메뉴 건너뛰기




Volumn 109, Issue 4, 2012, Pages 693-708

Accelerated evolution and coevolution drove the evolutionary history of AGPase sub-units during angiosperm radiation

Author keywords

AGPase; Angiosperms; coevolution; dicotyledons; molecular evolution; monocotyledons; neofunctionalization; paralogue genes; starch synthesis; subfunctionalization

Indexed keywords

GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; STARCH;

EID: 84857719341     PISSN: 03057364     EISSN: 10958290     Source Type: Journal    
DOI: 10.1093/aob/mcr303     Document Type: Article
Times cited : (9)

References (87)
  • 1
    • 33747891709 scopus 로고    scopus 로고
    • Evolutionary rate variation among vertebrate β globin genes: Implications for dating gene family duplication events
    • DOI 10.1016/j.gene.2006.04.019, PII S0378111906002939
    • Aguileta G, Bielawski JP, Yang Z. 2006. Evolutionary rate variation among vertebrate beta globin genes: Implications for dating gene family duplication events. Gene 380: 21-29. (Pubitemid 44293156)
    • (2006) Gene , vol.380 , Issue.1 , pp. 21-29
    • Aguileta, G.1    Bielawski, J.P.2    Yang, Z.3
  • 2
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus
    • Altschuh D, Lesk AM, Bloomer AC, Klug A. 1987. Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. Journal of Molecular Biology 193: 693-707.
    • (1987) Journal of Molecular Biology , vol.193 , pp. 693-707
    • Altschuh, D.1    Lesk, A.M.2    Bloomer, A.C.3    Klug, A.4
  • 3
    • 0033977832 scopus 로고    scopus 로고
    • Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis
    • Atchley WR, Wollenberg KR, Fitch WM, Terhalle W, Dress AW. 2000. Correlations among amino acid sites in bHLH protein domains: An information theoretic analysis. Molecular Biology and Evolution 17: 164-178. (Pubitemid 30057002)
    • (2000) Molecular Biology and Evolution , vol.17 , Issue.1 , pp. 164-178
    • Atchley, W.R.1    Wollenberg, K.R.2    Fitch, W.M.3    Terhalle, W.4    Dress, A.W.5
  • 4
    • 0029360584 scopus 로고
    • Adenosine 5'-diphosphate-glucose pyrophosphorylase from potato tuber. Significance of the N terminus of the small subunit for catalytic properties and heat stability
    • Ballicora MA, Laughlin MJ, Fu Y, Okita TW, Barry GF, Preiss J. 1995. Adenosine 5'-diphosphate-glucose pyrophosphorylase from potato tuber. Significance of the N terminus of the small subunit for catalytic properties and heat stability. Plant Physiology 109: 245-251.
    • (1995) Plant Physiology , vol.109 , pp. 245-251
    • Ballicora, M.A.1    Laughlin, M.J.2    Fu, Y.3    Okita, T.W.4    Barry, G.F.5    Preiss, J.6
  • 5
    • 0032161364 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sites
    • Ballicora MA, Fu YB, Nesbitt NM, Preiss J. 1998. ADP-glucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sites. Plant Physiology 118: 265-274. (Pubitemid 128652989)
    • (1998) Plant Physiology , vol.118 , Issue.1 , pp. 265-274
    • Ballicora, M.A.1    Fu, Y.2    Nesbitt, N.M.3    Preiss, J.4
  • 6
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis
    • DOI 10.1128/MMBR.67.2.213-225.2003
    • Ballicora MA, Iglesias AA, Preiss J. 2003. ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Microbiology and Molecular Biology Reviews 67: 213-225. (Pubitemid 36693472)
    • (2003) Microbiology and Molecular Biology Reviews , vol.67 , Issue.2 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 7
    • 0442314288 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
    • DOI 10.1023/B:PRES.0000011916.67519.58
    • Ballicora MA, Iglesias AA, Preiss J. 2004. ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis. Photosynthesis Research 79: 1-24. (Pubitemid 38184772)
    • (2004) Photosynthesis Research , vol.79 , Issue.1 , pp. 1-24
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 8
    • 73549111066 scopus 로고    scopus 로고
    • Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase
    • Baris I, Tuncel A, Ozber N, Keskin O, Kavakli IH. 2009. Investigation of the interaction between the large and small subunits of potato ADP-glucose pyrophosphorylase. PLoS Computational Biology 5: Pe1000546. http://dx.doi.org/ 10.1371/journal.pcbi.1000546.
