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Volumn 1604, Issue 3, 2003, Pages 135-150

The nuclear encoded subunits of complex I from bovine heart mitochondria

Author keywords

Complex I; Electron transport chain; Mitochondrion; NADH:ubiquinone oxidoreductase; Respiratory chain; Subunit composition

Indexed keywords

FLAVINE MONONUCLEOTIDE; MITOCHONDRIAL DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 0038771142     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(03)00059-8     Document Type: Review
Times cited : (344)

References (120)
  • 1
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • Walker J.E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25:1992;253-324.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 2
    • 0025760073 scopus 로고
    • The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
    • Weiss H., Friedrich T., Hofhaus G., Preis D. The respiratory-chain NADH dehydrogenase (complex I) of mitochondria. Eur. J. Biochem. 197:1991;563-576.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.2    Hofhaus, G.3    Preis, D.4
  • 5
    • 0032490117 scopus 로고    scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Friedrich T. The NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim. Biophys. Acta. 1364:1998;134-146.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 134-146
    • Friedrich, T.1
  • 6
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siècle
    • Saraste M. Oxidative phosphorylation at the fin de siècle. Science. 283:1999;1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 7
    • 0034984506 scopus 로고    scopus 로고
    • Structures and proton-pumping strategies of mitochondrial respiratory enzymes
    • Schultz B.E., Chan S.I. Structures and proton-pumping strategies of mitochondrial respiratory enzymes. Annu. Rev. Biophys. Biomol. Struct. 30:2001;23-65.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 23-65
    • Schultz, B.E.1    Chan, S.I.2
  • 8
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • Wikström M. Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone. FEBS Lett. 169:1984;300-304.
    • (1984) FEBS Lett. , vol.169 , pp. 300-304
    • Wikström, M.1
  • 9
    • 0024023239 scopus 로고
    • Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio
    • Brown G.C., Brand M.D. Proton/electron stoichiometry of mitochondrial complex I estimated from the equilibrium thermodynamic force ratio. Biochem. J. 252:1988;473-479.
    • (1988) Biochem. J. , vol.252 , pp. 473-479
    • Brown, G.C.1    Brand, M.D.2
  • 10
    • 0033179604 scopus 로고    scopus 로고
    • Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)
    • Grigorieff N. Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I). Curr. Opin. Struct. Biol. 9:1999;476-483.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 476-483
    • Grigorieff, N.1
  • 11
    • 0032512616 scopus 로고    scopus 로고
    • Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Guénebaut V., Schlitt A., Weiss H., Leonard K., Friedrich T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276:1998;105-112.
    • (1998) J. Mol. Biol. , vol.276 , pp. 105-112
    • Guénebaut, V.1    Schlitt, A.2    Weiss, H.3    Leonard, K.4    Friedrich, T.5
  • 12
    • 0028881842 scopus 로고
    • Structural analysis of NADH:ubiquinone oxidoreductase from bovine heart mitochondria
    • Walker J.E., Skehel J.M., Buchanan S.K. Structural analysis of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Methods Enzymol. 260:1995;14-34.
    • (1995) Methods Enzymol. , vol.260 , pp. 14-34
    • Walker, J.E.1    Skehel, J.M.2    Buchanan, S.K.3
  • 13
    • 0035914435 scopus 로고    scopus 로고
    • GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Fearnley I.M., Carroll J., Shannon R.J., Runswick M.J., Walker J.E., Hirst J. GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 276:2001;38345-38348.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38345-38348
    • Fearnley, I.M.1    Carroll, J.2    Shannon, R.J.3    Runswick, M.J.4    Walker, J.E.5    Hirst, J.6
  • 14
    • 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., Hirst J. Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I: identification of two new subunits. J. Biol. Chem. 277:2002;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
  • 18
    • 0023032242 scopus 로고
    • URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit
    • Chomyn A., Cleeter M.W.J., Ragan C.I., Riley M., Doolittle R.F., Attardi G. URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit. Science. 234:1986;614-618.
    • (1986) Science , vol.234 , pp. 614-618
    • Chomyn, A.1    Cleeter, M.W.J.2    Ragan, C.I.3    Riley, M.4    Doolittle, R.F.5    Attardi, G.6
  • 19
    • 0035349906 scopus 로고    scopus 로고
    • The genetics and pathology of oxidative phosphorylation
    • Smeitink J., van den Heuvel L., DiMauro S. The genetics and pathology of oxidative phosphorylation. Nat. Rev. Genet. 2:2001;342-352.
    • (2001) Nat. Rev. Genet. , vol.2 , pp. 342-352
    • Smeitink, J.1    Van den Heuvel, L.2    DiMauro, S.3
  • 20
    • 0034783191 scopus 로고    scopus 로고
    • On complex I and other NADH:ubiquinone reductases of Neurospora crassa mitochondria
    • Videira A., Duarte M. On complex I and other NADH:ubiquinone reductases of Neurospora crassa mitochondria. J. Bioenerg. Biomembr. 33:2001;197-203.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 197-203
    • Videira, A.1    Duarte, M.2
  • 21
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • Videira A., Duarte M. From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta. 1555:2002;187-191.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 187-191
    • Videira, A.1    Duarte, M.2
  • 22
    • 0034691658 scopus 로고    scopus 로고
    • Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica
    • Djafarzadeh R., Kerscher S., Zwicker K., Radermacher M., Lindahl M., Schägger H., Brandt U. Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta. 1459:2000;230-238.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 230-238
    • Djafarzadeh, R.1    Kerscher, S.2    Zwicker, K.3    Radermacher, M.4    Lindahl, M.5    Schägger, H.6    Brandt, U.7
  • 24
    • 0032751077 scopus 로고    scopus 로고
    • Analysis of wheat mitochondrial complex I purified by a one-step immunoaffinity chromatography
    • Combettes B., Grienenberger J.-M. Analysis of wheat mitochondrial complex I purified by a one-step immunoaffinity chromatography. Biochimie. 81:1999;645-653.
