메뉴 건너뛰기




Volumn 278, Issue 7, 2011, Pages 1112-1125

Modulation of F0F1-ATP synthase activity by cyclophilin D regulates matrix adenine nucleotide levels

Author keywords

adenine nucleotide carrier; control strength; metabolic control analysis; permeability transition pore; phosphate carrier

Indexed keywords

ADENINE NUCLEOTIDE; ADENINE NUCLEOTIDE TRANSLOCASE; ADENOSINE TRIPHOSPHATE; ARSENIC ACID; CYCLOPHILIN D; CYCLOSPORIN A; HYDROGEN; MATRIX PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; ADENOSINE DIPHOSPHATE; ARSENIC ACID DERIVATIVE; CYCLOPHILIN; CYCLOSPORIN; ENZYME INHIBITOR; HERBICIDE; MAGNESIUM; PROTON; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 79952837890     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08026.x     Document Type: Article
Times cited : (42)

References (78)
  • 3
  • 5
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • DOI 10.1038/nature03317
    • Nakagawa T, Shimizu S, Watanabe T, Yamaguchi O, Otsu K, Yamagata H, Inohara H, Kubo T, &, Tsujimoto Y, (2005) Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 434, 652-658. (Pubitemid 40488558)
    • (2005) Nature , vol.434 , Issue.7033 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 7
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of cyclophilin D
    • DOI 10.1074/jbc.C500089200
    • Basso E, Fante L, Fowlkes J, Petronilli V, Forte MA, &, Bernardi P, (2005) Properties of the permeability transition pore in mitochondria devoid of cyclophilin D. J Biol Chem 280, 18558-18561. (Pubitemid 41379552)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 8
    • 55549126837 scopus 로고    scopus 로고
    • Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation
    • Basso E, Petronilli V, Forte MA, &, Bernardi P, (2008) Phosphate is essential for inhibition of the mitochondrial permeability transition pore by cyclosporin A and by cyclophilin D ablation. J Biol Chem 283, 26307-26311.
    • (2008) J Biol Chem , vol.283 , pp. 26307-26311
    • Basso, E.1    Petronilli, V.2    Forte, M.A.3    Bernardi, P.4
  • 9
    • 0037163117 scopus 로고    scopus 로고
    • Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization
    • DOI 10.1074/jbc.M112035200
    • Lin DT, &, Lechleiter JD, (2002) Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J Biol Chem 277, 31134-31141. (Pubitemid 34970819)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 31134-31141
    • Lin, D.-T.1    Lechleiter, J.D.2
  • 10
    • 0030766182 scopus 로고    scopus 로고
    • Two modes of activation of the permeability transition pore: The role of mitochondrial cyclophilin
    • Scorrano L, Nicolli A, Basso E, Petronilli V, &, Bernardi P, (1997) Two modes of activation of the permeability transition pore: the role of mitochondrial cyclophilin. Mol Cell Biochem 174, 181-184.
    • (1997) Mol Cell Biochem , vol.174 , pp. 181-184
    • Scorrano, L.1    Nicolli, A.2    Basso, E.3    Petronilli, V.4    Bernardi, P.5
  • 11
    • 49449113953 scopus 로고    scopus 로고
    • Enhancement of anxiety, facilitation of avoidance behavior, and occurrence of adult-onset obesity in mice lacking mitochondrial cyclophilin D
    • Luvisetto S, Basso E, Petronilli V, Bernardi P, &, Forte M, (2008) Enhancement of anxiety, facilitation of avoidance behavior, and occurrence of adult-onset obesity in mice lacking mitochondrial cyclophilin D. Neuroscience 155, 585-596.
    • (2008) Neuroscience , vol.155 , pp. 585-596
    • Luvisetto, S.1    Basso, E.2    Petronilli, V.3    Bernardi, P.4    Forte, M.5
  • 12
    • 38949218420 scopus 로고    scopus 로고
    • Critical role for the mitochondrial permeability transition pore and cyclophilin D in platelet activation and thrombosis
    • DOI 10.1182/blood-2007-05-092684
    • Jobe SM, Wilson KM, Leo L, Raimondi A, Molkentin JD, Lentz SR, &, Di PJ, (2008) Critical role for the mitochondrial permeability transition pore and cyclophilin D in platelet activation and thrombosis. Blood 111, 1257-1265. (Pubitemid 351213408)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1257-1265
    • Jobe, S.M.1    Wilson, K.M.2    Leo, L.3    Raimondi, A.4    Molkentin, J.D.5    Lentz, S.R.6    Di Paola, J.7
  • 13
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • et al.
