메뉴 건너뛰기




Volumn 1788, Issue 10, 2009, Pages 2032-2047

Mitochondrial kinases and their molecular interaction with cardiolipin

Author keywords

Apoptosis; Creatine kinase; Lipid clustering; Lipid transfer; Microcompartment; Mitochondria; nm23; Nucleoside diphosphate kinase; Proteolipid complex

Indexed keywords

ANTHRACYCLINE; CARDIOLIPIN; CYTOCHROME C; GUANOSINE TRIPHOSPHATE; MITOCHONDRIAL CREATINE KINASE; MITOCHONDRIAL ENZYME; NUCLEOSIDE DIPHOSPHATE KINASE; PROTEIN BID; SCRAMBLASE;

EID: 70349517148     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.04.018     Document Type: Review
Times cited : (83)

References (210)
  • 2
    • 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 (2002) 43553-43556
    • (2002) J. Biol. Chem. , vol.277 , pp. 43553-43556
    • Zhang, M.1    Mileykovskaya, E.2    Dowhan, W.3
  • 3
    • 0028084988 scopus 로고
    • The reconstituted ADP/ATP carrier activity has an absolute requirement for cardiolipin as shown in cysteine mutants
    • Hoffmann B., Stockl 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 (1994) 1940-1944
    • (1994) J. Biol. Chem. , vol.269 , pp. 1940-1944
    • Hoffmann, B.1    Stockl, A.2    Schlame, M.3    Beyer, K.4    Klingenberg, M.5
  • 4
    • 51649096941 scopus 로고    scopus 로고
    • Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane
    • Claypool S.M., Oktay Y., Boontheung P., Loo J.A., and Koehler C.M. Cardiolipin defines the interactome of the major ADP/ATP carrier protein of the mitochondrial inner membrane. J. Cell Biol. 182 (2008) 937-950
    • (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
  • 5
    • 0028836142 scopus 로고
    • Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions
    • Rytomaa M., and Kinnunen P.K. Reversibility of the binding of cytochrome c to liposomes. Implications for lipid-protein interactions. J. Biol. Chem. 270 (1995) 3197-3202
    • (1995) J. Biol. Chem. , vol.270 , pp. 3197-3202
    • Rytomaa, M.1    Kinnunen, P.K.2
  • 10
    • 0033935979 scopus 로고    scopus 로고
    • Creatine and creatinine metabolism
    • Wyss M., and Kaddurah-Daouk R. Creatine and creatinine metabolism. Physiol. Rev. 80 (2000) 1107-1213
    • (2000) Physiol. Rev. , vol.80 , pp. 1107-1213
    • Wyss, M.1    Kaddurah-Daouk, R.2
  • 11
    • 0031712655 scopus 로고    scopus 로고
    • Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach
    • Schlattner U., Forstner M., Eder M., Stachowiak O., Fritz-Wolf K., and Wallimann T. Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach. Mol. Cell. Biochem. 184 (1998) 125-140
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 125-140
    • Schlattner, U.1    Forstner, M.2    Eder, M.3    Stachowiak, O.4    Fritz-Wolf, K.5    Wallimann, T.6
  • 12
    • 29344468308 scopus 로고    scopus 로고
    • Metabolite channeling: creatine kinase microcompartments
    • Lennarz W.J., and Lane M.D. (Eds), Academic Press, New York, USA
    • Schlattner U., and Wallimann T. Metabolite channeling: creatine kinase microcompartments. In: Lennarz W.J., and Lane M.D. (Eds). Encyclopedia of Biological Chemistry (2004), Academic Press, New York, USA 646-651
    • (2004) Encyclopedia of Biological Chemistry , pp. 646-651
    • Schlattner, U.1    Wallimann, T.2
  • 13
    • 0032406769 scopus 로고    scopus 로고
    • Some new aspects of creatine kinase (CK): compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology
    • Wallimann T., Dolder M., Schlattner U., Eder M., Hornemann T., O'Gorman E., Ruck A., and Brdiczka D. Some new aspects of creatine kinase (CK): compartmentation, structure, function and regulation for cellular and mitochondrial bioenergetics and physiology. Biofactors 8 (1998) 229-234
    • (1998) Biofactors , vol.8 , pp. 229-234
    • Wallimann, T.1    Dolder, M.2    Schlattner, U.3    Eder, M.4    Hornemann, T.5    O'Gorman, E.6    Ruck, A.7    Brdiczka, D.8
  • 15
    • 70449732876 scopus 로고    scopus 로고
    • The mammalian Nm23/NDPK family: From metastasis control to cilia movement
    • in press, doi:10.1007/s11010-009-0120-7
    • M. Boissan, S. Debernat, E. Peuchant, U. Schlattner, M.L. Lacombe, The mammalian Nm23/NDPK family: from metastasis control to cilia movement, Mol. Cell. Biochem. (in press), doi:10.1007/s11010-009-0120-7.
    • Mol. Cell. Biochem
    • Boissan, M.1    Debernat, S.2    Peuchant, E.3    Schlattner, U.4    Lacombe, M.L.5
  • 18
    • 0035052706 scopus 로고    scopus 로고
    • Evolution and physiological roles of phosphagen systems
    • Ellington W.R. Evolution and physiological roles of phosphagen systems. Annu. Rev. Physiol. 63 (2001) 289-325
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 289-325
    • Ellington, W.R.1
  • 19
    • 36148988728 scopus 로고    scopus 로고
    • Early evolution of the creatine kinase gene family and the capacity for creatine biosynthesis and membrane transport
    • Ellington W.R., and Suzuki T. Early evolution of the creatine kinase gene family and the capacity for creatine biosynthesis and membrane transport. Subcell. Biochem. 46 (2007) 17-26
    • (2007) Subcell. Biochem. , vol.46 , pp. 17-26
    • Ellington, W.R.1    Suzuki, T.2
  • 20
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis
    • Wallimann T., Wyss M., Brdiczka D., Nicolay K., and Eppenberger H.M. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem. J. 281 Pt 1 (1992) 21-40
    • (1992) Biochem. J. , vol.281 , Issue.PART 1 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 21
    • 45249095633 scopus 로고    scopus 로고
    • Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion
    • O'Connor R.S., Steeds C.M., Wiseman R.W., and Pavlath G.K. Phosphocreatine as an energy source for actin cytoskeletal rearrangements during myoblast fusion. J. Physiol. 586 (2008) 2841-2853
    • (2008) J. Physiol. , vol.586 , pp. 2841-2853
    • O'Connor, R.S.1    Steeds, C.M.2    Wiseman, R.W.3    Pavlath, G.K.4
  • 23
    • 12844260125 scopus 로고    scopus 로고
    • Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane
    • Speer O., Back N., Buerklen T., Brdiczka D., Koretsky A., Wallimann T., and Eriksson O. Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane. Biochem. J. 385 (2005) 445-450
    • (2005) Biochem. J. , vol.385 , pp. 445-450
    • Speer, O.1    Back, N.2    Buerklen, T.3    Brdiczka, D.4    Koretsky, A.5    Wallimann, T.6    Eriksson, O.7
  • 24
    • 67349166562 scopus 로고    scopus 로고
    • Interaction of NDPK-D with cardiolipin-containing membranes: structural basis and implications for mitochondrial physiology
    • Lacombe M.L., Tokarska-Schlattner M., Epand R.F., Boissan M., Epand R.M., and Schlattner U. Interaction of NDPK-D with cardiolipin-containing membranes: structural basis and implications for mitochondrial physiology. Biochimie 91 6 (2009) 779-783
    • (2009) Biochimie , vol.91 , Issue.6 , pp. 779-783
    • Lacombe, M.L.1    Tokarska-Schlattner, M.2    Epand, R.F.3    Boissan, M.4    Epand, R.M.5    Schlattner, U.6
  • 25
    • 0023775251 scopus 로고
    • Native mitochondrial creatine kinase forms octameric structures. I. Isolation of two interconvertible mitochondrial creatine kinase forms, dimeric and octameric mitochondrial creatine kinase: characterization, localization, structure-function relationships
    • Schlegel J., Zurbriggen B., Wegmann G., Wyss M., Eppenberger H.M., and Wallimann T. Native mitochondrial creatine kinase forms octameric structures. I. Isolation of two interconvertible mitochondrial creatine kinase forms, dimeric and octameric mitochondrial creatine kinase: characterization, localization, structure-function relationships. J. Biol. Chem. 263 (1988) 16942-16953
    • (1988) J. Biol. Chem. , vol.263 , pp. 16942-16953
    • Schlegel, J.1    Zurbriggen, B.2    Wegmann, G.3    Wyss, M.4    Eppenberger, H.M.5    Wallimann, T.6
  • 26
    • 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 (2000) 17314-17320
    • (2000) J. Biol. Chem. , vol.275 , pp. 17314-17320
    • Schlattner, U.1    Wallimann, T.2
  • 27
    • 0034658257 scopus 로고    scopus 로고
    • Crystal structure of human ubiquitous mitochondrial creatine kinase
