메뉴 건너뛰기




Volumn 78, Issue , 2013, Pages 123-133

Comparative proteomic analysis of early somatic and zygotic embryogenesis in Theobroma cacao L.

Author keywords

Embryogenesis; Metabolic pathways; Proteomics; Theobroma cacao

Indexed keywords

CARBOHYDRATE; PHOSPHOENOLPYRUVATE CARBOXYLASE;

EID: 84871774170     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.11.007     Document Type: Article
Times cited : (48)

References (81)
  • 1
    • 0033302442 scopus 로고    scopus 로고
    • Phylogeny of the core Malvales: evidence from ndhF sequence data
    • Alverson W.S., Whitlock B.A., Nyffeler R., Bayer C., Baum D.A. Phylogeny of the core Malvales: evidence from ndhF sequence data. Am J Bot 1999, 86:1474-1486.
    • (1999) Am J Bot , vol.86 , pp. 1474-1486
    • Alverson, W.S.1    Whitlock, B.A.2    Nyffeler, R.3    Bayer, C.4    Baum, D.A.5
  • 2
    • 0036182939 scopus 로고    scopus 로고
    • Evidence that the antioxidant flavonoids in tea and cocoa are beneficial for cardiovascular health
    • Kris-Etherton P.M., Keen C.L. Evidence that the antioxidant flavonoids in tea and cocoa are beneficial for cardiovascular health. Curr Opin Lipidol 2002, 13:41-49.
    • (2002) Curr Opin Lipidol , vol.13 , pp. 41-49
    • Kris-Etherton, P.M.1    Keen, C.L.2
  • 3
    • 0344198059 scopus 로고    scopus 로고
    • Cocoa has more phenolic phytochemicals and a higher antioxidant capacity than teas and red wine
    • Lee K.W., Kim Y.J., Lee H.J., Lee C.Y. Cocoa has more phenolic phytochemicals and a higher antioxidant capacity than teas and red wine. J Agric Food Chem 2003, 51:7292-7295.
    • (2003) J Agric Food Chem , vol.51 , pp. 7292-7295
    • Lee, K.W.1    Kim, Y.J.2    Lee, H.J.3    Lee, C.Y.4
  • 4
    • 71649091008 scopus 로고    scopus 로고
    • Polyphenols from cocoa and vascular health - a critical review
    • Rimbach G., Melchin M., Moehring J., Wagner A.E. Polyphenols from cocoa and vascular health - a critical review. Int J Mol Sci 2009, 10:4290-4309.
    • (2009) Int J Mol Sci , vol.10 , pp. 4290-4309
    • Rimbach, G.1    Melchin, M.2    Moehring, J.3    Wagner, A.E.4
  • 5
    • 71949107443 scopus 로고    scopus 로고
    • Flavonoids and brain health: multiple effects underpinned by common mechanisms
    • Spencer J.P. Flavonoids and brain health: multiple effects underpinned by common mechanisms. Genes Nutr 2009, 4:243-250.
    • (2009) Genes Nutr , vol.4 , pp. 243-250
    • Spencer, J.P.1
  • 6
    • 0007499464 scopus 로고
    • Incompatibility system in Theobroma cacao
    • Pandey K.K. Incompatibility system in Theobroma cacao. Am Nat 1960, 94:379-381.
    • (1960) Am Nat , vol.94 , pp. 379-381
    • Pandey, K.K.1
  • 7
    • 0032228679 scopus 로고    scopus 로고
    • Somatic embryogenesis and plant regeneration from floral explant of cocao (Theobroma cacao L.) using thidiazuron
    • Li Z., Traore A., Maximova S., Guiltinan M. Somatic embryogenesis and plant regeneration from floral explant of cocao (Theobroma cacao L.) using thidiazuron. In Vitro Cell Dev Biol Plant 1998, 34:293-299.