    • Du H, Guo L, Fang F, Chen D, Sosunov AA, McKhann GM, Yan Y, Wang C, Zhang H, Molkentin JD, et al. (2008) Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat Med 14, 10971105.
    • (2008) Nat Med , vol.14 , pp. 10971105
    • Du, H.1    Guo, L.2    Fang, F.3    Chen, D.4    Sosunov, A.A.5    McKhann, G.M.6    Yan, Y.7    Wang, C.8    Zhang, H.9    Molkentin, J.D.10
  • 20
    • 65349105507 scopus 로고    scopus 로고
    • A novel kinetic assay of mitochondrial ATP-ADP exchange rate mediated by the ANT
    • Chinopoulos C, Vajda S, Csanady L, Mandi M, Mathe K, &, Adam-Vizi V, (2009) A novel kinetic assay of mitochondrial ATP-ADP exchange rate mediated by the ANT. Biophys J 96, 2490-2504.
    • (2009) Biophys J , vol.96 , pp. 2490-2504
    • Chinopoulos, C.1    Vajda, S.2    Csanady, L.3    Mandi, M.4    Mathe, K.5    Adam-Vizi, V.6
  • 21
    • 71849096530 scopus 로고    scopus 로고
    • Mitochondria as ATP consumers in cellular pathology
    • Chinopoulos C, &, Adam-Vizi V, (2010) Mitochondria as ATP consumers in cellular pathology. Biochim Biophys Acta 1802, 221-227.
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 221-227
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 22
    • 70449720998 scopus 로고    scopus 로고
    • Modeling of ATP-ADP steady-state exchange rate mediated by the adenine nucleotide translocase in isolated mitochondria
    • Metelkin E, Demin O, Kovacs Z, &, Chinopoulos C, (2009) Modeling of ATP-ADP steady-state exchange rate mediated by the adenine nucleotide translocase in isolated mitochondria. FEBS J 276, 6942-6955.
    • (2009) FEBS J , vol.276 , pp. 6942-6955
    • Metelkin, E.1    Demin, O.2    Kovacs, Z.3    Chinopoulos, C.4
  • 23
    • 77954429761 scopus 로고    scopus 로고
    • Forward operation of adenine nucleotide translocase during F0F1-ATPase reversal: Critical role of matrix substrate-level phosphorylation
    • et al.
    • Chinopoulos C, Gerencser AA, Mandi M, Mathe K, Torocsik B, Doczi J, Turiak L, Kiss G, Konrad C, Vajda S, et al. (2010) Forward operation of adenine nucleotide translocase during F0F1-ATPase reversal: critical role of matrix substrate-level phosphorylation. FASEB J 24, 2405-2416.
    • (2010) FASEB J , vol.24 , pp. 2405-2416
    • Chinopoulos, C.1    Gerencser, A.A.2    Mandi, M.3    Mathe, K.4    Torocsik, B.5    Doczi, J.6    Turiak, L.7    Kiss, G.8    Konrad, C.9    Vajda, S.10
  • 24
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • Klingenberg M, (2008) The ADP and ATP transport in mitochondria and its carrier. Biochim Biophys Acta 1778, 1978-2021.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 25
    • 0019155420 scopus 로고
    • The ADP-ATP translocation in mitochondria, a membrane potential controlled transport
    • DOI 10.1007/BF01875961
    • Klingenberg M, (1980) The ADP-ATP translocation in mitochondria, a membrane potential controlled transport. J Membr Biol 56, 97-105. (Pubitemid 11207250)
    • (1980) Journal of Membrane Biology , vol.56 , Issue.2 , pp. 97-105
    • Klingenberg, M.1
  • 26
    • 0019316929 scopus 로고
    • Modulation of the reconstituted adenine nucleotide exchange by membrane potential
    • Kramer R, &, Klingenberg M, (1980) Modulation of the reconstituted adenine nucleotide exchange by membrane potential. Biochemistry 19, 556-560.
