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Volumn 62, Issue 3, 2006, Pages 319-331

Molecular evolution of cytochrome c oxidase in high-performance fish (Teleostei: Scombroidei)

Author keywords

Aerobic energy metabolism; Billfish; Cytochrome c oxidase; Endothermy; Mitochondrial DNA evolution; Positive selection; Tuna

Indexed keywords

CYTOCHROME C OXIDASE; CYTOCHROME C OXIDASE II; ISOENZYME; MITOCHONDRIAL DNA; UNCLASSIFIED DRUG;

EID: 33644882783     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00239-005-0110-7     Document Type: Article
Times cited : (58)

References (73)
  • 1
    • 0028347983 scopus 로고
    • Evolution of the primate cytochrome-c-oxidase subunit-II gene
    • Adkins RM, Honeycutt RL (1994) Evolution of the primate cytochrome-c-oxidase subunit-II gene. J Mol Evol 38:215-231
    • (1994) J Mol Evol , vol.38 , pp. 215-231
    • Adkins, R.M.1    Honeycutt, R.L.2
  • 2
    • 0029963745 scopus 로고    scopus 로고
    • Evolution of eutherian cytochrome c oxidase subunit II: Heterogeneous rates of protein evolution and altered interaction with cytochrome c
    • Adkins RM, Honeycutt RL, Disotell TR (1996) Evolution of eutherian cytochrome c oxidase subunit II: Heterogeneous rates of protein evolution and altered interaction with cytochrome c. Mol Biol Evol 13:1393-1404
    • (1996) Mol Biol Evol , vol.13 , pp. 1393-1404
    • Adkins, R.M.1    Honeycutt, R.L.2    Disotell, T.R.3
  • 3
    • 0032031485 scopus 로고    scopus 로고
    • 3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP
    • Arnold S, Goglia F, Kadenbach B (1998) 3,5-Diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP. Eur J Biochem 252:325-330
    • (1998) Eur J Biochem , vol.252 , pp. 325-330
    • Arnold, S.1    Goglia, F.2    Kadenbach, B.3
  • 6
    • 1642285792 scopus 로고    scopus 로고
    • The incomplete natural history of mitochondria
    • Ballard JW, Whitlock MC (2004) The incomplete natural history of mitochondria. Mol Ecol 13:729-744
    • (2004) Mol Ecol , vol.13 , pp. 729-744
    • Ballard, J.W.1    Whitlock, M.C.2
  • 7
    • 0035399727 scopus 로고    scopus 로고
    • Natural selection and the evolution of mtDNA-encoded peptides: Evidence for intergenomic co-adaptation
    • Blier PU, Dufresne F, Burton RS (2001) Natural selection and the evolution of mtDNA-encoded peptides: evidence for intergenomic co-adaptation. Trends Genet 17:400-406
    • (2001) Trends Genet , vol.17 , pp. 400-406
    • Blier, P.U.1    Dufresne, F.2    Burton, R.S.3
  • 8
    • 0022816822 scopus 로고
    • Structure of the brain and eye heater tissue in marlins, sailfish, and spearfish
    • Block BA (1986) Structure of the brain and eye heater tissue in marlins, sailfish, and spearfish. J Morphol 190:169-189
    • (1986) J Morphol , vol.190 , pp. 169-189
    • Block, B.A.1
  • 9
    • 0000157494 scopus 로고
    • Billfish brain and eye heater: A new look at nonshivering heat production
    • Block BA (1987) Billfish brain and eye heater: A new look at nonshivering heat production. News Physiol Sci 2:208-213
    • (1987) News Physiol Sci , vol.2 , pp. 208-213
    • Block, B.A.1
  • 10
    • 0028314350 scopus 로고
    • Thermogenesis in muscle
    • Block BA (1994) Thermogenesis in muscle. Annu Rev Physiol 56:535-577
    • (1994) Annu Rev Physiol , vol.56 , pp. 535-577
    • Block, B.A.1
  • 11
    • 0028561298 scopus 로고
    • Endothermy in fish: A phylogenetic analysis of constraints, predispositions, and selection pressures
    • Block BA, Finnerty JR (1994) Endothermy in fish: A phylogenetic analysis of constraints, predispositions, and selection pressures. Environ Biol Fish 40:283-302
    • (1994) Environ Biol Fish , vol.40 , pp. 283-302
    • Block, B.A.1    Finnerty, J.R.2
  • 12
    • 0027231871 scopus 로고
