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Volumn 1808, Issue 4, 2011, Pages 1129-1139

Acyl chain composition determines cardiolipin clustering induced by mitochondrial creatine kinase binding to monolayers

Author keywords

Acyl chain composition; Brewster angle microscopy; Cardiolipin; Langmuir monolayer; Lipid domain; Mitochondrial creatine kinase

Indexed keywords

CARDIOLIPIN; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; LAURDAN; MITOCHONDRIAL CREATINE KINASE;

EID: 79751529136     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.01.005     Document Type: Article
Times cited : (12)

References (59)
  • 1
    • 0034193996 scopus 로고    scopus 로고
    • The biosynthesis and functional role of cardiolipin
    • M. Schlame, D. Rua, M.L. Greenberg, 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
  • 2
    • 34247482333 scopus 로고    scopus 로고
    • Cardiolipin: Setting the beat of apoptosis
    • DOI 10.1007/s10495-007-0718-8, Special Issue on Mitochondria in Apoptosis
    • F. Gonzalvez, E. Gottlieb, Cardiolipin: setting the beat of apoptosis, Apoptosis 12 (2007) 877-885. (Pubitemid 46653287)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 877-885
    • Gonzalvez, F.1    Gottlieb, E.2
  • 4
    • 0025780260 scopus 로고
    • Analysis of cardiolipin molecular species by high-performance liquid chromatography of its derivative 1, 3-bisphosphatidyl-2-benzoyl-sn-glycerol dimethyl ester
    • M. Schlame, D. Otten, Analysis of cardiolipin molecular species by high-performance liquid chromatography of its derivative 1, 3-bisphosphatidyl-2- benzoyl-sn-glycerol dimethyl ester, Anal. Biochem. 195 (1991) 290-295.
    • (1991) Anal. Biochem. , vol.195 , pp. 290-295
    • Schlame, M.1    Otten, D.2
  • 6
    • 0023147598 scopus 로고
    • Only one of the two interconvertible forms of mitochondrial creatine kinase binds to heart mitoplasts
    • O. Marcillat, D. Goldschmidt, D. Eichenberger, C. Vial, Only one of the two interconvertible forms of mitochondrial creatine kinase binds to heart mitoplasts, Biochim. Biophys. Acta 890 (1987) 233-241.
    • (1987) Biochim. Biophys. Acta , vol.890 , pp. 233-241
    • Marcillat, O.1    Goldschmidt, D.2    Eichenberger, D.3    Vial, C.4
  • 7
    • 0015926899 scopus 로고
    • The localization of mitochondrial creatine kinase, and its use for the determination of the sidedness of submitochondrial particles
    • H.R. Scholte, P.J. Weijers, E.M. Wit-Peeters, The localization of mitochondrial creatine kinase, and its use for the determination of the sidedness of submitochondrial particles, Biochim. Biophys. Acta 291 (1973) 764-773.
    • (1973) Biochim. Biophys. Acta , vol.291 , pp. 764-773
    • Scholte, H.R.1    Weijers, P.J.2    Wit-Peeters, E.M.3
  • 8
    • 0015444810 scopus 로고
    • Membranes creatine kinase (E.C.2.7.3.2.) in pig heart mitochondria properties and role in phosphate potential regulation
    • C. Vial, C. Godinot, D. Gautheron, Membranes creatine kinase (E.C.2.7.3.2.) in pig heart mitochondria properties and role in phosphate potential regulation, Biochimie 54 (1972) 843-852.
    • (1972) Biochimie , vol.54 , pp. 843-852
    • Vial, C.1    Godinot, C.2    Gautheron, D.3
  • 9
    • 0021895146 scopus 로고
    • Cardiolipin is the membrane receptor for mitochondrial creatine phosphokinase
    • M. Muller, R. Moser, D. Cheneval, E. Carafoli, 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
  • 10
    • 0022343950 scopus 로고
    • Association of creatine kinase with rat heart mitochondria: High and low affinity binding sites and the involvement of phospholipids
    • M. Schlame, W. Augustin, 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
  • 12
    • 78649325209 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion
    • O. Maniti, M.F. Lecompte, O. Marcillat, C. Vial and T. Granjon, Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion, Eur Biophys J 39 1649-1655.
