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Volumn 37, Issue 1, 2012, Pages 32-41

The complexity of cardiolipin in health and disease

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOLIPIN; MONOLYSOCARDIOLIPIN ACYLTRANSFERASE 1; PHOSPHATIDATE PHOSPHATASE; PHOSPHATIDYLGLYCEROLPHOSPHATE PHOSPHATASE; PHOSPHOLIPASE A2; UNCLASSIFIED DRUG;

EID: 84855581252     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2011.09.003     Document Type: Review
Times cited : (275)

References (79)
  • 1
    • 72449137691 scopus 로고    scopus 로고
    • Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome
    • Gebert N., et al. Mitochondrial cardiolipin involved in outer-membrane protein biogenesis: implications for Barth syndrome. Curr. Biol. 2009, 19:2133-2139.
    • (2009) Curr. Biol. , vol.19 , pp. 2133-2139
    • Gebert, N.1
  • 2
    • 56349087780 scopus 로고    scopus 로고
    • Cellular functions of cardiolipin in yeast
    • Joshi A.S., et al. Cellular functions of cardiolipin in yeast. Biochim. Biophys. Acta 2009, 1793:212-218.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 212-218
    • Joshi, A.S.1
  • 3
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C., et al. Making heads or tails of phospholipids in mitochondria. J. Cell Biol. 2011, 192:7-16.
    • (2011) J. Cell Biol. , vol.192 , pp. 7-16
    • Osman, C.1
  • 4
    • 70349558836 scopus 로고    scopus 로고
    • The role of cardiolipin in the structural organization of mitochondrial membranes
    • Schlame M., Ren M. The role of cardiolipin in the structural organization of mitochondrial membranes. Biochim. Biophys. Acta 2009, 1788:2080-2083.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2080-2083
    • Schlame, M.1    Ren, M.2
  • 6
    • 51649096941 scopus 로고    scopus 로고
    • Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane
    • Claypool S.M., et al. Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane. J. Cell Biol. 2008, 182:937-950.
    • (2008) J. Cell Biol. , vol.182 , pp. 937-950
    • Claypool, S.M.1
  • 7
    • 70349523247 scopus 로고    scopus 로고
    • Cardiolipin membrane domains in prokaryotes and eukaryotes
    • Mileykovskaya E., Dowhan W. Cardiolipin membrane domains in prokaryotes and eukaryotes. Biochim. Biophys. Acta 2009, 1788:2084-2091.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2084-2091
    • Mileykovskaya, E.1    Dowhan, W.2
  • 8
    • 70349557331 scopus 로고    scopus 로고
    • Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function
    • Claypool S.M. Cardiolipin, a critical determinant of mitochondrial carrier protein assembly and function. Biochim. Biophys. Acta 2009, 1788:2059-2068.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2059-2068
    • Claypool, S.M.1
  • 9
    • 33646748055 scopus 로고    scopus 로고
    • Identification and characterization of human cardiolipin synthase
    • Houtkooper R.H., et al. Identification and characterization of human cardiolipin synthase. FEBS Lett. 2006, 580:3059-3064.
    • (2006) FEBS Lett. , vol.580 , pp. 3059-3064
    • Houtkooper, R.H.1
  • 10
    • 70349520283 scopus 로고    scopus 로고
    • The enigmatic role of tafazzin in cardiolipin metabolism
    • Houtkooper R.H., et al. The enigmatic role of tafazzin in cardiolipin metabolism. Biochim. Biophys. Acta 2009, 1788:2003-2014.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2003-2014
    • Houtkooper, R.H.1
  • 11
    • 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. 2008, 49:1607-1620.
    • (2008) J. Lipid Res. , vol.49 , pp. 1607-1620
    • Schlame, M.1
  • 12
    • 33749061065 scopus 로고    scopus 로고
    • Barth syndrome, a human disorder of cardiolipin metabolism
    • Schlame M., Ren M. Barth syndrome, a human disorder of cardiolipin metabolism. FEBS Lett. 2006, 580:5450-5455.
