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Volumn 20, Issue 12, 2014, Pages 1925-1953

Cardiolipin and mitochondrial function in health and disease

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CARDIOLIPIN; PHOSPHOLIPID;

EID: 84897092477     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2013.5280     Document Type: Review
Times cited : (88)

References (242)
  • 1
    • 79959727395 scopus 로고    scopus 로고
    • Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria
    • Acehan D, Malhotra A, Xu Y, Ren M, Stokes DL, and Schlame M. Cardiolipin affects the supramolecular organization of ATP synthase in mitochondria. Biophys J 100: 2184-2192, 2011
    • (2011) Biophys J , vol.100 , pp. 2184-2192
    • Acehan, D.1    Malhotra, A.2    Xu, Y.3    Ren, M.4    Stokes, D.L.5    Schlame, M.6
  • 4
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM and Cory S. The Bcl-2 protein family: Arbiters of cell survival. Science 281: 1322-1326, 1998
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 5
    • 84874117448 scopus 로고    scopus 로고
    • Mitochondrial handling of excess Ca2 + is substrate-dependent with implications for reactive oxygen species generation
    • Aldakkak M, Stowe DF, Dash RK, and Camara AK. Mitochondrial handling of excess Ca2 + is substrate-dependent with implications for reactive oxygen species generation. Free Radic Biol Med 56: 193-203, 2013
    • (2013) Free Radic Biol Med , vol.56 , pp. 193-203
    • Aldakkak, M.1    Stowe, D.F.2    Dash, R.K.3    Camara, A.K.4
  • 6
    • 0024392222 scopus 로고
    • An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques
    • Allen RD, Schroeder CC, and Fok AK. An investigation of mitochondrial inner membranes by rapid-freeze deep-etch techniques. J Cell Biol 108: 2233-2240, 1989
    • (1989) J Cell Biol , vol.108 , pp. 2233-2240
    • Allen, R.D.1    Schroeder, C.C.2    Fok, A.K.3
  • 7
    • 0026319007 scopus 로고
    • The relationship between oxygen radical generation and impairment of myocardial energy metabolism following post-ischemic reperfusion
    • Ambrosio G, Zweier JL, and Flaherty JT. The relationship between oxygen radical generation and impairment of myocardial energy metabolism following post-ischemic reperfusion. J Mol Cell Cardiol 12: 1359-1374, 1991
    • (1991) J Mol Cell Cardiol , vol.12 , pp. 1359-1374
    • Ambrosio, G.1    Zweier, J.L.2    Flaherty, J.T.3
  • 9
    • 0032534790 scopus 로고    scopus 로고
    • Yeast mitochondrial F1F0-ATP synthase exists as a dimer: Identification of three dimer-specific subunits
    • Arnold I, Pfeiffer K, Neupert W, Stuart RA, and Schägger H. Yeast mitochondrial F1F0-ATP synthase exists as a dimer: Identification of three dimer-specific subunits. EMBO J 17: 7170-7178, 1998
    • (1998) EMBO J , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schägger, H.5
  • 11
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • Baines CP, Kaiser RA, Sheiko T, Craigen WJ, and Molkentin JD. Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol 9: 550-555, 2007
    • (2007) Nat Cell Biol , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 12
    • 77953526521 scopus 로고    scopus 로고
    • OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation
    • Ban T, Heymann JA, Song Z, Hinshaw JE, and Chan DC. OPA1 disease alleles causing dominant optic atrophy have defects in cardiolipin-stimulated GTP hydrolysis and membrane tubulation. Hum Mol Genet 19: 2113-2122, 2010
    • (2010) Hum Mol Genet , vol.19 , pp. 2113-2122
    • Ban, T.1    Heymann, J.A.2    Song, Z.3    Hinshaw, J.E.4    Chan, D.C.5
  • 14
    • 55549126837 scopus 로고    scopus 로고
    • Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation
    • Basso E, Petronilli V, Forte MA, and Bernardi P. Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation. J Biol Chem 283: 26307-26311, 2008
    • (2008) J Biol Chem , vol.283 , pp. 26307-26311
    • Basso, E.1    Petronilli, V.2    Forte, M.A.3    Bernardi, P.4
  • 17
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman KB and Ames BN. The free radical theory of aging matures. Physiol Rev 78: 547-581, 1998
    • (1998) Physiol Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 18
    • 32844458032 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in NASH: Causes, consequences and possible means to prevent it
    • Begriche K, Igoudjil A, Pessayre D, and Fromenty B. Mitochondrial dysfunction in NASH: Causes, consequences and possible means to prevent it. Mitochondrion 6: 1-28, 2006
    • (2006) Mitochondrion , vol.6 , pp. 1-28
    • Begriche, K.1    Igoudjil, A.2    Pessayre, D.3    Fromenty, B.4
  • 20
    • 66449086494 scopus 로고    scopus 로고
    • Identification of a cardiolipin-specific phospholipase encoded by the gene CLD1 (YGR110W) in yeast
    • Beranek A, Rechberger G, Knauer H, Wolinski H, Kohlwein SD, and Leber R. Identification of a cardiolipin-specific phospholipase encoded by the gene CLD1 (YGR110W) in yeast. J Biol Chem 284: 11572-11578, 2009
    • (2009) J Biol Chem , vol.284 , pp. 11572-11578
    • Beranek, A.1    Rechberger, G.2    Knauer, H.3    Wolinski, H.4    Kohlwein, S.D.5    Leber, R.6
  • 21
    • 0022427458 scopus 로고
    • ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance
    • Beyer K and Klingenberg M. ADP/ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance. Biochemistry 24: 3821-3826, 1985
    • (1985) Biochemistry , vol.24 , pp. 3821-3826
    • Beyer, K.1    Klingenberg, M.2
  • 22
    • 4344561983 scopus 로고    scopus 로고
    • The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis
    • Bianchi C, Genova ML, Parenti Castelli G, and Lenaz G. The mitochondrial respiratory chain is partially organized in a supercomplex assembly: Kinetic evidence using flux control analysis. J Biol Chem 279: 36562-36569, 2004
    • (2004) J Biol Chem , vol.279 , pp. 36562-36569
    • Bianchi, C.1    Genova, M.L.2    Parenti Castelli, G.3    Lenaz, G.4
  • 24
    • 0021226779 scopus 로고
    • Specific elution from hydroxylapatite of the mitochondrial phosphate carrier by cardiolipin
    • Bisaccia F and Palmieri F. Specific elution from hydroxylapatite of the mitochondrial phosphate carrier by cardiolipin. Biochim Biophys Acta 766: 386-394, 1984
    • (1984) Biochim Biophys Acta , vol.766 , pp. 386-394
    • Bisaccia, F.1    Palmieri, F.2
  • 25
    • 0026019727 scopus 로고
    • Mapping of the locus for X-linked cardioskeletal myopathy with neutropenia and abnormal mitochondria (Barth syndrome) to Xq28
    • Bolhuis PA, Hensels GW, Hulsebos TJ, Baas F, and Barth PG. Mapping of the locus for X-linked cardioskeletal myopathy with neutropenia and abnormal mitochondria (Barth syndrome) to Xq28. Am J Hum Genet 48: 481-485, 1991
    • (1991) Am J Hum Genet , vol.48 , pp. 481-485
    • Bolhuis, P.A.1    Hensels, G.W.2    Hulsebos, T.J.3    Baas, F.4    Barth, P.G.5
  • 26
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbaric oxygen
    • Boveris A and Chance B. The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbaric oxygen. Biochem J 134: 707-716, 1973
    • (1973) Biochem J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 27
    • 27644437287 scopus 로고    scopus 로고
    • Taz1 an outer mitochondrial membrane protein affects stability and assembly of inner membrane protein complexes: Implications for barth syndrome
    • Brandner K, Mick DU, Frazier AE, Taylor RD, Meisinger C, and Rehling P. Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: Implications for Barth Syndrome. Mol Biol Cell 16: 5202-5214, 2005
    • (2005) Mol Biol Cell , vol.16 , pp. 5202-5214
    • Brandner, K.1    Mick, D.U.2    Frazier, A.E.3    Taylor, R.D.4    Meisinger, C.5    Rehling, P.6
  • 28
    • 0029953927 scopus 로고    scopus 로고
    • Mitochondrial ADP/ ATP carrier can be reversibly converted into a large channel by Ca2 +
    • Brustovetsky N and Klingenberg M. Mitochondrial ADP/ ATP carrier can be reversibly converted into a large channel by Ca2 + . Biochemistry 35: 8483-8488, 1996
    • (1996) Biochemistry , vol.35 , pp. 8483-8488
    • Brustovetsky, N.1    Klingenberg, M.2
  • 29
    • 67649756320 scopus 로고    scopus 로고
    • Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease
    • Büeler H. Impaired mitochondrial dynamics and function in the pathogenesis of Parkinson's disease. Exp Neurol 218: 235-246, 2009
    • (2009) Exp Neurol , vol.218 , pp. 235-246
    • Büeler, H.1
  • 30
    • 0016719078 scopus 로고
    • The reaction between the superoxide anion radical and cytochrome c
    • Butler J, Jayson GG, and Swallow AJ. The reaction between the superoxide anion radical and cytochrome c. Biochim Biophys Acta 408: 215-222, 1975
