메뉴 건너뛰기




Volumn , Issue , 2007, Pages 163-194

Mitochondrial VDAC and Its Complexes

Author keywords

Apoptosis; Cytochrome c; Energy transfer networks; Metabolic feedback regulation; Mitochondria; Mitochondrial VDAC; Modeling cellular energetics; Molecular system bioenergetics; Organizing kinases; VDAC complexes

Indexed keywords


EID: 77950907315     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527621095.ch6     Document Type: Chapter
Times cited : (5)

References (152)
  • 1
    • 0035197418 scopus 로고    scopus 로고
    • An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle
    • Martin, W., Hoffmeister, M., Rotte, C., Henze, K. (2001) An overview of endosymbiotic models for the origins of eukaryotes, their ATP-producing organelles (mitochondria and hydrogenosomes), and their heterotrophic lifestyle. Biol. Chem 382, 1521-1539.
    • (2001) Biol. Chem , vol.382 , pp. 1521-1539
    • Martin, W.1    Hoffmeister, M.2    Rotte, C.3    Henze, K.4
  • 2
    • 0015188004 scopus 로고
    • Compartmentation in relation to metabolic control in liver
    • Gumaa, K. A., McLean, P., Greenbaum, A. L. (1971) Compartmentation in relation to metabolic control in liver. Essays Biochem 7, 39-86.
    • (1971) Essays Biochem , vol.7 , pp. 39-86
    • Gumaa, K.A.1    McLean, P.2    Greenbaum, A.L.3
  • 3
    • 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., Eppenberger, H. M. (1992) 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, 21-40.
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 5
    • 0019888247 scopus 로고
    • Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes
    • Bernardi, P., Azzone, G. F. (1981) Cytochrome c as an electron shuttle between the outer and inner mitochondrial membranes. J. Biol. Chem. 256, 7187-7192.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7187-7192
    • Bernardi, P.1    Azzone, G.F.2
  • 6
    • 0033532508 scopus 로고    scopus 로고
    • Modulation of cytochrome c-mediated extramitochondrial NADH oxidation by contact site structure
    • Marzulli, D., La Piana, G., Franseve, E., Lofrumento, N. E. (1999) Modulation of cytochrome c-mediated extramitochondrial NADH oxidation by contact site structure. Biochem. Biophys. Res. Commun 259, 325-330.
    • (1999) Biochem. Biophys. Res. Commun , vol.259 , pp. 325-330
    • Marzulli, D.1    La Piana, G.2    Franseve, E.3    Lofrumento, N.E.4
  • 7
    • 29344439984 scopus 로고    scopus 로고
    • Mitochondrial contact sites: their role in energy metabolism and apoptosis
    • Brdiczka, D., Zorov, D. B., Sheu, S. S. (2006) Mitochondrial contact sites: their role in energy metabolism and apoptosis. Biochim Biophys Acta 1762, 148-63.
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 148-163
    • Brdiczka, D.1    Zorov, D.B.2    Sheu, S.S.3
  • 8
    • 0017054558 scopus 로고
    • Reconstitution in planar lipid bilayers of a voltage-dependent anionselective channel obtained from paramecium mitochondria
    • Schein, S. J., Colombini, M., Finkelstein, A. (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anionselective channel obtained from paramecium mitochondria. J Membr Biol 30, 99-120.
    • (1976) J Membr Biol , vol.30 , pp. 99-120
    • Schein, S.J.1    Colombini, M.2    Finkelstein, A.3
  • 9
    • 0029018094 scopus 로고
    • Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy
    • Reymann, S et al. (1995) Further evidence for multitopological localization of mammalian porin (VDAC) in the plasmalemma forming part of a chloride channel complex affected in cystic fibrosis and encephalomyopathy. Biochem Mol Med 54, 75-87.
    • (1995) Biochem Mol Med , vol.54 , pp. 75-87
    • Reymann, S.1
  • 10
    • 0022550296 scopus 로고
    • Enrichment and biochemical characterization of boundary membrane contact sites from rat-liver mitochondria
    • Ohlendieck, K., Riesinger, I., Adams, V., Krause, J., Brdiczka, D. (1986) Enrichment and biochemical characterization of boundary membrane contact sites from rat-liver mitochondria. Biochim Biophys Acta 860, 672-89.
    • (1986) Biochim Biophys Acta , vol.860 , pp. 672-689
    • Ohlendieck, K.1    Riesinger, I.2    Adams, V.3    Krause, J.4    Brdiczka, D.5
  • 11
    • 0024963096 scopus 로고
    • Further characterization of contact sites from mitochondria of different tissues: toplogy of peripheral kinases
    • Adams, V., Bosch, W., Schlegel, J., Wallimann, T., Brdiczka, D. (1989) Further characterization of contact sites from mitochondria of different tissues: toplogy of peripheral kinases. Biochim. Biophys. Acta 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
  • 12
    • 0026078044 scopus 로고
    • Location and regulation of octameric mitochondrial creatine kinase in the contact sites
    • Kottke, M., Adams, V., Wallimann, T., Nalam, V. K., Brdiczka, D. (1991) Location and regulation of octameric mitochondrial creatine kinase in the contact sites. Biochim Biophys Acta 1061, 215-25.
    • (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
  • 13
    • 1642524332 scopus 로고    scopus 로고
    • The intramitochondrial 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. Y., Zorova, L., Zorov, D., Heimlich, G., Jürgensmeier, J. M., Schreiner, D., Brdiczka, D. (2004) The intramitochondrial 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, 27-36.
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 27-36
    • Vyssokikh, M.Y.1    Zorova, L.2    Zorov, D.3    Heimlich, G.4    Jürgensmeier, J.M.5    Schreiner, D.6    Brdiczka, D.7
  • 14
    • 84889491283 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., Epand, R. M. (2006) Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes. Biophys. J. 106, 1529.
    • (2006) Biophys. J. , vol.106 , pp. 1529
    • Epand, R.F.1    Schlattner, U.2    Wallimann, T.3    Lacombe, M.-L.4    Epand, R.M.5
  • 15
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins
    • Benz, R. (1994) Permeation of hydrophilic solutes through mitochondrial outer membranes: Review on mitochondrial porins. Biochim. Biophys. Acta 1197, 167-196.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 16
    • 0025788323 scopus 로고
    • Peptidespecific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin
    • De Pinto, V., Prezioso, G., Thinnes, F., Link, T. A., Palmieri, F. (1991) Peptidespecific antibodies and proteases as probes of the transmembrane topology of the bovine heart mitochondrial porin. Biochemistry 30, 10191-200.
    • (1991) Biochemistry , vol.30 , pp. 10191-10200
    • De Pinto, V.1    Prezioso, G.2    Thinnes, F.3    Link, T.A.4    Palmieri, F.5
  • 17
    • 0842345400 scopus 로고    scopus 로고
    • VDAC: the channel at the interface between mitochondria and the cytosol
    • Colombini, M. (2004) VDAC: the channel at the interface between mitochondria and the cytosol. Mol Cell Biochem 256-257, 107-15.
