메뉴 건너뛰기




Volumn 137, Issue 2, 2005, Pages 447-459

The mitochondrial oxidative phosphorylation proteome of Chlamydomonas reinhardtii deduced from the genome sequencing project

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDOMONAS REINHARDTII;

EID: 19044375107     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.104.054148     Document Type: Review
Times cited : (68)

References (111)
  • 2
    • 0028114231 scopus 로고
    • Structure at 2.8 a resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams JP, Leslie AG, Lutter R, Walker JE (1994) Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621-628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 3
    • 0025357629 scopus 로고
    • ATP 10, a yeast nuclear gene required for the assembly of the mitochondrial F1-F0 complex
    • Ackerman SH, Tzagoloff A (1990a) ATP 10, a yeast nuclear gene required for the assembly of the mitochondrial F1-F0 complex. J Biol Chem 265: 9952-9959
    • (1990) J Biol Chem , vol.265 , pp. 9952-9959
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 4
    • 0025350272 scopus 로고
    • Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase
    • USA
    • Ackerman SH, Tzagoloff A (1990b) Identification of two nuclear genes (ATP11, ATP12) required for assembly of the yeast F1-ATPase. Proc Natl Acad Sci USA 87: 4986-4990
    • (1990) Proc Natl Acad Sci , vol.87 , pp. 4986-4990
    • Ackerman, S.H.1    Tzagoloff, A.2
  • 5
    • 0024220124 scopus 로고
    • cDNA and deduced amino acid sequences of cytochrome c from Chlamydomonas reinhardtii: Unexpected functional and phylogenetic implications
    • Amati BB, Goldschmidt-Clermont M, Wallace CJ, Rochaix JD (1988) cDNA and deduced amino acid sequences of cytochrome c from Chlamydomonas reinhardtii: unexpected functional and phylogenetic implications. J Mol Evol 28: 151-160
    • (1988) J Mol Evol , vol.28 , pp. 151-160
    • Amati, B.B.1    Goldschmidt-Clermont, M.2    Wallace, C.J.3    Rochaix, J.D.4
  • 7
    • 0028158405 scopus 로고
    • Identification of mitochondrial respiratory proteins from the green alga Chlamydomonas reinhardtii
    • Atteia A (1994) Identification of mitochondrial respiratory proteins from the green alga Chlamydomonas reinhardtii. C R Acad Sci III 317: 11-19
    • (1994) C R Acad Sci III , vol.317 , pp. 11-19
    • Atteia, A.1
  • 8
    • 0037293953 scopus 로고    scopus 로고
    • Structure, organization and expression of the genes encoding mitochondrial cytochrome c(1) and the Rieske iron-sulfur protein in Chlamydomonas reinhardtii
    • Atteia A, van Lis R, Wetterskog D, Gutierrez-Cirlos EB, Ongay-Larios L, Franzen LG, Gonzalez-Halphen D (2003) Structure, organization and expression of the genes encoding mitochondrial cytochrome c(1) and the Rieske iron-sulfur protein in Chlamydomonas reinhardtii. Mol Genet Genomics 268: 637-644
    • (2003) Mol Genet Genomics , vol.268 , pp. 637-644
    • Atteia, A.1    Van Lis, R.2    Wetterskog, D.3    Gutierrez-Cirlos, E.B.4    Ongay-Larios, L.5    Franzen, L.G.6    Gonzalez-Halphen, D.7
  • 9
    • 0037080769 scopus 로고    scopus 로고
    • Shy1p is necessary for full expression of mitochondrial COX1 in the yeast model of Leigh's syndrome
    • Barrientos A, Korr D, Tzagoloff A (2002) Shy1p is necessary for full expression of mitochondrial COX1 in the yeast model of Leigh's syndrome. EMBO J 21: 43-52
    • (2002) EMBO J , vol.21 , pp. 43-52
    • Barrientos, A.1    Korr, D.2    Tzagoloff, A.3
  • 10
    • 4644319049 scopus 로고    scopus 로고
    • Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae
    • Barrientos A, Zambrano A, Tzagoloff A (2004) Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae. EMBO J 23: 3472-3482
    • (2004) EMBO J , vol.23 , pp. 3472-3482
    • Barrientos, A.1    Zambrano, A.2    Tzagoloff, A.3
  • 11
    • 3843110146 scopus 로고    scopus 로고
    • COX23, a homologue of COX17, is required for cytochrome oxidase assembly
    • Barros MH, Johnson A, Tzagoloff A (2004) COX23, a homologue of COX17, is required for cytochrome oxidase assembly. J Biol Chem 279: 31943-31947
    • (2004) J Biol Chem , vol.279 , pp. 31943-31947
    • Barros, M.H.1    Johnson, A.2    Tzagoloff, A.3
  • 12
    • 0037051889 scopus 로고    scopus 로고
    • Regulation of the heme: A biosynthetic pathway in Saccharomyces cerevisiae
    • Barros MH, Tzagoloff A (2002) Regulation of the heme: a biosynthetic pathway in Saccharomyces cerevisiae. FEBS Lett 516: 119-123
    • (2002) FEBS Lett , vol.516 , pp. 119-123
    • Barros, M.H.1    Tzagoloff, A.2
  • 13
    • 0037353428 scopus 로고    scopus 로고
    • Regulation of the alternative oxidase Aox1 gene in Chlamydomonas reinhardtii: Role of the nitrogen source on the expression of a reporter gene under the control of the Aox1 promoter