    • Eur Biophys J , vol.39 , pp. 1649-1655
    • Maniti, O.1    Lecompte, M.F.2    Marcillat, O.3    Vial, C.4    Granjon, T.5
  • 13
    • 0025209799 scopus 로고
    • Immunological determination of the oligomeric form of mitochondrial creatine kinase in situ
    • DOI 10.1016/0014-5793(90)80209-2
    • E. Quemeneur, D. Eichenberger, C. Vial, Immunological determination of the oligomeric form of mitochondrial creatine kinase in situ, FEBS Lett. 262 (1990) 275-278. (Pubitemid 20104316)
    • (1990) FEBS Letters , vol.262 , Issue.2 , pp. 275-278
    • Quemeneur, E.1    Eichenberger, D.2    Vial, C.3
  • 14
    • 0022900823 scopus 로고
    • Interaction of creatine kinase with phosphorylating rabbit heart mitochondria and mitoplasts
    • C. Vial, O. Marcillat, D. Goldschmidt, B. Font, D. Eichenberger, Interaction of creatine kinase with phosphorylating rabbit heart mitochondria and mitoplasts, Arch. Biochem. Biophys. 251 (1986) 558-566. (Pubitemid 17234252)
    • (1986) Archives of Biochemistry and Biophysics , vol.251 , Issue.2 , pp. 558-566
    • Vial, C.1    Marcillat, O.2    Goldschmidt, D.3
  • 15
    • 0022639829 scopus 로고
    • Affinity modification of creatine kinase and ATP-ADP translocase in heart mitochondria: Determination of their molar stoichiometry
    • A.V. Kuznetsov, V.A. Saks, Affinity modification of creatine kinase and ATP-ADP translocase in heart mitochondria: determination of their molar stoichiometry, Biochem. Biophys. Res. Commun. 134 (1986) 359-366. (Pubitemid 16145342)
    • (1986) Biochemical and Biophysical Research Communications , vol.134 , Issue.1 , pp. 359-366
    • Kuznetsov, A.V.1    Saks, V.A.2
  • 16
    • 0016734199 scopus 로고
    • Purification of the carboxy-atractylate binding protein from mitochondria
    • P. Riccio, H. Aquila, M. Klingenberg, Purification of the carboxy-atractylate binding protein from mitochondria, FEBS Lett. 56 (1975) 133.
    • (1975) FEBS Lett. , vol.56 , pp. 133
    • Riccio, P.1    Aquila, H.2    Klingenberg, M.3
  • 17
    • 31344455097 scopus 로고    scopus 로고
    • Proteomic analysis of mitochondrial protein turnover: Identification of novel substrate proteins of the matrix protease Pim1
    • DOI 10.1128/MCB.26.3.762-776.2006
    • T. Major, B. von Janowsky, T. Ruppert, A. Mogk, W. Voos, Proteomic analysis of mitochondrial protein turnover: identification of novel substrate proteins of the matrix protease pim1, Mol. Cell. Biol. 26 (2006) 762-776. (Pubitemid 43146474)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.3 , pp. 762-776
    • Major, T.1    Von Janowsky, B.2    Ruppert, T.3    Mogk, A.4    Voos, W.5
  • 18
    • 0023686353 scopus 로고
    • Mitochondrial boundary membrane contact sites in brain: Points of hexokinase and creatine kinase location, and control of Ca2+ transport
    • M. Kottke, V. Adams, I. Riesinger, G. Bremm, W. Bosch, D. Brdiczka, G. Sandri, E. Panfili, Mitochondrial boundary membrane contact sites in brain: points of hexokinase and creatine kinase location, and control of Ca2+ transport, Biochim. Biophys. Acta 935 (1988) 87-102.
    • (1988) Biochim. Biophys. Acta , vol.935 , pp. 87-102
    • Kottke, M.1    Adams, V.2    Riesinger, I.3    Bremm, G.4    Bosch, W.5    Brdiczka, D.6    Sandri, G.7    Panfili, E.8
  • 19
    • 0026078044 scopus 로고
    • Location and regulation of octameric mitochondrial creatine kinase in the contact sites
    • M. Kottke, V. Adams, T. Wallimann, V.K. Nalam, D. Brdiczka, Location and regulation of octameric mitochondrial creatine kinase in the contact sites, Biochim. Biophys. Acta 1061 (1991) 215-225.