    • (1998) In Vitro Cell Dev Biol Plant , vol.34 , pp. 293-299
    • Li, Z.1    Traore, A.2    Maximova, S.3    Guiltinan, M.4
  • 8
    • 0038546872 scopus 로고    scopus 로고
    • Micropropagation of Theobroma cacao using somatic embryo-derived plants
    • Traore A., Maximova S., Guiltinan M. Micropropagation of Theobroma cacao using somatic embryo-derived plants. In Vitro Cell Dev Biol Plant 2003, 39:332-337.
    • (2003) In Vitro Cell Dev Biol Plant , vol.39 , pp. 332-337
    • Traore, A.1    Maximova, S.2    Guiltinan, M.3
  • 9
    • 12744279487 scopus 로고    scopus 로고
    • Characterisation of the cacao somatic embryogenesis receptor-like kinase (SERK) gene expressed during somatic embryogenesis
    • Santos M.O., Romanoa E., Yotoko K.S.C., Tinocoa M.L.P., Diasa B.B.A., Aragǎo F.J.L. Characterisation of the cacao somatic embryogenesis receptor-like kinase (SERK) gene expressed during somatic embryogenesis. Plant Sci 2004, 168:723-729.
    • (2004) Plant Sci , vol.168 , pp. 723-729
    • Santos, M.O.1    Romanoa, E.2    Yotoko, K.S.C.3    Tinocoa, M.L.P.4    Diasa, B.B.A.5    Aragǎo, F.J.L.6
  • 10
    • 38649086082 scopus 로고    scopus 로고
    • Characterization of leafy cotyledon1-like during embryogenesis in Theobroma cacao L
    • Alemanno L., Devic M., Niemenak N., Sanier C., Guilleminot J., Rio M., et al. Characterization of leafy cotyledon1-like during embryogenesis in Theobroma cacao L. Planta 2008, 227:853-866.
    • (2008) Planta , vol.227 , pp. 853-866
    • Alemanno, L.1    Devic, M.2    Niemenak, N.3    Sanier, C.4    Guilleminot, J.5    Rio, M.6
  • 12
    • 41049110787 scopus 로고    scopus 로고
    • Regeneration of somatic embryos in Theobroma cacao L. in temporary immersion bioreactor and analysis of free amino acids in different tissues
    • Niemenak N., Saare-Surminski K., Rohsius C., Omokolo N.D., Lieberei R. Regeneration of somatic embryos in Theobroma cacao L. in temporary immersion bioreactor and analysis of free amino acids in different tissues. Plant Cell Rep 2008, 27:667-676.
    • (2008) Plant Cell Rep , vol.27 , pp. 667-676
    • Niemenak, N.1    Saare-Surminski, K.2    Rohsius, C.3    Omokolo, N.D.4    Lieberei, R.5
  • 13
    • 0031463075 scopus 로고    scopus 로고
    • A comparison between Theobroma cacao L., zygotic embryogenesis and somatic embryogenesis from floral explants
    • Alemanno L., Berthouly M., Micheaux-Ferrière N. A comparison between Theobroma cacao L., zygotic embryogenesis and somatic embryogenesis from floral explants. In vitro Cell Dev Biol Plant 1997, 33:163-172.
    • (1997) In vitro Cell Dev Biol Plant , vol.33 , pp. 163-172
    • Alemanno, L.1    Berthouly, M.2    Micheaux-Ferrière, N.3
  • 14
    • 0030832022 scopus 로고    scopus 로고
    • Zygotic embryogenesis versus somatic embryogenesis
    • Dodeman V.L., Ducreux G., Kreis M. Zygotic embryogenesis versus somatic embryogenesis. J Exp Bot 1997, 48:1493-1509.
    • (1997) J Exp Bot , vol.48 , pp. 1493-1509
    • Dodeman, V.L.1    Ducreux, G.2    Kreis, M.3
  • 15
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • Callis J. Regulation of protein degradation. Plant Cell 1995, 7:845-857.
    • (1995) Plant Cell , vol.7 , pp. 845-857
    • Callis, J.1
  • 16
    • 0001874148 scopus 로고
    • Nature and utilization of seed reserves during germination and heterotrophic growth of young sugar beet seedlings
    • Elamrani A.J., Raymond P., Saglio P. Nature and utilization of seed reserves during germination and heterotrophic growth of young sugar beet seedlings. Seed Sci Res 1992, 2:1-8.