    • Baurain D, Dinant M, Coosemans N, Matagne RF (2003) Regulation of the alternative oxidase Aox1 gene in Chlamydomonas reinhardtii: role of the nitrogen source on the expression of a reporter gene under the control of the Aox1 promoter. Plant Physiol 131: 1418-1430
    • (2003) Plant Physiol , vol.131 , pp. 1418-1430
    • Baurain, D.1    Dinant, M.2    Coosemans, N.3    Matagne, R.F.4
  • 15
    • 0025886262 scopus 로고
    • ABC1, a novel yeast nuclear gene has a dual function in mitochondria: It suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex
    • Bousquet I, Dujardin G, Slonimski PP (1991) ABC1, a novel yeast nuclear gene has a dual function in mitochondria: It suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex. EMBO J 10: 2023-2031
    • (1991) EMBO J , vol.10 , pp. 2023-2031
    • Bousquet, I.1    Dujardin, G.2    Slonimski, P.P.3
  • 16
    • 0027416392 scopus 로고
    • The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex
    • Brandt U, Yu L, Yu CA, Trumpower BL (1993) The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex. J Biol Chem 268: 8387-8390
    • (1993) J Biol Chem , vol.268 , pp. 8387-8390
    • Brandt, U.1    Yu, L.2    Yu, C.A.3    Trumpower, B.L.4
  • 17
    • 0028857080 scopus 로고
    • The bifunctional cytochrome c reductase/ processing peptidase complex from plant mitochondria
    • Braun HP, Schmitz UK (1995) 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
  • 18
    • 0034780497 scopus 로고    scopus 로고
    • Peripheral mitochondrial inner membrane protein, Mss2p, required for export of the mitochondrially coded Cox2p C tail in Saccharomyces cerevisiae
    • Broadley SA, Demlow CM, Fox TD (2001) Peripheral mitochondrial inner membrane protein, Mss2p, required for export of the mitochondrially coded Cox2p C tail in Saccharomyces cerevisiae. Mol Cell Biol 21: 7663-7672
    • (2001) Mol Cell Biol , vol.21 , pp. 7663-7672
    • Broadley, S.A.1    Demlow, C.M.2    Fox, T.D.3
  • 19
    • 0036304765 scopus 로고    scopus 로고
    • Impact of mutations affecting ND mitochondria-encoded subunits on the activity and assembly of complex I in Chlamydomonas: Implication for the structural organization of the enzyme
    • Cardol P, Matagne RF, Remacle C (2002) Impact of mutations affecting ND mitochondria-encoded subunits on the activity and assembly of complex I in Chlamydomonas: implication for the structural organization of the enzyme. J Mol Biol 319: 1211-1221
    • (2002) J Mol Biol , vol.319 , pp. 1211-1221
    • Cardol, P.1    Matagne, R.F.2    Remacle, C.3
  • 20
    • 4644250423 scopus 로고    scopus 로고
    • Higher plant-like subunit composition of the mitochondrial complex I from Chlamydomonas reinhardtii: 31 conserved components among eukaryotes
    • Cardol P, Vanrobaeys F, Devreese B, Van Beeumen J, Matagne R, Remacle C (2004) Higher plant-like subunit composition of the mitochondrial complex I from Chlamydomonas reinhardtii: 31 conserved components among eukaryotes. Biochim Biophys Acta 1658: 212-214
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 212-214
    • Cardol, P.1    Vanrobaeys, F.2    Devreese, B.3    Van Beeumen, J.4    Matagne, R.5    Remacle, C.6
  • 21
    • 0037423199 scopus 로고    scopus 로고
    • COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae
    • Carlson CG, Barrientos A, Tzagoloff A, Glerum DM (2003) COX16 encodes a novel protein required for the assembly of cytochrome oxidase in Saccharomyces cerevisiae. J Biol Chem 278: 3770-3775
    • (2003) J Biol Chem , vol.278 , pp. 3770-3775
    • Carlson, C.G.1    Barrientos, A.2    Tzagoloff, A.3    Glerum, D.M.4
  • 23
    • 0027932892 scopus 로고
    • Characterization of CBP4, a new gene essential for the expression of ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae
    • Crivellone MD (1994) Characterization of CBP4, a new gene essential for the expression of ubiquinol-cytochrome c reductase in Saccharomyces cerevisiae. J Biol Chem 269: 21284-21292
    • (1994) J Biol Chem , vol.269 , pp. 21284-21292
    • Crivellone, M.D.1
  • 24
    • 0033214782 scopus 로고    scopus 로고
    • Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex
    • Cruciat CM, Hell K, Folsch H, Neupert W, Stuart RA (1999) Bcs1p, an AAA-family member, is a chaperone for the assembly of the cytochrome bc(1) complex. EMBO J 18: 5226-5233
    • (1999) EMBO J , vol.18 , pp. 5226-5233
    • Cruciat, C.M.1    Hell, K.2    Folsch, H.3    Neupert, W.4    Stuart, R.A.5
  • 25
    • 0036678103 scopus 로고    scopus 로고
    • Intracellular gene transfer: Reduced hydrophobicity facilitates gene transfer for subunit 2 of cytochrome c oxidase
    • USA