    • (1980) Biochemistry , vol.19 , pp. 556-560
    • Kramer, R.1    Klingenberg, M.2
  • 27
    • 33646172301 scopus 로고    scopus 로고
    • Mathematical modeling of mitochondrial adenine nucleotide translocase
    • Metelkin E, Goryanin I, &, Demin O, (2006) Mathematical modeling of mitochondrial adenine nucleotide translocase. Biophys J 90, 423-432.
    • (2006) Biophys J , vol.90 , pp. 423-432
    • Metelkin, E.1    Goryanin, I.2    Demin, O.3
  • 28
    • 0017641188 scopus 로고
    • Comparative studies on glutamate metabolism in synaptic and non-synaptic rat brain mitochondria
    • Dennis SC, Lai JC, &, Clark JB, (1977) Comparative studies on glutamate metabolism in synpatic and non-synaptic rat brain mitochondria. Biochem J 164, 727-736. (Pubitemid 8132930)
    • (1977) Biochemical Journal , vol.164 , Issue.3 , pp. 727-736
    • Dennis, S.C.1    Lai, J.C.K.2    Clark, J.B.3
  • 29
    • 0014572763 scopus 로고
    • The inhibition of pyruvate and Ls(+)isocitrate oxidation by succinate oxidation in rat liver mitochondria
    • Konig T, Nicholls DG, &, Garland PB, (1969) The inhibition of pyruvate and Ls(+)isocitrate oxidation by succinate oxidation in rat liver mitochondria. Biochem J 114, 589-596.
    • (1969) Biochem J , vol.114 , pp. 589-596
    • Konig, T.1    Nicholls, D.G.2    Garland, P.B.3
  • 31
    • 0141479590 scopus 로고    scopus 로고
    • 1 complex of mitochondria
    • Demin OV, Westerhoff HV, &, Kholodenko BN, (1998) Mathematical modelling of superoxide generation with the bc1 complex of mitochondria. Biochemistry (Mosc) 63, 634-649. (Pubitemid 128588072)
    • (1998) Biochemistry (Moscow) , vol.63 , Issue.6 , pp. 634-649
    • Demin, O.V.1    Westerhoff, H.V.2    Kholodenko, B.N.3
  • 32
    • 0035497854 scopus 로고    scopus 로고
    • Kinetic modeling of energy metabolism and superoxide generation in hepatocyte mitochondria
    • Demin OV, Gorianin II, Kholodenko BN, &, Westerhoff HV, (2001) [Kinetic modeling of energy metabolism and generation of active forms of oxygen in hepatocyte mitochondria]. Mol Biol (Mosk) 35, 1095-1104. (Pubitemid 33776311)
    • (2001) Molekulyarnaya Biologiya , vol.35 , Issue.6 , pp. 1095-1104
    • Demin, O.V.1    Kholodenko, B.N.2    Westerhoff, H.V.3
  • 34
    • 0018745859 scopus 로고
    • Quantitative dependence of mitochondrial oxidative phosphorylation on oxygen concentration: A mathematical model
    • DOI 10.1016/0003-9861(79)90376-X
    • Wilson DF, Owen CS, &, Erecinska M, (1979) Quantitative dependence of mitochondrial oxidative phosphorylation on oxygen concentration: a mathematical model. Arch Biochem Biophys 195, 494-504. (Pubitemid 9235082)
    • (1979) Archives of Biochemistry and Biophysics , vol.195 , Issue.2 , pp. 494-504
    • Wilson, D.F.1    Owen, C.S.2    Erecinska, M.3
  • 35
    • 0030848050 scopus 로고    scopus 로고
    • Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase
    • Arnold S, &, Kadenbach B, (1997) Cell respiration is controlled by ATP, an allosteric inhibitor of cytochrome-c oxidase. Eur J Biochem 249, 350-354. (Pubitemid 27432632)
    • (1997) European Journal of Biochemistry , vol.249 , Issue.1 , pp. 350-354
    • Arnold, S.1    Kadenbach, B.2
  • 36
    • 0025952644 scopus 로고
    • Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates
    • Moreno-Sanchez R, Devars S, Lopez-Gomez F, Uribe A, &, Corona N, (1991) Distribution of control of oxidative phosphorylation in mitochondria oxidizing NAD-linked substrates. Biochim Biophys Acta 1060, 284-292.