    • (1992) Seed Sci Res , vol.2 , pp. 1-8
    • Elamrani, A.J.1    Raymond, P.2    Saglio, P.3
  • 17
    • 1942469546 scopus 로고    scopus 로고
    • The effect of α-amanitin on the Arabidopsis seed proteome highlights the distinct roles of stored and neosynthesized mRNAs during germination
    • Rajjou L., Gallardo K., Debeaujon I., Vandekerckhove J., Job C., Job D. The effect of α-amanitin on the Arabidopsis seed proteome highlights the distinct roles of stored and neosynthesized mRNAs during germination. Plant Physiol 2004, 134:1598-1613.
    • (2004) Plant Physiol , vol.134 , pp. 1598-1613
    • Rajjou, L.1    Gallardo, K.2    Debeaujon, I.3    Vandekerckhove, J.4    Job, C.5    Job, D.6
  • 18
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi S.P., Rochon Y., Franza B.R., Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 1999, 19:1720-1730.
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 19
    • 0141920354 scopus 로고    scopus 로고
    • Comparing protein abundance and mRNA expression levels on a genomic scale
    • Greenbaum D., Colangelo C., Williams K., Gerstein M. Comparing protein abundance and mRNA expression levels on a genomic scale. Genome Biol 2003, 4:117-124.
    • (2003) Genome Biol , vol.4 , pp. 117-124
    • Greenbaum, D.1    Colangelo, C.2    Williams, K.3    Gerstein, M.4
  • 20
    • 4544265213 scopus 로고    scopus 로고
    • Tackling the plant proteome: practical approaches, hurdles and experimental tools
    • Rose J.K.C., Bashir S., Giovannoni J.J., Jahn M.M., Saravanan R.S. Tackling the plant proteome: practical approaches, hurdles and experimental tools. Plant J 2004, 39:715-733.
    • (2004) Plant J , vol.39 , pp. 715-733
    • Rose, J.K.C.1    Bashir, S.2    Giovannoni, J.J.3    Jahn, M.M.4    Saravanan, R.S.5
  • 21
    • 57449099068 scopus 로고    scopus 로고
    • Precision proteomics: the case for high resolution and high mass accuracy
    • Manna M., Kelleher N.L. Precision proteomics: the case for high resolution and high mass accuracy. Proc Natl Acad Sci U S A 2008, 105:18132-18138.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18132-18138
    • Manna, M.1    Kelleher, N.L.2
  • 24
    • 0036008020 scopus 로고    scopus 로고
    • Proteomics and a future generation of plant molecular biologists
    • Roberts J.K. Proteomics and a future generation of plant molecular biologists. Plant Mol Biol 2002, 48:143-154.
    • (2002) Plant Mol Biol , vol.48 , pp. 143-154
    • Roberts, J.K.1
  • 26
    • 33746903924 scopus 로고    scopus 로고
    • Proteomic analyses of somatic and zygotic embryos of Cyclamen persicum Mill. reveal new insights into seed and germination physiology
    • Winkelmann T., Heintz D., Van Dorsselaer A., Serek M., Braun H.P. Proteomic analyses of somatic and zygotic embryos of Cyclamen persicum Mill. reveal new insights into seed and germination physiology. Planta 2006, 224:508-519.
    • (2006) Planta , vol.224 , pp. 508-519
    • Winkelmann, T.1    Heintz, D.2    Van Dorsselaer, A.3    Serek, M.4    Braun, H.P.5
  • 27
    • 72449177326 scopus 로고    scopus 로고
    • Proteomic analysis of somatic embryogenesis in Cyclamen persicum Mill
    • Bian F., Zheng C., Qu F., Gong X., You C. Proteomic analysis of somatic embryogenesis in Cyclamen persicum Mill. Plant Mol Biol Rep 2010, 28:22-31.
