메뉴 건너뛰기




Volumn 9, Issue 3, 1996, Pages 357-368

New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; EMBRYOPHYTA; FUNGI; MAMMALIA; SOLANUM TUBEROSUM; TUBEROSUM;

EID: 0030111226     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1996.09030357.x     Document Type: Article
Times cited : (192)

References (63)
  • 1
    • 0028132103 scopus 로고
    • Complementary DNA sequences of the 24kDa and 21 kDa subunits of complex I from Neurospora
    • Azevedo, J.E., Duarte, M., Belo, J.A., Werner, S. and Videira, A. (1994) Complementary DNA sequences of the 24kDa and 21 kDa subunits of complex I from Neurospora. Biochim. Biophys. Acta, 1188, 159-161.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 159-161
    • Azevedo, J.E.1    Duarte, M.2    Belo, J.A.3    Werner, S.4    Videira, A.5
  • 2
    • 0028816203 scopus 로고
    • Human diseases with defects in oxidative phosphorylation. 1. Decreased amounts of assembled oxidative phosphorylation complexes in mitochondrial encephalomyopathies
    • Bentlage, H., de Coo, R., ter Laak, H. et al. (1995) Human diseases with defects in oxidative phosphorylation. 1. Decreased amounts of assembled oxidative phosphorylation complexes in mitochondrial encephalomyopathies. Eur. J. Biochem. 227, 909-915.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 909-915
    • Bentlage, H.1    De Coo, R.2    Ter Laak, H.3
  • 3
    • 0022379769 scopus 로고
    • Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of beef heart ubiquinol:cytochrome c reductase
    • Borchart, U., Machleidt, W., Schägger, H., Link, T.A. and von Jagow, G. (1985) Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of beef heart ubiquinol:cytochrome c reductase. FEBS Lett. 191, 125-130.
    • (1985) FEBS Lett. , vol.191 , pp. 125-130
    • Borchart, U.1    Machleidt, W.2    Schägger, H.3    Link, T.A.4    Von Jagow, G.5
  • 4
    • 0026571038 scopus 로고
    • Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria
    • Bourguignon, J., Macherel, D., Neuburger, M. and Douce, R. (1992) Isolation, characterization, and sequence analysis of a cDNA clone encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria. Eur. J. Biochem. 204, 865-873.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 865-873
    • Bourguignon, J.1    Macherel, D.2    Neuburger, M.3    Douce, R.4
  • 7
    • 0028857080 scopus 로고
    • The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria
    • Braun, H.P. and Schmitz, U.K. (1995a) The bifunctional cytochrome c reductase/processing peptidase complex from plant mitochondria. J. Bioenerg. Biomembr. 27, 423-436.
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 423-436
    • Braun, H.P.1    Schmitz, U.K.2
  • 8
    • 0028910492 scopus 로고
    • Molecular structure of the 8 kDa subunit of cytochrome c reductase from potato and its ΔΨ-dependent import into isolated mitochondria
    • Braun, H.P. and Schmitz, U.K. (1995b) Molecular structure of the 8 kDa subunit of cytochrome c reductase from potato and its ΔΨ-dependent import into isolated mitochondria. Biochim. Biophys. Acta, 1229, 181-186.
    • (1995) Biochim. Biophys. Acta , vol.1229 , pp. 181-186
    • Braun, H.P.1    Schmitz, U.K.2
  • 9
    • 0029066902 scopus 로고
    • 1 complex evolutionary relics of a processing peptidase?
    • 1 complex evolutionary relics of a processing peptidase? Trends Biol. Sci. 20, 171-175.
    • (1995) Trends Biol. Sci. , vol.20 , pp. 171-175
    • Braun, H.P.1    Schmitz, U.K.2
  • 10
    • 0026610063 scopus 로고
    • 1 from potato: A protein with a presequence for targeting to the mitochondrial intermembrane space
    • 1 from potato: a protein with a presequence for targeting to the mitochondrial intermembrane space. Mol. Gen. Genet. 231, 217-225.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 217-225
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 11
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun, H.P., Emmermann, M., Kruft, V. and Schmitz, U.K. (1992b) The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J. 11, 3219-3227.