    • (1975) Biochim Biophys Acta , vol.408 , pp. 215-222
    • Butler, J.1    Jayson, G.G.2    Swallow, A.J.3
  • 31
    • 80054978144 scopus 로고    scopus 로고
    • Mitochondrial approaches to protect against cardiac ischemia and reperfusion injury
    • Camara AK, Bienengraeber M, and Stowe DF. Mitochondrial approaches to protect against cardiac ischemia and reperfusion injury. Front Physiol 2:13, 2011
    • (2011) Front Physiol , vol.2 , Issue.13
    • Camara, A.K.1    Bienengraeber, M.2    Stowe, D.F.3
  • 32
    • 3843084029 scopus 로고    scopus 로고
    • A novel cardiolipin-remodeling pathway revealed by a gene encoding an endoplasmic reticulum-Associated acyl-CoA:lysocardiolipin acyltransferase (ALCAT1) in mouse
    • Cao J, Liu Y, Lockwood J, Burn P, and Shi Y. A novel cardiolipin- remodeling pathway revealed by a gene encoding an endoplasmic reticulum-Associated acyl-CoA:lysocardiolipin acyltransferase (ALCAT1) in mouse. J Biol Chem 279: 31727-31734, 2004
    • (2004) J Biol Chem , vol.279 , pp. 31727-31734
    • Cao, J.1    Liu, Y.2    Lockwood, J.3    Burn, P.4    Shi, Y.5
  • 33
    • 33746933765 scopus 로고    scopus 로고
    • The many shapes of mitochondrial death
    • Cereghetti GM and Scorrano L. The many shapes of mitochondrial death. Oncogene 25: 4717-4724, 2006
    • (2006) Oncogene , vol.25 , pp. 4717-4724
    • Cereghetti, G.M.1    Scorrano, L.2
  • 35
    • 33748347104 scopus 로고    scopus 로고
    • Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria
    • Chen D, Zhang XY, and Shi Y. Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria. Biochem J 398: 169-176, 2006
    • (2006) Biochem J , vol.398 , pp. 169-176
    • Chen, D.1    Zhang, X.Y.2    Shi, Y.3
  • 36
    • 42549160157 scopus 로고    scopus 로고
    • Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth
    • Chen S, He Q, and Greenberg ML. Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth. Mol Microbiol 68: 1061-1072, 2008
    • (2008) Mol Microbiol , vol.68 , pp. 1061-1072
    • Chen, S.1    He, Q.2    Greenberg, M.L.3
  • 37
    • 33846272138 scopus 로고    scopus 로고
    • Role of cardiolipin alterations in mitochondrial dysfunction and disease
    • Chicco AJ and Sparagna GC. Role of cardiolipin alterations in mitochondrial dysfunction and disease. Am J Physiol Cell Physiol 292: C33-C44, 2007
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Chicco, A.J.1    Sparagna, G.C.2
  • 38
    • 33745950626 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeabilization during apoptosis: The innocent bystander scenario
    • Chipuk JE, Bouchier-Hayes L, and Green DR. Mitochondrial outer membrane permeabilization during apoptosis: The innocent bystander scenario. Cell Death Differ 8: 1396-1402, 2006
    • (2006) Cell Death Differ , vol.8 , pp. 1396-1402
    • Chipuk, J.E.1    Bouchier-Hayes, L.2    Green, D.R.3
  • 39
    • 0035078484 scopus 로고    scopus 로고
    • Etiopathogenesis of nonalcoholic steatohepatitis
    • Chitturi S and Farrell GC. Etiopathogenesis of nonalcoholic steatohepatitis. Semin Liver Dis 21: 27-41, 2001
    • (2001) Semin Liver Dis , vol.21 , pp. 27-41
    • Chitturi, S.1    Farrell, G.C.2
  • 40
    • 33750526473 scopus 로고    scopus 로고
    • A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis
    • Choi SY, Huang P, Jenkins GM, Chan DC, Schiller J, and Frohman MA. A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis. Nat Cell Biol 11: 1255-1262, 2006
    • (2006) Nat Cell Biol , vol.11 , pp. 1255-1262
    • Choi, S.Y.1    Huang, P.2    Jenkins, G.M.3    Chan, D.C.4    Schiller, J.5    Frohman, M.A.6
  • 42
    • 33746606474 scopus 로고    scopus 로고
    • Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins
    • Claypool SM, McCaffery JM, and Koehler CM. Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins. J Cell Biol 174: 379-390, 2006
    • (2006) J Cell Biol , vol.174 , pp. 379-390
    • Claypool, S.M.1    McCaffery, J.M.2    Koehler, C.M.3
  • 43
    • 51649096941 scopus 로고    scopus 로고
    • Cardiolipin defines the interactome of the major ADP/ ATP carrier protein of the mitochondrial inner membrane
    • Claypool SM, Oktay Y, Boontheung P, Loo JA, and Koehler CM. Cardiolipin defines the interactome of the major ADP/ ATP carrier protein of the mitochondrial inner membrane. J Cell Biol 182: 937-950, 2008
    • (2008) J Cell Biol , vol.182 , pp. 937-950
    • Claypool, S.M.1    Oktay, Y.2    Boontheung, P.3    Loo, J.A.4    Koehler, C.M.5
  • 44
    • 70349557331 scopus 로고    scopus 로고
    • Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function
    • Claypool SM. Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function. Biochim Biophys Acta 1788: 2059-2068, 2009
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2059-2068
    • Claypool, S.M.1
  • 45
    • 44749085250 scopus 로고    scopus 로고
    • Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification
    • Cole NB, Dieuliis D, Leo P, Mitchell DC, and Nussbaum RL. Mitochondrial translocation of alpha-synuclein is promoted by intracellular acidification. Exp Cell Res 314: 2076-2089, 2008
    • (2008) Exp Cell Res , vol.314 , pp. 2076-2089
    • Cole, N.B.1    Dieuliis, D.2    Leo, P.3    Mitchell, D.C.4    Nussbaum, R.L.5
  • 46
    • 0023821864 scopus 로고
    • Inhibition by cyclosporin A of a Ca2 +-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • Crompton M, Ellinger H, and Costi A. Inhibition by cyclosporin A of a Ca2 +-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem J 255: 357-360, 1988
    • (1988) Biochem J , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 47
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J 341 (Pt 2): 233-249, 1999
    • (1999) Biochem J , vol.341 , Issue.PART 2 , pp. 233-249
    • Crompton, M.1
  • 48
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis PR and de Kruijff B. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim Biophys Acta 559: 399-420, 1979
    • (1979) Biochim Biophys Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 49
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum G. Lipids of mitochondria. Biochim Biophys Acta 822: 1-42, 1985
    • (1985) Biochim Biophys Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 50
    • 0031551023 scopus 로고    scopus 로고
    • Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membrané
    • de Kroon AI, Dolis D, Mayer A, Lill R, and de Kruijff B. Phospholipid composition of highly purified mitochondrial outer membranes of rat liver and Neurospora crassa. Is cardiolipin present in the mitochondrial outer membranéBiochim Biophys Acta 1325: 108-116, 1997
    • (1997) Biochim Biophys Acta , vol.1325 , pp. 108-116
    • De Kroon, A.I.1    Dolis, D.2    Mayer, A.3    Lill, R.4    De Kruijff, B.5
  • 52
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • Dowhan W. Molecular basis for membrane phospholipid diversity: Why are there so many lipids?Annu Rev Biochem 66: 199-232, 1997
    • (1997) Annu Rev Biochem , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 53
    • 0343964750 scopus 로고
    • Tightly associated cardiolipin in the bovine heart mitochondrial ATP synthase as analyzed by 31P nuclear magnetic resonance spectroscopy
    • Eble KS, Coleman WB, Hantgan RR, and Cunningham CC. Tightly associated cardiolipin in the bovine heart mitochondrial ATP synthase as analyzed by 31P nuclear magnetic resonance spectroscopy. J Biol Chem 265: 19434-19440, 1990
    • (1990) J Biol Chem , vol.265 , pp. 19434-19440
    • Eble, K.S.1    Coleman, W.B.2    Hantgan, R.R.3    Cunningham, C.C.4
  • 56
    • 33846023675 scopus 로고    scopus 로고
    • Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes
    • Epand RF, Schlattner U, Wallimann T, Lacombe ML, and Epand RM. Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes. Biophys J 92: 126-137, 2007
    • (2007) Biophys J , vol.92 , pp. 126-137
    • Epand, R.F.1    Schlattner, U.2    Wallimann, T.3    Lacombe, M.L.4    Epand, R.M.5
  • 59
    • 0019887784 scopus 로고
    • Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain
    • Fry M and Green DE. Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain. J Biol Chem 256: 1874-1880, 1981
    • (1981) J Biol Chem , vol.256 , pp. 1874-1880
    • Fry, M.1    Green, D.E.2
  • 61
    • 84855809495 scopus 로고    scopus 로고
    • Damage to mitochondrial complex I during cardiac ischemia reperfusion injury is reduced indirectly by anti-Anginal drug ranolazine
    • Gadicherla AK, Stowe DF, Antholine WE, Yang M, and Camara AK. Damage to mitochondrial complex I during cardiac ischemia reperfusion injury is reduced indirectly by anti-Anginal drug ranolazine. Biochim Biophys Acta 1817: 419-429, 2012