    • (2010) Plant Mol Biol Rep , vol.28 , pp. 22-31
    • Bian, F.1    Zheng, C.2    Qu, F.3    Gong, X.4    You, C.5
  • 28
    • 79151483037 scopus 로고    scopus 로고
    • Enolases: storage compounds in seeds? Evidence from a proteomic comparison of zygotic and somatic embryos of Cyclamen persicum Mill
    • Rode C., Gallien S., Heintz D., Van-Dorsselaer A., Braun H.P., Winkelmann T. Enolases: storage compounds in seeds? Evidence from a proteomic comparison of zygotic and somatic embryos of Cyclamen persicum Mill. Plant Mol Biol 2011, 75:305-319.
    • (2011) Plant Mol Biol , vol.75 , pp. 305-319
    • Rode, C.1    Gallien, S.2    Heintz, D.3    Van-Dorsselaer, A.4    Braun, H.P.5    Winkelmann, T.6
  • 29
    • 84860222292 scopus 로고    scopus 로고
    • From callus to embryo - a proteomic view on the development and maturation of somatic embryos in Cyclamen persicum
    • Rode C., Lindhorst K., Braun H.P., Winkelmann T. From callus to embryo - a proteomic view on the development and maturation of somatic embryos in Cyclamen persicum. Planta 2012, 35:995-1101.
    • (2012) Planta , vol.35 , pp. 995-1101
    • Rode, C.1    Lindhorst, K.2    Braun, H.P.3    Winkelmann, T.4
  • 30
    • 70349992917 scopus 로고    scopus 로고
    • Comparative 2-DE proteomic analysis of date palm (Phoenix dactylifera L.) somatic and zygotic embryos
    • Sghaier-Hammami B., Drira N., Jorrín-Novo V.J. Comparative 2-DE proteomic analysis of date palm (Phoenix dactylifera L.) somatic and zygotic embryos. J Proteomics 2009, 1:161-177.
    • (2009) J Proteomics , vol.1 , pp. 161-177
    • Sghaier-Hammami, B.1    Drira, N.2    Jorrín-Novo, V.J.3
  • 31
    • 79955153469 scopus 로고    scopus 로고
    • Proteomic analysis of Theobroma cacao pod husk
    • Awang A., Karim R., Mitsui T. Proteomic analysis of Theobroma cacao pod husk. J Appl Glycosci 2010, 57:245-267.
    • (2010) J Appl Glycosci , vol.57 , pp. 245-267
    • Awang, A.1    Karim, R.2    Mitsui, T.3
  • 32
    • 0027288745 scopus 로고
    • The major seed proteins of Theobroma cacao L.
    • Voigt J., Biehl B., Kamaruddin S. The major seed proteins of Theobroma cacao L. Food Chem 1993, 47:145-151.
    • (1993) Food Chem , vol.47 , pp. 145-151
    • Voigt, J.1    Biehl, B.2    Kamaruddin, S.3
  • 33
    • 19444378148 scopus 로고    scopus 로고
    • Soluble albumin and biological value of protein in cocoa (Theobroma cacao L.) beans as a function of roasting time
    • Abecia-Soria L., Pezoa-Garcia N.H., Amaya-Farfan J. Soluble albumin and biological value of protein in cocoa (Theobroma cacao L.) beans as a function of roasting time. J Food Sci 2005, 70:S294-S298.
    • (2005) J Food Sci , vol.70
    • Abecia-Soria, L.1    Pezoa-Garcia, N.H.2    Amaya-Farfan, J.3
  • 34
    • 79959664375 scopus 로고    scopus 로고
    • The protein profile of Theobroma cacao L. seeds as obtained by matrix-assisted laser desorption/ionization mass spectrometry
    • Bertazzo A., Agnolin F., Comai S., Zancato M., Costa C.V.L., Seraglia R., et al. The protein profile of Theobroma cacao L. seeds as obtained by matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 2011, 25:2035-2042.
