메뉴 건너뛰기




Volumn 151, Issue 1, 2009, Pages 67-77

Phylogenetic analysis of ADP-glucose pyrophosphorylase subunits reveals a role of subunit interfaces in the allosteric properties of the enzyme

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; ZEA MAYS;

EID: 70349223021     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.109.138933     Document Type: Article
Times cited : (28)

References (62)
  • 1
    • 24644503222 scopus 로고    scopus 로고
    • Gene expression of ADP-glucose pyrophosphorylase and starch contents in rice cultured cells are cooperatively regulated by sucrose and ABA
    • Akihiro T, Mizuno K, Fujimura T (2005) Gene expression of ADP-glucose pyrophosphorylase and starch contents in rice cultured cells are cooperatively regulated by sucrose and ABA. Plant Cell Physiol 46: 937-946
    • (2005) Plant Cell Physiol , vol.46 , pp. 937-946
    • Akihiro, T.1    Mizuno, K.2    Fujimura, T.3
  • 2
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A Web-based environment for protein structure homology modeling
    • Arnold K, Bordoli L, Kopp J, Schwede T (2006) The SWISS-MODEL Workspace: a Web-based environment for protein structure homology modeling. Bioinformatics 22: 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 3
    • 15444367832 scopus 로고    scopus 로고
    • Resurrecting the ancestral enzymatic role of a modulatory subunit
    • Ballicora MA, Dubay JR, Devillers CH, Preiss J (2005) Resurrecting the ancestral enzymatic role of a modulatory subunit. J Biol Chem 280: 10189-10195
    • (2005) J Biol Chem , vol.280 , pp. 10189-10195
    • Ballicora, M.A.1    Dubay, J.R.2    Devillers, C.H.3    Preiss, J.4
  • 4
    • 34447549169 scopus 로고    scopus 로고
    • Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis
    • Ballicora MA, Erben ED, Yazaki T, Bertolo AL, Demonte AM, Schmidt JR, Aleanzi M, Bejar CM, Figueroa CM, Fusari CM, et al (2007) Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis. J Bacteriol 189: 5325-5333
    • (2007) J Bacteriol , vol.189 , pp. 5325-5333
    • Ballicora, M.A.1    Erben, E.D.2    Yazaki, T.3    Bertolo, A.L.4    Demonte, A.M.5    Schmidt, J.R.6    Aleanzi, M.7    Bejar, C.M.8    Figueroa, C.M.9    Fusari, C.M.10
  • 5
    • 0032161364 scopus 로고    scopus 로고
    • ADP-Glc pyrophosphorylase from potato tubers: Site-directed mutagenesis studies of the regulatory sites
    • Ballicora MA, Fu Y, Nesbitt NM, Preiss J (1998) ADP-Glc pyrophosphorylase from potato tubers: site-directed mutagenesis studies of the regulatory sites. Plant Physiol 118: 265-274
    • (1998) Plant Physiol , vol.118 , pp. 265-274
    • Ballicora, M.A.1    Fu, Y.2    Nesbitt, N.M.3    Preiss, J.4
  • 6
    • 33845982238 scopus 로고    scopus 로고
    • Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases
    • Bejar CM, Jin X, Ballicora MA, Preiss J (2006) Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases. J Biol Chem 281: 40473-40484
    • (2006) J Biol Chem , vol.281 , pp. 40473-40484
    • Bejar, C.M.1    Jin, X.2    Ballicora, M.A.3    Preiss, J.4
  • 7
    • 20444396509 scopus 로고    scopus 로고
    • Directed mutagenesis confirms the functional importance of positively selected sites in polygalacturonase inhibitor protein
    • Bishop JG (2005) Directed mutagenesis confirms the functional importance of positively selected sites in polygalacturonase inhibitor protein. Mol Biol Evol 22: 1531-1534
    • (2005) Mol Biol Evol , vol.22 , pp. 1531-1534
    • Bishop, J.G.1
  • 8
    • 27244442142 scopus 로고    scopus 로고
    • Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics