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 419-429
    • Gadicherla, A.K.1    Stowe, D.F.2    Antholine, W.E.3    Yang, M.4    Camara, A.K.5
  • 62
    • 33748108494 scopus 로고    scopus 로고
    • Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import
    • Gallas MR, Dienhart MK, Stuart RA, and Long RM. Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import. Mol Biol Cell 17: 4051-4062, 2006
    • (2006) Mol Biol Cell , vol.17 , pp. 4051-4062
    • Gallas, M.R.1    Dienhart, M.K.2    Stuart, R.A.3    Long, R.M.4
  • 65
    • 0039843110 scopus 로고    scopus 로고
    • Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc1
    • Gomez B, Jr. and Robinson NC. Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc1. Biochemistry 38: 9031-9038, 1999
    • (1999) Biochemistry , vol.38 , pp. 9031-9038
    • Gomez Jr., B.1    Robinson, N.C.2
  • 66
    • 70349446460 scopus 로고    scopus 로고
    • Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart
    • Gómez LA, Monette JS, Chavez JD, Maier CS, and Hagen TM. Supercomplexes of the mitochondrial electron transport chain decline in the aging rat heart. Arch Biochem Biophys 490: 30-35, 2009
    • (2009) Arch Biochem Biophys , vol.490 , pp. 30-35
    • Gómez, L.A.1    Monette, J.S.2    Chavez, J.D.3    Maier, C.S.4    Hagen, T.M.5
  • 67
    • 34247482333 scopus 로고    scopus 로고
    • Cardiolipin: Setting the beat of apoptosis
    • Gonzalvez F and Gottlieb E. Cardiolipin: Setting the beat of apoptosis. Apoptosis 12: 877-885, 2007
    • (2007) Apoptosis , vol.12 , pp. 877-885
    • Gonzalvez, F.1    Gottlieb, E.2
  • 69
    • 0032589515 scopus 로고    scopus 로고
    • Ca2 +-induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of Ca2 +-stimulated generation of reactive oxygen species by the respiratory chain
    • Grijalba MT, Vercesi AE, and Schreier S. Ca2 +-induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of Ca2 +-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry 38: 13279-13287, 1999
    • (1999) Biochemistry , vol.38 , pp. 13279-13287
    • Grijalba, M.T.1    Vercesi, A.E.2    Schreier, S.3
  • 71
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • Hackenbrock CR, Chazotte B, and Gupte SS. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J Bioenerg Biomembr 18: 331-368, 1986
    • (1986) J Bioenerg Biomembr , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 72
    • 0037174138 scopus 로고    scopus 로고
    • Cardiolipin: A proton trap for oxidative phosphorylation
    • Haines TH and Dencher NA. Cardiolipin: A proton trap for oxidative phosphorylation. FEBS Lett 528: 35-39, 2002
    • (2002) FEBS Lett , vol.528 , pp. 35-39
    • Haines, T.H.1    Dencher, N.A.2
  • 73
    • 1142273368 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening during myocardial reperfusion-A target for cardioprotection
    • Halestrap AP, Clarke SJ, and Javadov SA. Mitochondrial permeability transition pore opening during myocardial reperfusion-A target for cardioprotection. Cardiovasc Res 61: 372-385, 2004
    • (2004) Cardiovasc Res , vol.61 , pp. 372-385
    • Halestrap, A.P.1    Clarke, S.J.2    Javadov, S.A.3
  • 74
    • 0025193488 scopus 로고
    • Inhibition of Ca2 (+)-induced large-Amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-Trans isomerase and preventing it interacting with the adenine nucleotide translocase
    • Halestrap AP and Davidson AM. Inhibition of Ca2 (+)-induced large-Amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl cis-Trans isomerase and preventing it interacting with the adenine nucleotide translocase. Biochem J 268: 153-160, 1990
    • (1990) Biochem J , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 75
    • 33645994183 scopus 로고    scopus 로고
    • Calcium, mitochondria and reperfusion injury: A pore way to die
    • Halestrap AP. Calcium, mitochondria and reperfusion injury: A pore way to die. Biochem Soc Trans 34: 232-237, 2006
    • (2006) Biochem Soc Trans , vol.34 , pp. 232-237
    • Halestrap, A.P.1
  • 76
    • 4344707798 scopus 로고    scopus 로고
    • Mitochondrial permeability: Dual role for the ADP/ATP translocator?
    • p following 983
    • Halestrap AP. Mitochondrial permeability: Dual role for the ADP/ATP translocator?Nature 430: 1 p following 983, 2004
    • (2004) Nature , vol.430 , pp. 1
    • Halestrap, A.P.1
  • 77
    • 0034668933 scopus 로고    scopus 로고
    • Diabetes-induced changes in specific lipid molecular species in rat myocardium
    • Han X, Abendschein DR, Kelley JG, and Gross RW. Diabetes-induced changes in specific lipid molecular species in rat myocardium. Biochem J 15 Pt 1: 79-89, 2000
    • (2000) Biochem J , vol.15 , Issue.PART 1 , pp. 79-89
    • Han, X.1    Abendschein, D.R.2    Kelley, J.G.3    Gross, R.W.4
  • 78
    • 29244477536 scopus 로고    scopus 로고
    • Shotgun lipidomics identifies cardiolipin depletion in diabetic myocardium linking altered substrate utilization with mitochondrial dysfunction
    • Han X, Yang J, Cheng H, Yang K, Abendschein DR, and Gross RW. Shotgun lipidomics identifies cardiolipin depletion in diabetic myocardium linking altered substrate utilization with mitochondrial dysfunction. Biochemistry 44: 16684-16694, 2005
    • (2005) Biochemistry , vol.44 , pp. 16684-16694
    • Han, X.1    Yang, J.2    Cheng, H.3    Yang, K.4    Abendschein, D.R.5    Gross, R.W.6
  • 79
    • 34249672811 scopus 로고    scopus 로고
    • Alterations in myocardial cardiolipin content and composition occur at the very earliest stages of diabetes: A shotgun lipidomics study
    • Han X, Yang J, Yang K, Zhao Z, Abendschein DR, and Gross RW. Alterations in myocardial cardiolipin content and composition occur at the very earliest stages of diabetes: A shotgun lipidomics study. Biochemistry 46: 6417-6428, 2007
    • (2007) Biochemistry , vol.46 , pp. 6417-6428
    • Han, X.1    Yang, J.2    Yang, K.3    Zhao, Z.4    Abendschein, D.R.5    Gross, R.W.6
  • 80
    • 0037383432 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: Its fundamental role in mediating cell death during ischaemia and reperfusion
    • Hausenloy DJ and Yellon DM. The mitochondrial permeability transition pore: Its fundamental role in mediating cell death during ischaemia and reperfusion. J Mol Cell Cardiol 35: 339-341, 2003
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 339-341
    • Hausenloy, D.J.1    Yellon, D.M.2
  • 81
    • 0036203605 scopus 로고    scopus 로고
    • Disease-specific remodeling of cardiac mitochondria after a left ventricular assist device
    • Heerdt PM, Schlame M, Jehle R, Barbone A, Burkhoff D, and Blanck TJ. Disease-specific remodeling of cardiac mitochondria after a left ventricular assist device. Ann Thorac Surg 73: 1216-1221, 2002
    • (2002) Ann Thorac Surg , vol.73 , pp. 1216-1221
    • Heerdt, P.M.1    Schlame, M.2    Jehle, R.3    Barbone, A.4    Burkhoff, D.5    Blanck, T.J.6
  • 82
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-Type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan M, Vogel F, Bornhovd C, Neupert W, and Reichert AS. Processing of Mgm1 by the rhomboid-Type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J Biol Chem 278: 27781-27788, 2003
    • (2003) J Biol Chem , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhovd, C.3    Neupert, W.4    Reichert, A.S.5
  • 83
    • 0033929763 scopus 로고    scopus 로고
    • Apoptosis in the aging process
    • Higami Y and Shimokawa I. Apoptosis in the aging process. Cell Tissue Res 301: 125-132, 2000
    • (2000) Cell Tissue Res , vol.301 , pp. 125-132
    • Higami, Y.1    Shimokawa, I.2
  • 84
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch FL. Cardiolipins and biomembrane function. Biochim Biophys Acta 1113: 71-133, 1992
    • (1992) Biochim Biophys Acta , vol.1113 , pp. 71-133
    • Hoch, F.L.1
  • 85
    • 0028084988 scopus 로고
    • The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants
    • Hoffmann B, Stöckl A, Schlame M, Beyer K, and Klingenberg M. The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants. J Biol Chem 269: 1940-1944, 1994
    • (1994) J Biol Chem , vol.269 , pp. 1940-1944
    • Hoffmann, B.1    Stöckl, A.2    Schlame, M.3    Beyer, K.4    Klingenberg, M.5
  • 86
    • 34250204271 scopus 로고    scopus 로고
    • The machines that divide and fuse mitochondria
    • Hoppins S, Lackner L, and Nunnari J. The machines that divide and fuse mitochondria. Annu Rev Biochem 76: 751-780, 2007
    • (2007) Annu Rev Biochem , vol.76 , pp. 751-780
    • Hoppins, S.1    Lackner, L.2    Nunnari, J.3
  • 87
    • 0026094952 scopus 로고
    • Effect of thyroxine on the activity of mitochondrial cardiolipin synthase in rat liver