    • (2009) PLoS Computational Biology , vol.5
    • Baris, I.1    Tuncel, A.2    Ozber, N.3    Keskin, O.4    Kavakli, I.H.5
  • 9
    • 0035109466 scopus 로고    scopus 로고
    • A cytosolic ADP-glucose pyrophosphorylase is a feature of graminaceous endosperms, but not of other starch-storing organs
    • DOI 10.1104/pp.125.2.818
    • Beckles DM, Smith AM, and Rees T. 2001. A cytosolic ADP-glucose pyrophosphorylase is a feature of graminaceous endosperms, but not of other starch-storing organs. Plant Physiology 125: 818-827. (Pubitemid 32169889)
    • (2001) Plant Physiology , vol.125 , Issue.2 , pp. 818-827
    • Beckles, D.M.1    Smith, A.M.2    Ap Rees, T.3
  • 10
    • 44449101058 scopus 로고    scopus 로고
    • Evidence that strong positive selection drives neofunctionalization in the tandemly duplicated polyhomeotic genes in Drosophila
    • DOI 10.1073/pnas.0710892105
    • Beisswanger S, Stephan W. 2008. Evidence that strong positive selection drives neofunctionalization in the tandemly duplicated polyhomeotic genes in Drosophila. Proceedings of the National Academy of Sciences, USA 105: 5447-5452. (Pubitemid 351753883)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.14 , pp. 5447-5452
    • Beisswanger, S.1    Stephan, W.2
  • 12
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y. 1995. Controlling the false discovery rate: A practical and powerful approach to multiple testing. Journal of the Royal Statistical Society Series B 57: 289-300.
    • (1995) Journal of the Royal Statistical Society Series B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 14
    • 0028832687 scopus 로고
    • Covariation of residues in the homeodomain sequence family
    • Clarke ND. 1995. Covariation of residues in the homeodomain sequence family. Protein Science 4: 2269-2278.
    • (1995) Protein Science , vol.4 , pp. 2269-2278
    • Clarke, N.D.1
  • 15
    • 67649324673 scopus 로고    scopus 로고
    • The evolution of the starch biosynthetic pathway in cereals and other grasses
    • Comparot-Moss S, Denyer K. 2009. The evolution of the starch biosynthetic pathway in cereals and other grasses. Journal of Experimental Botany 60: 2481-2492.
    • (2009) Journal of Experimental Botany , vol.60 , pp. 2481-2492
    • Comparot-Moss, S.1    Denyer, K.2
  • 16
    • 56549119570 scopus 로고    scopus 로고
    • Turning a hobby into a job: How duplicated genes find new functions
    • DOI 10.1038/nrg2482, PII NRG2482
    • Conant GC, Wolfe KH. 2008. Turning a hobby into a job: How duplicated genes find new functions. Nature Reviews Genetics 9: 938-950. (Pubitemid 352719432)
    • (2008) Nature Reviews Genetics , vol.9 , Issue.12 , pp. 938-950
    • Conant, G.C.1    Wolfe, K.H.2
  • 17
    • 14644409834 scopus 로고    scopus 로고
    • A polymorphic motif in the small subunit of ADP-glucose pyrophosphorylase modulates interactions between the small and large subunits
    • Cross JM, Clancy M, Shaw JR, et al. A polymorphic motif in the small subunit of ADP-glucose pyrophosphorylase modulates interactions between the small and large subunits. The Plant Journal 41: 501-511.
    • The Plant Journal , vol.41 , pp. 501-511
    • Cross, J.M.1    Clancy, M.2    Shaw, J.R.3
  • 19
    • 0030267532 scopus 로고    scopus 로고
    • The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial
    • Denyer K, Dunlap F, Thorbjornsen T, Keeling P, Smith AM. 1996. The major form of ADP-glucose pyrophosphorylase in maize endosperm is extra-plastidial. Plant Physiology 112: 779-785.
