메뉴 건너뛰기




Volumn 20, Issue 11, 2004, Pages 578-585

Accelerated evolution of the electron transport chain in anthropoid primates

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; PROSTAGLANDIN SYNTHASE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 4744342460     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tig.2004.09.002     Document Type: Review
Times cited : (156)

References (71)
  • 1
    • 0037726805 scopus 로고    scopus 로고
    • Intrinsic and extrinsic uncoupling of oxidative phosphorylation
    • B. Kadenbach Intrinsic and extrinsic uncoupling of oxidative phosphorylation Biochim. Biophys. Acta 1604 2003 77 94
    • (2003) Biochim. Biophys. Acta , vol.1604 , pp. 77-94
    • Kadenbach, B.1
  • 2
    • 0037459081 scopus 로고    scopus 로고
    • Mitochondria: Releasing power for life and unleashing the machineries of death
    • D.D. Newmeyer, and S. Ferguson-Miller Mitochondria: releasing power for life and unleashing the machineries of death Cell 112 2003 481 490
    • (2003) Cell , vol.112 , pp. 481-490
    • Newmeyer, D.D.1    Ferguson-Miller, S.2
  • 3
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Droge Free radicals in the physiological control of cell function Physiol. Rev. 82 2002 47 95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 4
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • T. Finkel Oxidant signals and oxidative stress Curr. Opin. Cell Biol. 15 2003 247 254
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 5
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Y.B. Li Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase Nat. Genet. 11 1995 376 381
    • (1995) Nat. Genet. , vol.11 , pp. 376-381
    • Li, Y.B.1
  • 6
    • 0035782650 scopus 로고    scopus 로고
    • Reactive oxygen species and mitochondrial diseases
    • I.G. Kirkinezos, and C.T. Moraes Reactive oxygen species and mitochondrial diseases Semin. Cell Dev. Biol. 12 2001 449 457
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 449-457
    • Kirkinezos, I.G.1    Moraes, C.T.2
  • 7
    • 0642375798 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, apoptotic cell death, and Alzheimer's disease
    • A. Eckert Mitochondrial dysfunction, apoptotic cell death, and Alzheimer's disease Biochem. Pharmacol. 66 2003 1627 1634
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1627-1634
    • Eckert, A.1
  • 8
    • 0035515923 scopus 로고    scopus 로고
    • Mitochondrial electron transport is a key determinant of life span in Caenorhabditis elegans
    • J. Feng Mitochondrial electron transport is a key determinant of life span in Caenorhabditis elegans Dev. Cell 1 2001 633 644
    • (2001) Dev. Cell , vol.1 , pp. 633-644
    • Feng, J.1
  • 9
    • 0035060368 scopus 로고    scopus 로고
    • Oxidative biochemical markers; Clues to understanding aging in long-lived species
    • R.A. Floyd Oxidative biochemical markers; clues to understanding aging in long-lived species Exp. Gerontol. 36 2001 619 640
    • (2001) Exp. Gerontol. , vol.36 , pp. 619-640
    • Floyd, R.A.1
  • 10
    • 0036829433 scopus 로고    scopus 로고
    • Rate of generation of oxidative stress-related damage and animal longevity
    • G. Barja Rate of generation of oxidative stress-related damage and animal longevity Free Radic. Biol. Med. 33 2002 1167 1172
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1167-1172
    • Barja, G.1
  • 11
    • 0037147103 scopus 로고    scopus 로고
    • Rates of behavior and aging specified by mitochondrial function during development
    • A. Dillin Rates of behavior and aging specified by mitochondrial function during development Science 298 2002 2398 2401
    • (2002) Science , vol.298 , pp. 2398-2401
    • Dillin, A.1
  • 12
    • 12144288373 scopus 로고    scopus 로고
    • Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging
    • H. Vanremmen Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging Physiol. Genomics 16 2003 29 37