    • (1992) EMBO J. , vol.11 , pp. 3219-3227
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 13
    • 0025322981 scopus 로고
    • Structure and function of cytochrome c oxidase
    • Capaldi, R.A. (1990) Structure and function of cytochrome c oxidase. Ann. Rev. Biochem. 59, 569-596.
    • (1990) Ann. Rev. Biochem. , vol.59 , pp. 569-596
    • Capaldi, R.A.1
  • 14
    • 0022981315 scopus 로고
    • Purification and properties of the groES morphogenetic protein of Escherichia coli
    • Chandrasekhar, G.N., Tilly, K., Woolford, C., Hendrix, R. and Georgopoulos, C. (1986) Purification and properties of the groES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261, 12414-12419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12414-12419
    • Chandrasekhar, G.N.1    Tilly, K.2    Woolford, C.3    Hendrix, R.4    Georgopoulos, C.5
  • 16
    • 0027639902 scopus 로고
    • Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase
    • Colas des Francs-Small, C., Ambard-Bretteville, F., Small, D. and René Rémy, R. (1993) Identification of a major soluble protein in mitochondria from nonphotosynthetic tissues as NAD-dependent formate dehydrogenase. Plant Physiol. 102, 1171-1177.
    • (1993) Plant Physiol. , vol.102 , pp. 1171-1177
    • Colas Des Francs-Small, C.1    Ambard-Bretteville, F.2    Small, D.3    René Rémy, R.4
  • 18
    • 0026673926 scopus 로고
    • Silent mitochondrial and active nuclear genes for subunit 2 of cytochrome c oxidase (cox2) in soybean: Evidence for RNA-mediated gene transfer
    • Covello, P.S. and Gray, M.W. (1992) Silent mitochondrial and active nuclear genes for subunit 2 of cytochrome c oxidase (cox2) in soybean: evidence for RNA-mediated gene transfer. EMBO J. 11, 3815-3820.
    • (1992) EMBO J. , vol.11 , pp. 3815-3820
    • Covello, P.S.1    Gray, M.W.2
  • 19
    • 0242651798 scopus 로고
    • The potato mitochondrial ATP synthase subunit 9: Gene structure, RNA editing and partial protein sequence
    • Dell'Orto, P., Moenne, A., Graves, P.V. and Jordana, X. (1993) The potato mitochondrial ATP synthase subunit 9: gene structure, RNA editing and partial protein sequence. Plant Sci. 88, 45-53.
    • (1993) Plant Sci. , vol.88 , pp. 45-53
    • Dell'Orto, P.1    Moenne, A.2    Graves, P.V.3    Jordana, X.4
  • 20
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P. and Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12, 387-395.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 21
    • 0028429953 scopus 로고
    • Molecular features, processing and import of the Rieske iron-sulfur protein from potato mitochondria
    • Emmermann, M., Clericus, M., Braun, H.P., Mozo, T., Heins, L., Kruft, V. and Schmitz, U.K. (1994) Molecular features, processing and import of the Rieske iron-sulfur protein from potato mitochondria. Plant Mol. Biol. 25, 271-281.
    • (1994) Plant Mol. Biol. , vol.25 , pp. 271-281
    • Emmermann, M.1    Clericus, M.2    Braun, H.P.3    Mozo, T.4    Heins, L.5    Kruft, V.6    Schmitz, U.K.7
  • 22
    • 0028075242 scopus 로고
    • The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing
    • Eriksson, A.C., Sjöling, S. and Glaser. E (1994) The ubiquinol cytochrome c oxidoreductase complex of spinach leaf mitochondria is involved in both respiration and protein processing. Biochim. Blophys. Acta, 1186, 221-231.
    • (1994) Biochim. Blophys. Acta , vol.1186 , pp. 221-231
    • Eriksson, A.C.1    Sjöling, S.2    Glaser, E.3
  • 23
    • 0028816953 scopus 로고
    • Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method
    • Geier, B., Schägger, H., Ortwein, C., Link, T.A., Hagen, W.R., Brandt, U. and von Jagow, G (1995) Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method. Eur. J. Biochem. 227, 296-302.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 296-302
    • Geier, B.1    Schägger, H.2    Ortwein, C.3    Link, T.A.4    Hagen, W.R.5    Brandt, U.6    Von Jagow, G.7
  • 24
    • 0025193235 scopus 로고
    • 0ATPase of plant mitochondria: Isolation and polypeptide composition
    • 0ATPase of plant mitochondria: isolation and polypeptide composition. Biochem. Biophys. Res. Commun. 170, 1352-1358.