    • (1996) Plant Physiology , vol.112 , pp. 779-785
    • Denyer, K.1    Dunlap, F.2    Thorbjornsen, T.3    Keeling, P.4    Smith, A.M.5
  • 20
    • 49649114289 scopus 로고    scopus 로고
    • Escape from adaptive conflict after duplication in an anthocyanin pathway gene
    • Des Marais DL, Rausher MD. 2008. Escape from adaptive conflict after duplication in an anthocyanin pathway gene. Nature 454: 762-765.
    • (2008) Nature , vol.454 , pp. 762-765
    • Des Marais, D.L.1    Rausher, M.D.2
  • 23
    • 39649100613 scopus 로고    scopus 로고
    • Detecting groups of coevolving positions in a molecule: A clustering approach
    • Dutheil J, Galtier N. 2007. Detecting groups of coevolving positions in a molecule: A clustering approach. BMC Evolutionary Biology 7: 242. http://dx.doi.org/10.1186/1471-2148-7-242.
    • (2007) BMC Evolutionary Biology , vol.7 , pp. 242
    • Dutheil, J.1    Galtier, N.2
  • 24
    • 33751017993 scopus 로고    scopus 로고
    • CAPS: Coevolution analysis using protein sequences
    • DOI 10.1093/bioinformatics/btl493
    • Fares MA, McNally D. 2006. CAPS: Coevolution analysis using protein sequences. Bioinformatics 22: 2821-2822. (Pubitemid 44742405)
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2821-2822
    • Fares, M.A.1    McNally, D.2
  • 26
    • 67650915748 scopus 로고    scopus 로고
    • Gene duplication and evolutionary novelty in plants
    • Flagel L, Wendel J. 2009. Gene duplication and evolutionary novelty in plants. New Phytologist 183: 557-564.
    • (2009) New Phytologist , vol.183 , pp. 557-564
    • Flagel, L.1    Wendel, J.2
  • 27
    • 0032893932 scopus 로고    scopus 로고
    • Preservation of duplicate genes by complementary, degenerative mutations
    • Force A, Lynch M, Pickett FB, Amores A, Yan YL, Postlethwait J. 1999. Preservation of duplicate genes by complementary, degenerative mutations. Genetics 151: 1531-1545. (Pubitemid 29177561)
    • (1999) Genetics , vol.151 , Issue.4 , pp. 1531-1545
    • Force, A.1    Lynch, M.2    Pickett, F.B.3    Amores, A.4    Yan, Y.-L.5    Postlethwait, J.6
  • 28
    • 0037327287 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase from potato tuber: Site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits
    • DOI 10.1046/j.1365-313X.2003.01643.x
    • Frueauf JB, Ballicora MA, Preiss J. 2003. ADP-glucose pyrophosphorylase from potato tuber: Site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits. The Plant Journal 33: 503-511. (Pubitemid 36251191)
    • (2003) Plant Journal , vol.33 , Issue.3 , pp. 503-511
    • Frueauf, J.B.1    Ballicora, M.A.2    Preiss, J.3
  • 29
    • 0001571196 scopus 로고    scopus 로고
    • Mutagenesis of the glucose-1-phosphate-binding site of potato tuber ADP-glucose pyrophosphorylase
    • Fu Y, Ballicora MA, Preiss J. 1998. Mutagenesis of the glucose-1-phosphate-binding site of potato tuber ADP-glucose pyrophosphorylase. Plant Physiology 117: 989-996. (Pubitemid 128652872)
    • (1998) Plant Physiology , vol.117 , Issue.3 , pp. 989-996
    • Fu, Y.1    Ballicora, M.A.2    Preiss, J.3
  • 30
    • 34347388786 scopus 로고    scopus 로고
    • The two AGPase subunits evolve at different rates in angiosperms, yet they are equally sensitive to activity-altering amino acid changes when expressed in bacteria
    • DOI 10.1105/tpc.106.049676
    • Georgelis N, Braun EL, Shaw JR, Hannah LC. 2007. The two AGPase subunits evolve at different rates in angiosperms, yet they are equally sensitive to activity-altering amino acid changes when expressed in bacteria. The Plant Cell 19: 1458-1472. (Pubitemid 47025370)
    • (2007) Plant Cell , vol.19 , Issue.5 , pp. 1458-1472
    • Georgelis, N.1    Braun, E.L.2    Shaw, J.R.3    Hannah, L.C.4
  • 31
    • 51249092997 scopus 로고    scopus 로고
    • Duplications and functional divergence of ADP-glucose pyrophosphorylase genes in plants
    • Georgelis N, Braun EL, Hannah LC. 2008. Duplications and functional divergence of ADP-glucose pyrophosphorylase genes in plants. BMC Evolutionary Biology 8: 232. http://dx.doi.org/10.1186/1471-2148-8-232.