    • Eder M., Fritz-Wolf K., Kabsch W., Wallimann T., and Schlattner U. Crystal structure of human ubiquitous mitochondrial creatine kinase. Proteins 39 (2000) 216-225
    • (2000) Proteins , vol.39 , pp. 216-225
    • Eder, M.1    Fritz-Wolf, K.2    Kabsch, W.3    Wallimann, T.4    Schlattner, U.5
  • 30
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao J.K., Bujacz G., and Wlodawer A. Crystal structure of rabbit muscle creatine kinase. FEBS Lett. 439 (1998) 133-137
    • (1998) FEBS Lett. , vol.439 , pp. 133-137
    • Rao, J.K.1    Bujacz, G.2    Wlodawer, A.3
  • 32
    • 0029646092 scopus 로고
    • X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution
    • Morera S., Lacombe M.L., Xu Y., LeBras G., and Janin J. X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure 3 (1995) 1307-1314
    • (1995) Structure , vol.3 , pp. 1307-1314
    • Morera, S.1    Lacombe, M.L.2    Xu, Y.3    LeBras, G.4    Janin, J.5
  • 33
    • 0028091859 scopus 로고
    • Refined X-ray structure of Dictyostelium discoideum nucleoside diphosphate kinase at 1.8 A resolution
    • Morera S., LeBras G., Lascu I., Lacombe M.L., Veron M., and Janin J. Refined X-ray structure of Dictyostelium discoideum nucleoside diphosphate kinase at 1.8 A resolution. J. Mol. Biol. 243 (1994) 873-890
    • (1994) J. Mol. Biol. , vol.243 , pp. 873-890
    • Morera, S.1    LeBras, G.2    Lascu, I.3    Lacombe, M.L.4    Veron, M.5    Janin, J.6
  • 37
    • 29344434866 scopus 로고    scopus 로고
    • The relevance of mitochondrial membrane topology to mitochondrial function
    • Mannella C.A. The relevance of mitochondrial membrane topology to mitochondrial function. Biochim. Biophys. Acta 1762 (2006) 140-147
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 140-147
    • Mannella, C.A.1
  • 38
    • 54449101307 scopus 로고    scopus 로고
    • The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration
    • Tokarska-Schlattner M., Boissan M., Munier A., Borot C., Mailleau C., Speer O., Schlattner U., and Lacombe M.L. The nucleoside diphosphate kinase D (NM23-H4) binds the inner mitochondrial membrane with high affinity to cardiolipin and couples nucleotide transfer with respiration. J. Biol. Chem. 283 (2008) 26198-26207
    • (2008) J. Biol. Chem. , vol.283 , pp. 26198-26207
    • Tokarska-Schlattner, M.1    Boissan, M.2    Munier, A.3    Borot, C.4    Mailleau, C.5    Speer, O.6    Schlattner, U.7    Lacombe, M.L.8
  • 39
    • 0028242198 scopus 로고
    • Crystallization of mitochondrial creatine kinase on negatively charged lipid layers
    • Schnyder T., Cyrklaff M., Fuchs K., and Wallimann T. Crystallization of mitochondrial creatine kinase on negatively charged lipid layers. J. Struct. Biol. 112 (1994) 136-147
    • (1994) J. Struct. Biol. , vol.112 , pp. 136-147
    • Schnyder, T.1    Cyrklaff, M.2    Fuchs, K.3    Wallimann, T.4
  • 41
    • 0033795931 scopus 로고    scopus 로고
    • The catalytic mechanism of nucleoside diphosphate kinases
    • Lascu I., and Gonin P. The catalytic mechanism of nucleoside diphosphate kinases. J. Bioenerg. Biomembr. 32 (2000) 237-246
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 237-246
    • Lascu, I.1    Gonin, P.2
  • 42
    • 0021895146 scopus 로고
    • Cardiolipin is the membrane receptor for mitochondrial creatine phosphokinase
    • Muller M., Moser R., Cheneval D., and Carafoli E. Cardiolipin is the membrane receptor for mitochondrial creatine phosphokinase. J. Biol. Chem. 260 (1985) 3839-3843
    • (1985) J. Biol. Chem. , vol.260 , pp. 3839-3843
    • Muller, M.1    Moser, R.2    Cheneval, D.3    Carafoli, E.4
  • 44
    • 0026035373 scopus 로고
    • Interaction of mitochondrial creatine kinase with model membranes. A monolayer study
    • Rojo M., Hovius R., Demel R., Wallimann T., Eppenberger H.M., and Nicolay K. Interaction of mitochondrial creatine kinase with model membranes. A monolayer study. FEBS Lett. 281 (1991) 123-129
    • (1991) FEBS Lett. , vol.281 , pp. 123-129
    • Rojo, M.1    Hovius, R.2    Demel, R.3    Wallimann, T.4    Eppenberger, H.M.5    Nicolay, K.6
  • 45
    • 0031571603 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase interaction with phospholipid vesicles
    • Vacheron M.J., Clottes E., Chautard C., and Vial C. Mitochondrial creatine kinase interaction with phospholipid vesicles. Arch. Biochem. Biophys. 344 (1997) 316-324
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 316-324
    • Vacheron, M.J.1    Clottes, E.2    Chautard, C.3    Vial, C.4
  • 46
    • 0035930592 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase and mitochondrial outer membrane porin show a direct interaction that is modulated by calcium
    • Schlattner U., Dolder M., Wallimann T., and Tokarska-Schlattner M. Mitochondrial creatine kinase and mitochondrial outer membrane porin show a direct interaction that is modulated by calcium. J. Biol. Chem. 276 (2001) 48027-48030
    • (2001) J. Biol. Chem. , vol.276 , pp. 48027-48030
    • Schlattner, U.1    Dolder, M.2    Wallimann, T.3    Tokarska-Schlattner, M.4
  • 47
    • 0031781884 scopus 로고    scopus 로고
    • Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: allocation of N-terminal binding epitope in MM-CK and BB-CK
    • Stolz M., and Wallimann T. Myofibrillar interaction of cytosolic creatine kinase (CK) isoenzymes: allocation of N-terminal binding epitope in MM-CK and BB-CK. J. Cell Sci. 111 (1998) 1207-1216
    • (1998) J. Cell Sci. , vol.111 , pp. 1207-1216
    • Stolz, M.1    Wallimann, T.2
  • 48
    • 0034494381 scopus 로고    scopus 로고
    • Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ
    • Kraft T., Hornemann T., Stolz M., Nier V., and Wallimann T. Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: a biochemical study in situ. J. Muscle Res. Cell Motil. 21 (2000) 691-703
    • (2000) J. Muscle Res. Cell Motil. , vol.21 , pp. 691-703
    • Kraft, T.1    Hornemann, T.2    Stolz, M.3    Nier, V.4    Wallimann, T.5
  • 49
    • 0026778172 scopus 로고
    • In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve
    • Wegmann G., Zanolla E., Eppenberger H.M., and Wallimann T. In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve. J. Muscle Res. Cell Motil. 13 (1992) 420-435
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 420-435
    • Wegmann, G.1    Zanolla, E.2    Eppenberger, H.M.3    Wallimann, T.4
  • 50
    • 0017324568 scopus 로고
    • The localization of the MM isozyme of creatine phosphokinase on the surface membrane of myocardial cells and its functional coupling to ouabain-inhibited (Na+, K+)-ATPase
    • Saks V.A., Lipina N.V., Sharov V.G., Smirnov V.N., Chazov E., and Grosse R. The localization of the MM isozyme of creatine phosphokinase on the surface membrane of myocardial cells and its functional coupling to ouabain-inhibited (Na+, K+)-ATPase. Biochim. Biophys. Acta 465 (1977) 550-558
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 550-558
    • Saks, V.A.1    Lipina, N.V.2    Sharov, V.G.3    Smirnov, V.N.4    Chazov, E.5    Grosse, R.6
  • 51
    • 0025257336 scopus 로고
    • Muscle-type MM creatine kinase is specifically bound to sarcoplasmic reticulum and can support Ca2+ uptake and regulate local ATP/ADP ratios
    • Rossi A.M., Eppenberger H.M., Volpe P., Cotrufo R., and Wallimann T. Muscle-type MM creatine kinase is specifically bound to sarcoplasmic reticulum and can support Ca2+ uptake and regulate local ATP/ADP ratios. J. Biol. Chem. 265 (1990) 5258-5266
    • (1990) J. Biol. Chem. , vol.265 , pp. 5258-5266
    • Rossi, A.M.1    Eppenberger, H.M.2    Volpe, P.3    Cotrufo, R.4    Wallimann, T.5
  • 52
    • 0034641108 scopus 로고    scopus 로고
    • Isoenzyme-specific interaction of muscle-type creatine kinase with the sarcomeric M-line is mediated by NH(2)-terminal lysine charge-clamps
    • Hornemann T., Stolz M., and Wallimann T. Isoenzyme-specific interaction of muscle-type creatine kinase with the sarcomeric M-line is mediated by NH(2)-terminal lysine charge-clamps. J. Cell Biol. 149 (2000) 1225-1234
    • (2000) J. Cell Biol. , vol.149 , pp. 1225-1234
    • Hornemann, T.1    Stolz, M.2    Wallimann, T.3
  • 53
    • 0041825389 scopus 로고    scopus 로고
    • Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein
    • Hornemann T., Kempa S., Himmel M., Hayess K., Furst D.O., and Wallimann T. Muscle-type creatine kinase interacts with central domains of the M-band proteins myomesin and M-protein. J. Mol. Biol. 332 (2003) 877-887
    • (2003) J. Mol. Biol. , vol.332 , pp. 877-887
    • Hornemann, T.1    Kempa, S.2    Himmel, M.3    Hayess, K.4    Furst, D.O.5    Wallimann, T.6
  • 54
    • 3042857526 scopus 로고    scopus 로고
    • Analysis of functional coupling: mitochondrial creatine kinase and adenine nucleotide translocase
    • Vendelin M., Lemba M., and Saks V.A. Analysis of functional coupling: mitochondrial creatine kinase and adenine nucleotide translocase. Biophys. J. 87 (2004) 696-713
    • (2004) Biophys. J. , vol.87 , pp. 696-713
    • Vendelin, M.1    Lemba, M.2    Saks, V.A.3
  • 55
    • 0034629141 scopus 로고    scopus 로고
    • Direct evidence for the control of mitochondrial respiration by mitochondrial creatine kinase in oxidative muscle cells in situ
    • Kay L., Nicolay K., Wieringa B., Saks V., and Wallimann T. Direct evidence for the control of mitochondrial respiration by mitochondrial creatine kinase in oxidative muscle cells in situ. J. Biol. Chem. 275 (2000) 6937-6944
    • (2000) J. Biol. Chem. , vol.275 , pp. 6937-6944
    • Kay, L.1    Nicolay, K.2    Wieringa, B.3    Saks, V.4    Wallimann, T.5
  • 56
    • 0038381490 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation
    • Dolder M., Walzel B., Speer O., Schlattner U., and Wallimann T. Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation. J. Biol. Chem. 278 (2003) 17760-17766
    • (2003) J. Biol. Chem. , vol.278 , pp. 17760-17766
    • Dolder, M.1    Walzel, B.2    Speer, O.3    Schlattner, U.4    Wallimann, T.5
  • 57
  • 58
    • 33846001693 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase activity prevents reactive oxygen species generation: antioxidant role of mitochondrial kinases-dependent ADP re-cycling activity
    • Meyer L.E., Machado L.B., Santiago A.P., da-Silva W.S., De Felice F.G., Holub O., Oliveira M.F., and Galina A. Mitochondrial creatine kinase activity prevents reactive oxygen species generation: antioxidant role of mitochondrial kinases-dependent ADP re-cycling activity. J. Biol. Chem. 281 (2006) 37361-37371
    • (2006) J. Biol. Chem. , vol.281 , pp. 37361-37371
    • Meyer, L.E.1    Machado, L.B.2    Santiago, A.P.3    da-Silva, W.S.4    De Felice, F.G.5    Holub, O.6    Oliveira, M.F.7    Galina, A.8
  • 59
    • 33846023675 scopus 로고    scopus 로고
    • Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes
    • Epand R.F., Schlattner U., Wallimann T., Lacombe M.L., and Epand R.M. Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes. Biophys. J. 92 (2007) 126-137
    • (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
  • 61
    • 0038037716 scopus 로고    scopus 로고
    • Phosphotransfer networks and cellular energetics
    • Dzeja P.P., and Terzic A. Phosphotransfer networks and cellular energetics. J. Exp. Biol. 206 (2003) 2039-2047
    • (2003) J. Exp. Biol. , vol.206 , pp. 2039-2047
    • Dzeja, P.P.1    Terzic, A.2
  • 65
    • 12344252100 scopus 로고    scopus 로고
    • Proteomics opens doors to the mechanisms of developmentally regulated secretion
    • Alexander S., Srinivasan S., and Alexander H. Proteomics opens doors to the mechanisms of developmentally regulated secretion. Mol. Cell. Proteomics 2 (2003) 1156-1163
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1156-1163
    • Alexander, S.1    Srinivasan, S.2    Alexander, H.3
  • 67
    • 37848998577 scopus 로고    scopus 로고
    • NM23 and metastasis suppressor genes: update
    • Boissan M., Poupon M.F., and Lacombe M.L. NM23 and metastasis suppressor genes: update. Med. Sci. (Paris) 23 (2007) 1115-1123
    • (2007) Med. Sci. (Paris) , vol.23 , pp. 1115-1123
    • Boissan, M.1    Poupon, M.F.2    Lacombe, M.L.3
  • 68
  • 69
    • 0033804989 scopus 로고    scopus 로고
    • Role of AWD/nucleoside diphosphate kinase in Drosophila development
    • Timmons L., and Shearn A. Role of AWD/nucleoside diphosphate kinase in Drosophila development. J. Bioenerg. Biomembr. 32 (2000) 293-300
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 293-300
    • Timmons, L.1    Shearn, A.2
  • 70
    • 33846828378 scopus 로고    scopus 로고
    • Interaction of nucleoside diphosphate kinase B with heterotrimeric G protein betagamma dimers: consequences on G protein activation and stability
    • Wieland T. Interaction of nucleoside diphosphate kinase B with heterotrimeric G protein betagamma dimers: consequences on G protein activation and stability. Naunyn-Schmiedeberg's Arch. Pharmacol. 374 (2007) 373-383
    • (2007) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.374 , pp. 373-383
    • Wieland, T.1
  • 71
    • 0033805226 scopus 로고    scopus 로고
    • NM23/nucleoside diphosphate kinase and signal transduction
    • Otero A.S. NM23/nucleoside diphosphate kinase and signal transduction. J. Bioenerg. Biomembr. 32 (2000) 269-275
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 269-275
    • Otero, A.S.1
  • 72
    • 0024963096 scopus 로고
    • Further characterization of contact sites from mitochondria of different tissues: topology of peripheral kinases
    • Adams V., Bosch W., Schlegel J., Wallimann T., and Brdiczka D. Further characterization of contact sites from mitochondria of different tissues: topology of peripheral kinases. Biochim. Biophys. Acta 981 (1989) 213-225
    • (1989) Biochim. Biophys. Acta , vol.981 , pp. 213-225
    • Adams, V.1    Bosch, W.2    Schlegel, J.3    Wallimann, T.4    Brdiczka, D.5
  • 73
    • 0028176942 scopus 로고
    • Characterization of the 3 beta-hydroxysteroid dehydrogenase activity associated with bovine adrenocortical mitochondria
    • Cherradi N., Defaye G., and Chambaz E.M. Characterization of the 3 beta-hydroxysteroid dehydrogenase activity associated with bovine adrenocortical mitochondria. Endocrinology 134 (1994) 1358-1364
    • (1994) Endocrinology , vol.134 , pp. 1358-1364
    • Cherradi, N.1    Defaye, G.2    Chambaz, E.M.3
  • 74
    • 0017864512 scopus 로고
    • Phosphorylation of adenosine monophosphate in the mitochondrial matrix
    • Krebs H.A., and Wiggins D. Phosphorylation of adenosine monophosphate in the mitochondrial matrix. Biochem. J. 174 (1978) 297-301
    • (1978) Biochem. J. , vol.174 , pp. 297-301
    • Krebs, H.A.1    Wiggins, D.2
  • 75
    • 33751091235 scopus 로고    scopus 로고
    • GTP in the mitochondrial matrix plays a crucial role in organellar iron homoeostasis
    • Gordon D.M., Lyver E.R., Lesuisse E., Dancis A., and Pain D. GTP in the mitochondrial matrix plays a crucial role in organellar iron homoeostasis. Biochem. J. 400 (2006) 163-168
    • (2006) Biochem. J. , vol.400 , pp. 163-168
    • Gordon, D.M.1    Lyver, E.R.2    Lesuisse, E.3    Dancis, A.4    Pain, D.5
  • 76
    • 0015784589 scopus 로고
    • Coupling of adenosine triphosphate formation in mitochondria to the formation of nucleoside triphosphates. Involvement of nucleoside diphosphokinase
    • Pedersen P.L. Coupling of adenosine triphosphate formation in mitochondria to the formation of nucleoside triphosphates. Involvement of nucleoside diphosphokinase. J. Biol. Chem. 248 (1973) 3956-3962
    • (1973) J. Biol. Chem. , vol.248 , pp. 3956-3962
    • Pedersen, P.L.1
  • 77
    • 0022482543 scopus 로고
    • The mitochondrial creatine phosphokinase is associated with inner membrane cardiolipin
    • Muller M., Cheneval D., and Carafoli E. The mitochondrial creatine phosphokinase is associated with inner membrane cardiolipin. Adv. Exp. Med. Biol. 194 (1986) 151-156
    • (1986) Adv. Exp. Med. Biol. , vol.194 , pp. 151-156
    • Muller, M.1    Cheneval, D.2    Carafoli, E.3
  • 78
    • 0022343950 scopus 로고
    • Association of creatine kinase with rat heart mitochondria: high and low affinity binding sites and the involvement of phospholipids
    • Schlame M., and Augustin W. Association of creatine kinase with rat heart mitochondria: high and low affinity binding sites and the involvement of phospholipids. Biomed. Biochim. Acta 44 (1985) 1083-1088