    • (2004) Mol Cell Biochem , vol.256 , pp. 107-115
    • Colombini, M.1
  • 18
    • 0024347661 scopus 로고
    • Interaction of non-classical detergents with the mitochondrial porin
    • A new purification procedure and characterization of the pore-forming unit
    • DePinto, V., Benz, R., Palmieri, F. (1989) Interaction of non-classical detergents with the mitochondrial porin. A new purification procedure and characterization of the pore-forming unit. Eur J Biochem 183, 179-187.
    • (1989) Eur J Biochem , vol.183 , pp. 179-187
    • DePinto, V.1    Benz, R.2    Palmieri, F.3
  • 19
    • 0027315863 scopus 로고
    • Mapping of residues forming the voltage sensor of the voltage-dependent anionselective channel
    • Thomas, L., Blachly-Dyson, E., Colombini, M., Forte, M. (1993) Mapping of residues forming the voltage sensor of the voltage-dependent anionselective channel. Proc Natl Acad Sci USA 90, 5446-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5446-5449
    • Thomas, L.1    Blachly-Dyson, E.2    Colombini, M.3    Forte, M.4
  • 22
    • 0022549645 scopus 로고
    • Cross-linking analysis of yeast mitochondrial outer membrane
    • Krause, J., Hay, R., Kowollik, C., Brdiczka, D. (1986) Cross-linking analysis of yeast mitochondrial outer membrane. Biochim. Biophys. Acta 860, 690-698.
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 690-698
    • Krause, J.1    Hay, R.2    Kowollik, C.3    Brdiczka, D.4
  • 23
    • 0021097241 scopus 로고
    • Hydrodynamic properties of porin isolated from outer membranes of rat liver mitochondria
    • Linden, M., Gellerfors, P. (1983) Hydrodynamic properties of porin isolated from outer membranes of rat liver mitochondria. Biochim Biophys Acta 736, 125-9.
    • (1983) Biochim Biophys Acta , vol.736 , pp. 125-129
    • Linden, M.1    Gellerfors, P.2
  • 24
    • 3242728582 scopus 로고    scopus 로고
    • Subcellular localization of VDAC in mitochondria and ER in the cerebellum
    • Shoshan-Barmatz, V., Zalk, R., Gincel, D., Vardi, N. (2004) Subcellular localization of VDAC in mitochondria and ER in the cerebellum. Biochim Biophys Acta 1657, 105-14.
    • (2004) Biochim Biophys Acta , vol.1657 , pp. 105-114
    • Shoshan-Barmatz, V.1    Zalk, R.2    Gincel, D.3    Vardi, N.4
  • 25
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltagedependent anion channel and cytochrome c release from mitochondria
    • Zalk, R., Israelson, A., Garty, E. S., Azoulay-Zohar, H., Shoshan-Barmatz, V. (2005) Oligomeric states of the voltagedependent anion channel and cytochrome c release from mitochondria. Biochem. J. 386, 73-83.
    • (2005) Biochem. J. , vol.386 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.S.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 26
    • 0042233916 scopus 로고    scopus 로고
    • New functions of an old protein: the eukaryotic porin or voltage dependent anion selective channel (VDAC)
    • De Pinto, V. E. A. (2003) New functions of an old protein: the eukaryotic porin or voltage dependent anion selective channel (VDAC). Ital J Biochem 52, 17-24.
    • (2003) Ital J Biochem , vol.52 , pp. 17-24
    • De Pinto, V.E.A.1
  • 27
    • 0942297436 scopus 로고    scopus 로고
    • The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death
    • Shoshan-Barmatz, V., Gincel, D. (2003) The voltage-dependent anion channel: characterization, modulation, and role in mitochondrial function in cell life and death. Cell Biochem Biophys 39, 279-92.
    • (2003) Cell Biochem Biophys , vol.39 , pp. 279-292
    • Shoshan-Barmatz, V.1    Gincel, D.2
  • 28
    • 0842345400 scopus 로고    scopus 로고
    • VDAC: the channel at the interface between mitochondria and the cytosol
    • Colombini, M. (2004) VDAC: the channel at the interface between mitochondria and the cytosol. Mol Cell Biochem 256-257, 107-15.
    • (2004) Mol Cell Biochem , vol.256 , pp. 107-115
    • Colombini, M.1
  • 29
    • 0030321041 scopus 로고    scopus 로고
    • Diameter of the mammalian porin channel in open and closed states: direct measurement at the single channel level in planar lipid bilayer
    • Krasilnikov, O. V., Carneiro, C. M., Yuldasheva, L. N., Campos-de-Carvalho, A. C., Nogueira, R. A. (1996) Diameter of the mammalian porin channel in open and closed states: direct measurement at the single channel level in planar lipid bilayer. Braz J Med Biol Res 29, 1691-7.
    • (1996) Braz J Med Biol Res , vol.29 , pp. 1691-1697
    • Krasilnikov, O.V.1    Carneiro, C.M.2    Yuldasheva, L.N.3    Campos-De-Carvalho, A.C.4    Nogueira, R.A.5
  • 30
    • 0024458675 scopus 로고
    • Voltage gating in the mitochondrial channel, VDAC
    • Colombini, M. (1989) Voltage gating in the mitochondrial channel, VDAC. J Membr Biol, 103-11.
    • (1989) J Membr Biol , pp. 103-111
    • Colombini, M.1
  • 31
    • 0025055329 scopus 로고
    • The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin
    • Benz, R., Kottke, M., Brdiczka, D. (1990) The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim. Biophys. Acta 1022, 311-318.
    • (1990) Biochim. Biophys. Acta , vol.1022 , pp. 311-318
    • Benz, R.1    Kottke, M.2    Brdiczka, D.3
  • 32
    • 0026574501 scopus 로고
    • The cationselective substate of the mitochondrial outer membrane pore: single-channel conductance and influence on intermembrane and peripheral kinases
    • Benz, R., Brdiczka, D. (1992) The cationselective substate of the mitochondrial outer membrane pore: single-channel conductance and influence on intermembrane and peripheral kinases. J Bioenerg Biomembr 24, 33-9.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 33-39
    • Benz, R.1    Brdiczka, D.2
  • 33
    • 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. (1997) VDAC channels mediate and gate the flow of ATP: implications for the regulation of mitochondrial function. Biophys. J. 72, 1954-1962.