    • (1999) Biochimie , vol.81 , pp. 645-653
    • Combettes, B.1    Grienenberger, J.-M.2
  • 25
    • 0031041453 scopus 로고    scopus 로고
    • The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8
    • Yano T., Chu S.S., Sled V.D., Ohnishi T., Yagi T. The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. J. Biol. Chem. 272:1997;4201-4211.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4201-4211
    • Yano, T.1    Chu, S.S.2    Sled, V.D.3    Ohnishi, T.4    Yagi, T.5
  • 26
    • 0027477868 scopus 로고
    • DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Xu X., Matsuno-Yagi A., Yagi T. DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry. 32:1993;968-981.
    • (1993) Biochemistry , vol.32 , pp. 968-981
    • Xu, X.1    Matsuno-Yagi, A.2    Yagi, T.3
  • 27
    • 0027519561 scopus 로고
    • The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli
    • Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. The gene locus of the proton-translocating NADH:ubiquinone oxidoreductase in Escherichia coli. J. Mol. Biol. 233:1993;109-122.
    • (1993) J. Mol. Biol. , vol.233 , pp. 109-122
    • Weidner, U.1    Geier, S.2    Ptock, A.3    Friedrich, T.4    Leif, H.5    Weiss, H.6
  • 31
    • 0033539647 scopus 로고    scopus 로고
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure
    • 2 digestion of cardiolipin bound to bovine cytochrome c oxidase alters both activity and quaternary structure. Biochemistry. 38:1999;14966-14972.
    • (1999) Biochemistry , vol.38 , pp. 14966-14972
    • Sedlák, E.1    Robinson, N.C.2
  • 32
    • 0034711184 scopus 로고    scopus 로고
    • α-terminal acetylation of eukaryotic proteins
    • α-terminal acetylation of eukaryotic proteins. J. Biol. Chem. 275:2000;36479-36482.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 33
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • Farazi T.A., Waksman G., Gordon J.I. The biology and enzymology of protein N-myristoylation. J. Biol. Chem. 276:2001;39501-39504.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 34
    • 0026472383 scopus 로고
    • Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centres of the enzyme
    • Finel M., Skehel J.M., Albracht S.P.J., Fearnley I.M., Walker J.E. Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centres of the enzyme. Biochemistry. 31:1992;11425-11434.
    • (1992) Biochemistry , vol.31 , pp. 11425-11434
    • Finel, M.1    Skehel, J.M.2    Albracht, S.P.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 35
    • 0034691280 scopus 로고    scopus 로고
    • Resolution of the membrane domain of bovine complex I into subcomplexes: Implications for the structural organization of the enzyme
    • Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E. Resolution of the membrane domain of bovine complex I into subcomplexes: implications for the structural organization of the enzyme. Biochemistry. 39:2000;7229-7235.
    • (2000) Biochemistry , vol.39 , pp. 7229-7235
    • Sazanov, L.A.1    Peak-Chew, S.Y.2    Fearnley, I.M.3    Walker, J.E.4
  • 36
    • 0027973585 scopus 로고
    • Isolation and characterisation of subcomplexes of the mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Finel M., Majander A.S., Tyynelä J., De Jong A.M.P., Albracht S.P.J., Wikström M. Isolation and characterisation of subcomplexes of the mitochondrial NADH:ubiquinone oxidoreductase (complex I). Eur. J. Biochem. 226:1994;237-242.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 237-242
    • Finel, M.1    Majander, A.S.2    Tyynelä, J.3    De Jong, A.M.P.4    Albracht, S.P.J.5    Wikström, M.6
  • 37
    • 0018438631 scopus 로고
    • Purification and molecular and enzymic properties of mitochondrial NADH dehydrogenase
    • Galante Y.M., Hatefi Y. Purification and molecular and enzymic properties of mitochondrial NADH dehydrogenase. Arch. Biochem. Biophys. 192:1979;559-568.
    • (1979) Arch. Biochem. Biophys. , vol.192 , pp. 559-568
    • Galante, Y.M.1    Hatefi, Y.2
  • 38
    • 0020473231 scopus 로고
    • Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins
    • Ragan C.I., Galante Y.M., Hatefi Y., Ohnishi T. Resolution of mitochondrial NADH dehydrogenase and isolation of two iron-sulfur proteins. Biochemistry. 21:1982;590-594.
    • (1982) Biochemistry , vol.21 , pp. 590-594
    • Ragan, C.I.1    Galante, Y.M.2    Hatefi, Y.3    Ohnishi, T.4
  • 39
    • 0026032458 scopus 로고
    • Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase
    • Pilkington S.J., Skehel J.M., Gennis R.B., Walker J.E. Relationship between mitochondrial NADH-ubiquinone reductase and a bacterial NAD-reducing hydrogenase. Biochemistry. 30:1991;2166-2175.
