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Volumn 41, Issue 3, 2016, Pages 261-273

Mitochondrial Cristae: Where Beauty Meets Functionality

Author keywords

Cristae; Mitochondrial shaping proteins; OXPHOS complexes and supercomplexes

Indexed keywords

CELL MEMBRANE PROTEIN; CL PROTEIN; MICOS PROTEIN; MITOCHONDRIAL PROTEIN; OPA1 PROTEIN; PHB SLP2 COMPLEX PROTEIN; PROTEIN MCL 1; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; UNCLASSIFIED DRUG;

EID: 84959521117     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2016.01.001     Document Type: Review
Times cited : (573)

References (110)
  • 1
    • 38549110110 scopus 로고    scopus 로고
    • Fission and selective fusion govern mitochondrial segregation and elimination by autophagy
    • Twig G., 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
  • 2
    • 79955623510 scopus 로고    scopus 로고
    • During autophagy mitochondria elongate, are spared from degradation and sustain cell viability
    • Gomes L.C., et al. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat. Cell Biol. 2011, 13:589-598.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 589-598
    • Gomes, L.C.1
  • 3
    • 79959987510 scopus 로고    scopus 로고
    • Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation
    • Rambold A.S., et al. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:10190-10195.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10190-10195
    • Rambold, A.S.1
  • 4
    • 67049089786 scopus 로고    scopus 로고
    • SLP-2 is required for stress-induced mitochondrial hyperfusion
    • Tondera D., et al. SLP-2 is required for stress-induced mitochondrial hyperfusion. EMBO. J. 2009, 28:1589-1600.
    • (2009) EMBO. J. , vol.28 , pp. 1589-1600
    • Tondera, D.1
  • 5
    • 53049099984 scopus 로고    scopus 로고
    • Short- and long-term alterations of mitochondrial morphology, dynamics and mtDNA after transient oxidative stress
    • Jendrach M., et al. Short- and long-term alterations of mitochondrial morphology, dynamics and mtDNA after transient oxidative stress. Mitochondrion 2008, 8:293-304.
    • (2008) Mitochondrion , vol.8 , pp. 293-304
    • Jendrach, M.1
  • 6
    • 70349650451 scopus 로고    scopus 로고
    • Mitochondrial networking protects beta-cells from nutrient-induced apoptosis
    • Molina A.J., et al. Mitochondrial networking protects beta-cells from nutrient-induced apoptosis. Diabetes 2009, 58:2303-2315.
    • (2009) Diabetes , vol.58 , pp. 2303-2315
    • Molina, A.J.1
  • 7
    • 33645840444 scopus 로고    scopus 로고
    • Nitric oxide impairs mitochondrial movement in cortical neurons during hypoxia
    • Zanelli S.A., et al. Nitric oxide impairs mitochondrial movement in cortical neurons during hypoxia. J. Neurochem. 2006, 97:724-736.
    • (2006) J. Neurochem. , vol.97 , pp. 724-736
    • Zanelli, S.A.1
  • 8
    • 0013936320 scopus 로고
    • Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria
    • Hackenbrock C.R. Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria. J. Cell Biol. 1966, 30:269-297.
    • (1966) J. Cell Biol. , vol.30 , pp. 269-297
    • Hackenbrock, C.R.1
  • 9
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • Scorrano L., et al. A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev. Cell 2002, 2:55-67.
    • (2002) Dev. Cell , vol.2 , pp. 55-67
    • Scorrano, L.1
  • 10
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza C., et al. OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 2006, 126:177-189.
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1
  • 11
    • 84884909413 scopus 로고    scopus 로고
    • Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency
    • Cogliati S., et al. Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency. Cell 2013, 155:160-171.
    • (2013) Cell , vol.155 , pp. 160-171
    • Cogliati, S.1
  • 12
    • 4644266043 scopus 로고    scopus 로고
    • Activation of endogenous Cdc42 visualized in living cells
    • Nalbant P., et al. Activation of endogenous Cdc42 visualized in living cells. Science 2004, 305:1615-1619.
    • (2004) Science , vol.305 , pp. 1615-1619
    • Nalbant, P.1
  • 13
    • 41949138471 scopus 로고    scopus 로고
    • Controlling the rates of biochemical reactions and signaling networks by shape and volume changes
    • Lizana L., et al. Controlling the rates of biochemical reactions and signaling networks by shape and volume changes. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:4099-4104.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4099-4104
    • Lizana, L.1
  • 14
    • 0035990298 scopus 로고    scopus 로고
    • Fasting induces cyanide-resistant respiration and oxidative stress in the amoeba Chaos carolinensis: implications for the cubic structural transition in mitochondrial membranes
    • Deng Y., et al. Fasting induces cyanide-resistant respiration and oxidative stress in the amoeba Chaos carolinensis: implications for the cubic structural transition in mitochondrial membranes. Protoplasma 2002, 219:160-167.