    • Hostetler KY. Effect of thyroxine on the activity of mitochondrial cardiolipin synthase in rat liver. Biochim Biophys Acta 1086: 139-140, 1991
    • (1991) Biochim Biophys Acta , vol.1086 , pp. 139-140
    • Hostetler, K.Y.1
  • 89
    • 50249148905 scopus 로고    scopus 로고
    • Cardiolipin, the heart of mitochondrial metabolism
    • Houtkooper RH and Vaz FM. Cardiolipin, the heart of mitochondrial metabolism. Cell Mol Life Sci 65: 2493-2506, 2008
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2493-2506
    • Houtkooper, R.H.1    Vaz, F.M.2
  • 91
    • 79953745644 scopus 로고    scopus 로고
    • The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis
    • Hüttemann M, Pecina P, Rainbolt M, Sanderson TH, Kagan VE, Samavati L, Doan JW, and Lee I. The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis. Mitochondrion 11: 369-381, 2011
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Hüttemann, M.1    Pecina, P.2    Rainbolt, M.3    Sanderson, T.H.4    Kagan, V.E.5    Samavati, L.6    Doan, J.W.7    Lee, I.8
  • 92
    • 0038584862 scopus 로고    scopus 로고
    • Protection from inactivation of the adenine nucleotide translocator during hypoglycaemia-induced apoptosis by mitochondrial phospholipid hydroperoxide glutathione peroxidase
    • Imai H, Koumura T, Nakajima R, Nomura K, and Nakagawa Y. Protection from inactivation of the adenine nucleotide translocator during hypoglycaemia-induced apoptosis by mitochondrial phospholipid hydroperoxide glutathione peroxidase. Biochem J 371: 799-809, 2003
    • (2003) Biochem J , vol.371 , pp. 799-809
    • Imai, H.1    Koumura, T.2    Nakajima, R.3    Nomura, K.4    Nakagawa, Y.5
  • 98
    • 3042723249 scopus 로고    scopus 로고
    • Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release
    • Kim TH, Zhao Y, Ding WX, Shin JN, He X, Seo YW, Chen J, Rabinowich H, Amoscato AA, and Yin XM. Bid-cardiolipin interaction at mitochondrial contact site contributes to mitochondrial cristae reorganization and cytochrome C release. Mol Biol Cell 7: 3061-3072, 2004
    • (2004) Mol Biol Cell , vol.7 , pp. 3061-3072
    • Kim, T.H.1    Zhao, Y.2    Ding, W.X.3    Shin, J.N.4    He, X.5    Seo, Y.W.6    Chen, J.7    Rabinowich, H.8    Amoscato, A.A.9    Yin, X.M.10
  • 99
    • 33947096050 scopus 로고    scopus 로고
    • Redox-linked protonation state changes in cytochrome bc1 identified by Poisson-Boltzmann electrostatics calculations
    • Klingen AR, Palsdottir H, Hunte C, and Ullmann GM. Redox-linked protonation state changes in cytochrome bc1 identified by Poisson-Boltzmann electrostatics calculations. Biochim Biophys Acta 1767: 204-221, 2007
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 204-221
    • Klingen, A.R.1    Palsdottir, H.2    Hunte, C.3    Ullmann, G.M.4
  • 100
    • 70349518563 scopus 로고    scopus 로고
    • Cardiolipin and mitochondrial carriers
    • Klingenberg M. Cardiolipin and mitochondrial carriers. Biochim Biophys Acta 1788: 2048-2058, 2009
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2048-2058
    • Klingenberg, M.1
  • 105
    • 0022924993 scopus 로고
    • Reconstitution of mitochondrial F0.F1-ATPase with phosphatidylcholine using the nonionic detergent, octylglucoside
    • Laird DM, Eble KS, and Cunningham CC. Reconstitution of mitochondrial F0.F1-ATPase with phosphatidylcholine using the nonionic detergent, octylglucoside. J Biol Chem 261: 14844-14850, 1986
    • (1986) J Biol Chem , vol.261 , pp. 14844-14850
    • Laird, D.M.1    Eble, K.S.2    Cunningham, C.C.3
  • 106
    • 0035803487 scopus 로고    scopus 로고
    • Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure
    • Lange C, Nett JH, Trumpower BL, and Hunte C. Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure. EMBO J 20: 6591-6600, 2001
    • (2001) EMBO J , vol.20 , pp. 6591-6600
    • Lange, C.1    Nett, J.H.2    Trumpower, B.L.3    Hunte, C.4
  • 107
    • 0344756428 scopus 로고
    • On the structure of cardiolipin
    • Lecocq J and Ballou CE. On the structure of cardiolipin. Biochemistry 3: 976-980, 1964
    • (1964) Biochemistry , vol.3 , pp. 976-980
    • Lecocq, J.1    Ballou, C.E.2
  • 109
    • 77949634569 scopus 로고    scopus 로고
    • Structure and organization of mitochondrial respiratory complexes: A new understanding of an old subject
    • Lenaz G and Genova ML. Structure and organization of mitochondrial respiratory complexes: A new understanding of an old subject. Antioxid Redox Signal 12: 961-1008, 2010
    • (2010) Antioxid Redox Signal , vol.12 , pp. 961-008
    • Lenaz, G.1    Genova, M.L.2
  • 111
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A, Bassik MC, Walensky LD, Sorcinelli MD, Weiler S, and Korsmeyer SJ. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 3: 183-192, 2002
    • (2002) Cancer Cell , vol.3 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 112
    • 55549091082 scopus 로고    scopus 로고
    • The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition
    • Leung AW, Varanyuwatana P, and Halestrap AP. The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition. J Biol Chem 283: 26312-26323, 2008
    • (2008) J Biol Chem , vol.283 , pp. 26312-26323
    • Leung, A.W.1    Varanyuwatana, P.2    Halestrap, A.P.3
  • 113
    • 0142156049 scopus 로고    scopus 로고
    • Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response
    • Liu J, Dai Q, Chen J, Durrant D, Freeman A, Liu T, Grossman D, and Lee RM. Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response. Mol Cancer Res 12: 892-902, 2003
    • (2003) Mol Cancer Res , vol.12 , pp. 892-902
    • Liu, J.1    Dai, Q.2    Chen, J.3    Durrant, D.4    Freeman, A.5    Liu, T.6    Grossman, D.7    Lee, R.M.8
  • 114
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, and Wang X. Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 86: 147-157, 1996
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 117
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, and Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94: 481-490, 1998
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 118
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter M, Fang M, Luo X, Nishijima M, Xie X, and Wang X. Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat Cell Biol 2: 754-761, 2000
    • (2000) Nat Cell Biol , vol.2 , pp. 754-761
    • Lutter, M.1    Fang, M.2    Luo, X.3    Nishijima, M.4    Xie, X.5    Wang, X.6
  • 119
    • 18744374204 scopus 로고    scopus 로고
    • The pro-Apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites
    • Lutter M, Perkins GA, and Wang X. The pro-Apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites. BMC Cell Biol 2: 22, 2001
    • (2001) BMC Cell Biol , vol.2 , pp. 22
    • Lutter, M.1    Perkins, G.A.2    Wang, X.3
  • 120
    • 84855181568 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and b-cell failure in type 2 diabetes mellitus
    • Ma ZA, Zhao Z, and Turk J. Mitochondrial dysfunction and b-cell failure in type 2 diabetes mellitus. Exp Diabetes Res 2012: 703538, 2012
    • (2012) Exp Diabetes Res , vol.2012 , pp. 703538
    • Ma, Z.A.1    Zhao, Z.2    Turk, J.3
  • 121
    • 62249151764 scopus 로고    scopus 로고
    • Formation of molecular species of mitochondrial cardiolipin 1 A novel transacylation mechanism to shuttle fatty acids between sn-1 and sn-2 positions of multiple phospholipid species
    • Malhotra A, Xu Y, Ren M, and Schlame M. Formation of molecular species of mitochondrial cardiolipin. 1. A novel transacylation mechanism to shuttle fatty acids between sn-1 and sn-2 positions of multiple phospholipid species. Biochim Biophys Acta 1791: 314-320, 2009
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 314-320
    • Malhotra, A.1    Xu, Y.2    Ren, M.3    Schlame, M.4
  • 122
    • 72149127390 scopus 로고    scopus 로고
    • Genetic ablation of calcium-independent phospholipase A2{gamma} leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy, and cognitive dysfunction
    • Mancuso DJ, Kotzbauer P, Wozniak DF, Sims HF, Jenkins CM, Guan S, Han X, Yang K, Sun G, Malik I, Conyers S, Green KG, Schmidt RE, and Gross RW. Genetic ablation of calcium-independent phospholipase A2{gamma} leads to alterations in hippocampal cardiolipin content and molecular species distribution, mitochondrial degeneration, autophagy, and cognitive dysfunction. J Biol Chem 284: 35632-35644, 2009
    • (2009) J Biol Chem , vol.284 , pp. 35632-35644
    • Mancuso, D.J.1    Kotzbauer, P.2    Wozniak, D.F.3    Sims, H.F.4    Jenkins, C.M.5    Guan, S.6    Han, X.7    Yang, K.8    Sun, G.9    Malik, I.10    Conyers, S.11    Green, K.G.12    Schmidt, R.E.13    Gross, R.W.14
  • 126
    • 0023831219 scopus 로고
    • Free radicals and myocardial ischemia: Overview and outlook
