tooth type 2A gene product, Mfn2, up-regulates fuel oxidation through expression of OXPHOS system. Hum Mol Genet 14:1405-1415
    • (2005) Hum Mol Genet , vol.14 , pp. 1405-1415
    • Pich, S.1    Bach, D.2    Briones, P.3
  • 101
    • 0037593949 scopus 로고    scopus 로고
    • Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity
    • 12598526 1:CAS:528:DC%2BD3sXjsVKmsrk%3D 10.1074/jbc.M212754200
    • Bach D, Pich S, Soriano FX et al (2003) Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism. A novel regulatory mechanism altered in obesity. J Biol Chem 278:17190-17197
    • (2003) J Biol Chem , vol.278 , pp. 17190-17197
    • Bach, D.1    Pich, S.2    Soriano, F.X.3
  • 102
    • 52449134835 scopus 로고    scopus 로고
    • Preventing mitochondrial fission impairs mitochondrial function and leads to loss of mitochondrial DNA
    • 18806874 10.1371/journal.pone.0003257 1:CAS:528:DC%2BD1cXht1amtb7K
    • Parone PA, Da CS, Tondera D et al (2008) Preventing mitochondrial fission impairs mitochondrial function and leads to loss of mitochondrial DNA. PLoS ONE 3:e3257
    • (2008) PLoS ONE , vol.3 , pp. 3257
    • Parone, P.A.1    Da, C.S.2    Tondera, D.3
  • 103
    • 52249096823 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy
    • 18783614 10.1186/1471-2091-9-22 1:CAS:528:DC%2BD1cXhsV2msrbI
    • Mayorov VI, Lowrey AJ, Biousse V, Newman NJ, Cline SD, Brown MD (2008) Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy. BMC Biochem 9:22
    • (2008) BMC Biochem , vol.9 , pp. 22
    • Mayorov, V.I.1    Lowrey, A.J.2    Biousse, V.3    Newman, N.J.4    Cline, S.D.5    Brown, M.D.6
  • 104
    • 34047173074 scopus 로고    scopus 로고
    • Mitochondrial bioenergetics and structural network organization
    • 17298981 1:CAS:528:DC%2BD2sXkt1Cgsrk%3D 10.1242/jcs.03381
    • Benard G, Bellance N, James D et al (2007) Mitochondrial bioenergetics and structural network organization. J Cell Sci 120:838-848
    • (2007) J Cell Sci , vol.120 , pp. 838-848
    • Benard, G.1    Bellance, N.2    James, D.3
  • 105
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • 18200046 1:CAS:528:DC%2BD1cXhtVKkurs%3D 10.1038/sj.emboj.7601963
    • Twig G, Elorza A, Molina AJ et al (2008) Fission and selective fusion govern mitochondrial segregation and elimination by autophagy. EMBO J 27:433-446
    • (2008) EMBO J , vol.27 , pp. 433-446
    • Twig, G.1    Elorza, A.2    Molina, A.J.3
  • 106
    • 33644552417 scopus 로고    scopus 로고
    • Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology
    • 16477035 1:CAS:528:DC%2BD28XksF2rsbk%3D 10.1073/pnas.0511154103
    • Yu T, Robotham JL, Yoon Y (2006) Increased production of reactive oxygen species in hyperglycemic conditions requires dynamic change of mitochondrial morphology. Proc Natl Acad Sci USA 103:2653-2658
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2653-2658
    • Yu, T.1    Robotham, J.L.2    Yoon, Y.3
  • 107
    • 0031720535 scopus 로고    scopus 로고
    • Differential distribution of dynamin isoforms in mammalian cells
    • 9725914 1:CAS:528:DyaK1cXmtFSrurw%3D
    • Cao H, Garcia F, McNiven MA (1998) Differential distribution of dynamin isoforms in mammalian cells. Mol Biol Cell 9:2595-2609