    • (1985) Biomed. Biochim. Acta , vol.44 , pp. 1083-1088
    • Schlame, M.1    Augustin, W.2
  • 79
    • 0029857123 scopus 로고    scopus 로고
    • Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer
    • Stachowiak O., Dolder M., and Wallimann T. Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer. Biochemistry 35 (1996) 15522-15528
    • (1996) Biochemistry , vol.35 , pp. 15522-15528
    • Stachowiak, O.1    Dolder, M.2    Wallimann, T.3
  • 80
    • 7044274626 scopus 로고    scopus 로고
    • Lipids in membrane protein structures
    • Palsdottir H., and Hunte C. Lipids in membrane protein structures. Biochim. Biophys. Acta 1666 (2004) 2-18
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 2-18
    • Palsdottir, H.1    Hunte, C.2
  • 81
    • 0034057235 scopus 로고    scopus 로고
    • A quantitative approach to membrane binding of human ubiquitous mitochondrial creatine kinase using surface plasmon resonance
    • Schlattner U., and Wallimann T. A quantitative approach to membrane binding of human ubiquitous mitochondrial creatine kinase using surface plasmon resonance. J. Bioenerg. Biomembr. 32 (2000) 123-131
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 123-131
    • Schlattner, U.1    Wallimann, T.2
  • 82
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • Schlame M., Rua D., and Greenberg M.L. The biosynthesis and functional role of cardiolipin. Prog. Lipid Res. 39 (2000) 257-288
    • (2000) Prog. Lipid Res. , vol.39 , pp. 257-288
    • Schlame, M.1    Rua, D.2    Greenberg, M.L.3
  • 83
    • 0022979484 scopus 로고
    • Heart mitochondria in physiological salt solution: not ionic strength but salt composition is important for association of creatine kinase with the inner membrane surface
    • Saks V.A., Khuchua Z.A., Kuznetsov A.V., Veksler V.I., and Sharov V.G. Heart mitochondria in physiological salt solution: not ionic strength but salt composition is important for association of creatine kinase with the inner membrane surface. Biochem. Biophys. Res. Commun. 139 (1986) 1262-1271
    • (1986) Biochem. Biophys. Res. Commun. , vol.139 , pp. 1262-1271
    • Saks, V.A.1    Khuchua, Z.A.2    Kuznetsov, A.V.3    Veksler, V.I.4    Sharov, V.G.5
  • 84
    • 0035918580 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase binding to phospholipids decreases fluidity of membranes and promotes new lipid-induced beta structures as monitored by red edge excitation shift, laurdan fluorescence, and FTIR
    • Granjon T., Vacheron M.J., Vial C., and Buchet R. Mitochondrial creatine kinase binding to phospholipids decreases fluidity of membranes and promotes new lipid-induced beta structures as monitored by red edge excitation shift, laurdan fluorescence, and FTIR. Biochemistry 40 (2001) 6016-6026
    • (2001) Biochemistry , vol.40 , pp. 6016-6026
    • Granjon, T.1    Vacheron, M.J.2    Vial, C.3    Buchet, R.4
  • 85
    • 0026498492 scopus 로고
    • Reversible, nonionic, and pH-dependent association of cytochrome c with cardiolipin-phosphatidylcholine liposomes
    • Rytomaa M., Mustonen P., and Kinnunen P.K. Reversible, nonionic, and pH-dependent association of cytochrome c with cardiolipin-phosphatidylcholine liposomes. J. Biol. Chem. 267 (1992) 22243-22248
    • (1992) J. Biol. Chem. , vol.267 , pp. 22243-22248
    • Rytomaa, M.1    Mustonen, P.2    Kinnunen, P.K.3
  • 86
    • 0029738341 scopus 로고    scopus 로고
    • Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase
    • Salamon Z., and Tollin G. Surface plasmon resonance studies of complex formation between cytochrome c and bovine cytochrome c oxidase incorporated into a supported planar lipid bilayer. I. Binding of cytochrome c to cardiolipin/phosphatidylcholine membranes in the absence of oxidase. Biophys. J. 71 (1996) 848-857
    • (1996) Biophys. J. , vol.71 , pp. 848-857
    • Salamon, Z.1    Tollin, G.2
  • 88
    • 0021111174 scopus 로고
    • Changes in freeze-fractured mitochondrial membranes correlated to their energetic state. Dynamic interactions of the boundary membranes
    • Knoll G., and Brdiczka D. Changes in freeze-fractured mitochondrial membranes correlated to their energetic state. Dynamic interactions of the boundary membranes. Biochim. Biophys. Acta 733 (1983) 102-110
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 102-110
    • Knoll, G.1    Brdiczka, D.2
  • 89
    • 0014347959 scopus 로고
    • Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states
    • Hackenbrock C.R. Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states. Proc. Natl. Acad. Sci. U. S. A. 61 (1968) 598-605
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.61 , pp. 598-605
    • Hackenbrock, C.R.1
  • 90
    • 0020489067 scopus 로고
    • Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study
    • Van Venetie R., and Verkleij A.J. Possible role of non-bilayer lipids in the structure of mitochondria. A freeze-fracture electron microscopy study. Biochim. Biophys. Acta 692 (1982) 397-405
    • (1982) Biochim. Biophys. Acta , vol.692 , pp. 397-405
    • Van Venetie, R.1    Verkleij, A.J.2
  • 91
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • Frey T.G., and Mannella C.A. The internal structure of mitochondria. Trends Biochem. Sci. 25 (2000) 319-324
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 93
    • 33845983303 scopus 로고    scopus 로고
    • Voltage gating of VDAC is regulated by nonlamellar lipids of mitochondrial membranes
    • Rostovtseva T.K., Kazemi N., Weinrich M., and Bezrukov S.M. Voltage gating of VDAC is regulated by nonlamellar lipids of mitochondrial membranes. J. Biol. Chem. 281 (2006) 37496-37506
    • (2006) J. Biol. Chem. , vol.281 , pp. 37496-37506
    • Rostovtseva, T.K.1    Kazemi, N.2    Weinrich, M.3    Bezrukov, S.M.4
  • 95
    • 2342542370 scopus 로고    scopus 로고
    • Cell biology of cardiac mitochondrial phospholipids
    • Hatch G.M. Cell biology of cardiac mitochondrial phospholipids. Biochem. Cell Biol. 82 (2004) 99-112
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 99-112
    • Hatch, G.M.1
  • 97
    • 33846568510 scopus 로고    scopus 로고
    • Detecting the presence of membrane domains using DSC
    • Epand R.M. Detecting the presence of membrane domains using DSC. Biophys. Chem. 126 (2007) 197-200
    • (2007) Biophys. Chem. , vol.126 , pp. 197-200
    • Epand, R.M.1
  • 98
    • 0003002628 scopus 로고    scopus 로고
    • Changes in intramitochondrial cardiolipin distribution in apoptosis-resistant HCW-2 cells, derived from the human promyelocytic leukemia HL-60
    • Garcia Fernandez M., Troiano L., Moretti L., Pedrazzi J., Salvioli S., Castilla-Cortazar I., and Cossarizza A. Changes in intramitochondrial cardiolipin distribution in apoptosis-resistant HCW-2 cells, derived from the human promyelocytic leukemia HL-60. FEBS Lett. 478 (2000) 290-294
    • (2000) FEBS Lett. , vol.478 , pp. 290-294
    • Garcia Fernandez, M.1    Troiano, L.2    Moretti, L.3    Pedrazzi, J.4    Salvioli, S.5    Castilla-Cortazar, I.6    Cossarizza, A.7
  • 100
    • 0142185928 scopus 로고    scopus 로고
    • Capillary electrophoresis of cardiolipin with on-line dye interaction and spectrophotometric detection
    • Qi L., Danielson N.D., Dai Q., and Lee R.M. Capillary electrophoresis of cardiolipin with on-line dye interaction and spectrophotometric detection. Electrophoresis 24 (2003) 1680-1686
    • (2003) Electrophoresis , vol.24 , pp. 1680-1686
    • Qi, L.1    Danielson, N.D.2    Dai, Q.3    Lee, R.M.4
  • 101
    • 29244449326 scopus 로고    scopus 로고
    • Pro-apoptotic effect of maize lipid transfer protein on mammalian mitochondria
    • Crimi M., Astegno A., Zoccatelli G., and Esposti M.D. Pro-apoptotic effect of maize lipid transfer protein on mammalian mitochondria. Arch. Biochem. Biophys. 445 (2006) 65-71
    • (2006) Arch. Biochem. Biophys. , vol.445 , pp. 65-71
    • Crimi, M.1    Astegno, A.2    Zoccatelli, G.3    Esposti, M.D.4
  • 102
    • 34247482333 scopus 로고    scopus 로고
    • Cardiolipin: setting the beat of apoptosis
    • Gonzalvez F., and Gottlieb E. Cardiolipin: setting the beat of apoptosis. Apoptosis 12 (2007) 877-885