    • (1991) Biochemistry , vol.30 , pp. 2166-2175
    • Pilkington, S.J.1    Skehel, J.M.2    Gennis, R.B.3    Walker, J.E.4
  • 40
    • 0032539640 scopus 로고    scopus 로고
    • Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli
    • Braun M., Bungert S., Friedrich T. Characterization of the overproduced NADH dehydrogenase fragment of the NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochemistry. 37:1998;1861-1867.
    • (1998) Biochemistry , vol.37 , pp. 1861-1867
    • Braun, M.1    Bungert, S.2    Friedrich, T.3
  • 41
    • 0037417865 scopus 로고    scopus 로고
    • Sodium ion cycling mediates energy coupling between complex I and ATP synthase
    • Gemperli A.C., Dimroth P., Steuber J. Sodium ion cycling mediates energy coupling between complex I and ATP synthase. Proc. Natl. Acad. Sci. U. S. A. 100:2003;839-844.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 839-844
    • Gemperli, A.C.1    Dimroth, P.2    Steuber, J.3
  • 42
    • 0037417806 scopus 로고    scopus 로고
    • The dichotomy of complex I: A sodium ion pump or a proton pump
    • Hirst J. The dichotomy of complex I: a sodium ion pump or a proton pump. Proc. Natl. Acad. Sci. U. S. A. 100:2003;773-775.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 773-775
    • Hirst, J.1
  • 43
    • 0027970164 scopus 로고
    • Identification of amino acid residues associated with the [2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano T., Sled V.D., Ohnishi T., Yagi T. Identification of amino acid residues associated with the [2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. FEBS Lett. 354:1994;160-164.
    • (1994) FEBS Lett. , vol.354 , pp. 160-164
    • Yano, T.1    Sled, V.D.2    Ohnishi, T.3    Yagi, T.4
  • 44
    • 0035976815 scopus 로고    scopus 로고
    • Ferredoxins of the third kind
    • Meyer J. Ferredoxins of the third kind. FEBS Lett. 509:2001;1-5.
    • (2001) FEBS Lett. , vol.509 , pp. 1-5
    • Meyer, J.1
  • 45
    • 0037031281 scopus 로고    scopus 로고
    • Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (complex I)
    • Zu Y., Di Bernardo S., Yagi T., Hirst J. Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 41:2002;10056-10069.
    • (2002) Biochemistry , vol.41 , pp. 10056-10069
    • Zu, Y.1    Di Bernardo, S.2    Yagi, T.3    Hirst, J.4
  • 46
    • 0029864414 scopus 로고    scopus 로고
    • Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano T., Sled V.D., Ohnishi T., Yagi T. Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 271:1996;5907-5913.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5907-5913
    • Yano, T.1    Sled, V.D.2    Ohnishi, T.3    Yagi, T.4
  • 47
    • 0019888311 scopus 로고
    • + with the mitochondrial NADH dehydrogenase
    • + with the mitochondrial NADH dehydrogenase. J. Biol. Chem. 256:1981;8318-8323.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8318-8323
    • Chen, S.1    Guillory, R.J.2
  • 48
  • 49
    • 77956772373 scopus 로고
    • Structural and functional diversity of ferredoxins and related proteins
    • Matsubara H., Saeki K. Structural and functional diversity of ferredoxins and related proteins. Adv. Inorg. Chem. 38:1992;223-280.
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 223-280
    • Matsubara, H.1    Saeki, K.2
  • 50
    • 0027990677 scopus 로고
    • Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Sled V.D., Rudnitzky N.I., Hatefi Y., Ohnishi T. Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 33:1994;10069-10075.
    • (1994) Biochemistry , vol.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 51
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta. 1364:1998;186-206.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 52
    • 0025886958 scopus 로고
    • Primary structures of two subunits of NADH:ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus
    • Preis D., Weidner U., Conzen C., Azevedo J.E., Nehls U., Röhlen D., Van der Pas J., Sackmann U., Schneider R., Werner S., Weiss H. Primary structures of two subunits of NADH:ubiquinone reductase from Neurospora crassa concerned with NADH-oxidation. Relationship to a soluble NAD-reducing hydrogenase of Alcaligenes eutrophus. Biochim. Biophys. Acta. 1090:1991;133-138.
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 133-138
    • Preis, D.1    Weidner, U.2    Conzen, C.3    Azevedo, J.E.4    Nehls, U.5    Röhlen, D.6    Van der Pas, J.7    Sackmann, U.8    Schneider, R.9    Werner, S.10    Weiss, H.11
  • 53
    • 0029112808 scopus 로고
    • Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans
    • Yano T., Yagi T., Sled V.D., Ohnishi T. Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans. J. Biol. Chem. 270:1995;18264-18270.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18264-18270
    • Yano, T.1    Yagi, T.2    Sled, V.D.3    Ohnishi, T.4
  • 54
    • 0037844859 scopus 로고    scopus 로고
    • Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans
    • Yano T., Sklar J., Nakamaru-Ogiso E., Takahashi Y., Yagi T., Ohnishi T. Characterization of cluster N5 as a fast-relaxing [4Fe-4S] cluster in the Nqo3 subunit of the proton-translocating NADH-ubiquinone oxidoreductase from Paracoccus denitrificans. J. Biol. Chem. 278:2003;15514-15522.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15514-15522
    • Yano, T.1    Sklar, J.2    Nakamaru-Ogiso, E.3    Takahashi, Y.4    Yagi, T.5    Ohnishi, T.6
  • 55
    • 0037127215 scopus 로고    scopus 로고
    • 27C) in the Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8
    • 27C) in the Nqo3 subunit in the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Thermus thermophilus HB-8. J. Biol. Chem. 277:2002;1680-1688.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1680-1688
    • Nakamaru-Ogiso, E.1    Yano, T.2    Ohnishi, T.3    Yagi, T.4
  • 56
    • 0025854234 scopus 로고
    • A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes
    • Dupuis A., Skehel J.M., Walker J.E. A homologue of a nuclear-coded iron-sulfur protein subunit of bovine mitochondrial complex I is encoded in chloroplast genomes. Biochemistry. 30:1991;2954-2960.