    • (1998) Mol Biol Cell , vol.9 , pp. 2595-2609
    • Cao, H.1    Garcia, F.2    McNiven, M.A.3
  • 108
    • 84856111189 scopus 로고    scopus 로고
    • Dynamin, a membrane-remodelling GTPase
    • 22233676 1:CAS:528:DC%2BC38XlsF2gsw%3D%3D
    • Ferguson SM, De Camilli P (2012) Dynamin, a membrane-remodelling GTPase. Nat Rev Mol Cell Biol 13:75-88
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 75-88
    • Ferguson, S.M.1    De Camilli, P.2
  • 109
    • 0026094996 scopus 로고
    • Predominant and developmentally regulated expression of dynamin in neurons
    • 1832879 1:CAS:528:DyaK3MXmsFakt70%3D 10.1016/0896-6273(91)90298-E
    • Nakata T, Iwamoto A, Noda Y, Takemura R, Yoshikura H, Hirokawa N (1991) Predominant and developmentally regulated expression of dynamin in neurons. Neuron 7:461-469
    • (1991) Neuron , vol.7 , pp. 461-469
    • Nakata, T.1    Iwamoto, A.2    Noda, Y.3    Takemura, R.4    Yoshikura, H.5    Hirokawa, N.6
  • 110
    • 71649086146 scopus 로고    scopus 로고
    • Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits
    • 20059951 1:CAS:528:DC%2BC3cXht1Cjsbs%3D 10.1016/j.devcel.2009.11.005
    • Ferguson SM, Raimondi A, Paradise S et al (2009) Coordinated actions of actin and BAR proteins upstream of dynamin at endocytic clathrin-coated pits. Dev Cell 17:811-822
    • (2009) Dev Cell , vol.17 , pp. 811-822
    • Ferguson, S.M.1    Raimondi, A.2    Paradise, S.3
  • 111
    • 0027155543 scopus 로고
    • A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis
    • 8360266 1:CAS:528:DyaK3sXmsVKgtbk%3D
    • Nakata T, Takemura R, Hirokawa N (1993) A novel member of the dynamin family of GTP-binding proteins is expressed specifically in the testis. J Cell Sci 105:1-5
    • (1993) J Cell Sci , vol.105 , pp. 1-5
    • Nakata, T.1    Takemura, R.2    Hirokawa, N.3
  • 112
    • 0029799506 scopus 로고    scopus 로고
    • Three dynamin-encoding genes are differentially expressed in developing rat brain
    • 8752097 1:CAS:528:DyaK28XltlKktrk%3D 10.1046/j.1471-4159.1996.67030927.x
    • Cook T, Mesa K, Urrutia R (1996) Three dynamin-encoding genes are differentially expressed in developing rat brain. J Neurochem 67:927-931
    • (1996) J Neurochem , vol.67 , pp. 927-931
    • Cook, T.1    Mesa, K.2    Urrutia, R.3
  • 113
    • 0037452948 scopus 로고    scopus 로고
    • Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer
    • 12646135 1:CAS:528:DC%2BD3sXit12nurg%3D 10.1016/S0960-9822(03)00136-2
    • Gray NW, Fourgeaud L, Huang B (2003) Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer. Curr Biol 13:510-515
    • (2003) Curr Biol , vol.13 , pp. 510-515
    • Gray, N.W.1    Fourgeaud, L.2    Huang, B.3
  • 114
    • 34247583278 scopus 로고    scopus 로고
    • A selective activity-dependent requirement for dynamin 1 in synaptic vesicle endocytosis
    • 17463283 1:CAS:528:DC%2BD2sXksFeksbc%3D 10.1126/science.1140621
    • Ferguson SM, Brasnjo G, Hayashi M et al (2007) A selective activity-dependent requirement for dynamin 1 in synaptic vesicle endocytosis. Science 316:570-574
    • (2007) Science , vol.316 , pp. 570-574