    • Evolution of endothermy in fish: Mapping physiological traits on a molecular phylogeny
    • Block BA, Finnerty JR, Stewart AF, Kidd J (1993) Evolution of endothermy in fish: mapping physiological traits on a molecular phylogeny. Science 260:210-214
    • (1993) Science , vol.260 , pp. 210-214
    • Block, B.A.1    Finnerty, J.R.2    Stewart, A.F.3    Kidd, J.4
  • 13
    • 0025801060 scopus 로고
    • Evolution of energy metabolism. Proton permeability of the inner membrane of liver mitochondria is greater in a mammal than in a reptile
    • Brand MD, Couture P, Else PL, Withers KW, Hulbert AJ (1991) Evolution of energy metabolism. Proton permeability of the inner membrane of liver mitochondria is greater in a mammal than in a reptile. Biochem J 275:81-86
    • (1991) Biochem J , vol.275 , pp. 81-86
    • Brand, M.D.1    Couture, P.2    Else, P.L.3    Withers, K.W.4    Hulbert, A.J.5
  • 14
    • 0029870612 scopus 로고    scopus 로고
    • Selective advantages conferred by the high performance physiology of tuna, billfish, and dolphin fish
    • Brill RW (1996) Selective advantages conferred by the high performance physiology of tuna, billfish, and dolphin fish. Comp Biochem Physiol A Physiol 113:3-15
    • (1996) Comp Biochem Physiol A Physiol , vol.113 , pp. 3-15
    • Brill, R.W.1
  • 15
    • 0020287356 scopus 로고
    • A brain heater in the swordfish
    • Carey FG (1982) A brain heater in the swordfish. Science 216:1327-1329
    • (1982) Science , vol.216 , pp. 1327-1329
    • Carey, F.G.1
  • 16
    • 0037331904 scopus 로고    scopus 로고
    • Repeatability of clades as a criterion of reliability: A case study for molecular phylogeny of Acanthomorpha (Teleostei) with larger number of taxa
    • Chen WJ, Bonillo C, Lecointre G (2003) Repeatability of clades as a criterion of reliability: a case study for molecular phylogeny of Acanthomorpha (Teleostei) with larger number of taxa. Mol Phylogenet Evol 26:262-288
    • (2003) Mol Phylogenet Evol , vol.26 , pp. 262-288
    • Chen, W.J.1    Bonillo, C.2    Lecointre, G.3
  • 17
    • 35648985741 scopus 로고    scopus 로고
    • Systematics of the tuna and mackerels (scombridae)
    • Block BA, Stevens ED (eds). Academic Press, San Diego, CA
    • Collette BB, Reeb C, Block BA (2001) Systematics of the tuna and mackerels (scombridae). In: Block BA, Stevens ED (eds) Tuna: Physiology, ecology, and evolution. Academic Press, San Diego, CA, pp 1-30
    • (2001) Tuna: Physiology, Ecology, and Evolution , pp. 1-30
    • Collette, B.B.1    Reeb, C.2    Block, B.A.3
  • 18
    • 11144285408 scopus 로고    scopus 로고
    • Mitochondrial enzyme content in the muscles of high-performance fish: Evolution and variation among fiber types
    • Dalziel AC, Moore SE, Moyes CD (2005) Mitochondrial enzyme content in the muscles of high-performance fish: evolution and variation among fiber types. Am J Physiol Regul Integr Comp Physiol 288:R163-R172
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Dalziel, A.C.1    Moore, S.E.2    Moyes, C.D.3
  • 19
    • 3242748398 scopus 로고    scopus 로고
    • Comparison of diverse protein sequences of the nuclear-encoded subunits of cytochrome C oxidase suggests conservation of structure underlies evolving functional sites
    • Das J, Miller ST, Stern DL (2004) Comparison of diverse protein sequences of the nuclear-encoded subunits of cytochrome C oxidase suggests conservation of structure underlies evolving functional sites. Mol Biol Evol 21:1572-1582
    • (2004) Mol Biol Evol , vol.21 , pp. 1572-1582
    • Das, J.1    Miller, S.T.2    Stern, D.L.3
  • 20
    • 0029932682 scopus 로고    scopus 로고
    • Locomotor muscle of high-performance fish: What do comparisons of tuna with ectothermic sister taxa reveal?