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 2035-2042
    • Bertazzo, A.1    Agnolin, F.2    Comai, S.3    Zancato, M.4    Costa, C.V.L.5    Seraglia, R.6
  • 35
    • 84871753197 scopus 로고    scopus 로고
    • ICGD (International Cocoa Germplasm Database)
    • Available:, (Accessed January 2nd, 2012)
    • ICGD (International Cocoa Germplasm Database) NYSE Liffe/CRA Ltd./University of Reading, UK Available:, (Accessed January 2nd, 2012). http://www.icgd.reading.ac.uk.
    • NYSE Liffe/CRA Ltd./University of Reading, UK
  • 36
    • 0001467258 scopus 로고
    • In vitro propagation of Paradox walnut root stock
    • Driver J.A., Kuniyuki A.H. In vitro propagation of Paradox walnut root stock. HortScience 1984, 19:507-509.
    • (1984) HortScience , vol.19 , pp. 507-509
    • Driver, J.A.1    Kuniyuki, A.H.2
  • 37
    • 12744281106 scopus 로고    scopus 로고
    • Proteomic approach: Identification of Medicago truncatula proteins induced in roots after infection with the pathogenic oomycete Aphanomyces euteiches
    • Colditz F., Nyamsuren O., Niehaus H., Eubel H., Braun H.P., Krajinski F. Proteomic approach: Identification of Medicago truncatula proteins induced in roots after infection with the pathogenic oomycete Aphanomyces euteiches. Plant Mol Biol 2004, 55:109-120.
    • (2004) Plant Mol Biol , vol.55 , pp. 109-120
    • Colditz, F.1    Nyamsuren, O.2    Niehaus, H.3    Eubel, H.4    Braun, H.P.5    Krajinski, F.6
  • 38
    • 33645062273 scopus 로고    scopus 로고
    • Proteomics in plant biology
    • Humana Press, Totowa, P.M. Conn (Ed.)
    • Mihr C., Braun H.P. Proteomics in plant biology. Handbook of proteomic methods 2003, 409-416. Humana Press, Totowa. P.M. Conn (Ed.).
    • (2003) Handbook of proteomic methods , pp. 409-416
    • Mihr, C.1    Braun, H.P.2
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100kDalton
    • Schägger H., von Jagow G. Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1-100kDalton. Anal Biochem 1987, 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 40
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schägger H. Tricine-SDS-PAGE. Nat Protoc 2006, 1:16-22.
    • (2006) Nat Protoc , vol.1 , pp. 16-22
    • Schägger, H.1
  • 41
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: a systematic analysis
    • Neuhoff V., Stamm R., Eibl H. Clear background and highly sensitive protein staining with Coomassie Blue dyes in polyacrylamide gels: a systematic analysis. Electrophoresis 1985, 6:427-448.
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 42
    • 0025320429 scopus 로고
    • Essential problems in quantification of proteins following colloidal staining with Coomassie Brilliant Blue dyes in polyacrylamide gels, and their solution
    • Neuhoff V., Stamm R., Pardowitz I., Arold N., Ehrhardt W., Taube D. Essential problems in quantification of proteins following colloidal staining with Coomassie Brilliant Blue dyes in polyacrylamide gels, and their solution. Electrophoresis 1990, 11:101-117.
    • (1990) Electrophoresis , vol.11 , pp. 101-117
    • Neuhoff, V.1    Stamm, R.2    Pardowitz, I.3    Arold, N.4    Ehrhardt, W.5    Taube, D.6
  • 43
    • 34648834050 scopus 로고    scopus 로고
    • The state of the art in the analysis of two-dimensional gel electrophoresis images
    • Berth M., Moser F.M., Kolbe M., Bernhardt J. The state of the art in the analysis of two-dimensional gel electrophoresis images. Appl Microbiol Biotechnol 2007, 76:1223-1243.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 1223-1243
    • Berth, M.1    Moser, F.M.2    Kolbe, M.3    Bernhardt, J.4
  • 44
    • 77953226426 scopus 로고    scopus 로고
    • Internal architecture of mitochondrial complex I from Arabidopsis thaliana
    • Klodmann J., Sunderhaus S., Nimtz M., Jansch L., Braun H.P. Internal architecture of mitochondrial complex I from Arabidopsis thaliana. Plant Cell 2010, 22:797-810.