    • (2003) Physiol. Genomics , vol.16 , pp. 29-37
    • Vanremmen, H.1
  • 14
    • 0031046679 scopus 로고    scopus 로고
    • Subunit change in cytochrome c oxidase: Identification of the oxygen switch in Dictyostelium
    • R. Bisson Subunit change in cytochrome c oxidase: Identification of the oxygen switch in Dictyostelium EMBO J. 16 1997 739 749
    • (1997) EMBO J. , vol.16 , pp. 739-749
    • Bisson, R.1
  • 15
    • 0026771433 scopus 로고
    • Oxygen regulated transcription of cytochrome c and cytochrome c oxidase genes in yeast
    • R.O. Poyton, and P.V. Burke Oxygen regulated transcription of cytochrome c and cytochrome c oxidase genes in yeast Biochim. Biophys. Acta 1101 1992 252 256
    • (1992) Biochim. Biophys. Acta , vol.1101 , pp. 252-256
    • Poyton, R.O.1    Burke, P.V.2
  • 16
    • 0033033002 scopus 로고    scopus 로고
    • The intramitochondrial ATP/ADP-ratio controls cytochrome c oxidase activity allosterically
    • S. Arnold, and B. Kadenbach The intramitochondrial ATP/ADP-ratio controls cytochrome c oxidase activity allosterically FEBS Lett. 443 1999 105 108
    • (1999) FEBS Lett. , vol.443 , pp. 105-108
    • Arnold, S.1    Kadenbach, B.2
  • 17
    • 0035382613 scopus 로고    scopus 로고
    • Cytochrome c oxidase and the regulation of oxidative phosphorylation
    • B. Ludwig Cytochrome c oxidase and the regulation of oxidative phosphorylation ChemBioChem 2 2001 392 403
    • (2001) ChemBioChem , vol.2 , pp. 392-403
    • Ludwig, B.1
  • 18
    • 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
    • S. Arnold 3,5-diiodothyronine binds to subunit Va of cytochrome-c oxidase and abolishes the allosteric inhibition of respiration by ATP Eur. J. Biochem. 252 1998 325 330
    • (1998) Eur. J. Biochem. , vol.252 , pp. 325-330
    • Arnold, S.1
  • 19
    • 0344861886 scopus 로고    scopus 로고
    • Protein interaction: Same network, different hubs
    • R. Hoffmann, and A. Valencia Protein interaction: same network, different hubs Trends Genet. 19 2003 681 683
    • (2003) Trends Genet. , vol.19 , pp. 681-683
    • Hoffmann, R.1    Valencia, A.2
  • 20
    • 0017755023 scopus 로고
    • Cytochrome oxidase deficiency during development of amphibian nucleocytoplasmic hybrids
    • A. Liepins, and S. Hennen Cytochrome oxidase deficiency during development of amphibian nucleocytoplasmic hybrids Dev. Biol. 57 1977 284 292
    • (1977) Dev. Biol. , vol.57 , pp. 284-292
    • Liepins, A.1    Hennen, S.2
  • 21
    • 1542405309 scopus 로고    scopus 로고
    • Evolution of interacting proteins in the mitochondrial electron transport system in a marine copepod
    • C.S. Willett, and R.S. Burton Evolution of interacting proteins in the mitochondrial electron transport system in a marine copepod Mol. Biol. Evol. 21 2004 443 453
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 443-453
    • Willett, C.S.1    Burton, R.S.2
  • 22
    • 0033428028 scopus 로고    scopus 로고
    • Cytochrome c oxidase activity in interpopulation hybrids of a marine copepod: A test for nuclear-nuclear or nuclear-cytoplasmic coadaptation
    • S. Edmands, and R.S. Burton Cytochrome c oxidase activity in interpopulation hybrids of a marine copepod: a test for nuclear-nuclear or nuclear-cytoplasmic coadaptation Evolution 53 1999 1972 1978
    • (1999) Evolution , vol.53 , pp. 1972-1978
    • Edmands, S.1    Burton, R.S.2
  • 23
    • 0036791993 scopus 로고    scopus 로고
    • Functional coadaptation between cytochrome c and cytochrome c oxidase within allopatric populations of a marine copepod
    • P.D. Rawson, and R.S. Burton Functional coadaptation between cytochrome c and cytochrome c oxidase within allopatric populations of a marine copepod Proc. Natl. Acad. Sci. U. S. A. 99 2002 12955 12958
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12955-12958
    • Rawson, P.D.1    Burton, R.S.2
  • 24
    • 0030750574 scopus 로고    scopus 로고