    • Dickson KA (1996) Locomotor muscle of high-performance fish: What do comparisons of tuna with ectothermic sister taxa reveal? Comp Biochem Physiol 113:39-49
    • (1996) Comp Biochem Physiol , vol.113 , pp. 39-49
    • Dickson, K.A.1
  • 21
    • 11144312476 scopus 로고    scopus 로고
    • Evolution and consequences of endothermy in fish
    • Dickson KA, Graham JB (2004) Evolution and consequences of endothermy in fish. Physiol Biochem Zool 77:998-1018
    • (2004) Physiol Biochem Zool , vol.77 , pp. 998-1018
    • Dickson, K.A.1    Graham, J.B.2
  • 22
    • 0001907716 scopus 로고
    • Evolution of cytochrome-b in the scombroidei (Teleostei) - Molecular insights into billfish (Istiophoridae and Xiphiidae) relationships
    • Finnerty JR, Block BA (1995) Evolution of cytochrome-b in the scombroidei (Teleostei) - Molecular insights into billfish (Istiophoridae and Xiphiidae) relationships. Fish Bull 93:78-96
    • (1995) Fish Bull , vol.93 , pp. 78-96
    • Block, B.A.1
  • 23
    • 0033040623 scopus 로고    scopus 로고
    • Action of thyroid hormones at the cellular level: The mitochondrial target
    • Goglia F, Moreno M, Lanni A (1999) Action of thyroid hormones at the cellular level: the mitochondrial target. FEBS Lett 452:115-120
    • (1999) FEBS Lett , vol.452 , pp. 115-120
    • Goglia, F.1    Moreno, M.2    Lanni, A.3
  • 24
    • 0028168856 scopus 로고
    • A codon-based model of nucleotide substitution for protein-coding DNA sequences
    • Goldman N, Yang Z (1994) A codon-based model of nucleotide substitution for protein-coding DNA sequences. Mol Biol Evol 11:725-36
    • (1994) Mol Biol Evol , vol.11 , pp. 725-736
    • Goldman, N.1    Yang, Z.2
  • 25
    • 35648968235 scopus 로고    scopus 로고
    • Anatomical and physiological specializations for endothermy
    • Block BA, Stevens ED (eds). Academic Press, San Diego, CA
    • Graham JB, Dickson KA (2001) Anatomical and physiological specializations for endothermy. In: Block BA, Stevens ED (eds) Tuna: Physiology, ecology, and evolution. Academic Press, San Diego, CA
    • (2001) Tuna: Physiology, Ecology, and Evolution
    • Graham, J.B.1    Dickson, K.A.2
  • 26
    • 4744342460 scopus 로고    scopus 로고
    • Accelerated evolution of the electron transport chain in anthropoid primates
    • Grossman LI, Wildman DE, Schmidt TR, Goodman M (2004) Accelerated evolution of the electron transport chain in anthropoid primates. Trends Genet 20:578-585
    • (2004) Trends Genet , vol.20 , pp. 578-585
    • Grossman, L.I.1    Wildman, D.E.2    Schmidt, T.R.3    Goodman, M.4
  • 27
    • 0031973948 scopus 로고    scopus 로고
    • Oxygen and proton pathways in cytochrome c oxidase
    • Hofacker I, Schulten K (1998) Oxygen and proton pathways in cytochrome c oxidase. Proteins 30:100-107
    • (1998) Proteins , vol.30 , pp. 100-107
    • Hofacker, I.1    Schulten, K.2
  • 28
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck JP, Ronquist F (2001) MRBAYES: Bayesian inference of phylogenetic trees. Bioinformatics 17:754-755
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 29
    • 0036806280 scopus 로고    scopus 로고
    • Potential applications and pitfalls of Bayesian inference of phylogeny
    • Huelsenbeck JP, Larget B, Miller RE, Ronquist F (2002) Potential applications and pitfalls of Bayesian inference of phylogeny. Syst Biol 51:673-688
    • (2002) Syst Biol , vol.51 , pp. 673-688
    • Huelsenbeck, J.P.1    Larget, B.2    Miller, R.E.3    Ronquist, F.4
  • 30
    • 0033618860 scopus 로고    scopus 로고
    • The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis
    • Huttemann M, Frank V, Kadenbach B (1999) The possible role of isoforms of cytochrome c oxidase subunit VIa in mammalian thermogenesis. Cell Mol Life Sci 55:1482-1490
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1482-1490
    • Huttemann, M.1    Frank, V.2    Kadenbach, B.3
  • 31
    • 0034904214 scopus 로고    scopus 로고
    • A mitogenomic perspective on the basal teleostean phylogeny: Resolving higher-level relationships with longer DNA sequences
    • Inoue JG, Miya M, Tsukamoto K, Nishida M (2001) A mitogenomic perspective on the basal teleostean phylogeny: resolving higher-level relationships with longer DNA sequences. Mol Phylogenet Evol 20:275-285
    • (2001) Mol Phylogenet Evol , vol.20 , pp. 275-285
    • Inoue, J.G.1    Miya, M.2    Tsukamoto, K.3    Nishida, M.4
  • 32
    • 11144246408 scopus 로고    scopus 로고
    • Adaptive evolution of cytochrome c oxidase: Infrastructure for a carnivorous plant radiation
    • USA
    • Jobson RW, Nielsen R, Laakkonen L, Wikstrom M, Albert VA (2004) Adaptive evolution of cytochrome c oxidase: Infrastructure for a carnivorous plant radiation. Proc Natl Acad Sci USA 101:18064-18068
    • (2004) Proc Natl Acad Sci , vol.101 , pp. 18064-18068
    • Jobson, R.W.1    Nielsen, R.2    Laakkonen, L.3    Wikstrom, M.4    Albert, V.A.5
  • 33
    • 0037726805 scopus 로고    scopus 로고
    • Intrinsic and extrinsic uncoupling of oxidative phosphorylation
    • Kadenbach B (2003) Intrinsic and extrinsic uncoupling of oxidative phosphorylation. Biochim Biophys Acta 1604:77-94
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 77-94
    • Kadenbach, B.1
  • 34
    • 35648946954 scopus 로고    scopus 로고
    • Tuna metabolism and energetics
    • Block BA, Stevens ED (eds). Academic Press, San Diego, CA
    • Korsmeyer KE, Dewar H (2001) Tuna metabolism and energetics. In: Block BA, Stevens ED (eds) Tuna: Physiology, ecology, and evolution. Academic Press, San Diego, CA, pp 36-78
    • (2001) Tuna: Physiology, Ecology, and Evolution , pp. 36-78
    • Korsmeyer, K.E.1    Dewar, H.2
  • 35
    • 0031821079 scopus 로고    scopus 로고
    • 3,5-Diiodo-L-thyronine and 3,5,3′-triiodo-L-thyronine both improve the cold tolerance of hypothyroid rats, but possibly via different mechanisms
    • Lanni A, Moreno M, Lombardi A, Goglia F (1998) 3,5-Diiodo-L-thyronine and 3,5,3′-triiodo-L-thyronine both improve the cold tolerance of hypothyroid rats, but possibly via different mechanisms. Pflugers Arch 436:407-14
    • (1998) Pflugers Arch , vol.436 , pp. 407-414
    • Lanni, A.1    Moreno, M.2    Lombardi, A.3    Goglia, F.4
  • 37
    • 0032491564 scopus 로고    scopus 로고
    • Second-site reversion analysis is not a reliable method to determine distances in membrane proteins: An assessment using mutations in yeast cytochrome c oxidase subunits I and II
    • Meunier B, Rich PR (1998) Second-site reversion analysis is not a reliable method to determine distances in membrane proteins: an assessment using mutations in yeast cytochrome c oxidase subunits I and II. J Mol Biol 283:727-730
    • (1998) J Mol Biol , vol.283 , pp. 727-730
    • Meunier, B.1    Rich, P.R.2
  • 40
    • 0037338934 scopus 로고    scopus 로고
    • 2+-ATPase isoforms in the thermogenic heater organ of blue marlin (Makaira nigricans)
    • 2+-ATPase isoforms in the thermogenic heater organ of blue marlin (Makaira nigricans). J Exp Biol 206:805-812
    • (2003) J Exp Biol , vol.206 , pp. 805-812
    • Morrissette, J.M.1    Franck, J.P.2    Block, B.A.3
  • 41
    • 0000415145 scopus 로고
    • Mitochondrial metabolism of cardiac and skeletal muscles from a fast (Katsuwonus pelamis) and a slow (Cyprinus carpio) fish