    • Daley DO, Clifton R, Whelan J (2002) Intracellular gene transfer: Reduced hydrophobicity facilitates gene transfer for subunit 2 of cytochrome c oxidase. Proc Natl Acad Sci USA 99: 10510-10515
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 10510-10515
    • Daley, D.O.1    Clifton, R.2    Whelan, J.3
  • 26
    • 0033610793 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II)
    • Dibrov E, Fu S, Lemire BD (1998) The Saccharomyces cerevisiae TCM62 gene encodes a chaperone necessary for the assembly of the mitochondrial succinate dehydrogenase (complex II). J Biol Chem 273: 32042-32048
    • (1998) J Biol Chem , vol.273 , pp. 32042-32048
    • Dibrov, E.1    Fu, S.2    Lemire, B.D.3
  • 27
    • 0020320758 scopus 로고
    • Identification and cloning of a yeast nuclear gene (CBP1) involved in expression of mitochondrial cytochrome b
    • USA
    • Dieckmann CL, Pape LK, Tzagoloff A (1982) Identification and cloning of a yeast nuclear gene (CBP1) involved in expression of mitochondrial cytochrome b. Proc Natl Acad Sci USA 79: 1805-1809
    • (1982) Proc Natl Acad Sci , vol.79 , pp. 1805-1809
    • Dieckmann, C.L.1    Pape, L.K.2    Tzagoloff, A.3
  • 28
    • 0021913292 scopus 로고
    • Assembly of the mitochondrial membrane system: CBP6, a yeast nuclear gene necessary for synthesis of cytochrome b
    • Dieckmann CL, Tzagoloff A (1985) Assembly of the mitochondrial membrane system: CBP6, a yeast nuclear gene necessary for synthesis of cytochrome b. J Biol Chem 260: 1513-1520
    • (1985) J Biol Chem , vol.260 , pp. 1513-1520
    • Dieckmann, C.L.1    Tzagoloff, A.2
  • 29
    • 0035013011 scopus 로고    scopus 로고
    • Characterization of two genes encoding the mitochondrial alternative oxidase in Chlamydomonas reinhardtii
    • Dinant M, Baurain D, Coosemans N, Joris B, Matagne RF (2001) Characterization of two genes encoding the mitochondrial alternative oxidase in Chlamydomonas reinhardtii. Curr Genet 39: 101-108
    • (2001) Curr Genet , vol.39 , pp. 101-108
    • Dinant, M.1    Baurain, D.2    Coosemans, N.3    Joris, B.4    Matagne, R.F.5
  • 31
    • 1942533644 scopus 로고    scopus 로고
    • Aep3p stabilizes the mitochondrial bicistronic mRNA encoding subunits 6 and 8 of the H+-translocating ATP synthase of Saccharomyces cerevisiae
    • Ellis TP, Helfenbein KG, Tzagoloff A, Dieckmann CL (2004) Aep3p stabilizes the mitochondrial bicistronic mRNA encoding subunits 6 and 8 of the H+-translocating ATP synthase of Saccharomyces cerevisiae. J Biol Chem 279: 15728-15733
    • (2004) J Biol Chem , vol.279 , pp. 15728-15733
    • Ellis, T.P.1    Helfenbein, K.G.2    Tzagoloff, A.3    Dieckmann, C.L.4
  • 32
    • 0029110550 scopus 로고
    • Isolation, purification and characterization of mitochondria from Chlamydomonas reinhardtii
    • Eriksson M, Gardestrom P, Samuelsson G (1995) Isolation, purification and characterization of mitochondria from Chlamydomonas reinhardtii. Plant Physiol 107: 479-483
    • (1995) Plant Physiol , vol.107 , pp. 479-483
    • Eriksson, M.1    Gardestrom, P.2    Samuelsson, G.3
  • 33
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria: Supercomplexes and a unique composition of complex II
    • Eubel H, Jansch L, Braun HP (2003) New insights into the respiratory chain of plant mitochondria: supercomplexes and a unique composition of complex II. Plant Physiol 133: 274-286
    • (2003) Plant Physiol , vol.133 , pp. 274-286
    • Eubel, H.1    Jansch, L.2    Braun, H.P.3
  • 34
    • 0035986910 scopus 로고    scopus 로고
    • Mitochondrial genome of the colorless green alga Polytomella parva: Two linear DNA molecules with homologous inverted repeat Termini
    • Fan J, Lee RW (2002) Mitochondrial genome of the colorless green alga Polytomella parva: two linear DNA molecules with homologous inverted repeat Termini. Mol Biol Evol 19: 999-1007
    • (2002) Mol Biol Evol , vol.19 , pp. 999-1007
    • Fan, J.1    Lee, R.W.2
  • 35
    • 0029086227 scopus 로고
    • The mature AEP2 gene product of Saccharomyces cerevisiae, required for the expression of subunit 9 of ATP synthase, is a 58 kDa mitochondrial protein
    • Finnegan PM, Ellis TP, Nagley P, Lukins HB (1995) The mature AEP2 gene product of Saccharomyces cerevisiae, required for the expression of subunit 9 of ATP synthase, is a 58 kDa mitochondrial protein. FEBS Lett 368: 505-508
    • (1995) FEBS Lett , vol.368 , pp. 505-508
    • Finnegan, P.M.1    Ellis, T.P.2    Nagley, P.3    Lukins, H.B.4
  • 36
    • 0034870789 scopus 로고    scopus 로고
    • Structure and function of Pet100p, a molecular chaperone required for the assembly of cytochrome c oxidase in Saccharomyces cerevisiae
    • Forsha D, Church C, Wazny P, Poyton RO (2001) Structure and function of Pet100p, a molecular chaperone required for the assembly of cytochrome c oxidase in Saccharomyces cerevisiae. Biochem Soc Trans 29: 436-441
