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Volumn 99, Issue 3, 2007, Pages 461-475

Divergent evolution of the chloroplast small heat shock protein gene in the genera Rhododendron (Ericaceae) and Machilus (Lauraceae)

Author keywords

Adaptive evolution; Chloroplast small heat shock protein; Machilus; Rhododendron

Indexed keywords

ANGIOSPERM; CHLOROPLAST; DIVERGENCE; EVOLUTION; GENETIC VARIATION; PROTEIN;

EID: 34247891576     PISSN: 03057364     EISSN: 10958290     Source Type: Journal    
DOI: 10.1093/aob/mcl288     Document Type: Article
Times cited : (10)

References (64)
  • 2
    • 0036272936 scopus 로고    scopus 로고
    • Accuracy and power of Bayes prediction of amino acid sites under positive selection
    • Anisimova M, Bielawski JP, Yang Z. 2002. Accuracy and power of Bayes prediction of amino acid sites under positive selection. Molecular Biology and Evolution 19: 950-958.
    • (2002) Molecular Biology and Evolution , vol.19 , pp. 950-958
    • Anisimova, M.1    Bielawski, J.P.2    Yang, Z.3
  • 3
    • 0344099425 scopus 로고    scopus 로고
    • Variation in chloroplast small heat-shock protein function is a major determinant of variation in thermotolerance of photosynthetic electron transport among ecotypes of Chenopodium album
    • Barua D, Heckathorn SA, Downs CA. 2003. Variation in chloroplast small heat-shock protein function is a major determinant of variation in thermotolerance of photosynthetic electron transport among ecotypes of Chenopodium album. Functional Plant Biology 30: 1071-1079.
    • (2003) Functional Plant Biology , vol.30 , pp. 1071-1079
    • Barua, D.1    Heckathorn, S.A.2    Downs, C.A.3
  • 4
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved 'α-crystallin domain'
    • Caspers GJ, Leunissen JAM, de Jong WW. 1995. The expanding small heat-shock protein family, and structure predictions of the conserved 'α-crystallin domain'. Journal of Molecular Evolution 40: 238-248.
    • (1995) Journal of Molecular Evolution , vol.40 , pp. 238-248
    • Caspers, G.J.1    Leunissen, J.A.M.2    de Jong, W.W.3
  • 5
    • 0025764158 scopus 로고
    • Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein
    • Chen Q, Vierling E. 1991. Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein. Molecular and General Genetics 226: 425-431.
    • (1991) Molecular and General Genetics , vol.226 , pp. 425-431
    • Chen, Q.1    Vierling, E.2
  • 6
    • 3242776825 scopus 로고    scopus 로고
    • Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity
    • Chowdary TK, Raman B, Ramakrishna T, Rao CM. 2004. Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity. Biochemistry Journal 381: 379-387.
    • (2004) Biochemistry Journal , vol.381 , pp. 379-387
    • Chowdary, T.K.1    Raman, B.2    Ramakrishna, T.3    Rao, C.M.4
  • 7
    • 33751010187 scopus 로고    scopus 로고
    • Phylogeographic study reveals the origin and evolutionary history of a Rhododendron species complex in Taiwan
    • Chung JD, Lin TP, Chen YL, Cheng YP, Hwang SY. 2007. Phylogeographic study reveals the origin and evolutionary history of a Rhododendron species complex in Taiwan. Molecular Phylogenetics and Evolution 42: 14-24.
    • (2007) Molecular Phylogenetics and Evolution , vol.42 , pp. 14-24
    • Chung, J.D.1    Lin, T.P.2    Chen, Y.L.3    Cheng, Y.P.4    Hwang, S.Y.5
  • 8
    • 0002594984 scopus 로고
    • A rapid DNA isolation procedure for small quantities of fresh leaf material
    • Doyle JJ, Doyle JL. 1987. A rapid DNA isolation procedure for small quantities of fresh leaf material. Phytochemistry Bulletin 19: 11-15.
    • (1987) Phytochemistry Bulletin , vol.19 , pp. 11-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 9
    • 0042708023 scopus 로고    scopus 로고
    • DNA sequence variation and latitudinal associations in hsp23, hsp26 and hsp27 from natural populations of Drosophila melanogaster
    • Frydenberg J, Hoffmann AA, Loeschcke V. 2003. DNA sequence variation and latitudinal associations in hsp23, hsp26 and hsp27 from natural populations of Drosophila melanogaster. Molecular Ecology 12: 2025-2032.