    • (1997) Biophys. J. , vol.72 , pp. 1954-1962
    • Rostovtseva, T.1    Colombini, M.2
  • 34
    • 0031806216 scopus 로고    scopus 로고
    • The sensor regions 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. (1998) The sensor regions of VDAC are translocated from within the membrane to the surface during the gating processes. Biophys. J. 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
  • 35
  • 36
    • 0028946589 scopus 로고
    • Control of cellular respiration in vivo by mitochondrial outer membrane and by creatine kinase
    • A new speculative hypothesis: possible involvement of mitochondrialcytoskeleton interactions
    • Saks, V., Kuznetsov, A., Khuchua, Z., Vasilyeva, E., Belikova, J., Kesvatera, T., Tiivel, T. (1995) Control of cellular respiration in vivo by mitochondrial outer membrane and by creatine kinase. A new speculative hypothesis: possible involvement of mitochondrialcytoskeleton interactions. J. Mol. Cell. Cardiol. 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
  • 37
    • 0023820549 scopus 로고
    • Effect of oleate on the apparent Km of monoamine oxidase and the amount of membrane-bound hexokinase in isolated rat hepatocytes
    • Wojtczak, L., Adams, V., Brdiczka, D. (1988) Effect of oleate on the apparent Km of monoamine oxidase and the amount of membrane-bound hexokinase in isolated rat hepatocytes. Mol. Cell. Biochem. 79, 25-3.
    • (1988) Mol. Cell. Biochem. , vol.79 , pp. 25-23
    • Wojtczak, L.1    Adams, V.2    Brdiczka, D.3
  • 38
    • 0036151794 scopus 로고    scopus 로고
    • Model of the outer membrane potential generation by the inner membrane of mitochondria
    • Lemeshko, V. V. (2002) Model of the outer membrane potential generation by the inner membrane of mitochondria. Biophys. J. 82, 684-692.
    • (2002) Biophys. J. , vol.82 , pp. 684-692
    • Lemeshko, V.V.1
  • 39
    • 0030856487 scopus 로고    scopus 로고
    • The murine voltagedependent anion channel gene family
    • Conserved structure and function
    • Sampson, M. J., Lovell, R. S., Craigen, W. J. (1997) The murine voltagedependent anion channel gene family. Conserved structure and function. J Biol Chem 272, 18966-73.
    • (1997) J Biol Chem , vol.272 , pp. 18966-18973
    • Sampson, M.J.1    Lovell, R.S.2    Craigen, W.J.3
  • 40
    • 0030873947 scopus 로고    scopus 로고
    • Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein
    • Blachly-Dyson, E., Song, J., Wolfgang, W. J., Colombini, M., Forte, M. (1997) Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein. Mol Cell Biol 17, 5727-38.
    • (1997) Mol Cell Biol , vol.17 , pp. 5727-5738
    • Blachly-Dyson, E.1    Song, J.2    Wolfgang, W.J.3    Colombini, M.4    Forte, M.5
  • 42
    • 0031656931 scopus 로고    scopus 로고
    • Yeast mitochondrial metabolism: from in vitro to in situ quantitative study
    • Averet, N., Fitton, V., Bunoust, O., Rigoulet, M., Guerin, B. (1998) Yeast mitochondrial metabolism: from in vitro to in situ quantitative study. Mol Cell Biochem 184, 67-79.
    • (1998) Mol Cell Biochem , vol.184 , pp. 67-79
    • Averet, N.1    Fitton, V.2    Bunoust, O.3    Rigoulet, M.4    Guerin, B.5
  • 43
    • 0344211846 scopus 로고    scopus 로고
    • NADH is specifically channeled through the mitochondrial porin channel in Saccharomyces cerevisiae
    • Averet, N., Aguilaniu, H., Bunoust, O., Gustafsson, L., Rigoulet, M. (2002) NADH is specifically channeled through the mitochondrial porin channel in Saccharomyces cerevisiae. J Bioenerg Biomembr 34, 499-506.
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 499-506
    • Averet, N.1    Aguilaniu, H.2    Bunoust, O.3    Gustafsson, L.4    Rigoulet, M.5
  • 44
    • 0034695130 scopus 로고    scopus 로고
    • Involvement of the TOM complex in external NADH transport into yeast mitochondria depleted of mitochondrial porin1
    • Kmita, H., Budzinska, M. (2000) Involvement of the TOM complex in external NADH transport into yeast mitochondria depleted of mitochondrial porin1. Biochim Biophys Acta 1509, 86-94.
    • (2000) Biochim Biophys Acta , vol.1509 , pp. 86-94
    • Kmita, H.1    Budzinska, M.2
  • 45
    • 0027389308 scopus 로고
    • Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltagedependent anion channel
    • Blachly-Dyson, E., Zambronicz, E. B., Yu, W. H., Adams, V., McCabe, E. R., Adelman, J., Colombini, M., Forte, M. (1993) Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltagedependent anion channel. J Biol Chem 268, 1835-41.
    • (1993) J Biol Chem , vol.268 , pp. 1835-1841
    • Blachly-Dyson, E.1    Zambronicz, E.B.2    Yu, W.H.3    Adams, V.4    McCabe, E.R.5    Adelman, J.6    Colombini, M.7    Forte, M.8
  • 46
    • 0032765963 scopus 로고    scopus 로고
    • Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability
    • Xu, X., Decker, W., Sampson, M. J., Craigen, W. J., Colombini, M. (1999) Mouse VDAC isoforms expressed in yeast: channel properties and their roles in mitochondrial outer membrane permeability. J Membr Biol 170, 89-102.
    • (1999) J Membr Biol , vol.170 , pp. 89-102
    • Xu, X.1    Decker, W.2    Sampson, M.J.3    Craigen, W.J.4    Colombini, M.5
  • 47
    • 0030586893 scopus 로고    scopus 로고
    • A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8
    • Sampson, M. J., Lovell, R. S., Davison, D. B., Craigen, W. J. (1996) A novel mouse mitochondrial voltage-dependent anion channel gene localizes to chromosome 8. Genomics 36, 192-6.
    • (1996) Genomics , vol.36 , pp. 192-196
    • Sampson, M.J.1    Lovell, R.S.2    Davison, D.B.3    Craigen, W.J.4
  • 50
    • 0029040549 scopus 로고
    • Subcellular localization of human voltage-dependent anion channel isoforms
    • Yu, W. H., Wolfgang, W., Forte, M. (1995) Subcellular localization of human voltage-dependent anion channel isoforms. J Biol Chem 270, 13998-4006.
    • (1995) J Biol Chem , vol.270 , pp. 13998-14006
    • Yu, W.H.1    Wolfgang, W.2    Forte, M.3
  • 53
    • 0035823558 scopus 로고    scopus 로고
    • A role for mitochondrial Bak in apoptotic response to anticancer drugs
    • Wang, G. Q. e. a. (2001) A role for mitochondrial Bak in apoptotic response to anticancer drugs. J Biol Chem 276, 34307-17.
    • (2001) J Biol Chem , vol.276 , pp. 34307-34317
    • Wang, G.Q.E.A.1
  • 54
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton, M. (1999) The mitochondrial permeability transition pore and its role in cell death. Biochem J 341, 233-49.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 55
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death
    • Halestrap, A. P., Brenner, C. (2003) The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death. Curr Med Chem 10, 1507-25.