    • (2001) Biochem Soc Trans , vol.29 , pp. 436-441
    • Forsha, D.1    Church, C.2    Wazny, P.3    Poyton, R.O.4
  • 39
    • 1642423514 scopus 로고    scopus 로고
    • The Oxa2 protein of Neurospora crassa plays a critical role in the biogenesis of cytochrome oxidase and defines a ubiquitous subbranch of the Oxa1/YidC/Alb3 protein family
    • Funes S, Nargang FE, Neupert W, Herrmann JM (2004) The Oxa2 protein of Neurospora crassa plays a critical role in the biogenesis of cytochrome oxidase and defines a ubiquitous subbranch of the Oxa1/YidC/Alb3 protein family. Mol Biol Cell 15: 1853-1861
    • (2004) Mol Biol Cell , vol.15 , pp. 1853-1861
    • Funes, S.1    Nargang, F.E.2    Neupert, W.3    Herrmann, J.M.4
  • 40
    • 0032738979 scopus 로고    scopus 로고
    • Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants
    • Glaser E, Dessi P (1999) Integration of the mitochondrial-processing peptidase into the cytochrome bc1 complex in plants. J Bioenerg Biomembr 31: 259-274
    • (1999) J Bioenerg Biomembr , vol.31 , pp. 259-274
    • Glaser, E.1    Dessi, P.2
  • 41
    • 0028038276 scopus 로고
    • Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant
    • USA
    • Glerum DM, Tzagoloff A (1994) Isolation of a human cDNA for heme A:farnesyltransferase by functional complementation of a yeast cox10 mutant. Proc Natl Acad Sci USA 91: 8452-8456
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 8452-8456
    • Glerum, D.M.1    Tzagoloff, A.2
  • 43
    • 0024300787 scopus 로고
    • Organization and expression of algal (Chlamydomonas reinhardtii) mitochondrial DNA
    • Gray MW, Boer PH (1988) Organization and expression of algal (Chlamydomonas reinhardtii) mitochondrial DNA. Philos Trans R Soc Lond B Biol Sci 319: 135-147
    • (1988) Philos Trans R Soc Lond B Biol Sci , vol.319 , pp. 135-147
    • Gray, M.W.1    Boer, P.H.2
  • 44
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • Gray MW, Burger G, Lang BF (1999) Mitochondrial evolution. Science 283: 1476-1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 45
    • 0033149979 scopus 로고    scopus 로고
    • Identification of cDNA encoding cytochrome c oxidase subunit 5c (COX5c) from rice: Comparison of its expression with nuclear-encoded and mitochondrial-encoded COX genes
    • Hamanaka S, Ohtsu K, Kadowaki K, Nakazono M, Hirai A (1999) Identification of cDNA encoding cytochrome c oxidase subunit 5c (COX5c) from rice: comparison of its expression with nuclear-encoded and mitochondrial- encoded COX genes. Genes Genet Syst 74: 71-75
    • (1999) Genes Genet Syst , vol.74 , pp. 71-75
    • Hamanaka, S.1    Ohtsu, K.2    Kadowaki, K.3    Nakazono, M.4    Hirai, A.5
  • 46
    • 0018337615 scopus 로고
    • Proteins, polypeptides, prosthetic groups, and enzymic properties of complexes I, II, III, IV, and V of the mitochondrial oxidative phosphorylation system
    • Hatefi Y, Galante YM, Stiggall DL, Ragan CI (1979) Proteins, polypeptides, prosthetic groups, and enzymic properties of complexes I, II, III, IV, and V of the mitochondrial oxidative phosphorylation system. Methods Enzymol 56: 577-602
    • (1979) Methods Enzymol , vol.56 , pp. 577-602
    • Hatefi, Y.1    Galante, Y.M.2    Stiggall, D.L.3    Ragan, C.I.4
  • 47
    • 0030952628 scopus 로고    scopus 로고
    • Membrane translocation of mitochondrially coded Cox2p: Distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p
    • He S, Fox TD (1997) Membrane translocation of mitochondrially coded Cox2p: distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p. Mol Biol Cell 8: 1449-1460
    • (1997) Mol Biol Cell , vol.8 , pp. 1449-1460
    • He, S.1    Fox, T.D.2
  • 48
    • 0038433229 scopus 로고    scopus 로고
    • Mitochondrial complex I from Arabidopsis and rice: Orthologs of mammalian and fungal components coupled with plant-specific subunits
    • Heazlewood JL, Howell KA, Millar AH (2003a) Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits. Biochim Biophys Acta 1604: 159-169
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 159-169
    • Heazlewood, J.L.1    Howell, K.A.2    Millar, A.H.3
  • 49
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • Heazlewood JL, Tonti-Filippini JS, Gout AM, Day DA, Whelan J, Millar AH (2004) Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins. Plant Cell 16: 241-256
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 50
    • 0037430978 scopus 로고    scopus 로고
    • The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase
    • Heazlewood JL, Whelan J, Millar AH (2003b) The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase. FEBS Lett 540: 201-205
    • (2003) FEBS Lett , vol.540 , pp. 201-205