    • McCord JM. Free radicals and myocardial ischemia: Overview and outlook. Free Radic Biol Med 4: 9-14, 1988
    • (1988) Free Radic Biol Med , vol.4 , pp. 9-14
    • McCord, J.M.1
  • 127
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients
    • McKenzie M, Lazarou M, Thorburn DR, and Ryan MT. Mitochondrial respiratory chain supercomplexes are destabilized in Barth Syndrome patients. J Mol Biol 361: 462-469, 2006
    • (2006) J Mol Biol , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 129
    • 0026751740 scopus 로고
    • Relation of mitochondrial and cytosolic free calcium to cardiac myocyte recovery after exposure to anoxia
    • Miyata H, Lakatta EG, Stern MD, and Silverman HS. Relation of mitochondrial and cytosolic free calcium to cardiac myocyte recovery after exposure to anoxia. Circ Res 71: 605-613, 1992
    • (1992) Circ Res , vol.71 , pp. 605-613
    • Miyata, H.1    Lakatta, E.G.2    Stern, M.D.3    Silverman, H.S.4
  • 133
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 417: 1-13, 2009
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 134
    • 33745270756 scopus 로고    scopus 로고
    • Contribution of peroxidized cardiolipin to inactivation of bovine heart cytochrome c oxidase
    • Musatov A. Contribution of peroxidized cardiolipin to inactivation of bovine heart cytochrome c oxidase. Free Radic Biol Med 41: 238-246, 2006
    • (2006) Free Radic Biol Med , vol.41 , pp. 238-246
    • Musatov, A.1
  • 136
    • 0026705820 scopus 로고
    • The activity of pyruvate carrier in a reconstituted system: Substrate specificity and inhibitor sensitivity
    • Na1ecz KA, Kamiń ska J, Na1ecz MJ, and Azzi A. The activity of pyruvate carrier in a reconstituted system: Substrate specificity and inhibitor sensitivity. Arch Biochem Biophys 297: 162-168, 1992
    • (1992) Arch Biochem Biophys , vol.297 , pp. 162-168
    • Nalecz, K.A.1    Kamińska, J.2    Naiecz, M.J.3    Azzi, A.4
  • 137
    • 33847059997 scopus 로고    scopus 로고
    • The mitochondrial energy transduction system and the aging process
    • Navarro A and Boveris A. The mitochondrial energy transduction system and the aging process. Am J Physiol Cell Physiol 292: C670-C686, 2007
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Navarro, A.1    Boveris, A.2
  • 138
    • 0022461266 scopus 로고
    • An essential requirement of cardiolipin for mitochondrial carnitine acylcarnitine translocase activity. Lipid requirement of carnitine acylcarnitine translocase
    • Noél H and Pande SV. An essential requirement of cardiolipin for mitochondrial carnitine acylcarnitine translocase activity. Lipid requirement of carnitine acylcarnitine translocase. Eur J Biochem 155: 99-102, 1986
    • (1986) Eur J Biochem , vol.155 , pp. 99-102
    • Noél, H.1    Pande, S.V.2
  • 139
    • 0026436685 scopus 로고
    • Ubisemiquinones of the mitochondrial respiratory chain do not interact with molecular oxygen
    • Nohl H and Stolze K. Ubisemiquinones of the mitochondrial respiratory chain do not interact with molecular oxygen. Free Radic Res Commun 16: 409-419, 1992
    • (1992) Free Radic Res Commun , vol.16 , pp. 409-419
    • Nohl, H.1    Stolze, K.2
  • 140
    • 0025679160 scopus 로고
    • Effect of ADP/ATP antiporter conformational state on the suppression of the nonspecific permeability of the inner mitochondrial membrane by cyclosporine A
    • Novgorodov SA, Gudz TI, Kushnareva YE, Zorov DB, and Kudrjashov YB. Effect of ADP/ATP antiporter conformational state on the suppression of the nonspecific permeability of the inner mitochondrial membrane by cyclosporine A. FEBS Lett 277: 123-126, 1990
    • (1990) FEBS Lett , vol.277 , pp. 123-126
    • Novgorodov, S.A.1    Gudz, T.I.2    Kushnareva, Y.E.3    Zorov, D.B.4    Kudrjashov, Y.B.5
  • 144
    • 0026517889 scopus 로고
    • Effects of adrenoceptor blockade on cardiac hypertrophy and myocardial phospholipids
    • O'Rourke B and Reibel DK. Effects of adrenoceptor blockade on cardiac hypertrophy and myocardial phospholipids. Proc Soc Exp Biol Med 200: 95-100, 1992
    • (1992) Proc Soc Exp Biol Med , vol.200 , pp. 95-100
    • O'Rourke, B.1    Reibel, D.K.2
  • 146
    • 61449229779 scopus 로고    scopus 로고
    • The genetic interactome of prohibitins: Coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria
    • Osman C, Haag M, Potting C, Rodenfels J, Dip PV, Wieland FT, Brügger B, Westermann B, and Langer T. The genetic interactome of prohibitins: Coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J Cell Biol 184: 583-596, 2009
    • (2009) J Cell Biol , vol.184 , pp. 583-596
    • Osman, C.1    Haag, M.2    Potting, C.3    Rodenfels, J.4    Dip, P.V.5    Wieland, F.T.6    Brügger, B.7    Westermann, B.8    Langer, T.9
  • 147
    • 77953614272 scopus 로고    scopus 로고
    • A mitochondrial phosphatase required for cardiolipin biosyn thesis: The PGP phosphatase Gep4
    • Osman C, Haag M, Wieland FT, Brügger B, and Langer T. A mitochondrial phosphatase required for cardiolipin biosynthesis: The PGP phosphatase Gep4. EMBO J 29: 1976-1987, 2010
    • (2010) EMBO J , vol.29 , pp. 1976-1987
    • Osman, C.1    Haag, M.2    Wieland, F.T.3    Brügger, B.4    Langer, T.5
  • 148
    • 0345600249 scopus 로고    scopus 로고
    • The division of endosymbiotic organelles
    • Osteryoung KW and Nunnari J. The division of endosymbiotic organelles. Science 302: 1698-1704, 2003
    • (2003) Science , vol.302 , pp. 1698-1704
    • Osteryoung, K.W.1    Nunnari, J.2
  • 150
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): Physiological and pathological implications
    • Palmieri F. The mitochondrial transporter family (SLC25): Physiological and pathological implications. Pflugers Arch 447: 689-709, 2004
    • (2004) Pflugers Arch , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 151
    • 84872841535 scopus 로고    scopus 로고
    • Changes in the mitochondrial permeability transition pore in aging and age-Associated diseases
    • Paradies G, Paradies V, Ruggiero FM, and Petrosillo G. Changes in the mitochondrial permeability transition pore in aging and age-Associated diseases. Mech Ageing Dev 134: 1-9, 2013
    • (2013) Mech Ageing Dev , vol.134 , pp. 1-9
    • Paradies, G.1    Paradies, V.2    Ruggiero, F.M.3    Petrosillo, G.4
  • 152
    • 79952101282 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in brain aging: Role of oxidative stress and cardiolipin
    • Paradies G, Petrosillo G, Paradies V, and Ruggiero FM. Mitochondrial dysfunction in brain aging: Role of oxidative stress and cardiolipin. Neurochem Int 58: 447-457, 2011
    • (2011) Neurochem Int , vol.58 , pp. 447-457
    • Paradies, G.1    Petrosillo, G.2    Paradies, V.3    Ruggiero, F.M.4
  • 153
    • 77951937320 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial bioenergetics, and cardiolipin in aging
    • Paradies G, Petrosillo G, Paradies V, and Ruggiero FM. Oxidative stress, mitochondrial bioenergetics, and cardiolipin in aging. Free Radic Biol Med 48: 1286-1295, 2010
    • (2010) Free Radic Biol Med , vol.48 , pp. 1286-1295
    • Paradies, G.1    Petrosillo, G.2    Paradies, V.3    Ruggiero, F.M.4
  • 154
    • 67349131607 scopus 로고    scopus 로고
    • Role of cardiolipin peroxidation and Ca2 + in mitochondrial dysfunction and disease
    • Paradies G, Petrosillo G, Paradies V, and Ruggiero FM. Role of cardiolipin peroxidation and Ca2 + in mitochondrial dysfunction and disease. Cell Calcium 45: 643-650, 2009
    • (2009) Cell Calcium , vol.45 , pp. 643-650
    • Paradies, G.1    Petrosillo, G.2    Paradies, V.3    Ruggiero, F.M.4
  • 155
    • 0346059551 scopus 로고    scopus 로고
    • Decrease in mitochondrial complex I activity in ischemic/reperfused rat heart: Involvement of reactive oxygen species and cardiolipin
    • Paradies G, Petrosillo G, Pistolese M, Di Venosa N, Federici A, and Ruggiero FM. Decrease in mitochondrial complex I activity in ischemic/reperfused rat heart: Involvement of reactive oxygen species and cardiolipin. Circ Res 94: 53-59, 2004
    • (2004) Circ Res , vol.94 , pp. 53-59
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Federici, A.5    Ruggiero, F.M.6
  • 156
    • 0032775546 scopus 로고    scopus 로고
    • Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion
    • Paradies G, Petrosillo G, Pistolese M, Di Venosa N, Serena D, and Ruggiero FM. Lipid peroxidation and alterations to oxidative metabolism in mitochondria isolated from rat heart subjected to ischemia and reperfusion. Free Radic Biol Med 27: 42-50, 1999
    • (1999) Free Radic Biol Med , vol.27 , pp. 42-50
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Serena, D.5    Ruggiero, F.M.6
  • 157
