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Volumn 1828, Issue 9, 2013, Pages 2121-2133

Progressive stages of mitochondrial destruction caused by cell toxic bile salts

Author keywords

Bile salts; Cholestasis; Liver; Mitochondria; Mitochondrial permeability transition

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; BILE SALT; CALCIUM; GLYCOCHENODEOXYCHOLIC ACID; LIPOSOME; TAUROCHENODEOXYCHOLIC ACID; TAUROURSODEOXYCHOLIC ACID; 4-METHYLUMBELLIFERYL PHOSPHATE; CARBONYL CYANIDE 4 (TRIFLUOROMETHOXY)PHENYLHYDRAZONE; CARRIER PROTEIN; CYCLOSPORIN A; CYTOCHROME C; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; PHOSPHATIDYLCHOLINE; REACTIVE OXYGEN METABOLITE; RHODAMINE 123; ROS; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 84879234547     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.05.007     Document Type: Article
Times cited : (65)

References (77)
  • 1
    • 0017089948 scopus 로고
    • Relationship between configuration, function, and permeability in calcium-treated mitochondria
    • D.R. Hunter, R.A. Haworth, and J.H. Southard Relationship between configuration, function, and permeability in calcium-treated mitochondria J. Biol. Chem. 251 1976 5069 5077
    • (1976) J. Biol. Chem. , vol.251 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 2
    • 0027508994 scopus 로고
    • 2+
    • V. Petronilli, C. Cola, and P. Bernardi Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore. II. The minimal requirements for pore induction underscore a key role for transmembrane electrical potential, matrix pH, and matrix Ca2 + J. Biol. Chem. 268 1993 1011 1016 (Pubitemid 23019735)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.2 , pp. 1011-1016
    • Petronilli, V.1    Cola, C.2    Bernardi, P.3
  • 3
    • 0030613796 scopus 로고    scopus 로고
    • Bcl-x(L) regulates the membrane potential and volume homeostasis of mitochondria
    • M.G. Vander Heiden, N.S. Chandel, E.K. Williamson, P.T. Schumacker, and C.B. Thompson Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria Cell 91 1997 627 637 (Pubitemid 27513654)
    • (1997) Cell , vol.91 , Issue.5 , pp. 627-637
    • Vander Heiden, M.G.1    Chandel, N.S.2    Williamson, E.K.3    Schumacker, P.T.4    Thompson, C.B.5
  • 4
    • 33746912767 scopus 로고    scopus 로고
    • The permeability transition pore complex in cancer cell death
    • DOI 10.1038/sj.onc.1209609, PII 1209609
    • C. Brenner, and S. Grimm The permeability transition pore complex in cancer cell death Oncogene 25 2006 4744 4756 (Pubitemid 44192088)
    • (2006) Oncogene , vol.25 , Issue.34 , pp. 4744-4756
    • Brenner, C.1    Grimm, S.2
  • 6
    • 34247540380 scopus 로고    scopus 로고
    • The permeability transition pore in cell death
    • DOI 10.1007/s10495-007-0747-3, Special Issue on Mitochondria in Apoptosis
    • S. Grimm, and D. Brdiczka The permeability transition pore in cell death Apoptosis 12 2007 841 855 (Pubitemid 46653295)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 841-855
    • Grimm, S.1    Brdiczka, D.2
  • 7
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • DOI 10.1152/physrev.00013.2006
    • G. Kroemer, L. Galluzzi, and C. Brenner Mitochondrial membrane permeabilization in cell death Physiol. Rev. 87 2007 99 163 (Pubitemid 46209992)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 8
    • 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
    • M. Crompton, S. Virji, and J.M. Ward 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 1998 729 735 (Pubitemid 28557940)
    • (1998) European Journal of Biochemistry , vol.258 , Issue.2 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 9
    • 77955955395 scopus 로고    scopus 로고
    • A pore way to die: The role of mitochondria in reperfusion injury and cardioprotection
    • A.P. Halestrap A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection Biochem. Soc. Trans. 38 2010 841 860
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 841-860
    • Halestrap, A.P.1
  • 10
    • 17144417734 scopus 로고    scopus 로고
    • A historical review of cellular calcium handling, with emphasis on mitochondria
    • DOI 10.1007/s10541-005-0100-9
    • N.E. Saris, and E. Carafoli A historical review of cellular calcium handling, with emphasis on mitochondria Biochemistry (Mosc.) 70 2005 187 194 (Pubitemid 40512327)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.2 , pp. 187-194
    • Saris, N.-E.L.1    Carafoli, E.2
  • 11
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • DOI 10.1038/ncb1575, PII NCB1575
    • C.P. Baines, R.A. Kaiser, T. Sheiko, W.J. Craigen, and J.D. Molkentin Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat. Cell Biol. 9 2007 550 555 (Pubitemid 46696536)
    • (2007) Nature Cell Biology , vol.9 , Issue.5 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 12
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function?