    • (1991) Biochemistry , vol.30 , pp. 2954-2960
    • Dupuis, A.1    Skehel, J.M.2    Walker, J.E.3
  • 57
    • 0033215197 scopus 로고    scopus 로고
    • Characterization of the putative 2×[4Fe-4S]-binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans
    • Yano T., Magnitsky S., Sled V.D., Ohnishi T., Yagi T. Characterization of the putative 2×[4Fe-4S]-binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. J. Biol. Chem. 274:1999;28598-28605.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28598-28605
    • Yano, T.1    Magnitsky, S.2    Sled, V.D.3    Ohnishi, T.4    Yagi, T.5
  • 58
    • 0019324533 scopus 로고
    • An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria
    • Ingledew W.J., Ohnishi T. An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria. Biochem. J. 186:1980;111-117.
    • (1980) Biochem. J. , vol.186 , pp. 111-117
    • Ingledew, W.J.1    Ohnishi, T.2
  • 59
    • 0035918512 scopus 로고    scopus 로고
    • Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I)
    • Rasmussen T., Scheide D., Brors B., Kintscher L., Weiss H., Friedrich T. Identification of two tetranuclear FeS clusters on the ferredoxin-type subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry. 40:2001;6124-6131.
    • (2001) Biochemistry , vol.40 , pp. 6124-6131
    • Rasmussen, T.1    Scheide, D.2    Brors, B.3    Kintscher, L.4    Weiss, H.5    Friedrich, T.6
  • 61
    • 0034778053 scopus 로고    scopus 로고
    • Toward a characterization of the connecting module of complex I
    • Dupuis A., Prieur I., Lunardi J. Toward a characterization of the connecting module of complex I. J. Bioenerg. Biomembr. 33:2001;159-168.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 159-168
    • Dupuis, A.1    Prieur, I.2    Lunardi, J.3
  • 63
    • 0034604568 scopus 로고    scopus 로고
    • Function of conserved acidic residues in the PSST homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica
    • Ahlers P., Zwicker K., Kerscher S., Brandt U. Function of conserved acidic residues in the PSST homologue of complex I (NADH:ubiquinone oxidoreductase) from Yarrowia lipolytica. J. Biol. Chem. 275:2000;23577-23582.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23577-23582
    • Ahlers, P.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 64
    • 0035968167 scopus 로고    scopus 로고
    • A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I
    • Kashani-Poor N., Zwicker K., Kerscher S., Brandt U. A central functional role for the 49-kDa subunit within the catalytic core of mitochondrial complex I. J. Biol. Chem. 276:2001;24082-24087.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24082-24087
    • Kashani-Poor, N.1    Zwicker, K.2    Kerscher, S.3    Brandt, U.4
  • 65
    • 0027328631 scopus 로고
    • Intimate relationships of the large and small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH:ubiquinone oxidoreductase
    • Albracht S.P.J. Intimate relationships of the large and small subunits of all nickel hydrogenases with two nuclear-encoded subunits of mitochondrial NADH:ubiquinone oxidoreductase. Biochim. Biophys. Acta. 1144:1993;221-224.
    • (1993) Biochim. Biophys. Acta , vol.1144 , pp. 221-224
    • Albracht, S.P.J.1
  • 66
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 68
    • 0032970653 scopus 로고    scopus 로고
    • A second mechanism of respiratory control
    • Kadenbach B., Arnold S. A second mechanism of respiratory control. FEBS Lett. 447:1999;131-134.
    • (1999) FEBS Lett. , vol.447 , pp. 131-134
    • Kadenbach, B.1    Arnold, S.2
  • 69
    • 0027225845 scopus 로고
    • Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria
    • Emmermann M., Braun H.-P., Arretz M., Schmitz U.K. Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria. J. Biol. Chem. 268:1993;18936-18942.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18936-18942
    • Emmermann, M.1    Braun, H.-P.2    Arretz, M.3    Schmitz, U.K.4
  • 72
    • 0026484793 scopus 로고
    • Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins
    • Fearnley I.M., Walker J.E. Conservation of sequences of subunits of mitochondrial complex I and their relationships with other proteins. Biochim. Biophys. Acta. 1140:1992;105-134.