    • Ferguson, S.M.1    Brasnjo, G.2    Hayashi, M.3
  • 115
    • 0034938453 scopus 로고    scopus 로고
    • Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria
    • 11431699 1:CAS:528:DC%2BD3MXltFSmtLs%3D 10.1038/90116
    • Ono T, Isobe K, Nakada K, Hayashi JI (2001) Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria. Nat Genet 28:272-275
    • (2001) Nat Genet , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 116
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: Mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • 11479626 1:CAS:528:DC%2BD3MXlvVOktrc%3D 10.1038/90976
    • Nakada K, Inoue K, Ono T et al (2001) Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat Med 7:934-940
    • (2001) Nat Med , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3
  • 117
    • 33847054348 scopus 로고    scopus 로고
    • Cell and animal models of mtDNA biology: Progress and prospects
    • 16899549 1:CAS:528:DC%2BD2sXjt1Gmtb8%3D 10.1152/ajpcell.00224.2006
    • Khan SM, Smigrodzki RM, Swerdlow RH (2007) Cell and animal models of mtDNA biology: progress and prospects. Am J Physiol Cell Physiol 292:C658-C669
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Khan, S.M.1    Smigrodzki, R.M.2    Swerdlow, R.H.3
  • 118
    • 0032168434 scopus 로고    scopus 로고
    • Abnormal mitochondrial function in myocardium of dogs with chronic heart failure
    • 9769231 1:CAS:528:DyaK1cXms1Snur0%3D 10.1006/jmcc.1998.0739
    • Sharov VG, Goussev A, Lesch M, Goldstein S, Sabbah HN (1998) Abnormal mitochondrial function in myocardium of dogs with chronic heart failure. J Mol Cell Cardiol 30:1757-1762
    • (1998) J Mol Cell Cardiol , vol.30 , pp. 1757-1762
    • Sharov, V.G.1    Goussev, A.2    Lesch, M.3    Goldstein, S.4    Sabbah, H.N.5
  • 120
    • 0026099413 scopus 로고
    • Impairment of the myocardial ultrastructure and changes of the cytoskeleton in dilated cardiomyopathy
    • 1991369 1:STN:280:DyaK3M7itFKluw%3D%3D 10.1161/01.CIR.83.2.504
    • Schaper J, Froede R, Hein S et al (1991) Impairment of the myocardial ultrastructure and changes of the cytoskeleton in dilated cardiomyopathy. Circulation 83:504-514
    • (1991) Circulation , vol.83 , pp. 504-514
    • Schaper, J.1    Froede, R.2    Hein, S.3
  • 121
    • 0042339525 scopus 로고    scopus 로고
    • Myocardial hibernation in coronary artery disease
    • 11822979 10.1007/s11883-002-0039-x
    • Kalra DK, Zoghbi WA (2002) Myocardial hibernation in coronary artery disease. Curr Atheroscler Rep 4:149-155
    • (2002) Curr Atheroscler Rep , vol.4 , pp. 149-155
    • Kalra, D.K.1    Zoghbi, W.A.2
  • 122
    • 33845976357 scopus 로고    scopus 로고
    • Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology
    • 17003040 1:CAS:528:DC%2BD28Xht1Kit7zO 10.1074/jbc.M606059200
    • Duvezin-Caubet S, Jagasia R, Wagener J et al (2006) Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology. J Biol Chem 281:37972-37979
    • (2006) J Biol Chem , vol.281 , pp. 37972-37979
    • Duvezin-Caubet, S.1    Jagasia, R.2    Wagener, J.3
  • 123
    • 79958797425 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology and function by O-GlcNAcylation in neonatal cardiac myocytes