    • (2003) Molecular Ecology , vol.12 , pp. 2025-2032
    • Frydenberg, J.1    Hoffmann, A.A.2    Loeschcke, V.3
  • 10
    • 0034855811 scopus 로고    scopus 로고
    • Chaperone-like activity of α-crystallin and other small heat shock proteins
    • Ganea E. 2001. Chaperone-like activity of α-crystallin and other small heat shock proteins. Current Protein and Peptide Science 2: 205-225.
    • (2001) Current Protein and Peptide Science , vol.2 , pp. 205-225
    • Ganea, E.1
  • 11
    • 25444453179 scopus 로고    scopus 로고
    • SplitTester: Software to identify domains responsible for functional divergence in protein family
    • Gao X, VanderVelden KA, Voytas DF, Gu X. 2005. SplitTester: software to identify domains responsible for functional divergence in protein family. BioMed Central Bioinformatics 6: 137.
    • (2005) BioMed Central Bioinformatics , vol.6 , pp. 137
    • Gao, X.1    VanderVelden, K.A.2    Voytas, D.F.3    Gu, X.4
  • 12
    • 3543039976 scopus 로고    scopus 로고
    • Mutants in a small heat shock protein that affect the oligomeric state
    • Giese KC, Vierling E. 2004. Mutants in a small heat shock protein that affect the oligomeric state. The Journal of Biological Chemistry 279: 32674-32683.
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 32674-32683
    • Giese, K.C.1    Vierling, E.2
  • 13
    • 0036107253 scopus 로고    scopus 로고
    • Evolutionary analysis for functional divergence of Jak protein kinase domains and tissue-specific genes
    • Gu J, Wang Y, Gu X. 2002. Evolutionary analysis for functional divergence of Jak protein kinase domains and tissue-specific genes. Journal of Molecular Evolution 54: 725-733
    • (2002) Journal of Molecular Evolution , vol.54 , pp. 725-733
    • Gu, J.1    Wang, Y.2    Gu, X.3
  • 14
    • 0345009031 scopus 로고    scopus 로고
    • Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer
    • Gustavsson N, Härndahl U, Emanuelsson A, Roepstorff P, Sundby C. 1999. Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer. Protein Science 8: 2506-2512.
    • (1999) Protein Science , vol.8 , pp. 2506-2512
    • Gustavsson, N.1    Härndahl, U.2    Emanuelsson, A.3    Roepstorff, P.4    Sundby, C.5
  • 15
    • 0034841455 scopus 로고    scopus 로고
    • Substitution of conserved methionines by leucines in chloroplast small heat shock protein results in loss of redox-response but retained chaperone-like activity
    • Gustavsson N, Kokke BPA, Anzelius B, Boelens WC, Sundby C. 2001. Substitution of conserved methionines by leucines in chloroplast small heat shock protein results in loss of redox-response but retained chaperone-like activity. Protein Science 10: 1785-1793.
    • (2001) Protein Science , vol.10 , pp. 1785-1793
    • Gustavsson, N.1    Kokke, B.P.A.2    Anzelius, B.3    Boelens, W.C.4    Sundby, C.5
  • 16
    • 34548401215 scopus 로고    scopus 로고
    • Hall TA. 1999. BIOEDIT: a user-friendly biological sequence alignment, editor and analysis program for Windows 95/98/NT. Nucleic Acids Symposium Series 41: 95-98.
    • Hall TA. 1999. BIOEDIT: a user-friendly biological sequence alignment, editor and analysis program for Windows 95/98/NT. Nucleic Acids Symposium Series 41: 95-98.
  • 17
    • 0022376704 scopus 로고
    • Dating of the human-ape splitting by a molecular clock of mitochondrial DNA
    • Hasegawa M, Kishino H, Yano TA. 1985. Dating of the human-ape splitting by a molecular clock of mitochondrial DNA. Journal of Molecular Evolution 22: 160-174.
    • (1985) Journal of Molecular Evolution , vol.22 , pp. 160-174
    • Hasegawa, M.1    Kishino, H.2    Yano, T.A.3
  • 19
    • 0031757704 scopus 로고    scopus 로고
    • The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress
    • Heckathorn SA, Downs CA, Sharkey TD, Coleman JS. 1998. The small, methionine-rich chloroplast heat-shock protein protects photosystem II electron transport during heat stress. Plant Physiology 116: 439-444.
    • (1998) Plant Physiology , vol.116 , pp. 439-444
    • Heckathorn, S.A.1    Downs, C.A.2    Sharkey, T.D.3    Coleman, J.S.4
  • 21
    • 3543058331 scopus 로고    scopus 로고
    • Composition, endemism and phytogeographical affinities of the Taiwan flora
    • Hsieh CF. 2002. Composition, endemism and phytogeographical affinities of the Taiwan flora. Taiwania 47: 298-310.