    • (1992) Biochim. Biophys. Acta , vol.1140 , pp. 105-134
    • Fearnley, I.M.1    Walker, J.E.2
  • 73
    • 0032478597 scopus 로고    scopus 로고
    • Mitochondrial NADH-ubiquinone oxidoreductase (complex I) - Effects of substrates on the fragmentation of subunits by trypsin
    • Yamaguchi M., Belogrudov G.I., Hatefi Y. Mitochondrial NADH-ubiquinone oxidoreductase (complex I) - effects of substrates on the fragmentation of subunits by trypsin. J. Biol. Chem. 273:1998;8094-8098.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8094-8098
    • Yamaguchi, M.1    Belogrudov, G.I.2    Hatefi, Y.3
  • 74
    • 0033979304 scopus 로고    scopus 로고
    • The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Yamaguchi M., Belogrudov G.I., Matsuno-Yagi A., Hatefi Y. The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (complex I). Eur. J. Biochem. 267:2000;329-336.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 329-336
    • Yamaguchi, M.1    Belogrudov, G.I.2    Matsuno-Yagi, A.3    Hatefi, Y.4
  • 75
    • 0033600871 scopus 로고    scopus 로고
    • A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex
    • Schulte U., Haupt V., Abelmann K., Fecke W., Brors B., Rasmussen T., Friedrich T., Weiss H. A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex. J. Mol. Biol. 292:1999;569-580.
    • (1999) J. Mol. Biol. , vol.292 , pp. 569-580
    • Schulte, U.1    Haupt, V.2    Abelmann, K.3    Fecke, W.4    Brors, B.5    Rasmussen, T.6    Friedrich, T.7    Weiss, H.8
  • 76
    • 0032898876 scopus 로고    scopus 로고
    • A common ancestor for a subunit in the mitochondrial proton-translocating NADH:ubiquinone oxidoreductase (complex I) and short-chain dehydrogenases/reductases
    • Baker M.E., Grundy W.N., Elkan C.P. A common ancestor for a subunit in the mitochondrial proton-translocating NADH:ubiquinone oxidoreductase (complex I) and short-chain dehydrogenases/reductases. Cell. Mol. Life Sci. 55:1999;450-455.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 450-455
    • Baker, M.E.1    Grundy, W.N.2    Elkan, C.P.3
  • 78
    • 0039699818 scopus 로고    scopus 로고
    • SDR and MDR: Completed genome sequences show these protein families to be large, of old origin and of complex nature
    • Jörnvall H., Höög J.-O., Persson B. SDR and MDR: completed genome sequences show these protein families to be large, of old origin and of complex nature. FEBS Lett. 445:1999;261-264.
    • (1999) FEBS Lett. , vol.445 , pp. 261-264
    • Jörnvall, H.1    Höög, J.-O.2    Persson, B.3
  • 79
    • 0034656330 scopus 로고    scopus 로고
    • The X-ray structure of Brassica napus β-keto acyl carrier protein reductase and its implications for substrate binding and catalysis
    • Fisher M., Kroon J.T.M., Martindale W., Stuitje A.R., Slabas A.R., Rafferty J.B. The X-ray structure of Brassica napus β-keto acyl carrier protein reductase and its implications for substrate binding and catalysis. Structure. 8:2000;339-347.
    • (2000) Structure , vol.8 , pp. 339-347
    • Fisher, M.1    Kroon, J.T.M.2    Martindale, W.3    Stuitje, A.R.4    Slabas, A.R.5    Rafferty, J.B.6
  • 81
    • 0025827137 scopus 로고
    • Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria
    • Runswick M.J., Fearnley I.M., Skehel J.M., Walker J.E. Presence of an acyl carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett. 286:1991;121-124.
    • (1991) FEBS Lett. , vol.286 , pp. 121-124
    • Runswick, M.J.1    Fearnley, I.M.2    Skehel, J.M.3    Walker, J.E.4
  • 82
    • 0025779382 scopus 로고
    • The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH:ubiquinone reductase (complex I)
    • Sackmann U., Zensen R., Röhlen D., Jahnke U., Weiss H. The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH:ubiquinone reductase (complex I). Eur. J. Biochem. 200:1991;463-469.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 463-469
    • Sackmann, U.1    Zensen, R.2    Röhlen, D.3    Jahnke, U.4    Weiss, H.5
  • 83
    • 0023904887 scopus 로고
    • Neurospora mitochondria contain an acyl-carrier protein
    • Brody S., Mikolajczyk S. Neurospora mitochondria contain an acyl-carrier protein. Eur. J. Biochem. 173:1988;353-359.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 353-359
    • Brody, S.1    Mikolajczyk, S.2
  • 84
    • 0025012826 scopus 로고
    • De novo fatty acid synthesis mediated by acyl-carrier protein in Neurospora crassa mitochondria
    • Mikolajczyk S., Brody S. De novo fatty acid synthesis mediated by acyl-carrier protein in Neurospora crassa mitochondria. Eur. J. Biochem. 187:1990;431-437.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 431-437
    • Mikolajczyk, S.1    Brody, S.2
  • 85
    • 0026662355 scopus 로고
    • De novo synthesis and desaturation of fatty acids at the mitochondrial acyl-carrier protein, a subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa
    • Zensen R., Husmann H., Schneider R., Peine T., Weiss H. De novo synthesis and desaturation of fatty acids at the mitochondrial acyl-carrier protein, a subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa. FEBS Lett. 310:1992;179-181.