    • Boehlein SK, Sewell AK, Cross J, Stewart JD, Hannah LC (2005) Purification and characterization of adenosine diphosphate glucose pyrophosphorylase from maize/potato mosaics. Plant Physiol 138: 1552-1562
    • (2005) Plant Physiol , vol.138 , pp. 1552-1562
    • Boehlein, S.K.1    Sewell, A.K.2    Cross, J.3    Stewart, J.D.4    Hannah, L.C.5
  • 9
    • 40749101539 scopus 로고    scopus 로고
    • Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined
    • Boehlein SK, Shaw JR, Stewart JD, Hannah LC (2008) Heat stability and allosteric properties of the maize endosperm ADP-glucose pyrophosphorylase are intimately intertwined. Plant Physiol 146: 289-299
    • (2008) Plant Physiol , vol.146 , pp. 289-299
    • Boehlein, S.K.1    Shaw, J.R.2    Stewart, J.D.3    Hannah, L.C.4
  • 10
    • 58449095237 scopus 로고    scopus 로고
    • Characterization of an autonomously activated plant adenosine diphosphate glucose pyrophosphorylase
    • Boehlein SK, Shaw JR, Stewart JD, Hannah LC (2009) Characterization of an autonomously activated plant adenosine diphosphate glucose pyrophosphorylase. Plant Physiol 149: 318-326
    • (2009) Plant Physiol , vol.149 , pp. 318-326
    • Boehlein, S.K.1    Shaw, J.R.2    Stewart, J.D.3    Hannah, L.C.4
  • 11
    • 0042206877 scopus 로고    scopus 로고
    • Relative turnover numbers of maize endosperm and potato tuber ADP-glucose pyrophosphorylases in the absence and presence of 3-PGA
    • Burger BT, Cross J, Shaw JR, Caren J, Greene TW, Okita TW, Hannah LC (2003) Relative turnover numbers of maize endosperm and potato tuber ADP-glucose pyrophosphorylases in the absence and presence of 3-PGA. Planta 217: 449-456
    • (2003) Planta , vol.217 , pp. 449-456
    • Burger, B.T.1    Cross, J.2    Shaw, J.R.3    Caren, J.4    Greene, T.W.5    Okita, T.W.6    Hannah, L.C.7
  • 12
    • 55949127642 scopus 로고    scopus 로고
    • Positive Darwinian selection at single amino acid sites conferring plant virus resistance
    • Cavatorta JR, Savage AE, Yeam I, Gray SM, Jahn MM (2008) Positive Darwinian selection at single amino acid sites conferring plant virus resistance. J Mol Evol 67: 551-557
    • (2008) J Mol Evol , vol.67 , pp. 551-557
    • Cavatorta, J.R.1    Savage, A.E.2    Yeam, I.3    Gray, S.M.4    Jahn, M.M.5
  • 13
    • 44349103701 scopus 로고    scopus 로고
    • Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6
    • Courville P, Urbankova E, Rensing C, Chaloupka R, Quick M, Cellier MF (2008) Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6. J Biol Chem 283: 9651-9658
    • (2008) J Biol Chem , vol.283 , pp. 9651-9658
    • Courville, P.1    Urbankova, E.2    Rensing, C.3    Chaloupka, R.4    Quick, M.5    Cellier, M.F.6
  • 14
    • 0043210400 scopus 로고    scopus 로고
    • The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme
    • Crevillen P, Ballicora MA, Merida A, Preiss J, Romero JM (2003) The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme. J Biol Chem 278: 28508-28515
    • (2003) J Biol Chem , vol.278 , pp. 28508-28515
    • Crevillen, P.1    Ballicora, M.A.2    Merida, A.3    Preiss, J.4    Romero, J.M.5
  • 15
    • 14844307622 scopus 로고    scopus 로고
    • Differential pattern of expression and sugar regulation of Arabidopsis thaliana ADP-glucose pyrophosphorylase-encoding genes
    • Crevillen P, Ventriglia T, Pinto F, Orea A, Merida A, Romero JM (2005) Differential pattern of expression and sugar regulation of Arabidopsis thaliana ADP-glucose pyrophosphorylase-encoding genes. J Biol Chem 280: 8143-8149
    • (2005) J Biol Chem , vol.280 , pp. 8143-8149
    • Crevillen, P.1    Ventriglia, T.2    Pinto, F.3    Orea, A.4    Merida, A.5    Romero, J.M.6
