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Volumn , Issue , 2005, Pages 339-358

Function of the Outer Mitochondrial Membrane Pore (Voltage-Dependent Anion Channel) in Intracellular Signaling

Author keywords

Cytochrome c; Function of the outer mitochondrial membrane pore in intracellular signaling; Influence of phospholipids on VDAC structure; Porins as specific binding sites; Structure and isotypes of VDAC; VDAC conductance and ion selectivity; VDAC ANT complexes

Indexed keywords


EID: 34247483763     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/3527603875ch.16     Document Type: Chapter
Times cited : (2)

References (75)
  • 1
    • 0018775962 scopus 로고
    • A candidate for the per-meability pathway of the outer mito-chondrial membrane
    • Colombini M. A candidate for the per-meability pathway of the outer mito-chondrial membrane. Nature 1979, 279, 643-645.
    • (1979) Nature , vol.279 , pp. 643-645
    • Colombini, M.1
  • 2
    • 0028341536 scopus 로고
    • Permeation of hydrophilic so-lutes through mitochondrial outer membranes: Review on mitochondrial porins
    • Benz R. Permeation of hydrophilic so-lutes through mitochondrial outer membranes: review on mitochondrial porins. Biochim Biophys Acta Rev Bio-membr 1994, 1197, 167-196.
    • (1994) Biochim Biophys Acta Rev Bio-membr , vol.1197 , pp. 167-196
    • Benz, R.1
  • 3
    • 0037024368 scopus 로고    scopus 로고
    • A 3D model of the voltage-dependent anion channel (VDAC)
    • Casadio R, Jacoboni I, Messina A, De Pinto V. A 3D model of the voltage-dependent anion channel (VDAC). FEBS Lett 2002, 520, 1-7.
    • (2002) FEBS Lett , vol.520 , pp. 1-7
    • Casadio, R.1    Jacoboni, I.2    Messina, A.3    De Pinto, V.4
  • 4
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltage-dependent anion channel gene family. Conserved struc-ture and function
    • Sampson MJ, Lovell RS, Craigen WJ. The murine voltage-dependent anion channel gene family. Conserved struc-ture and function. J Biol Chem 1997, 272, 18966-18973.
    • (1997) J Biol Chem , vol.272 , pp. 18966-18973
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 5
    • 0034695130 scopus 로고    scopus 로고
    • Involvement of the TOM complex in external NADH transport into yeast mitochon-dria depleted of mitochondrial porin1
    • Kmita H, Budzinska M. Involvement of the TOM complex in external NADH transport into yeast mitochon-dria depleted of mitochondrial porin1 Biochim Biophys Acta 2000, 1509, 86-94.
    • (2000) Biochim Biophys Acta , vol.1509 , pp. 86-94
    • Kmita, H.1    Budzinska, M.2
  • 6
    • 0032581566 scopus 로고    scopus 로고
    • Characterization of rat porin isoforms: Cloning of cardiac style-3 variant en-coding an additional methionine at its putative N-terminal region
    • Anflous K, Blondel O, Bernard A, Khrestchatisky M, Ventura-Clapier R. Characterization of rat porin isoforms: cloning of cardiac style-3 variant en-coding an additional methionine at its putative N-terminal region. Biochim Biophys Acta 1998, 1399, 47-50.
    • (1998) Biochim Biophys Acta , vol.1399 , pp. 47-50
    • Anflous, K.1    Blondel, O.2    Bernard, A.3    Khrestchatisky, M.4    Ventura-Clapier, R.5
  • 7
    • 0020121213 scopus 로고
    • Purifi-cation and characterization of a pore protein of the outer mitochondrial membrane from Neurospora crassa
    • Freitag H, Neupert W, Benz R. Purifi-cation and characterization of a pore protein of the outer mitochondrial membrane from Neurospora crassa. Eur J Biochem 1982, 162, 629-636.
