메뉴 건너뛰기




Volumn 387, Issue 3, 2005, Pages 677-683

Inhibitory effect of palmitate on the mitochondrial NADH:ubiquinone oxidoreductase (complex I) as related to the active-de-active enzyme transition

Author keywords

Energy transduction; Fatty acid; Mitochondria; NADH:ubiquinone oxidoreductase; Palmitate; Respiratory chain

Indexed keywords

BIOLOGICAL ORGANS; CATALYSIS; CONCENTRATION (PROCESS); ENZYME INHIBITION; FATTY ACIDS; LIVING SYSTEMS STUDIES; OXIDATION;

EID: 18844417373     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041703     Document Type: Article
Times cited : (56)

References (50)
  • 1
    • 0037184987 scopus 로고    scopus 로고
    • Definition of the nuclear encoded protein composition of bovine heart mitochondrial Complex I: Identification of two new subunits
    • Carroll, J., Shannon, R. J., Fearnley, I. M., Walker, J. E. and Hirst, J. (2002) Definition of the nuclear encoded protein composition of bovine heart mitochondrial Complex I: identification of two new subunits. J. Biol. Chem. 277, 50311-50317
    • (2002) J. Biol. Chem. , vol.277 , pp. 50311-50317
    • Carroll, J.1    Shannon, R.J.2    Fearnley, I.M.3    Walker, J.E.4    Hirst, J.5
  • 2
    • 0032852758 scopus 로고    scopus 로고
    • EPR studies of the possible binding sites of the cluster N2, semiquinones, and specific inhibitors of the NADH:quinone oxidoreductase (complex I)
    • Ohnishi, T., Magnitsky, S., Toulokhonova, L., Yano, T., Yagi, T., Burbaev, D. S. and Vinogradov, A. D. (1999) EPR studies of the possible binding sites of the cluster N2, semiquinones, and specific inhibitors of the NADH:quinone oxidoreductase (complex I). Biochem. Soc. Trans. 27, 586-591
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 586-591
    • Ohnishi, T.1    Magnitsky, S.2    Toulokhonova, L.3    Yano, T.4    Yagi, T.5    Burbaev, D.S.6    Vinogradov, A.D.7
  • 3
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli: Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I
    • Weidner, U., Geiger, S., Ptock, A., Friedrich, T., Leif, H. and Weiss, H. (1993) The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli: organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J. Mol. Biol. 233, 109-122
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geiger, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 4
    • 0027477868 scopus 로고
    • DNA sequencing of the remaining genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Xu, X., Matsuno-Yagi, A. and Yagi, T. (1993) DNA sequencing of the remaining genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 32, 968-981
    • (1993) Biochemistry , vol.32 , pp. 968-981
    • Xu, X.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 6
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins
    • Fearnley, I. M. and Walker, J. E. (1992) Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim. Biophys. Acta 1140, 105-134
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 7
    • 0345059204 scopus 로고    scopus 로고
    • The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: Similarities and dissimilarities of the quinone-junction sites
    • Grivennikova, V. G., Roth, R., Zakharova, N. V., Hägerhäll, C. and Vinogradov, A. D. (2003) The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites. Biochim. Biophys. Acta 1607, 79-90
    • (2003) Biochim. Biophys. Acta , vol.1607 , pp. 79-90
    • Grivennikova, V.G.1    Roth, R.2    Zakharova, N.V.3    Hägerhäll, C.4    Vinogradov, A.D.5
  • 8
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • Videira, A. and Duarte, M. (2002) From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta 1555, 187-191
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 187-191
    • Videira, A.1    Duarte, M.2
  • 9
    • 0032490088 scopus 로고    scopus 로고
    • Physiological, biochemical and molecular aspects of mitochondrial complex I in plants
    • Rasmusson, A. G., Heiser, V., Zabaleta, E., Brennicke, A. and Grohmann, L. (1998) Physiological, biochemical and molecular aspects of mitochondrial complex I in plants. Biochim. Biophys. Acta 1364, 101-111