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage
    • Paradies G, Petrosillo G, Pistolese M, and Ruggiero FM. Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage. Gene 286: 135-141, 2002
    • (2002) Gene , vol.286 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 158
    • 0008724863 scopus 로고    scopus 로고
    • Reactive oxygen species generated by the mitochondrial respiratory chain affect the complex III activity via cardiolipin peroxidation in beef-heart submitochondrial particles
    • Paradies G, Petrosillo G, Pistolese M, and Ruggiero FM. Reactive oxygen species generated by the mitochondrial respiratory chain affect the complex III activity via cardiolipin peroxidation in beef-heart submitochondrial particles. Mitochondrion 1: 151-159, 2001
    • (2001) Mitochondrion , vol.1 , pp. 151-159
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 159
    • 0033984710 scopus 로고    scopus 로고
    • The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles
    • Paradies G, Petrosillo G, Pistolese M, and Ruggiero FM. The effect of reactive oxygen species generated from the mitochondrial electron transport chain on the cytochrome c oxidase activity and on the cardiolipin content in bovine heart submitochondrial particles. FEBS Lett 466: 323-326, 2000
    • (2000) FEBS Lett , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 160
    • 0030929650 scopus 로고    scopus 로고
    • Cardiolipindependent decrease of cytochrome c oxidase activity in heart mitochondria from hypothyroid rats
    • Paradies G, Petrosillo G, and Ruggiero FM. Cardiolipindependent decrease of cytochrome c oxidase activity in heart mitochondria from hypothyroid rats. Biochim Biophys Acta 1319: 5-8, 1997
    • (1997) Biochim Biophys Acta , vol.1319 , pp. 5-8
    • Paradies, G.1    Petrosillo, G.2    Ruggiero, F.M.3
  • 161
    • 0027489678 scopus 로고
    • Decreased cytochrome oxidase activity and changes in phospholipids in heart mitochondria from hypothyroid rats
    • Paradies G, Ruggiero FM, Dinoi P, Petrosillo G, and Quagliariello E. Decreased cytochrome oxidase activity and changes in phospholipids in heart mitochondria from hypothyroid rats. Arch Biochem Biophys 307: 91-95, 1993
    • (1993) Arch Biochem Biophys , vol.307 , pp. 91-95
    • Paradies, G.1    Ruggiero, F.M.2    Dinoi, P.3    Petrosillo, G.4    Quagliariello, E.5
  • 162
    • 0026068262 scopus 로고
    • The influence of hypothyroidism on the transport of phosphate and on the lipid composition in rat-liver mitochondria
    • Paradies G, Ruggiero FM, and Dinoi P. The influence of hypothyroidism on the transport of phosphate and on the lipid composition in rat-liver mitochondria. Biochim Biophys Acta 1070: 180-186, 1991
    • (1991) Biochim Biophys Acta , vol.1070 , pp. 180-186
    • Paradies, G.1    Ruggiero, F.M.2    Dinoi, P.3
  • 163
    • 0031593137 scopus 로고    scopus 로고
    • Alterations in carnitine-Acylcarnitine translocase activity and in phospholipid composition in heart mitochondria from hypothyroid rats
    • Paradies G, Ruggiero FM, Petrosillo G, and Quagliariello E. Alterations in carnitine-Acylcarnitine translocase activity and in phospholipid composition in heart mitochondria from hypothyroid rats. Biochim Biophys Acta 1362: 193-200, 1997
    • (1997) Biochim Biophys Acta , vol.1362 , pp. 193-200
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 164
    • 0027979906 scopus 로고
    • Enhanced cytochrome oxidase activity and modification of lipids in heart mitochondria from hyperthyroid rats
    • Paradies G, Ruggiero FM, Petrosillo G, and Quagliariello E. Enhanced cytochrome oxidase activity and modification of lipids in heart mitochondria from hyperthyroid rats. Biochim Biophys Acta 1225: 165-170, 1994
    • (1994) Biochim Biophys Acta , vol.1225 , pp. 165-170
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 165
    • 0030592774 scopus 로고    scopus 로고
    • Stimulation of carnitine acylcarnitine translocase activity in heart mitochondria from hyperthyroid rats
    • Paradies G, Ruggiero FM, Petrosillo G, and Quagliariello E. Stimulation of carnitine acylcarnitine translocase activity in heart mitochondria from hyperthyroid rats. FEBS Lett 397: 260-262, 1996
    • (1996) FEBS Lett , vol.397 , pp. 260-262
    • Paradies, G.1    Ruggiero, F.M.2    Petrosillo, G.3    Quagliariello, E.4
  • 166
    • 0025260953 scopus 로고
    • Enhanced activity of the tricarboxylate carrier and modification of lipids in hepatic mitochondria from hyperthyroid rats
    • Paradies G and Ruggiero FM. Enhanced activity of the tricarboxylate carrier and modification of lipids in hepatic mitochondria from hyperthyroid rats. Arch Biochem Biophys 278: 425-430, 1990
    • (1990) Arch Biochem Biophys , vol.278 , pp. 425-430
    • Paradies, G.1    Ruggiero, F.M.2
  • 167
    • 0025072728 scopus 로고
    • Stimulation of phosphate transport in rat-liver mitochondria by thyroid hormones
    • Paradies G and Ruggiero FM. Stimulation of phosphate transport in rat-liver mitochondria by thyroid hormones. Biochim Biophys Acta 1019: 133-136, 1990
    • (1990) Biochim Biophys Acta , vol.1019 , pp. 133-136
    • Paradies, G.1    Ruggiero, F.M.2
  • 169
    • 18844389970 scopus 로고    scopus 로고
    • NASH a mitochondrial disease
    • Pessayre D and Fromenty B NASH: A mitochondrial disease. J Hepatol 42: 928-940, 2005
    • (2005) J Hepatol , vol.42 , pp. 928-940
    • Pessayre, D.1    Fromenty, B.2
  • 170
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter ME and Krammer PH. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ 10: 26-35, 2003
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 171
    • 33750979541 scopus 로고    scopus 로고
    • Interaction of peroxidized cardiolipin with ratheart mitochondrial membranes: Induction of permeability transition and cytochrome c release
    • Petrosillo G, Casanova G, Matera M, Ruggiero FM, and Paradies G. Interaction of peroxidized cardiolipin with ratheart mitochondrial membranes: Induction of permeability transition and cytochrome c release. FEBS Lett 580: 6311-6316, 2006
    • (2006) FEBS Lett , vol.580 , pp. 6311-6316
    • Petrosillo, G.1    Casanova, G.2    Matera, M.3    Ruggiero, F.M.4    Paradies, G.5
  • 174
    • 52049089147 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in rat brain with aging Involvement of complex I, reactive oxygen species and cardiolipin
    • Petrosillo G, Matera M, Casanova G, Ruggiero FM, and Paradies G. Mitochondrial dysfunction in rat brain with aging Involvement of complex I, reactive oxygen species and cardiolipin. Neurochem Int 53: 126-131, 2008
    • (2008) Neurochem Int , vol.53 , pp. 126-131
    • Petrosillo, G.1    Matera, M.2    Casanova, G.3    Ruggiero, F.M.4    Paradies, G.5
  • 175
    • 57449084690 scopus 로고    scopus 로고
    • Mitochondrial complex I dysfunction in rat heart with aging: Critical role of reactive oxygen species and cardiolipin
    • Petrosillo G, Matera M, Moro N, Ruggiero FM, and Paradies G. Mitochondrial complex I dysfunction in rat heart with aging: Critical role of reactive oxygen species and cardiolipin. Free Radic Biol Med 46: 88-94, 2009
    • (2009) Free Radic Biol Med , vol.46 , pp. 88-94
    • Petrosillo, G.1    Matera, M.2    Moro, N.3    Ruggiero, F.M.4    Paradies, G.5
  • 176
    • 77950670564 scopus 로고    scopus 로고
    • Increased susceptibility to Ca(2 +)-induced permeability transition and to cytochrome c release in rat heart mitochondria with aging: Effect of melatonin
    • Petrosillo G, Moro N, Paradies V, Ruggiero FM, and Paradies G. Increased susceptibility to Ca(2 +)-induced permeability transition and to cytochrome c release in rat heart mitochondria with aging: Effect of melatonin. J Pineal Res 48: 340-346, 2010
    • (2010) J Pineal Res , vol.48 , pp. 340-346
    • Petrosillo, G.1    Moro, N.2    Paradies, V.3    Ruggiero, F.M.4    Paradies, G.5
  • 177
    • 69249217642 scopus 로고    scopus 로고
    • Melatonin inhibits cardiolipin peroxidation in mitochondria and prevents the mitochondrial permeability transition and cytochrome c release
    • Petrosillo G, Moro N, Ruggiero FM, and Paradies G. Melatonin inhibits cardiolipin peroxidation in mitochondria and prevents the mitochondrial permeability transition and cytochrome c release. Free Radic Biol Med 47: 969-974, 2009
    • (2009) Free Radic Biol Med , vol.47 , pp. 969-974
    • Petrosillo, G.1    Moro, N.2    Ruggiero, F.M.3    Paradies, G.4
  • 179
    • 0037387920 scopus 로고    scopus 로고
    • Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: Role of reactive oxygen species and cardiolipin