    • Heazlewood, J.L.1    Whelan, J.2    Millar, A.H.3
  • 51
    • 0038165486 scopus 로고    scopus 로고
    • ATP22, a nuclear gene required for expression of the F0 sector of mitochondrial ATPase in Saccharomyces cerevisiae
    • Helfenbein KG, Ellis TP, Dieckmann CL, Tzagoloff A (2003) ATP22, a nuclear gene required for expression of the F0 sector of mitochondrial ATPase in Saccharomyces cerevisiae. J Biol Chem 278: 19751-19756
    • (2003) J Biol Chem , vol.278 , pp. 19751-19756
    • Helfenbein, K.G.1    Ellis, T.P.2    Dieckmann, C.L.3    Tzagoloff, A.4
  • 52
    • 0034681389 scopus 로고    scopus 로고
    • Identification of Cox20p, a novel protein involved in the maturation and assembly of cytochrome oxidase subunit 2
    • Hell K, Tzagoloff A, Neupert W, Stuart RA (2000) Identification of Cox20p, a novel protein involved in the maturation and assembly of cytochrome oxidase subunit 2. J Biol Chem 275: 4571-4578
    • (2000) J Biol Chem , vol.275 , pp. 4571-4578
    • Hell, K.1    Tzagoloff, A.2    Neupert, W.3    Stuart, R.A.4
  • 54
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase
    • Horng YC, Cobine PA, Maxfield AB, Carr HS, Winge DR (2004) Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. J Biol Chem 279: 35334-35340
    • (2004) J Biol Chem , vol.279 , pp. 35334-35340
    • Horng, Y.C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 56
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jansch L, Kruft V, Schmitz UK, Braun HP (1996) New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J 9: 357-368
    • (1996) Plant J , vol.9 , pp. 357-368
    • Jansch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 57
    • 0036523991 scopus 로고    scopus 로고
    • CIA30 complex I assembly factor: A candidate for human complex I deficiency?
    • Janssen R, Smeitink J, Smeets R, van Den Heuvel L (2002) CIA30 complex I assembly factor: a candidate for human complex I deficiency? Hum Genet 110: 264-270
    • (2002) Hum Genet , vol.110 , pp. 264-270
    • Janssen, R.1    Smeitink, J.2    Smeets, R.3    Van Den Heuvel, L.4
  • 60
    • 0034737796 scopus 로고    scopus 로고
    • The chaperonin-related protein Tcm62p ensures mitochondrial gene expression under heat stress
    • Klanner C, Neupert W, Langer T (2000) The chaperonin-related protein Tcm62p ensures mitochondrial gene expression under heat stress. FEBS Lett 470: 365-369
    • (2000) FEBS Lett , vol.470 , pp. 365-369
    • Klanner, C.1    Neupert, W.2    Langer, T.3
  • 61
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz R, Lill R, Goldman B, Bonnard G, Merchant S (1998) Molecular mechanisms of cytochrome c biogenesis: three distinct systems. Mol Microbiol 29: 383-396
    • (1998) Mol Microbiol , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 62
    • 0032561134 scopus 로고    scopus 로고
    • Involvement of two novel chaperones in the assembly of mitochondrial NADH: Ubiquinone oxidoreductase (complex I)
    • Kuffner R, Rohr A, Schmiede A, Krull C, Schulte U (1998) Involvement of two novel chaperones in the assembly of mitochondrial NADH: Ubiquinone oxidoreductase (complex I). J Mol Biol 283: 409-417
    • (1998) J Mol Biol , vol.283 , pp. 409-417
    • Kuffner, R.1    Rohr, A.2    Schmiede, A.3    Krull, C.4    Schulte, U.5
  • 63
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 64
    • 0037022594 scopus 로고    scopus 로고
    • Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c
    • USA
    • Lange C, Hunte C (2002) Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c. Proc Natl Acad Sci USA 99: 2800-2805
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 2800-2805
    • Lange, C.1    Hunte, C.2
  • 66
    • 0035794147 scopus 로고    scopus 로고
    • Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions
    • Lefebvre-Legendre L, Vaillier J, Benabdelhak H, Velours J, Slonimski PP, di Rago JP (2001) Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions. J Biol Chem 276: 6789-6796
    • (2001) J Biol Chem , vol.276 , pp. 6789-6796
    • Lefebvre-Legendre, L.1    Vaillier, J.2    Benabdelhak, H.3    Velours, J.4    Slonimski, P.P.5    Di Rago, J.P.6
  • 67
    • 0037122946 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase
    • Lemire BD, Oyedotun KS (2002) The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase. Biochim Biophys Acta 1553: 102-116
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 102-116
    • Lemire, B.D.1    Oyedotun, K.S.2
  • 68
    • 0023197942 scopus 로고
    • Purification of highly active cytochrome bc1 complexes from phylogenetically diverse species by a single chromatographic procedure
    • Ljungdahl PO, Pennoyer JD, Robertson DE, Trumpower BL (1987) Purification of highly active cytochrome bc1 complexes from phylogenetically diverse species by a single chromatographic procedure. Biochim Biophys Acta 891: 227-241