    • Expanding the functional human mitochondrial DNA database by the establishment of primate xenomitochondrial cybrids
    • L. Kenyon, and C.T. Moraes Expanding the functional human mitochondrial DNA database by the establishment of primate xenomitochondrial cybrids Proc. Natl. Acad. Sci. U. S. A. 94 1997 9131 9135
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9131-9135
    • Kenyon, L.1    Moraes, C.T.2
  • 25
    • 0032486399 scopus 로고    scopus 로고
    • Human xenomitochondrial cybrids - Cellular models of mitochondrial complex I deficiency
    • A. Barrientos Human xenomitochondrial cybrids - cellular models of mitochondrial complex I deficiency J. Biol. Chem. 273 1998 14210 14217
    • (1998) J. Biol. Chem. , vol.273 , pp. 14210-14217
    • Barrientos, A.1
  • 26
    • 0032088632 scopus 로고    scopus 로고
    • Toward a phylogenetic classification of primates based on DNA evidence complemented by fossil evidence
    • M. Goodman Toward a phylogenetic classification of primates based on DNA evidence complemented by fossil evidence Mol. Phylogenet. Evol. 9 1998 585 598
    • (1998) Mol. Phylogenet. Evol. , vol.9 , pp. 585-598
    • Goodman, M.1
  • 27
    • 0031029962 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells
    • G. Villani, and G. Attardi In vivo control of respiration by cytochrome c oxidase in wild-type and mitochondrial DNA mutation-carrying human cells Proc. Natl. Acad. Sci. U. S. A. 94 1997 1166 1171
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1166-1171
    • Villani, G.1    Attardi, G.2
  • 28
    • 0033795824 scopus 로고    scopus 로고
    • In vivo control of respiration by cytochrome c oxidase in human cells
    • G. Villani, and G. Attardi In vivo control of respiration by cytochrome c oxidase in human cells Free Radic. Biol. Med. 29 2000 202 210
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 202-210
    • Villani, G.1    Attardi, G.2
  • 29
    • 0026651787 scopus 로고
    • Rapid evolution of the human gene for cytochrome c oxidase subunit IV
    • M.I. Lomax Rapid evolution of the human gene for cytochrome c oxidase subunit IV Proc. Natl. Acad. Sci. U. S. A. 89 1992 5266 5270
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5266-5270
    • Lomax, M.I.1
  • 30
    • 0030915138 scopus 로고    scopus 로고
    • Molecular evolution of cytochrome c oxidase subunit IV: Evidence for positive selection in simian primates
    • W. Wu Molecular evolution of cytochrome c oxidase subunit IV: Evidence for positive selection in simian primates J. Mol. Evol. 44 1997 477 491
    • (1997) J. Mol. Evol. , vol.44 , pp. 477-491
    • Wu, W.1
  • 31
    • 0036790004 scopus 로고    scopus 로고
    • Episodic positive selection in ape cytochrome c oxidase subunit IV
    • D.E. Wildman Episodic positive selection in ape cytochrome c oxidase subunit IV Mol. Biol. Evol. 19 2002 1812 1815
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 1812-1815
    • Wildman, D.E.1
  • 32
    • 0028347983 scopus 로고
    • Evolution of the primate cytochrome c oxidase subunit II gene
    • R.M. Adkins, and R.L. Honeycutt Evolution of the primate cytochrome c oxidase subunit II gene J. Mol. Evol. 38 1994 215 231
    • (1994) J. Mol. Evol. , vol.38 , pp. 215-231
    • Adkins, R.M.1    Honeycutt, R.L.2
  • 33
    • 0020486102 scopus 로고
    • Positive selection causes purifying selection
    • M. Goodman Positive selection causes purifying selection Nature 295 1982 630
    • (1982) Nature , vol.295 , pp. 630
    • Goodman, M.1
  • 34
    • 7444255456 scopus 로고    scopus 로고
    • Coadaptive evolution in cytochrome c oxidase: 9 of 13 subunits show accelerated rates of nonsynonymous substitution in anthropoid primates
    • (in press)
    • Doan, J.W. et al. Coadaptive evolution in cytochrome c oxidase: 9 of 13 subunits show accelerated rates of nonsynonymous substitution in anthropoid primates. Mol. Phylogenet. Evol. (in press)
    • Mol. Phylogenet. Evol.