    • (1991) Biochem. Biophys. Res. Commun. , vol.170 , pp. 1352-1358
    • Hamasur, B.1    Glaser, E.2
  • 25
    • 0026611883 scopus 로고
    • 0 ATP synthase. Identification of the individual subunits and properties of the purified spinach leaf mitochondrial ATP synthase
    • 0 ATP synthase. Identification of the individual subunits and properties of the purified spinach leaf mitochondrial ATP synthase. Eur. J. Biochem. 205, 409-416.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 409-416
    • Hamasur, B.1    Glaser, E.2
  • 26
    • 0021891869 scopus 로고
    • The mitochondrial electron transport and oxidative phosphorylation system
    • Hatefi, Y. (1985) The mitochondrial electron transport and oxidative phosphorylation system. Ann. Rev. Biochem. 54, 1015-1069.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 1015-1069
    • Hatefi, Y.1
  • 27
    • 0000183369 scopus 로고
    • Subunit composition of cytochrome c oxidase in mitochondria of Zea mays
    • Hawkesford. M.J., Liddell, A.D. and Leaver, C.J. (1989) Subunit composition of cytochrome c oxidase in mitochondria of Zea mays. Plant Physiol. 91, 1535-1542.
    • (1989) Plant Physiol. , vol.91 , pp. 1535-1542
    • Hawkesford, M.J.1    Liddell, A.D.2    Leaver, C.J.3
  • 28
    • 0028079979 scopus 로고
    • Biochemical, molecular and functional characterization of porin isoforms from potato mitochondria
    • Heins, L., Mentzel, H., Schmid, A., Benz, R. and Schmitz, U.K. (1994) Biochemical, molecular and functional characterization of porin isoforms from potato mitochondria. J. Biol. Chem. 269, 26 402-26410.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26402-26410
    • Heins, L.1    Mentzel, H.2    Schmid, A.3    Benz, R.4    Schmitz, U.K.5
  • 30
    • 0018791204 scopus 로고
    • Purification and properties of groE, a host protein involved in bacteriophage assembly
    • Hendrix, R.W. (1979) Purification and properties of groE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129, 375-392.
    • (1979) J. Mol. Biol. , vol.129 , pp. 375-392
    • Hendrix, R.W.1
  • 31
    • 0028174957 scopus 로고
    • Purification of the NADH:ubiquinone oxidoreductase (complex I) of the respiratory chain from the inner mitochondrial membrane of Solanum tuberosum
    • Herz, U., Schröder, W., Liddell, A., Leaver, C.J., Brennicke, A. and Grohmann, L. (1994) Purification of the NADH:ubiquinone oxidoreductase (complex I) of the respiratory chain from the inner mitochondrial membrane of Solanum tuberosum. J. Biol. Chem. 269, 2263-2269.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2263-2269
    • Herz, U.1    Schröder, W.2    Liddell, A.3    Leaver, C.J.4    Brennicke, A.5    Grohmann, L.6
  • 32
    • 0028234368 scopus 로고
    • Role of the chaperonin cofactor HsplO in protein folding and sorting in yeast mitochondria
    • Höhfeld, J. and Hartl, F.U. (1994) Role of the chaperonin cofactor HsplO in protein folding and sorting in yeast mitochondria. J. Cell Biol. 126, 305-315.
    • (1994) J. Cell Biol. , vol.126 , pp. 305-315
    • Höhfeld, J.1    Hartl, F.U.2
  • 33
    • 0024396544 scopus 로고
    • Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochondria
    • Hutchinson, E G., Tichelaar, W., Hofhaus, G., Weiss, H. and Leonard, K.R. (1989) Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa mitochondria. EMBO J. 8, 1485-1490.