    • (2006) FEBS Lett. , vol.580 , pp. 5450-5455
    • Schlame, M.1    Ren, M.2
  • 13
    • 27644533754 scopus 로고    scopus 로고
    • Molecular symmetry in mitochondrial cardiolipins
    • Schlame M., et al. Molecular symmetry in mitochondrial cardiolipins. Chem. Phys. Lipids 2005, 138:38-49.
    • (2005) Chem. Phys. Lipids , vol.138 , pp. 38-49
    • Schlame, M.1
  • 14
    • 44349165818 scopus 로고    scopus 로고
    • Shotgun lipidomics reveals the temporally dependent, highly diversified cardiolipin profile in the mammalian brain: temporally coordinated postnatal diversification of cardiolipin molecular species with neuronal remodeling
    • Cheng H., et al. Shotgun lipidomics reveals the temporally dependent, highly diversified cardiolipin profile in the mammalian brain: temporally coordinated postnatal diversification of cardiolipin molecular species with neuronal remodeling. Biochemistry 2008, 47:5869-5880.
    • (2008) Biochemistry , vol.47 , pp. 5869-5880
    • Cheng, H.1
  • 15
    • 77953614272 scopus 로고    scopus 로고
    • A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4
    • Osman C., et al. A mitochondrial phosphatase required for cardiolipin biosynthesis: the PGP phosphatase Gep4. EMBO J. 2010, 29:1976-1987.
    • (2010) EMBO J. , vol.29 , pp. 1976-1987
    • Osman, C.1
  • 16
    • 79958034094 scopus 로고    scopus 로고
    • Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis
    • Zhang J., et al. Mitochondrial phosphatase PTPMT1 is essential for cardiolipin biosynthesis. Cell Metab. 2011, 13:690-700.
    • (2011) Cell Metab. , vol.13 , pp. 690-700
    • Zhang, J.1
  • 17
    • 61449229779 scopus 로고    scopus 로고
    • The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria
    • Osman C., et al. The genetic interactome of prohibitins: coordinated control of cardiolipin and phosphatidylethanolamine by conserved regulators in mitochondria. J. Cell Biol. 2009, 184:583-596.
    • (2009) J. Cell Biol. , vol.184 , pp. 583-596
    • Osman, C.1
  • 18
    • 22544454482 scopus 로고    scopus 로고
    • Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells
    • Pagliarini D.J., et al. Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells. Mol. Cell 2005, 19:197-207.
    • (2005) Mol. Cell , vol.19 , pp. 197-207
    • Pagliarini, D.J.1
  • 19
    • 79961063234 scopus 로고    scopus 로고
    • Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis
    • Xiao J., et al. Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:11860-11865.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11860-11865
    • Xiao, J.1
  • 20
    • 0027497625 scopus 로고
    • Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria
    • Schlame M., Haldar D. Cardiolipin is synthesized on the matrix side of the inner membrane in rat liver mitochondria. J. Biol. Chem. 1993, 268:74-79.
    • (1993) J. Biol. Chem. , vol.268 , pp. 74-79
    • Schlame, M.1    Haldar, D.2
  • 21
    • 66449086494 scopus 로고    scopus 로고
    • Identification of a cardiolipin-specific phospholipase encoded by the gene CLD1 (YGR110W) in yeast
    • Beranek A., et al. Identification of a cardiolipin-specific phospholipase encoded by the gene CLD1 (YGR110W) in yeast. J. Biol. Chem. 2009, 284:11572-11578.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11572-11578
    • Beranek, A.1
  • 22
    • 61849141218 scopus 로고    scopus 로고
    • Cardiolipin and monolysocardiolipin analysis in fibroblasts, lymphocytes, and tissues using high-performance liquid chromatography-mass spectrometry as a diagnostic test for Barth syndrome
    • Houtkooper R.H., et al. Cardiolipin and monolysocardiolipin analysis in fibroblasts, lymphocytes, and tissues using high-performance liquid chromatography-mass spectrometry as a diagnostic test for Barth syndrome. Anal. Biochem. 2009, 387:230-237.