    • (2002) Taiwania , vol.47 , pp. 298-310
    • Hsieh, C.F.1
  • 22
    • 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
  • 23
    • 0035466407 scopus 로고    scopus 로고
    • Molecular phylogeny of eight Taiwanese Rhododendron species based on chloroplast trnF-trnL DNA sequences
    • in Chinese with English summary
    • Hwang SY, Hsu KK. 2001. Molecular phylogeny of eight Taiwanese Rhododendron species based on chloroplast trnF-trnL DNA sequences. Taiwan Journal of Forest Science 16: 153-160 (in Chinese with English summary).
    • (2001) Taiwan Journal of Forest Science , vol.16 , pp. 153-160
    • Hwang, S.Y.1    Hsu, K.K.2
  • 24
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • Jones DT, Taylor WR, Thornton JM. 1992. A new approach to protein fold recognition. Nature 358: 86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 26
    • 8744268628 scopus 로고    scopus 로고
    • Duplicated genes evolve slower than singletons despite the initial rate increase
    • Jordan IK, Wolf YI, Koonin EV. 2004. Duplicated genes evolve slower than singletons despite the initial rate increase. BioMed Central Evolutionary Biology 4: 22.
    • (2004) BioMed Central Evolutionary Biology , vol.4 , pp. 22
    • Jordan, I.K.1    Wolf, Y.I.2    Koonin, E.V.3
  • 27
    • 0019296687 scopus 로고
    • A simple method for estimating evolutionary rate of base substitution through comparative studies of nucleotide sequences
    • Kimura M. 1980. A simple method for estimating evolutionary rate of base substitution through comparative studies of nucleotide sequences. Journal of Molecular Evolution 16: 111-120.
    • (1980) Journal of Molecular Evolution , vol.16 , pp. 111-120
    • Kimura, M.1
  • 28
    • 0002819133 scopus 로고    scopus 로고
    • Correlated evolution of chloroplast heat shock protein expression in closely related plant species
    • Knight CA, Ackerly DD. 2001. Correlated evolution of chloroplast heat shock protein expression in closely related plant species. American Journal of Botany 88: 411-418.
    • (2001) American Journal of Botany , vol.88 , pp. 411-418
    • Knight, C.A.1    Ackerly, D.D.2
  • 29
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: Integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S, Tamura K, Nei M. 2004. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Briefings in Bioinformatics 5: 150-163.
    • (2004) Briefings in Bioinformatics , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 30
    • 0035807886 scopus 로고    scopus 로고
    • A likelihood ratio test for evolutionary rate shifts and functional divergence among proteins
    • Kundsen B, Miyamoto M. 2001. A likelihood ratio test for evolutionary rate shifts and functional divergence among proteins. Proceedings of the National Academy of Sciences of the USA 98: 14512-14517.
    • (2001) Proceedings of the National Academy of Sciences of the USA , vol.98 , pp. 14512-14517
    • Kundsen, B.1    Miyamoto, M.2
  • 31
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle R. 1982. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 157: 105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.2
  • 32
    • 0003421005 scopus 로고    scopus 로고
    • Sunderland, MA: Sinauer Associates
    • Li WH. 1997. Molecular evolution. Sunderland, MA: Sinauer Associates.
    • (1997) Molecular evolution
    • Li, W.H.1
  • 33
    • 0034594704 scopus 로고    scopus 로고
    • Heat-induced conformational change of human lens recombinant αA- and αB-crystallins
    • Liang JJ, Sun TX, Akhtar NJ. 2000. Heat-induced conformational change of human lens recombinant αA- and αB-crystallins. Molecular Vision 6: 10-14.
    • (2000) Molecular Vision , vol.6 , pp. 10-14
    • Liang, J.J.1    Sun, T.X.2    Akhtar, N.J.3
  • 34
  • 35
    • 4744343021 scopus 로고    scopus 로고
    • The altered evolutionary trajectories of gene duplicates
    • Lynch L, Katju V. 2004. The altered evolutionary trajectories of gene duplicates. Trends in Genetics 20: 544-549.
    • (2004) Trends in Genetics , vol.20 , pp. 544-549
    • Lynch, L.1    Katju, V.2
  • 36
    • 0034634395 scopus 로고    scopus 로고
    • The evolutionary fate and consequences of duplicate genes
    • Lynch M, Conery JS. 2000. The evolutionary fate and consequences of duplicate genes. Science 290: 1151-1154.