    • (2007) Apoptosis , vol.12 , pp. 877-885
    • Gonzalvez, F.1    Gottlieb, E.2
  • 103
    • 1642524332 scopus 로고    scopus 로고
    • The intra-mitochondrial cytochrome c distribution varies correlated to the formation of a complex between VDAC and the adenine nucleotide translocase: this affects Bax-dependent cytochrome c release
    • Vyssokikh M., Zorova L., Zorov D., Heimlich G., Jurgensmeier J., Schreiner D., and Brdiczka D. The intra-mitochondrial cytochrome c distribution varies correlated to the formation of a complex between VDAC and the adenine nucleotide translocase: this affects Bax-dependent cytochrome c release. Biochim. Biophys. Acta 1644 (2004) 27-36
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 27-36
    • Vyssokikh, M.1    Zorova, L.2    Zorov, D.3    Heimlich, G.4    Jurgensmeier, J.5    Schreiner, D.6    Brdiczka, D.7
  • 104
    • 0018422156 scopus 로고
    • Role of bound water in biological membrane structure: fluorescence and infrared studies
    • Schneider A.S., Middaugh C.R., and Oldewurtel M.D. Role of bound water in biological membrane structure: fluorescence and infrared studies. J. Supramol. Struct. 10 (1979) 265-275
    • (1979) J. Supramol. Struct. , vol.10 , pp. 265-275
    • Schneider, A.S.1    Middaugh, C.R.2    Oldewurtel, M.D.3
  • 105
    • 0032957027 scopus 로고    scopus 로고
    • Transbilayer movement and distribution of spin-labelled phospholipids in the inner mitochondrial membrane
    • Gallet P.F., Zachowski A., Julien R., Fellmann P., Devaux P.F., and Maftah A. Transbilayer movement and distribution of spin-labelled phospholipids in the inner mitochondrial membrane. Biochim. Biophys. Acta 1418 (1999) 61-70
    • (1999) Biochim. Biophys. Acta , vol.1418 , pp. 61-70
    • Gallet, P.F.1    Zachowski, A.2    Julien, R.3    Fellmann, P.4    Devaux, P.F.5    Maftah, A.6
  • 106
    • 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 R.M. Phospholipid scramblase 3 controls mitochondrial structure, function, and apoptotic response. Mol. Cancer Res. 1 (2003) 892-902
    • (2003) Mol. Cancer Res. , vol.1 , 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
  • 107
    • 0028338272 scopus 로고
    • Dual electron microscopic localization of mitochondrial creatine kinase in brain mitochondria
    • Kottke M., Wallimann T., and Brdiczka D. Dual electron microscopic localization of mitochondrial creatine kinase in brain mitochondria. Biochem. Med. Metab. Biol. 51 (1994) 105-117
    • (1994) Biochem. Med. Metab. Biol. , vol.51 , pp. 105-117
    • Kottke, M.1    Wallimann, T.2    Brdiczka, D.3
  • 110
    • 0035107677 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase in contact sites: interaction with porin and adenine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage
    • Dolder M., Wendt S., and Wallimann T. Mitochondrial creatine kinase in contact sites: interaction with porin and adenine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage. Biol. Signals Recept. 10 (2001) 93-111
    • (2001) Biol. Signals Recept. , vol.10 , pp. 93-111
    • Dolder, M.1    Wendt, S.2    Wallimann, T.3
  • 112
    • 0842345401 scopus 로고    scopus 로고
    • Functional coupling as a basic mechanism of feedback regulation of cardiac energy metabolism
    • Saks V.A., Kuznetsov A.V., Vendelin M., Guerrero K., Kay L., and Seppet E.K. Functional coupling as a basic mechanism of feedback regulation of cardiac energy metabolism. Mol. Cell. Biochem. 256-257 (2004) 185-199
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 185-199
    • Saks, V.A.1    Kuznetsov, A.V.2    Vendelin, M.3    Guerrero, K.4    Kay, L.5    Seppet, E.K.6
  • 113
    • 0032422634 scopus 로고    scopus 로고
    • The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition
    • Brdiczka D., Beutner G., Ruck A., Dolder M., and Wallimann T. The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition. Biofactors 8 (1998) 235-242
    • (1998) Biofactors , vol.8 , pp. 235-242
    • Brdiczka, D.1    Beutner, G.2    Ruck, A.3    Dolder, M.4    Wallimann, T.5
  • 114
    • 49649092231 scopus 로고    scopus 로고
    • The creatine kinase phosphotransfer network: thermodynamic and kinetic considerations, the impact of the mitochondrial outer membrane and modelling approaches
    • Saks V., Kaambre T., Guzun R., Anmann T., Sikk P., Schlattner U., Wallimann T., Aliev M., and Vendelin M. The creatine kinase phosphotransfer network: thermodynamic and kinetic considerations, the impact of the mitochondrial outer membrane and modelling approaches. Subcell. Biochem. 46 (2007) 27-65
    • (2007) Subcell. Biochem. , vol.46 , pp. 27-65
    • Saks, V.1    Kaambre, T.2    Guzun, R.3    Anmann, T.4    Sikk, P.5    Schlattner, U.6    Wallimann, T.7    Aliev, M.8    Vendelin, M.9
  • 115
    • 18744434646 scopus 로고
    • Cause and consequences of dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space in respect to exchange of energy rich phosphates between cytosol and mitochondria
    • Gellerich F.N., and Kunz W. Cause and consequences of dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space in respect to exchange of energy rich phosphates between cytosol and mitochondria. Biomed. Biochim. Acta 46 (1987) S545-S548
    • (1987) Biomed. Biochim. Acta , vol.46
    • Gellerich, F.N.1    Kunz, W.2
  • 116
    • 0021860981 scopus 로고
    • Creatine kinase of rat heart mitochondria. The demonstration of functional coupling to oxidative phosphorylation in an inner membrane-matrix preparation
    • Saks V.A., Kuznetsov A.V., Kupriyanov V.V., Miceli M.V., and Jacobus W.E. Creatine kinase of rat heart mitochondria. The demonstration of functional coupling to oxidative phosphorylation in an inner membrane-matrix preparation. J. Biol. Chem. 260 (1985) 7757-7764
    • (1985) J. Biol. Chem. , vol.260 , pp. 7757-7764
    • Saks, V.A.1    Kuznetsov, A.V.2    Kupriyanov, V.V.3    Miceli, M.V.4    Jacobus, W.E.5
  • 119
    • 2442681775 scopus 로고    scopus 로고
    • Use of phosphocreatine kinetics to determine the influence of creatine on muscle mitochondrial respiration: an in vivo 31P-MRS study of oral creatine ingestion
    • Smith S.A., Montain S.J., Zientara G.P., and Fielding R.A. Use of phosphocreatine kinetics to determine the influence of creatine on muscle mitochondrial respiration: an in vivo 31P-MRS study of oral creatine ingestion. J. Appl. Physiol. 96 (2004) 2288-2292
    • (2004) J. Appl. Physiol. , vol.96 , pp. 2288-2292
    • Smith, S.A.1    Montain, S.J.2    Zientara, G.P.3    Fielding, R.A.4
  • 121
  • 122
    • 38449092423 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore
    • discussion 164-9
    • Bernardi P., and Forte M. The mitochondrial permeability transition pore. Novartis Found. Symp. 287 (2007) 157-164 discussion 164-9
    • (2007) Novartis Found. Symp. , vol.287 , pp. 157-164
    • Bernardi, P.1    Forte, M.2
  • 123
    • 0034668791 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their role in cell death
    • Crompton M. Mitochondrial intermembrane junctional complexes and their role in cell death. J. Physiol. 529 Pt 1 (2000) 11-21
    • (2000) J. Physiol. , vol.529 , Issue.PART 1 , pp. 11-21
    • Crompton, M.1
  • 124
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green D.R., and Kroemer G. The pathophysiology of mitochondrial cell death. Science 305 (2004) 626-629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 125
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • Beutner G., Ruck A., Riede B., Welte W., and Brdiczka D. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 396 (1996) 189-195
    • (1996) FEBS Lett. , vol.396 , pp. 189-195
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 127
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
    • Beutner G., Ruck A., Riede B., and Brdiczka D. Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim. Biophys. Acta 1368 (1998) 7-18
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 128
    • 46349097952 scopus 로고    scopus 로고
    • Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore
    • Leung A.W., and Halestrap A.P. Recent progress in elucidating the molecular mechanism of the mitochondrial permeability transition pore. Biochim. Biophys. Acta 1777 (2008) 946-952