    • (2009) Anal. Biochem. , vol.387 , pp. 230-237
    • Houtkooper, R.H.1
  • 23
    • 60549086949 scopus 로고    scopus 로고
    • Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome
    • Malhotra A., et al. Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:2337-2341.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2337-2341
    • Malhotra, A.1
  • 24
    • 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 D.J., et al. 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. 2009, 284:35632-35644.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35632-35644
    • Mancuso, D.J.1
  • 25
    • 36849074624 scopus 로고    scopus 로고
    • Genetic ablation of calcium-independent phospholipase A2gamma leads to alterations in mitochondrial lipid metabolism and function resulting in a deficient mitochondrial bioenergetic phenotype
    • Mancuso D.J., et al. Genetic ablation of calcium-independent phospholipase A2gamma leads to alterations in mitochondrial lipid metabolism and function resulting in a deficient mitochondrial bioenergetic phenotype. J. Biol. Chem. 2007, 282:34611-34622.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34611-34622
    • Mancuso, D.J.1
  • 26
    • 78449252456 scopus 로고    scopus 로고
    • Genetic ablation of calcium-independent phospholipase A2gamma prevents obesity and insulin resistance during high fat feeding by mitochondrial uncoupling and increased adipocyte fatty acid oxidation
    • Mancuso D.J., et al. Genetic ablation of calcium-independent phospholipase A2gamma prevents obesity and insulin resistance during high fat feeding by mitochondrial uncoupling and increased adipocyte fatty acid oxidation. J. Biol. Chem. 2010, 285:36495-36510.
    • (2010) J. Biol. Chem. , vol.285 , pp. 36495-36510
    • Mancuso, D.J.1
  • 27
    • 33746606474 scopus 로고    scopus 로고
    • Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins
    • Claypool S.M., et al. Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins. J. Cell Biol. 2006, 174:379-390.
    • (2006) J. Cell Biol. , vol.174 , pp. 379-390
    • Claypool, S.M.1
  • 28
    • 33845983684 scopus 로고    scopus 로고
    • The enzymatic function of tafazzin
    • Xu Y., et al. The enzymatic function of tafazzin. J. Biol. Chem. 2006, 281:39217-39224.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39217-39224
    • Xu, Y.1
  • 29
    • 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., et al. 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 2009, 1791:314-320.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 314-320
    • Malhotra, A.1
  • 30
    • 62249192800 scopus 로고    scopus 로고
    • Formation of molecular species of mitochondrial cardiolipin. 2. A mathematical model of pattern formation by phospholipid transacylation
    • Schlame M. Formation of molecular species of mitochondrial cardiolipin. 2. A mathematical model of pattern formation by phospholipid transacylation. Biochim. Biophys. Acta 2009, 1791:321-325.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 321-325
    • Schlame, M.1
  • 31
    • 0242322008 scopus 로고    scopus 로고
    • Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism
    • Vaz F.M., et al. Only one splice variant of the human TAZ gene encodes a functional protein with a role in cardiolipin metabolism. J. Biol. Chem. 2003, 278:43089-43094.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43089-43094
    • Vaz, F.M.1
  • 32
    • 70349520221 scopus 로고    scopus 로고
    • Cardiolipin molecular species with shorter acyl chains accumulate in Saccharomyces cerevisiae mutants lacking the acyl coenzyme A-binding protein Acb1p: new insights into acyl chain remodeling of cardiolipin
    • Rijken P.J., et al. Cardiolipin molecular species with shorter acyl chains accumulate in Saccharomyces cerevisiae mutants lacking the acyl coenzyme A-binding protein Acb1p: new insights into acyl chain remodeling of cardiolipin. J. Biol. Chem. 2009, 284:27609-27619.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27609-27619
    • Rijken, P.J.1
  • 33
    • 0038644881 scopus 로고    scopus 로고
    • Purification and characterization of monolysocardiolipin acyltransferase from pig liver mitochondria
    • Taylor W.A., Hatch G.M. Purification and characterization of monolysocardiolipin acyltransferase from pig liver mitochondria. J. Biol. Chem. 2003, 278:12716-12721.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12716-12721
    • Taylor, W.A.1    Hatch, G.M.2
  • 34
    • 71049193103 scopus 로고    scopus 로고
    • Identification of the human mitochondrial linoleoyl-coenzyme A monolysocardiolipin acyltransferase (MLCL AT-1)
    • Taylor W.A., Hatch G.M. Identification of the human mitochondrial linoleoyl-coenzyme A monolysocardiolipin acyltransferase (MLCL AT-1). J. Biol. Chem. 2009, 284:30360-30371.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30360-30371
    • Taylor, W.A.1    Hatch, G.M.2
  • 35
    • 0026558042 scopus 로고
    • Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound β-oxidation enzyme of mitochondria
    • Carpenter K., et al. Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound β-oxidation enzyme of mitochondria. Biochem. Biophys. Res. Commun. 1992, 183:443-448.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 443-448
    • Carpenter, K.1
  • 36
    • 77957280386 scopus 로고    scopus 로고
    • Structural and functional characterization of the recombinant human mitochondrial trifunctional protein
    • Fould B., et al. Structural and functional characterization of the recombinant human mitochondrial trifunctional protein. Biochemistry 2010, 49:8608-8617.