    • (1991) Biochim. Biophys. Acta , vol.1061 , pp. 215-225
    • Kottke, M.1    Adams, V.2    Wallimann, T.3    Nalam, V.K.4    Brdiczka, D.5
  • 20
    • 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
    • G. Beutner, A. Ruck, B. Riede, D. Brdiczka, 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
  • 21
    • 0032422634 scopus 로고    scopus 로고
    • The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition
    • D. Brdiczka, G. Beutner, A. Ruck, M. Dolder, T. Wallimann, The molecular structure of mitochondrial contact sites. Their role in regulation of energy metabolism and permeability transition, Biofactors 8 (1998) 235-242. (Pubitemid 29021354)
    • (1998) BioFactors , vol.8 , Issue.3-4 , pp. 235-242
    • Brdiczka, D.1    Beutner, G.2    Ruck, A.3    Dolder, M.4    Wallimann, T.5
  • 22
    • 0028034636 scopus 로고
    • In vitro complex formation between the octamer of mitochondrial creatine kinase and porin
    • D. Brdiczka, P. Kaldis, T. Wallimann, In vitro complex formation between the octamer of mitochondrial creatine kinase and porin, J. Biol. Chem. 269 (1994) 27640-27644.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 23
    • 0038381490 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation
    • DOI 10.1074/jbc.M208705200
    • M. Dolder, B. Walzel, O. Speer, U. Schlattner, T. Wallimann, Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation, J. Biol. Chem. 278 (2003) 17760-17766. (Pubitemid 36799379)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 17760-17766
    • Dolder, M.1    Walzel, B.2    Speer, O.3    Schlattner, U.4    Wallimann, T.5
  • 24
    • 12844260125 scopus 로고    scopus 로고
    • Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane
    • DOI 10.1042/BJ20040386
    • O. Speer, N. Back, T. Buerklen, D. Brdiczka, A. Koretsky, T. Wallimann, O. Eriksson, Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane, Biochem. J. 385 (2005) 445-450. (Pubitemid 40165077)
    • (2005) Biochemical Journal , vol.385 , Issue.2 , pp. 445-450
    • Speer, O.1    Back, N.2    Buerklen, T.3    Brdiczka, D.4    Koretsky, A.5    Wallimann, T.6    Eriksson, O.7
  • 26
    • 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
    • DOI 10.1021/bi002293e
    • T. Granjon, M.J. Vacheron, C. Vial, R. Buchet, 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. (Pubitemid 32466304)
    • (2001) Biochemistry , vol.40 , Issue.20 , pp. 6016-6026
    • Granjon, T.1    Vacheron, M.-J.2    Vial, C.3    Buchet, R.4
  • 28
    • 66149106292 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation
    • O. Maniti, M.F. Lecompte, O. Marcillat, B. Desbat, R. Buchet, C. Vial, T. Granjon, Mitochondrial creatine kinase binding to phospholipid monolayers induces cardiolipin segregation, Biophys. J. 96 (2009) 2428-2438.
    • (2009) Biophys. J. , vol.96 , pp. 2428-2438
    • Maniti, O.1    Lecompte, M.F.2    Marcillat, O.3    Desbat, B.4    Buchet, R.5    Vial, C.6    Granjon, T.7
  • 31
    • 0033213586 scopus 로고    scopus 로고
    • Cloning, Escherichia coli expression, and phase-transition chromatography-based purification of recombinant rabbit heart mitochondrial creatine kinase
    • O. Marcillat, C. Perraut, T. Granjon, C. Vial, M.J. Vacheron, Cloning, Escherichia coli expression, and phase-transition chromatography-based purification of recombinant rabbit heart mitochondrial creatine kinase, Prot. Expr. Purif. 17 (1999) 163-168.
    • (1999) Prot. Expr. Purif. , vol.17 , pp. 163-168
    • Marcillat, O.1    Perraut, C.2    Granjon, T.3    Vial, C.4    Vacheron, M.J.5
  • 32
    • 0020714669 scopus 로고
    • Effects of SH group reagents on creatine kinase interaction with the mitochondrial membrane
    • B. Font, C. Vial, D. Goldschmidt, D. Eichenberger, D.C. Gautheron, Effects of SH group reagents on creatine kinase interaction with the mitochondrial membrane, Arch. Biochem. Biophys. 220 (1983) 541-548.