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 101-111
    • Rasmusson, A.G.1    Heiser, V.2    Zabaleta, E.3    Brennicke, A.4    Grohmann, L.5
  • 10
    • 0036139815 scopus 로고    scopus 로고
    • The mitochondrial Complex I: Progress in understanding of catalytic properties
    • Vinogradov, A. D. and Grivennikova, V. G. (2001) The mitochondrial Complex I: progress in understanding of catalytic properties. IUBMB Life 52, 129-134
    • (2001) IUBMB Life , vol.52 , pp. 129-134
    • Vinogradov, A.D.1    Grivennikova, V.G.2
  • 11
    • 0037325411 scopus 로고    scopus 로고
    • The transition between active and de-activated forms of NADH:ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa
    • Grivennikova, V. G., Serebryanaya, D. V., Isakova, E. P., Belozerskaya, T. A. and Vinogradov, A. D. (2003) The transition between active and de-activated forms of NADH:ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa. Biochem. J. 369, 619-626
    • (2003) Biochem. J. , vol.369 , pp. 619-626
    • Grivennikova, V.G.1    Serebryanaya, D.V.2    Isakova, E.P.3    Belozerskaya, T.A.4    Vinogradov, A.D.5
  • 12
    • 0142106477 scopus 로고    scopus 로고
    • Active/de-active transition of respiratory Complex I in bacteria, fungi and animals
    • Maklashina, E., Kotlyar, A. B. and Cecchini, G. (2003) Active/de-active transition of respiratory Complex I in bacteria, fungi and animals. Biochim. Biophys. Acta 1606, 95-103
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 95-103
    • Maklashina, E.1    Kotlyar, A.B.2    Cecchini, G.3
  • 13
    • 0027121489 scopus 로고
    • 2+ ions on the slow active/inactive transition of the mitochondrial NADH:ubiquinone reductase
    • 2+ ions on the slow active/inactive transition of the mitochondrial NADH:ubiquinone reductase. Biochim. Biophys. Acta 1098, 144-150
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 144-150
    • Kotlyar, A.B.1    Sled, V.D.2    Vinogradov, A.D.3
  • 14
    • 0033042196 scopus 로고    scopus 로고
    • Active/de-active transition of the mitochondrial complex I as revealed by specific sulfhydryl group labeling
    • Gavrikova, E. V. and Vinogradov, A. D. (1999) Active/de-active transition of the mitochondrial complex I as revealed by specific sulfhydryl group labeling. FEBS Lett. 455, 36-40
    • (1999) FEBS Lett. , vol.455 , pp. 36-40
    • Gavrikova, E.V.1    Vinogradov, A.D.2
  • 15
    • 0001595528 scopus 로고
    • Hysteresis in the behavior of bovine heart mitochondrial Complex I: Kinetic and thermodynamic parameters of the slow reversible active/inactive transition
    • Maklashina, E. O., Sled, V. D. and Vinogradov, A. D. (1994) Hysteresis in the behavior of bovine heart mitochondrial Complex I: kinetic and thermodynamic parameters of the slow reversible active/inactive transition. Biochemistry (Moscow) 59, 707-714
    • (1994) Biochemistry (Moscow) , vol.59 , pp. 707-714
    • Maklashina, E.O.1    Sled, V.D.2    Vinogradov, A.D.3
  • 16
    • 0025072729 scopus 로고
    • Slow active/inactive transition of the NADH:ubiquinone reductase
    • Kotlyar, A. B. and Vinogradov, A. D. (1990) Slow active/inactive transition of the NADH:ubiquinone reductase. Biochim. Biophys. Acta 1019, 151-158
    • (1990) Biochim. Biophys. Acta , vol.1019 , pp. 151-158
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 17
    • 0035937792 scopus 로고    scopus 로고
    • Catalytic activity of NADH-ubiquinone oxidoreductase (Complex I) in intact mitochondria. Evidence for the slow active/inactive transition
    • Grivennikova, V. G., Kapustin, A. N. and Vinogradov, A. D. (2001) Catalytic activity of NADH-ubiquinone oxidoreductase (Complex I) in intact mitochondria. Evidence for the slow active/inactive transition. J. Biol. Chem. 276, 9038-9044
    • (2001) J. Biol. Chem. , vol.276 , pp. 9038-9044
    • Grivennikova, V.G.1    Kapustin, A.N.2    Vinogradov, A.D.3
  • 18
    • 0037015692 scopus 로고    scopus 로고
    • Effect of anoxia/reperfusion on the reversible active/deactive transition of NADH-ubiquinone oxidoreductase (Complex I) in rat heart