    • 21346246 1:CAS:528:DC%2BC3MXot1Grs7c%3D 10.1152/ajpregu.00437.2010
    • Makino A, Suarez J, Gawlowski T et al (2011) Regulation of mitochondrial morphology and function by O-GlcNAcylation in neonatal cardiac myocytes. Am J Physiol Regul Integr Comp Physiol 300:R1296-R1302
    • (2011) Am J Physiol Regul Integr Comp Physiol , vol.300
    • Makino, A.1    Suarez, J.2    Gawlowski, T.3
  • 124
    • 79952265711 scopus 로고    scopus 로고
    • Mitofusin-2 maintains mitochondrial structure and contributes to stress-induced permeability transition in cardiac myocytes
    • 21245373 1:CAS:528:DC%2BC3MXhtVWks7fI 10.1128/MCB.00911-10
    • Papanicolaou KN, Khairallah RJ, Ngoh GA et al (2011) Mitofusin-2 maintains mitochondrial structure and contributes to stress-induced permeability transition in cardiac myocytes. Mol Cell Biol 31:1309-1328
    • (2011) Mol Cell Biol , vol.31 , pp. 1309-1328
    • Papanicolaou, K.N.1    Khairallah, R.J.2    Ngoh, G.A.3
  • 125
    • 84856109625 scopus 로고    scopus 로고
    • Mitochondrial fusion is essential for organelle function and cardiac homeostasis
    • 22052916 1:CAS:528:DC%2BC3MXhsF2jsrrN 10.1161/CIRCRESAHA.111.258723
    • Chen Y, Liu Y, Dorn GW II et al (2011) Mitochondrial fusion is essential for organelle function and cardiac homeostasis. Circ Res 109:1327-1331
    • (2011) Circ Res , vol.109 , pp. 1327-1331
    • Chen, Y.1    Liu, Y.2    Dorn, I.I.G.W.3
  • 126
    • 34547601410 scopus 로고    scopus 로고
    • Mitochondrial fusion protects against neurodegeneration in the cerebellum
    • 17693261 1:CAS:528:DC%2BD2sXptlynurY%3D 10.1016/j.cell.2007.06.026
    • Chen H, McCaffery JM, Chan DC (2007) Mitochondrial fusion protects against neurodegeneration in the cerebellum. Cell 130:548-562
    • (2007) Cell , vol.130 , pp. 548-562
    • Chen, H.1    McCaffery, J.M.2    Chan, D.C.3
  • 127
    • 77951737783 scopus 로고    scopus 로고
    • Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations
    • 20403324 1:CAS:528:DC%2BC3cXmtVWnsLg%3D 10.1016/j.cell.2010.02.026
    • Chen H, Vermulst M, Wang YE et al (2010) Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations. Cell 141:280-289
    • (2010) Cell , vol.141 , pp. 280-289
    • Chen, H.1    Vermulst, M.2    Wang, Y.E.3
  • 128
    • 0028116218 scopus 로고
    • Idiopathic dilated cardiomyopathy
    • 7969328 1:STN:280:DyaK2M%2FlvFartw%3D%3D 10.1056/NEJM199412083312307
    • Dec GW, Fuster V (1994) Idiopathic dilated cardiomyopathy. N Engl J Med 331:1564-1575
    • (1994) N Engl J Med , vol.331 , pp. 1564-1575
    • Dec, G.W.1    Fuster, V.2
  • 129
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • 11239412 1:CAS:528:DC%2BD3MXis1Kks70%3D 10.1016/S0092-8674(01)00242-2
    • Seidman JG, Seidman C (2001) The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell 104:557-567
    • (2001) Cell , vol.104 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 130
    • 34247124771 scopus 로고    scopus 로고
    • Genetics of dilated cardiomyopathy
    • 17453673 1:CAS:528:DC%2BD2sXmtVGrtLk%3D 10.1080/07853890601145821