    • Moyes CD, Mathieu-Costello OA, Brill RW, Hochachka PW (1992) Mitochondrial metabolism of cardiac and skeletal muscles from a fast (Katsuwonus pelamis) and a slow (Cyprinus carpio) fish. Can J Zool 70:1246-1253
    • (1992) Can J Zool , vol.70 , pp. 1246-1253
    • Moyes, C.D.1    Mathieu-Costello, O.A.2    Brill, R.W.3    Hochachka, P.W.4
  • 42
    • 0001171131 scopus 로고
    • Systematics of the billfish (Xiphiidae and Istiophoridae)
    • Nakamura I (1983) Systematics of the billfish (Xiphiidae and Istiophoridae). Publ Set Mar Biol Lab 28:255-396
    • (1983) Publ Set Mar Biol Lab , vol.28 , pp. 255-396
    • Nakamura, I.1
  • 43
    • 0031972161 scopus 로고    scopus 로고
    • Likelihood models for detecting positively selected amino acid sites and applications to the HIV-1 envelope gene
    • Nielsen R, Yang Z (1998) Likelihood models for detecting positively selected amino acid sites and applications to the HIV-1 envelope gene. Genetics 148:929-936
    • (1998) Genetics , vol.148 , pp. 929-936
    • Nielsen, R.1    Yang, Z.2
  • 44
    • 0029967656 scopus 로고    scopus 로고
    • The effect of amino acid substitutions in the conserved aromatic region of subunit II of cytochrome c oxidase in Saccharomyces cerevisiae
    • Overholtzer MH, Yakowec PS, Cameron V (1996) The effect of amino acid substitutions in the conserved aromatic region of subunit II of cytochrome c oxidase in Saccharomyces cerevisiae. J Biol Chem 271:7719-7724
    • (1996) J Biol Chem , vol.271 , pp. 7719-7724
    • Overholtzer, M.H.1    Yakowec, P.S.2    Cameron, V.3
  • 45
    • 0031773680 scopus 로고    scopus 로고
    • MODELTEST: Testing the model of DNA substitution
    • Posada D, Crandall KA (1998) MODELTEST: Testing the model of DNA substitution. Bioinformatics 14:817-818
    • (1998) Bioinformatics , vol.14 , pp. 817-818
    • Posada, D.1    Crandall, K.A.2
  • 46
    • 0000107725 scopus 로고
    • Cartilage and bone development in scombroid fish
    • Potthoff T, Kelley S, Javech JC (1986) Cartilage and bone development in scombroid fish. Fish Bull 84:647-678
    • (1986) Fish Bull , vol.84 , pp. 647-678
    • Potthoff, T.1    Kelley, S.2    Javech, J.C.3
  • 49
    • 0035673444 scopus 로고    scopus 로고
    • The units of selection on mitochondrial DNA
    • Rand DM (2001) The units of selection on mitochondrial DNA. Annu Rev Ecol Syst 32:415-448
    • (2001) Annu Rev Ecol Syst , vol.32 , pp. 415-448
    • Rand, D.M.1
  • 50
    • 8144226823 scopus 로고    scopus 로고
    • Cytonuclear coevolution: The genomics of cooperation
    • Rand DM, Haney RA, Fry AJ (2004) Cytonuclear coevolution: The genomics of cooperation. Trends Ecol Evol 19:645-653
    • (2004) Trends Ecol Evol , vol.19 , pp. 645-653
    • Rand, D.M.1    Haney, R.A.2    Fry, A.J.3
  • 51
    • 0036791993 scopus 로고    scopus 로고
    • Functional coadaptation between cytochrome c and cytochrome c oxidase within allopatric populations of a marine copepod
    • USA
    • Rawson PD, Burton RS (2002) Functional coadaptation between cytochrome c and cytochrome c oxidase within allopatric populations of a marine copepod. Proc Natl Acad Sci USA 99:12955-12958
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 12955-12958
    • Rawson, P.D.1    Burton, R.S.2
  • 52
    • 0642283837 scopus 로고    scopus 로고
    • Cytochrome c oxidase - Structure, function, and physiology of a redox-driven molecular machine
    • Richter OM, Ludwig B (2003) Cytochrome c oxidase - structure, function, and physiology of a redox-driven molecular machine. Rev Physiol Biochem Pharmacol 147:47-74