    • (1982) Eur J Biochem , vol.162 , pp. 629-636
    • Freitag, H.1    Neupert, W.2    Benz, R.3
  • 8
    • 0024347661 scopus 로고
    • Inter-action of non-classical detergents with the mitochondrial porin. A new puri-fication procedure and characterization of the pore-forming unit
    • DePinto V Benz R, Palmieri F. Inter-action of non-classical detergents with the mitochondrial porin. A new puri-fication procedure and characterization of the pore-forming unit. Eur J Bio-chem 1989, 183, 179-187.
    • (1989) Eur J Bio-chem , vol.183 , pp. 179-187
    • DePinto, V.1    Benz, R.2    Palmieri, F.3
  • 9
    • 0028940707 scopus 로고
    • Role of sterols in the functional reconstitution of water-soluble mitochondrial porins from different organisms
    • Popp B, Schmid A, Benz R. Role of sterols in the functional reconstitution of water-soluble mitochondrial porins from different organisms. Biochemistry 1995, 34, 3352-3361.
    • (1995) Biochemistry , vol.34 , pp. 3352-3361
    • Popp, B.1    Schmid, A.2    Benz, R.3
  • 10
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum G. Lipids of mitochondria. Bio-chim Biophys Acta 1985, 822, 1-42.
    • (1985) Bio-chim Biophys Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 11
    • 0025013378 scopus 로고
    • Louisot P Mito-chondrial contact sites. Lipid composi-tion and dynamics
    • Ardail D, Privat JP, Egret-Charlier M, Levrat C, Lerme F, Louisot P Mito-chondrial contact sites. Lipid composi-tion and dynamics. J Biol Chem 1990, 265, 18797-18802.
    • (1990) J Biol Chem , vol.265 , pp. 18797-18802
    • Ardail, D.1    Privat, J.P.2    Egret-Charlier, M.3    Levrat, C.4    Lerme, F.5
  • 12
    • 0027934365 scopus 로고
    • The impor-tance of the outer mitochondrial com-partment in regulation of energy metabolism
    • Brdiczka D, Wallimann T. The impor-tance of the outer mitochondrial com-partment in regulation of energy metabolism. Mol Cell Biochem 1994, 133/134, 69-83.
    • (1994) Mol Cell Biochem , vol.133-134 , pp. 69-83
    • Brdiczka, D.1    Wallimann, T.2
  • 13
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 1997, 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 14
    • 0031806216 scopus 로고    scopus 로고
    • The sensor re-gions of VDAC are translocated from within the membrane to the surface during the gating processes
    • Song J, Midson C, Blachly-Dyson E, Forte M, Colombini M. The sensor re-gions of VDAC are translocated from within the membrane to the surface during the gating processes. Biophys J 1998, 74, 2926-2944.
    • (1998) Biophys J , vol.74 , pp. 2926-2944
    • Song, J.1    Midson, C.2    Blachly-Dyson, E.3    Forte, M.4    Colombini, M.5
  • 16
    • 0023041574 scopus 로고
    • Polymer inaccessible volume changes during opening and closing of a voltage-de-pendent ionic channel
    • Zimmerberg J, Parsegian VA. Polymer inaccessible volume changes during opening and closing of a voltage-de-pendent ionic channel. Nature 1986, 323, 36-39.
    • (1986) Nature , vol.323 , pp. 36-39
    • Zimmerberg, J.1    Parsegian, V.A.2
  • 17
    • 0027166976 scopus 로고
    • Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate ki-nase in the inter-membrane space
    • Gellerich FN, Wagner M, Kapischke M, Wicker U, Brdiczka D. Effect of macromolecules on the regulation of the mitochondrial outer membrane pore and the activity of adenylate ki-nase in the inter-membrane space. Biochim Biophys Acta 1993, 1142, 217-227.
