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Volumn 79, Issue , 2012, Pages 27-38

Molecular cloning and biochemical characterization of three phosphoglycerate kinase isoforms from developing sunflower (Helianthus annuus L.) seeds

Author keywords

Fatty acids; Helianthus annuus; Oil; Phosphoglycerate kinase; Seed; Sunflower

Indexed keywords

COMPLEMENTARY DNA; ISOENZYME; PHOSPHOGLYCERATE KINASE;

EID: 84862025763     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2012.04.001     Document Type: Article
Times cited : (17)

References (66)
  • 1
    • 35148880253 scopus 로고    scopus 로고
    • Carbon conversion efficiency and central metabolic fluxes in developing sunflower (Helianthus annuus L.) embryos
    • A.P. Alonso, F.D. Goffman, J.B. Ohlrogge, and Y. Shachar-Hill Carbon conversion efficiency and central metabolic fluxes in developing sunflower (Helianthus annuus L.) embryos Plant J. 52 2007 296 308
    • (2007) Plant J. , vol.52 , pp. 296-308
    • Alonso, A.P.1    Goffman, F.D.2    Ohlrogge, J.B.3    Shachar-Hill, Y.4
  • 2
    • 0028317569 scopus 로고
    • Purification of a DNA-binding protein from a multi-protein complex associated with DNA polymerase-α in pea (Pisum sativum)
    • J. Al-Rashdi, and J.A. Bryant Purification of a DNA-binding protein from a multi-protein complex associated with DNA polymerase-α in pea (Pisum sativum) J. Exp. Bot. 45 1994 1867 1871
    • (1994) J. Exp. Bot. , vol.45 , pp. 1867-1871
    • Al-Rashdi, J.1    Bryant, J.A.2
  • 4
    • 0000249948 scopus 로고
    • Chloroplast and cytoplasmic enzymes: Three distinct isoenzymes associated with the reductive pentose phosphate cycle
    • L.E. Anderson, and V.R. Advani Chloroplast and cytoplasmic enzymes: three distinct isoenzymes associated with the reductive pentose phosphate cycle Plant Physiol. 45 1970 583 585
    • (1970) Plant Physiol. , vol.45 , pp. 583-585
    • Anderson, L.E.1    Advani, V.R.2
  • 5
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • P.A. Bates, L.A. Kelley, R.M. MacCallum, and M.J.E. Sternberg Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM Proteins 45 2001 39 46
    • (2001) Proteins , vol.45 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 6
    • 33645365200 scopus 로고    scopus 로고
    • Computational and experimental analysis identifies Arabidopsis genes specifically expressed during early seed development
    • C. Becerra, P. Puigdomenech, and C.M. Vicient Computational and experimental analysis identifies Arabidopsis genes specifically expressed during early seed development BMC Genomics 7 2006 38
    • (2006) BMC Genomics , vol.7 , pp. 38
    • Becerra, C.1    Puigdomenech, P.2    Vicient, C.M.3
  • 7
    • 61649117957 scopus 로고    scopus 로고
    • The oxygen status of the developing seed
    • L. Borisjuk, and H. Rolletschek The oxygen status of the developing seed New Phytol. 182 2009 17 30
    • (2009) New Phytol. , vol.182 , pp. 17-30
    • Borisjuk, L.1    Rolletschek, H.2
  • 9
    • 79961073194 scopus 로고    scopus 로고
    • Comparative transcriptome and metabolite analysis of oil palm and date palm mesocarp that differ dramatically in carbon partitioning
    • F. Bourgis, A. Kilaru, X. Cao, G.F. Ngando-Ebongue, N. Drira, J.B. Ohlrogge, and V. Arondel Comparative transcriptome and metabolite analysis of oil palm and date palm mesocarp that differ dramatically in carbon partitioning Proc. Natl. Acad. Sci. USA 26 2011 12527 12532
    • (2011) Proc. Natl. Acad. Sci. USA , vol.26 , pp. 12527-12532
    • Bourgis, F.1    Kilaru, A.2    Cao, X.3    Ngando-Ebongue, G.F.4    Drira, N.5    Ohlrogge, J.B.6    Arondel, V.7
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 1942542419 scopus 로고    scopus 로고
    • Cloning and expression of cytosolic phosphoglycerate kinase from pea (Pisum sativum L.)