    • (2003) Curr Med Chem , vol.10 , pp. 1507-1525
    • Halestrap, A.P.1    Brenner, C.2
  • 56
    • 0029953927 scopus 로고    scopus 로고
    • Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2{thorn}
    • Brustovetsky, N., Klingenberg, M. (1996) Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2{thorn}. Biochemistry 35, 8483-8.
    • (1996) Biochemistry , vol.35 , pp. 8483-8488
    • Brustovetsky, N.1    Klingenberg, M.2
  • 57
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • Ruck, A., Dolder, M., Wallimann, T., Brdiczka, D. (1998) Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore. FEBS Let. 426, 97-101.
    • (1998) FEBS Let. , vol.426 , pp. 97-101
    • Ruck, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 58
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • Crompton, M., Virji, S., Ward, J. M. (1998) Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore. Eur J Biochem 258, 729-35.
    • (1998) Eur J Biochem , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 59
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • Woodfield, K., Ruck, A., Brdiczka, D., Halestrap, A. P. (1998) Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Biochem J 336, 287-90.
    • (1998) Biochem J , vol.336 , pp. 287-290
    • Woodfield, K.1    Ruck, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 61
    • 0035448294 scopus 로고    scopus 로고
    • Adenine nucleotide translocator isoforms 1 and 2 are differently distributed in the mitochondrial inner membrane and have distinct affinities to cyclophilin D
    • Vyssokikh, M. Y., Katz, A., Rück, A., Wuensch, C., Dörner, A., Zorov, D. B., Brdiczka, D. (2001) Adenine nucleotide translocator isoforms 1 and 2 are differently distributed in the mitochondrial inner membrane and have distinct affinities to cyclophilin D. Biochem. J. 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
  • 63
    • 27144447720 scopus 로고    scopus 로고
    • DNA methylation is required for silencing of ant4, an adenine nucleotide translocase selectively expressed in mouse embryonic stem cells and germ cells
    • Rodic, N., Oka, M., Hamazaki, T., Murawski, M. R., Jorgensen, M., Maatouk, D. M., Resnick, J. L., Li, E., Terada, N. (2005) DNA methylation is required for silencing of ant4, an adenine nucleotide translocase selectively expressed in mouse embryonic stem cells and germ cells. Stem Cells 23, 1314-1323.
    • (2005) Stem Cells , vol.23 , pp. 1314-1323
    • Rodic, N.1    Oka, M.2    Hamazaki, T.3    Murawski, M.R.4    Jorgensen, M.5    Maatouk, D.M.6    Resnick, J.L.7    Li, E.8    Terada, N.9
  • 64
    • 4344707798 scopus 로고    scopus 로고
    • Mitochondrial permeability: dual role for the ADP/ATP translocator?
    • following
    • Halestrap, A. P. (2004) Mitochondrial permeability: dual role for the ADP/ATP translocator? Nature 430, 1 p following 983.
    • (2004) Nature , vol.430 , Issue.1 , pp. 983
    • Halestrap, A.P.1
  • 65
    • 0020482168 scopus 로고
    • Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria
    • Fiek, C., Benz, R., Roos, N., Brdiczka, D. (1982) Evidence for identity between the hexokinase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. Biochim Biophys Acta 688, 429-40.
    • (1982) Biochim Biophys Acta , vol.688 , pp. 429-440
    • Fiek, C.1    Benz, R.2    Roos, N.3    Brdiczka, D.4
  • 66
    • 0020485742 scopus 로고
    • Pore protein and the hexokinasebinding protein from the outer membrane of rat liver mitochondria are identical
    • Lindén, M., Gellerfors, P., Nelson, B. D. (1982) Pore protein and the hexokinasebinding protein from the outer membrane of rat liver mitochondria are identical. FEBS-Letters 141, 189-192.
    • (1982) FEBS-Letters , vol.141 , pp. 189-192
    • Lindén, M.1    Gellerfors, P.2    Nelson, B.D.3
  • 67
    • 0028034636 scopus 로고
    • Vitro complex formation between octamer of creatine kinase and porin
    • Brdiczka, D., Kaldis, P., Wallimann, T. (1994) In vitro complex formation between octamer of creatine kinase and porin. J. Biol. Chem. 269, 27640-27644.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27640-27644
    • Brdiczka, D.1    Kaldis, P.2    Wallimann, T.3
  • 68
    • 0017900492 scopus 로고
    • Ambiquitous enzymes: variation in intracellular distribution as a regulatory mechanism
    • Wilson, J. E. (1978) Ambiquitous enzymes: variation in intracellular distribution as a regulatory mechanism. Trends. Biochem. Sci 3, 124-125.
    • (1978) Trends. Biochem. Sci , vol.3 , pp. 124-125
    • Wilson, J.E.1
  • 69
    • 0027230203 scopus 로고
    • Effect of macromolecules on the structure of the mitochondrial intermembrane space and the regulation of hexokinase
    • Wicker, U., Bücheler, K., Gellerich, F. N., Wagner, M., Kapischke, M., Brdiczka, D. (1993) Effect of macromolecules on the structure of the mitochondrial intermembrane space and the regulation of hexokinase. Biochim. Biophys. Acta 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
  • 70
    • 0021111174 scopus 로고
    • Changes in freeze-fracture mitochondrial membranes correlated to their energetic state
    • Knoll, G., Brdiczka, D. (1983) Changes in freeze-fracture mitochondrial membranes correlated to their energetic state. Biochim. Biophys. Acta 733, 102-110.
    • (1983) Biochim. Biophys. Acta , vol.733 , pp. 102-110
    • Knoll, G.1    Brdiczka, D.2
  • 71
    • 0029117317 scopus 로고
    • Macromolecules increase the channeling of ADP from externally associated hexokinase to the matrix of mitochondria
    • Laterveer, F. D., Gellerich, F. N., Nicolay, K. (1995) Macromolecules increase the channeling of ADP from externally associated hexokinase to the matrix of mitochondria. Eur J Biochem. 232, 569-77.
    • (1995) Eur J Biochem. , vol.232 , pp. 569-577
    • Laterveer, F.D.1    Gellerich, F.N.2    Nicolay, K.3
  • 72
    • 0025103254 scopus 로고
    • Tetrameric structure of mitochondrially bound rat brain hexokinase: A crossliking study
    • Xie, G., Wilson, J. E. (1990) Tetrameric structure of mitochondrially bound rat brain hexokinase: A crossliking study. Arch. Biochem. Biophys 276, 285-293.
    • (1990) Arch. Biochem. Biophys , vol.276 , pp. 285-293
    • Xie, G.1    Wilson, J.E.2
  • 73
    • 0034541155 scopus 로고    scopus 로고
    • Membrane potential-dependent conformational changes in mitochondrially bound hexokinase in brain
    • Hashimoto, M., Wilson, J. E. (2000) Membrane potential-dependent conformational changes in mitochondrially bound hexokinase in brain. Arch. Biochem. Biophys. 884, 163-173.