    • (1991) Biochim Biophys Acta , vol.1060 , pp. 284-292
    • Moreno-Sanchez, R.1    Devars, S.2    Lopez-Gomez, F.3    Uribe, A.4    Corona, N.5
  • 38
    • 0027157645 scopus 로고
    • Phosphate affects the distribution of flux control among the enzymes of oxidative phosphorylation in rat skeletal muscle mitochondria
    • Wisniewski E, Kunz WS, &, Gellerich FN, (1993) Phosphate affects the distribution of flux control among the enzymes of oxidative phosphorylation in rat skeletal muscle mitochondria. J Biol Chem 268, 9343-9346. (Pubitemid 23145981)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.13 , pp. 9343-9346
    • Wisniewski, E.1    Kunz, W.S.2    Gellerich, F.N.3
  • 41
    • 0021233473 scopus 로고
    • Developmental changes in the adenine nucleotide translocase in the guinea pig
    • Hale DE, &, Williamson JR, (1984) Developmental changes in the adenine nucleotide translocase in the guinea pig. J Biol Chem 259, 8737-8742. (Pubitemid 14097935)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.14 , pp. 8737-8742
    • Hale, D.E.1    Williamson, J.R.2
  • 43
    • 0023681888 scopus 로고
    • Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain
    • Brand MD, Hafner RP, &, Brown GC, (1988) Control of respiration in non-phosphorylating mitochondria is shared between the proton leak and the respiratory chain. Biochem J 255, 535-539.
    • (1988) Biochem J , vol.255 , pp. 535-539
    • Brand, M.D.1    Hafner, R.P.2    Brown, G.C.3
  • 44
    • 0034629141 scopus 로고    scopus 로고
    • Direct evidence for the control of mitochondrial respiration by mitochondrial creatine kinase in oxidative muscle cells in situ
    • DOI 10.1074/jbc.275.10.6937
    • Kay L, Nicolay K, Wieringa B, Saks V, &, Wallimann T, (2000) Direct evidence for the control of mitochondrial respiration by mitochondrial creatine kinase in oxidative muscle cells in situ. J Biol Chem 275, 6937-6944. (Pubitemid 30146236)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.10 , pp. 6937-6944
    • Kay, L.1    Nicolay, K.2    Wieringa, B.3    Saks, V.4    Wallimann, T.5
  • 45
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • Groen AK, Wanders RJ, Westerhoff HV, van der MR, &, Tager JM, (1982) Quantification of the contribution of various steps to the control of mitochondrial respiration. J Biol Chem, 257, 2754-2757.
    • (1982) J Biol Chem , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.2    Westerhoff, H.V.3    Van Der, M.R.4    Tager, J.M.5
  • 46
    • 0021186307 scopus 로고
    • Control of mitochondrial oxidative phosphorylation
    • Kholodenko BN, (1984) Control of mitochondrial oxidative phosphorylation. J Theor Biol 107, 179-188. (Pubitemid 14108673)
    • (1984) Journal of Theoretical Biology , vol.107 , Issue.2 , pp. 179-188
    • Kholodenko, B.N.1
  • 47
    • 0028786786 scopus 로고
    • Developmental changes of the adenine nucleotide translocation in rat brain
    • Schonfeld P, &, Bohnensack R, (1995) Developmental changes of the adenine nucleotide translocation in rat brain. Biochim Biophys Acta 1232, 75-80.
    • (1995) Biochim Biophys Acta , vol.1232 , pp. 75-80
    • Schonfeld, P.1    Bohnensack, R.2
  • 48
    • 0029039749 scopus 로고
    • Distribution of flux control among the enzymes of mitochondrial oxidative phosphorylation in calcium-activated saponin-skinned rat musculus soleus fibers
    • Wisniewski E, Gellerich FN, &, Kunz WS, (1995) Distribution of flux control among the enzymes of mitochondrial oxidative phosphorylation in calcium-activated saponin-skinned rat musculus soleus fibers. Eur J Biochem 230, 549-554.