    • D.C. Brice, J.A. Bryant, G. Dambrauskas, S.C. Drury, and J.A. Littlechild Cloning and expression of cytosolic phosphoglycerate kinase from pea (Pisum sativum L.) J. Exp. Bot. 55 2004 955 956
    • (2004) J. Exp. Bot. , vol.55 , pp. 955-956
    • Brice, D.C.1    Bryant, J.A.2    Dambrauskas, G.3    Drury, S.C.4    Littlechild, J.A.5
  • 12
    • 0030088014 scopus 로고    scopus 로고
    • Differential gene expression of chloroplast and cytosolic phosphoglycerate kinase in tobacco
    • D.H. Bringloe, S.K. Rao, T.A. Dyer, C.A. Raines, and J.W. Bradbeer Differential gene expression of chloroplast and cytosolic phosphoglycerate kinase in tobacco Plant Mol. Biol. 30 1996 637 640
    • (1996) Plant Mol. Biol. , vol.30 , pp. 637-640
    • Bringloe, D.H.1    Rao, S.K.2    Dyer, T.A.3    Raines, C.A.4    Bradbeer, J.W.5
  • 13
    • 0006739586 scopus 로고    scopus 로고
    • What's a nice enzyme like you doing in a place like this? A possible link between glycolysis and DNA replication
    • J.A. Bryant, M.M. Burrell, N.J. Kruger, Bios Scientific Publishers Oxford
    • J.A. Bryant, and L.E. Anderson What's a nice enzyme like you doing in a place like this? A possible link between glycolysis and DNA replication J.A. Bryant, M.M. Burrell, N.J. Kruger, Plant carbohydrate biochemistry 1999 Bios Scientific Publishers Oxford 295 304
    • (1999) Plant Carbohydrate Biochemistry , pp. 295-304
    • Bryant, J.A.1    Anderson, L.E.2
  • 14
    • 0034530807 scopus 로고    scopus 로고
    • A novel DNA-binding protein associated with DNA polymerase-a in pea stimulates polymerase activity on frequently primed templates
    • J.A. Bryant, D.C. Brice, P.N. Fitchett, and L.E. Anderson A novel DNA-binding protein associated with DNA polymerase-a in pea stimulates polymerase activity on frequently primed templates J. Exp. Bot. 51 2000 1945 1947
    • (2000) J. Exp. Bot. , vol.51 , pp. 1945-1947
    • Bryant, J.A.1    Brice, D.C.2    Fitchett, P.N.3    Anderson, L.E.4
  • 15
    • 9844254489 scopus 로고    scopus 로고
    • Novel DNA-binding characteristics of a protein associated with DNA polymerase-α in pea
    • S.K. Burton, J. Van't Hof, and J.A. Bryant Novel DNA-binding characteristics of a protein associated with DNA polymerase-α in pea Plant J. 12 1997 357 365
    • (1997) Plant J. , vol.12 , pp. 357-365
    • Burton, S.K.1    Van'T Hof, J.2    Bryant, J.A.3
  • 16
    • 0034663597 scopus 로고    scopus 로고
    • Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction
    • J.A. Cuff, and G.J. Barton Application of enhanced multiple sequence alignment profiles to improve protein secondary structure prediction Proteins: Struct. Funct. Genet. 40 2000 502 511
    • (2000) Proteins: Struct. Funct. Genet. , vol.40 , pp. 502-511
    • Cuff, J.A.1    Barton, G.J.2
  • 18
    • 33744476422 scopus 로고    scopus 로고
    • Characterization of a cytosolic nucleoside diphosphate kinase associated with cell division and growth in potato
    • S. Dorion, D.P. Matton, and J. Rivoal Characterization of a cytosolic nucleoside diphosphate kinase associated with cell division and growth in potato Planta 224 2006 108 124
    • (2006) Planta , vol.224 , pp. 108-124
    • Dorion, S.1    Matton, D.P.2    Rivoal, J.3
  • 19
    • 7944236532 scopus 로고    scopus 로고
    • Cloning and characterization of a cytosolic triosephosphate isomerase developmentally regulated in potato leaves