    • (2000) Arch. Biochem. Biophys. , vol.884 , pp. 163-173
    • Hashimoto, M.1    Wilson, J.E.2
  • 74
    • 0037056002 scopus 로고    scopus 로고
    • Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention
    • Pedersen, P. L., Mathupala, S., Rempel, A., Geschwind, J. F., Ko, Y. H. (2002) Mitochondrial bound type II hexokinase: a key player in the growth and survival of many cancers and an ideal prospect for therapeutic intervention. Biochim Biophys Acta 1555, 14-20.
    • (2002) Biochim Biophys Acta , vol.1555 , pp. 14-20
    • Pedersen, P.L.1    Mathupala, S.2    Rempel, A.3    Geschwind, J.F.4    Ko, Y.H.5
  • 75
    • 0032545759 scopus 로고    scopus 로고
    • Clotrimazole and bifonazole detach hexokinase from mitochondria of melanoma cells
    • Penso, J., Beitner, R. (1998) Clotrimazole and bifonazole detach hexokinase from mitochondria of melanoma cells. Eur J Pharmacol 342, 113-7.
    • (1998) Eur J Pharmacol , vol.342 , pp. 113-117
    • Penso, J.1    Beitner, R.2
  • 76
    • 0001007512 scopus 로고
    • The Crabtree effect: a review
    • Ibsen, H. K. (1961) The Crabtree effect: a review. Cancer Res 21, 829-841.
    • (1961) Cancer Res , vol.21 , pp. 829-841
    • Ibsen, H.K.1
  • 78
    • 0000935827 scopus 로고
    • Localization 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 mitochondria
    • Bücheler, K., Adams, V., Brdiczka, D. (1991) Localization 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 mitochondria. Biochim Biophys Acta 1061, 215-225.
    • (1991) Biochim Biophys Acta , vol.1061 , pp. 215-225
    • Bücheler, K.1    Adams, V.2    Brdiczka, D.3
  • 79
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • Beutner, G., Rück, A., Riede, B., Welte, W., Brdiczka, D. (1996) Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett 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
  • 80
    • 0031044060 scopus 로고    scopus 로고
    • Complexes between hexokinase, mitochondrial porin and adenylate translocator in brain: regulation of hexokinase, oxidative phosphorylation and permeability transition pore
    • Beutner, G., Ruck, A., Riede, B., Brdiczka, D. (1997) Complexes between hexokinase, mitochondrial porin and adenylate translocator in brain: regulation of hexokinase, oxidative phosphorylation and permeability transition pore. Biochem Soc Trans 25, 151-7.
    • (1997) Biochem Soc Trans , vol.25 , pp. 151-157
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 81
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cellfree extracts: requirement for dATP and cytochrome c
    • Liu, X., Kim, C. N., Yang, J., Jemmerson, R., Wang, X. (1996) Induction of apoptotic program in cellfree extracts: requirement for dATP and cytochrome c. Cell 86, 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 82
    • 0033782031 scopus 로고    scopus 로고
    • Cytochrome c release from mitochondria: all or nothing
    • Martinou, J. C., Desagher, S., Antonsson, B. (2000) Cytochrome c release from mitochondria: all or nothing. Nat Cell Biol 2, E41-3.
    • (2000) Nat Cell Biol , vol.2
    • Martinou, J.C.1    Desagher, S.2    Antonsson, B.3
  • 83
    • 0034212442 scopus 로고    scopus 로고
    • Cytochrome c release from isolated rat liver mitochondria can occur independently of outer-membrane rupture: possible role of contact sites
    • Doran, E., Halestrap, A. P. (2000) Cytochrome c release from isolated rat liver mitochondria can occur independently of outer-membrane rupture: possible role of contact sites. Biochem. J., 343-350.
    • (2000) Biochem. J , pp. 343-350
    • Doran, E.1    Halestrap, A.P.2
  • 84
    • 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., Klingenberg, M. (1985) ADP/ ATP carrier protein from beef heart mitochondria has high amounts of tightly bound cardiolipin, as revealed by 31P nuclear magnetic resonance. Biochemistry 24, 3821-3826.
    • (1985) Biochemistry , vol.24 , pp. 3821-3826
    • Beyer, K.1    Klingenberg, M.2
  • 85
    • 0020121213 scopus 로고
    • Purification and characterization of a pore protein of the outer mitochondrial membrane from Neurospora crassa
    • Freitag, H., Neupert, W., Benz, R. (1982) Purification and characterization of a pore protein of the outer mitochondrial membrane from Neurospora crassa. Eur J Biochem 162, 629-636.
    • (1982) Eur J Biochem , vol.162 , pp. 629-636
    • Freitag, H.1    Neupert, W.2    Benz, R.3
  • 86
    • 0028940707 scopus 로고
    • Role of sterols in the functional reconstitution of water-soluble mitochondrial porins from different organisms
    • Popp, B., Schmid, A., Benz, R. (1995) Role of sterols in the functional reconstitution of water-soluble mitochondrial porins from different organisms. Biochemistry 34, 3352-3361.
    • (1995) Biochemistry , vol.34 , pp. 3352-3361
    • Popp, B.1    Schmid, A.2    Benz, R.3
  • 87
    • 0021804591 scopus 로고
    • Lipids of mitochondria
    • Daum, G. (1985) Lipids of mitochondria. Biochim Biophys Acta 822, 1-42.
    • (1985) Biochim Biophys Acta , vol.822 , pp. 1-42
    • Daum, G.1
  • 89
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., Ikonen, E. (1997) Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 90
    • 34247483763 scopus 로고    scopus 로고
    • Function of the Outer Mitochondrial Membrane Pore (Voltage-dependent Anion Channel) in Intracellular Signaling
    • Function, Mechanism (Benz, R., Ed.), Wiley-VCH, Weinheim Germany
    • Vyssokikh, M., Brdiczka, D. (2004) Function of the Outer Mitochondrial Membrane Pore (Voltage-dependent Anion Channel) in Intracellular Signaling, in Bacterial and Eukaryotic Porins Structure, Function, Mechanism (Benz, R., Ed.) pp 339-358, Wiley-VCH, Weinheim Germany.
    • (2004) Bacterial and Eukaryotic Porins Structure , pp. 339-358
    • Vyssokikh, M.1    Brdiczka, D.2
  • 91
    • 0033557949 scopus 로고    scopus 로고
    • Increased Sensitivity of Acute Myeloid Leukemias to Lovastatin-Induced Apoptosis: A Potential Therapeutic Approach
    • Dimitroulakos, J., Nohynek, D., Backway, K. L., Hedley, D. W., Yeger, H., Freedman, M. H., Minden, M. D., Penn, L. Z. (1999) Increased Sensitivity of Acute Myeloid Leukemias to Lovastatin-Induced Apoptosis: A Potential Therapeutic Approach. Blood 93, 1308-1318.