    • (2003) Rev Physiol Biochem Pharmacol , vol.147 , pp. 47-74
    • Richter, O.M.1    Ludwig, B.2
  • 53
    • 0033621360 scopus 로고    scopus 로고
    • Definition of the interaction domain for cytochrome c on cytochrome c oxidase. III. Prediction of the docked complex by a complete, systematic search
    • Roberts VA, Pique ME (1999) Definition of the interaction domain for cytochrome c on cytochrome c oxidase. III. Prediction of the docked complex by a complete, systematic search. J Biol Chem 274:38051-38060
    • (1999) J Biol Chem , vol.274 , pp. 38051-38060
    • Roberts, V.A.1    Pique, M.E.2
  • 54
    • 0347356538 scopus 로고    scopus 로고
    • Effects of purifying and adaptive selection on regional variation in human mtDNA
    • Ruiz-Pesini E, Mishmar D, Brandon M, Procaccio V, Wallace DC (2004) Effects of purifying and adaptive selection on regional variation in human mtDNA. Science 303:223-226
    • (2004) Science , vol.303 , pp. 223-226
    • Ruiz-Pesini, E.1    Mishmar, D.2    Brandon, M.3    Procaccio, V.4    Wallace, D.C.5
  • 55
    • 0346103674 scopus 로고    scopus 로고
    • A discrete water exit pathway in the membrane protein cytochrome c oxidase
    • USA
    • Schmidt B, McCracken J, Ferguson-Miller S (2003) A discrete water exit pathway in the membrane protein cytochrome c oxidase. Proc Natl Acad Sci USA 100:15539-15542
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 15539-15542
    • Schmidt, B.1    McCracken, J.2    Ferguson-Miller, S.3
  • 56
    • 0035056971 scopus 로고    scopus 로고
    • Evolution of nuclear- and mitochondrial-encoded subunit interaction in cytochrome c oxidase
    • Schmidt TR, Wu W, Goodman M, Grossman LI (2001) Evolution of nuclear- and mitochondrial-encoded subunit interaction in cytochrome c oxidase. Mol Biol Evol 18:563-569
    • (2001) Mol Biol Evol , vol.18 , pp. 563-569
    • Schmidt, T.R.1    Wu, W.2    Goodman, M.3    Grossman, L.I.4
  • 57
    • 1642546638 scopus 로고    scopus 로고
    • Efficiently resolving the basal clades of a phylogenetic tree using Bayesian and parsimony approaches: A case study using mitogenomic data from 100 higher teleost fish
    • Simmons MP, Miya M (2004) Efficiently resolving the basal clades of a phylogenetic tree using Bayesian and parsimony approaches: a case study using mitogenomic data from 100 higher teleost fish. Mol Phylogenet Evol 31:351-362
    • (2004) Mol Phylogenet Evol , vol.31 , pp. 351-362
    • Simmons, M.P.1    Miya, M.2
  • 58
    • 0035349906 scopus 로고    scopus 로고
    • The genetics and pathology of oxidative phosphorylation
    • Smeitink J, van den Heuvel L, DiMauro S (2001) The genetics and pathology of oxidative phosphorylation. Nat Rev Genet 2:342-352
    • (2001) Nat Rev Genet , vol.2 , pp. 342-352
    • Smeitink, J.1    Van Den Heuvel, L.2    DiMauro, S.3
  • 59
    • 0002215847 scopus 로고
    • Organization of proteins within the mitochondrion
    • Welch GR (ed). Academic Press, New York, London
    • Srere PA (1985) Organization of proteins within the mitochondrion. In: Welch GR (ed) Organized multienzyme systems. Catalytic properties. Academic Press, New York, London, pp 1-61
    • (1985) Organized Multienzyme Systems. Catalytic Properties , pp. 1-61
    • Srere, P.A.1
  • 61
    • 0034857191 scopus 로고    scopus 로고
    • The cyclope gene of Drosophila encodes a cytochrome c oxidase subunit VIc homolog
    • Szuplewski S, Terracol R (2001) The cyclope gene of Drosophila encodes a cytochrome c oxidase subunit VIc homolog. Genetics 158:1629-1643
    • (2001) Genetics , vol.158 , pp. 1629-1643