    • (2010) Biochemistry , vol.49 , pp. 8608-8617
    • Fould, B.1
  • 37
    • 0028956322 scopus 로고
    • Two α subunit donor splice site mutations cause human trifunctional protein deficiency
    • Brackett J.C., et al. Two α subunit donor splice site mutations cause human trifunctional protein deficiency. J. Clin. Invest. 1995, 95:2076-2082.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2076-2082
    • Brackett, J.C.1
  • 38
    • 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., et al. A novel cardiolipin-remodeling pathway revealed by a gene encoding an endoplasmic reticulum-associated acyl-CoA:lysocardiolipin acyltransferase (ALCAT1) in mouse. J. Biol. Chem. 2004, 279:31727-31734.
    • (2004) J. Biol. Chem. , vol.279 , pp. 31727-31734
    • Cao, J.1
  • 39
    • 65649086419 scopus 로고    scopus 로고
    • ALCAT1 is a polyglycerophospholipid acyltransferase potently regulated by adenine nucleotide and thyroid status
    • Cao J., et al. ALCAT1 is a polyglycerophospholipid acyltransferase potently regulated by adenine nucleotide and thyroid status. Am. J. Physiol. Endocrinol. Metab. 2009, 296:E647-E653.
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.296
    • Cao, J.1
  • 40
    • 78049407128 scopus 로고    scopus 로고
    • Cardiolipin remodeling by ALCAT1 links oxidative stress and mitochondrial dysfunction to obesity
    • Li J., et al. Cardiolipin remodeling by ALCAT1 links oxidative stress and mitochondrial dysfunction to obesity. Cell Metab. 2010, 12:154-165.
    • (2010) Cell Metab. , vol.12 , pp. 154-165
    • Li, J.1
  • 41
    • 33846272138 scopus 로고    scopus 로고
    • Role of cardiolipin alterations in mitochondrial dysfunction and disease
    • Chicco A.J., Sparagna G.C. Role of cardiolipin alterations in mitochondrial dysfunction and disease. Am. J. Physiol. Cell Physiol. 2007, 292:C33-C44.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Chicco, A.J.1    Sparagna, G.C.2
  • 42
    • 67349137486 scopus 로고    scopus 로고
    • Enhanced modification of cardiolipin during ischemia in the aged heart
    • Lesnefsky E.J., et al. Enhanced modification of cardiolipin during ischemia in the aged heart. J. Mol. Cell. Cardiol. 2009, 46:1008-1015.
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 1008-1015
    • Lesnefsky, E.J.1
  • 43
    • 69449084720 scopus 로고    scopus 로고
    • Cardiolipin biosynthesis and remodeling enzymes are altered during development of heart failure
    • Saini-Chohan H.K., et al. Cardiolipin biosynthesis and remodeling enzymes are altered during development of heart failure. J. Lipid Res. 2009, 50:1600-1608.