    • S. Dorion, J.J. Parveen, D.P. Matton, and J. Rivoal Cloning and characterization of a cytosolic triosephosphate isomerase developmentally regulated in potato leaves Plant Sci. 168 2005 183 194
    • (2005) Plant Sci. , vol.168 , pp. 183-194
    • Dorion, S.1    Parveen, J.J.2    Matton, D.P.3    Rivoal, J.4
  • 20
    • 0347981309 scopus 로고    scopus 로고
    • Oxygen deficiency and root metabolism: Injury and acclimation under hypoxia and anoxia
    • M.C. Drew Oxygen deficiency and root metabolism: Injury and acclimation under hypoxia and anoxia Ann. Rev. Plant Physiol. Plant Mol. Biol. 48 1997 223 250
    • (1997) Ann. Rev. Plant Physiol. Plant Mol. Biol. , vol.48 , pp. 223-250
    • Drew, M.C.1
  • 21
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • K.J. Ellis, and J.F. Morrison Buffers of constant ionic strength for studying pH-dependent processes Methods Enzymol. 87 1982 405 426
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 22
    • 0032037523 scopus 로고    scopus 로고
    • Expression and localization of phosphoenolpyruvate carboxylase in developing and germinating wheat grains
    • M.C. González, L. Osuna, C. Echevarria, J. Vidal, and F.J. Cejudo Expression and localization of phosphoenolpyruvate carboxylase in developing and germinating wheat grains Plant Physiol. 116 1998 1249 1258
    • (1998) Plant Physiol. , vol.116 , pp. 1249-1258
    • González, M.C.1    Osuna, L.2    Echevarria, C.3    Vidal, J.4    Cejudo, F.J.5
  • 23
    • 0035109430 scopus 로고    scopus 로고
    • Origin of the cytoplasmic pH changes during anaerobic stress in higher plant cells. Carbon-13 and phosphorus-31 nuclear magnetic resonance studies
    • E. Gout, A.M. Boisson, S. Aubert, and R. Bligny Origin of the cytoplasmic pH changes during anaerobic stress in higher plant cells. Carbon-13 and phosphorus-31 nuclear magnetic resonance studies Plant Physiol. 125 2001 912 925
    • (2001) Plant Physiol. , vol.125 , pp. 912-925
    • Gout, E.1    Boisson, A.M.2    Aubert, S.3    Bligny, R.4
  • 24
    • 0031473847 scopus 로고    scopus 로고
    • Swiss Model and Swiss Pdb Viewer: An environment for comparative protein modelling
    • R.E.F. Guex, and M.C. Peitsch Swiss Model and Swiss Pdb Viewer: an environment for comparative protein modelling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, R.E.F.1    Peitsch, M.C.2
  • 25
    • 0037248286 scopus 로고    scopus 로고
    • Metabolism of sugars in the endosperm of developing seeds of oilseed rape
    • L.M. Hill, E.R. Morley-Smith, and S. Rawsthorne Metabolism of sugars in the endosperm of developing seeds of oilseed rape Plant Physiol. 131 2003 228 236
    • (2003) Plant Physiol. , vol.131 , pp. 228-236
    • Hill, L.M.1    Morley-Smith, E.R.2    Rawsthorne, S.3
  • 26
    • 70349644993 scopus 로고    scopus 로고
    • Quantitative Proteomics of seed filling in castor: Comparison with soybean and rapeseed reveals differences between photosynthetic and non-photosynthetic seed metabolism
    • N.L. Houston, M. Hajduch, and J.J. Thelen Quantitative Proteomics of seed filling in castor: comparison with soybean and rapeseed reveals differences between photosynthetic and non-photosynthetic seed metabolism Plant Physiol. 151 2009 857 868
    • (2009) Plant Physiol. , vol.151 , pp. 857-868
    • Houston, N.L.1    Hajduch, M.2    Thelen, J.J.3
  • 28