    • DOI 10.1016/S0014-5793(01)03314-2, PII S0014579301033142
    • L. He, and J.J. Lemasters Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function? FEBS Lett. 512 2002 1 7 (Pubitemid 34164440)
    • (2002) FEBS Letters , vol.512 , Issue.1-3 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 13
    • 33645994183 scopus 로고    scopus 로고
    • Calcium, mitochondria and reperfusion injury: A pore way to die
    • A.P. Halestrap Calcium, mitochondria and reperfusion injury: a pore way to die Biochem. Soc. Trans. 34 2006 232 237
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 232-237
    • Halestrap, A.P.1
  • 14
    • 34247506768 scopus 로고    scopus 로고
    • A tale of two mitochondrial channels, MAC and PTP, in apoptosis
    • K.W. Kinnally, and B. Antonsson A tale of two mitochondrial channels, MAC and PTP, in apoptosis Apoptosis 2007
    • (2007) Apoptosis
    • Kinnally, K.W.1    Antonsson, B.2
  • 15
    • 34247485841 scopus 로고    scopus 로고
    • Role of the mitochondrial membrane permeability transition in cell death
    • DOI 10.1007/s10495-006-0525-7, Special Issue on Mitochondria in Apoptosis
    • Y. Tsujimoto, and S. Shimizu Role of the mitochondrial membrane permeability transition in cell death Apoptosis 12 2007 835 840 (Pubitemid 46653286)
    • (2007) Apoptosis , vol.12 , Issue.5 , pp. 835-840
    • Tsujimoto, Y.1    Shimizu, S.2
  • 16
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • DOI 10.1126/science.1099320
    • D.R. Green, and G. Kroemer The pathophysiology of mitochondrial cell death Science 305 2004 626 629 (Pubitemid 39006738)
    • (2004) Science , vol.305 , Issue.5684 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 17
    • 58149352994 scopus 로고    scopus 로고
    • Targeting mitochondrial permeability in cancer drug development
    • M.V. Berridge, P.M. Herst, and A. Lawen Targeting mitochondrial permeability in cancer drug development Mol. Nutr. Food Res. 53 2009 76 86
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 76-86
    • Berridge, M.V.1    Herst, P.M.2    Lawen, A.3
  • 19
    • 84862663864 scopus 로고    scopus 로고
    • Effect of ursodeoxycholic acid on bile acid profiles and intestinal detoxification machinery in primary biliary cirrhosis and health
    • K. Dilger, S. Hohenester, U. Winkler-Budenhofer, B.A. Bastiaansen, F.G. Schaap, C. Rust, and U. Beuers Effect of ursodeoxycholic acid on bile acid profiles and intestinal detoxification machinery in primary biliary cirrhosis and health J. Hepatol. 57 2012 133 140
    • (2012) J. Hepatol. , vol.57 , pp. 133-140
    • Dilger, K.1    Hohenester, S.2    Winkler-Budenhofer, U.3    Bastiaansen, B.A.4    Schaap, F.G.5    Rust, C.6    Beuers, U.7
  • 20
    • 21744449745 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-dependent signaling modulates taurochenodeoxycholic acid-induced liver injury and cholestasis in perfused rat livers
    • C. Rust, K. Bauchmuller, P. Fickert, A. Fuchsbichler, and U. Beuers Phosphatidylinositol 3-kinase-dependent signaling modulates taurochenodeoxycholic acid-induced liver injury and cholestasis in perfused rat livers Am. J. Physiol. Gastrointest. Liver Physiol. 289 2005 G88 94
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.289 , pp. 88-94
    • Rust, C.1    Bauchmuller, K.2    Fickert, P.3    Fuchsbichler, A.4    Beuers, U.5