    • Szuplewski, S.1    Terracol, R.2
  • 62
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 64
    • 0026246534 scopus 로고
    • Activities of key metabolic enzymes in the heater organs of scombroid fish
    • Tullis A, Block BA, Sidell BD (1991) Activities of key metabolic enzymes in the heater organs of scombroid fish. J Exp Biol 161:383-403
    • (1991) J Exp Biol , vol.161 , pp. 383-403
    • Tullis, A.1    Block, B.A.2    Sidell, B.D.3
  • 65
    • 0023921078 scopus 로고
    • Organ blood flow haemodynamics and metabolism of the albacore tuna Thunnus alalunga (Bonnaterre)
    • White FC, Kelly R, Kemper S, Schumacker PT, Gallagher KR, Laurs RM (1988) Organ blood flow haemodynamics and metabolism of the albacore tuna Thunnus alalunga (Bonnaterre). Exp Biol 47:161-9
    • (1988) Exp Biol , vol.47 , pp. 161-169
    • White, F.C.1    Kelly, R.2    Kemper, S.3    Schumacker, P.T.4    Gallagher, K.R.5    Laurs, R.M.6
  • 66
    • 0242499394 scopus 로고    scopus 로고
    • Environmental influences on epistatic interactions: Viabilities of cytochrome c genotypes in interpopulation crosses
    • Willett CS, Burton RS (2003) Environmental influences on epistatic interactions: Viabilities of cytochrome c genotypes in interpopulation crosses. Evolution 57:2286-2292
    • (2003) Evolution , vol.57 , pp. 2286-2292
    • Willett, C.S.1    Burton, R.S.2
  • 67
    • 1542405309 scopus 로고    scopus 로고
    • Evolution of interacting proteins in the mitochondrial electron transport system in a marine copepod
    • Willett CS, Burton RS (2004) Evolution of interacting proteins in the mitochondrial electron transport system in a marine copepod. Mol Biol Evol 21:443-453
    • (2004) Mol Biol Evol , vol.21 , pp. 443-453
    • Willett, C.S.1    Burton, R.S.2
  • 68
    • 0027132974 scopus 로고
    • Maximum-likelihood estimation of phylogeny from DNA sequences when substitution rates differ over sites
    • Yang Z (1993) Maximum-likelihood estimation of phylogeny from DNA sequences when substitution rates differ over sites. Mol Biol Evol 10:1396-1401
    • (1993) Mol Biol Evol , vol.10 , pp. 1396-1401
    • Yang, Z.1
  • 69
    • 0030683599 scopus 로고    scopus 로고
    • PAML: A program package for phylogenetic analysis by maximum likelihood
    • Yang Z (1997) PAML: A program package for phylogenetic analysis by maximum likelihood. Comput Appl Biosci 13:555-556
    • (1997) Comput Appl Biosci , vol.13 , pp. 555-556
    • Yang, Z.1
  • 70
    • 0031897964 scopus 로고    scopus 로고
    • Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution
    • Yang Z (1998) Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution. Mol Biol Evol 15:568-573
    • (1998) Mol Biol Evol , vol.15 , pp. 568-573
    • Yang, Z.1
  • 71
    • 0036270185 scopus 로고    scopus 로고
    • Codon-substitution models for detecting molecular adaptation at individual sites along specific lineages
    • Yang Z, Nielsen R (2002) Codon-substitution models for detecting molecular adaptation at individual sites along specific lineages. Mol Biol Evol 19:908-917
    • (2002) Mol Biol Evol , vol.19 , pp. 908-917
    • Yang, Z.1    Nielsen, R.2
  • 72
    • 0034097381 scopus 로고    scopus 로고
    • Codon-substitution models for heterogeneous selection pressure at amino acid sites
    • Yang Z, Nielsen R, Goldman N, Pedersen AM (2000) Codon-substitution models for heterogeneous selection pressure at amino acid sites. Genetics 155:431-449
    • (2000) Genetics , vol.155 , pp. 431-449
    • Yang, Z.1    Nielsen, R.2    Goldman, N.3    Pedersen, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.