    • Karkkainen S, Peuhkurinen K (2007) Genetics of dilated cardiomyopathy. Ann Med 39:91-107
    • (2007) Ann Med , vol.39 , pp. 91-107
    • Karkkainen, S.1    Peuhkurinen, K.2
  • 131
    • 0019515381 scopus 로고
    • Electron microscopic investigation of endomyocardial biopsy samples in hypertrophy and cardiomyopathy. A semiquantitative study in 48 patients
    • 6452971 1:STN:280:DyaL3M7os1Ohsg%3D%3D 10.1161/01.CIR.63.6.1289
    • Baandrup U, Florio RA, Roters F, Olsen EG (1981) Electron microscopic investigation of endomyocardial biopsy samples in hypertrophy and cardiomyopathy. A semiquantitative study in 48 patients. Circulation 63:1289-1298
    • (1981) Circulation , vol.63 , pp. 1289-1298
    • Baandrup, U.1    Florio, R.A.2    Roters, F.3    Olsen, E.G.4
  • 132
    • 0014458555 scopus 로고
    • Formation of gigantic mitochondria in hypoxic isolated perfused rat hearts
    • 5809311 1:STN:280:DyaF1M3osFGmtQ%3D%3D 10.1007/BF01897616
    • Sun CN, Dhalla NS, Olson RE (1969) Formation of gigantic mitochondria in hypoxic isolated perfused rat hearts. Experientia 25:763-764
    • (1969) Experientia , vol.25 , pp. 763-764
    • Sun, C.N.1    Dhalla, N.S.2    Olson, R.E.3
  • 133
    • 77954169092 scopus 로고    scopus 로고
    • A mutation in the mitochondrial fission gene Dnm1 l leads to cardiomyopathy
    • 20585624 10.1371/journal.pgen.1001000 1:CAS:528:DC%2BC3cXotlGqtLk%3D
    • Ashrafian H, Docherty L, Leo V et al (2010) A mutation in the mitochondrial fission gene Dnm1 l leads to cardiomyopathy. PLoS Genet 6:e1001000
    • (2010) PLoS Genet , vol.6 , pp. 1001000
    • Ashrafian, H.1    Docherty, L.2    Leo, V.3
  • 134
    • 33846513580 scopus 로고    scopus 로고
    • The dynamin middle domain is critical for tetramerization and higher-order self-assembly
    • 17170701 1:CAS:528:DC%2BD2sXotFKhtA%3D%3D 10.1038/sj.emboj.7601491
    • Ramachandran R, Surka M, Chappie JS et al (2007) The dynamin middle domain is critical for tetramerization and higher-order self-assembly. EMBO J 26:559-566
    • (2007) EMBO J , vol.26 , pp. 559-566
    • Ramachandran, R.1    Surka, M.2    Chappie, J.S.3
  • 135
    • 35148862219 scopus 로고    scopus 로고
    • A corkscrew model for dynamin constriction
    • 17937909 1:CAS:528:DC%2BD2sXhtFKhsL%2FE 10.1016/j.str.2007.08.012
    • Mears JA, Ray P, Hinshaw JE (2007) A corkscrew model for dynamin constriction. Structure 15:1190-1202
    • (2007) Structure , vol.15 , pp. 1190-1202
    • Mears, J.A.1    Ray, P.2    Hinshaw, J.E.3
  • 137
    • 70449724857 scopus 로고    scopus 로고
    • Mitochondrial OPA1, apoptosis, and heart failure
    • 19493956 1:CAS:528:DC%2BD1MXhtFarsbrF 10.1093/cvr/cvp181
    • Chen L, Gong Q, Stice JP, Knowlton AA (2009) Mitochondrial OPA1, apoptosis, and heart failure. Cardiovasc Res 84:91-99
    • (2009) Cardiovasc Res , vol.84 , pp. 91-99
    • Chen, L.1    Gong, Q.2    Stice, J.P.3    Knowlton, A.A.4
  • 138
    • 70349650451 scopus 로고    scopus 로고
    • Mitochondrial networking protects beta-cells from nutrient-induced apoptosis
    • 19581419 1:CAS:528:DC%2BD1MXht1yku7bE 10.2337/db07-1781