    • (2002) Protoplasma , vol.219 , pp. 160-167
    • Deng, Y.1
  • 15
    • 0034709621 scopus 로고    scopus 로고
    • Lipid peroxidation in small and large phospholipid unilamellar vesicles induced by water-soluble free radical sources
    • Li Q.T., et al. Lipid peroxidation in small and large phospholipid unilamellar vesicles induced by water-soluble free radical sources. Biochem. Biophys. Res. Commun. 2000, 273:72-76.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 72-76
    • Li, Q.T.1
  • 16
    • 84923357261 scopus 로고    scopus 로고
    • Trans-mitochondrial coordination of cristae at regulated membrane junctions
    • Picard M., et al. Trans-mitochondrial coordination of cristae at regulated membrane junctions. Nat. Commun. 2015, 6:6259.
    • (2015) Nat. Commun. , vol.6 , pp. 6259
    • Picard, M.1
  • 17
    • 0037494885 scopus 로고    scopus 로고
    • The cristal membrane of mitochondria is the principal site of oxidative phosphorylation
    • Gilkerson R.W., et al. The cristal membrane of mitochondria is the principal site of oxidative phosphorylation. FEBS Lett. 2003, 546:355-358.
    • (2003) FEBS Lett. , vol.546 , pp. 355-358
    • Gilkerson, R.W.1
  • 18
    • 84930926530 scopus 로고    scopus 로고
    • Ancient homology of the mitochondrial contact site and cristae organizing system points to an endosymbiotic origin of mitochondrial cristae
    • Munoz-Gomez S.A., et al. Ancient homology of the mitochondrial contact site and cristae organizing system points to an endosymbiotic origin of mitochondrial cristae. Curr. Biol. 2015, 25:1489-1495.
    • (2015) Curr. Biol. , vol.25 , pp. 1489-1495
    • Munoz-Gomez, S.A.1
  • 19
    • 41949123425 scopus 로고    scopus 로고
    • Dimer ribbons of ATP synthase shape the inner mitochondrial membrane
    • Strauss M., et al. Dimer ribbons of ATP synthase shape the inner mitochondrial membrane. EMBO J. 2008, 27:1154-1160.
    • (2008) EMBO J. , vol.27 , pp. 1154-1160
    • Strauss, M.1
  • 20
    • 80052177663 scopus 로고    scopus 로고
    • Macromolecular organization of ATP synthase and complex I in whole mitochondria
    • Davies K.M., et al. Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:14121-14126.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 14121-14126
    • Davies, K.M.1
  • 21
    • 26844548023 scopus 로고    scopus 로고
    • Structure of dimeric ATP synthase from mitochondria: an angular association of monomers induces the strong curvature of the inner membrane
    • Dudkina N.V., et al. Structure of dimeric ATP synthase from mitochondria: an angular association of monomers induces the strong curvature of the inner membrane. FEBS. Lett. 2005, 579:5769-5772.
    • (2005) FEBS. Lett. , vol.579 , pp. 5769-5772
    • Dudkina, N.V.1
  • 22
    • 84875601992 scopus 로고    scopus 로고
    • Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution
    • Wilkens V., et al. Restricted diffusion of OXPHOS complexes in dynamic mitochondria delays their exchange between cristae and engenders a transitory mosaic distribution. J. Cell Sci. 2013, 126:103-116.
    • (2013) J. Cell Sci. , vol.126 , pp. 103-116
    • Wilkens, V.1
  • 23
    • 84920407372 scopus 로고    scopus 로고
    • Lateral pH gradient between OXPHOS complex IV and F(0)F(1) ATP-synthase in folded mitochondrial membranes
    • Rieger B., et al. Lateral pH gradient between OXPHOS complex IV and F(0)F(1) ATP-synthase in folded mitochondrial membranes. Nat. Commun. 2014, 5:3103.
    • (2014) Nat. Commun. , vol.5 , pp. 3103
    • Rieger, B.1
  • 24
    • 58149308564 scopus 로고    scopus 로고
    • Membrane deformation under local pH gradient: mimicking mitochondrial cristae dynamics
    • Khalifat N., et al. Membrane deformation under local pH gradient: mimicking mitochondrial cristae dynamics. Biophys. J. 2008, 95:4924-4933.
    • (2008) Biophys. J. , vol.95 , pp. 4924-4933
    • Khalifat, N.1
  • 25
    • 84925949899 scopus 로고    scopus 로고
    • Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals
    • Jiko C., et al. Bovine F1Fo ATP synthase monomers bend the lipid bilayer in 2D membrane crystals. eLife 2015, 4:e06119.
    • (2015) eLife , vol.4 , pp. e06119
    • Jiko, C.1
  • 26
    • 84923685347 scopus 로고    scopus 로고
    • Mitochondria: from cell death executioners to regulators of cell differentiation
    • Kasahara A., Scorrano L. Mitochondria: from cell death executioners to regulators of cell differentiation. Trends Cell Biol. 2014, 24:761-770.
    • (2014) Trends Cell Biol. , vol.24 , pp. 761-770
    • Kasahara, A.1    Scorrano, L.2
  • 27
    • 84897518469 scopus 로고    scopus 로고
    • Uniform nomenclature for the mitochondrial contact site and cristae organizing system
    • Pfanner N., et al. Uniform nomenclature for the mitochondrial contact site and cristae organizing system. J. Cell Biol. 2014, 204:1083-1086.