  • 16
    • 14644409834 scopus 로고    scopus 로고
    • A polymorphic motif in the small subunit of ADPglucose pyrophosphorylase modulates interactions between the small and large subunits
    • Cross JM, Clancy M, Shaw J, Boehlein S, Greene T, Schmidt R, Okita T, Hannah LC (2005) A polymorphic motif in the small subunit of ADPglucose pyrophosphorylase modulates interactions between the small and large subunits. Plant J 41: 501-511
    • (2005) Plant J , vol.41 , pp. 501-511
    • Cross, J.M.1    Clancy, M.2    Shaw, J.3    Boehlein, S.4    Greene, T.5    Schmidt, R.6    Okita, T.7    Hannah, L.C.8
  • 18
    • 0035824612 scopus 로고    scopus 로고
    • Aspartate residue 142 is important for catalysis by ADP-Glc pyrophosphorylase from Escherichia coli
    • Frueauf JB, Ballicora MA, Preiss J (2001) Aspartate residue 142 is important for catalysis by ADP-Glc pyrophosphorylase from Escherichia coli. J Biol Chem 276: 46319-46325
    • (2001) J Biol Chem , vol.276 , pp. 46319-46325
    • Frueauf, J.B.1    Ballicora, M.A.2    Preiss, J.3
  • 19
    • 0037327287 scopus 로고    scopus 로고
    • ADP-Glc pyrophosphorylase from potato tuber: Site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits
    • Frueauf JB, Ballicora MA, Preiss J (2003) ADP-Glc pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits. Plant J 33: 503-511
    • (2003) Plant J , vol.33 , pp. 503-511
    • Frueauf, J.B.1    Ballicora, M.A.2    Preiss, J.3
  • 20
    • 0001571196 scopus 로고    scopus 로고
    • Mutagenesis of the Glc-1-phosphatebinding site of potato tuber ADP-Glc pyrophosphorylase
    • Fu Y, Ballicora MA, Preiss J (1998) Mutagenesis of the Glc-1-phosphatebinding site of potato tuber ADP-Glc pyrophosphorylase. Plant Physiol 117: 989-996
    • (1998) Plant Physiol , vol.117 , pp. 989-996
    • Fu, Y.1    Ballicora, M.A.2    Preiss, J.3
  • 21
    • 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 Evol Biol 8: 232
    • (2008) BMC Evol Biol , vol.8 , pp. 232
    • Georgelis, N.1    Braun, E.L.2    Hannah, L.C.3
  • 22
    • 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
    • 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. Plant Cell 19: 1458-1472
    • (2007) Plant Cell , vol.19 , pp. 1458-1472
    • Georgelis, N.1    Braun, E.L.2    Shaw, J.R.3    Hannah, L.C.4
  • 23
    • 47549083279 scopus 로고    scopus 로고
    • Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant
    • Georgelis N, Hannah LC (2008) Isolation of a heat-stable maize endosperm ADP-glucose pyrophosphorylase variant. Plant Sci 175: 247-254
    • (2008) Plant Sci , vol.175 , pp. 247-254
    • Georgelis, N.1    Hannah, L.C.2
  • 24
    • 0029866101 scopus 로고    scopus 로고
    • Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation
    • Greene TW, Chantler SE, Kahn ML, Barry GF, Preiss J, Okita TW (1996a) Mutagenesis of the potato ADPglucose pyrophosphorylase and characterization of an allosteric mutant defective in 3-phosphoglycerate activation. Proc Natl Acad Sci USA 93: 1509-1513
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1509-1513
    • Greene, T.W.1    Chantler, S.E.2    Kahn, M.L.3    Barry, G.F.4    Preiss, J.5    Okita, T.W.6
  • 25
    • 0031772789 scopus 로고    scopus 로고
    • Maize endosperm ADP-glucose pyrophosphorylase SHRUNKEN2 and BRITTLE2 subunit interactions
    • Greene TW, Hannah LC (1998a) Maize endosperm ADP-glucose pyrophosphorylase SHRUNKEN2 and BRITTLE2 subunit interactions. Plant Cell 10: 1295-1306
    • (1998) Plant Cell , vol.10 , pp. 1295-1306
    • Greene, T.W.1    Hannah, L.C.2
  • 26
    • 0032573220 scopus 로고    scopus 로고
    • Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions
    • Greene TW, Hannah LC (1998b) Enhanced stability of maize endosperm ADP-glucose pyrophosphorylase is gained through mutants that alter subunit interactions. Proc Natl Acad Sci USA 95: 13342-13347
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13342-13347
    • Greene, T.W.1    Hannah, L.C.2
  • 27
    • 0032544014 scopus 로고    scopus 로고
    • Generation of upregulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics
    • Greene TW, Kavakli IH, Kahn M, Okita TW (1998) Generation of upregulated allosteric variants of potato ADP-glucose pyrophosphorylase by reversion genetics. Proc Natl Acad Sci USA 95: 10322-10327
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10322-10327
    • Greene, T.W.1    Kavakli, I.H.2    Kahn, M.3    Okita, T.W.4
  • 28
    • 0030296208 scopus 로고    scopus 로고
    • Aspartic acid 413 is important for the normal allosteric functioning of ADP-glucose pyrophosphorylase
    • Greene TW, Woodbury RL, Okita TW (1996b) Aspartic acid 413 is important for the normal allosteric functioning of ADP-glucose pyrophosphorylase. Plant Physiol 112: 1315-1320
    • (1996) Plant Physiol , vol.112 , pp. 1315-1320
    • Greene, T.W.1    Woodbury, R.L.2    Okita, T.W.3
  • 29
    • 0242666374 scopus 로고    scopus 로고
    • Functional divergence prediction from evolutionary analysis: A case study of vertebrate hemoglobin
    • Gribaldo S, Casane D, Lopez P, Philippe H (2003) Functional divergence prediction from evolutionary analysis: a case study of vertebrate hemoglobin. Mol Biol Evol 20: 1754-1759
    • (2003) Mol Biol Evol , vol.20 , pp. 1754-1759
    • Gribaldo, S.1    Casane, D.2    Lopez, P.3    Philippe, H.4
  • 30
    • 0032728408 scopus 로고    scopus 로고
    • Statistical methods for testing functional divergence after gene duplication
    • Gu X (1999) Statistical methods for testing functional divergence after gene duplication. Mol Biol Evol 16: 1664-1674
    • (1999) Mol Biol Evol , vol.16 , pp. 1664-1674
    • Gu, X.1
  • 31
    • 33748784344 scopus 로고    scopus 로고
    • A simple statistical method for estimating type-II (clusterspecific) functional divergence of protein sequences
    • Gu X (2006) A simple statistical method for estimating type-II (clusterspecific) functional divergence of protein sequences. Mol Biol Evol 23: 1937-1945
    • (2006) Mol Biol Evol , vol.23 , pp. 1937-1945
    • Gu, X.1
  • 32
    • 0036205440 scopus 로고    scopus 로고
    • DIVERGE: Phylogeny-based analysis for functionalstructural divergence of a protein family
    • Gu X, Velden K (2002) DIVERGE: phylogeny-based analysis for functionalstructural divergence of a protein family. Bioinformatics 18: 500-501
    • (2002) Bioinformatics , vol.18 , pp. 500-501
    • Gu, X.1    Velden, K.2
  • 33
    • 34250312693 scopus 로고    scopus 로고
    • Starch synthesis in the maize endosperm
    • Hannah LC (2005) Starch synthesis in the maize endosperm. Maydica 50: 497-506
    • (2005) Maydica , vol.50 , pp. 497-506
    • Hannah, L.C.1
  • 34
    • 0017151912 scopus 로고
    • Characterization of ADP-glucose pyrophosphorylase from Shrunken-2 and brittle-2 mutants of maize
    • Hannah LC, Nelson OE Jr (1976) Characterization of ADP-glucose pyrophosphorylase from Shrunken-2 and brittle-2 mutants of maize. Biochem Genet 14: 547-560
    • (1976) Biochem Genet , vol.14 , pp. 547-560
    • Hannah, L.C.1    Nelson Jr, O.E.2
  • 35
    • 0003037055 scopus 로고
    • Chemical composition
    • In P Gerhandt, RGE Murray, RN Costilow, EW Nester, WAWood, NR Krieg, GB Phillips, eds, American Society for Microbiology, Washington, DC