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 541-548
    • Font, B.1    Vial, C.2    Goldschmidt, D.3    Eichenberger, D.4    Gautheron, D.C.5
  • 33
    • 0011379718 scopus 로고
    • Direct visualization of monolayers at the air-water interface by Brewster angle microscopy
    • D. Hönig, D. Möbius, Direct visualization of monolayers at the air-water interface by Brewster angle microscopy, J. Phys. Chem. 95 (12) (1991) 4590-4592.
    • (1991) J. Phys. Chem. , vol.95 , Issue.12 , pp. 4590-4592
    • Hönig, D.1    Möbius, D.2
  • 34
    • 25944442748 scopus 로고
    • Microscope at the Brewster angle: Direct observation of first-order phase transitions in monolayers
    • S. Henon, J. Meunier, Microscope at the Brewster angle: direct observation of first-order phase transitions in monolayers, Rev. Sci. Instrum. 62 (1991) 936-939.
    • (1991) Rev. Sci. Instrum. , vol.62 , pp. 936-939
    • Henon, S.1    Meunier, J.2
  • 35
    • 0039136059 scopus 로고    scopus 로고
    • Structural and morphological characteristics of [beta]-casein monolayers at the air-water interface
    • J.M. Rodriguez Patino, C.C. Sanchez, M.R. Rodriguez Nino, Structural and morphological characteristics of [beta]-casein monolayers at the air-water interface, Food Hydrocolloids 13 (1999) 401.
    • (1999) Food Hydrocolloids , vol.13 , pp. 401
    • Rodriguez Patino, J.M.1    Sanchez, C.C.2    Rodriguez Nino, M.R.3
  • 36
    • 0041025996 scopus 로고    scopus 로고
    • Morphological and structural characteristics of monoglyceride monolayers at the air-water interface observed by Brewster angle microscopy
    • J.M. Rodriguez Patino, C. Carrera Sanchez, M.R. Rodriguez Nino, Morphological and structural characteristics of monoglyceride monolayers at the air-water interface observed by Brewster angle microscopy, Langmuir 15 (1999) 2484-2492.
    • (1999) Langmuir , vol.15 , pp. 2484-2492
    • Rodriguez Patino, J.M.1    Carrera Sanchez, C.2    Rodriguez Nino, M.R.3
  • 37
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • P.K. Glasoe, F.A. Long, Use of glass electrodes to measure acidities in deuterium oxide, J. Phys. Chem. (1960) 188-190.
    • (1960) J. Phys. Chem. , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 38
    • 0000110909 scopus 로고
    • Equilibrium properties of electrified interphases
    • J.O.M. Bockris, B.E. Conway (Eds.) Butterworths, London, Chapter 3
    • R. Parsons, Equilibrium properties of electrified interphases, in: J.O.M. Bockris, B.E. Conway (Eds.), Modern Aspects of Electrochemistry, Butterworths, London, 1954,, Chapter 3.
    • (1954) Modern Aspects of Electrochemistry
    • Parsons, R.1
  • 39
    • 0027957287 scopus 로고
    • Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids
    • M.F. Lecompte, G. Bouix, K.G. Mann, Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids, J. Biol. Chem. 269 (1994) 1905-1910.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1905-1910
    • Lecompte, M.F.1    Bouix, G.2    Mann, K.G.3
  • 40
    • 0032542013 scopus 로고    scopus 로고
    • Binding steps of apolipoprotein A-I with phospholipid monolayers: Adsorption and penetration
    • DOI 10.1021/bi9813072
    • M.F. Lecompte, A.C. Bras, N. Dousset, I. Portas, R. Salvayre, M. Ayrault-Jarrier, Binding steps of apolipoprotein A-I with phospholipid monolayers: adsorption and penetration, Biochemistry 37 (1998) 16165-16171. (Pubitemid 28536252)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16165-16171
    • Lecompte, M.-F.1    Bras, A.-C.2    Dousset, N.3    Portas, I.4    Salvayre, R.5    Ayrault-Jarrier, M.6
  • 41
    • 24144464238 scopus 로고    scopus 로고
    • Effect of 4-hydroxynonenal on phosphatidylethanolamine containing condensed monolayer and on its interaction with apolipoprotein A-I
    • DOI 10.1016/j.febslet.2005.07.086, PII S0014579305009592
    • M.F. Lecompte, J. Clavilier, C. Rolland, X. Collet, A. Negre-Salvayre, R. Salvayre, Effect of 4-hydroxynonenal on phosphatidylethanolamine containing condensed monolayer and on its interaction with apolipoprotein A-I, FEBS Lett. 579 (2005) 5074-5078. (Pubitemid 41242855)
    • (2005) FEBS Letters , vol.579 , Issue.22 , pp. 5074-5078
    • Lecompte, M.-F.1    Clavilier, J.2    Rolland, C.3    Collet, X.4    Negre-Salvayre, A.5    Salvayre, R.6
  • 42
    • 23144449807 scopus 로고    scopus 로고
    • Interaction of an amphitropic protein (factor Xa) with membrane models in a complex system
    • M.F. Lecompte, Interaction of an amphitropic protein (factor Xa) with membrane models in a complex system, Biochim. Biophys. Acta 1724 (2005) 307-314.