    • (2008) BMC Evolutionary Biology , vol.8 , pp. 232
    • Georgelis, N.1    Braun, E.L.2    Hannah, L.C.3
  • 32
    • 70349223021 scopus 로고    scopus 로고
    • Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme
    • Georgelis N, Shaw JR, Hannah LC. 2009. Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme. Plant Physiology 151: 67-77.
    • (2009) Plant Physiology , vol.151 , pp. 67-77
    • Georgelis, N.1    Shaw, J.R.2    Hannah, L.C.3
  • 33
    • 18544362952 scopus 로고    scopus 로고
    • Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions
    • DOI 10.1021/bi050293e
    • Gloor GB, Martin LC, Wahl LM, Dunn SD. 2005. Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions. Biochemistry 44: 7156-7165. (Pubitemid 40656660)
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 7156-7165
    • Gloor, G.B.1    Martin, L.C.2    Wahl, L.M.3    Dunn, S.D.4
  • 34
    • 0036435908 scopus 로고    scopus 로고
    • Co-evolutionary analysis reveals insights into protein-protein interactions
    • DOI 10.1016/S0022-2836(02)01038-0
    • Goh CS, Cohen FE. 2002. Co-evolutionary analysis reveals insights into protein-protein interactions. Journal of Molecular Biology 324: 177-192. (Pubitemid 35352188)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.1 , pp. 177-192
    • Goh, C.-S.1    Cohen, F.E.2
  • 36
    • 0016197604 scopus 로고
    • Amino acid difference formula to help explain protein evolution
    • Grantham R. 1974. Amino acid difference formula to help explain protein evolution. Science 185: 862-864.
    • (1974) Science , vol.185 , pp. 862-864
    • Grantham, R.1
  • 38
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. 2010. New algorithms and methods to estimate maximum-likelihood phylogenies: Assessing the performance of PhyML 3.0. Systematic Biology 59: 307-321.
    • (2010) Systematic Biology , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 39
    • 66049128566 scopus 로고    scopus 로고
    • Distinguishing among evolutionary models for the maintenance of gene duplicates
    • Hahn MW. 2009. Distinguishing among evolutionary models for the maintenance of gene duplicates. Journal of Heredity 100: 605-617.
    • (2009) Journal of Heredity , vol.100 , pp. 605-617
    • Hahn, M.W.1
  • 40
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: Evolutionary units of three-dimensional structure
    • Halabi N, Rivoire O, Leibler S, Ranganathan R. 2009. Protein sectors: Evolutionary units of three-dimensional structure. Cell 138: 774-786.
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Leibler, S.3    Ranganathan, R.4
  • 42
    • 0142214642 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of arabidopsis and other plant species
    • DOI 10.1104/pp.103.024513
    • Hendriks JH, Kolbe A, Gibon Y, Stitt M, Geigenberger P. 2003. ADP-glucose pyrophosphorylase is activated by posttranslational redoxmodification in response to light and to sugars in leaves of Arabidopsis and other plant species. Plant Physiology 133: 838-849. (Pubitemid 37325692)
    • (2003) Plant Physiology , vol.133 , Issue.2 , pp. 838-849
    • Hendriks, J.H.M.1    Kolbe, A.2    Gibon, Y.3    Stitt, M.4    Geigenberger, P.5
  • 43
    • 0025775694 scopus 로고
    • Biosynthesis of bacterial glycogen mutagenesis of a catalytic site residue of adp-glucose pyrophosphorylase from escherichia coli
    • Hill MA, Kaufmann K, Otero J, Preiss J. 1991. Biosynthesis of bacterial glycogen. Mutagenesis of a catalytic site residue of ADP-glucose pyrophosphorylase from Escherichia coli. Journal of Biological Chemistry 266: 12455-12460. (Pubitemid 21907116)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.19 , pp. 12455-12460
    • Hill, M.A.1    Kaufmann, K.2    Otero, J.3    Preiss, J.4
  • 44
    • 0028342845 scopus 로고
    • The evolution of functionally novel proteins after gene duplication