    • (2014) J. Cell Biol. , vol.204 , pp. 1083-1086
    • Pfanner, N.1
  • 28
    • 84878437545 scopus 로고    scopus 로고
    • STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria
    • Jans D.C., et al. STED super-resolution microscopy reveals an array of MINOS clusters along human mitochondria. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:8936-8941.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 8936-8941
    • Jans, D.C.1
  • 29
    • 84929154199 scopus 로고    scopus 로고
    • MICOS coordinates with respiratory complexes and lipids to establish mitochondrial inner membrane architecture
    • Friedman J.R., et al. MICOS coordinates with respiratory complexes and lipids to establish mitochondrial inner membrane architecture. eLife 2015, 4:07739.
    • (2015) eLife , vol.4 , pp. 07739
    • Friedman, J.R.1
  • 30
    • 78951493639 scopus 로고    scopus 로고
    • ChChd3, an inner mitochondrial membrane protein, is essential for maintaining cristae integrity and mitochondrial function
    • Darshi M., et al. ChChd3, an inner mitochondrial membrane protein, is essential for maintaining cristae integrity and mitochondrial function. J. Biol. Chem. 2010, 288:2918-2932.
    • (2010) J. Biol. Chem. , vol.288 , pp. 2918-2932
    • Darshi, M.1
  • 31
    • 84857869559 scopus 로고    scopus 로고
    • Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes
    • Ott C., et al. Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes. Mol. Cell. Biol. 2012, 32:1173-1188.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1173-1188
    • Ott, C.1
  • 32
    • 84893650998 scopus 로고    scopus 로고
    • C1orf163/RESA1 is a novel mitochondrial intermembrane space protein connected to respiratory chain assembly
    • Kozjak-Pavlovic V., et al. C1orf163/RESA1 is a novel mitochondrial intermembrane space protein connected to respiratory chain assembly. J. Mol. Biol. 2014, 426:908-920.
    • (2014) J. Mol. Biol. , vol.426 , pp. 908-920
    • Kozjak-Pavlovic, V.1
  • 33
    • 84861627801 scopus 로고    scopus 로고
    • Anti-apoptotic MCL-1 localizes to the mitochondrial matrix and couples mitochondrial fusion to respiration
    • Perciavalle R.M., et al. Anti-apoptotic MCL-1 localizes to the mitochondrial matrix and couples mitochondrial fusion to respiration. Nat. Cell Biol. 2012, 14:575-583.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 575-583
    • Perciavalle, R.M.1
  • 34
    • 8644270474 scopus 로고    scopus 로고
    • OPA1 requires mitofusin 1 to promote mitochondrial fusion
    • Cipolat S., et al. OPA1 requires mitofusin 1 to promote mitochondrial fusion. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:15927-15932.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15927-15932
    • Cipolat, S.1
  • 35
    • 49349112331 scopus 로고    scopus 로고
    • OPA1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization
    • Yamaguchi R., et al. OPA1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization. Mol. Cell 2008, 31:557-569.
    • (2008) Mol. Cell , vol.31 , pp. 557-569
    • Yamaguchi, R.1
  • 36
    • 78650284389 scopus 로고    scopus 로고
    • Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli
    • Costa V., et al. Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli. EMBO Mol. Med. 2010, 2:490-503.
    • (2010) EMBO Mol. Med. , vol.2 , pp. 490-503
    • Costa, V.1
  • 37
    • 77953123212 scopus 로고    scopus 로고
    • The BH3-only Bnip3 binds to the dynamin OPA1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms
    • Landes T., et al. The BH3-only Bnip3 binds to the dynamin OPA1 to promote mitochondrial fragmentation and apoptosis by distinct mechanisms. EMBO Rep. 2010, 11:459-465.
    • (2010) EMBO Rep. , vol.11 , pp. 459-465
    • Landes, T.1
  • 38
    • 9144238312 scopus 로고    scopus 로고
    • Deficit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy
    • Lodi R., et al. Deficit of in vivo mitochondrial ATP production in OPA1-related dominant optic atrophy. Ann. Neurol. 2004, 56:719-723.
    • (2004) Ann. Neurol. , vol.56 , pp. 719-723
    • Lodi, R.1
  • 39
    • 38849190029 scopus 로고    scopus 로고
    • OPA1 mutations associated with dominant optic atrophy impair oxidative phosphorylation and mitochondrial fusion
    • Zanna C., 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
  • 40
    • 84864193527 scopus 로고    scopus 로고
    • Defective mitochondrial fusion, altered respiratory function, and distorted cristae structure in skin fibroblasts with heterozygous OPA1 mutations
    • Agier V., et al. Defective mitochondrial fusion, altered respiratory function, and distorted cristae structure in skin fibroblasts with heterozygous OPA1 mutations. Biochim. Biophys. Acta 2012, 1822:1570-1580.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1570-1580
    • Agier, V.1
  • 41
    • 54449084658 scopus 로고    scopus 로고
    • A novel deletion in the GTPase domain of OPA1 causes defects in mitochondrial morphology and distribution, but not in function
    • Spinazzi M., et al. A novel deletion in the GTPase domain of OPA1 causes defects in mitochondrial morphology and distribution, but not in function. Hum. Mol. Genet. 2008, 17:3291-3302.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3291-3302
    • Spinazzi, M.1
  • 42
    • 52249096823 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy
    • Mayorov V.I., et al. Mitochondrial oxidative phosphorylation in autosomal dominant optic atrophy. BMC. Biochem. 2008, 9:22.