    • Doan, J.W.1
  • 35
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 angstrom
    • T. Tsukihara The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 angstrom Science 272 1996 1136 1144
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1
  • 36
    • 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
    • V.A. Roberts, and M.E. Pique 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 1999 38051 38060
    • (1999) J. Biol. Chem. , vol.274 , pp. 38051-38060
    • Roberts, V.A.1    Pique, M.E.2
  • 37
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • P. Mitchell Possible molecular mechanisms of the protonmotive function of cytochrome systems J. Theor. Biol. 62 1976 327 367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 39
    • 0028277764 scopus 로고
    • The protonmotive Q cycle in mitochondria and bacteria
    • U. Brandt, and B. Trumpower The protonmotive Q cycle in mitochondria and bacteria Crit. Rev. Biochem. Mol. Biol. 29 1994 165 197
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 165-197
    • Brandt, U.1    Trumpower, B.2
  • 40
    • 0036139856 scopus 로고    scopus 로고
    • The mitochondrial production of reactive oxygen species: Mechanisms and implications in human pathology
    • G. Lenaz The mitochondrial production of reactive oxygen species: mechanisms and implications in human pathology IUBMB Life 52 2001 159 164
    • (2001) IUBMB Life , vol.52 , pp. 159-164
    • Lenaz, G.1
  • 41
    • 0037771389 scopus 로고    scopus 로고
    • Are mitochondria a spontaneous and permanent source of reactive oxygen species?
    • H. Nohl Are mitochondria a spontaneous and permanent source of reactive oxygen species? Redox Rep. 8 2003 135 141
    • (2003) Redox Rep. , vol.8 , pp. 135-141
    • Nohl, H.1
  • 42
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria - Central role of complex III
    • Q. Chen Production of reactive oxygen species by mitochondria - central role of complex III J. Biol. Chem. 278 2003 36027 36031
    • (2003) J. Biol. Chem. , vol.278 , pp. 36027-36031
    • Chen, Q.1
  • 43
    • 0031714828 scopus 로고    scopus 로고
    • Accelerated evolution of cytochrome b in simian primates: Adaptive evolution in concert with other mitochondrial proteins?
    • T.D. Andrews Accelerated evolution of cytochrome b in simian primates: adaptive evolution in concert with other mitochondrial proteins? J. Mol. Evol. 47 1998 249 257
    • (1998) J. Mol. Evol. , vol.47 , pp. 249-257
    • Andrews, T.D.1
  • 44
    • 0035147609 scopus 로고    scopus 로고
    • Molecular evolution of aerobic energy metabolism in primates
    • L.I. Grossman Molecular evolution of aerobic energy metabolism in primates Mol. Phylogenet. Evol. 18 2001 26 36
    • (2001) Mol. Phylogenet. Evol. , vol.18 , pp. 26-36
    • Grossman, L.I.1
  • 45
    • 0036246373 scopus 로고    scopus 로고
    • Search for genes positively selected during primate evolution by 5′-end-sequence screening of cynomolgus monkey cDNAs
    • N. Osada Search for genes positively selected during primate evolution by 5′-end-sequence screening of cynomolgus monkey cDNAs Genomics 79 2002 657 662
    • (2002) Genomics , vol.79 , pp. 657-662
    • Osada, N.1
  • 46
    • 0019360101 scopus 로고
    • Evolution of cytochrome c investigated by the maximum parsimony method
    • M.L. Baba Evolution of cytochrome c investigated by the maximum parsimony method J. Mol. Evol. 17 1981 197 213
    • (1981) J. Mol. Evol. , vol.17 , pp. 197-213
    • Baba, M.L.1
  • 47
    • 0002515876 scopus 로고
    • Amino acid sequence evidence on the phylogeny of primates and other eutherians
    • M. Goodman Plenum
    • M. Goodman Amino acid sequence evidence on the phylogeny of primates and other eutherians M. Goodman Macromolecular sequences in systematic and evolutionary biology 1982 Plenum 115 191
    • (1982) Macromolecular Sequences in Systematic and Evolutionary Biology , pp. 115-191
    • Goodman, M.1
  • 48
    • 0021099431 scopus 로고
    • The reaction of primate cytochromes c with cytochrome c oxidase. Analysis of the polarographic assay
    • N. Osheroff The reaction of primate cytochromes c with cytochrome c oxidase. analysis of the polarographic assay J. Biol. Chem. 258 1983 5731 5738
    • (1983) J. Biol. Chem. , vol.258 , pp. 5731-5738
    • Osheroff, N.1
  • 49
    • 0029963745 scopus 로고    scopus 로고
    • Evolution of eutherian cytochrome c oxidase subunit II: Heterogeneous rates of protein evolution and altered interaction with cytochrome c
    • R.M. Adkins Evolution of eutherian cytochrome c oxidase subunit II: heterogeneous rates of protein evolution and altered interaction with cytochrome c Mol. Biol. Evol. 13 1996 1393 1404
    • (1996) Mol. Biol. Evol. , vol.13 , pp. 1393-1404
    • Adkins, R.M.1
  • 50
    • 0033916987 scopus 로고    scopus 로고
    • Evolutionary rate acceleration of cytochrome c oxidase subunit I in simian primates
    • T.D. Andrews, and S. Easteal Evolutionary rate acceleration of cytochrome c oxidase subunit I in simian primates J. Mol. Evol. 50 2000 562 568
    • (2000) J. Mol. Evol. , vol.50 , pp. 562-568
    • Andrews, T.D.1    Easteal, S.2
  • 51
    • 0033709702 scopus 로고    scopus 로고
    • Molecular evolution of cytochrome c oxidase subunit I in primates: Is there co-evolution between mitochondrial and nuclear genomes?