    • (1992) FEBS Lett. , vol.310 , pp. 179-181
    • Zensen, R.1    Husmann, H.2    Schneider, R.3    Peine, T.4    Weiss, H.5
  • 86
    • 0029556942 scopus 로고
    • Different respiratory-defective phenotypes of Neurospora crassa and Saccharomyces cerevisiae after inactivation of the gene encoding the mitochondrial acyl carrier protein
    • Schneider R., Massow M., Lisowsky T., Weiss H. Different respiratory-defective phenotypes of Neurospora crassa and Saccharomyces cerevisiae after inactivation of the gene encoding the mitochondrial acyl carrier protein. Curr. Genet. 29:1995;10-17.
    • (1995) Curr. Genet. , vol.29 , pp. 10-17
    • Schneider, R.1    Massow, M.2    Lisowsky, T.3    Weiss, H.4
  • 87
    • 0030915349 scopus 로고    scopus 로고
    • Mitochondrial fatty acid synthesis: A relic of endosymbiontic origin and a specialized means for respiration
    • Schneider R., Brors B., Massow M., Weiss H. Mitochondrial fatty acid synthesis: a relic of endosymbiontic origin and a specialized means for respiration. FEBS Lett. 407:1997;249-252.
    • (1997) FEBS Lett. , vol.407 , pp. 249-252
    • Schneider, R.1    Brors, B.2    Massow, M.3    Weiss, H.4
  • 88
    • 0030925929 scopus 로고    scopus 로고
    • Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae
    • Brody S., Oh C., Hoja U., Schweizer E. Mitochondrial acyl carrier protein is involved in lipoic acid synthesis in Saccharomyces cerevisiae. FEBS Lett. 408:1997;217-220.
    • (1997) FEBS Lett. , vol.408 , pp. 217-220
    • Brody, S.1    Oh, C.2    Hoja, U.3    Schweizer, E.4
  • 89
    • 0030747906 scopus 로고    scopus 로고
    • A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria
    • Jordan S.W., Cronan J.E. A new metabolic link. The acyl carrier protein of lipid synthesis donates lipoic acid to the pyruvate dehydrogenase complex in Escherichia coli and mitochondria. J. Biol. Chem. 272:1997;17903-17906.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17903-17906
    • Jordan, S.W.1    Cronan, J.E.2
  • 90
    • 0031026270 scopus 로고    scopus 로고
    • Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production
    • Wada H., Shintani D., Ohlrogge J. Why do mitochondria synthesize fatty acids? Evidence for involvement in lipoic acid production. Proc. Natl. Acad. Sci. U. S. A. 94:1997;1591-1596.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1591-1596
    • Wada, H.1    Shintani, D.2    Ohlrogge, J.3
  • 93
    • 13044310136 scopus 로고    scopus 로고
    • The NDUFA1 gene product (MWFE protein) is essential for activity of complex I in mammalian mitochondria
    • Au H.C., Seo B.B., Matsuno-Yagi A., Yagi T., Scheffler I.E. The NDUFA1 gene product (MWFE protein) is essential for activity of complex I in mammalian mitochondria. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4354-4359.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4354-4359
    • Au, H.C.1    Seo, B.B.2    Matsuno-Yagi, A.3    Yagi, T.4    Scheffler, I.E.5
  • 94
    • 0034783193 scopus 로고    scopus 로고
    • Molecular genetics of the mammalian NADH-ubiquinone oxidoreductase
    • Scheffler I.E., Yadava N. Molecular genetics of the mammalian NADH-ubiquinone oxidoreductase. J. Bioenerg. Biomembr. 33:2001;243-250.
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 243-250
    • Scheffler, I.E.1    Yadava, N.2
  • 96
    • 0034721920 scopus 로고    scopus 로고
    • Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-β and retinoic acid combination, using a genetic approach
    • Angell J.E., Lindner D.J., Shapiro P.S., Hofmann E.R., Kalvakolanu D.V. Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-β and retinoic acid combination, using a genetic approach. J. Biol. Chem. 275:2000;33416-33426.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33416-33426
    • Angell, J.E.1    Lindner, D.J.2    Shapiro, P.S.3    Hofmann, E.R.4    Kalvakolanu, D.V.5
  • 97
    • 0033910295 scopus 로고    scopus 로고
    • Chromosomal localization of human GRIM-19, a novel IFN-β and retinoic acid-activated regulator of cell death
    • Chidambaram N.V., Angell J.E., Ling W., Hofmann E.R., Kalvakolanu D.V. Chromosomal localization of human GRIM-19, a novel IFN-β and retinoic acid-activated regulator of cell death. J. Interferon Cytokine Res. 20:2000;661-665.
    • (2000) J. Interferon Cytokine Res. , vol.20 , pp. 661-665
    • Chidambaram, N.V.1    Angell, J.E.2    Ling, W.3    Hofmann, E.R.4    Kalvakolanu, D.V.5
  • 98
    • 0036333658 scopus 로고    scopus 로고
    • Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus interacts with a cell death regulator, GRIM-19, and inhibits interferon/retinoic acid-induced cell death
    • Seo T., Lee D., Shim Y.S., Angell J.E., Chidambaram N.V., Kalvakolanu D.V., Choe J. Viral interferon regulatory factor 1 of Kaposi's sarcoma-associated herpesvirus interacts with a cell death regulator, GRIM-19, and inhibits interferon/retinoic acid-induced cell death. J. Virol. 76:2002;8789-8807.