    • (2008) BMC. Biochem. , vol.9 , pp. 22
    • Mayorov, V.I.1
  • 43
    • 84930607266 scopus 로고    scopus 로고
    • The OPA1-dependent mitochondrial cristae remodeling pathway controls atrophic, apoptotic, and ischemic tissue damage
    • Varanita T., et al. The OPA1-dependent mitochondrial cristae remodeling pathway controls atrophic, apoptotic, and ischemic tissue damage. Cell Metab. 2015, 21:834-844.
    • (2015) Cell Metab. , vol.21 , pp. 834-844
    • Varanita, T.1
  • 44
    • 84930588143 scopus 로고    scopus 로고
    • OPA1 overexpression ameliorates the phenotype of two mitochondrial disease mouse models
    • Civiletto G., et al. OPA1 overexpression ameliorates the phenotype of two mitochondrial disease mouse models. Cell Metab. 2015, 21:845-854.
    • (2015) Cell Metab. , vol.21 , pp. 845-854
    • Civiletto, G.1
  • 45
    • 84897382106 scopus 로고    scopus 로고
    • Acidosis overrides oxygen deprivation to maintain mitochondrial function and cell survival
    • Khacho M., et al. Acidosis overrides oxygen deprivation to maintain mitochondrial function and cell survival. Nat. Commun. 2014, 5:3550.
    • (2014) Nat. Commun. , vol.5 , pp. 3550
    • Khacho, M.1
  • 46
    • 84894475127 scopus 로고    scopus 로고
    • ROMO1 is an essential redox-dependent regulator of mitochondrial dynamics
    • Norton M., et al. ROMO1 is an essential redox-dependent regulator of mitochondrial dynamics. Sci. Signal. 2014, 7:ra10.
    • (2014) Sci. Signal. , vol.7 , pp. ra10
    • Norton, M.1
  • 47
    • 84896689137 scopus 로고    scopus 로고
    • A new non-canonical pathway of Galpha(q) protein regulating mitochondrial dynamics and bioenergetics
    • Beninca C., et al. A new non-canonical pathway of Galpha(q) protein regulating mitochondrial dynamics and bioenergetics. Cell. Signal. 2014, 26:1135-1146.
    • (2014) Cell. Signal. , vol.26 , pp. 1135-1146
    • Beninca, C.1
  • 48
    • 80054831882 scopus 로고    scopus 로고
    • Structural biology. Up close with membrane lipid-protein complexes
    • Whitelegge J. Structural biology. Up close with membrane lipid-protein complexes. Science 2011, 334:320-321.
    • (2011) Science , vol.334 , pp. 320-321
    • Whitelegge, J.1
  • 49
    • 84876514398 scopus 로고    scopus 로고
    • Cellular microcompartments constitute general suborganellar functional units in cells
    • Holthuis J.C., Ungermann C. Cellular microcompartments constitute general suborganellar functional units in cells. Biol. Chem. 2013, 394:151-161.
    • (2013) Biol. Chem. , vol.394 , pp. 151-161
    • Holthuis, J.C.1    Ungermann, C.2
  • 50
    • 0033046823 scopus 로고    scopus 로고
    • X-linked cardioskeletal myopathy and neutropenia (Barth syndrome) (MIM 302060)
    • Barth P.G., et al. X-linked cardioskeletal myopathy and neutropenia (Barth syndrome) (MIM 302060). J. Inherit. Metab. Dis. 1999, 22:555-567.
    • (1999) J. Inherit. Metab. Dis. , vol.22 , pp. 555-567
    • Barth, P.G.1
  • 51
    • 84867579830 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and cardiolipin differentially affect the stability of mitochondrial respiratory chain supercomplexes
    • Bottinger L., et al. Phosphatidylethanolamine and cardiolipin differentially affect the stability of mitochondrial respiratory chain supercomplexes. J. Mol. Biol. 2012, 423:677-686.
    • (2012) J. Mol. Biol. , vol.423 , pp. 677-686
    • Bottinger, L.1
  • 52
    • 79959727395 scopus 로고    scopus 로고
    • Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria
    • Acehan D., et al. Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria. Biophys. J. 2011, 100:2184-2192.
    • (2011) Biophys. J. , vol.100 , pp. 2184-2192
    • Acehan, D.1
  • 53
    • 84879493450 scopus 로고    scopus 로고
    • Cardiolipin deficiency affects respiratory chain function and organization in an induced pluripotent stem cell model of Barth syndrome
    • Dudek J., et al. Cardiolipin deficiency affects respiratory chain function and organization in an induced pluripotent stem cell model of Barth syndrome. Stem Cell Res. 2013, 11:806-819.