    • DOI 10.1098/rspb.1994.0058
    • Hughes AL. 1994. The evolution of functionally novel proteins after gene duplication. Proceedings of the Royal Society B: Biological Sciences 256: 119-124. (Pubitemid 24168165)
    • (1994) Proceedings of the Royal Society B: Biological Sciences , vol.256 , Issue.1346 , pp. 119-124
    • Hughes, A.L.1
  • 45
    • 13844261305 scopus 로고    scopus 로고
    • Allosteric regulation of the higher plant ADP-glucose pyrophosphorylase is a product of synergy between the two subunits
    • DOI 10.1016/j.febslet.2004.12.067
    • Hwang SK, Salamone PR, Okita TW. 2005. Allosteric regulation of the higher plant ADP-glucose pyrophosphorylase is a product of synergy between the two subunits. FEBS Letters 579: 983-990. (Pubitemid 40248657)
    • (2005) FEBS Letters , vol.579 , Issue.5 , pp. 983-990
    • Hwang, S.-K.1    Salamone, P.R.2    Okita, T.W.3
  • 46
    • 33846581912 scopus 로고    scopus 로고
    • Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit
    • DOI 10.1016/j.phytochem.2006.11.027, PII S0031942206007333
    • Hwang SK, Hamada S, Okita TW. 2007. Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit. Phytochemistry 68: 464-477. (Pubitemid 46186448)
    • (2007) Phytochemistry , vol.68 , Issue.4 , pp. 464-477
    • Hwang, S.-K.1    Hamada, S.2    Okita, T.W.3
  • 47
    • 0001172247 scopus 로고
    • The rb mutation of peas causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos
    • Hylton C, Smith AM. 1992. The rb mutation of peas causes structural and regulatory changes in ADP glucose pyrophosphorylase from developing embryos. Plant Physiology 99: 1626-1634.
    • (1992) Plant Physiology , vol.99 , pp. 1626-1634
    • Hylton, C.1    Smith, A.M.2
  • 48
    • 15444377849 scopus 로고    scopus 로고
    • Crystal structure of potato tuber ADP-glucose pyrophosphorylase
    • DOI 10.1038/sj.emboj.7600551
    • Jin X, Ballicora MA, Preiss J, Geiger JH. 2005. Crystal structure of potato tuber ADP-glucose pyrophosphorylase. EMBO Journal 24: 694-704. (Pubitemid 40396100)
    • (2005) EMBO Journal , vol.24 , Issue.4 , pp. 694-704
    • Jin, X.1    Ballicora, M.A.2    Preies, J.3    Geiger, J.H.4
  • 49
    • 0025895035 scopus 로고
    • Subunit interactions control protein phosphatase 2A: Effcts of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit
    • Kamibayashi C, Estes R, Slaughter C, Mumby MC. 1991. Subunit interactions control protein phosphatase 2A. Effects of limited proteolysis, N-ethylmaleimide, and heparin on the interaction of the B subunit. Journal of Biological Chemistry 266: 13251-13260. (Pubitemid 21907336)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.20 , pp. 13251-13260
    • Kamibayashi, C.1    Estes, R.2    Slaughter, C.3    Mumby, M.C.4
  • 50
    • 34548241238 scopus 로고    scopus 로고
    • Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase
    • DOI 10.1016/j.bbrc.2007.07.162, PII S0006291X07016075
    • Kim D, Hwang SK, Okita TW. 2007. Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase. Biochemical and Biophysical Research Communications 362: 301-306. (Pubitemid 47332405)
    • (2007) Biochemical and Biophysical Research Communications , vol.362 , Issue.2 , pp. 301-306
    • Kim, D.1    Hwang, S.-K.2    Okita, T.W.3
  • 51
    • 0019296687 scopus 로고
    • A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences
    • DOI 10.1007/BF01731581
    • Kimura M. 1980. A simple method for estimating evolutionary rates of base substitutions through comparative studies of nucleotide sequences. Journal of Molecular Evolution 16: 111-120. (Pubitemid 11166431)
    • (1980) Journal of Molecular Evolution , vol.16 , Issue.2 , pp. 111-120
    • Kimura, M.1
  • 52
    • 0345107239 scopus 로고    scopus 로고
    • Selection in the evolution of gene duplications
    • research0008.