    • (2010) Plant Cell , vol.22 , pp. 797-810
    • Klodmann, J.1    Sunderhaus, S.2    Nimtz, M.3    Jansch, L.4    Braun, H.P.5
  • 47
    • 0036269594 scopus 로고    scopus 로고
    • Efficiency, genotypic variability, and cellular origin of primary and secondary somatic embryogenesis of Theobroma cacao L.
    • Maximova S.N., Alemanno L., Young A., Ferriere N., Traore A., Guiltinan M. Efficiency, genotypic variability, and cellular origin of primary and secondary somatic embryogenesis of Theobroma cacao L. In Vitro Cell Dev Biol Plant 2002, 38:252-259.
    • (2002) In Vitro Cell Dev Biol Plant , vol.38 , pp. 252-259
    • Maximova, S.N.1    Alemanno, L.2    Young, A.3    Ferriere, N.4    Traore, A.5    Guiltinan, M.6
  • 48
    • 0000164049 scopus 로고
    • Somatic embryogenesis in Camellia spp.
    • Somatic embryogenesis in woody plants
    • Vieitez A. Somatic embryogenesis in Camellia spp. Angiosperm 1995, vol. 2:63-70.
    • (1995) Angiosperm , vol.2 , pp. 63-70
    • Vieitez, A.1
  • 49
    • 66249138826 scopus 로고    scopus 로고
    • Proteomics, analysis of the development and germination of date palm (Phoenix dactylifera L.) zygotic embryos
    • Sghaier-Hammami B., Valledor L., Drira N., Jorrin-Novo V.J. Proteomics, analysis of the development and germination of date palm (Phoenix dactylifera L.) zygotic embryos. Proteomics 2009, 9:2543-2554.
    • (2009) Proteomics , vol.9 , pp. 2543-2554
    • Sghaier-Hammami, B.1    Valledor, L.2    Drira, N.3    Jorrin-Novo, V.J.4
  • 50
    • 0035196195 scopus 로고    scopus 로고
    • Analysis of carbohydrate metabolism enzymes and cellular contents of sugar and proteins during spruce somatic embryogenesis suggests a regulatory role of exogenous sucrose in embryo development
    • Iraqi D., Tremblay F.M. Analysis of carbohydrate metabolism enzymes and cellular contents of sugar and proteins during spruce somatic embryogenesis suggests a regulatory role of exogenous sucrose in embryo development. J Exp Bot 2001, 52:2301-2311.
    • (2001) J Exp Bot , vol.52 , pp. 2301-2311
    • Iraqi, D.1    Tremblay, F.M.2
  • 51
    • 0037700830 scopus 로고    scopus 로고
    • Enhanced low oxygen survival in Arabidopsis through increased metabolic flux in the fermentation pathway
    • Rudy K.P.I., Mary De Pauw D., Dennis E.S., Good A.G. Enhanced low oxygen survival in Arabidopsis through increased metabolic flux in the fermentation pathway. Plant Physiol 2003, 132:1292-1302.
    • (2003) Plant Physiol , vol.132 , pp. 1292-1302
    • Rudy, K.P.I.1    Mary De Pauw, D.2    Dennis, E.S.3    Good, A.G.4
  • 53
    • 72149108422 scopus 로고    scopus 로고
    • Fatty acid beta-oxidation in germinating Arabidopsis seeds is supported by peroxisomal hydroxypyruvate reductase when malate dehydrogenase is absent
    • Pracharoenwattana I., Zhou W., Smith S.M. Fatty acid beta-oxidation in germinating Arabidopsis seeds is supported by peroxisomal hydroxypyruvate reductase when malate dehydrogenase is absent. Plant Mol Biol 2010, 72:101-109.