    • (1999) Blood , vol.93 , pp. 1308-1318
    • Dimitroulakos, J.1    Nohynek, D.2    Backway, K.L.3    Hedley, D.W.4    Yeger, H.5    Freedman, M.H.6    Minden, M.D.7    Penn, L.Z.8
  • 92
    • 0020489067 scopus 로고
    • Possible role of non-bilayer lipids in the structure of mitochondria A freezefracture electron microscopy study
    • Van Venetie, R., Verkleij, A. J. (1982) Possible role of non-bilayer lipids in the structure of mitochondria A freezefracture electron microscopy study. Biochim Biophys Acta 692, 397-405.
    • (1982) Biochim Biophys Acta , vol.692 , pp. 397-405
    • Van Venetie, R.1    Verkleij, A.J.2
  • 93
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: releasing power for life and unleashing the machineries of death
    • Newmeyer, D. D., Ferguson-Miller, S. (2003) Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112, 481-90.
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 94
    • 1042302135 scopus 로고    scopus 로고
    • The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis
    • Iverson, S. L., Orrenius, S. (2004) The cardiolipin-cytochrome c interaction and the mitochondrial regulation of apoptosis. Archives of Biochemistry and Biophysics 423, 37-46.
    • (2004) Archives of Biochemistry and Biophysics , vol.423 , pp. 37-46
    • Iverson, S.L.1    Orrenius, S.2
  • 97
    • 0034306169 scopus 로고    scopus 로고
    • Cardiolipin provides specificity for targeting of tBid to mitochondria
    • Lutter, M., Fang, M., Luo, X., Nishijima, M., Xie, X., Wang, X. (2000) Cardiolipin provides specificity for targeting of tBid to mitochondria. Nat Cell Biol 2, 754-61.
    • (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
  • 99
    • 0033615649 scopus 로고    scopus 로고
    • Functional consequences of sustained or transient activation by Bax of the mitochondrial permeability transition pore
    • Pastorino, J. G., Tafani, M., Rothman, R. J., Marcineviciute, A., Hoek, J. B., Farber, J. L. (1999) Functional consequences of sustained or transient activation by Bax of the mitochondrial permeability transition pore. J. Biol. Chem. 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
  • 100
    • 0036799548 scopus 로고    scopus 로고
    • Biphasic translocation of BAX to mitochondria
    • Capano, M., Crompton, M. (2002) Biphasic translocation of BAX to mitochondria. Biochem J 367, 169-178.
    • (2002) Biochem J , vol.367 , pp. 169-178
    • Capano, M.1    Crompton, M.2
  • 102
    • 0034983918 scopus 로고    scopus 로고
    • Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase
    • Gottlob, K., Majewski, N., Kennedy, S., Kandel, E., Robey, R., Hay, N. (2001) Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase. Genes Dev. 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.5    Hay, N.6
  • 104
    • 0036042248 scopus 로고    scopus 로고
    • Bax releases cytochrome c preferentially from a complex between porin and adenine nucleotide translocator
    • Hexokinase activity suppresses this effect
    • Vyssokikh, M. Y., Zorova, L., Zorov, D., Heimlich, G., Jürgensmeier, J. M., Brdiczka, D. (2002) Bax releases cytochrome c preferentially from a complex between porin and adenine nucleotide translocator. Hexokinase activity suppresses this effect. Mol. Biol. Rep. 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
  • 105
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits bax-induced cytochrome c release and apoptosis
    • Pastorino, J. G., Shulga, N., Hoek, J. B. (2002) Mitochondrial binding of hexokinase II inhibits bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277, 7610-7618.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 106
    • 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., Rück, A., Riede, B., Brdiczka, D. (1998) 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, 7-18.
    • (1998) Biochim. Biophys. Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Rück, A.2    Riede, B.3    Brdiczka, D.4
  • 107
    • 0141905919 scopus 로고    scopus 로고
    • Roles of 50-AMPactivated protein kinase (AMPK) in mammalian glucose homeostasis
    • Rutter, G. A., Da Silva Xavier, G., Leclerc, I. (2003) Roles of 50-AMPactivated protein kinase (AMPK) in mammalian glucose homeostasis. Biochem. J. 375, 1-16.
    • (2003) Biochem. J. , vol.375 , pp. 1-16
    • Rutter, G.A.1    Da Silva Xavier, G.2    Leclerc, I.3
  • 108
    • 0041854190 scopus 로고    scopus 로고
    • AMPK activation increases uncoupling protein-3 expression and mitochondrial enzyme activities in rat muscle without fibre type transitions
    • Putman, C. T., Kiricsi, M., Pearcey, J., MacLean, I. M., Bamford, J. A., Murdoch, G. K., Dixon, W. T., Pette, D. (2003) AMPK activation increases uncoupling protein-3 expression and mitochondrial enzyme activities in rat muscle without fibre type transitions. J. Physiol. 551, 169-178.
    • (2003) J. Physiol. , vol.551 , pp. 169-178
    • Putman, C.T.1    Kiricsi, M.2    Pearcey, J.3    MacLean, I.M.4    Bamford, J.A.5    Murdoch, G.K.6    Dixon, W.T.7    Pette, D.8
  • 109
    • 0031041578 scopus 로고    scopus 로고
    • Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat
    • Parra, J., Brdiczka, D., Cusso, R., Pette, D. (1997) Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat. FEBS Lett 403, 279-282.
    • (1997) FEBS Lett , vol.403 , pp. 279-282
    • Parra, J.1    Brdiczka, D.2    Cusso, R.3    Pette, D.4
  • 110
    • 0035793432 scopus 로고    scopus 로고
    • The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes
    • Blasquez, C., Geelen, M. J., Velasco, G., Guzman, M. (2001) The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes. FEBS Lett 489, 149-153.
    • (2001) FEBS Lett , vol.489 , pp. 149-153
    • Blasquez, C.1    Geelen, M.J.2    Velasco, G.3    Guzman, M.4
  • 111
    • 0035930592 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase and mitochondrial outer membrane porin show direct interaction that is modulated by calcium
    • Schlattner, U., Dolder, M., Wallimann, T., Tokarska-Schlattner, M. (2001) Mitochondrial creatine kinase and mitochondrial outer membrane porin show direct interaction that is modulated by calcium. J. Biol. Chem. 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
  • 112
    • 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., Eriksson, O. (2005) Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane. Biochem J 385, 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
  • 114
    • 1642588263 scopus 로고    scopus 로고
    • Free radical induced inactivation of creatine kinase: influence on the octameric and dimeric states of the mitochondrial enzyme (Mib-CK)
    • Koufen, P., Rück, A., Brdiczka, D., Wendt, S., Wallimann, T., Stark, G. (1999) Free radical induced inactivation of creatine kinase: influence on the octameric and dimeric states of the mitochondrial enzyme (Mib-CK). Biochem J. 344, 413-417.
    • (1999) Biochem J. , vol.344 , pp. 413-417
    • Koufen, P.1    Rück, A.2    Brdiczka, D.3    Wendt, S.4    Wallimann, T.5    Stark, G.6
  • 115
    • 0032479147 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation
    • Stachowiak, O., Dolder, M., Wallimann, T., Richter, C. (1998) Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation. J Biol Chem 273, 16694-9.