    • Molina AJ, Wikstrom JD, Stiles L et al (2009) Mitochondrial networking protects beta-cells from nutrient-induced apoptosis. Diabetes 58:2303-2315
    • (2009) Diabetes , vol.58 , pp. 2303-2315
    • Molina, A.J.1    Wikstrom, J.D.2    Stiles, L.3
  • 139
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
    • 15356267 1:CAS:528:DC%2BD2cXpslKns7c%3D 10.1091/mbc.E04-04-0294
    • Lee YJ, Jeong SY, Karbowski M, Smith CL, Youle RJ (2004) Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis. Mol Biol Cell 15:5001-5011
    • (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
  • 140
    • 33845885125 scopus 로고    scopus 로고
    • Mitochondrial fragmentation in apoptosis
    • 17116393 1:CAS:528:DC%2BD2sXis1aksQ%3D%3D 10.1016/j.tcb.2006.11.001
    • Arnoult D (2007) Mitochondrial fragmentation in apoptosis. Trends Cell Biol 17:6-12
    • (2007) Trends Cell Biol , vol.17 , pp. 6-12
    • Arnoult, D.1
  • 141
    • 79960230433 scopus 로고    scopus 로고
    • Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics
    • 21763611 1:CAS:528:DC%2BC3MXptVSqsrw%3D 10.1016/j.devcel.2011.06.017
    • Martinou JC, Youle RJ (2011) Mitochondria in apoptosis: Bcl-2 family members and mitochondrial dynamics. Dev Cell 21:92-101
    • (2011) Dev Cell , vol.21 , pp. 92-101
    • Martinou, J.C.1    Youle, R.J.2
  • 142
    • 38849095253 scopus 로고    scopus 로고
    • Changes in mitochondrial dynamics during ceramide-induced cardiomyocyte early apoptosis
    • 18006463 1:CAS:528:DC%2BD1cXis12ku7Y%3D 10.1093/cvr/cvm029
    • Parra V, Eisner V, Chiong M et al (2008) Changes in mitochondrial dynamics during ceramide-induced cardiomyocyte early apoptosis. Cardiovasc Res 77:387-397
    • (2008) Cardiovasc Res , vol.77 , pp. 387-397
    • Parra, V.1    Eisner, V.2    Chiong, M.3
  • 143
    • 34248182897 scopus 로고    scopus 로고
    • Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death
    • 17470634 1:CAS:528:DC%2BD2sXltF2gtrc%3D 10.1083/jcb.200610042
    • Wasiak S, Zunino R, McBride HM (2007) Bax/Bak promote sumoylation of DRP1 and its stable association with mitochondria during apoptotic cell death. J Cell Biol 177:439-450
    • (2007) J Cell Biol , vol.177 , pp. 439-450
    • Wasiak, S.1    Zunino, R.2    McBride, H.M.3
  • 144
    • 78651468702 scopus 로고    scopus 로고
    • The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes
    • 21255726 1:CAS:528:DC%2BC3MXhtVWqtbg%3D 10.1016/j.molcel.2010.11.030
    • Hoppins S, Edlich F, Cleland MM et al (2011) The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes. Mol Cell 41:150-160
    • (2011) Mol Cell , vol.41 , pp. 150-160
    • Hoppins, S.1    Edlich, F.2    Cleland, M.M.3
  • 145
    • 36348989007 scopus 로고    scopus 로고
    • Mitofusin 2 triggers vascular smooth muscle cell apoptosis via mitochondrial death pathway
    • 17901359 1:CAS:528:DC%2BD2sXhtlahurjM 10.1161/CIRCRESAHA.107.157644
    • Guo X, Chen KH, Guo Y, Liao H, Tang J, Xiao RP (2007) Mitofusin 2 triggers vascular smooth muscle cell apoptosis via mitochondrial death pathway. Circ Res 101:1113-1122
    • (2007) Circ Res , vol.101 , pp. 1113-1122
    • Guo, X.1    Chen, K.H.2    Guo, Y.3    Liao, H.4    Tang, J.5    Xiao, R.P.6
  • 146