    • 0025239322 scopus 로고
    • Functional identity of a primer recognition protein as phosphoglycerate kinase
    • H.K. Jindal, and J.K. Vishwanatha Functional identity of a primer recognition protein as phosphoglycerate kinase J. Biol. Chem. 265 1990 6540 6543
    • (1990) J. Biol. Chem. , vol.265 , pp. 6540-6543
    • Jindal, H.K.1    Vishwanatha, J.K.2
  • 29
    • 0023002623 scopus 로고
    • Biochemical changes during sucrose deprivation in higher plant cells
    • E.P. Journet, R. Bligny, and R. Douce Biochemical changes during sucrose deprivation in higher plant cells J. Biol. Chem. 261 1986 3193 3199
    • (1986) J. Biol. Chem. , vol.261 , pp. 3193-3199
    • Journet, E.P.1    Bligny, R.2    Douce, R.3
  • 30
    • 34547658908 scopus 로고    scopus 로고
    • Parallel determination of enzyme activities an in vitro fluxes in Brassica napus embryos grown on organic or inorganic nitrogen source
    • B.H. Junker, J. Lonien, L.E. Heady, A. Rogers, and J. Schwender Parallel determination of enzyme activities an in vitro fluxes in Brassica napus embryos grown on organic or inorganic nitrogen source Phytochemistry 68 2007 2232 2242
    • (2007) Phytochemistry , vol.68 , pp. 2232-2242
    • Junker, B.H.1    Lonien, J.2    Heady, L.E.3    Rogers, A.4    Schwender, J.5
  • 31
    • 9844261395 scopus 로고
    • Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves
    • E. Köpke-Secundo, I. Molnar, and C. Schnarrenberger Isolation and characterization of the cytosolic and chloroplastic 3-phosphoglycerate kinase from spinach leaves Plant Physiol. 93 1990 40 47
    • (1990) Plant Physiol. , vol.93 , pp. 40-47
    • Köpke-Secundo, E.1    Molnar, I.2    Schnarrenberger, C.3
  • 32
    • 0037118690 scopus 로고    scopus 로고
    • Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP and analogues: Correlation between nucleotide binding mode and helix flexibility
    • Z. Kovári, B. Flachner, G. Náray-Szabó, and M. Vas Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP and analogues: correlation between nucleotide binding mode and helix flexibility Biochemistry 41 2002 8796 8806
    • (2002) Biochemistry , vol.41 , pp. 8796-8806
    • Kovári, Z.1    Flachner, B.2    Náray-Szabó, G.3    Vas, M.4
  • 33
    • 0025917329 scopus 로고
    • Immunoelectron microscopic analysis of the intracellular distribution of primer recognition proteins, annexin 2 and phosphoglycerate kinase, in normal and transformed cells
    • K.D. Kumble, and J.K. Vishwanatha Immunoelectron microscopic analysis of the intracellular distribution of primer recognition proteins, annexin 2 and phosphoglycerate kinase, in normal and transformed cells J. Cell Sci. 99 1991 751 758
    • (1991) J. Cell Sci. , vol.99 , pp. 751-758
    • Kumble, K.D.1    Vishwanatha, J.K.2
  • 34
    • 0015241483 scopus 로고
    • Inhibition of phosphoglycerate kinase by products and product homologues
    • M. Larsson-Raznikiewicz, and L. Arvidsson Inhibition of phosphoglycerate kinase by products and product homologues Eur. J. Biochem. 22 1971 506 512
    • (1971) Eur. J. Biochem. , vol.22 , pp. 506-512
    • Larsson-Raznikiewicz, M.1    Arvidsson, L.2
  • 36
    • 0024978453 scopus 로고
    • Wheat phosphoglycerate kinase: Evidence for recombination between the genes for the chloroplastic and cytosolic enzymes