    • (1989) EMBO J. , vol.8 , pp. 1485-1490
    • Hutchinson, E.G.1    Tichelaar, W.2    Hofhaus, G.3    Weiss, H.4    Leonard, K.R.5
  • 34
    • 0028934057 scopus 로고
    • Cytochrome c reductase from potato does not comprise three core proteins but contains an additional low molecular weight subunit
    • Jänsch, L., Kruft, V., Schmitz, U.K. and Braun, H.P. (1995) Cytochrome c reductase from potato does not comprise three core proteins but contains an additional low molecular weight subunit. Eur. J. Biochem. 228, 878-885.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 878-885
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 35
    • 0020724790 scopus 로고
    • Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoretic procedure
    • Kadenbach, B., Jarausch, J., Hartmann, R. and Merle, P. (1983) Separation of mammalian cytochrome c oxidase into 13 polypeptides by a sodium dodecyl sulfate-gel electrophoretic procedure. Anal. Biochem. 129, 517-521.
    • (1983) Anal. Biochem. , vol.129 , pp. 517-521
    • Kadenbach, B.1    Jarausch, J.2    Hartmann, R.3    Merle, P.4
  • 38
    • 11144329338 scopus 로고    scopus 로고
    • Purification of mitochondria from Arabidopsis
    • (Martinez-Zapater, J.M. and Salinas, J., eds). Totowa, NJ: Humana Press Inc., in press
    • Klein, M., Binder, S. and Brennicke, A. (1996) Purification of mitochondria from Arabidopsis. In: Arabidopsis Protocols, Methods in Molecular Biology Series (Martinez-Zapater, J.M. and Salinas, J., eds). Totowa, NJ: Humana Press Inc., in press.
    • (1996) Arabidopsis Protocols, Methods in Molecular Biology Series
    • Klein, M.1    Binder, S.2    Brennicke, A.3
  • 39
    • 0027605516 scopus 로고
    • Purification and preliminary characterization of mitochondrial complex I (NADH:ubiquinone reductase) from broad bean (Vicia faba L.)
    • Leterme, S. and Boutry, M. (1993) Purification and preliminary characterization of mitochondrial complex I (NADH:ubiquinone reductase) from broad bean (Vicia faba L.). Plant Physiol, 102, 435-443.
    • (1993) Plant Physiol , vol.102 , pp. 435-443
    • Leterme, S.1    Boutry, M.2
  • 40
    • 0019616647 scopus 로고
    • The subunit composition of pea cytochrome c oxidase
    • Matsuoka, M., Maeshima, M. and Asahi, T. (1981) The subunit composition of pea cytochrome c oxidase. J. Biochem. 90, 649-655.
    • (1981) J. Biochem. , vol.90 , pp. 649-655
    • Matsuoka, M.1    Maeshima, M.2    Asahi, T.3
  • 42
    • 0025079832 scopus 로고
    • Molecular cloning of a cDNA for the smallest nuclear encoded subunit of sweet potato cytochrome c oxidase
    • Nakagawa, T., Maeshima, M., Nakamura, K. and Asahi, T. (1990) Molecular cloning of a cDNA for the smallest nuclear encoded subunit of sweet potato cytochrome c oxidase. Eur. J, Biochem. 191, 557-561.
    • (1990) Eur. J, Biochem. , vol.191 , pp. 557-561
    • Nakagawa, T.1    Maeshima, M.2    Nakamura, K.3    Asahi, T.4
  • 43
    • 0027611620 scopus 로고
    • The nuclear gene for subunit Vc of sweet potato cytochrome c oxidase
    • Nakagawa, T., Maeshima, M., Nakamura, K. and Asahi, T. (1993) The nuclear gene for subunit Vc of sweet potato cytochrome c oxidase. Plant Cell Physiol. 34, 621-626.
    • (1993) Plant Cell Physiol. , vol.34 , pp. 621-626
    • Nakagawa, T.1    Maeshima, M.2    Nakamura, K.3    Asahi, T.4
  • 44
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann, J., Norwich, A.L., Neupert, W. and Hartl, F.U. (1989) Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature, 341, 125-130.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Norwich, A.L.2    Neupert, W.3    Hartl, F.U.4
  • 45
    • 0025143280 scopus 로고
    • Structurally unique plant cytochrome c oxidase isolated from wheat germ, a rich source of plant mitochondrial enzymes
    • Pfeiffer, W.E., Ingle, R.T. and Ferguson-Miller, S. (1990) Structurally unique plant cytochrome c oxidase isolated from wheat germ, a rich source of plant mitochondrial enzymes. Biochemistry, 29, 8696-8701.