    • (1987) Biochim Biophys Acta , vol.891 , pp. 227-241
    • Ljungdahl, P.O.1    Pennoyer, J.D.2    Robertson, D.E.3    Trumpower, B.L.4
  • 69
    • 0034872201 scopus 로고    scopus 로고
    • Chlamydomonas nuclear mutants that fail to assemble respiratory or photosynthetic electron transfer complexes
    • Lown FJ, Watson AT, Purton S (2001) Chlamydomonas nuclear mutants that fail to assemble respiratory or photosynthetic electron transfer complexes. Biochem Soc Trans 29: 452-455
    • (2001) Biochem Soc Trans , vol.29 , pp. 452-455
    • Lown, F.J.1    Watson, A.T.2    Purton, S.3
  • 70
    • 0032544505 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH
    • Luttik MA, Overkamp KM, Kotter P, de Vries S, van Dijken JF, Pronk JT (1998) The Saccharomyces cerevisiae NDE1 and NDE2 genes encode separate mitochondrial NADH dehydrogenases catalyzing the oxidation of cytosolic NADH. J Biol Chem 273: 24529-24534
    • (1998) J Biol Chem , vol.273 , pp. 24529-24534
    • Luttik, M.A.1    Overkamp, K.M.2    Kotter, P.3    De Vries, S.4    Van Dijken, J.F.5    Pronk, J.T.6
  • 71
    • 0026089901 scopus 로고
    • Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: Ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae
    • Marres CA, de Vries S, Grivell LA (1991) Isolation and inactivation of the nuclear gene encoding the rotenone-insensitive internal NADH: ubiquinone oxidoreductase of mitochondria from Saccharomyces cerevisiae. Eur J Biochem 195: 857-862
    • (1991) Eur J Biochem , vol.195 , pp. 857-862
    • Marres, C.A.1    De Vries, S.2    Grivell, L.A.3
  • 72
    • 2642689666 scopus 로고    scopus 로고
    • The hydrogen hypothesis for the first eukaryote
    • Martin W, Muller M (1998) The hydrogen hypothesis for the first eukaryote. Nature 392: 37-41
    • (1998) Nature , vol.392 , pp. 37-41
    • Martin, W.1    Muller, M.2
  • 73
    • 0024652878 scopus 로고
    • Induction and characterization of mitochondrial DNA mutants in Chlamydomonas reinhardtii
    • Matagne RF, Michel-Wolwertz MR, Munaut C, Duyckaerts C, Sluse F (1989) Induction and characterization of mitochondrial DNA mutants in Chlamydomonas reinhardtii. J Cell Biol 108: 1221-1226
    • (1989) J Cell Biol , vol.108 , pp. 1221-1226
    • Matagne, R.F.1    Michel-Wolwertz, M.R.2    Munaut, C.3    Duyckaerts, C.4    Sluse, F.5
  • 74
    • 0033529335 scopus 로고    scopus 로고
    • The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells
    • USA
    • Maxwell DP, Wang Y, McIntosh L (1999) The alternative oxidase lowers mitochondrial reactive oxygen production in plant cells. Proc Natl Acad Sci USA 96: 8271-8276
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 8271-8276
    • Maxwell, D.P.1    Wang, Y.2    McIntosh, L.3
  • 75
    • 0027434536 scopus 로고
    • Sequence and chromosomal localization of two PET genes required for cytochrome c oxidase assembly in Saccharomyces cerevisiae
    • McEwen JE, Hong KH, Park S, Preciado GT (1993) Sequence and chromosomal localization of two PET genes required for cytochrome c oxidase assembly in Saccharomyces cerevisiae. Curr Genet 23: 9-14
    • (1993) Curr Genet , vol.23 , pp. 9-14
    • McEwen, J.E.1    Hong, K.H.2    Park, S.3    Preciado, G.T.4
  • 76
    • 0021099817 scopus 로고
    • Assembly of the mitochondrial membrane system: Characterization of a yeast nuclear gene involved in the processing of the cytochrome b pre-mRNA
    • McGraw P, Tzagoloff A (1983) Assembly of the mitochondrial membrane system: characterization of a yeast nuclear gene involved in the processing of the cytochrome b pre-mRNA. J Biol Chem 258: 9459-9468
    • (1983) J Biol Chem , vol.258 , pp. 9459-9468
    • McGraw, P.1    Tzagoloff, A.2
  • 77
    • 0025096489 scopus 로고
    • Mitochondrial DNA of Chlamydomonas reinhardtii: The gene for apocytochrome b and the complete functional map of the 15.8 kb DNA
    • Michaelis G, Vahrenholz C, Pratje E (1990) Mitochondrial DNA of Chlamydomonas reinhardtii: the gene for apocytochrome b and the complete functional map of the 15.8 kb DNA. Mol Gen Genet 223: 211-216
    • (1990) Mol Gen Genet , vol.223 , pp. 211-216
    • Michaelis, G.1    Vahrenholz, C.2    Pratje, E.3
  • 78
  • 80
    • 0037238395 scopus 로고    scopus 로고
    • Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae
    • Naithani S, Saracco SA, Butler CA, Fox TD (2003) Interactions among COX1, COX2, and COX3 mRNA-specific translational activator proteins on the inner surface of the mitochondrial inner membrane of Saccharomyces cerevisiae. Mol Biol Cell 14: 324-333
    • (2003) Mol Biol Cell , vol.14 , pp. 324-333
    • Naithani, S.1    Saracco, S.A.2    Butler, C.A.3    Fox, T.D.4