    • (2009) J. Lipid Res. , vol.50 , pp. 1600-1608
    • Saini-Chohan, H.K.1
  • 44
    • 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., et al. Alterations in myocardial cardiolipin content and composition occur at the very earliest stages of diabetes: a shotgun lipidomics study. Biochemistry 2007, 46:6417-6428.
    • (2007) Biochemistry , vol.46 , pp. 6417-6428
    • Han, X.1
  • 45
    • 55349102294 scopus 로고    scopus 로고
    • Cardiolipin and electron transport chain abnormalities in mouse brain tumor mitochondria: lipidomic evidence supporting the Warburg theory of cancer
    • Kiebish M.A., et al. Cardiolipin and electron transport chain abnormalities in mouse brain tumor mitochondria: lipidomic evidence supporting the Warburg theory of cancer. J. Lipid Res. 2008, 49:2545-2556.
    • (2008) J. Lipid Res. , vol.49 , pp. 2545-2556
    • Kiebish, M.A.1
  • 46
    • 79960213739 scopus 로고    scopus 로고
    • Fragmentation of mitochondrial cardiolipin by copper ions in the Atp7b(-/-) mouse model of Wilson's disease
    • Yurkova I.L., et al. Fragmentation of mitochondrial cardiolipin by copper ions in the Atp7b(-/-) mouse model of Wilson's disease. Chem. Phys. Lipids 2011, 164:393-400.
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 393-400
    • Yurkova, I.L.1
  • 47
    • 24944563130 scopus 로고    scopus 로고
    • Monolysocardiolipins accumulate in Barth syndrome but do not lead to enhanced apoptosis
    • Valianpour F., et al. Monolysocardiolipins accumulate in Barth syndrome but do not lead to enhanced apoptosis. J. Lipid Res. 2005, 46:1182-1195.
    • (2005) J. Lipid Res. , vol.46 , pp. 1182-1195
    • Valianpour, F.1
  • 48
    • 70350350048 scopus 로고    scopus 로고
    • Characterization of tafazzin splice variants from humans and fruit flies
    • Xu Y., et al. Characterization of tafazzin splice variants from humans and fruit flies. J. Biol. Chem. 2009, 284:29230-29239.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29230-29239
    • Xu, Y.1
  • 49
    • 59449108212 scopus 로고    scopus 로고
    • The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome
    • Claypool S.M., et al. The cardiolipin transacylase, tafazzin, associates with two distinct respiratory components providing insight into Barth syndrome. Mol. Biol. Cell 2008, 19:5143-5155.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5143-5155
    • Claypool, S.M.1
  • 50
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients
    • McKenzie M., et al. Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients. J. Mol. Biol. 2006, 361:462-469.
    • (2006) J. Mol. Biol. , vol.361 , pp. 462-469
    • McKenzie, M.1
  • 51
    • 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., et al. Taz1, an outer mitochondrial membrane protein, affects stability and assembly of inner membrane protein complexes: implications for Barth syndrome. Mol. Biol. Cell 2005, 16:5202-5214.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5202-5214
    • Brandner, K.1
  • 52
    • 62549139167 scopus 로고    scopus 로고
    • Distinct effects of tafazzin deletion in differentiated and undifferentiated mitochondria
    • Acehan D., et al. Distinct effects of tafazzin deletion in differentiated and undifferentiated mitochondria. Mitochondrion 2009, 9:86-95.
    • (2009) Mitochondrion , vol.9 , pp. 86-95
    • Acehan, D.1
  • 53
    • 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
  • 54
    • 78651408755 scopus 로고    scopus 로고
    • Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome
    • Acehan D., et al. Cardiac and skeletal muscle defects in a mouse model of human Barth syndrome. J. Biol. Chem. 2011, 286:899-908.
    • (2011) J. Biol. Chem. , vol.286 , pp. 899-908
    • Acehan, D.1
  • 55
    • 33845752499 scopus 로고    scopus 로고
    • Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography
    • Acehan D., et al. Comparison of lymphoblast mitochondria from normal subjects and patients with Barth syndrome using electron microscopic tomography. Lab. Invest. 2007, 87:40-48.