    • (2005) Biochim. Biophys. Acta , vol.1724 , pp. 307-314
    • Lecompte, M.F.1
  • 45
    • 0033957859 scopus 로고    scopus 로고
    • Ideally amphipathic beta-sheeted peptides at interfaces: Structure, orientation, affinities for lipids and hemolytic activity of (KL)(m)K peptides
    • DOI 10.1016/S0005-2736(99)00175-3, PII S0005273699001753
    • S. Castano, B. Desbat, J. Dufourcq, Ideally amphipathic beta-sheeted peptides at interfaces: structure, orientation, affinities for lipids and hemolytic activity of (KL) (m)K peptides, Biochim. Biophys. Acta 1463 (2000) 65-80. (Pubitemid 30019236)
    • (2000) Biochimica et Biophysica Acta - Biomembranes , vol.1463 , Issue.1 , pp. 65-80
    • Castano, S.1    Desbat, B.2    Dufourcq, J.3
  • 46
    • 0032952095 scopus 로고    scopus 로고
    • Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic L(i)K(j)(i=2j) peptides
    • DOI 10.1016/S0005-2736(98)00220-X, PII S000527369800220X
    • S. Castano, B. Desbat, M. Laguerre, J. Dufourcq, Structure, orientation and affinity for interfaces and lipids of ideally amphipathic lytic LiKj(i=2j) peptides, Biochim. Biophys. Acta 1416 (1999) 176-194. (Pubitemid 29065435)
    • (1999) Biochimica et Biophysica Acta - Biomembranes , vol.1416 , Issue.1-2 , pp. 176-194
    • Castano, S.1    Desbat, B.2    Laguerre, M.3    Dufourcq, J.4
  • 47
    • 0000968060 scopus 로고
    • Ellipsometric study of the physical states of phosphatidylcholines at the air-water interface
    • D. Ducharme, J.J. Max, C. Salesse, R.M. Leblanc, Ellipsometric study of the physical states of phosphatidylcholines at the air-water interface, J. Phys. Chem. 94 (1990) 1925-1932.
    • (1990) J. Phys. Chem. , vol.94 , pp. 1925-1932
    • Ducharme, D.1    Max, J.J.2    Salesse, C.3    Leblanc, R.M.4
  • 48
    • 0033212099 scopus 로고    scopus 로고
    • A model for the interaction of 6-lauroyl-2-(N, N-dimethylamino) naphthalene with lipid environments: Implications for spectral properties
    • L.A. Bagatolli, T. Parasassi, G.D. Fidelio, E. Gratton, A model for the interaction of 6-lauroyl-2-(N, N-dimethylamino)naphthalene with lipid environments: implications for spectral properties, Photochem. Photobiol. 70 (1999) 557-564.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 557-564
    • Bagatolli, L.A.1    Parasassi, T.2    Fidelio, G.D.3    Gratton, E.4
  • 49
    • 0022647019 scopus 로고
    • Time-resolved fluorescence emission spectra of Laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry
    • T. Parasassi, F. Conti, E. Gratton, Time-resolved fluorescence emission spectra of Laurdan in phospholipid vesicles by multifrequency phase and modulation fluorometry, Cell. Mol. Biol. 32 (1986) 103-108. (Pubitemid 16147183)
    • (1986) Cellular and Molecular Biology , vol.32 , Issue.1 , pp. 103-108
    • Parasassi, T.1    Conti, F.2    Gratton, E.3
  • 50
    • 0025295884 scopus 로고
    • Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence
    • T. Parasassi, G. De Stasio, A. d'Ubaldo, E. Gratton, Phase fluctuation in phospholipid membranes revealed by Laurdan fluorescence, Biophys. J. 57 (1990) 1179-1186.