    • (1995) Eur J Biochem , vol.230 , pp. 549-554
    • Wisniewski, E.1    Gellerich, F.N.2    Kunz, W.S.3
  • 49
    • 0025238864 scopus 로고
    • Analysis of the control of respiration rate, phosphorylation rate, proton leak rate and protonmotive force in isolated mitochondria using the 'top-down' approach of metabolic control theory
    • Hafner RP, Brown GC, &, Brand MD, (1990) Analysis of the control of respiration rate, phosphorylation rate, proton leak rate and protonmotive force in isolated mitochondria using the 'top-down' approach of metabolic control theory. Eur J Biochem 188, 313-319. (Pubitemid 20106243)
    • (1990) European Journal of Biochemistry , vol.188 , Issue.2 , pp. 313-319
    • Hafner, R.P.1    Brown, G.C.2    Brand, M.D.3
  • 52
    • 0018527496 scopus 로고
    • Molecular democracy: Who shares the controls?
    • Kacser H, &, Burns JA, (1979) Molecular democracy: who shares the controls? Biochem Soc Trans 7, 1149-1160.
    • (1979) Biochem Soc Trans , vol.7 , pp. 1149-1160
    • Kacser, H.1    Burns, J.A.2
  • 53
    • 0015989446 scopus 로고
    • A linear steady-state treatment of enzymatic chains. General properties, control and effector strength
    • Heinrich R, &, Rapoport TA, (1974) A linear steady-state treatment of enzymatic chains. General properties, control and effector strength. Eur J Biochem 42, 89-95.
    • (1974) Eur J Biochem , vol.42 , pp. 89-95
    • Heinrich, R.1    Rapoport, T.A.2
  • 54
    • 0000228422 scopus 로고
    • A naturally occurring inhibitor of mitochondrial adenosine triphosphatase
    • Pullman ME, &, Monroy GC, (1963) A naturally occurring inhibitor of mitochondrial adenosine triphosphatase. J Biol Chem 238, 3762-3769.
    • (1963) J Biol Chem , vol.238 , pp. 3762-3769
    • Pullman, M.E.1    Monroy, G.C.2
  • 56
    • 0029661427 scopus 로고    scopus 로고
    • 1 function in situ in uncoupler-challenged ischemic rabbit, rat, and pigeon hearts
    • DOI 10.1074/jbc.271.39.23638
    • Rouslin W, &, Broge CW, (1996) IF1 function in situ in uncoupler-challenged ischemic rabbit, rat, and pigeon hearts. J Biol Chem 271, 23638-23641. (Pubitemid 26327324)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.39 , pp. 23638-23641
    • Rouslin, W.1    Broge, C.W.2
  • 57
    • 0027289039 scopus 로고
    • 1, to the mitochondrial ATPase of slow and fast heart-rate hearts
    • DOI 10.1006/abbi.1993.1307
    • Rouslin W, &, Broge CW, (1993) Factors affecting the species-homologous and species-heterologous binding of mitochondrial ATPase inhibitor, IF1, to the mitochondrial ATPase of slow and fast heart-rate hearts. Arch Biochem Biophys 303, 443-450. (Pubitemid 23199845)
    • (1993) Archives of Biochemistry and Biophysics , vol.303 , Issue.2 , pp. 443-450
    • Rouslin, W.1    Broge, C.W.2
  • 58
    • 0017332369 scopus 로고
    • Relation between the gradient of the ATP/ADP ratio and the membrane potential across the mitochondrial membrane
    • Klingenberg M, &, Rottenberg H, (1977) Relation between the gradient of the ATP/ADP ratio and the membrane potential across the mitochondrial membrane. Eur J Biochem 73, 125-130. (Pubitemid 8044270)
    • (1977) European Journal of Biochemistry , vol.73 , Issue.1 , pp. 125-130
    • Klingenberg, M.1    Rottenberg, H.2
  • 59
    • 0014028023 scopus 로고
    • Hydrogen ion concentration changes in mitochondrial membranes
    • Chance B, &, Mela L, (1966) Hydrogen ion concentration changes in mitochondrial membranes. J Biol Chem 241, 4588-4599.