    • (2007) Lab. Invest. , vol.87 , pp. 40-48
    • Acehan, D.1
  • 56
    • 79960343132 scopus 로고    scopus 로고
    • Characterization of a transgenic short hairpin RNA-induced murine model of tafazzin deficiency
    • Soustek M.S., et al. Characterization of a transgenic short hairpin RNA-induced murine model of tafazzin deficiency. Hum. Gene Ther. 2011, 22:865-871.
    • (2011) Hum. Gene Ther. , vol.22 , pp. 865-871
    • Soustek, M.S.1
  • 57
    • 33750312705 scopus 로고    scopus 로고
    • Membranes of the world unite!
    • Chernomordik L.V., et al. Membranes of the world unite!. J. Cell Biol. 2006, 175:201-207.
    • (2006) J. Cell Biol. , vol.175 , pp. 201-207
    • Chernomordik, L.V.1
  • 58
    • 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
  • 59
    • 42549160157 scopus 로고    scopus 로고
    • Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth
    • Chen S., et al. Loss of tafazzin in yeast leads to increased oxidative stress during respiratory growth. Mol. Microbiol. 2008, 68:1061-1072.
    • (2008) Mol. Microbiol. , vol.68 , pp. 1061-1072
    • Chen, S.1
  • 60
    • 79959382588 scopus 로고    scopus 로고
    • Antiphospholipid syndrome: laboratory detection, mechanisms of action and treatment
    • Tripodi A., et al. Antiphospholipid syndrome: laboratory detection, mechanisms of action and treatment. J. Intern. Med. 2011, 270:110-122.
    • (2011) J. Intern. Med. , vol.270 , pp. 110-122
    • Tripodi, A.1
  • 61
    • 67649782034 scopus 로고    scopus 로고
    • Determination of cellular lipids bound to human CD1d molecules
    • Cox D., et al. Determination of cellular lipids bound to human CD1d molecules. PLoS ONE 2009, 4:e5325.
    • (2009) PLoS ONE , vol.4
    • Cox, D.1
  • 62
    • 79955001657 scopus 로고    scopus 로고
    • Cardiolipin binds to CD1d and stimulates CD1d-restricted γδ T cells in the normal murine repertoire
    • Dieude M., et al. Cardiolipin binds to CD1d and stimulates CD1d-restricted γδ T cells in the normal murine repertoire. J. Immunol. 2011, 186:4771-4781.
    • (2011) J. Immunol. , vol.186 , pp. 4771-4781
    • Dieude, M.1
  • 63
    • 77957788222 scopus 로고    scopus 로고
    • Dynamic regulation of cardiolipin by the lipid pump Atp8b1 determines the severity of lung injury in experimental pneumonia
    • Ray N.B., et al. Dynamic regulation of cardiolipin by the lipid pump Atp8b1 determines the severity of lung injury in experimental pneumonia. Nat. Med. 2010, 16:1120-1127.
    • (2010) Nat. Med. , vol.16 , pp. 1120-1127
    • Ray, N.B.1
  • 64
    • 33750526473 scopus 로고    scopus 로고
    • A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis
    • Choi S.Y., et al. A common lipid links Mfn-mediated mitochondrial fusion and SNARE-regulated exocytosis. Nat. Cell Biol. 2006, 8:1255-1262.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1255-1262
    • Choi, S.Y.1
  • 65
    • 27444446738 scopus 로고    scopus 로고
    • Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine and cardiolipin biosynthetic pathways in Saccharomyces cerevisiae
    • Gohil V.M., et al. Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine and cardiolipin biosynthetic pathways in Saccharomyces cerevisiae. J. Biol. Chem. 2005, 280:35410-35416.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35410-35416
    • Gohil, V.M.1
  • 66
    • 70450265196 scopus 로고    scopus 로고
    • Prohibitins and the functional compartmentalization of mitochondrial membranes
    • Osman C., et al. Prohibitins and the functional compartmentalization of mitochondrial membranes. J. Cell Sci. 2009, 122:3823-3830.
    • (2009) J. Cell Sci. , vol.122 , pp. 3823-3830
    • Osman, C.1
  • 67
    • 67449138848 scopus 로고    scopus 로고
    • Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria
    • Tamura Y., et al. Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria. J. Cell Biol. 2009, 185:1029-1045.