    • Kondrashov FA, Rogozin IB, Wolf YI, Koonin EV. 2002. Selection in the evolution of gene duplications. Genome Biology 3: Research0008. http://dx.doi.org/10.1186/gb-2002-3-2-research0008.
    • (2002) Genome Biology , vol.3
    • Kondrashov, F.A.1    Rogozin, I.B.2    Wolf, Y.I.3    Koonin, E.V.4
  • 53
    • 77958114505 scopus 로고    scopus 로고
    • An integrated view of molecular coevolution in protein-protein interactions
    • Lovell SC, Robertson DL. 2010. An integrated view of molecular coevolution in protein-protein interactions. Molecular Biology and Evolution 27: 2567-2575.
    • (2010) Molecular Biology and Evolution , vol.27 , pp. 2567-2575
    • Lovell, S.C.1    Robertson, D.L.2
  • 54
    • 0033972072 scopus 로고    scopus 로고
    • The probability of duplicate gene preservation by subfunctionalization
    • Lynch M, Force A. 2000. The probability of duplicate gene preservation by subfunctionalization. Genetics 154: 459-473. (Pubitemid 30045935)
    • (2000) Genetics , vol.154 , Issue.1 , pp. 459-473
    • Lynch, M.1    Force, A.2
  • 56
    • 45549091203 scopus 로고    scopus 로고
    • Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive docking
    • DOI 10.1073/pnas.0707032105
    • Madaoui H, Guerois R. 2008. Coevolution at protein complex interfaces can be detected by the complementarity trace with important impact for predictive docking. Proceedings of the National Academy of Sciences, USA 105: 7708-7713. (Pubitemid 351872703)
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.22 , pp. 7708-7713
    • Madaoui, H.1    Guerois, R.2
  • 57
    • 0031504952 scopus 로고    scopus 로고
    • Gene trees in species trees
    • Maddison WP. 1997. Gene trees in species trees. Systematic Biology 46: 523-536.
    • (1997) Systematic Biology , vol.46 , pp. 523-536
    • Maddison, W.P.1
  • 59
    • 0033616825 scopus 로고    scopus 로고
    • Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization
    • DOI 10.1073/pnas.96.7.3595
    • Mateu MG, Fersht AR. 1999. Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization. Proceedings of the National Academy of Sciences, USA 96: 3595-3599. (Pubitemid 29168955)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.7 , pp. 3595-3599
    • Mateu, M.G.1    Fersht, A.R.2
  • 61
    • 0036737630 scopus 로고    scopus 로고
    • Impact of the presence of paralogs on sequence divergence in a set of mouse-human orthologs
    • Nembaware V, Crum K, Kelso J, Seoighe C. 2002. Impact of the presence of paralogs on sequence divergence in a set of mouse-human orthologs. Genome Research 12: 1370-1376.
    • (2002) Genome Research , vol.12 , pp. 1370-1376
    • Nembaware, V.1    Crum, K.2    Kelso, J.3    Seoighe, C.4
  • 62
    • 84857699479 scopus 로고
    • Evolution by gene duplication berlin: Springer-verlag. Otto SP. 2007. The evolutionary consequences of polyploidy
    • Ohno S. 1970. Evolution by gene duplication. Berlin: Springer-Verlag. Otto SP. 2007. The evolutionary consequences of polyploidy. Cell, 131: 452-462.
    • (1970) Cell , vol.131 , pp. 452-462
    • Ohno, S.1
  • 63
    • 0030821675 scopus 로고    scopus 로고
    • Correlated mutations contain information about protein - protein interaction
    • DOI 10.1006/jmbi.1997.1198
    • Pazos F, Helmer-Citterich M, Ausiello G, Valencia A. 1997. Correlated mutations contain information about protein-protein interaction. Journal of Molecular Biology 271: 511-523. (Pubitemid 27373087)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.4 , pp. 511-523
    • Pazos, F.1    Helmer-Citterich, M.2    Ausiello, G.3    Valencia, A.4
  • 64
    • 0000388198 scopus 로고
    • Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm
    • Plaxton WC, Preiss J. 1987. Purification and properties of nonproteolytic degraded ADPglucose pyrophosphorylase from maize endosperm. Plant Physiology 83: 105-112.