    • (1966) J Biol Chem , vol.241 , pp. 4588-4599
    • Chance, B.1    Mela, L.2
  • 60
    • 0027508994 scopus 로고
    • 2+
    • Petronilli V, Cola C, &, Bernardi P, (1993) 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, 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
  • 61
    • 65349166528 scopus 로고    scopus 로고
    • A re-evaluation of the role of matrix acidification in uncoupler-induced Ca2+ release from mitochondria
    • Vajda S, Mandi M, Konrad C, Kiss G, Ambrus A, Adam-Vizi V, &, Chinopoulos C, (2009) A re-evaluation of the role of matrix acidification in uncoupler-induced Ca2+ release from mitochondria. FEBS J 276, 2713-2724.
    • (2009) FEBS J , vol.276 , pp. 2713-2724
    • Vajda, S.1    Mandi, M.2    Konrad, C.3    Kiss, G.4    Ambrus, A.5    Adam-Vizi, V.6    Chinopoulos, C.7
  • 62
    • 77956324397 scopus 로고    scopus 로고
    • Mitochondrial Ca(2+) sequestration and precipitation revisited
    • Chinopoulos C, &, Adam-Vizi V, (2010) Mitochondrial Ca(2+) sequestration and precipitation revisited. FEBS J 277, 3637-3651.
    • (2010) FEBS J , vol.277 , pp. 3637-3651
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 63
    • 33751118765 scopus 로고    scopus 로고
    • A hinge of the endogeneous ATP synthase inhibitor protein: The link between inhibitory and anchoring domains
    • DOI 10.1002/prot.21189
    • Dominguez-Ramirez L, Gomez-Puyou A, &, De Gomez-Puyou MT, (2006) A hinge of the endogeneous ATP synthase inhibitor protein: the link between inhibitory and anchoring domains. Proteins 65, 999-1007. (Pubitemid 44772896)
    • (2006) Proteins: Structure, Function and Genetics , vol.65 , Issue.4 , pp. 999-1007
    • Dominguez-Ramirez, L.1    Gomez-Puyou, A.2    De Gomez-Puyou, M.T.3
  • 64
    • 34848846351 scopus 로고    scopus 로고
    • Mammalian ATPsynthase monomer versus dimer profiled by blue native PAGE and activity stain
    • DOI 10.1002/elps.200700066
    • Bisetto E, Di PF, Simula MP, Mavelli I, &, Lippe G, (2007) Mammalian ATPsynthase monomer versus dimer profiled by blue native PAGE and activity stain. Electrophoresis 28, 3178-3185. (Pubitemid 47506446)
    • (2007) Electrophoresis , vol.28 , Issue.18 , pp. 3178-3185
    • Bisetto, E.1    Di Pancrazio, F.2    Simula, M.P.3    Mavelli, I.4    Lippe, G.5
  • 65
    • 0014193456 scopus 로고
    • Uncoupling of respiratory-chain phosphorylation by arsenate
    • ter Welle HF, &, Slater EC, (1967) Uncoupling of respiratory-chain phosphorylation by arsenate. Biochim Biophys Acta 143, 1-17.
    • (1967) Biochim Biophys Acta , vol.143 , pp. 1-17
    • Ter Welle, H.F.1    Slater, E.C.2
  • 66
    • 0000998388 scopus 로고
    • The effect of arsenate on aerobic phosphorylation
    • Crane RK, &, Lipmann F, (1953) The effect of arsenate on aerobic phosphorylation. J Biol Chem 201, 235-243.
    • (1953) J Biol Chem , vol.201 , pp. 235-243
    • Crane, R.K.1    Lipmann, F.2
  • 67
    • 70449540012 scopus 로고
    • Stimulation of adenosine triphosphatase activity of mitochondria and submitochondrial particles by arsenate
    • Wadkins CL, (1960) Stimulation of adenosine triphosphatase activity of mitochondria and submitochondrial particles by arsenate. J Biol Chem 235, 33003303.