    • Petrosillo G, Ruggiero FM, Di Venosa N, and Paradies G. Decreased complex III activity in mitochondria isolated from rat heart subjected to ischemia and reperfusion: Role of reactive oxygen species and cardiolipin. FASEB J 17: 714-716, 2003
    • (2003) FASEB J , vol.17 , pp. 714-716
    • Petrosillo, G.1    Ruggiero, F.M.2    Di Venosa, N.3    Paradies, G.4
  • 180
    • 0035861885 scopus 로고    scopus 로고
    • Reactive oxygen species generated from the mitochondrial electron transport chain induce cytochrome c dissociation from beef-heart submitochondrial particles via cardiolipin peroxidation. Possible role in the apoptosis
    • Petrosillo G, Ruggiero FM, Pistolese M, and Paradies G. Reactive oxygen species generated from the mitochondrial electron transport chain induce cytochrome c dissociation from beef-heart submitochondrial particles via cardiolipin peroxidation. Possible role in the apoptosis. FEBS Lett 509: 435-438, 2001
    • (2001) FEBS Lett , vol.509 , pp. 435-438
    • Petrosillo, G.1    Ruggiero, F.M.2    Pistolese, M.3    Paradies, G.4
  • 182
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: Activation, specificity, and regulation
    • Pop C and Salvesen GS. Human caspases: Activation, specificity, and regulation. J Biol Chem 284: 21777-21781, 2009
    • (2009) J Biol Chem , vol.284 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 183
    • 79960279832 scopus 로고    scopus 로고
    • A-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding
    • Pranke IM, Morello V, Bigay J, Gibson K, Verbavatz JM, Antonny B, and Jackson CL. a-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding. J Cell Biol 194: 89-103, 2011
    • (2011) J Cell Biol , vol.194 , pp. 89-103
    • Pranke, I.M.1    Morello, V.2    Bigay, J.3    Gibson, K.4    Verbavatz, J.M.5    Antonny, B.6    Jackson, C.L.7
  • 184
    • 84863683962 scopus 로고    scopus 로고
    • Asynuclein and mitochondrial dysfunction: A pathogenic partnership in Parkinson's diseasé
    • Protter D, Lang C, and Cooper AA. aSynuclein and mitochondrial dysfunction: A pathogenic partnership in Parkinson's diseaséParkinsons Dis 2012: 829207, 2012
    • (2012) Parkinsons Dis , vol.2012 , pp. 829207
    • Protter, D.1    Lang, C.2    Cooper, A.A.3
  • 185
    • 0016734199 scopus 로고
    • Purification of the carboxy-Atractylate binding protein from mitochondria
    • Riccio P, Aquila H, and Klingenberg M. Purification of the carboxy-Atractylate binding protein from mitochondria. FEBS Lett 56: 133-138, 1975
    • (1975) FEBS Lett , vol.56 , pp. 133-138
    • Riccio, P.1    Aquila, H.2    Klingenberg, M.3
  • 186
    • 0027252494 scopus 로고
    • Functional binding of cardiolipin to cytochrome c oxidase
    • Robinson NC. Functional binding of cardiolipin to cytochrome c oxidase. J Bioenerg Biomembr 25: 153-163, 1993
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 153-163
    • Robinson, N.C.1
  • 189
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger H and Pfeiffer K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19: 1777-1783, 2000
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 190
    • 0037056045 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes of mitochondria and bacteria
    • Schägger H. Respiratory chain supercomplexes of mitochondria and bacteria. Biochim Biophys Acta 1555: 154-159, 2002
    • (2002) Biochim Biophys Acta , vol.1555 , pp. 154-159
    • Schägger, H.1
  • 192
    • 0027497625 scopus 로고
    • Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria
    • Schlame M and Haldar D. Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria. J Biol Chem 268: 74-79, 1993
    • (1993) J Biol Chem , vol.268 , pp. 74-79
    • Schlame, M.1    Haldar, D.2
  • 193
    • 0031552931 scopus 로고    scopus 로고
    • Cardiolipin synthase from mammalian mitochondria
    • Schlame M and Hostetler KY. Cardiolipin synthase from mammalian mitochondria. Biochim Biophys Acta 1348: 207-213, 1997
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 207-213
    • Schlame, M.1    Hostetler, K.Y.2
  • 194
    • 0025838755 scopus 로고
    • Solubilization, purification, and characterization of cardiolipin synthase from rat liver mitochondria. Demonstration of its phospholipid requirement
    • Schlame M and Hostetler KY. Solubilization, purification, and characterization of cardiolipin synthase from rat liver mitochondria. Demonstration of its phospholipid requirement. J Biol Chem 266: 22398-22403, 1991
    • (1991) J Biol Chem , vol.266 , pp. 22398-22403
    • Schlame, M.1    Hostetler, K.Y.2
  • 195
    • 33749061065 scopus 로고    scopus 로고
    • Barth syndrome, a human disorder of cardiolipin metabolism
    • Schlame M and Ren M. Barth syndrome, a human disorder of cardiolipin metabolism. FEBS Lett 580: 5450-5455, 2006
    • (2006) FEBS Lett , vol.580 , pp. 5450-5455
    • Schlame, M.1    Ren, M.2
  • 196
    • 70349558836 scopus 로고    scopus 로고
    • The role of cardiolipin in the structural organization of mitochondrial membranes
    • Schlame M and Ren M. The role of cardiolipin in the structural organization of mitochondrial membranes. Biochim Biophys Acta 1788: 2080-2083, 2009
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2080-2083
    • Schlame, M.1    Ren, M.2
  • 197
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M, Rua D, and Greenberg ML. The biosynthesis and functional role of cardiolipin. Prog Lipid Res 39: 257-288, 2000
    • (2000) Prog Lipid Res , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 199
    • 0029153947 scopus 로고
    • Kinetic analysis of cardiolipin synthase: A membrane enzyme with two glycerophospholipid substrates
    • Schlame M, Zhao M, Rua D, Haldar D, and Greenberg ML. Kinetic analysis of cardiolipin synthase: A membrane enzyme with two glycerophospholipid substrates. Lipids 30: 633-640, 1995
    • (1995) Lipids , vol.30 , pp. 633-640
    • Schlame, M.1    Zhao, M.2    Rua, D.3    Haldar, D.4    Greenberg, M.L.5
  • 200
    • 84873167935 scopus 로고    scopus 로고
    • Cardiolipin remodeling and the function of tafazzin
    • Schlame M. Cardiolipin remodeling and the function of tafazzin. Biochim Biophys Acta 1831: 582-588, 2013
    • (2013) Biochim Biophys Acta , vol.1831 , pp. 582-588
    • Schlame, M.1
  • 201
    • 51449112852 scopus 로고    scopus 로고
    • Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes
    • Schlame M. Cardiolipin synthesis for the assembly of bacterial and mitochondrial membranes. J Lipid Res 49: 1607-1620, 2008
    • (2008) J Lipid Res , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 203
    • 0034625438 scopus 로고    scopus 로고
    • Octamers of mitochondrial creatine kinase isoenzymes differ in stability and membrane binding
    • Schlattner U and Wallimann T. Octamers of mitochondrial creatine kinase isoenzymes differ in stability and membrane binding. J Biol Chem 275: 17314-17320, 2000
    • (2000) J Biol Chem , vol.275 , pp. 17314-17320
    • Schlattner, U.1    Wallimann, T.2
  • 204
    • 77956090193 scopus 로고    scopus 로고
    • Mitochondrial protein import: From proteomics to functional mechanisms
    • Schmidt O, Pfanner N, and Meisinger C. Mitochondrial protein import: From proteomics to functional mechanisms. Nat Rev Mol Cell Biol 11: 655-667, 2010
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 655-667
    • Schmidt, O.1    Pfanner, N.2    Meisinger, C.3
  • 205
    • 70349524664 scopus 로고    scopus 로고
    • Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
    • Schug ZT and Gottlieb E. Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis. Biochim Biophys Acta 1788: 2022-2031, 2009
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2022-2031
    • Schug, Z.T.1    Gottlieb, E.2
  • 206
    • 84862242000 scopus 로고    scopus 로고
    • The stability and activity of respiratory Complex II is cardiolipindependent
    • Schwall CT, Greenwood VL, and Alder NN. The stability and activity of respiratory Complex II is cardiolipindependent. Biochim Biophys Acta 1817: 1588-1596, 2012
    • (2012) Biochim Biophys Acta , vol.1817 , pp. 1588-1596
    • Schwall, C.T.1    Greenwood, V.L.2    Alder, N.N.3
  • 208
    • 0033539647 scopus 로고    scopus 로고
    • Phospholipase A(2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure
    • Sedlák E and Robinson NC. Phospholipase A(2) digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure. Biochemistry 38: 14966-14972, 1999
    • (1999) Biochemistry , vol.38 , pp. 14966-14972
    • Sedlák, E.1    Robinson, N.C.2
  • 209
    • 30144445462 scopus 로고    scopus 로고
    • Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria
    • Sharpley MS, Shannon RJ, Draghi F, and Hirst J. Interactions between phospholipids and NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria. Biochemistry 45: 241-248, 2006