    • (1987) Plant Physiology , vol.83 , pp. 105-112
    • Plaxton, W.C.1    Preiss, J.2
  • 65
    • 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. (Pubitemid 28552116)
    • (1998) Bioinformatics , vol.14 , Issue.9 , pp. 817-818
    • Posada, D.1    Crandall, K.A.2
  • 67
    • 79958266884 scopus 로고    scopus 로고
    • A new, fast algorithm for detecting protein coevolution using maximum compatible cliques
    • Rodionov A, Bezginov A, Rose J, Tillier ER. 2011. A new, fast algorithm for detecting protein coevolution using maximum compatible cliques. Algorithms in Molecular Biology 6: 17.
    • (2011) Algorithms in Molecular Biology , vol.6 , pp. 17
    • Rodionov, A.1    Bezginov, A.2    Rose, J.3    Tillier, E.R.4
  • 68
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • DOI 10.1093/bioinformatics/btg180
    • Ronquist F, Huelsenbeck JP. 2003. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574. (Pubitemid 37038874)
    • (2003) Bioinformatics , vol.19 , Issue.12 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 69
    • 0034879793 scopus 로고    scopus 로고
    • Subcellular compartmentation and allosteric regulation of the rice endosperm ADPglucose pyrophosphorylase
    • DOI 10.1016/S0168-9452(01)00431-9, PII S0168945201004319
    • Sikka VK, Choi SB, Kavakli IH, Sakulsingharoj C, Gupta S, Ito H Okita T. 2001. Subcellular compartimentation and allosteric regulation of the rice endosperm ADPglucose pyrophosphorylase. Plant Science 161: 461-468. (Pubitemid 32750902)
    • (2001) Plant Science , vol.161 , Issue.3 , pp. 461-468
    • Sikka, V.K.1    Choi, S.-B.2    Kavakli I.Halil3    Sakulsingharoj, C.4    Gupta, S.5    Ito, H.6    Okita, T.W.7
  • 72
    • 0347298559 scopus 로고    scopus 로고
    • Subcellular localization of ADPglucose pyrophosphorylase in developing wheat endosperm and analysis of the properties of a plastidial isoform
    • DOI 10.1093/jxb/erg088
    • Tetlow IJ, Davies EJ, Vardy KA, Bowsher CG, Burrell MM, Emes MJ. 2003. Subcellular localization of ADPglucose pyrophosphorylase in developing wheat endosperm and analysis of the properties of a plastidial isoform. Journal of Experimental Botany 54: 715-725. (Pubitemid 36189217)
    • (2003) Journal of Experimental Botany , vol.54 , Issue.383 , pp. 715-725
    • Tetlow, I.J.1    Davies, E.J.2    Vardy, K.A.3    Bowsher, C.G.4    Burrell, M.M.5    Emes, M.J.6
  • 73
    • 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 Research 22: 4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 74
    • 34047228912 scopus 로고    scopus 로고
    • Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses
    • DOI 10.1093/molbev/msm022
    • Travers SA, Fares MA. 2007. Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses. Molecular Biology and Evolution 24: 1032-44. (Pubitemid 46536714)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.4 , pp. 1032-1044
    • Travers, S.A.A.1    Fares, M.A.2
  • 75
    • 56049114881 scopus 로고    scopus 로고
    • Insights into subunit interactions in the heterotetrameric structure of potato ADP-glucose pyrophosphorylase
    • Tuncel A, Kavakli IH, Keskin O. 2008. Insights into subunit interactions in the heterotetrameric structure of potato ADP-glucose pyrophosphorylase. Biophysical Journal 95: 3628-3639.
    • (2008) Biophysical Journal , vol.95 , pp. 3628-3639
    • Tuncel, A.1    Kavakli, I.H.2    Keskin, O.3
  • 77
    • 0028893838 scopus 로고
    • How often do duplicated genes evolve new functions?
    • Walsh JB. 1995. How often do duplicated genes evolve new functions? Genetics 139: 421-428.
    • (1995) Genetics , vol.139 , pp. 421-428
    • Walsh, J.B.1
  • 78
    • 0029108075 scopus 로고
    • Cell-type specific, coordinate expression of two ADP-glucose pyrophosphorylase genes in relation to starch biosynthesis during seed development of Vicia faba L
    • Weber H, Heim U, Borisjuk L, Wobus U. 1995. Cell-type specific, coordinate expression of two ADP-glucose pyrophosphorylase genes in relation to starch biosynthesis during seed development of Vicia faba L. Planta 195: 352-361.