  • 21
    • 65649124573 scopus 로고    scopus 로고
    • Bile-acid-induced cell injury and protection
    • M.J. Perez, and O. Briz Bile-acid-induced cell injury and protection World J. Gastroenterol. 15 2009 1677 1689
    • (2009) World J. Gastroenterol. , vol.15 , pp. 1677-1689
    • Perez, M.J.1    Briz, O.2
  • 22
    • 77957338101 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-kinase p110gamma contributes to bile salt-induced apoptosis in primary rat hepatocytes and human hepatoma cells
    • S. Hohenester, A. Gates, R. Wimmer, U. Beuers, M.S. Anwer, C. Rust, and C.R. Webster Phosphatidylinositol-3-kinase p110gamma contributes to bile salt-induced apoptosis in primary rat hepatocytes and human hepatoma cells J. Hepatol. 53 2010 918 926
    • (2010) J. Hepatol. , vol.53 , pp. 918-926
    • Hohenester, S.1    Gates, A.2    Wimmer, R.3    Beuers, U.4    Anwer, M.S.5    Rust, C.6    Webster, C.R.7
  • 23
    • 4444311570 scopus 로고    scopus 로고
    • Mitochondrially-mediated toxicity of bile acids
    • DOI 10.1016/j.tox.2004.06.001, PII S0300483X04003269
    • C.M. Palmeira, and A.P. Rolo Mitochondrially-mediated toxicity of bile acids Toxicology 203 2004 1 15 (Pubitemid 39200934)
    • (2004) Toxicology , vol.203 , Issue.1-3 , pp. 1-15
    • Palmeira, C.M.1    Rolo, A.P.2
  • 24
    • 0033852206 scopus 로고    scopus 로고
    • Bile acids affect liver mitochondrial bioenergetics: Possible relevance for cholestasis therapy
    • A.P. Rolo, P.J. Oliveira, A.J. Moreno, and C.M. Palmeira Bile acids affect liver mitochondrial bioenergetics: possible relevance for cholestasis therapy Toxicol. Sci. 57 2000 177 185
    • (2000) Toxicol. Sci. , vol.57 , pp. 177-185
    • Rolo, A.P.1    Oliveira, P.J.2    Moreno, A.J.3    Palmeira, C.M.4
  • 25
    • 0028816461 scopus 로고
    • Ursodeoxycholate (UDCA) inhibits the mitochondrial membrane permeability transition induced by glycochenodeoxycholate: A mechanism of UDCA cytoprotection
    • R. Botla, J.R. Spivey, H. Aguilar, S.F. Bronk, and G.J. Gores Ursodeoxycholate (UDCA) inhibits the mitochondrial membrane permeability transition induced by glycochenodeoxycholate: a mechanism of UDCA cytoprotection J. Pharmacol. Exp. Ther. 272 1995 930 938
    • (1995) J. Pharmacol. Exp. Ther. , vol.272 , pp. 930-938
    • Botla, R.1    Spivey, J.R.2    Aguilar, H.3    Bronk, S.F.4    Gores, G.J.5
  • 26
    • 0032504695 scopus 로고    scopus 로고
    • Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis: A potential role for mitochondrial proteases
    • DOI 10.1016/S0005-2728(98)00111-X, PII S000527289800111X
    • G.J. Gores, H. Miyoshi, R. Botla, H.I. Aguilar, and S.F. Bronk Induction of the mitochondrial permeability transition as a mechanism of liver injury during cholestasis: a potential role for mitochondrial proteases Biochim. Biophys. Acta 1366 1998 167 175 (Pubitemid 28467030)
    • (1998) Biochimica et Biophysica Acta - Bioenergetics , vol.1366 , Issue.1-2 , pp. 167-175
    • Gores, G.J.1    Miyoshi, H.2    Botla, R.3    Aguilar, H.I.4    Bronk, S.F.5
  • 29
    • 0032502866 scopus 로고    scopus 로고
    • Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: The impact of irreversible permeability transition
    • DOI 10.1016/S0014-5793(98)00318-4, PII S0014579398003184