    • (2006) Biochemistry , vol.45 , pp. 241-248
    • Sharpley, M.S.1    Shannon, R.J.2    Draghi, F.3    Hirst, J.4
  • 212
    • 0032570577 scopus 로고    scopus 로고
    • Cytochrome c in the apoptotic and antioxidant cascades
    • Skulachev VP. Cytochrome c in the apoptotic and antioxidant cascades. FEBS Lett 423: 275-280, 1998
    • (1998) FEBS Lett , vol.423 , pp. 275-280
    • Skulachev, V.P.1
  • 213
    • 34548313688 scopus 로고    scopus 로고
    • OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L
    • Song Z, Chen H, Fiket M, Alexander C, and Chan DC. OPA1 processing controls mitochondrial fusion and is regulated by mRNA splicing, membrane potential, and Yme1L. J Cell Biol 178: 749-755, 2007
    • (2007) J Cell Biol , vol.178 , pp. 749-755
    • Song, Z.1    Chen, H.2    Fiket, M.3    Alexander, C.4    Chan, D.C.5
  • 215
    • 24944544909 scopus 로고    scopus 로고
    • Quantitation of cardiolipin molecular species in spontaneously hypertensive heart failure rats using electrospray ionization mass spectrometry
    • Sparagna GC, Johnson CA, McCune SA, Moore RL, and Murphy RC. Quantitation of cardiolipin molecular species in spontaneously hypertensive heart failure rats using electrospray ionization mass spectrometry. J Lipid Res 46: 1196-1204, 2005
    • (2005) J Lipid Res , vol.46 , pp. 1196-1204
    • Sparagna, G.C.1    Johnson, C.A.2    McCune, S.A.3    Moore, R.L.4    Murphy, R.C.5
  • 216
    • 65349123514 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function
    • Stowe DF and Camara AK. Mitochondrial reactive oxygen species production in excitable cells: Modulators of mitochondrial and cell function. Antioxid Redox Signal 11: 1373-1414, 2009
    • (2009) Antioxid Redox Signal , vol.11 , pp. 1373-1414
    • Stowe, D.F.1    Camara, A.K.2
  • 217
    • 0027234336 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore
    • Szabó I and Zoratti M. The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore. FEBS Lett 330: 201-205, 1993
    • (1993) FEBS Lett , vol.330 , pp. 201-205
    • Szabó, I.1    Zoratti, M.2
  • 218
    • 0038644881 scopus 로고    scopus 로고
    • Purification and characterization of monolysocardiolipin acyltransferase from pig liver mitochondria
    • Taylor WA and Hatch GM. Purification and characterization of monolysocardiolipin acyltransferase from pig liver mitochondria. J Biol Chem 278: 12716-12721, 2003
    • (2003) J Biol Chem , vol.278 , pp. 12716-12721
    • Taylor, W.A.1    Hatch, G.M.2
  • 220
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: Evidence for the extended lipid anchorage
    • Tuominen EK, Wallace CJ, and Kinnunen PK. Phospholipid-cytochrome c interaction: Evidence for the extended lipid anchorage. J Biol Chem 277: 8822-8826, 2002
    • (2002) J Biol Chem , vol.277 , pp. 8822-8826
    • Tuominen, E.K.1    Wallace, C.J.2    Kinnunen, P.K.3
  • 222
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, and Lehninger AL. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys 237: 408-414, 1985
    • (1985) Arch Biochem Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 224
    • 0036182137 scopus 로고    scopus 로고
    • Lipotoxic diseases
    • Unger RH. Lipotoxic diseases. Annu Rev Med 53: 319-336, 2002
    • (2002) Annu Rev Med , vol.53 , pp. 319-336
    • Unger, R.H.1
  • 226
    • 0032541173 scopus 로고    scopus 로고
    • Reactive oxygen species released from mitochondria during brief hypoxia induce preconditioning in cardiomyocytes
    • Vanden Hoek TL, Becker LB, Shao Z, Li C, and Schumacker PT. Reactive oxygen species released from mitochondria during brief hypoxia induce preconditioning in cardiomyocytes. J Biol Chem 273: 18092-18098, 1998
    • (1998) J Biol Chem , vol.273 , pp. 18092-18098
    • Vanden Hoek, T.L.1    Becker, L.B.2    Shao, Z.3    Li, C.4    Schumacker, P.T.5
  • 227
    • 0031239737 scopus 로고    scopus 로고
    • Significant levels of oxidants are generated by isolated cardiomyocytes during ischemia prior to reperfusion
    • Vanden Hoek TL, Li C, Shao Z, Schumacker PT, and Becker LB. Significant levels of oxidants are generated by isolated cardiomyocytes during ischemia prior to reperfusion. J Mol Cell Cardiol 29: 2571-2583, 1997
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 2571-2583
    • Vanden Hoek, T.L.1    Li, C.2    Shao, Z.3    Schumacker, P.T.4    Becker, L.B.5
  • 229
    • 0027104114 scopus 로고
    • The NADH: Ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker JE. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q Rev Biophys 25: 253-324, 1992
    • (1992) Q Rev Biophys , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 231
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss H, Friedrich T, Hofhaus G, and Preis D. The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur J Biochem 197: 563-576, 1991
    • (1991) Eur J Biochem , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 232
    • 33748986546 scopus 로고    scopus 로고
    • Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation
    • Wittig I, Carrozzo R, Santorelli FM, and Schägger H. Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation. Biochim Biophys Acta 1757: 1066-1072, 2006
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 1066-1072
    • Wittig, I.1    Carrozzo, R.2    Santorelli, F.M.3    Schägger, H.4
  • 234
    • 33845983684 scopus 로고    scopus 로고
    • The enzymatic function of tafazzin
    • Xu Y, Malhotra A, Ren M, and Schlame M. The enzymatic function of tafazzin. J Biol Chem 281: 39217-39224, 2006
    • (2006) J Biol Chem , vol.281 , pp. 39217-39224
    • Xu, Y.1    Malhotra, A.2    Ren, M.3    Schlame, M.4
  • 235
    • 0032573066 scopus 로고    scopus 로고
    • Mitochondrial adenine nucleotide translocase is modified oxidatively during aging
    • Yan LJ and Sohal RS. Mitochondrial adenine nucleotide translocase is modified oxidatively during aging. Proc Natl Acad Sci U S A 95: 12896-12901, 1998
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12896-12901
    • Yan, L.J.1    Sohal, R.S.2
  • 236
    • 84863960346 scopus 로고    scopus 로고
    • Free radical oxidation of cardiolipin: Chemical mechanisms, detection and implication in apoptosis, mitochondrial dysfunction and human diseases
    • Yin H and Zhu M. Free radical oxidation of cardiolipin: Chemical mechanisms, detection and implication in apoptosis, mitochondrial dysfunction and human diseases. Free Radic Res 46: 959-974, 2012
    • (2012) Free Radic Res , vol.46 , pp. 959-974
    • Yin, H.1    Zhu, M.2
  • 238
    • 0016668191 scopus 로고
    • Lipid composition of the Golgi apparatus of rat kidney and liver in comparison with other subcellular organelles
    • Zambrano F, Fleischer S, and Fleischer B. Lipid composition of the Golgi apparatus of rat kidney and liver in comparison with other subcellular organelles. Biochim Biophys Acta 380: 357-369, 1975
    • (1975) Biochim Biophys Acta , vol.380 , pp. 357-369
    • Zambrano, F.1    Fleischer, S.2    Fleischer, B.3
  • 239
    • 23844540312 scopus 로고    scopus 로고
    • Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria
    • Zhang M, Mileykovskaya E, and Dowhan W. Cardiolipin is essential for organization of complexes III and IV into a supercomplex in intact yeast mitochondria. J Biol Chem 280: 29403-29408, 2005
    • (2005) J Biol Chem , vol.280 , pp. 29403-29408
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 240
    • 0037113864 scopus 로고    scopus 로고
    • Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane
    • Zhang M, Mileykovskaya E, and Dowhan W. Gluing the respiratory chain together. Cardiolipin is required for supercomplex formation in the inner mitochondrial membrane. J Biol Chem 277: 43553-43556, 2002
    • (2002) J Biol Chem , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 241
    • 0031890382 scopus 로고    scopus 로고
    • Cardiolipin synthase is associated with a large complex in yeast mitochondria
    • Zhao M, Schlame M, Rua D, and Greenberg ML. Cardiolipin synthase is associated with a large complex in yeast mitochondria. J Biol Chem 273: 2402-2408, 1998
    • (1998) J Biol Chem , vol.273 , pp. 2402-2408
    • Zhao, M.1    Schlame, M.2    Rua, D.3    Greenberg, M.L.4
  • 242
    • 11144300815 scopus 로고    scopus 로고
    • Mitochondrial permeability transitions: How many doors to the housé
    • Zoratti M, Szabò I, and De Marchi U. Mitochondrial permeability transitions: How many doors to the houséBiochim Biophys Acta 1706: 40-52, 2005.
    • (2005) Biochim Biophys Acta , vol.1706 , pp. 40-52
    • Zoratti, M.1    Szabò, I.2    De Marchi, U.3


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