    • (2013) Stem Cell Res. , vol.11 , pp. 806-819
    • Dudek, J.1
  • 54
    • 84924917575 scopus 로고    scopus 로고
    • C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization
    • Desmurs M., et al. C11orf83, a mitochondrial cardiolipin-binding protein involved in bc1 complex assembly and supercomplex stabilization. Mol. Cell. Biol. 2015, 35:1139-1156.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 1139-1156
    • Desmurs, M.1
  • 55
    • 39449112660 scopus 로고    scopus 로고
    • Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria
    • Merkwirth C., et al. Prohibitins control cell proliferation and apoptosis by regulating OPA1-dependent cristae morphogenesis in mitochondria. Genes Dev. 2008, 22:476-488.
    • (2008) Genes Dev. , vol.22 , pp. 476-488
    • Merkwirth, C.1
  • 56
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • Steglich G., et al. Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Mol. Cell. Biol. 1999, 19:3435-3442.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3435-3442
    • Steglich, G.1
  • 57
    • 0034213904 scopus 로고    scopus 로고
    • Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins
    • Nijtmans L.G., et al. Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins. EMBO J. 2000, 19:2444-2451.
    • (2000) EMBO J. , vol.19 , pp. 2444-2451
    • Nijtmans, L.G.1
  • 58
    • 84867916208 scopus 로고    scopus 로고
    • Stomatin-like protein 2 deficiency in T cells is associated with altered mitochondrial respiration and defective CD4+ T cell responses
    • Christie D.A., et al. Stomatin-like protein 2 deficiency in T cells is associated with altered mitochondrial respiration and defective CD4+ T cell responses. J. Immunol. 2012, 189:4349-4360.
    • (2012) J. Immunol. , vol.189 , pp. 4349-4360
    • Christie, D.A.1
  • 59
    • 84929222831 scopus 로고    scopus 로고
    • Stomatin-like protein 2 is required for in vivo mitochondrial respiratory chain supercomplex formation and optimal cell function
    • Mitsopoulos P., et al. Stomatin-like protein 2 is required for in vivo mitochondrial respiratory chain supercomplex formation and optimal cell function. Mol. Cell. Biol. 2015, 35:1838-1847.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 1838-1847
    • Mitsopoulos, P.1
  • 60
    • 84872081577 scopus 로고    scopus 로고
    • Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV
    • Bazan S., et al. Cardiolipin-dependent reconstitution of respiratory supercomplexes from purified Saccharomyces cerevisiae complexes III and IV. J. Biol. Chem. 2013, 288:401-411.
    • (2013) J. Biol. Chem. , vol.288 , pp. 401-411
    • Bazan, S.1
  • 61
    • 84888419234 scopus 로고    scopus 로고
    • The importance of cardiolipin synthase for mitochondrial ultrastructure, respiratory function, plant development, and stress responses in Arabidopsis
    • Pineau B., et al. The importance of cardiolipin synthase for mitochondrial ultrastructure, respiratory function, plant development, and stress responses in Arabidopsis. Plant Cell 2013, 25:4195-4208.
    • (2013) Plant Cell , vol.25 , pp. 4195-4208
    • Pineau, B.1
  • 62
    • 84897600256 scopus 로고    scopus 로고
    • An Arabidopsis stomatin-like protein affects mitochondrial respiratory supercomplex organization
    • Gehl B., et al. An Arabidopsis stomatin-like protein affects mitochondrial respiratory supercomplex organization. Plant Physiol. 2014, 164:1389-1400.
    • (2014) Plant Physiol. , vol.164 , pp. 1389-1400
    • Gehl, B.1
  • 63
    • 84901049393 scopus 로고    scopus 로고
    • Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly?
    • Gehl B., Sweetlove L.J. Mitochondrial Band-7 family proteins: scaffolds for respiratory chain assembly?. Front. Plant Sci. 2014, 5:141.
    • (2014) Front. Plant Sci. , vol.5 , pp. 141
    • Gehl, B.1    Sweetlove, L.J.2
  • 64
    • 0036470775 scopus 로고    scopus 로고
    • The ATP synthase is involved in generating mitochondrial cristae morphology
    • Paumard P., et al. The ATP synthase is involved in generating mitochondrial cristae morphology. EMBO J. 2002, 21:221-230.
    • (2002) EMBO J. , vol.21 , pp. 221-230
    • Paumard, P.1
  • 65
    • 84884863198 scopus 로고    scopus 로고
    • Human F1F0 ATP synthase, mitochondrial ultrastructure and OXPHOS impairment: a (super-)complex matter?
    • Habersetzer J., et al. Human F1F0 ATP synthase, mitochondrial ultrastructure and OXPHOS impairment: a (super-)complex matter?. PLoS ONE 2013, 8:e75429.
    • (2013) PLoS ONE , vol.8 , pp. e75429
    • Habersetzer, J.1
  • 66
    • 84860528911 scopus 로고    scopus 로고
    • The effect of ethidium bromide and chloramphenicol on mitochondrial biogenesis in primary human fibroblasts
    • Kao L.P., et al. The effect of ethidium bromide and chloramphenicol on mitochondrial biogenesis in primary human fibroblasts. Toxicol. Appl. Pharmacol. 2012, 261:42-49.