    • P.X. Petit, M. Goubern, P. Diolez, S.A. Susin, N. Zamzami, and G. Kroemer Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: the impact of irreversible permeability transition FEBS Lett. 426 1998 111 116 (Pubitemid 28198166)
    • (1998) FEBS Letters , vol.426 , Issue.1 , pp. 111-116
    • Petit, P.X.1    Goubern, M.2    Diolez, P.3    Susin, S.A.4    Zamzami, N.5    Kroemer, G.6
  • 30
    • 0033927209 scopus 로고    scopus 로고
    • Quantitation of mitochondrial transmembrane potential in cells and in isolated mitochondria
    • N. Zamzami, D. Metivier, and G. Kroemer Quantitation of mitochondrial transmembrane potential in cells and in isolated mitochondria Methods Enzymol. 322 2000 208 213 (Pubitemid 30482057)
    • (2000) Methods in Enzymology , vol.322 , pp. 208-213
    • Zamzami, N.1    Metivier, D.2    Kroemer, G.3
  • 32
    • 35448934538 scopus 로고    scopus 로고
    • Free-flow electrophoresis for purification of plant mitochondria by surface charge
    • DOI 10.1111/j.1365-313X.2007.03253.x
    • H. Eubel, C.P. Lee, J. Kuo, E.H. Meyer, N.L. Taylor, and A.H. Millar Free-flow electrophoresis for purification of plant mitochondria by surface charge Plant J. 52 2007 583 594 (Pubitemid 47621877)
    • (2007) Plant Journal , vol.52 , Issue.3 , pp. 583-594
    • Eubel, H.1    Lee, C.P.2    Kuo, J.3    Meyer, E.H.4    Taylor, N.L.5    Millar, A.H.6
  • 34
    • 84934443121 scopus 로고    scopus 로고
    • Purification of Saccharomyces cerevisiae mitochondria by zone electrophoresis in a free flow device
    • H. Zischka, N. Kinkl, R.J. Braun, and M. Ueffing Purification of Saccharomyces cerevisiae mitochondria by zone electrophoresis in a free flow device Methods Mol. Biol. 432 2008 51 64
    • (2008) Methods Mol. Biol. , vol.432 , pp. 51-64
    • Zischka, H.1    Kinkl, N.2    Braun, R.J.3    Ueffing, M.4
  • 37
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • DOI 10.1016/S0014-5793(98)00317-2, PII S0014579398003172
    • A. Ruck, M. Dolder, T. Wallimann, and D. Brdiczka Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore FEBS Lett. 426 1998 97 101 (Pubitemid 28198163)
    • (1998) FEBS Letters , vol.426 , Issue.1 , pp. 97-101
    • Ruck, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 38
    • 0023651581 scopus 로고
    • A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues
    • V. de Pinto, G. Prezioso, and F. Palmieri A simple and rapid method for the purification of the mitochondrial porin from mammalian tissues Biochim. Biophys. Acta 905 1987 499 502
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 499-502
    • De Pinto, V.1    Prezioso, G.2    Palmieri, F.3
  • 39
    • 0035866407 scopus 로고    scopus 로고
    • Apoptosis induction by the photosensitizer verteporfin: Identification of mitochondrial adenine nucleotide translocator as a critical target
    • A.S. Belzacq, E. Jacotot, H.L. Vieira, D. Mistro, D.J. Granville, Z. Xie, J.C. Reed, G. Kroemer, and C. Brenner Apoptosis induction by the photosensitizer verteporfin: identification of mitochondrial adenine nucleotide translocator as a critical target Cancer Res. 61 2001 1260 1264 (Pubitemid 34292537)
    • (2001) Cancer Research , vol.61 , Issue.4 , pp. 1260-1264
    • Belzacq, A.-S.1    Jacotot, E.2    Vieira, H.L.A.3    Mistro, D.4    Granville, D.J.5    Xie, Z.6    Reed, J.C.7    Kroemer, G.8    Brenner, C.9
  • 45
    • 0015676651 scopus 로고