    • M. Longstaff, C.A. Raines, E.M. McMorrow, J.W. Bradbeer, and T.A. Dyer Wheat phosphoglycerate kinase: evidence for recombination between the genes for the chloroplastic and cytosolic enzymes Nucleic Acids Res. 17 1989 6569 6580
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6569-6580
    • Longstaff, M.1    Raines, C.A.2    McMorrow, E.M.3    Bradbeer, J.W.4    Dyer, T.A.5
  • 37
    • 5844264416 scopus 로고
    • Separation, purification, and comparative properties of chloroplast and cytoplasmic phosphoglycerate kinase from barley leaves
    • E.M. McMorrow, and J.W. Bradbeer Separation, purification, and comparative properties of chloroplast and cytoplasmic phosphoglycerate kinase from barley leaves Plant Physiol. 93 1990 374 383
    • (1990) Plant Physiol. , vol.93 , pp. 374-383
    • McMorrow, E.M.1    Bradbeer, J.W.2
  • 38
    • 0027234028 scopus 로고
    • Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase - Correlation between equilibrium dialysis binding and enzyme kinetic data
    • M. Molnar, and M. Vas Mg2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase - correlation between equilibrium dialysis binding and enzyme kinetic data Biochem. J. 293 1993 595 599
    • (1993) Biochem. J. , vol.293 , pp. 595-599
    • Molnar, M.1    Vas, M.2
  • 39
    • 0033544945 scopus 로고    scopus 로고
    • Involvement of a cellular glycolytic enzyme, phosphoglycerate kinase, in Sendai virus transcription
    • T. Ogino, M. Iwama, J. Kinouchi, Y. Shibagaki, T. Tsukamoto, and K. Mizumoto Involvement of a cellular glycolytic enzyme, phosphoglycerate kinase, in Sendai virus transcription J. Biol. Chem. 274 1999 35999 36008
    • (1999) J. Biol. Chem. , vol.274 , pp. 35999-36008
    • Ogino, T.1    Iwama, M.2    Kinouchi, J.3    Shibagaki, Y.4    Tsukamoto, T.5    Mizumoto, K.6
  • 40
    • 2542461193 scopus 로고    scopus 로고
    • Biochemical characterization and crystallization of recombinant 3-phosphoglycerate kinase of Plasmodium falciparum
    • B. Pal, B. Pybus, D.D. Muccio, and D. Chattopadhyay Biochemical characterization and crystallization of recombinant 3-phosphoglycerate kinase of Plasmodium falciparum Biochim. Biophys. Acta 1699 2004 277 280
    • (2004) Biochim. Biophys. Acta , vol.1699 , pp. 277-280
    • Pal, B.1    Pybus, B.2    Muccio, D.D.3    Chattopadhyay, D.4
  • 42
    • 33645536135 scopus 로고    scopus 로고
    • The functional organization and control of plant respiration
    • W.C. Plaxton, and F.E. Podestá The functional organization and control of plant respiration Crit. Rev. Plant Sci. 25 2006 159 198
    • (2006) Crit. Rev. Plant Sci. , vol.25 , pp. 159-198
    • Plaxton, W.C.1    Podestá, F.E.2
  • 43
    • 0032053510 scopus 로고    scopus 로고
    • Modulation of DNA polymerases alpha, delta and epsilon by lactate dehydrogenase and 3-phosphoglycerate kinase
    • O. Popanda, G. Fox, and H.W. Thielmann Modulation of DNA polymerases alpha, delta and epsilon by lactate dehydrogenase and 3-phosphoglycerate kinase Biochim. Biophys. Acta 1397 1998 102 117
    • (1998) Biochim. Biophys. Acta , vol.1397 , pp. 102-117
    • Popanda, O.1    Fox, G.2    Thielmann, H.W.3
  • 44
    • 0021450296 scopus 로고
    • Mechanisms of cytoplasmic pH regulation in hypoxic maize root tips and its role in survival under hypoxia
    • J.K. Roberts, J. Callis, D. Wemmer, V. Walbot, and O. Jardetzky Mechanisms of cytoplasmic pH regulation in hypoxic maize root tips and its role in survival under hypoxia Proc. Natl. Acad. Sci. USA 81 1984 3379 3383