    • Hanson RS, Phillips JA (1981) Chemical composition. In P Gerhandt, RGE Murray, RN Costilow, EW Nester, WAWood, NR Krieg, GB Phillips, eds, Manual of Methods for General Bacteriology. American Society for Microbiology, Washington, DC, pp 328-364
    • (1981) Manual of Methods for General Bacteriology , pp. 328-364
    • Hanson, R.S.1    Phillips, J.A.2
  • 36
    • 34347372235 scopus 로고    scopus 로고
    • ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit
    • Hwang SK, Hamada S, Okita TW (2006) ATP binding site in the plant ADP-glucose pyrophosphorylase large subunit. FEBS Lett 580: 6741-6748
    • (2006) FEBS Lett , vol.580 , pp. 6741-6748
    • Hwang, S.K.1    Hamada, S.2    Okita, T.W.3
  • 37
    • 33846581912 scopus 로고    scopus 로고
    • Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit
    • Hwang SK, Hamada S, Okita TW (2007) Catalytic implications of the higher plant ADP-glucose pyrophosphorylase large subunit. Phytochemistry 68: 464-477
    • (2007) Phytochemistry , vol.68 , pp. 464-477
    • Hwang, S.K.1    Hamada, S.2    Okita, T.W.3
  • 38
    • 43749106494 scopus 로고    scopus 로고
    • Direct appraisal of the potato tuber ADP-glucose pyrophosphorylase large subunit in enzyme function by study of a novel mutant form
    • Hwang SK, Nagai Y, Kim D, Okita TW (2008) Direct appraisal of the potato tuber ADP-glucose pyrophosphorylase large subunit in enzyme function by study of a novel mutant form. J Biol Chem 283: 6640-6647
    • (2008) J Biol Chem , vol.283 , pp. 6640-6647
    • Hwang, S.K.1    Nagai, Y.2    Kim, D.3    Okita, T.W.4
  • 39
    • 13844261305 scopus 로고    scopus 로고
    • Allosteric regulation of the higher plant ADP-glucose pyrophosphorylase is a product of synergy between the two subunits
    • 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 Lett 579: 983-990
    • (2005) FEBS Lett , vol.579 , pp. 983-990
    • Hwang, S.K.1    Salamone, P.R.2    Okita, T.W.3
  • 42
    • 15444377849 scopus 로고    scopus 로고
    • Crystal structure of potato tuber ADP-Glc pyrophosphorylase
    • Jin X, Ballicora MA, Preiss J, Geiger JH (2005) Crystal structure of potato tuber ADP-Glc pyrophosphorylase. EMBO J 24: 694-704
    • (2005) EMBO J , vol.24 , pp. 694-704
    • Jin, X.1    Ballicora, M.A.2    Preiss, J.3    Geiger, J.H.4
  • 44
    • 0035798634 scopus 로고    scopus 로고
    • Analysis of allosteric effector binding sites of potato ADPglucose pyrophosphorylase through reverse genetics
    • Kavakli IH, Park JS, Slattery CJ, Salamone PR, Frohlick J, Okita TW (2001a) Analysis of allosteric effector binding sites of potato ADPglucose pyrophosphorylase through reverse genetics. J Biol Chem 276: 40834-40840
    • (2001) J Biol Chem , vol.276 , pp. 40834-40840
    • Kavakli, I.H.1    Park, J.S.2    Slattery, C.J.3    Salamone, P.R.4    Frohlick, J.5    Okita, T.W.6
  • 45
    • 34548241238 scopus 로고    scopus 로고
    • Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase
    • Kim D, Hwang SK, Okita TW (2007) Subunit interactions specify the allosteric regulatory properties of the potato tuber ADP-glucose pyrophosphorylase. Biochem Biophys Res Commun 362: 301-306
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 301-306
    • Kim, D.1    Hwang, S.K.2    Okita, T.W.3
  • 46
    • 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. Brief Bioinform 5: 150-163
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 47
    • 0032007679 scopus 로고    scopus 로고
    • Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase
    • Laughlin MJ, Payne JW, Okita TW (1998) Substrate binding mutants of the higher plant ADP-glucose pyrophosphorylase. Phytochemistry 47: 621-629