    • (2000) Science , vol.290 , pp. 1151-1154
    • Lynch, M.1    Conery, J.S.2
  • 37
    • 0035930948 scopus 로고    scopus 로고
    • Site-directed mutation on the only universally conserved residue Leu122 of small heat shock protein Hsp16.3
    • Mao Q, Chang Z. 2001. Site-directed mutation on the only universally conserved residue Leu122 of small heat shock protein Hsp16.3. Biochemical and Biophysical Research Communications 289: 1257-1261.
    • (2001) Biochemical and Biophysical Research Communications , vol.289 , pp. 1257-1261
    • Mao, Q.1    Chang, Z.2
  • 38
    • 33745562481 scopus 로고    scopus 로고
    • Genetic mechanisms and evolutionary significance of natural variation in Arabidopsis
    • Mitchell-Olds T, Schmitt J. 2006. Genetic mechanisms and evolutionary significance of natural variation in Arabidopsis. Nature 441: 947-952.
    • (2006) Nature , vol.441 , pp. 947-952
    • Mitchell-Olds, T.1    Schmitt, J.2
  • 39
    • 0025936264 scopus 로고
    • Multigene families and the evolution of complexity
    • Ohta T. 1991. Multigene families and the evolution of complexity. Journal of Molecular Evolution 33: 34-41.
    • (1991) Journal of Molecular Evolution , vol.33 , pp. 34-41
    • Ohta, T.1
  • 40
    • 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
  • 41
    • 0034988391 scopus 로고    scopus 로고
    • Selecting models of nucleotide substitution: An application to the human immunodeficiency virus 1 (HIV-1)
    • Posada D, Crandall KA. 2001. Selecting models of nucleotide substitution: an application to the human immunodeficiency virus 1 (HIV-1). Molecular Biology and Evolution 18: 897-906.
    • (2001) Molecular Biology and Evolution , vol.18 , pp. 897-906
    • Posada, D.1    Crandall, K.A.2
  • 42
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP. 2003. MrBayes 3: bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 44
    • 0037387451 scopus 로고    scopus 로고
    • Significantly different patterns of amino acid replacement after gene duplication as compared to after speciation
    • Seoighe C, Johnston CR, Shields DC. 2003. Significantly different patterns of amino acid replacement after gene duplication as compared to after speciation. Molecular Biology and Evoution. 20: 484-490.
    • (2003) Molecular Biology and Evoution , vol.20 , pp. 484-490
    • Seoighe, C.1    Johnston, C.R.2    Shields, D.C.3
  • 45
    • 0032502739 scopus 로고    scopus 로고
    • Interaction of 1,1′Bi(4-anilino)naphthalene-5,5′-Disulfonic acid with α-crystallin
    • Sharma KK, Kaur H, Kumar GS, Kester K. 1998. Interaction of 1,1′Bi(4-anilino)naphthalene-5,5′-Disulfonic acid with α-crystallin. Journal of Biological Chemistry 273: 8965-8970.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 8965-8970
    • Sharma, K.K.1    Kaur, H.2    Kumar, G.S.3    Kester, K.4
  • 46
    • 0033537845 scopus 로고    scopus 로고
    • Biochemical characterization of the small heat shock proteins IbpB from Escherichia coli
    • Shearstone J, Baneyx F. 1999. Biochemical characterization of the small heat shock proteins IbpB from Escherichia coli. Journal of Biological Chemistry 274: 9937-9945.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 9937-9945
    • Shearstone, J.1    Baneyx, F.2
  • 47
    • 0242574386 scopus 로고    scopus 로고
    • The evolutionary and ecological role of heat shock proteins
    • Sørensen JG, Kristensen TN, Loeschcke V. 2003. The evolutionary and ecological role of heat shock proteins. Ecology Letters 6: 1025-1037.
    • (2003) Ecology Letters , vol.6 , pp. 1025-1037
    • Sørensen, J.G.1    Kristensen, T.N.2    Loeschcke, V.3
  • 50
    • 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 Research 25: 4876-4882.
    • (1997) Nucleic Acids Research , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 51
  • 53
    • 0036792156 scopus 로고    scopus 로고
    • Asymmetric functional divergence of duplicate genes
    • Wagner A. 2002. Asymmetric functional divergence of duplicate genes. Molecular Biology and Evolution 19: 1760-1768.
    • (2002) Molecular Biology and Evolution , vol.19 , pp. 1760-1768
    • Wagner, A.1
  • 54
    • 0029112270 scopus 로고
    • The molecular evolution of the small heat-shock proteins in plants
    • Waters ER. 1995. The molecular evolution of the small heat-shock proteins in plants. Genetics 141: 785-795.