    • (2002) J. Virol. , vol.76 , pp. 8789-8807
    • Seo, T.1    Lee, D.2    Shim, Y.S.3    Angell, J.E.4    Chidambaram, N.V.5    Kalvakolanu, D.V.6    Choe, J.7
  • 99
    • 0037451235 scopus 로고    scopus 로고
    • GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction
    • Lufei C., Ma J., Huang G., Zhang T., Novotny-Diermayr V., Ong C.T., Cao X. GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. EMBO J. 22:2003;1325-1335.
    • (2003) EMBO J. , vol.22 , pp. 1325-1335
    • Lufei, C.1    Ma, J.2    Huang, G.3    Zhang, T.4    Novotny-Diermayr, V.5    Ong, C.T.6    Cao, X.7
  • 100
    • 0036440556 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies against GRIM-19, a novel IFN-β and retinoic acid-activated regulator of cell death
    • Hu J., Angell J.E., Zhang J., Ma X., Seo T., Raha A., Hayashi J., Choe J., Kalvakolanu D.V. Characterization of monoclonal antibodies against GRIM-19, a novel IFN-β and retinoic acid-activated regulator of cell death. J. Interferon Cytokine Res. 22:2002;1017-1026.
    • (2002) J. Interferon Cytokine Res. , vol.22 , pp. 1017-1026
    • Hu, J.1    Angell, J.E.2    Zhang, J.3    Ma, X.4    Seo, T.5    Raha, A.6    Hayashi, J.7    Choe, J.8    Kalvakolanu, D.V.9
  • 101
    • 0033133729 scopus 로고    scopus 로고
    • Mitochondrial-matrix proteins at unexpected locations: Are they exported?
    • Soltys B.J., Gupta R.S. Mitochondrial-matrix proteins at unexpected locations: are they exported? Trends Biochem. Sci. 24:1999;174-177.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 174-177
    • Soltys, B.J.1    Gupta, R.S.2
  • 102
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li L.Y., Luo X., Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature. 412:2001;95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 103
    • 0035824633 scopus 로고    scopus 로고
    • Mitochondrial respiration is uniquely associated with the prooxidant and apoptotic effects of N-(4-hydroxyphenyl)retinamide
    • Hail N., Lotan R. Mitochondrial respiration is uniquely associated with the prooxidant and apoptotic effects of N-(4-hydroxyphenyl)retinamide. J. Biol. Chem. 276:2001;45614-45621.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45614-45621
    • Hail, N.1    Lotan, R.2
  • 105
    • 0024350374 scopus 로고
    • Mitochondrial NADH:ubiquinone reductase: Complementary DNA sequence of the import precursor of the bovine 75-kDa subunit
    • Runswick M.J., Gennis R.B., Fearnley I.M., Walker J.E. Mitochondrial NADH:ubiquinone reductase: complementary DNA sequence of the import precursor of the bovine 75-kDa subunit. Biochemistry. 28:1989;9452-9459.
    • (1989) Biochemistry , vol.28 , pp. 9452-9459
    • Runswick, M.J.1    Gennis, R.B.2    Fearnley, I.M.3    Walker, J.E.4
  • 107
    • 0024634879 scopus 로고
    • A homologue of the nuclear coded 49 kd subunit of bovine mitochondrial NADH-ubiquinone reductase is coded in chloroplast DNA
    • Fearnley I.M., Runswick M.J., Walker J.E. A homologue of the nuclear coded 49 kd subunit of bovine mitochondrial NADH-ubiquinone reductase is coded in chloroplast DNA. EMBO J. 8:1989;665-672.
    • (1989) EMBO J. , vol.8 , pp. 665-672
    • Fearnley, I.M.1    Runswick, M.J.2    Walker, J.E.3
  • 108
    • 0025805272 scopus 로고
    • The 30-kilodalton subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA
    • Pilkington S.J., Skehel J.M., Walker J.E. The 30-kilodalton subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA. Biochemistry. 30:1991;1901-1908.
    • (1991) Biochemistry , vol.30 , pp. 1901-1908
    • Pilkington, S.J.1    Skehel, J.M.2    Walker, J.E.3
  • 109
    • 0024559488 scopus 로고
    • Mitochondrial NADH-ubiquinone reductase: Complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit
    • Pilkington S.J., Walker J.E. Mitochondrial NADH-ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit. Biochemistry. 28:1989;3257-3264.
    • (1989) Biochemistry , vol.28 , pp. 3257-3264
    • Pilkington, S.J.1    Walker, J.E.2
  • 110
    • 0024444899 scopus 로고
    • CDNA of the 24 kDa subunit of the bovine respiratory chain NADH dehydrogenase: High sequence conservation in mammals and tissue-specific and growth-dependent expression
    • Chomyn A., Tsai Lai S.S.-A. cDNA of the 24 kDa subunit of the bovine respiratory chain NADH dehydrogenase: high sequence conservation in mammals and tissue-specific and growth-dependent expression. Curr. Genet. 16:1989;117-125.