    • (1993) Biochim Biophys Acta , vol.1142 , pp. 217-227
    • Gellerich, F.N.1    Wagner, M.2    Kapischke, M.3    Wicker, U.4    Brdiczka, D.5
  • 18
    • 0025055329 scopus 로고
    • The cationically selective state of the mito-chondrial outer membrane pore: A study with intact mitochondria and reconstituted mitochondrial porin
    • Benz R, Kottke M, Brdiczka D. The cationically selective state of the mito-chondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim Biophys Acta 1990, 1022, 311-318.
    • (1990) Biochim Biophys Acta , vol.1022 , pp. 311-318
    • Benz, R.1    Kottke, M.2    Brdiczka, D.3
  • 19
    • 0036151794 scopus 로고    scopus 로고
    • Model of the outer membrane potential generation by the inner membrane of mitochondria
    • Lemeshko VV. Model of the outer membrane potential generation by the inner membrane of mitochondria. Biophys J 2002, 82, 684-692.
    • (2002) Biophys J , vol.82 , pp. 684-692
    • Lemeshko, V.V.1
  • 20
    • 0030947935 scopus 로고    scopus 로고
    • VDAC channels mediate and gate the flow of ATP: Implications for the regulation of mitochondrial function
    • Rostovtseva T, Colombini M. VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys J 1997, 72, 1954-1962.
    • (1997) Biophys J , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 22
    • 0024284216 scopus 로고
    • Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion
    • Benz R, Wojtczak L, Bosch W, Brdiczka D. Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion. FEBS Lett 1988, 210, 75-80.
    • (1988) FEBS Lett , vol.210 , pp. 75-80
    • Benz, R.1    Wojtczak, L.2    Bosch, W.3    Brdiczka, D.4
  • 23
    • 0028946589 scopus 로고
    • Control of cellular respiration in viva by mitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: Possible involvement of mitochondrial-cytoskeleton interac-tions
    • Saks V, Kuznetsov A, Khuchua Z, Va-silyeva E, Belikova J, Kesvatera T, Tiivel T. Control of cellular respiration in viva by mitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: possible involvement of mitochondrial-cytoskeleton interac-tions. J. Mol Cell Cardiol 1995, 27, 625-645.
    • (1995) J. Mol Cell Cardiol , vol.27 , pp. 625-645
    • Saks, V.1    Kuznetsov, A.2    Khuchua, Z.3    Vasilyeva, E.4    Belikova, J.5    Kesvatera, T.6    Tiivel, T.7
  • 24
    • 0026507895 scopus 로고
    • A soluble mi-tochondrial protein increases the vol-tage dependence of the mitochondrial channel, VDAC
    • Liu MY, Colombini M. A soluble mi-tochondrial protein increases the vol-tage dependence of the mitochondrial channel, VDAC. J Bioenerg Biomembr 1992, 24, 41-46.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 41-46
    • Liu, M.Y.1    Colombini, M.2
  • 26
    • 0020482168 scopus 로고
    • Evidence for identity between the hex-okinase-binding protein and the mitochondrial porin in the outer mem-brane of rat liver mitochondria
    • Fiek Ch, Benz R, Roos N, Brdiczka D. Evidence for identity between the hex-okinase-binding protein and the mitochondrial porin in the outer mem-brane of rat liver mitochondria. Bio-chim Biophys Acta 1982, 688, 429-440.
    • (1982) Bio-chim Biophys Acta , vol.688 , pp. 429-440
    • Fiek, Ch1    Benz, R.2    Roos, N.3    Brdiczka, D.4
  • 27
    • 0021064868 scopus 로고
    • The binding of glycerol kinase to the outer membrane of rat liver mitochondria: Its importance in metabolic regulation
    • Östlund A.K, Göhring U, Krause J, Brdiczka D. The binding of glycerol kinase to the outer membrane of rat liver mitochondria: its importance in metabolic regulation. Biochem Med 1983, 30, 231-245.
    • (1983) Biochem Med , vol.30 , pp. 231-245
    • Östlund, A.K.1    Göhring, U.2    Krause, J.3    Brdiczka, D.4
  • 28
    • 0021997991 scopus 로고
    • The regulation of mito-chondrial-bound hexokinases in the liver
    • Weiler U, Riesinger I, Knoll G, Brdiczka D. The regulation of mito-chondrial-bound hexokinases in the liver. Biochem Med 1985, 33, 223-235.