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 3379-3383
    • Roberts, J.K.1    Callis, J.2    Wemmer, D.3    Walbot, V.4    Jardetzky, O.5
  • 46
    • 0023375195 scopus 로고
    • The neighbour-joining method - A new method for reconstructing phylogenetic trees
    • N. Saitou, and M. Nei The neighbour-joining method - a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 4 1987 406 425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 47
    • 0023472472 scopus 로고
    • Tricine sodium dodecyl-sulfate polyacrylamide-gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa
    • H. Schagger, and G. Vonjagow Tricine sodium dodecyl-sulfate polyacrylamide-gel electrophoresis for the separation of proteins in the range from 1 kDa to 100 kDa Anal. Biochem. 166 1987 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Vonjagow, G.2
  • 49
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res. 31 2003 3381 3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 50
    • 0036740911 scopus 로고    scopus 로고
    • Probing in vivo metabolism by stable isotope labeling of storage lipids and proteins in developing Brassica napus embryos
    • J. Schwender, and J.B. Ohlrogge Probing in vivo metabolism by stable isotope labeling of storage lipids and proteins in developing Brassica napus embryos Plant Physiol. 130 2002 347 361
    • (2002) Plant Physiol. , vol.130 , pp. 347-361
    • Schwender, J.1    Ohlrogge, J.B.2
  • 51
    • 0028039333 scopus 로고
    • The occurrence of chloroplastic and cytosolic isoenzymes of phosphoglycerate kinase in a range of plant species
    • N. Shah, and J.W. Bradbeer The occurrence of chloroplastic and cytosolic isoenzymes of phosphoglycerate kinase in a range of plant species Planta 193 1994 232 237
    • (1994) Planta , vol.193 , pp. 232-237
    • Shah, N.1    Bradbeer, J.W.2
  • 53
    • 37049027476 scopus 로고    scopus 로고
    • Reversible and irreversible unfolding of multi-domain proteins
    • K.H. Strucksberg, T. Rosenkranz, and J. Fitter Reversible and irreversible unfolding of multi-domain proteins Biochim. Biophys. Acta 1774 2007 1591 1603
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 1591-1603
    • Strucksberg, K.H.1    Rosenkranz, T.2    Fitter, J.3
  • 54
    • 0038790723 scopus 로고    scopus 로고
    • Anion activation of 3-phosphoglycerate kinase requires domain closure
    • A.N. Szilagyi, and M. Vas Anion activation of 3-phosphoglycerate kinase requires domain closure Biochemistry 37 1998 8551 8563
    • (1998) Biochemistry , vol.37 , pp. 8551-8563
    • Szilagyi, A.N.1    Vas, M.2
  • 55
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • K. Tamura, J. Dudley, M. Nei, and S. Kumar MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24 2007 1596 1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 57
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X windows interface. flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL-X windows interface. flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25 1997 4876 4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 58
    • 78049456086 scopus 로고    scopus 로고
    • Glycolytic enzymatic activities in developing seeds involved in the differences between standard and low oil content sunflowers (Helianthus annuus L.)