    • (1990) Biochemistry , vol.29 , pp. 8696-8701
    • Pfeiffer, W.E.1    Ingle, R.T.2    Ferguson-Miller, S.3
  • 48
  • 49
    • 0026832009 scopus 로고
    • cDNA clones encoding Arabidopsis thaliana and Zea Mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock
    • Prasad, T.K. and Stewart, C.R. (1992) cDNA clones encoding Arabidopsis thaliana and Zea Mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock. Plant Mol. Biol. 18, 873-885.
    • (1992) Plant Mol. Biol. , vol.18 , pp. 873-885
    • Prasad, T.K.1    Stewart, C.R.2
  • 50
    • 0028025890 scopus 로고
    • Isolation of the rotenone-sensitive NADH-ubiquinone reductase (complex I) from red beet mitochondria
    • Rasmusson, A.G., Mendel-Hartvig, J., Moller, I.M. and Wiskich, J T. (1994) Isolation of the rotenone-sensitive NADH-ubiquinone reductase (complex I) from red beet mitochondria. Physiol. Plant. 90, 607-615.
    • (1994) Physiol. Plant. , vol.90 , pp. 607-615
    • Rasmusson, A.G.1    Mendel-Hartvig, J.2    Moller, I.M.3    Wiskich, J.T.4
  • 51
    • 0029013434 scopus 로고
    • Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: Normal complex I protein amounts in Parkinson's disease conflict with reduced catalytic activities
    • Schägger, H. (1995) Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: normal complex I protein amounts in Parkinson's disease conflict with reduced catalytic activities. Electrophoresis, 16, 763-770.
    • (1995) Electrophoresis , vol.16 , pp. 763-770
    • Schägger, H.1
  • 52
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 53
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger, H. and von Jagow, G. (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223-231.
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schägger, H.1    Von Jagow, G.2
  • 55
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane complexes by two dimensional native electrophoresis
    • Schägger, H., Cramer, W.A. and von Jagow, G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane complexes by two dimensional native electrophoresis. Anal. Biochem. 217, 220-230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 56
    • 0019889799 scopus 로고
    • Proton-adenosinetriphosphate complex of rat liver mitochondria: Effect of energy state on its interaction with the adenosinetriphosphataseinhibitory peptide
    • Schwerzmann, K. and Pedersen, P.L. (1981) Proton-adenosinetriphosphate complex of rat liver mitochondria: effect of energy state on its interaction with the adenosinetriphosphataseinhibitory peptide. Biochemistry, 20, 6305-6311.
    • (1981) Biochemistry , vol.20 , pp. 6305-6311
    • Schwerzmann, K.1    Pedersen, P.L.2
  • 57
    • 0028141711 scopus 로고
    • Isolation of a novel soybean gene encoding a mitochondrial ATP synthase subunit
    • Smith, M.K., Day, D.A. and Whelan, J. (1994) Isolation of a novel soybean gene encoding a mitochondrial ATP synthase subunit. Arch. Biochem. Biophys. 313, 235-240.
    • (1994) Arch. Biochem. Biophys. , vol.313 , pp. 235-240
    • Smith, M.K.1    Day, D.A.2    Whelan, J.3
  • 58
    • 0023424956 scopus 로고
    • Molecular cloning and further characterization of cDNAs for rat nuclear-encoded cytochrome c oxidase subunits Vlc and VIII
    • Suske, G., Mengel, T., Cordingley, M. and Kadenbach, B. (1987) Molecular cloning and further characterization of cDNAs for rat nuclear-encoded cytochrome c oxidase subunits Vlc and VIII. Eur. J. Biochem. 168, 233-237.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 233-237
    • Suske, G.1    Mengel, T.2    Cordingley, M.3    Kadenbach, B.4
  • 59
    • 0026660875 scopus 로고
    • Purification, cDNA cloning and Northern-blot analysis of mitochondrial chaperonin 60 from pumpkin cotyledons
    • Tsugeki, R., Mori, H. and Nishimura, M. (1992) Purification, cDNA cloning and Northern-blot analysis of mitochondrial chaperonin 60 from pumpkin cotyledons. Eur. J. Biochem. 209, 453-458.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 453-458
    • Tsugeki, R.1    Mori, H.2    Nishimura, M.3
  • 60
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker, J.E. (1992) The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25, 253-324.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 62
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss, H., Friedrich, T., Hofhaus, G. and Preis, D. (1991) The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197, 563-576.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.