    • (1985) Biochem Med , vol.33 , pp. 223-235
    • Weiler, U.1    Riesinger, I.2    Knoll, G.3    Brdiczka, D.4
  • 29
    • 0027230203 scopus 로고
    • Effect of macromolecules on the structure of the mitochondrial inter-membrane space and the regulation of hexokinase
    • Wicker U, Bücheler K, Gellerich FN, Wagner M, Kapischke M, Brdiczka D. Effect of macromolecules on the structure of the mitochondrial inter-membrane space and the regulation of hexokinase. Biochim Biophys Acta 1993, 1142, 228-239.
    • (1993) Biochim Biophys Acta , vol.1142 , pp. 228-239
    • Wicker, U.1    Bücheler, K.2    Gellerich, F.N.3    Wagner, M.4    Kapischke, M.5    Brdiczka, D.6
  • 30
    • 0000935827 scopus 로고
    • Lo-calization of the ATP/ADP translocator in the inner membrane and regulation of contact sites between mitochondrial envelope membranes by ADP. A study on freeze fractured isolated liver mito-chondria
    • Bücheler K, Adams V, Brdiczka D. Lo-calization of the ATP/ADP translocator in the inner membrane and regulation of contact sites between mitochondrial envelope membranes by ADP. A study on freeze fractured isolated liver mito-chondria. Biochim Biophys Acta 1991, 1061, 215-225.
    • (1991) Biochim Biophys Acta , vol.1061 , pp. 215-225
    • Bücheler, K.1    Adams, V.2    Brdiczka, D.3
  • 31
    • 0025103254 scopus 로고
    • Tetrameric structure of mitochondrially bound rat brain hexokinase: A cross-linking study
    • Xie G, Wilson JE. Tetrameric structure of mitochondrially bound rat brain hexokinase: a cross-linking study. Arch Biochem Biophys 1990, 276, 285-293.
    • (1990) Arch Biochem Biophys , vol.276 , pp. 285-293
    • Xie, G.1    Wilson, J.E.2
  • 32
    • 0034541155 scopus 로고    scopus 로고
    • Membrane potential-dependent conformational changes in mitochondrially bound hexokinase in brain
    • Hashimoto M, Wilson JE. Membrane potential-dependent conformational changes in mitochondrially bound hexokinase in brain. Arch Biochem Biophys 2000, 884, 163-173.
    • (2000) Arch Biochem Biophys , vol.884 , pp. 163-173
    • Hashimoto, M.1    Wilson, J.E.2
  • 33
    • 0032252072 scopus 로고    scopus 로고
    • Mass spectrometric mapping of ion channel proteins (Porins) and identifi-cation of their supramolecular mem-brane assembly
    • Bühler S, Michels J, Wendt S, Rück A, Brdiczka D, Welte W, Przybylski M. Mass spectrometric mapping of ion channel proteins (Porins) and identifi-cation of their supramolecular mem-brane assembly. Proteins 1998, 2, 63-73.
    • (1998) Proteins , vol.2 , pp. 63-73
    • Bühler, S.1    Michels, J.2    Wendt, S.3    Rück, A.4    Brdiczka, D.5    Welte, W.6    Przybylski, M.7
  • 34
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between ki-nases, mitochondrial porin and adeny-late translocator in rat brain resemble the permeability transition pore
    • Beutner G. Rück A, Riede, B, Welte W, Brdiczka D. Complexes between ki-nases, mitochondrial porin and adeny-late translocator in rat brain resemble the permeability transition pore. FEBS Lett 1996, 396, 189-195.