  • 81
    • 0026702012 scopus 로고
    • BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae
    • Nobrega FG, Nobrega MP, Tzagoloff A (1992) BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae. EMBO J 11: 3821-3829
    • (1992) EMBO J , vol.11 , pp. 3821-3829
    • Nobrega, F.G.1    Nobrega, M.P.2    Tzagoloff, A.3
  • 82
    • 0037174842 scopus 로고    scopus 로고
    • Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase
    • Nobrega MP, Bandeira SC, Beers J, Tzagoloff A (2002) Characterization of COX19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase. J Biol Chem 277: 40206-40211
    • (2002) J Biol Chem , vol.277 , pp. 40206-40211
    • Nobrega, M.P.1    Bandeira, S.C.2    Beers, J.3    Tzagoloff, A.4
  • 83
    • 0030237421 scopus 로고    scopus 로고
    • Isolation and characterization of the mitochondrial ATP synthase from Chlamydomonas reinhardtii: CDNA sequence and deduced protein sequence of the alpha subunit
    • Nurani G, Franzen LG (1996) Isolation and characterization of the mitochondrial ATP synthase from Chlamydomonas reinhardtii: cDNA sequence and deduced protein sequence of the alpha subunit. Plant Mol Biol 31: 1105-1116
    • (1996) Plant Mol Biol , vol.31 , pp. 1105-1116
    • Nurani, G.1    Franzen, L.G.2
  • 85
    • 0025818601 scopus 로고
    • Properties of two nuclear pet mutants affecting expression of the mitochondrial olil gene of Saccharomyces cerevisiae
    • Payne MJ, Schweizer E, Lukins HB (1991) Properties of two nuclear pet mutants affecting expression of the mitochondrial olil gene of Saccharomyces cerevisiae. Curr Genet 19: 343-351
    • (1991) Curr Genet , vol.19 , pp. 343-351
    • Payne, M.J.1    Schweizer, E.2    Lukins, H.B.3
  • 87
    • 0036648834 scopus 로고    scopus 로고
    • Characterization of oxidative phosphorylation in the colorless chlorophyte Polytomella sp.: Its mitochondrial respiratory chain lacks a plant-like alternative oxidase
    • Reyes-Prieto A, El-Hafidi M, Moreno-Sanchez R, Gonzalez-Halphen D (2002) Characterization of oxidative phosphorylation in the colorless chlorophyte Polytomella sp.: Its mitochondrial respiratory chain lacks a plant-like alternative oxidase. Biochim Biophys Acta 1554: 170-179
    • (2002) Biochim Biophys Acta , vol.1554 , pp. 170-179
    • Reyes-Prieto, A.1    El-Hafidi, M.2    Moreno-Sanchez, R.3    Gonzalez-Halphen, D.4
  • 88
    • 0038015611 scopus 로고    scopus 로고
    • Evolutionary diversification of mitochondrial proteomes: Implications for human disease
    • Richly E, Chinnery PF, Leister D (2003) Evolutionary diversification of mitochondrial proteomes: implications for human disease. Trends Genet 19: 356-362
    • (2003) Trends Genet , vol.19 , pp. 356-362
    • Richly, E.1    Chinnery, P.F.2    Leister, D.3
  • 89
    • 0026068070 scopus 로고
    • The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: Primary structure of subunit V from the slime mold Dictyostelium discoideum
    • Rizzuto R, Sandona D, Brini M, Capaldi RA, Bisson R (1991) The most conserved nuclear-encoded polypeptide of cytochrome c oxidase is the putative zinc-binding subunit: primary structure of subunit V from the slime mold Dictyostelium discoideum. Biochim Biophys Acta 1129: 100-104
    • (1991) Biochim Biophys Acta , vol.1129 , pp. 100-104
    • Rizzuto, R.1    Sandona, D.2    Brini, M.3    Capaldi, R.A.4    Bisson, R.5
  • 90
    • 0022885377 scopus 로고
    • Two yeast nuclear genes, CBS1 and CBS2, are required for translation of mitochondrial transcripts bearing the 5′-untranslated COB leader
    • Rodel G (1986) Two yeast nuclear genes, CBS1 and CBS2, are required for translation of mitochondrial transcripts bearing the 5′-untranslated COB leader. Curr Genet 11: 41-45
    • (1986) Curr Genet , vol.11 , pp. 41-45
    • Rodel, G.1
  • 91
    • 0036223216 scopus 로고    scopus 로고
    • Cox18p is required for export of the mitochondrially encoded Saccharomyces cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner membrane
    • Saracco SA, Fox TD (2002) Cox18p is required for export of the mitochondrially encoded Saccharomyces cerevisiae Cox2p C-tail and interacts with Pnt1p and Mss2p in the inner membrane. Mol Biol Cell 13: 1122-1131
    • (2002) Mol Biol Cell , vol.13 , pp. 1122-1131
    • Saracco, S.A.1    Fox, T.D.2
  • 92
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger H, Pfeiffer K (2000) Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J 19: 1777-1783
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 93
    • 0037625091 scopus 로고    scopus 로고
    • Gene products present in mitochondria of yeast and animal cells
    • L Wilson, P Matsudaira, eds, Academic Press, San Diego