    • (1989) Curr. Genet. , vol.16 , pp. 117-125
    • Chomyn, A.1    Tsai Lai, S.S.-A.2
  • 111
    • 0026517071 scopus 로고
    • NADH:ubiquinone oxidoreductase from bovine heart mitochondria. A fourth nuclear encoded subunit with a homologue encoded in chloroplast genomes
    • Arizmendi J.M., Runswick M.J., Skehel J.M., Walker J.E. NADH:ubiquinone oxidoreductase from bovine heart mitochondria. A fourth nuclear encoded subunit with a homologue encoded in chloroplast genomes. FEBS Lett. 301:1992;237-242.
    • (1992) FEBS Lett. , vol.301 , pp. 237-242
    • Arizmendi, J.M.1    Runswick, M.J.2    Skehel, J.M.3    Walker, J.E.4
  • 112
    • 0025738723 scopus 로고
    • NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits
    • Fearnley I.M., Finel M., Skehel J.M., Walker J.E. NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits. Biochem. J. 278:1991;821-829.
    • (1991) Biochem. J. , vol.278 , pp. 821-829
    • Fearnley, I.M.1    Finel, M.2    Skehel, J.M.3    Walker, J.E.4
  • 113
    • 0025731633 scopus 로고
    • The amino acid sequences of two 13 kDa polypeptides and partial amino acid sequence of 30 kDa polypeptide of complex I from bovine heart mitochondria: Possible location of iron-sulfur clusters
    • Masui R., Wakabayashi S., Matsubara H., Hatefi Y. The amino acid sequences of two 13 kDa polypeptides and partial amino acid sequence of 30 kDa polypeptide of complex I from bovine heart mitochondria: possible location of iron-sulfur clusters. J. Biochem. 109:1991;534-543.
    • (1991) J. Biochem. , vol.109 , pp. 534-543
    • Masui, R.1    Wakabayashi, S.2    Matsubara, H.3    Hatefi, Y.4
  • 114
    • 0025755811 scopus 로고
    • NADH:ubiquinone oxidoreductase from bovine heart mitochondria: Complementary DNA sequence of the import precursor of the 10 kDa subunit of the flavoprotein fragment
    • Skehel J.M., Pilkington S.J., Runswick M.J., Fearnley I.M., Walker J.E. NADH:ubiquinone oxidoreductase from bovine heart mitochondria: complementary DNA sequence of the import precursor of the 10 kDa subunit of the flavoprotein fragment. FEBS Lett. 282:1991;135-138.
    • (1991) FEBS Lett. , vol.282 , pp. 135-138
    • Skehel, J.M.1    Pilkington, S.J.2    Runswick, M.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 115
    • 0025994347 scopus 로고
    • The amino acid sequence of the 9 kDa polypeptide and partial amino acid sequence of the 20 kDa polypeptide of mitochondrial NADH:ubiquinone oxidoreductase
    • Masui R., Wakabayashi S., Matsubara H., Hatefi Y. The amino acid sequence of the 9 kDa polypeptide and partial amino acid sequence of the 20 kDa polypeptide of mitochondrial NADH:ubiquinone oxidoreductase. J. Biochem. 110:1991;575-582.
    • (1991) J. Biochem. , vol.110 , pp. 575-582
    • Masui, R.1    Wakabayashi, S.2    Matsubara, H.3    Hatefi, Y.4
  • 116
    • 0025915639 scopus 로고
    • NADH:ubiquinone oxidoreductase from bovine mitochondria; CDNA sequence of a 19 kDa cysteine-rich subunit
    • Dupuis A., Skehel J.M., Walker J.E. NADH:ubiquinone oxidoreductase from bovine mitochondria; cDNA sequence of a 19 kDa cysteine-rich subunit. Biochem. J. 277:1991;11-15.
    • (1991) Biochem. J. , vol.277 , pp. 11-15
    • Dupuis, A.1    Skehel, J.M.2    Walker, J.E.3
  • 117
    • 0031765679 scopus 로고    scopus 로고
    • NADH:ubiquinone oxidoreductase from bovine heart mitochondria: Sequence of a novel 17.2-kDa subunit
    • Skehel J.M., Fearnley I.M., Walker J.E. NADH:ubiquinone oxidoreductase from bovine heart mitochondria: sequence of a novel 17.2-kDa subunit. FEBS Lett. 438:1998;301-305.
    • (1998) FEBS Lett. , vol.438 , pp. 301-305
    • Skehel, J.M.1    Fearnley, I.M.2    Walker, J.E.3
  • 118
    • 0026473063 scopus 로고
    • Complementary DNA sequences of two 14.5 kDa subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria; Completion of the primary structure of the enzyme?
    • Arizmendi J.M., Skehel J.M., Runswick M.J., Fearnley I.M., Walker J.E. Complementary DNA sequences of two 14.5 kDa subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria; completion of the primary structure of the enzyme? FEBS Lett. 313:1992;80-84.
    • (1992) FEBS Lett. , vol.313 , pp. 80-84
    • Arizmendi, J.M.1    Skehel, J.M.2    Runswick, M.J.3    Fearnley, I.M.4    Walker, J.E.5
  • 119
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Applications to topology prediction
    • Tusnády G.E., Simon I. Principles governing amino acid composition of integral membrane proteins: applications to topology prediction. J. Mol. Biol. 283:1998;489-506.
    • (1998) J. Mol. Biol. , vol.283 , pp. 489-506
    • Tusnády, G.E.1    Simon, I.2
  • 120
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh A., Larsson B., von Heijne G., Sonnhammer E.L.L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:2001;567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.