    • (1995) Genetics , vol.141 , pp. 785-795
    • Waters, E.R.1
  • 55
    • 0033453223 scopus 로고    scopus 로고
    • Chloroplast small heart shock proteins: Evidence for atypical evolution of an organelle-localized protein
    • Waters ER, Vierling E. 1999. Chloroplast small heart shock proteins: evidence for atypical evolution of an organelle-localized protein. Proceedings of the National Academy of Sciences of the USA 96: 14394-14399.
    • (1999) Proceedings of the National Academy of Sciences of the USA , vol.96 , pp. 14394-14399
    • Waters, E.R.1    Vierling, E.2
  • 56
    • 0030068653 scopus 로고    scopus 로고
    • Evolution, structure and function of the small heat shock proteins in plants
    • Waters ER, Lee GJ, Vierling E. 1996. Evolution, structure and function of the small heat shock proteins in plants. Journal of Experimental Botany 47: 325-338.
    • (1996) Journal of Experimental Botany , vol.47 , pp. 325-338
    • Waters, E.R.1    Lee, G.J.2    Vierling, E.3
  • 57
    • 14544306215 scopus 로고    scopus 로고
    • Molecular population genetics and the search for adaptive evolution in plants
    • Wright SI, Gaut BS. 2005. Molecular population genetics and the search for adaptive evolution in plants. Molecular Biology and Evolution 22: 506-519.
    • (2005) Molecular Biology and Evolution , vol.22 , pp. 506-519
    • Wright, S.I.1    Gaut, B.S.2
  • 58
    • 13144252278 scopus 로고    scopus 로고
    • Asymmetric evolution of duplicate genes encoding the CCAAT-binding factor NF-Y in plant genomes
    • Yang J, Xie Z, Blover BJ. 2005. Asymmetric evolution of duplicate genes encoding the CCAAT-binding factor NF-Y in plant genomes. New Phytologist 165: 623-631.
    • (2005) New Phytologist , vol.165 , pp. 623-631
    • Yang, J.1    Xie, Z.2    Blover, B.J.3
  • 59
    • 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. Computer Applications in Biosciences 13: 555-556.
    • (1997) Computer Applications in Biosciences , vol.13 , pp. 555-556
    • Yang, Z.1
  • 60
    • 0031960185 scopus 로고    scopus 로고
    • Synonymous and nonsynonymous rate variation in nuclear genes of mammals
    • Yang Z, Nielsen R. 1998. Synonymous and nonsynonymous rate variation in nuclear genes of mammals. Journal of Molecular Evolution 46: 409-418.
    • (1998) Journal of Molecular Evolution , vol.46 , pp. 409-418
    • Yang, Z.1    Nielsen, R.2
  • 61
    • 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. Molecular Biology and Evolution 19: 908-917.
    • (2002) Molecular Biology and Evolution , vol.19 , pp. 908-917
    • Yang, Z.1    Nielsen, R.2
  • 62
    • 0034097381 scopus 로고    scopus 로고
    • Codon-substitution models for heterogeneous selection pressure at amino acid sites
    • Yang Z, Nielsen R, Goldman N, Pedersen AMK. 2003. Codon-substitution models for heterogeneous selection pressure at amino acid sites. Genetics 22: 431-449.
    • (2003) Genetics , vol.22 , pp. 431-449
    • Yang, Z.1    Nielsen, R.2    Goldman, N.3    Pedersen, A.M.K.4
  • 63
    • 0037500141 scopus 로고    scopus 로고
    • Evolution by gene duplication: An update
    • Zhang J. 2003. Evolution by gene duplication: an update. Trends in Ecology and Evolution 18: 292-298.
    • (2003) Trends in Ecology and Evolution , vol.18 , pp. 292-298
    • Zhang, J.1
  • 64
    • 0036811122 scopus 로고    scopus 로고
    • Population genetics of duplicated disease-defense genes, hm1 and hm2, in Maize (Zea mays ssp. mays L.) and its wild ancestor (Zea mays ssp. parviglumis)
    • Zhang L, Peek AS, Dunams D, Gaut BS. 2002. Population genetics of duplicated disease-defense genes, hm1 and hm2, in Maize (Zea mays ssp. mays L.) and its wild ancestor (Zea mays ssp. parviglumis). Genetics 162: 851-860.
    • (2002) Genetics , vol.162 , pp. 851-860
    • Zhang, L.1    Peek, A.S.2    Dunams, D.3    Gaut, B.S.4


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