    • (1995) Planta , vol.195 , pp. 352-361
    • Weber, H.1    Heim, U.2    Borisjuk, L.3    Wobus, U.4
  • 79
    • 0028214103 scopus 로고
    • Estimating the pattern of nucleotide substitution
    • Yang Z. 1994. Estimating the pattern of nucleotide substitution. Journal of Molecular Evolution 39: 105-11. (Pubitemid 24181131)
    • (1994) Journal of Molecular Evolution , vol.39 , Issue.1 , pp. 105-111
    • Yang, Z.1
  • 80
    • 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. Molecular Biology and Evolution 15: 568-73. (Pubitemid 28194621)
    • (1998) Molecular Biology and Evolution , vol.15 , Issue.5 , pp. 568-573
    • Yang, Z.1
  • 81
    • 34547803197 scopus 로고    scopus 로고
    • PAML 4: Phylogenetic analysis by maximum likelihood
    • DOI 10.1093/molbev/msm088
    • Yang Z. 2007. PAML 4: Phylogenetic analysis by maximum likelihood. Molecular Biology and Evolution 24: 1586-1591. (Pubitemid 47236688)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1586-1591
    • Yang, Z.1
  • 82
    • 0031960185 scopus 로고    scopus 로고
    • Synonymous and nonsynonymous rate variation in nuclear genes of mammals
    • DOI 10.1007/PL00006320
    • Yang Z, Nielsen R. 1998. Synonymous and nonsynonymous rate variation in nuclear genes of mammals. Journal of Molecular Evolution 46: 409-418. (Pubitemid 28164945)
    • (1998) Journal of Molecular Evolution , vol.46 , Issue.4 , pp. 409-418
    • Yang, Z.1    Nielsen, R.2
  • 83
    • 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. (Pubitemid 34602960)
    • (2002) Molecular Biology and Evolution , vol.19 , Issue.6 , pp. 908-917
    • Yang, Z.1    Nielsent, R.2
  • 84
    • 16344378246 scopus 로고    scopus 로고
    • Bayes empirical Bayes inference of amino acid sites under positive selection
    • DOI 10.1093/molbev/msi097
    • Yang Z, Wong WS, Nielsen R. 2005. Bayes empirical bayes inference of amino acid sites under positive selection. Molecular Biology and Evolution 22: 1107-1118. (Pubitemid 40471423)
    • (2005) Molecular Biology and Evolution , vol.22 , Issue.4 , pp. 1107-1118
    • Yang, Z.1    Wong, W.S.W.2    Nielsen, R.3
  • 85
    • 36949019322 scopus 로고    scopus 로고
    • Detecting coevolution in and among protein domains
    • Yeang CH, Haussler D. 2007. Detecting coevolution in and among protein domains. PLoS Computational Biology 3: E211. http://dx.doi.org/10. 1371/journal.pcbi.0030211.
    • (2007) PLoS Computational Biology , vol.3
    • Yeang, C.H.1    Haussler, D.2
  • 86
    • 33748423352 scopus 로고    scopus 로고
    • The ADP-glucose binding site of the Escherichia coli glycogen synthase
    • DOI 10.1016/j.abb.2006.07.003, PII S0003986106002463
    • Yep A, Ballicora MA, Preiss J. 2006. The ADP-glucose binding site of the Escherichia coli glycogen synthase. Archives of Biochemistry and Biophysics 453: 188-196. (Pubitemid 44344215)
    • (2006) Archives of Biochemistry and Biophysics , vol.453 , Issue.2 , pp. 188-196
    • Yep, A.1    Ballicora, M.A.2    Preiss, J.3
  • 87
    • 27844439855 scopus 로고    scopus 로고
    • Evaluation of an improved branch-site likelihood method for detecting positive selection at the molecular level
    • DOI 10.1093/molbev/msi237
    • Zhang J, Nielsen R, Yang Z. 2005. Evaluation of an improved branch-site likelihood method for detecting positive selection at the molecular level. Molecular Biology and Evolution 22: 2472-2479. (Pubitemid 41661383)
    • (2005) Molecular Biology and Evolution , vol.22 , Issue.12 , pp. 2472-2479
    • Zhang, J.1    Nielsen, R.2    Yang, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.