    • W. Wu Molecular evolution of cytochrome c oxidase subunit I in primates: is there co-evolution between mitochondrial and nuclear genomes? Mol. Phylogenet. Evol. 17 2000 294 304
    • (2000) Mol. Phylogenet. Evol. , vol.17 , pp. 294-304
    • Wu, W.1
  • 52
    • 1542297747 scopus 로고    scopus 로고
    • Sister grouping of chimpanzees and humans as revealed by genome-wide phylogenetic analysis of brain gene expression profiles
    • M. Uddin Sister grouping of chimpanzees and humans as revealed by genome-wide phylogenetic analysis of brain gene expression profiles Proc. Natl. Acad. Sci. U. S. A. 101 2004 2957 2962
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2957-2962
    • Uddin, M.1
  • 53
    • 0022464172 scopus 로고
    • Molecular evidence on the ape subfamily homininae
    • H. Gershowitz Alan R. Liss New York, et al.
    • M. Goodman Molecular evidence on the ape subfamily homininae H. Gershowitz Evolutionary perspectives and the new genetics 1986 Alan R. Liss New York 121 132
    • (1986) Evolutionary Perspectives and the New Genetics , pp. 121-132
    • Goodman, M.1
  • 54
    • 0035804655 scopus 로고    scopus 로고
    • Mammalian subunit IV isoforms of cytochrome c oxidase
    • M. Hüttemann Mammalian subunit IV isoforms of cytochrome c oxidase Gene 267 2001 111 123
    • (2001) Gene , vol.267 , pp. 111-123
    • Hüttemann, M.1
  • 55
    • 0016669094 scopus 로고
    • Evolution at two levels in humans and chimpanzees
    • M.C. King, and A.C. Wilson Evolution at two levels in humans and chimpanzees Science 188 1975 107 116
    • (1975) Science , vol.188 , pp. 107-116
    • King, M.C.1    Wilson, A.C.2
  • 57
    • 0036787796 scopus 로고    scopus 로고
    • ASPM is a major determinant of cerebral cortical size
    • J. Bond ASPM is a major determinant of cerebral cortical size Nat. Genet. 32 2002 316 320
    • (2002) Nat. Genet. , vol.32 , pp. 316-320
    • Bond, J.1
  • 58
    • 0036302105 scopus 로고    scopus 로고
    • Identification of microcephalin, a protein implicated in determining the size of the human brain
    • A.P. Jackson Identification of microcephalin, a protein implicated in determining the size of the human brain Am. J. Hum. Genet. 71 2002 136 142
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 136-142
    • Jackson, A.P.1
  • 59
    • 0347992009 scopus 로고    scopus 로고
    • Evolution of the human ASPM gene, a major determinant of brain size
    • J. Zhang Evolution of the human ASPM gene, a major determinant of brain size Genetics 165 2003 2063 2070
    • (2003) Genetics , vol.165 , pp. 2063-2070
    • Zhang, J.1
  • 60
    • 2942744749 scopus 로고    scopus 로고
    • Reconstructing the evolutionary history of microcephalin, a gene controlling human brain size
    • P.D. Evans Reconstructing the evolutionary history of microcephalin, a gene controlling human brain size Hum. Mol. Genet. 13 2004 1139 1145
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1139-1145
    • Evans, P.D.1
  • 61
    • 1542329549 scopus 로고    scopus 로고
    • Adaptive evolution of ASPM, a major determinant of cerebral cortical size in humans
    • P.D. Evans Adaptive evolution of ASPM, a major determinant of cerebral cortical size in humans Hum. Mol. Genet. 13 2004 489 494
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 489-494
    • Evans, P.D.1
  • 62
    • 19344374302 scopus 로고    scopus 로고
    • Accelerated evolution of the ASPM gene controlling brain size begins prior to human brain expansion