    • (1996) FEBS Lett , vol.396 , pp. 189-195
    • Beutner, G.1    Rück, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 35
    • 0035448294 scopus 로고    scopus 로고
    • Adenine nucleotide trans-locator isoforms 1 and 2 are differently distributed in the mitochondrial inner membrane and have distinct affinities to cyclophilin D
    • Vyssokikh MY, Katz A, Rück A, Wuensch C, Dörner A, Zorov DB, Brdiczka D. Adenine nucleotide trans-locator isoforms 1 and 2 are differently distributed in the mitochondrial inner membrane and have distinct affinities to cyclophilin D. Biochem J 2001, 358, 349-358.
    • (2001) Biochem J , vol.358 , pp. 349-358
    • Vyssokikh, M.Y.1    Katz, A.2    Rück, A.3    Wuensch, C.4    Dörner, A.5    Zorov, D.B.6    Brdiczka, D.7
  • 36
    • 0022550296 scopus 로고
    • Enrichment and biochemical characterization of boundary membrane contact sites in rat-liver mitochondria
    • Ohlendieck K, Riesinger I, Adams V, Krause J, Brdiczka D. Enrichment and biochemical characterization of boundary membrane contact sites in rat-liver mitochondria. Biochim Biophys Acta 1986, 860, 672-689.
    • (1986) Biochim Biophys Acta , vol.860 , pp. 672-689
    • Ohlendieck, K.1    Riesinger, I.2    Adams, V.3    Krause, J.4    Brdiczka, D.5
  • 37
    • 0024963096 scopus 로고
    • Further charac-terization of contact sites from mito-chondria of different tissues: Topology of peripheral kinases
    • Adams V. Bosch W, Schlegel J, Walli-mann T, Brdiczka D. Further charac-terization of contact sites from mito-chondria of different tissues: topology of peripheral kinases Biochim Biophys Acta 1989, 981, 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
  • 38
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexoki-nase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transi-tion pore. Implication for regulation of permeability transition by the kinases
    • Beutner G, Rück A, Riede B, Brdiczka D. Complexes between porin, hexoki-nase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transi-tion pore. Implication for regulation of permeability transition by the kinases. Biochim Biophys Acta 1998, 1368, 7-18.
    • (1998) Biochim Biophys Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Rück, A.2    Riede, B.3    Brdiczka, D.4
  • 39
    • 0022549645 scopus 로고
    • Cross-linking analysis of yeast mi-tochondrial outer membrane
    • Krause J, Hay R, Kowollik C, Brdiczka D. Cross-linking analysis of yeast mi-tochondrial outer membrane. Biochim Biophys Acta 1986, 860, 690-698.
    • (1986) Biochim Biophys Acta , vol.860 , pp. 690-698
    • Krause, J.1    Hay, R.2    Kowollik, C.3    Brdiczka, D.4
  • 40
    • 0026431776 scopus 로고
    • Mitochondrial crea-tine kinase mediates contact formation between mitochondrial membranes
    • Rojo M, Hovius R, Demel RA, Nicolay K, Wallimann T. Mitochondrial crea-tine kinase mediates contact formation between mitochondrial membranes. J Biol Chem 1991, 266, 20290-20295.
    • (1991) J Biol Chem , vol.266 , pp. 20290-20295
    • Rojo, M.1    Hovius, R.2    Demel, R.A.3    Nicolay, K.4    Wallimann, T.5
  • 41
    • 0028034636 scopus 로고
    • In vitro complex formation between octamer of creatine kinase and porin
    • Brdiczka D, Kaldis Ph, Wallimann Th. In vitro complex formation between octamer of creatine kinase and porin. J Biol Chem 1994, 269, 27640-27644.
    • (1994) J Biol , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 42
    • 0035930592 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase and mitochondrial outer membrane porin show direct in-teraction that is modulated by calcium
    • Schlattner U, Dolder M, Wallimann T, Tokarska-Schlattner M. Mitochondrial creatine kinase and mitochondrial outer membrane porin show direct in-teraction that is modulated by calcium. J Biol Chem 2001, 276, 48027-48030.