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 946-952
    • Leung, A.W.1    Halestrap, A.P.2
  • 129
    • 0017735164 scopus 로고
    • Nucleoside diphosphokinase of rat heart mitochondria. Dual localization in matrix and intermembrane space
    • Jacobus W.E., and Evans J.J. Nucleoside diphosphokinase of rat heart mitochondria. Dual localization in matrix and intermembrane space. J. Biol. Chem. 252 (1977) 4232-4241
    • (1977) J. Biol. Chem. , vol.252 , pp. 4232-4241
    • Jacobus, W.E.1    Evans, J.J.2
  • 130
    • 0344440701 scopus 로고    scopus 로고
    • Plant mitochondrial nucleoside diphosphate kinase is attached to the membrane through interaction with the adenine nucleotide translocator
    • Knorpp C., Johansson M., and Baird A.M. Plant mitochondrial nucleoside diphosphate kinase is attached to the membrane through interaction with the adenine nucleotide translocator. FEBS Lett. 555 (2003) 363-366
    • (2003) FEBS Lett. , vol.555 , pp. 363-366
    • Knorpp, C.1    Johansson, M.2    Baird, A.M.3
  • 131
    • 33750445482 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in mammals
    • Chan D.C. Mitochondrial fusion and fission in mammals. Annu. Rev. Cell Dev. Biol. 22 (2006) 79-99
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 79-99
    • Chan, D.C.1
  • 132
    • 33947434544 scopus 로고    scopus 로고
    • OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis
    • Olichon A., Elachouri G., Baricault L., Delettre C., Belenguer P., and Lenaers G. OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis. Cell Death Differ. 14 (2007) 682-692
    • (2007) Cell Death Differ. , vol.14 , pp. 682-692
    • Olichon, A.1    Elachouri, G.2    Baricault, L.3    Delettre, C.4    Belenguer, P.5    Lenaers, G.6
  • 134
    • 0029121016 scopus 로고
    • Mice deficient in ubiquitous mitochondrial creatine kinase are viable and fertile
    • Steeghs K., Oerlemans F., and Wieringa B. Mice deficient in ubiquitous mitochondrial creatine kinase are viable and fertile. Biochim. Biophys. Acta 1230 (1995) 130-138
    • (1995) Biochim. Biophys. Acta , vol.1230 , pp. 130-138
    • Steeghs, K.1    Oerlemans, F.2    Wieringa, B.3
  • 135
    • 49649099046 scopus 로고    scopus 로고
    • In vivo magnetic resonance spectroscopy of transgenic mice with altered expression of guanidinoacetate methyltransferase and creatine kinase isoenzymes
    • Heerschap A., Kan H.E., Nabuurs C.I., Renema W.K., Isbrandt D., and Wieringa B. In vivo magnetic resonance spectroscopy of transgenic mice with altered expression of guanidinoacetate methyltransferase and creatine kinase isoenzymes. Subcell. Biochem. 46 (2007) 119-148
    • (2007) Subcell. Biochem. , vol.46 , pp. 119-148
    • Heerschap, A.1    Kan, H.E.2    Nabuurs, C.I.3    Renema, W.K.4    Isbrandt, D.5    Wieringa, B.6
  • 136
    • 0037085252 scopus 로고    scopus 로고
    • The creatine kinase system is essential for optimal refill of the sarcoplasmic reticulum Ca2+ store in skeletal muscle
    • de Groof A.J., Fransen J.A., Errington R.J., Willems P.H., Wieringa B., and Koopman W.J. The creatine kinase system is essential for optimal refill of the sarcoplasmic reticulum Ca2+ store in skeletal muscle. J. Biol. Chem. 277 (2002) 5275-5284
    • (2002) J. Biol. Chem. , vol.277 , pp. 5275-5284
    • de Groof, A.J.1    Fransen, J.A.2    Errington, R.J.3    Willems, P.H.4    Wieringa, B.5    Koopman, W.J.6
  • 137
    • 0842323745 scopus 로고    scopus 로고
    • Mice lacking the UbCKmit isoform of creatine kinase reveal slower spatial learning acquisition, diminished exploration and habituation, and reduced acoustic startle reflex responses
    • Streijger F., Jost C.R., Oerlemans F., Ellenbroek B.A., Cools A.R., Wieringa B., and Van der Zee C.E. Mice lacking the UbCKmit isoform of creatine kinase reveal slower spatial learning acquisition, diminished exploration and habituation, and reduced acoustic startle reflex responses. Mol. Cell. Biochem. 256-257 (2004) 305-318
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 305-318
    • Streijger, F.1    Jost, C.R.2    Oerlemans, F.3    Ellenbroek, B.A.4    Cools, A.R.5    Wieringa, B.6    Van der Zee, C.E.7
  • 138
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., and Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10 (2000) 369-377
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 139
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 140
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 141
    • 1042302135 scopus 로고    scopus 로고
    • The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis
    • Iverson S.L., and Orrenius S. The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis. Arch. Biochem. Biophys. 423 (2004) 37-46
    • (2004) Arch. Biochem. Biophys. , vol.423 , pp. 37-46
    • Iverson, S.L.1    Orrenius, S.2
  • 142
    • 0037088593 scopus 로고    scopus 로고
    • Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage
    • Tuominen E.K., Wallace C.J., and Kinnunen P.K. Phospholipid-cytochrome c interaction: evidence for the extended lipid anchorage. J. Biol. Chem. 277 (2002) 8822-8826
    • (2002) J. Biol. Chem. , vol.277 , pp. 8822-8826
    • Tuominen, E.K.1    Wallace, C.J.2    Kinnunen, P.K.3
  • 143
    • 0015536161 scopus 로고
    • Cytochrome c interaction with membranes. I. Use of a fluorescent chromophore in the study of cytochrome c interaction with artificial and mitochondrial membranes
    • Vanderkooi J., Erecinska M., and Chance B. Cytochrome c interaction with membranes. I. Use of a fluorescent chromophore in the study of cytochrome c interaction with artificial and mitochondrial membranes. Arch. Biochem. Biophys. 154 (1973) 219-229
    • (1973) Arch. Biochem. Biophys. , vol.154 , pp. 219-229
    • Vanderkooi, J.1    Erecinska, M.2    Chance, B.3
  • 144
    • 1642361233 scopus 로고    scopus 로고
    • Binding and release of cytochrome c in brain mitochondria is influenced by membrane potential and hydrophobic interactions with cardiolipin
    • Piccotti L., Buratta M., Giannini S., Gresele P., Roberti R., and Corazzi L. Binding and release of cytochrome c in brain mitochondria is influenced by membrane potential and hydrophobic interactions with cardiolipin. J. Membr. Biol. 198 (2004) 43-53
    • (2004) J. Membr. Biol. , vol.198 , pp. 43-53
    • Piccotti, L.1    Buratta, M.2    Giannini, S.3    Gresele, P.4    Roberti, R.5    Corazzi, L.6
  • 145
    • 41249101827 scopus 로고    scopus 로고
    • The mitochondrial permeability transition regulates cytochrome c release for apoptosis during endoplasmic reticulum stress by remodeling the cristae junction
    • Zhang D., Lu C., Whiteman M., Chance B., and Armstrong J.S. The mitochondrial permeability transition regulates cytochrome c release for apoptosis during endoplasmic reticulum stress by remodeling the cristae junction. J. Biol. Chem. 283 (2008) 3476-3486
    • (2008) J. Biol. Chem. , vol.283 , pp. 3476-3486
    • Zhang, D.1    Lu, C.2    Whiteman, M.3    Chance, B.4    Armstrong, J.S.5
  • 146
    • 29344439984 scopus 로고    scopus 로고
    • Mitochondrial contact sites: their role in energy metabolism and apoptosis
    • Brdiczka D.G., Zorov D.B., and Sheu S.S. Mitochondrial contact sites: their role in energy metabolism and apoptosis. Biochim. Biophys. Acta 1762 (2006) 148-163
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 148-163
    • Brdiczka, D.G.1    Zorov, D.B.2    Sheu, S.S.3
  • 147
    • 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 (1985) 3821-3826
    • (1985) Biochemistry , vol.24 , pp. 3821-3826
    • Beyer, K.1    Klingenberg, M.2
  • 148
    • 0842302355 scopus 로고    scopus 로고
    • VDAC and peripheral channelling complexes in health and disease
    • Vyssokikh M., and Brdiczka D. VDAC and peripheral channelling complexes in health and disease. Mol. Cell. Biochem. 256-257 (2004) 117-126
    • (2004) Mol. Cell. Biochem. , vol.256-257 , pp. 117-126
    • Vyssokikh, M.1    Brdiczka, D.2
  • 150
  • 151
    • 33746872880 scopus 로고    scopus 로고
    • Mitochondria and cancer: is there a morphological connection?