    • Determination of bile acids in needle biopsies of human liver
    • H. Greim, P. Czygan, F. Schaffner, and H. Popper Determination of bile acids in needle biopsies of human liver Biochem. Med. 8 1973 280 286
    • (1973) Biochem. Med. , vol.8 , pp. 280-286
    • Greim, H.1    Czygan, P.2    Schaffner, F.3    Popper, H.4
  • 47
    • 0023821864 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. 255 1988 357 360
    • (1988) Biochem. J. , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 49
    • 0027433653 scopus 로고
    • Physiological effectors modify voltage sensing by the cyclosporin A- sensitive permeability transition pore of mitochondria
    • V. Petronilli, C. Cola, S. Massari, R. Colonna, and P. Bernardi Physiological effectors modify voltage sensing by the cyclosporin A-sensitive permeability transition pore of mitochondria J. Biol. Chem. 268 1993 21939 21945 (Pubitemid 23320699)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.29 , pp. 21939-21945
    • Petronilli, V.1    Cola, C.2    Massari, S.3    Colonna, R.4    Bernardi, P.5
  • 50
    • 0034535252 scopus 로고    scopus 로고
    • Quantitative biochemical and ultrastructural comparison of mitochondrial permeability transition in isolated brain and liver mitochondria: Evidence for reduced sensitivity of brain mitochondria
    • DOI 10.1006/exnr.2000.7438
    • S.B. Berman, S.C. Watkins, and T.G. Hastings Quantitative biochemical and ultrastructural comparison of mitochondrial permeability transition in isolated brain and liver mitochondria: evidence for reduced sensitivity of brain mitochondria Exp. Neurol. 164 2000 415 425 (Pubitemid 32008986)
    • (2000) Experimental Neurology , vol.164 , Issue.2 , pp. 415-425
    • Berman, S.B.1    Watkins, S.C.2    Hastings, T.G.3
  • 53
    • 0033470181 scopus 로고    scopus 로고
    • Bile acids: The good, the bad, and the ugly
    • A.F. Hofmann Bile acids: the good, the bad, and the ugly News Physiol. Sci. 14 1999 24 29
    • (1999) News Physiol. Sci. , vol.14 , pp. 24-29
    • Hofmann, A.F.1
  • 55
    • 0018750668 scopus 로고
    • Partitioning of bile acids into subcellular organelles and the in vivo distribution of bile acids in rat liver
    • R.C. Strange, B.T. Chapman, J.D. Johnston, I.A. Nimmo, and I.W. Percy-Robb Partitioning of bile acids into subcellular organelles and the in vivo distribution of bile acids in rat liver Biochim. Biophys. Acta 573 1979 535 545 (Pubitemid 9208087)
    • (1979) Biochimica et Biophysica Acta , vol.573 , Issue.3 , pp. 535-545
    • Strange, R.C.1    Chapman, B.T.2    Johnston, J.D.3
  • 56
    • 0029099276 scopus 로고
    • Bile acid/phosphatidylcholine interactions in mixed monomolecular layers: Differences in condensation effects but not interfacial orientation between hydrophobic and hydrophilic bile acid species
    • D.A. Fahey, M.C. Carey, and J.M. Donovan Bile acid/phosphatidylcholine interactions in mixed monomolecular layers: differences in condensation effects but not interfacial orientation between hydrophobic and hydrophilic bile acid species Biochemistry 34 1995 10886 10897
    • (1995) Biochemistry , vol.34 , pp. 10886-10897
    • Fahey, D.A.1    Carey, M.C.2    Donovan, J.M.3
  • 60
    • 0004235430 scopus 로고    scopus 로고
    • 2nd ed. John Wiley & Sons, Inc. Hoboken, New Jersey