    • Maklashina, E., Sher, Y., Zong-Zhou, H., Gray, M. O., Karliner, J. S. and Cecchini, G. (2002) Effect of anoxia/reperfusion on the reversible active/deactive transition of NADH-ubiquinone oxidoreductase (Complex I) in rat heart. Biochim. Biophys. Acta 1556, 6-12
    • (2002) Biochim. Biophys. Acta , vol.1556 , pp. 6-12
    • Maklashina, E.1    Sher, Y.2    Zong-Zhou, H.3    Gray, M.O.4    Karliner, J.S.5    Cecchini, G.6
  • 19
    • 0030969014 scopus 로고    scopus 로고
    • Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition
    • Grivennikova, V. G., Maklashina, E. O., Gavrikova, E. V. and Vinogradov, A. D. (1997) Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition. Biochim. Biophys. Acta 1319, 223-232
    • (1997) Biochim. Biophys. Acta , vol.1319 , pp. 223-232
    • Grivennikova, V.G.1    Maklashina, E.O.2    Gavrikova, E.V.3    Vinogradov, A.D.4
  • 20
    • 0032490114 scopus 로고    scopus 로고
    • Inhibitors of NADH-ubiquinone reductase: An overview
    • Degli Esposti, M. (1998) Inhibitors of NADH-ubiquinone reductase: an overview. Biochim. Biophys. Acta 1364, 222-235
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 222-235
    • Degli Esposti, M.1
  • 21
    • 0032490106 scopus 로고    scopus 로고
    • Structure-activity relationships of some Complex I inhibitors
    • Miyoshi, H. (1998) Structure-activity relationships of some Complex I inhibitors. Biochim. Biophys. Acta 1364, 236-244
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 236-244
    • Miyoshi, H.1
  • 22
    • 0016378057 scopus 로고
    • Determination of the activity of succinate, NADH, choline, and α-glycerophosphate dehydrogenase
    • Singer, T. P. (1974) Determination of the activity of succinate, NADH, choline, and α-glycerophosphate dehydrogenase. Methods Biochem. Anal. 22, 123-175
    • (1974) Methods Biochem. Anal. , vol.22 , pp. 123-175
    • Singer, T.P.1
  • 23
    • 0027523109 scopus 로고
    • Kinetics of the mitochondrial NADH-ubiquinone oxidoreductase interaction with hexaammineruthenium (III)
    • Sled, V. D. and Vinogradov, A. D. (1993) Kinetics of the mitochondrial NADH-ubiquinone oxidoreductase interaction with hexaammineruthenium (III). Biochim. Biophys. Acta 1141, 262-268
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 262-268
    • Sled, V.D.1    Vinogradov, A.D.2
  • 24
    • 0028209931 scopus 로고
    • Natural variation in the potency and binding sites of mitochondrial quinone-like inhibitors
    • Degli Esposti, M., Crimi, M. and Ghelli, A. (1994) Natural variation in the potency and binding sites of mitochondrial quinone-like inhibitors. Biochem. Soc. Trans. 22, 209-213
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 209-213
    • Degli Esposti, M.1    Crimi, M.2    Ghelli, A.3
  • 25
    • 0344820721 scopus 로고    scopus 로고
    • Three classes of inhibitors share a common binding domain in mitochondrial Complex I (NADH:ubiquinone oxidoreductase)
    • Okun, J. G., Lummen, P. and Brandt, U. (1999) Three classes of inhibitors share a common binding domain in mitochondrial Complex I (NADH:ubiquinone oxidoreductase). J. Biol. Chem. 274, 2625-2630
    • (1999) J. Biol. Chem. , vol.274 , pp. 2625-2630
    • Okun, J.G.1    Lummen, P.2    Brandt, U.3
  • 26
    • 0014931662 scopus 로고
    • Comparative study of thermal degradation of electron transfer particle and reconstituted respiratory chain. Relation of electron transfer to reactivation of submitochondrial particles
    • Luzikov, V. N., Saks, V. A. and Berezin, I. V. (1970) Comparative study of thermal degradation of electron transfer particle and reconstituted respiratory chain. Relation of electron transfer to reactivation of submitochondrial particles. Biochim. Biophys. Acta 223, 16-30
    • (1970) Biochim. Biophys. Acta , vol.223 , pp. 16-30
    • Luzikov, V.N.1    Saks, V.A.2    Berezin, I.V.3
  • 27
    • 18744431390 scopus 로고
    • Über die beziehunġ zwischen molekülstructur und hemmwirkunġ von fettsäuren und monoġlyzeriden auf die atmunġskette von mitochondrien-partikeln