    • Alirol E., and Martinou J.C. Mitochondria and cancer: is there a morphological connection?. Oncogene 25 (2006) 4706-4716
    • (2006) Oncogene , vol.25 , pp. 4706-4716
    • Alirol, E.1    Martinou, J.C.2
  • 152
    • 2442421118 scopus 로고    scopus 로고
    • Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria
    • Griparic L., van der Wel N.N., Orozco I.J., Peters P.J., and van der Bliek A.M. Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria. J. Biol. Chem. 279 (2004) 18792-18798
    • (2004) J. Biol. Chem. , vol.279 , pp. 18792-18798
    • Griparic, L.1    van der Wel, N.N.2    Orozco, I.J.3    Peters, P.J.4    van der Bliek, A.M.5
  • 153
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon A., Baricault L., Gas N., Guillou E., Valette A., Belenguer P., and Lenaers G. Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 278 (2003) 7743-7746
    • (2003) J. Biol. Chem. , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 154
    • 34250768073 scopus 로고    scopus 로고
    • Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis
    • Pellegrini L., Scorrano L., and cut short to death A. Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis. Cell Death Differ. 14 (2007) 1275-1284
    • (2007) Cell Death Differ. , vol.14 , pp. 1275-1284
    • Pellegrini, L.1    Scorrano, L.2    cut short to death, A.3
  • 155
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult D., Grodet A., Lee Y.J., Estaquier J., and Blackstone C. Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J. Biol. Chem. 280 (2005) 35742-35750
    • (2005) J. Biol. Chem. , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 156
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer D.D., and Ferguson-Miller S. Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112 (2003) 481-490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 157
    • 0036308059 scopus 로고    scopus 로고
    • Mitochondria, the killer organelles and their weapons
    • Ravagnan L., Roumier T., and Kroemer G. Mitochondria, the killer organelles and their weapons. J. Cell. Physiol. 192 (2002) 131-137
    • (2002) J. Cell. Physiol. , vol.192 , pp. 131-137
    • Ravagnan, L.1    Roumier, T.2    Kroemer, G.3
  • 158
    • 0037428477 scopus 로고    scopus 로고
    • Differential effects of peroxynitrite on human mitochondrial creatine kinase isoenzymes. Inactivation, octamer destabilization, and identification of involved residues
    • Wendt S., Schlattner U., and Wallimann T. Differential effects of peroxynitrite on human mitochondrial creatine kinase isoenzymes. Inactivation, octamer destabilization, and identification of involved residues. J. Biol. Chem. 278 (2003) 1125-1130
    • (2003) J. Biol. Chem. , vol.278 , pp. 1125-1130
    • Wendt, S.1    Schlattner, U.2    Wallimann, T.3
  • 159
    • 0036175343 scopus 로고    scopus 로고
    • Multiple interference of anthracyclines with mitochondrial creatine kinases: preferential damage of the cardiac isoenzyme and its implications for drug cardiotoxicity
    • Tokarska-Schlattner M., Wallimann T., and Schlattner U. Multiple interference of anthracyclines with mitochondrial creatine kinases: preferential damage of the cardiac isoenzyme and its implications for drug cardiotoxicity. Mol. Pharmacol. 61 (2002) 516-523
    • (2002) Mol. Pharmacol. , vol.61 , pp. 516-523
    • Tokarska-Schlattner, M.1    Wallimann, T.2    Schlattner, U.3
  • 161
    • 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 F.M. 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 (2000) 323-326
    • (2000) FEBS Lett. , vol.466 , pp. 323-326
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 162
    • 0035851186 scopus 로고    scopus 로고
    • Decreased cardiolipin synthesis corresponds with cytochrome c release in palmitate-induced cardiomyocyte apoptosis
    • Ostrander D.B., Sparagna G.C., Amoscato A.A., McMillin J.B., and Dowhan W. Decreased cardiolipin synthesis corresponds with cytochrome c release in palmitate-induced cardiomyocyte apoptosis. J. Biol. Chem. 276 (2001) 38061-38067
    • (2001) J. Biol. Chem. , vol.276 , pp. 38061-38067
    • Ostrander, D.B.1    Sparagna, G.C.2    Amoscato, A.A.3    McMillin, J.B.4    Dowhan, W.5
  • 163
    • 0033595780 scopus 로고    scopus 로고
    • Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation
    • Shidoji Y., Hayashi K., Komura S., Ohishi N., and Yagi K. Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation. Biochem. Biophys. Res. Commun. 264 (1999) 343-347
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 343-347
    • Shidoji, Y.1    Hayashi, K.2    Komura, S.3    Ohishi, N.4    Yagi, K.5
  • 166
    • 4744373181 scopus 로고    scopus 로고
    • Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria
    • Chang T.S., Cho C.S., Park S., Yu S., Kang S.W., and Rhee S.G. Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria. J. Biol. Chem. 279 (2004) 41975-41984
    • (2004) J. Biol. Chem. , vol.279 , pp. 41975-41984
    • Chang, T.S.1    Cho, C.S.2    Park, S.3    Yu, S.4    Kang, S.W.5    Rhee, S.G.6
  • 167
    • 0034306791 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis
    • Nomura K., Imai H., Koumura T., Kobayashi T., and Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis. Biochem. J. 351 (2000) 183-193
    • (2000) Biochem. J. , vol.351 , pp. 183-193
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Kobayashi, T.4    Nakagawa, Y.5
  • 169
    • 0015761138 scopus 로고
    • Correlations between structure and spectroscopic properties in membrane model system. Fluorescence and circular dichroism of the cytochrome c-cardiolipin system
    • Letellier L., and Shechter E. Correlations between structure and spectroscopic properties in membrane model system. Fluorescence and circular dichroism of the cytochrome c-cardiolipin system. Eur. J. Biochem. 40 (1973) 507-512
    • (1973) Eur. J. Biochem. , vol.40 , pp. 507-512
    • Letellier, L.1    Shechter, E.2
  • 170
    • 0035808391 scopus 로고    scopus 로고
    • Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces. A CD and EPR investigation
    • Nantes I.L., Zucchi M.R., Nascimento O.R., and Faljoni-Alario A. Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces. A CD and EPR investigation. J. Biol. Chem. 276 (2001) 153-158
    • (2001) J. Biol. Chem. , vol.276 , pp. 153-158
    • Nantes, I.L.1    Zucchi, M.R.2    Nascimento, O.R.3    Faljoni-Alario, A.4
  • 171
    • 0028080126 scopus 로고
    • The interaction of horse heart cytochrome c with phospholipid bilayers. Structural and dynamic effects
    • Pinheiro T.J. The interaction of horse heart cytochrome c with phospholipid bilayers. Structural and dynamic effects. Biochimie 76 (1994) 489-500
    • (1994) Biochimie , vol.76 , pp. 489-500
    • Pinheiro, T.J.1
  • 172
    • 0037195257 scopus 로고    scopus 로고
    • Peroxidase activity as a tool for studying the folding of c-type cytochromes
    • Diederix R.E., Ubbink M., and Canters G.W. Peroxidase activity as a tool for studying the folding of c-type cytochromes. Biochemistry 41 (2002) 13067-13077
    • (2002) Biochemistry , vol.41 , pp. 13067-13077
    • Diederix, R.E.1    Ubbink, M.2    Canters, G.W.3
  • 177
    • 39149098440 scopus 로고    scopus 로고
    • Interplay between bax, reactive oxygen species production, and cardiolipin oxidation during apoptosis
    • Jiang J., Huang Z., Zhao Q., Feng W., Belikova N.A., and Kagan V.E. Interplay between bax, reactive oxygen species production, and cardiolipin oxidation during apoptosis. Biochem. Biophys. Res. Commun. 368 (2008) 145-150
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 145-150
    • Jiang, J.1    Huang, Z.2    Zhao, Q.3    Feng, W.4    Belikova, N.A.5    Kagan, V.E.6
  • 178
    • 52449104836 scopus 로고    scopus 로고
    • VDAC regulation: role of cytosolic proteins and mitochondrial lipids
    • Rostovtseva T.K., and Bezrukov S.M. VDAC regulation: role of cytosolic proteins and mitochondrial lipids. J. Bioenerg. Biomembr. 40 (2008) 163-170
    • (2008) J. Bioenerg. Biomembr. , vol.40 , pp. 163-170
    • Rostovtseva, T.K.1    Bezrukov, S.M.2
  • 179
    • 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 (2000) 754-761
    • (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
  • 180
    • 4344661748 scopus 로고    scopus 로고
    • The cardiolipin-binding domain of Bid affects mitochondrial respiration and enhances cytochrome c release
    • Liu J., Weiss A., Durrant D., Chi N.W., and Lee R.M. The cardiolipin-binding domain of Bid affects mitochondrial respiration and enhances cytochrome c release. Apoptosis 9 (2004) 533-541
    • (2004) Apoptosis , vol.9 , pp. 533-541
    • Liu, J.1    Weiss, A.2    Durrant, D.3    Chi, N.W.4    Lee, R.M.5
  • 183
    • 0348038751 scopus 로고    scopus 로고
    • Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death
    • Esposti M.D., Cristea I.M., Gaskell S.J., Nakao Y., and Dive C. Proapoptotic Bid binds to monolysocardiolipin, a new molecular connection between mitochondrial membranes and cell death. Cell Death Differ. 10 (2003) 1300-1309
    • (2003) Cell Death Differ. , vol.10 , pp. 1300-1309
    • Esposti, M.D.1    Cristea, I.M.2    Gaskell, S.J.3    Nakao, Y.4    Dive, C.5
  • 185
    • 35549010278 scopus 로고    scopus 로고
    • Reduced creatine-stimulated respiration in doxorubicin challenged mitochondria: particular sensitivity of the heart
    • Tokarska-Schlattner M., Dolder M., Gerber I., Speer O., Wallimann T., and Schlattner U. Reduced creatine-stimulated respiration in doxorubicin challenged mitochondria: particular sensitivity of the heart. Biochim. Biophys. Acta 1767 (2007) 1276-1284
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1276-1284
    • Tokarska-Schlattner, M.1    Dolder, M.2    Gerber, I.3    Speer, O.4    Wallimann, T.5    Schlattner, U.6
  • 186
    • 18744374204 scopus 로고    scopus 로고
    • The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites
    • Lutter M., Perkins G.A., and Wang X. The pro-apoptotic Bcl-2 family member tBid localizes to mitochondrial contact sites. BMC Cell Biol. 2 (2001) 22
    • (2001) BMC Cell Biol. , vol.2 , pp. 22
    • Lutter, M.1    Perkins, G.A.2    Wang, X.3
  • 188
    • 0037458090 scopus 로고    scopus 로고
    • Apoptosis: mitochondrial membrane permeabilization - the (w)hole story?