    • (2001) J Biol Chem , vol.276 , pp. 48027-48030
    • Schlattner, U.1    Dolder, M.2    Wallimann, T.3    Tokarska-Schlattner, M.4
  • 44
    • 77956819723 scopus 로고
    • Metabolite car-riers in mitochondria
    • In: Ernster L (Ed.), Elsevier, Amsterdam
    • Krämer R, Palmieri F. Metabolite car-riers in mitochondria. In: Ernster L (Ed.), Molecular Mechanisms in Bioener-getics. Elsevier, Amsterdam, 1992, pp. 359-384.
    • (1992) Molecular Mechanisms in Bioener-getics , pp. 359-384
    • Krämer, R.1    Palmieri, F.2
  • 45
    • 0025170604 scopus 로고
    • The mitochondrial aspartate/ glutamate and ADP/ATP carrier switch from obligate counterexchange to uni-directional transport after modification by SH-reagents
    • Dierks T Salentin A, Heberger C, Krä-mer R. The mitochondrial aspartate/ glutamate and ADP/ATP carrier switch from obligate counterexchange to uni-directional transport after modification by SH-reagents. Biochim Biophys Acta 1990, 1028, 268-280.
    • (1990) Biochim Biophys Acta , vol.1028 , pp. 268-280
    • Dierks, T.1    Salentin, A.2    Heberger, C.3    Krä-mer, R.4
  • 46
    • 0015497424 scopus 로고
    • Differences between the ATP-ADP ratios in the mitochondrial matrix and in the extramitochondrial space
    • Heldt H.W, Klingenberg M, Milovan-cev M. Differences between the ATP-ADP ratios in the mitochondrial matrix and in the extramitochondrial space. Eur J Biochem 1972, 30, 434-440.
    • (1972) Eur J Biochem , vol.30 , pp. 434-440
    • Heldt, H.W.1    Klingenberg, M.2    Milovancev, M.3
  • 47
    • 0019230323 scopus 로고
    • 2+-activated hydro-philic channel of the mitochondrial inner membrane by nucleotides
    • 2+-activated hydro-philic channel of the mitochondrial inner membrane by nucleotides. J Membr Biol 1980, 57, 231-236.
    • (1980) J Membr Biol , vol.57 , pp. 231-236
    • Harworth, R.A.1    Hunter, P.R.2
  • 49
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zorati M, Szabao I. The mitochondrial permeability transition. Biochim Bio-phys Acta 1995, 1241, 139-176.
    • (1995) Biochim Bio-phys Acta , vol.1241 , pp. 139-176
    • Zorati, M.1    Szabao, I.2
  • 51
    • 0025193488 scopus 로고
    • 2+-induced large amplitude swelling of mitochondria by cyclos-porin A is probably caused by binding to a matrix peptidylprolyl cis-trans-iso-merase and preventing it interacting with the adenine nucleotide trans-locase
    • 2+-induced large amplitude swelling of mitochondria by cyclos-porin A is probably caused by binding to a matrix peptidylprolyl cis-trans-iso-merase and preventing it interacting with the adenine nucleotide trans-locase. Biochem J 1990, 268, 153-160.
    • (1990) Biochem J , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 52
    • 0032401567 scopus 로고    scopus 로고
    • Cyclo-philin-D binds strongly to complexes of the voltage-dependent anion chan-nel and the adenine nucleotide trans-locase to form the permeability transi-tion pore
    • Crompton M, Virji S, Ward JM. Cyclo-philin-D binds strongly to complexes of the voltage-dependent anion chan-nel and the adenine nucleotide trans-locase to form the permeability transi-tion pore. Eur J Biochem 1998, 258, 729-735.
    • (1998) Eur J Biochem , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 54
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • Rück A. Dolder M, Wallimann T, Brdiczka D. Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore. FEBS Lett 1998, 426, 97-101.
    • (1998) FEBS Lett , vol.426 , pp. 97-101
    • Rück, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 55
    • 84934504826 scopus 로고
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem J 1888, 255, 257-360.