    • N. Kouprina Accelerated evolution of the ASPM gene controlling brain size begins prior to human brain expansion PLos Biol. 2 2004 E126
    • (2004) PLos Biol. , vol.2
    • Kouprina, N.1
  • 63
    • 2942737273 scopus 로고    scopus 로고
    • Molecular evolution of microcephalin, a gene determining human brain size
    • Y.Q. Wang, and B. Su Molecular evolution of microcephalin, a gene determining human brain size Hum. Mol. Genet. 13 2004 1131 1137
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1131-1137
    • Wang, Y.Q.1    Su, B.2
  • 64
    • 0025186837 scopus 로고
    • The anterior cingulate cortex mediates processing selection in the Stroop attentional conflict paradigm
    • J.V. Pardo The anterior cingulate cortex mediates processing selection in the Stroop attentional conflict paradigm Proc. Natl. Acad. Sci. U. S. A. 87 1990 256 259
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 256-259
    • Pardo, J.V.1
  • 65
    • 0033609014 scopus 로고    scopus 로고
    • A neuronal morphologic type unique to humans and great apes
    • E.A. Nimchinsky A neuronal morphologic type unique to humans and great apes Proc. Natl. Acad. Sci. U. S. A. 96 1999 5268 5273
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5268-5273
    • Nimchinsky, E.A.1
  • 66
    • 0034652146 scopus 로고    scopus 로고
    • Parsing executive processes: Strategic vs. evaluative functions of the anterior cingulate cortex
    • C.S. Carter Parsing executive processes: strategic vs. evaluative functions of the anterior cingulate cortex Proc. Natl. Acad. Sci. U. S. A. 97 2000 1944 1948
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1944-1948
    • Carter, C.S.1
  • 67
    • 0034625673 scopus 로고    scopus 로고
    • Dissociating the role of the dorsolateral prefrontal and anterior cingulate cortex in cognitive control
    • A.W. Macdonald 3rd Dissociating the role of the dorsolateral prefrontal and anterior cingulate cortex in cognitive control Science 288 2000 1835 1838
    • (2000) Science , vol.288 , pp. 1835-1838
    • Macdonald III, A.W.1
  • 68
    • 0037029048 scopus 로고    scopus 로고
    • Amino acid replacement is rapid in primates for the mature polypeptides of COX subunits, but not for their targeting presequences
    • T.R. Schmidt Amino acid replacement is rapid in primates for the mature polypeptides of COX subunits, but not for their targeting presequences Gene 286 2002 13 19
    • (2002) Gene , vol.286 , pp. 13-19
    • Schmidt, T.R.1
  • 69
    • 0030924878 scopus 로고    scopus 로고
    • Molecular evolution of cytochrome c oxidase: Rate variation among subunit VIa isoforms
    • T.R. Schmidt Molecular evolution of cytochrome c oxidase: rate variation among subunit VIa isoforms Mol. Biol. Evol. 14 1997 595 601
    • (1997) Mol. Biol. Evol. , vol.14 , pp. 595-601
    • Schmidt, T.R.1
  • 70
    • 0032953315 scopus 로고    scopus 로고
    • Molecular evolution of the COX7A gene family in primates
    • T.R. Schmidt Molecular evolution of the COX7A gene family in primates Mol. Biol. Evol. 16 1999 619 626
    • (1999) Mol. Biol. Evol. , vol.16 , pp. 619-626
    • Schmidt, T.R.1
  • 71
    • 0037947749 scopus 로고    scopus 로고
    • Adaptive evolution of cytochrome c oxidase subunit VIII in anthropoid primates
    • A. Goldberg Adaptive evolution of cytochrome c oxidase subunit VIII in anthropoid primates Proc. Natl. Acad. Sci. U. S. A. 100 2003 5873 5878
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5873-5878
    • Goldberg, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.