    • M.A. Troncoso-Ponce, R. Garcés, and E. Martínez-Force Glycolytic enzymatic activities in developing seeds involved in the differences between standard and low oil content sunflowers (Helianthus annuus L.) Plant Physiol. Biochem. 48 2010 961 965
    • (2010) Plant Physiol. Biochem. , vol.48 , pp. 961-965
    • Troncoso-Ponce, M.A.1    Garcés, R.2    Martínez-Force, E.3
  • 59
    • 77955841533 scopus 로고    scopus 로고
    • Cloning, biochemical characterisation, tissue localization and possible post-translational regulatory mechanism of the cytosolic phosphoglucose isomerase from developing sunflower seeds
    • M.A. Troncoso-Ponce, J. Rivoal, F.J. Cejudo, S. Dorion, R. Garcés, and E. Martínez-Force Cloning, biochemical characterisation, tissue localization and possible post-translational regulatory mechanism of the cytosolic phosphoglucose isomerase from developing sunflower seeds Planta 232 2010 845 859
    • (2010) Planta , vol.232 , pp. 845-859
    • Troncoso-Ponce, M.A.1    Rivoal, J.2    Cejudo, F.J.3    Dorion, S.4    Garcés, R.5    Martínez-Force, E.6
  • 61
    • 78651416766 scopus 로고    scopus 로고
    • Cloning, biochemical characterization and expression of a sunflower (Helianthus annuus L.) hexokinase associated with seed storage compounds accumulation
    • M.A. Troncoso-Ponce, J. Rivoal, S. Dorion, M.-C. Moisan, R. Garcés, and E. Martínez-Force Cloning, biochemical characterization and expression of a sunflower (Helianthus annuus L.) hexokinase associated with seed storage compounds accumulation J. Plant Physiol. 168 2011 299 308
    • (2011) J. Plant Physiol. , vol.168 , pp. 299-308
    • Troncoso-Ponce, M.A.1    Rivoal, J.2    Dorion, S.3    Moisan, M.-C.4    Garcés, R.5    Martínez-Force, E.6
  • 62
    • 69249245314 scopus 로고    scopus 로고
    • Characterization of glycolytic initial metabolites and enzyme activities in developing sunflower (Helianthus annuus L.) seeds
    • M.A. Troncoso-Ponce, N.J. Kruger, R.G. Ratcliffe, R. Garcés, and E. Martínez-Force Characterization of glycolytic initial metabolites and enzyme activities in developing sunflower (Helianthus annuus L.) seeds Phytochemistry 70 2009 1117 1122
    • (2009) Phytochemistry , vol.70 , pp. 1117-1122
    • Troncoso-Ponce, M.A.1    Kruger, N.J.2    Ratcliffe, R.G.3    Garcés, R.4    Martínez-Force, E.5
  • 63
    • 0026502305 scopus 로고
    • The role of primer recognition proteins in DNA replication: Association with nuclear matrix in HeLa cells
    • J.K. Vishwanatha, H.K. Jindal, and R.G. Davis The role of primer recognition proteins in DNA replication: association with nuclear matrix in HeLa cells J. Cell Sci. 101 1992 25 34
    • (1992) J. Cell Sci. , vol.101 , pp. 25-34
    • Vishwanatha, J.K.1    Jindal, H.K.2    Davis, R.G.3
  • 66
    • 0032575259 scopus 로고    scopus 로고
    • Purification and characterisation of the phosphoglycerate kinase isoenzymes of Trypanosoma brucei expressed in Escherichia coli
    • A.W.M. Zomer, S. Allert, N. Chevalier, M. Callens, F.R. Opperdoes, and P.A.M. Michels Purification and characterisation of the phosphoglycerate kinase isoenzymes of Trypanosoma brucei expressed in Escherichia coli Biochim. Biophys. Acta 1386 1998 179 188
    • (1998) Biochim. Biophys. Acta , vol.1386 , pp. 179-188
    • Zomer, A.W.M.1    Allert, S.2    Chevalier, N.3    Callens, M.4    Opperdoes, F.R.5    Michels, P.A.M.6


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