    • Schewe, T., Coutelle, Ch. and Rapoport, S. (1971) Über die Beziehunġ zwischen Molekülstructur und Hemmwirkunġ von Fettsäuren und Monoġlyzeriden auf die Atmunġskette von Mitochondrien-Partikeln. Acta Biol. Med. Ger. 27, 13-28
    • (1971) Acta Biol. Med. Ger. , vol.27 , pp. 13-28
    • Schewe, T.1    Coutelle, Ch.2    Rapoport, S.3
  • 28
    • 0023870802 scopus 로고    scopus 로고
    • Effects of arachidonic acid on respiratory activities in isolated brain mitochondria
    • Hillered, L. and Chan, P. H. (1998) Effects of arachidonic acid on respiratory activities in isolated brain mitochondria. J. Neurosci. Res. 19, 94-100
    • (1998) J. Neurosci. Res. , vol.19 , pp. 94-100
    • Hillered, L.1    Chan, P.H.2
  • 29
    • 0026094280 scopus 로고
    • A possible mechanism of mitochondrial dysfunction during cerebral ischemia: Inhibition of mitochondrial respiration by arachidonic acid
    • Takeuchi, Y., Morii, H., Tamura, M., Hayaishi, O. and Watanabe, Y. (1991) A possible mechanism of mitochondrial dysfunction during cerebral ischemia: inhibition of mitochondrial respiration by arachidonic acid. Arch. Biochem. Biophys. 289, 33-38
    • (1991) Arch. Biochem. Biophys. , vol.289 , pp. 33-38
    • Takeuchi, Y.1    Morii, H.2    Tamura, M.3    Hayaishi, O.4    Watanabe, Y.5
  • 30
    • 0017568943 scopus 로고
    • Lanġsame irreversible hemmunġ der atmunġskette nichtpnospnorylierender submitochondrialer partikel durch freie fettsäuren und deren monoġlyzeride und methylester
    • Ludwig, P., Schewe, T. and Rapoport, S. (1977) Lanġsame irreversible Hemmunġ der Atmunġskette nichtpnospnorylierender submitochondrialer Partikel durch freie Fettsäuren und deren Monoġlyzeride und Methylester. Acta Biol. Med. Ger. 36, 981-998
    • (1977) Acta Biol. Med. Ger. , vol.36 , pp. 981-998
    • Ludwig, P.1    Schewe, T.2    Rapoport, S.3
  • 31
    • 0018169699 scopus 로고
    • Selective inactivation of the NADH-ubiquinone segment of the respiratory chain of submitocnondrial particles by endogenous free fatty acids during hyperthermia
    • Ludwig, P., Bartels, M., Schewe, T. and Rapoport, S. (1978) Selective inactivation of the NADH-ubiquinone segment of the respiratory chain of submitocnondrial particles by endogenous free fatty acids during hyperthermia. FEBS Lett. 95, 181-184
    • (1978) FEBS Lett. , vol.95 , pp. 181-184
    • Ludwig, P.1    Bartels, M.2    Schewe, T.3    Rapoport, S.4
  • 32
    • 0023024427 scopus 로고
    • The modes of action of long chain alkyl compounds on the respiratory chain-linked energy transducing system in submitochondrial particles
    • Batayneh, N., Kopacz, S. J. and Lee, C. P. (1986) The modes of action of long chain alkyl compounds on the respiratory chain-linked energy transducing system in submitochondrial particles. Arch. Biochem. Biophys. 250, 476-487
    • (1986) Arch. Biochem. Biophys. , vol.250 , pp. 476-487
    • Batayneh, N.1    Kopacz, S.J.2    Lee, C.P.3
  • 33
    • 0016175589 scopus 로고
    • On a slow inhibitory effect of free fatty acids on the respiratory chain of non-phosphorylating submitochondrial particles from beef heart
    • Schewe, T., Ludwig, P. and Rapoport, S. (1974) On a slow inhibitory effect of free fatty acids on the respiratory chain of non-phosphorylating submitochondrial particles from beef heart. FEBS Lett. 46, 39-41
    • (1974) FEBS Lett. , vol.46 , pp. 39-41
    • Schewe, T.1    Ludwig, P.2    Rapoport, S.3
  • 34
    • 0021792122 scopus 로고
    • Two modes of irreversible inactivation of the mitochondrial electron-transfer system by tetradecanoic acid
    • Schewe, T., Albracht, S. P. J., Ludwig, P. and Rapoport, S. M. (1985) Two modes of irreversible inactivation of the mitochondrial electron-transfer system by tetradecanoic acid. Biochim. Biophys. Acta 807, 210-215
    • (1985) Biochim. Biophys. Acta , vol.807 , pp. 210-215
    • Schewe, T.1    Albracht, S.P.J.2    Ludwig, P.3    Rapoport, S.M.4
  • 35
    • 0842287450 scopus 로고    scopus 로고
    • Mitochondrial β-oxidation
    • Bartlett, K. and Eaton, S. (2004) Mitochondrial β-oxidation. Eur. J. Biochem. 271, 462-469
    • (2004) Eur. J. Biochem. , vol.271 , pp. 462-469
    • Bartlett, K.1    Eaton, S.2
  • 39