    • 34548170490 scopus 로고    scopus 로고
    • Mitofusin-2 is a major determinant of oxidative stress-mediated heart muscle cell apoptosis
    • 17562700 1:CAS:528:DC%2BD2sXosVyrsb0%3D 10.1074/jbc.M702657200
    • Shen T, Zheng M, Cao C et al (2007) Mitofusin-2 is a major determinant of oxidative stress-mediated heart muscle cell apoptosis. J Biol Chem 282:23354-23361
    • (2007) J Biol Chem , vol.282 , pp. 23354-23361
    • Shen, T.1    Zheng, M.2    Cao, C.3
  • 147
    • 57349100367 scopus 로고    scopus 로고
    • Mitofusin 2 tethers endoplasmic reticulum to mitochondria
    • 19052620 10.1038/nature07534 1:CAS:528:DC%2BD1cXhsVGlur7J
    • de Brito OM, Scorrano L (2008) Mitofusin 2 tethers endoplasmic reticulum to mitochondria. Nature 456:605-610
    • (2008) Nature , vol.456 , pp. 605-610
    • De Brito, O.M.1    Scorrano, L.2
  • 148
    • 21644455319 scopus 로고    scopus 로고
    • Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization
    • 15878861 1:CAS:528:DC%2BD2MXlsFyqtrg%3D 10.1074/jbc.M501599200
    • Neuspiel M, Zunino R, Gangaraju S, Rippstein P, McBride H (2005) Activated mitofusin 2 signals mitochondrial fusion, interferes with Bax activation, and reduces susceptibility to radical induced depolarization. J Biol Chem 280:25060-25070
    • (2005) J Biol Chem , vol.280 , pp. 25060-25070
    • Neuspiel, M.1    Zunino, R.2    Gangaraju, S.3    Rippstein, P.4    McBride, H.5
  • 149
    • 0038783254 scopus 로고    scopus 로고
    • Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells
    • 12759376 1:CAS:528:DC%2BD3sXlsFamtbg%3D 10.1242/jcs.00479
    • Santel A, Frank S, Gaume B, Herrler M, Youle RJ, Fuller MT (2003) Mitofusin-1 protein is a generally expressed mediator of mitochondrial fusion in mammalian cells. J Cell Sci 116:2763-2774
    • (2003) J Cell Sci , vol.116 , pp. 2763-2774
    • Santel, A.1    Frank, S.2    Gaume, B.3    Herrler, M.4    Youle, R.J.5    Fuller, M.T.6
  • 150
    • 68949156263 scopus 로고    scopus 로고
    • Mitochondria in cardiomyocyte Ca2+ signaling
    • 19703657 1:CAS:528:DC%2BD1MXhtVentbjL 10.1016/j.biocel.2009.03.011
    • Lukyanenko V, Chikando A, Lederer WJ (2009) Mitochondria in cardiomyocyte Ca2+ signaling. Int J Biochem Cell Biol 41:1957-1971
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1957-1971
    • Lukyanenko, V.1    Chikando, A.2    Lederer, W.J.3
  • 151
    • 79952265711 scopus 로고    scopus 로고
    • Mitofusin-2 maintains mitochondrial structure and contributes to stress-induced permeability transition in cardiac myocytes
    • 21245373 1:CAS:528:DC%2BC3MXhtVWks7fI 10.1128/MCB.00911-10
    • Papanicolaou KN, Khairallah RJ, Ngoh GA et al (2011) Mitofusin-2 maintains mitochondrial structure and contributes to stress-induced permeability transition in cardiac myocytes. Mol Cell Biol 31:1309-1328
    • (2011) Mol Cell Biol , vol.31 , pp. 1309-1328
    • Papanicolaou, K.N.1    Khairallah, R.J.2    Ngoh, G.A.3
  • 152
    • 0015371731 scopus 로고
    • Possible division of cardiac mitochondria
    • 5039085 1:STN:280:DyaE383hvFSqtA%3D%3D 10.1002/ar.1091730306
    • Tandler B, Hoppel CL (1972) Possible division of cardiac mitochondria. Anat Rec 173:309-323