    • (1998) J Biol Chem , vol.273 , pp. 16694-16699
    • Stachowiak, O.1    Dolder, M.2    Wallimann, T.3    Richter, C.4
  • 116
    • 0029144638 scopus 로고
    • Nitric oxide and oxygen radicals: a question of balance
    • Darley-Usmar, V., Wiseman, H., Halliwell, B. (1995) Nitric oxide and oxygen radicals: a question of balance. FEBS Lett 369, 131-5.
    • (1995) FEBS Lett , vol.369 , pp. 131-135
    • Darley-Usmar, V.1    Wiseman, H.2    Halliwell, B.3
  • 117
    • 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., Wallimann, T. (2003) Differential effects of peroxynitrite on human mitochondrial creatine kinase isoenzymes Inactivation, octamer destabilization, and identification of involved residues. J Biol Chem 278, 1125-30.
    • (2003) J Biol Chem , vol.278 , pp. 1125-1130
    • Wendt, S.1    Schlattner, U.2    Wallimann, T.3
  • 119
  • 120
    • 0036073201 scopus 로고    scopus 로고
    • Mitochondrial creatine kinase is critically necessary for normal myocardial high-energy phosphate metabolism
    • Spindler, M., Niebler, R., Remkes, H., Horn, M., Lanz, T., Neubauer, S. (2002) Mitochondrial creatine kinase is critically necessary for normal myocardial high-energy phosphate metabolism. Am J Physiol Heart Circ Physiol 283, H680-7.
    • (2002) Am J Physiol Heart Circ Physiol , vol.283
    • Spindler, M.1    Niebler, R.2    Remkes, H.3    Horn, M.4    Lanz, T.5    Neubauer, S.6
  • 121
    • 4143141967 scopus 로고    scopus 로고
    • Creatine kinasedeficient hearts exhibit increased susceptibility to ischemia-reperfusion injury and impaired calcium homeostasis
    • Spindler, M., Meyer, K., Stromer, H., Leupold, A., Boehm, E., Wagner, H., Neubauer, S. (2004) Creatine kinasedeficient hearts exhibit increased susceptibility to ischemia-reperfusion injury and impaired calcium homeostasis. Am J Physiol Heart Circ Physiol 287, H1039-45.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287
    • Spindler, M.1    Meyer, K.2    Stromer, H.3    Leupold, A.4    Boehm, E.5    Wagner, H.6    Neubauer, S.7
  • 122
    • 0142187307 scopus 로고    scopus 로고
    • Signaling and cellular mechanisms in cardiac protection by ischemic and pharmacological preconditioning
    • Zaugg, M., Schaub, M. C. (2003) Signaling and cellular mechanisms in cardiac protection by ischemic and pharmacological preconditioning. J Muscle Res Cell Motil 24, 219-49.
    • (2003) J Muscle Res Cell Motil , vol.24 , pp. 219-249
    • Zaugg, M.1    Schaub, M.C.2
  • 123
    • 0034976578 scopus 로고    scopus 로고
    • Cardioprotection by ischemic preconditioning preserves mitochondrial function and functional coupling between adenine nucleotide translocase and creatine kinase
    • Laclau, M. N., Boudina, S., Thambo, J. B., Tariosse, L., Gouverneur, G., Bonoron-Adele, S., Saks, V. A., Garlid, K. D., Dos Santos, P. (2001) Cardioprotection by ischemic preconditioning preserves mitochondrial function and functional coupling between adenine nucleotide translocase and creatine kinase. J Mol Cell Cardiol 33, 947-56.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 947-956
    • Laclau, M.N.1    Boudina, S.2    Thambo, J.B.3    Tariosse, L.4    Gouverneur, G.5    Bonoron-Adele, S.6    Saks, V.A.7    Garlid, K.D.8    Dos Santos, P.9
  • 125
    • 0032482127 scopus 로고    scopus 로고
    • Impaired cardiac energetics in mice lacking musclespecific isoenzymes of creatine kinase
    • Saupe, K. W., Spindler, M., Tian, R., Ingwall, J. S. (1998) Impaired cardiac energetics in mice lacking musclespecific isoenzymes of creatine kinase. Circ Res. 82, 898-907.
    • (1998) Circ Res. , vol.82 , pp. 898-907
    • Saupe, K.W.1    Spindler, M.2    Tian, R.3    Ingwall, J.S.4
  • 126
    • 0030010439 scopus 로고    scopus 로고
    • Decreased energy reserve in an animal model of dilated cardiomyopathy
    • Relationship to contractile performance
    • Liao, R., Nascimben, L., Friedrich, J., Gwathmey, J. K., Ingwall, J. S. (1996) Decreased energy reserve in an animal model of dilated cardiomyopathy. Relationship to contractile performance. Circ Res. 78, 893-902.
    • (1996) Circ Res. , vol.78 , pp. 893-902
    • Liao, R.1    Nascimben, L.2    Friedrich, J.3    Gwathmey, J.K.4    Ingwall, J.S.5
  • 127
    • 12444260720 scopus 로고    scopus 로고
    • Alterations in the myocardial creatine kinase system precede the development of contractile dysfunction in beta[1]-adrenergic receptor transgenic mice
    • Spindler, M., Engelhardt, S., Niebler, R., Wagner, H., Hein, L., Lohse, M. J., Neubauer, S. (2003) Alterations in the myocardial creatine kinase system precede the development of contractile dysfunction in beta[1]-adrenergic receptor transgenic mice. J Mol Cell Cardiol 35, 389-97.
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 389-397
    • Spindler, M.1    Engelhardt, S.2    Niebler, R.3    Wagner, H.4    Hein, L.5    Lohse, M.J.6    Neubauer, S.7
  • 130
    • 0026640887 scopus 로고
    • Structurefunction of the ADP/ATP carrier Biochem Soc Trans
    • Klingenberg, M. (1992) Structurefunction of the ADP/ATP carrier Biochem Soc Trans 20, 547-50.
    • (1992) , vol.20 , pp. 547-550
    • Klingenberg, M.1
  • 131
  • 132
    • 0025170604 scopus 로고
    • The mitochondrial aspartate/glutamate and ADP/ATP carrier switch from obligate counterexchange to unidirectional transport after modification by SHreagents
    • Dierks, T., Salentin, A., Heberger, C., Krämer, R. (1990) The mitochondrial aspartate/glutamate and ADP/ATP carrier switch from obligate counterexchange to unidirectional transport after modification by SHreagents. Biochim. Biophys. Acta 1028, 268-280.
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 268-280
    • Dierks, T.1    Salentin, A.2    Heberger, C.3    Krämer, R.4
  • 133
  • 134
    • 0019230323 scopus 로고
    • Allosteric inhibition of the Ca2{thorn}activated hydrophilic channel of the mitochondrial inner membrane by nucleotides
    • Haworth, R. A., Hunter, P. R. (1980) Allosteric inhibition of the Ca2{thorn}activated hydrophilic channel of the mitochondrial inner membrane by nucleotides. J. Membr. Biol. 57, 231-236.