    • I.E. Scheffler Mitochondria 2nd ed. 2008 John Wiley & Sons, Inc. Hoboken, New Jersey
    • (2008) Mitochondria
    • Scheffler, I.E.1
  • 61
    • 0022628376 scopus 로고
    • Molecular architecture of the inner membrane of mitochondria from rat liver: A combined biochemical and stereological study
    • DOI 10.1083/jcb.102.1.97
    • K. Schwerzmann, L.M. Cruz-Orive, R. Eggman, A. Sanger, and E.R. Weibel Molecular architecture of the inner membrane of mitochondria from rat liver: a combined biochemical and stereological study J. Cell Biol. 102 1986 97 103 (Pubitemid 16155557)
    • (1986) Journal of Cell Biology , vol.102 , Issue.1 , pp. 97-103
    • Schwerzmann, K.1    Cruz-Orive, L.M.2    Eggman, R.3
  • 62
    • 0028274635 scopus 로고
    • Effect of mitochondrial protein concentration on the efficiency of outer membrane removal by the cholesterol-selective detergent digitonin
    • DOI 10.1016/0005-2736(94)90088-4
    • C.S. Boyer, E.P. Neve, G.A. Moore, and P. Moldeus Effect of mitochondrial protein concentration on the efficiency of outer membrane removal by the cholesterol-selective detergent digitonin Biochim. Biophys. Acta 1190 1994 304 308 (Pubitemid 24098492)
    • (1994) Biochimica et Biophysica Acta - Biomembranes , vol.1190 , Issue.2 , pp. 304-308
    • Boyer, C.S.1    Neve, E.P.A.2    Moore, G.A.3    Moldeus, P.4
  • 63
    • 0014310452 scopus 로고
    • Enzymatic properties of the inner and outer membranes of rat liver mitochondria
    • C. Schnaitman, and J.W. Greenawalt Enzymatic properties of the inner and outer membranes of rat liver mitochondria J. Cell Biol. 38 1968 158 175
    • (1968) J. Cell Biol. , vol.38 , pp. 158-175
    • Schnaitman, C.1    Greenawalt, J.W.2
  • 65
    • 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, and 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
  • 66
    • 0036498771 scopus 로고    scopus 로고
    • Isolation of hepatic mitochondrial contact sites: Previously unrecognized inner membrane components
    • DOI 10.1006/abio.2001.5531
    • C. Hoppel, J. Kerner, P. Turkaly, P. Minkler, and B. Tandler Isolation of hepatic mitochondrial contact sites: previously unrecognized inner membrane components Anal. Biochem. 302 2002 60 69 (Pubitemid 34174609)
    • (2002) Analytical Biochemistry , vol.302 , Issue.1 , pp. 60-69
    • Hoppel, C.1    Kerner, J.2    Turkaly, P.3    Minkler, P.4    Tandler, B.5
  • 67
    • 29344439984 scopus 로고    scopus 로고
    • Mitochondrial contact sites: Their role in energy metabolism and apoptosis
    • DOI 10.1016/j.bbadis.2005.09.007, PII S0925443905001444, Mitochondria in Diseases and Therapeutics
    • D.G. Brdiczka, D.B. Zorov, and S.S. Sheu Mitochondrial contact sites: their role in energy metabolism and apoptosis Biochim. Biophys. Acta 1762 2006 148 163 (Pubitemid 43006022)
    • (2006) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1762 , Issue.2 , pp. 148-163
    • Brdiczka, D.G.1    Zorov, D.B.2    Sheu, S.-S.3
  • 68
    • 0037009088 scopus 로고    scopus 로고
    • Contact sites between the outer and inner membrane of mitochondria - Role in protein transport
    • DOI 10.1016/S0167-4889(02)00263-X, PII S016748890200263X
    • A.S. Reichert, and W. Neupert Contact sites between the outer and inner membrane of mitochondria-role in protein transport Biochim. Biophys. Acta 1592 2002 41 49 (Pubitemid 35015164)