    • (1960) J Biol Chem , vol.235 , pp. 33003303
    • Wadkins, C.L.1
  • 68
    • 0014690695 scopus 로고
    • Kinetics of phosphorylation of intramitochondrial and extramitochondrial adenine nucleotides as related to nucleotide translocation
    • Duee ED, &, Vignais PV, (1969) Kinetics of phosphorylation of intramitochondrial and extramitochondrial adenine nucleotides as related to nucleotide translocation. J Biol Chem 244, 3932-3940.
    • (1969) J Biol Chem , vol.244 , pp. 3932-3940
    • Duee, E.D.1    Vignais, P.V.2
  • 69
    • 0027241092 scopus 로고
    • Control of the effective P/O ratio of oxidative phosphorylation in liver mitochondria and hepatocytes
    • Brand MD, Harper ME, &, Taylor HC, (1993) Control of the effective P/O ratio of oxidative phosphorylation in liver mitochondria and hepatocytes. Biochem J 291 (Pt 3), 739-748. (Pubitemid 23148447)
    • (1993) Biochemical Journal , vol.291 , Issue.3 , pp. 739-748
    • Brand, M.D.1    Harper, M.-E.2    Taylor, H.C.3
  • 70
    • 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 AP, (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 (Pt 2), 287-290. (Pubitemid 28564382)
    • (1998) Biochemical Journal , vol.336 , Issue.2 , pp. 287-290
    • Woodfield, K.1    Ruck, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 71
    • 0026801183 scopus 로고
    • Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization
    • Bernardi P, (1992) Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization. J Biol Chem 267, 8834-8839.
    • (1992) J Biol Chem , vol.267 , pp. 8834-8839
    • Bernardi, P.1
  • 72
    • 0027433653 scopus 로고
    • Physiological effectors modify voltage sensing by the cyclosporin A- sensitive permeability transition pore of mitochondria
    • Petronilli V, Cola C, Massari S, Colonna R, &, Bernardi P, (1993) Physiological effectors modify voltage sensing by the cyclosporin A-sensitive permeability transition pore of mitochondria. J Biol Chem 268, 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
  • 73
    • 0030995428 scopus 로고    scopus 로고
    • On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal
    • DOI 10.1074/jbc.272.19.12295
    • Scorrano L, Petronilli V, &, Bernardi P, (1997) On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal. J Biol Chem 272, 12295-12299. (Pubitemid 27203313)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.19 , pp. 12295-12299
    • Scorrano, L.1    Petronilli, V.2    Bernardi, P.3
  • 74
    • 0002156536 scopus 로고
    • The preparation of heart mitochondria from laboratory animals
    • Tyler DD, &, Gonze J, (1967) The preparation of heart mitochondria from laboratory animals. Methods Enzymol 10, 75-77.
    • (1967) Methods Enzymol , vol.10 , pp. 75-77
    • Tyler, D.D.1    Gonze, J.2
  • 75
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • DOI 10.1016/0003-2697(85)90442-7
    • Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, &, Klenk DC, (1985) Measurement of protein using bicinchoninic acid. Anal Biochem 150, 76-85. (Pubitemid 16258399)
    • (1985) Analytical Biochemistry , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 77
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • Akerman KE, &, Wikstrom MK, (1976) Safranine as a probe of the mitochondrial membrane potential. FEBS Lett 68, 191-197.
    • (1976) FEBS Lett , vol.68 , pp. 191-197
    • Akerman, K.E.1    Wikstrom, M.K.2
  • 78
    • 0027349772 scopus 로고
    • Continuous recording of intramitochondrial pH with fluorescent pH indicators: Novel probes and limitations of the method
    • Zolkiewska A, Czyz A, Duszynski J, &, Wojtczak L, (1993) Continuous recording of intramitochondrial pH with fluorescent pH indicators: novel probes and limitations of the method. Acta Biochim Pol 40, 241-250.
    • (1993) Acta Biochim Pol , vol.40 , pp. 241-250
    • Zolkiewska, A.1    Czyz, A.2    Duszynski, J.3    Wojtczak, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.