    • (1888) Biochem J , vol.255 , pp. 257-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 56
    • 0042494245 scopus 로고
    • 35S-atractyloside and bongkrekic acid at mitochondrial membranes
    • 35S-atractyloside and bongkrekic acid at mitochondrial membranes. FEBS Lett 1971, 16, 301-303.
    • (1971) FEBS Lett , vol.16 , pp. 301-303
    • Klingenberg, M.1    Grebe, K.2    Falkner, G.3
  • 58
    • 0028338272 scopus 로고
    • Dual localization of mitochondrial creatine kinase in brain mitochondria
    • Kottke M, Wallimann Th, Brdiczka D. Dual localization of mitochondrial creatine kinase in brain mitochondria. Biochem Med Metabol Biol 1994, 51, 105-117.
    • (1994) Biochem Med Metabol Biol , vol.51 , pp. 105-117
    • Kottke, M.1    Wallimann, T.H.2    Brdiczka, D.3
  • 60
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic pro-gram in cell-free extracts: Requirement for dATP and cytochrome
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic pro-gram in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996, 86, 147-157.
    • (1996) C. Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 61
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mi-tochondria: A primary site for Bcl-reg-ulation of apoptosis
    • Kluck RM, Green DR, Newmeyer DD. The release of cytochrome c from mi-tochondria: a primary site for Bcl-reg-ulation of apoptosis. Science 1997, 275, 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Green, D.R.2    Newmeyer, D.D.3
  • 62
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activa-tion
    • Saleh A S. S, Acharya S, Fishel R, Al-nemri ES. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activa-tion. J Biol Chem 1999, 274, 17941-17945.
    • (1999) J Biol Chem , vol.274 , pp. 17941-17945
    • Saleh, A.S.S.1    Acharya, S.2    Fishel, R.3    Alnemri, E.S.4
  • 63
    • 0036510541 scopus 로고    scopus 로고
    • Mi-tochondrial binding of hexokinase II inhibits Bax-induced cytochrome c re-lease and apoptosis
    • Pastorino JG, Shulga N, Hoek JB. Mi-tochondrial binding of hexokinase II inhibits Bax-induced cytochrome c re-lease and apoptosis. J Biol Chem 2002, 277, 7610-7618.
    • (2002) J Biol Chem , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 64
    • 0036799548 scopus 로고    scopus 로고
    • Biphasic translocation of BAX to mitochondria
    • Capano M, Crompton M. Biphasic translocation of BAX to mitochondria. Biochem J 2002, 367, 169-178.
    • (2002) Biochem J , vol.367 , pp. 169-178
    • Capano, M.1    Crompton, M.2
  • 65
    • 0036042248 scopus 로고    scopus 로고
    • Bax releases cytochrome c preferentially from a complex between porin and adenine nucleotide translo-cator. Hexokinase activity suppresses this effect
    • Vyssokikh MY, Zorova L, Zorov D, Heimlich G, Jürgensmeier JM, Brdiczka D. Bax releases cytochrome c preferentially from a complex between porin and adenine nucleotide translo-cator. Hexokinase activity suppresses this effect. Mol Biol Rep 2002, 29, 93-96.
    • (2002) Mol Biol Rep , vol.29 , pp. 93-96
    • Vyssokikh, M.Y.1    Zorova, L.2    Zorov, D.3    Heimlich, G.4    Jürgensmeier, J.M.5    Brdiczka, D.6
  • 66
    • 0033615649 scopus 로고    scopus 로고
    • Functional consequences of sustained or transient activation by Bax of the mitochondrial permeability transition pore
    • Pastorino JG, Tafani, M, Rothman, RJ, Marcineviciute A, Hoek JB, Farber JL. Functional consequences of sustained or transient activation by Bax of the mitochondrial permeability transition pore. J Biol Chem 1999, 274, 31734-31739.