    • (1972) Anat Rec , vol.173 , pp. 309-323
    • Tandler, B.1    Hoppel, C.L.2
  • 153
    • 77953810265 scopus 로고    scopus 로고
    • Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes
    • 20347716 1:CAS:528:DC%2BC3cXnvV2qtr8%3D 10.1016/j.bbabio.2010.03.018
    • Hom J, Yu T, Yoon Y, Porter G, Sheu SS (2010) Regulation of mitochondrial fission by intracellular Ca2+ in rat ventricular myocytes. Biochim Biophys Acta 1797:913-921
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 913-921
    • Hom, J.1    Yu, T.2    Yoon, Y.3    Porter, G.4    Sheu, S.S.5
  • 154
    • 33748414614 scopus 로고    scopus 로고
    • Autophagy as a protective response to Bnip3-mediated apoptotic signaling in the heart
    • 16874059 1:CAS:528:DC%2BD28XhtVGisbvM
    • Hamacher-Brady A, Brady NR, Gottlieb RA, Gustafsson AB (2006) Autophagy as a protective response to Bnip3-mediated apoptotic signaling in the heart. Autophagy 2:307-309
    • (2006) Autophagy , vol.2 , pp. 307-309
    • Hamacher-Brady, A.1    Brady, N.R.2    Gottlieb, R.A.3    Gustafsson, A.B.4
  • 155
    • 34147168105 scopus 로고    scopus 로고
    • Distinct roles of autophagy in the heart during ischemia and reperfusion: Roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy
    • 17332429 1:CAS:528:DC%2BD2sXjtlWmsbo%3D 10.1161/01.RES.0000261924.76669. 36
    • Matsui Y, Takagi H, Qu X et al (2007) Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy. Circ Res 100:914-922
    • (2007) Circ Res , vol.100 , pp. 914-922
    • Matsui, Y.1    Takagi, H.2    Qu, X.3
  • 156
    • 79957940535 scopus 로고    scopus 로고
    • Mitochondrial turnover in the heart
    • 21147177 1:CAS:528:DC%2BC3MXntV2lsL0%3D 10.1016/j.bbamcr.2010.11.017
    • Gottlieb RA, Gustafsson AB (2011) Mitochondrial turnover in the heart. Biochim Biophys Acta 1813:1295-1301
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1295-1301
    • Gottlieb, R.A.1    Gustafsson, A.B.2
  • 157
    • 80052966447 scopus 로고    scopus 로고
    • Mitochondrial dynamics: A potential new therapeutic target for heart failure
    • 21820793 10.1016/j.recesp.2011.05.018
    • Kuzmicic J, Del Campo A, Lopez-Crisosto C et al (2011) Mitochondrial dynamics: a potential new therapeutic target for heart failure. Rev Esp Cardiol 64:916-923
    • (2011) Rev Esp Cardiol , vol.64 , pp. 916-923
    • Kuzmicic, J.1    Del Campo, A.2    Lopez-Crisosto, C.3
  • 158
    • 79951802995 scopus 로고    scopus 로고
    • Integrative systems biology and networks in autophagy
    • 20842363 10.1007/s00281-010-0225-9
    • Ng AC (2010) Integrative systems biology and networks in autophagy. Semin Immunopathol 32:355-361
    • (2010) Semin Immunopathol , vol.32 , pp. 355-361
    • Ng, A.C.1
  • 159
    • 77955437274 scopus 로고    scopus 로고
    • How could Parkin-mediated ubiquitination of mitofusin promote mitophagy?
    • 20484985 10.4161/auto.6.5.12242
    • Ziviani E, Whitworth AJ (2010) How could Parkin-mediated ubiquitination of mitofusin promote mitophagy? Autophagy 6:660-662
    • (2010) Autophagy , vol.6 , pp. 660-662
    • Ziviani, E.1    Whitworth, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.