    • (2012) Toxicol. Appl. Pharmacol. , vol.261 , pp. 42-49
    • Kao, L.P.1
  • 67
    • 84877583490 scopus 로고    scopus 로고
    • IF1 limits the apoptotic-signalling cascade by preventing mitochondrial remodelling
    • Faccenda D., et al. IF1 limits the apoptotic-signalling cascade by preventing mitochondrial remodelling. Cell Death Differ. 2013, 20:686-697.
    • (2013) Cell Death Differ. , vol.20 , pp. 686-697
    • Faccenda, D.1
  • 68
    • 79959915345 scopus 로고    scopus 로고
    • Atypical cristae morphology of human syncytiotrophoblast mitochondria: role for complex V
    • De los Rios C.D., et al. Atypical cristae morphology of human syncytiotrophoblast mitochondria: role for complex V. J. Biol. Chem. 2011, 286:23911-23919.
    • (2011) J. Biol. Chem. , vol.286 , pp. 23911-23919
    • De los Rios, C.D.1
  • 69
    • 84863719422 scopus 로고    scopus 로고
    • Optic atrophy 1-dependent mitochondrial remodeling controls steroidogenesis in trophoblasts
    • Wasilewski M., et al. Optic atrophy 1-dependent mitochondrial remodeling controls steroidogenesis in trophoblasts. Curr. Biol. 2012, 22:1228-1234.
    • (2012) Curr. Biol. , vol.22 , pp. 1228-1234
    • Wasilewski, M.1
  • 70
    • 84928938497 scopus 로고    scopus 로고
    • ATP synthase promotes germ cell differentiation independent of oxidative phosphorylation
    • Teixeira F.K., et al. ATP synthase promotes germ cell differentiation independent of oxidative phosphorylation. Nat. Cell Biol. 2015, 17:689-696.
    • (2015) Nat. Cell Biol. , vol.17 , pp. 689-696
    • Teixeira, F.K.1
  • 71
    • 80052691753 scopus 로고    scopus 로고
    • The permeability transition pore controls cardiac mitochondrial maturation and myocyte differentiation
    • Hom J.R., et al. The permeability transition pore controls cardiac mitochondrial maturation and myocyte differentiation. Dev. Cell 2011, 21:469-478.
    • (2011) Dev. Cell , vol.21 , pp. 469-478
    • Hom, J.R.1
  • 72
    • 84887321199 scopus 로고    scopus 로고
    • Mitochondrial fusion directs cardiomyocyte differentiation via calcineurin and Notch signaling
    • Kasahara A., et al. Mitochondrial fusion directs cardiomyocyte differentiation via calcineurin and Notch signaling. Science 2013, 342:734-737.
    • (2013) Science , vol.342 , pp. 734-737
    • Kasahara, A.1
  • 73
    • 84876031864 scopus 로고    scopus 로고
    • Dimers of mitochondrial ATP synthase form the permeability transition pore
    • Giorgio V., et al. Dimers of mitochondrial ATP synthase form the permeability transition pore. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:5887-5892.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5887-5892
    • Giorgio, V.1
  • 74
    • 84884344280 scopus 로고    scopus 로고
    • Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria
    • Daum B., et al. Age-dependent dissociation of ATP synthase dimers and loss of inner-membrane cristae in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:15301-15306.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 15301-15306
    • Daum, B.1
  • 75
    • 67449168381 scopus 로고    scopus 로고
    • Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g
    • Rabl R., et al. Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e/g. J. Cell Biol. 2009, 185:1047-1063.
    • (2009) J. Cell Biol. , vol.185 , pp. 1047-1063
    • Rabl, R.1
  • 76
    • 84875906572 scopus 로고    scopus 로고
    • Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure
    • Liesa M., Shirihai O.S. Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure. Cell Metab. 2013, 17:491-506.
    • (2013) Cell Metab. , vol.17 , pp. 491-506
    • Liesa, M.1    Shirihai, O.S.2
  • 77
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
    • Tanaka A., et al. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 2010, 191:1367-1380.
    • (2010) J. Cell Biol. , vol.191 , pp. 1367-1380
    • Tanaka, A.1
  • 78
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg M.E., et al. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 2010, 19:4861-4870.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4861-4870
    • Gegg, M.E.1
  • 79
    • 84865395988 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis
    • Leboucher G.P., et al. Stress-induced phosphorylation and proteasomal degradation of mitofusin 2 facilitates mitochondrial fragmentation and apoptosis. Mol. Cell 2012, 47:547-557.
    • (2012) Mol. Cell , vol.47 , pp. 547-557
    • Leboucher, G.P.1
  • 80
    • 84871802627 scopus 로고    scopus 로고
    • Recent advances into the understanding of mitochondrial fission
    • Elgass K., et al. Recent advances into the understanding of mitochondrial fission. Biochim. Biophys. Acta 2013, 1833:150-161.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 150-161
    • Elgass, K.1
  • 81
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • Ishihara N., et al. Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 2006, 25:2966-2977.