    • (1990) Biophys. J. , vol.57 , pp. 1179-1186
    • Parasassi, T.1    De Stasio, G.2    D'Ubaldo, A.3    Gratton, E.4
  • 51
    • 33749046710 scopus 로고    scopus 로고
    • To see or not to see: Lateral organization of biological membranes and fluorescence microscopy
    • L.A. Bagatolli, To see or not to see: lateral organization of biological membranes and fluorescence microscopy, Biochim. Biophys. Acta 1758 (2006) 1541-1556.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1541-1556
    • Bagatolli, L.A.1
  • 52
    • 0002711524 scopus 로고
    • Substrate-induced structural changes in electrode-adsorbed lipid layers. Experimental evidence from the behaviour of phospholipid layers on the mercury-water interface
    • A. Nelson, F.A.M. Leermakers, Substrate-induced structural changes in electrode-adsorbed lipid layers. Experimental evidence from the behaviour of phospholipid layers on the mercury-water interface, J. Electroanal. Chem. 278 (1990) 73-83.
    • (1990) J. Electroanal. Chem. , vol.278 , pp. 73-83
    • Nelson, A.1    Leermakers, F.A.M.2
  • 53
    • 65549125291 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase interaction with heterogeneous monolayers: Effect on lipid lateral organization
    • N. Vernoux, O. Maniti, O. Marcillat, C. Vial, T. Granjon, Mitochondrial creatine kinase interaction with heterogeneous monolayers: effect on lipid lateral organization, Biochimie 91 (2009) 752-764.
    • (2009) Biochimie , vol.91 , pp. 752-764
    • Vernoux, N.1    Maniti, O.2    Marcillat, O.3    Vial, C.4    Granjon, T.5
  • 54
    • 61349086716 scopus 로고    scopus 로고
    • Morphology modifications in negatively charged lipid monolayers upon mitochondrial creatine kinase binding
    • O. Maniti, M. Cheniour, O. Marcillat, C. Vial, T. Granjon, Morphology modifications in negatively charged lipid monolayers upon mitochondrial creatine kinase binding, Mol. Membr. Biol. 26 (2009) 171-185.
    • (2009) Mol. Membr. Biol. , vol.26 , pp. 171-185
    • Maniti, O.1    Cheniour, M.2    Marcillat, O.3    Vial, C.4    Granjon, T.5
  • 55
    • 0029884566 scopus 로고    scopus 로고
    • Structure of mitochondrial creatine kinase
    • DOI 10.1038/381341a0
    • K. Fritz-Wolf, T. Schnyder, T. Wallimann, W. Kabsch, Structure of mitochondrial creatine kinase, Nature 381 (1996) 341-345. (Pubitemid 26156092)
    • (1996) Nature , vol.381 , Issue.6580 , pp. 341-345
    • Fritz-Wolf, K.1    Schnyder, T.2    Wallimann, T.3    Kabsch, W.4
  • 56
    • 0032511048 scopus 로고    scopus 로고
    • Isolation and characterization of the gene (CLS1) encoding cardiolipin synthase in Saccharomyces cerevisiae
    • S.C. Chang, P.N. Heacock, E. Mileykovskaya, D.R. Voelker, W. Dowhan, Isolation and characterization of the gene (CLS1) encoding cardiolipin synthase in Saccharomyces cerevisiae, J. Biol. Chem. 273 (1998) 14933-14941.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14933-14941
    • Chang, S.C.1    Heacock, P.N.2    Mileykovskaya, E.3    Voelker, D.R.4    Dowhan, W.5
  • 59
    • 70349524664 scopus 로고    scopus 로고
    • Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis
    • Z.T. Schug, E. Gottlieb, Cardiolipin acts as a mitochondrial signalling platform to launch apoptosis, Biochim. Biophys. Acta 1788 (2009) 2022-2031.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2022-2031
    • Schug, Z.T.1    Gottlieb, E.2


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