    • (1998) Phytochemistry , vol.47 , pp. 621-629
    • Laughlin, M.J.1    Payne, J.W.2    Okita, T.W.3
  • 48
    • 33645013647 scopus 로고    scopus 로고
    • Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N terminus of the small subunit
    • Linebarger CR, Boehlein SK, Sewell AK, Shaw J, Hannah LC (2005) Heat stability of maize endosperm ADP-glucose pyrophosphorylase is enhanced by insertion of a cysteine in the N terminus of the small subunit. Plant Physiol 139: 1625-1634
    • (2005) Plant Physiol , vol.139 , pp. 1625-1634
    • Linebarger, C.R.1    Boehlein, S.K.2    Sewell, A.K.3    Shaw, J.4    Hannah, L.C.5
  • 49
    • 0026610767 scopus 로고
    • Assessment of protein models with 3-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D (1992) Assessment of protein models with 3-dimensional profiles. Nature 356: 83-85
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 50
    • 0015353022 scopus 로고
    • Intermediary metabolite levels in Escherichia coli
    • Moses V, Sharp PB (1972) Intermediary metabolite levels in Escherichia coli. J Gen Microbiol 71: 181-190
    • (1972) J Gen Microbiol , vol.71 , pp. 181-190
    • Moses, V.1    Sharp, P.B.2
  • 51
    • 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
  • 52
    • 33645529663 scopus 로고    scopus 로고
    • Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution
    • Norrgård MA, Ivarsson Y, Tars T, Mannervik B (2006) Alternative mutations of a positively selected residue elicit gain or loss of functionalities in enzyme evolution. Proc Natl Acad Sci USA 103: 4876-4881
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4876-4881
    • Ivarsson, Y.1    Tars, T.2    Mannervik, B.3
  • 53
    • 28544439070 scopus 로고    scopus 로고
    • Expression profiling of genes involved in starch synthesis in sink and source organs of rice
    • Ohdan T, Francisco PB Jr, Sawada T, Hirose T, Terao T, Satoh H, Nakamura Y (2005) Expression profiling of genes involved in starch synthesis in sink and source organs of rice. J Exp Bot 56: 3229-3244
    • (2005) J Exp Bot , vol.56 , pp. 3229-3244
    • Ohdan, T.1    Francisco Jr, P.B.2    Sawada, T.3    Hirose, T.4    Terao, T.5    Satoh, H.6    Nakamura, Y.7
  • 56
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31: 3381-3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 57
    • 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. Biophys J 95: 3628-3639
    • (2008) Biophys J , vol.95 , pp. 3628-3639
    • Tuncel, A.1    Kavakli, I.H.2    Keskin, O.3
  • 58
    • 0017963722 scopus 로고
    • 31P nuclear magnetic resonance studies of bioenergetics and glycolysis in anaerobic Escherichia coli cells
    • 31P nuclear magnetic resonance studies of bioenergetics and glycolysis in anaerobic Escherichia coli cells. Proc Natl Acad Sci USA 75: 2244-2248
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 2244-2248
    • Ugurbil, K.1    Rottenberg, H.2    Glynn, P.3    Shulman, R.G.4
  • 60
    • 0025398721 scopus 로고
    • What If: A molecular modeling and drug design program
    • Vriend G (1990) What If: a molecular modeling and drug design program. J Mol Graph 8: 52-56
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 61
    • 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
  • 62
    • 0034097381 scopus 로고    scopus 로고
    • Codonsubstitution models for heterogenous selection pressure at amino acid sites
    • Yang Z, Nielsen R, Goldman N, Krabbe Pedersen AM (2000) Codonsubstitution models for heterogenous 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    Krabbe Pedersen, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.