    • (2006) EMBO J. , vol.25 , pp. 2966-2977
    • Ishihara, N.1
  • 82
    • 76149140917 scopus 로고    scopus 로고
    • Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1
    • Ehses S., et al. Regulation of OPA1 processing and mitochondrial fusion by m-AAA protease isoenzymes and OMA1. J. Cell Biol. 2009, 187:1023-1036.
    • (2009) J. Cell Biol. , vol.187 , pp. 1023-1036
    • Ehses, S.1
  • 83
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat S., et al. Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 2006, 126:163-175.
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1
  • 84
    • 84941710348 scopus 로고    scopus 로고
    • Metalloprotease OMA1 fine-tunes mitochondrial bioenergetic function and respiratory supercomplex stability
    • Bohovych I., et al. Metalloprotease OMA1 fine-tunes mitochondrial bioenergetic function and respiratory supercomplex stability. Sci. Rep. 2015, 5:13989.
    • (2015) Sci. Rep. , vol.5 , pp. 13989
    • Bohovych, I.1
  • 85
    • 79958797425 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology and function by O-GlcNAcylation in neonatal cardiac myocytes
    • Makino A., et al. Regulation of mitochondrial morphology and function by O-GlcNAcylation in neonatal cardiac myocytes. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2011, 300:R1296-R1302.
    • (2011) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.300 , pp. R1296-R1302
    • Makino, A.1
  • 86
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban T., et al. OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum. Mol. Genet. 2010, 19:2113-2122.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2113-2122
    • Ban, T.1
  • 87
    • 84909595098 scopus 로고    scopus 로고
    • A Mitofusin-2-dependent inactivating cleavage of OPA1 links changes in mitochondria cristae and ER contacts in the postprandial liver
    • Sood A., et al. A Mitofusin-2-dependent inactivating cleavage of OPA1 links changes in mitochondria cristae and ER contacts in the postprandial liver. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:16017-16022.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 16017-16022
    • Sood, A.1
  • 88
    • 84949653400 scopus 로고    scopus 로고
    • The oxidation status of Mic19 regulates MICOS assembly
    • Sakowska P., et al. The oxidation status of Mic19 regulates MICOS assembly. Mol. Cell. Biol. 2015, 35:4222-4237.
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 4222-4237
    • Sakowska, P.1
  • 89
    • 84878527132 scopus 로고    scopus 로고
    • Age-associated metabolic and morphologic changes in mitochondria of individual mouse and hamster oocytes
    • Simsek-Duran F., et al. Age-associated metabolic and morphologic changes in mitochondria of individual mouse and hamster oocytes. PLoS ONE 2013, 8:e64955.
    • (2013) PLoS ONE , vol.8 , pp. e64955
    • Simsek-Duran, F.1
  • 90
    • 70349446460 scopus 로고    scopus 로고
    • Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart
    • Gomez L.A., et al. Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart. Arch. Biochem. Biophys. 2009, 490:30-35.
    • (2009) Arch. Biochem. Biophys. , vol.490 , pp. 30-35
    • Gomez, L.A.1
  • 91
    • 84859822387 scopus 로고    scopus 로고
    • OXPHOS supercomplexes as a hallmark of the mitochondrial phenotype of adipogenic differentiated human MSCs
    • Hofmann A.D., et al. OXPHOS supercomplexes as a hallmark of the mitochondrial phenotype of adipogenic differentiated human MSCs. PLoS ONE 2012, 7:e35160.
    • (2012) PLoS ONE , vol.7 , pp. e35160
    • Hofmann, A.D.1
  • 92
    • 0029685882 scopus 로고    scopus 로고
    • VDAC, a channel in the outer mitochondrial membrane
    • Colombini M., et al. VDAC, a channel in the outer mitochondrial membrane. Ion Channels 1996, 4:169-202.
    • (1996) Ion Channels , vol.4 , pp. 169-202
    • Colombini, M.1
  • 93
    • 0036702195 scopus 로고    scopus 로고
    • Mitochondrial protein import: two membranes, three translocases
    • Pfanner N., Wiedemann N. Mitochondrial protein import: two membranes, three translocases. Curr. Opin. Cell Biol. 2002, 14:400-411.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 400-411
    • Pfanner, N.1    Wiedemann, N.2
  • 94
    • 0030910776 scopus 로고    scopus 로고
    • The Tom and Tim machine
    • Pfanner N., Meijer M. The Tom and Tim machine. Curr. Biol. 1997, 7:R100-R103.
    • (1997) Curr. Biol. , vol.7 , pp. R100-R103
    • Pfanner, N.1    Meijer, M.2
  • 95
    • 0037815083 scopus 로고    scopus 로고
    • Protein insertion into the inner membrane of mitochondria
    • Herrmann J.M., Neupert W. Protein insertion into the inner membrane of mitochondria. IUBMB Life 2003, 55:219-225.
    • (2003) IUBMB Life , vol.55 , pp. 219-225
    • Herrmann, J.M.1    Neupert, W.2
  • 96
    • 55949098781 scopus 로고    scopus 로고
    • Respiratory active mitochondrial supercomplexes
    • Acin-Perez R., et al. Respiratory active mitochondrial supercomplexes. Mol. Cell 2008, 32:529-539.