    • Schon EA (2001) Gene products present in mitochondria of yeast and animal cells. In L Wilson, P Matsudaira, eds, Mitochondria. Academic Press, San Diego, pp 463-482
    • (2001) Mitochondria , pp. 463-482
    • Schon, E.A.1
  • 94
    • 0035903029 scopus 로고    scopus 로고
    • Identification of functional regions of Cbp3p, an enzyme-specific chaperone required for the assembly of ubiquinol-cytochrome c reductase in yeast mitochondria
    • Shi G, Crivellone MD, Edderkaoui B (2001) Identification of functional regions of Cbp3p, an enzyme-specific chaperone required for the assembly of ubiquinol-cytochrome c reductase in yeast mitochondria. Biochim Biophys Acta 1506: 103-116
    • (2001) Biochim Biophys Acta , vol.1506 , pp. 103-116
    • Shi, G.1    Crivellone, M.D.2    Edderkaoui, B.3
  • 96
    • 0033607504 scopus 로고    scopus 로고
    • Molecular architecture of the rotary motor in ATP synthase
    • Stock D, Leslie AG, Walker JE (1999) Molecular architecture of the rotary motor in ATP synthase. Science 286: 1700-1705
    • (1999) Science , vol.286 , pp. 1700-1705
    • Stock, D.1    Leslie, A.G.2    Walker, J.E.3
  • 97
    • 0026591885 scopus 로고
    • Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme
    • Taanman JW, Capaldi RA (1992) Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme. J Biol Chem 267: 22481-22485
    • (1992) J Biol Chem , vol.267 , pp. 22481-22485
    • Taanman, J.W.1    Capaldi, R.A.2
  • 98
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 99
    • 0038645365 scopus 로고    scopus 로고
    • The role of mitochondria in the life of the nematode, Caenorhabditis elegans
    • Tsang WY, Lemire BD (2003) The role of mitochondria in the life of the nematode, Caenorhabditis elegans. Biochim Biophys Acta 1638: 91-105
    • (2003) Biochim Biophys Acta , vol.1638 , pp. 91-105
    • Tsang, W.Y.1    Lemire, B.D.2
  • 101
    • 2442489927 scopus 로고    scopus 로고
    • Atp10p assists assembly of Atp6p into the F0 unit of the yeast mitochondrial ATPase
    • Tzagoloff A, Barrientos A, Neupert W, Herrmann JM (2004) Atp10p assists assembly of Atp6p into the F0 unit of the yeast mitochondrial ATPase. J Biol Chem 279: 19775-19780
    • (2004) J Biol Chem , vol.279 , pp. 19775-19780
    • Tzagoloff, A.1    Barrientos, A.2    Neupert, W.3    Herrmann, J.M.4
  • 102
    • 0037986673 scopus 로고    scopus 로고
    • Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii: A proteomic approach
    • van Lis R, Atteia A, Mendoza-Hernandez G, Gonzalez-Halphen D (2003) Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii: a proteomic approach. Plant Physiol 132: 318-330
    • (2003) Plant Physiol , vol.132 , pp. 318-330
    • Van Lis, R.1    Atteia, A.2    Mendoza-Hernandez, G.3    Gonzalez-Halphen, D.4
  • 103
    • 0034530609 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae ATP synthase
    • Velours J, Arselin G (2000) The Saccharomyces cerevisiae ATP synthase. J Bioenerg Biomembr 32: 383-390
    • (2000) J Bioenerg Biomembr , vol.32 , pp. 383-390
    • Velours, J.1    Arselin, G.2
  • 105
    • 0037056054 scopus 로고    scopus 로고
    • From NADH to ubiquinone in Neurospora mitochondria
    • Videira A, 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
  • 106
    • 0035903210 scopus 로고    scopus 로고
    • Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria
    • Wang ZG, White PS, Ackerman SH (2001) Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human mitochondria. J Biol Chem 276: 30773-30778
    • (2001) J Biol Chem , vol.276 , pp. 30773-30778
    • Wang, Z.G.1    White, P.S.2    Ackerman, S.H.3
  • 107
    • 0038053885 scopus 로고    scopus 로고
    • ATP synthesis driven by proton transport in F1F0-ATP synthase
    • Weber J, Senior AE (2003) ATP synthesis driven by proton transport in F1F0-ATP synthase. FEBS Lett 545: 61-70
    • (2003) FEBS Lett , vol.545 , pp. 61-70
    • Weber, J.1    Senior, A.E.2
  • 109
    • 4344595430 scopus 로고    scopus 로고
    • The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: Mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA
    • Xu F, Morin C, Mitchell G, Ackerley C, Robinson BH (2004) The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA. Biochem J 382: 331-336
    • (2004) Biochem J , vol.382 , pp. 331-336
    • Xu, F.1    Morin, C.2    Mitchell, G.3    Ackerley, C.4    Robinson, B.H.5
  • 110
    • 0024298851 scopus 로고
    • Tissue-specific differences between heart and liver cytochrome c oxidase
    • Yanamura W, Zhang YZ, Takamiya S, Capaldi RA (1988) Tissue-specific differences between heart and liver cytochrome c oxidase. Biochemistry 27: 4909-4914
    • (1988) Biochemistry , vol.27 , pp. 4909-4914
    • Yanamura, W.1    Zhang, Y.Z.2    Takamiya, S.3    Capaldi, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.