    • (1980) J. Membr. Biol. , vol.57 , pp. 231-236
    • Haworth, R.A.1    Hunter, P.R.2
  • 135
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas, F., Jouaville, L. S., Mazat, J. P. (1997) Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell 89, 1145-1153.
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 136
    • 0029998621 scopus 로고    scopus 로고
    • The permeability transition pore as a mitochondrial calcium release channel: a critical appraisal
    • Bernardi, P., Petronilli, V. (1996) The permeability transition pore as a mitochondrial calcium release channel: a critical appraisal. J Bioenerg Biomembr 28, 131-8.
    • (1996) J Bioenerg Biomembr , vol.28 , pp. 131-138
    • Bernardi, P.1    Petronilli, V.2
  • 137
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S. S., Skulachev, V. P., Starkov, A. A. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 416, 15-18.
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 138
    • 0842323739 scopus 로고    scopus 로고
    • Interplay between mitochondria and cellular calcium signalling
    • Jacobson, J., Duchen, M. R. (2004) Interplay between mitochondria and cellular calcium signalling. Mol. Cell. Biochem. 256/257, 209-218.
    • (2004) Mol. Cell. Biochem , vol.256 , pp. 209-218
    • Jacobson, J.1    Duchen, M.R.2
  • 139
    • 0038381490 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by creatine kinase substrates
    • Requirement for micro-compartmentation
    • Dolder, M., Walzel, B., Speer, O., Schlattner, U., Wallimann, T. (2003) Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for micro-compartmentation. J Biol Chem 278, 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
  • 140
    • 3342967512 scopus 로고    scopus 로고
    • Is the Failing Heart Energy Starved? On Using Chemical Energy to Support Cardiac Function
    • Ingwall, J. S., Weiss, R. G. (2004) Is the Failing Heart Energy Starved? On Using Chemical Energy to Support Cardiac Function. Circ Res. 95, 35-145.
    • (2004) Circ Res. , vol.95 , pp. 35-145
    • Ingwall, J.S.1    Weiss, R.G.2
  • 141
    • 0030008105 scopus 로고    scopus 로고
    • Energetic basis for reduced contractile reserve in isolated rat hearts
    • Tian, R., Ingwall, J. S. (1996) Energetic basis for reduced contractile reserve in isolated rat hearts. Am. J. Physiol. 270, H1207-H1216.
    • (1996) Am. J. Physiol. , vol.270
    • Tian, R.1    Ingwall, J.S.2
  • 143
    • 0034111130 scopus 로고    scopus 로고
    • Oral creatine supplementation in Duchenne muscular dystrophy: a clinical and 31P magnetic resonance spectroscopy study
    • Felber, S., Skladal, D., Wyss, M., Kremser, C., Koller, A., Sperl, W. (2000) Oral creatine supplementation in Duchenne muscular dystrophy: a clinical and 31P magnetic resonance spectroscopy study. Neurol Res 22, 145-50.
    • (2000) Neurol Res , vol.22 , pp. 145-150
    • Felber, S.1    Skladal, D.2    Wyss, M.3    Kremser, C.4    Koller, A.5    Sperl, W.6
  • 144
    • 0030731246 scopus 로고    scopus 로고
    • A randomized, controlled trial of creatine monohydrate in patients with mitochondrial cytopathies
    • Tarnopolsky, M. A., Roy, B. D., MacDonald, J. R. (1997) A randomized, controlled trial of creatine monohydrate in patients with mitochondrial cytopathies. Muscle Nerve 20, 1502-9.
    • (1997) Muscle Nerve , vol.20 , pp. 1502-1509
    • Tarnopolsky, M.A.1    Roy, B.D.2    MacDonald, J.R.3
  • 146
    • 0942287666 scopus 로고    scopus 로고
    • Additive neuroprotective effects of creatine and cyclooxygenase 2 inhibitors in a transgenic mouse model of amyotrophic lateral sclerosis
    • Klivenyi, P., Kiaei, M., Gardian, G., Calingasan, N. Y., Beal, M. F. (2004) Additive neuroprotective effects of creatine and cyclooxygenase 2 inhibitors in a transgenic mouse model of amyotrophic lateral sclerosis. J Neurochem 88, 576-82.
    • (2004) J Neurochem , vol.88 , pp. 576-582
    • Klivenyi, P.1    Kiaei, M.2    Gardian, G.3    Calingasan, N.Y.4    Beal, M.F.5
  • 148
    • 0038115294 scopus 로고    scopus 로고
    • Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice
    • Dedeoglu, A., Kubilus, J. K., Yang, L., Ferrante, K. L., Hersch, S. M., Beal, M. F., Ferrante, R. J. (2003) Creatine therapy provides neuroprotection after onset of clinical symptoms in Huntington's disease transgenic mice. J Neurochem 85, 1359-67.
    • (2003) J Neurochem , vol.85 , pp. 1359-1367
    • Dedeoglu, A.1    Kubilus, J.K.2    Yang, L.3    Ferrante, K.L.4    Hersch, S.M.5    Beal, M.F.6    Ferrante, R.J.7
  • 149
    • 4344680646 scopus 로고    scopus 로고
    • Additive neuroprotective effects of creatine and a cyclooxygenase 2 inhibitor against dopamine depletion in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease
    • Klivenyi, P., Gardian, G., Calingasan, N. Y., Yang, L., Beal, M. F. (2003) Additive neuroprotective effects of creatine and a cyclooxygenase 2 inhibitor against dopamine depletion in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease. J Mol Neurosci 21, 191-8.
    • (2003) J Mol Neurosci , vol.21 , pp. 191-198
    • Klivenyi, P.1    Gardian, G.2    Calingasan, N.Y.3    Yang, L.4    Beal, M.F.5
  • 150
    • 0036949481 scopus 로고    scopus 로고
    • Neuroprotection of creatine supplementation in neonatal rats with transient cerebral hypoxia-ischemia Dev Neurosci
    • Adcock, K. H., Nedelcu, J., Loenneker, T., Martin, E., Wallimann, T., Wagner, B. P. (2002) Neuroprotection of creatine supplementation in neonatal rats with transient cerebral hypoxia-ischemia Dev Neurosci 24, 382-8.
    • (2002) , vol.24 , pp. 382-388
    • Adcock, K.H.1    Nedelcu, J.2    Loenneker, T.3    Martin, E.4    Wallimann, T.5    Wagner, B.P.6
  • 152
    • 1842427203 scopus 로고    scopus 로고
    • Creatine: are the benefits worth the risk?
    • Brudnak, M. A. (2004) Creatine: are the benefits worth the risk? Toxicol Lett 150, 123-130.
    • (2004) Toxicol Lett , vol.150 , pp. 123-130
    • Brudnak, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.