    • (2008) Mol. Cell , vol.32 , pp. 529-539
    • Acin-Perez, R.1
  • 97
    • 0035851099 scopus 로고    scopus 로고
    • The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes
    • Schagger H., Pfeiffer K. The ratio of oxidative phosphorylation complexes I-V in bovine heart mitochondria and the composition of respiratory chain supercomplexes. J. Biol. Chem. 2001, 276:37861-37867.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37861-37867
    • Schagger, H.1    Pfeiffer, K.2
  • 98
    • 2942700102 scopus 로고    scopus 로고
    • Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserina
    • Krause F., et al. Supramolecular organization of cytochrome c oxidase- and alternative oxidase-dependent respiratory chains in the filamentous fungus Podospora anserina. J. Biol. Chem. 2004, 279:26453-26461.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26453-26461
    • Krause, F.1
  • 99
    • 37549019364 scopus 로고    scopus 로고
    • Supramolecular organization of the respiratory chain in Neurospora crassa mitochondria
    • Marques I., et al. Supramolecular organization of the respiratory chain in Neurospora crassa mitochondria. Eukaryot. Cell 2007, 6:2391-2405.
    • (2007) Eukaryot. Cell , vol.6 , pp. 2391-2405
    • Marques, I.1
  • 100
    • 84896691807 scopus 로고    scopus 로고
    • Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation
    • Chaban Y., et al. Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation. Biochim. Biophys. Acta 2014, 1837:418-426.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 418-426
    • Chaban, Y.1
  • 101
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • Stroh A., et al. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J. Biol. Chem. 2004, 279:5000-5007.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5000-5007
    • Stroh, A.1
  • 102
    • 14744270722 scopus 로고    scopus 로고
    • Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III
    • Dudkina N.V., et al. Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:3225-3229.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 3225-3229
    • Dudkina, N.V.1
  • 103
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II
    • Eubel H., et al. New insights into the respiratory chain of plant mitochondria. Supercomplexes and a unique composition of complex II. Plant Physiol. 2003, 133:274-286.
    • (2003) Plant Physiol. , vol.133 , pp. 274-286
    • Eubel, H.1
  • 104
    • 77955638748 scopus 로고    scopus 로고
    • Respiratory chain complexes in dynamic mitochondria display a patchy distribution in life cells
    • Muster B., et al. Respiratory chain complexes in dynamic mitochondria display a patchy distribution in life cells. PLoS ONE 2010, 5:e11910.
    • (2010) PLoS ONE , vol.5 , pp. e11910
    • Muster, B.1
  • 105
    • 84861320506 scopus 로고    scopus 로고
    • Rcf1 and Rcf2, members of the hypoxia-induced gene 1 protein family, are critical components of the mitochondrial cytochrome bc1-cytochrome c oxidase supercomplex
    • Strogolova V., et al. Rcf1 and Rcf2, members of the hypoxia-induced gene 1 protein family, are critical components of the mitochondrial cytochrome bc1-cytochrome c oxidase supercomplex. Mol. Cell. Biol. 2012, 32:1363-1373.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 1363-1373
    • Strogolova, V.1
  • 106
    • 84863229229 scopus 로고    scopus 로고
    • Identification of a protein mediating respiratory supercomplex stability
    • Chen Y.C., et al. Identification of a protein mediating respiratory supercomplex stability. Cell Metab. 2012, 15:348-360.
    • (2012) Cell Metab. , vol.15 , pp. 348-360
    • Chen, Y.C.1
  • 107
    • 84879617853 scopus 로고    scopus 로고
    • Supercomplex assembly determines electron flux in the mitochondrial electron transport chain
    • Lapuente-Brun E., et al. Supercomplex assembly determines electron flux in the mitochondrial electron transport chain. Science 2013, 340:1567-1570.
    • (2013) Science , vol.340 , pp. 1567-1570
    • Lapuente-Brun, E.1
  • 108
    • 84892986978 scopus 로고    scopus 로고
    • Genetic variability of respiratory complex abundance, organization and activity in mouse brain
    • Buck K.J., et al. Genetic variability of respiratory complex abundance, organization and activity in mouse brain. Genes Brain Behav. 2014, 13:135-143.
    • (2014) Genes Brain Behav. , vol.13 , pp. 135-143
    • Buck, K.J.1
  • 109
    • 84938336729 scopus 로고    scopus 로고
    • RCF1-dependent respiratory supercomplexes are integral for lifespan-maintenance in a fungal ageing model
    • Fischer F., et al. RCF1-dependent respiratory supercomplexes are integral for lifespan-maintenance in a fungal ageing model. Sci. Rep. 2015, 5:12697.
    • (2015) Sci. Rep. , vol.5 , pp. 12697
    • Fischer, F.1
  • 110
    • 84878989199 scopus 로고    scopus 로고
    • MCJ/DnaJC15, an endogenous mitochondrial repressor of the respiratory chain that controls metabolic alterations
    • Hatle K.M., et al. MCJ/DnaJC15, an endogenous mitochondrial repressor of the respiratory chain that controls metabolic alterations. Mol. Cell. Biol. 2013, 33:2302-2314.
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2302-2314
    • Hatle, K.M.1


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