    • Zamzami N., and Kroemer G. Apoptosis: mitochondrial membrane permeabilization - the (w)hole story?. Curr. Biol. 13 (2003) R71-R73
    • (2003) Curr. Biol. , vol.13
    • Zamzami, N.1    Kroemer, G.2
  • 190
    • 33845580062 scopus 로고    scopus 로고
    • Monolysocardiolipin in cultured fibroblasts is a sensitive and specific marker for Barth Syndrome
    • van Werkhoven M.A., Thorburn D.R., Gedeon A.K., and Pitt J.J. Monolysocardiolipin in cultured fibroblasts is a sensitive and specific marker for Barth Syndrome. J. Lipid Res. 47 (2006) 2346-2351
    • (2006) J. Lipid Res. , vol.47 , pp. 2346-2351
    • van Werkhoven, M.A.1    Thorburn, D.R.2    Gedeon, A.K.3    Pitt, J.J.4
  • 192
    • 33748347104 scopus 로고    scopus 로고
    • Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria
    • Chen D., Zhang X.Y., and Shi Y. Identification and functional characterization of hCLS1, a human cardiolipin synthase localized in mitochondria. Biochem. J. 398 (2006) 169-176
    • (2006) Biochem. J. , vol.398 , pp. 169-176
    • Chen, D.1    Zhang, X.Y.2    Shi, Y.3
  • 193
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum G. Lipids of mitochondria. Biochim. Biophys. Acta 822 (1985) 1-42
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 194
    • 23744478870 scopus 로고    scopus 로고
    • Give lipids a START: the StAR-related lipid transfer (START) domain in mammals
    • Alpy F., and Tomasetto C. Give lipids a START: the StAR-related lipid transfer (START) domain in mammals. J. Cell Sci. 118 (2005) 2791-2801
    • (2005) J. Cell Sci. , vol.118 , pp. 2791-2801
    • Alpy, F.1    Tomasetto, C.2
  • 195
    • 0025296914 scopus 로고
    • Lipid transfer in plants
    • Arondel V., and Kader J.C. Lipid transfer in plants. Experientia 46 (1990) 579-585
    • (1990) Experientia , vol.46 , pp. 579-585
    • Arondel, V.1    Kader, J.C.2
  • 197
    • 0034795258 scopus 로고    scopus 로고
    • Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity
    • Esposti M.D., Erler J.T., Hickman J.A., and Dive C. Bid, a widely expressed proapoptotic protein of the Bcl-2 family, displays lipid transfer activity. Mol. Cell. Biol. 21 (2001) 7268-7276
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7268-7276
    • Esposti, M.D.1    Erler, J.T.2    Hickman, J.A.3    Dive, C.4
  • 198
    • 0037085029 scopus 로고    scopus 로고
    • Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins
    • Degli Esposti M. Sequence and functional similarities between pro-apoptotic Bid and plant lipid transfer proteins. Biochim. Biophys. Acta 1553 (2002) 331-340
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 331-340
    • Degli Esposti, M.1
  • 199
    • 0023231498 scopus 로고
    • Regulation of mitochondrial hexokinase in cultured HT 29 human cancer cells. An ultrastructural and biochemical study
    • Denis-Pouxviel C., Riesinger I., Buhler C., Brdiczka D., and Murat J.C. Regulation of mitochondrial hexokinase in cultured HT 29 human cancer cells. An ultrastructural and biochemical study. Biochim. Biophys. Acta 902 (1987) 335-348
    • (1987) Biochim. Biophys. Acta , vol.902 , pp. 335-348
    • Denis-Pouxviel, C.1    Riesinger, I.2    Buhler, C.3    Brdiczka, D.4    Murat, J.C.5
  • 200
    • 0041309460 scopus 로고    scopus 로고
    • Hexokinase II: the integration of energy metabolism and control of apoptosis
    • Pastorino J.G., and Hoek J.B. Hexokinase II: the integration of energy metabolism and control of apoptosis. Curr. Med. Chem. 10 (2003) 1535-1551
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1535-1551
    • Pastorino, J.G.1    Hoek, J.B.2
  • 201
    • 0347481136 scopus 로고    scopus 로고
    • Transbilayer lipid diffusion promoted by Bax: implications for apoptosis
    • Epand R.F., Martinou J.C., Montessuit S., and Epand R.M. Transbilayer lipid diffusion promoted by Bax: implications for apoptosis. Biochemistry 42 (2003) 14576-14582
    • (2003) Biochemistry , vol.42 , pp. 14576-14582
    • Epand, R.F.1    Martinou, J.C.2    Montessuit, S.3    Epand, R.M.4
  • 202
    • 0037444392 scopus 로고    scopus 로고
    • Phospholipid scramblase 3 is the mitochondrial target of protein kinase C delta-induced apoptosis
    • Liu J., Chen J., Dai Q., and Lee R.M. Phospholipid scramblase 3 is the mitochondrial target of protein kinase C delta-induced apoptosis. Cancer Res. 63 (2003) 1153-1156
    • (2003) Cancer Res. , vol.63 , pp. 1153-1156
    • Liu, J.1    Chen, J.2    Dai, Q.3    Lee, R.M.4
  • 204
    • 0032562186 scopus 로고    scopus 로고
    • Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids
    • Zhou Q., Sims P.J., and Wiedmer T. Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry 37 (1998) 2356-2360
    • (1998) Biochemistry , vol.37 , pp. 2356-2360
    • Zhou, Q.1    Sims, P.J.2    Wiedmer, T.3
  • 205
    • 42049102578 scopus 로고    scopus 로고
    • Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis
    • Liu J., Epand R.F., Durrant D., Grossman D., Chi N.W., Epand R.M., and Lee R.M. Role of phospholipid scramblase 3 in the regulation of tumor necrosis factor-alpha-induced apoptosis. Biochemistry 47 (2008) 4518-4529
    • (2008) Biochemistry , vol.47 , pp. 4518-4529
    • Liu, J.1    Epand, R.F.2    Durrant, D.3    Grossman, D.4    Chi, N.W.5    Epand, R.M.6    Lee, R.M.7
  • 206
    • 33846287596 scopus 로고    scopus 로고
    • Phospholipid scramblase-3 regulates cardiolipin de novo biosynthesis and its resynthesis in growing HeLa cells
    • Van Q., Liu J., Lu B., Feingold K.R., Shi Y., Lee R.M., and Hatch G.M. Phospholipid scramblase-3 regulates cardiolipin de novo biosynthesis and its resynthesis in growing HeLa cells. Biochem. J. 401 (2007) 103-109
    • (2007) Biochem. J. , vol.401 , pp. 103-109
    • Van, Q.1    Liu, J.2    Lu, B.3    Feingold, K.R.4    Shi, Y.5    Lee, R.M.6    Hatch, G.M.7
  • 207
    • 46549087800 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3
    • Ndebele K., Gona P., Jin T.G., Benhaga N., Chalah A., Degli-Esposti M., and Khosravi-Far R. Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) induced mitochondrial pathway to apoptosis and caspase activation is potentiated by phospholipid scramblase-3. Apoptosis 13 (2008) 845-856
    • (2008) Apoptosis , vol.13 , pp. 845-856
    • Ndebele, K.1    Gona, P.2    Jin, T.G.3    Benhaga, N.4    Chalah, A.5    Degli-Esposti, M.6    Khosravi-Far, R.7
  • 209
    • 34547911748 scopus 로고    scopus 로고
    • Phosphorylation of mitochondrial phospholipid scramblase 3 by protein kinase C-delta induces its activation and facilitates mitochondrial targeting of tBid
    • He Y., Liu J., Grossman D., Durrant D., Sweatman T., Lothstein L., Epand R.F., Epand R.M., and Lee R.M. Phosphorylation of mitochondrial phospholipid scramblase 3 by protein kinase C-delta induces its activation and facilitates mitochondrial targeting of tBid. J. Cell. Biochem. 101 (2007) 1210-1221
    • (2007) J. Cell. Biochem. , vol.101 , pp. 1210-1221
    • He, Y.1    Liu, J.2    Grossman, D.3    Durrant, D.4    Sweatman, T.5    Lothstein, L.6    Epand, R.F.7    Epand, R.M.8    Lee, R.M.9
  • 210
    • 0034536628 scopus 로고    scopus 로고
    • Divergent enzyme kinetics and structural properties of the two human mitochondrial creatine kinase isoenzymes
    • Schlattner U., Eder M., Dolder M., Khuchua Z.A., Strauss A.W., and Wallimann T. Divergent enzyme kinetics and structural properties of the two human mitochondrial creatine kinase isoenzymes. Biol. Chem. 381 (2000) 1063-1070
    • (2000) Biol. Chem. , vol.381 , pp. 1063-1070
    • Schlattner, U.1    Eder, M.2    Dolder, M.3    Khuchua, Z.A.4    Strauss, A.W.5    Wallimann, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.