    • 0037328645 scopus 로고    scopus 로고
    • In situ assay of the intramitochondrial enzymes: Use of alamethicin for permeabilization of mitochondria
    • Gostimskaya, I. S., Grivennikova, V. G., Zharova, T. V., Bakeeva, L. E. and Vinogradov, A. D. (2003) In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria. Anal. Biochem. 313, 46-52
    • (2003) Anal. Biochem. , vol.313 , pp. 46-52
    • Gostimskaya, I.S.1    Grivennikova, V.G.2    Zharova, T.V.3    Bakeeva, L.E.4    Vinogradov, A.D.5
  • 40
    • 0027384310 scopus 로고
    • Effect of fatty acids on energy coupling processes in mitochondria
    • Wojtczak, L. and Schönfeld, P. (1993) Effect of fatty acids on energy coupling processes in mitochondria. Biochim. Biophys. Acta 1183, 41-165
    • (1993) Biochim. Biophys. Acta , vol.1183 , pp. 41-165
    • Wojtczak, L.1    Schönfeld, P.2
  • 41
    • 0033387853 scopus 로고    scopus 로고
    • Anion carriers in fatty acid-mediated physiological uncoupling
    • Skulachev, V. P. (1999) Anion carriers in fatty acid-mediated physiological uncoupling J. Bioenerg. Biomembr. 31, 431-445
    • (1999) J. Bioenerg. Biomembr. , vol.31 , pp. 431-445
    • Skulachev, V.P.1
  • 42
    • 0036044373 scopus 로고    scopus 로고
    • Mitochondrial energy dissipation by fatty acids; mechanisms and implications for cell death
    • Bernardi, P., Penzo, D. and Wojtczak, L. (2002) Mitochondrial energy dissipation by fatty acids; mechanisms and implications for cell death. Vitam. Horm. 65, 97-126
    • (2002) Vitam. Horm. , vol.65 , pp. 97-126
    • Bernardi, P.1    Penzo, D.2    Wojtczak, L.3
  • 43
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev, V. P. (1996) Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29, 169-202
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 44
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: New approaches to an old problem of bioenergetics
    • Skulachev, V. P. (1998) Uncoupling: new approaches to an old problem of bioenergetics. Biochim. Biophys. Acta 1363, 100-124
    • (1998) Biochim. Biophys. Acta , vol.1363 , pp. 100-124
    • Skulachev, V.P.1
  • 45
    • 0027260708 scopus 로고
    • Thyroid hormone action on mitochondrial energy transfer
    • Soboll, S. (1993) Thyroid hormone action on mitochondrial energy transfer. Biochim. Biophys. Acta 1144, 1-16
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 1-16
    • Soboll, S.1
  • 46
    • 0014829235 scopus 로고
    • The role of fatty acids in mitochondrial changes during liver ischemia
    • Boime, I., Smith, E. E. and Hunter, Jr, F. E. (1970) The role of fatty acids in mitochondrial changes during liver ischemia. Arch. Biochem. Biophys. 139, 425-443
    • (1970) Arch. Biochem. Biophys. , vol.139 , pp. 425-443
    • Boime, I.1    Smith, E.E.2    Hunter Jr., F.E.3
  • 47
    • 0017817828 scopus 로고
    • Uncoupling activity of endogenous free fatty acids in rat liver mitochondria
    • Chan, S. H. P. and Higgins, Jr, E. (1978) Uncoupling activity of endogenous free fatty acids in rat liver mitochondria. Can. J. Biochem. 56, 111-116
    • (1978) Can. J. Biochem. , vol.56 , pp. 111-116
    • Chan, S.H.P.1    Higgins Jr., E.2
  • 48
    • 0026501020 scopus 로고
    • Global ischaemia induces a biphasic response of the mitochondrial respiratory chain
    • Veitch, K., Hombroeckx, A., Caucheteux, D., Pouleur, H. and Hue, L. (1992) Global ischaemia induces a biphasic response of the mitochondrial respiratory chain. Biochem. J. 281, 709-715
    • (1992) Biochem. J. , vol.281 , pp. 709-715
    • Veitch, K.1    Hombroeckx, A.2    Caucheteux, D.3    Pouleur, H.4    Hue, L.5
  • 50
    • 0141566277 scopus 로고    scopus 로고
    • Transmembrane movement of exogenous long-chain fatty acids: Proteins, enzymes, and vectorial esterification
    • Black, P. N. and DiRusso, C. C. (2003) Transmembrane movement of exogenous long-chain fatty acids: proteins, enzymes, and vectorial esterification. Microbiol. Mol. Biol. Rev. 67, 454-472
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 454-472
    • Black, P.N.1    DiRusso, C.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.