    • (2002) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1592 , Issue.1 , pp. 41-49
    • Reichert, A.S.1    Neupert, W.2
  • 69
    • 0031708617 scopus 로고    scopus 로고
    • Cholestasis confers resistance to the rat liver mitochondrial permeability transition
    • M.J. Lieser, J. Park, S. Natori, B.A. Jones, S.F. Bronk, and G.J. Gores Cholestasis confers resistance to the rat liver mitochondrial permeability transition Gastroenterology 115 1998 693 701 (Pubitemid 28397305)
    • (1998) Gastroenterology , vol.115 , Issue.3 , pp. 693-701
    • Liesee, M.J.1    Park, J.2    Natori, S.3    Jones, B.A.4    Bronk, S.F.5    Gores, G.J.6
  • 71
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • DOI 10.1073/pnas.031461598
    • H. Li, Z. Yao, B. Degenhardt, G. Teper, and V. Papadopoulos Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide Proc. Natl. Acad. Sci. U.S.A. 98 2001 1267 1272 (Pubitemid 32121221)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.3 , pp. 1267-1272
    • Li, H.1    Yao, Z.-X.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 73
    • 0242497235 scopus 로고    scopus 로고
    • Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
    • DOI 10.1038/nature02056
    • E. Pebay-Peyroula, C. Dahout-Gonzalez, R. Kahn, V. Trezeguet, G.J. Lauquin, and G. Brandolin Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside Nature 426 2003 39 44 (Pubitemid 37432535)
    • (2003) Nature , vol.426 , Issue.6962 , pp. 39-44
    • Pebay-Peyroula, E.1    Dahout-Gonzalez, C.2    Kahn, R.3    Trezeguet, V.4    Lauquin, G.J.-M.5    Brandolin, G.6
  • 74
    • 77956092161 scopus 로고    scopus 로고
    • Adsorption of bile salts and pancreatic colipase and lipase onto digalactosyldiacylglycerol and dipalmitoylphosphatidylcholine monolayers
    • B.S. Chu, A.P. Gunning, G.T. Rich, M.J. Ridout, R.M. Faulks, M.S. Wickham, V.J. Morris, and P.J. Wilde Adsorption of bile salts and pancreatic colipase and lipase onto digalactosyldiacylglycerol and dipalmitoylphosphatidylcholine monolayers Langmuir 26 2010 9782 9793
    • (2010) Langmuir , vol.26 , pp. 9782-9793
    • Chu, B.S.1    Gunning, A.P.2    Rich, G.T.3    Ridout, M.J.4    Faulks, R.M.5    Wickham, M.S.6    Morris, V.J.7    Wilde, P.J.8
  • 76
    • 0028135420 scopus 로고
    • Increases of intracellular magnesium promote glycodeoxycholate-induced apoptosis in rat hepatocytes
    • T. Patel, S.F. Bronk, and G.J. Gores Increases of intracellular magnesium promote glycodeoxycholate-induced apoptosis in rat hepatocytes J. Clin. Invest. 94 1994 2183 2192 (Pubitemid 24379587)
    • (1994) Journal of Clinical Investigation , vol.94 , Issue.6 , pp. 2183-2192
    • Patel, T.1    Bronk, S.F.2    Gores, G.J.3
  • 77
    • 2442644019 scopus 로고    scopus 로고
    • Role of mitochondrial dysfunction in combined bile acid-induced cytotoxicity: The switch between apoptosis and necrosis
    • DOI 10.1093/toxsci/kfh078
    • A.P. Rolo, C.M. Palmeira, J.M. Holy, and K.B. Wallace Role of mitochondrial dysfunction in combined bile acid-induced cytotoxicity: the switch between apoptosis and necrosis Toxicol. Sci. 79 2004 196 204 (Pubitemid 38660263)
    • (2004) Toxicological Sciences , vol.79 , Issue.1 , pp. 196-204
    • Rolo, A.P.1    Palmeira, C.M.2    Holy, J.M.3    Wallace, K.B.4


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