    • (2009) J. Cell Biol. , vol.185 , pp. 1029-1045
    • Tamura, Y.1
  • 68
    • 77956391459 scopus 로고    scopus 로고
    • Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35
    • Potting C., et al. Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins depends on proteolysis and Mdm35. EMBO J. 2010, 29:2888-2898.
    • (2010) EMBO J. , vol.29 , pp. 2888-2898
    • Potting, C.1
  • 69
    • 77956378766 scopus 로고    scopus 로고
    • Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation
    • Tamura Y., et al. Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation. EMBO J. 2010, 29:2875-2887.
    • (2010) EMBO J. , vol.29 , pp. 2875-2887
    • Tamura, Y.1
  • 70
    • 12144280303 scopus 로고    scopus 로고
    • Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast
    • Dimmer K.S., et al. Mdm31 and Mdm32 are inner membrane proteins required for maintenance of mitochondrial shape and stability of mitochondrial DNA nucleoids in yeast. J. Cell Biol. 2005, 168:103-115.
    • (2005) J. Cell Biol. , vol.168 , pp. 103-115
    • Dimmer, K.S.1
  • 71
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann B., et al. An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 2009, 325:477-481.
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1
  • 72
    • 79953043224 scopus 로고    scopus 로고
    • FMP30 is required for the maintenance of a normal cardiolipin level and mitochondrial morphology in the absence of mitochondrial phosphatidylethanolamine synthesis
    • Kuroda T., et al. FMP30 is required for the maintenance of a normal cardiolipin level and mitochondrial morphology in the absence of mitochondrial phosphatidylethanolamine synthesis. Mol. Microbiol. 2011, 80:248-265.
    • (2011) Mol. Microbiol. , vol.80 , pp. 248-265
    • Kuroda, T.1
  • 73
    • 59449088611 scopus 로고    scopus 로고
    • The translocator maintenance protein Tam41 is required for mitochondrial cardiolipin biosynthesis
    • Kutik S., et al. The translocator maintenance protein Tam41 is required for mitochondrial cardiolipin biosynthesis. J. Cell Biol. 2008, 183:1213-1221.
    • (2008) J. Cell Biol. , vol.183 , pp. 1213-1221
    • Kutik, S.1
  • 74
    • 79551700415 scopus 로고    scopus 로고
    • Barth syndrome mutations that cause tafazzin complex lability
    • Claypool S.M., et al. Barth syndrome mutations that cause tafazzin complex lability. J. Cell Biol. 2011, 192:447-462.
    • (2011) J. Cell Biol. , vol.192 , pp. 447-462
    • Claypool, S.M.1
  • 75
    • 70349495692 scopus 로고    scopus 로고
    • A new look at Cardiolipin
    • Haines T.H. A new look at Cardiolipin. Biochim. Biophys. Acta 2009, 1788:1997-2002.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1997-2002
    • Haines, T.H.1
  • 76
    • 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
  • 77
    • 70349930116 scopus 로고    scopus 로고
    • Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion
    • DeVay R.M., et al. Coassembly of Mgm1 isoforms requires cardiolipin and mediates mitochondrial inner membrane fusion. J. Cell Biol. 2009, 186:793-803.
    • (2009) J. Cell Biol. , vol.186 , pp. 793-803
    • DeVay, R.M.1
  • 78
    • 77956634444 scopus 로고    scopus 로고
    • Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization
    • Montessuit S., et al. Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization. Cell 2010, 142:889-901.
    • (2010) Cell , vol.142 , pp. 889-901
    • Montessuit, S.1
  • 79
    • 58149201240 scopus 로고    scopus 로고
    • Cardiolipin provides an essential activating platform for caspase-8 on mitochondria
    • Gonzalvez F., et al. Cardiolipin provides an essential activating platform for caspase-8 on mitochondria. J. Cell Biol. 2008, 183:681-696.
    • (2008) J. Cell Biol. , vol.183 , pp. 681-696
    • Gonzalvez, F.1


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