    • (1999) J Biol Chem , vol.274 , pp. 31734-31739
    • Pastorino, J.G.1    Tafani, M.2    Rothman, R.J.3    Marcineviciute, A.4    Hoek, J.B.5    Farber, J.L.6
  • 67
    • 0036478989 scopus 로고    scopus 로고
    • The permeability transition pore com-plex: Another view
    • Halestrap AP, McStay GP, Clarke SJ. The permeability transition pore com-plex: another view. Biochimie 2002, 84, 153-166.
    • (2002) Biochimie , vol.84 , pp. 153-166
    • Halestrap, A.P.1    McStay, G.P.2    Clarke, S.J.3
  • 69
    • 0037156869 scopus 로고    scopus 로고
    • The quantification of ADP diffusion gradients across the outer membrane of heart mitochondria in the presence of macromolecules
    • Gellerich FN, Laterveer FD, Zierz S, Nicolay K. The quantification of ADP diffusion gradients across the outer membrane of heart mitochondria in the presence of macromolecules. Bio-chim Biophys Acta 2002, 1554, 48-56.
    • (2002) Bio-chim Biophys Acta , vol.1554 , pp. 48-56
    • Gellerich, F.N.1    Laterveer, F.D.2    Zierz, S.3    Nicolay, K.4
  • 70
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexo-kinase
    • Gottlob K, Majewski N, Kennedy S, Kandel E, Robey RB, Hay N. Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexo-kinase. Genes Dev 2001, 15, 1406-1418.
    • (2001) Genes Dev , vol.15 , pp. 1406-1418
    • Gottlob, K.1    Majewski, N.2    Kennedy, S.3    Kandel, E.4    Robey, R.B.5    Hay, N.6
  • 72
    • 0033611057 scopus 로고    scopus 로고
    • Adenine nucleotide translo-case-1, a component of the permeabil-ity transition pore, can dominantly in-duce apoptosis
    • Bauer MK, Schubert A, Rocks O, Grimm S. Adenine nucleotide translo-case-1, a component of the permeabil-ity transition pore, can dominantly in-duce apoptosis. J Cell Biol 1999, 147, 1493-1502.
    • (1999) J Cell Biol , vol.147 , pp. 1493-1502
    • Bauer, M.K.1    Schubert, A.2    Rocks, O.3    Grimm, S.4
  • 73
    • 0030853574 scopus 로고    scopus 로고
    • Adenine nucleotide translocator in dilated cardiomyopathy: Pathophysiological alterations in ex-pression and function
    • Dörner A. Schulze K. Rauch U, Schultheiss HP. Adenine nucleotide translocator in dilated cardiomyopathy: pathophysiological alterations in ex-pression and function. Mol Cell Bio-chem 1997, 174, 261-269.
    • (1997) Mol Cell Bio-chem , vol.174 , pp. 261-269
    • Dörner, A.1    Schulze, K.2    Rauch, U.3    Schultheiss, H.P.4
  • 74
    • 0035107677 scopus 로고    scopus 로고
    • Mi-tochondrial creatine kinase in contact sites: Interaction with porin and ade-nine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage [Review]
    • Dolder M, Wendt S, Wallimann T. Mi-tochondrial creatine kinase in contact sites: interaction with porin and ade-nine nucleotide translocase, role in permeability transition and sensitivity to oxidative damage [Review]. Biol Sig-nals Recept 2001, 10, 93-111.
    • (2001) Biol Sig-nals Recept , vol.10 , pp. 93-111
    • Dolder, M.1    Wendt, S.2    Wallimann, T.3
  • 75
    • 0021111174 scopus 로고
    • Changes in freeze-fracture mitochondrial mem-branes correlated to their energetic state
    • Knoll G, Brdiczka D. Changes in freeze-fracture mitochondrial mem-branes correlated to their energetic state. Biochim Biophys Acta 1983, 733, 102-110.
    • (1983) Biochim Biophys Acta , vol.733 , pp. 102-110
    • Knoll, G.1    Brdiczka, D.2


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