    • (2010) Plant Mol Biol , vol.72 , pp. 101-109
    • Pracharoenwattana, I.1    Zhou, W.2    Smith, S.M.3
  • 54
    • 51149110721 scopus 로고    scopus 로고
    • Contrasting globulin and cysteine proteinase gene expression patterns reveal fundamental developmental differences between zygotic and somatic embryos of oil palm
    • Aberlenc-bertossi F., Chabrillange N., Duval Y., Tregear J. Contrasting globulin and cysteine proteinase gene expression patterns reveal fundamental developmental differences between zygotic and somatic embryos of oil palm. Tree Physiol 2008, 28:1157-1167.
    • (2008) Tree Physiol , vol.28 , pp. 1157-1167
    • Aberlenc-bertossi, F.1    Chabrillange, N.2    Duval, Y.3    Tregear, J.4
  • 55
    • 0000756509 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase: a ubiquitous, highly regulated enzyme in plants
    • Chollet R., Vidal J., O'Leary M.H. Phosphoenolpyruvate carboxylase: a ubiquitous, highly regulated enzyme in plants. Annu Rev Plant Physiol Plant Mol Biol 1996, 47:273-298.
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 273-298
    • Chollet, R.1    Vidal, J.2    O'Leary, M.H.3
  • 56
    • 0033103735 scopus 로고    scopus 로고
    • Phosphoenolpyruvate carboxylase in developing seeds on Vicia faba. Gene expression and metabolic regulation
    • Golombek S., Heim U., Horstmann C., Wobus U., Weber H. Phosphoenolpyruvate carboxylase in developing seeds on Vicia faba. Gene expression and metabolic regulation. Planta 1999, 208:66-72.
    • (1999) Planta , vol.208 , pp. 66-72
    • Golombek, S.1    Heim, U.2    Horstmann, C.3    Wobus, U.4    Weber, H.5
  • 57
    • 79955530030 scopus 로고    scopus 로고
    • The remarkable diversity of plant phosphoenolpyruvate carboxylase (PEPC): recent insights into the physiological functions and post-translational controls of nonphotosynthetic PEPCs
    • O'Leary B., Park J., Plaxton W.C. The remarkable diversity of plant phosphoenolpyruvate carboxylase (PEPC): recent insights into the physiological functions and post-translational controls of nonphotosynthetic PEPCs. Biochem J 2011, 436:15-34.
    • (2011) Biochem J , vol.436 , pp. 15-34
    • O'Leary, B.1    Park, J.2    Plaxton, W.C.3
  • 58
    • 51849182149 scopus 로고
    • Regulation of the activity of phosphoenolpyruvate carboxylase isolated from germinating maize (Zea mays L.) Seeds by Some Metabolites
    • Leblová S., Strakošová A., Vojtcehová M. Regulation of the activity of phosphoenolpyruvate carboxylase isolated from germinating maize (Zea mays L.) Seeds by Some Metabolites. Biol Plant 1991, 33:66-74.
    • (1991) Biol Plant , vol.33 , pp. 66-74
    • Leblová, S.1    Strakošová, A.2    Vojtcehová, M.3
  • 59
    • 0038271027 scopus 로고
    • PEP carboxylase and pyruvate kinase involvement in protein and oil biosynthesis during soybean seed development
    • Smith A.J., Rinne R.W., Seif R.D. PEP carboxylase and pyruvate kinase involvement in protein and oil biosynthesis during soybean seed development. Crop Sci 1989, 29:349-353.
    • (1989) Crop Sci , vol.29 , pp. 349-353
    • Smith, A.J.1    Rinne, R.W.2    Seif, R.D.3
  • 60
    • 0032037523 scopus 로고    scopus 로고
    • Expression and localization of PEP carboxylase in developing and germinating wheat grains
    • Gonzalez M.C., Osuna L., Echevarria C., Vidal J., Cejudo F.J. Expression and localization of PEP carboxylase in developing and germinating wheat grains. Plant Physiol 1998, 116:1249-1258.
    • (1998) Plant Physiol , vol.116 , pp. 1249-1258
    • Gonzalez, M.C.1    Osuna, L.2    Echevarria, C.3    Vidal, J.4    Cejudo, F.J.5
  • 61
    • 6444229398 scopus 로고    scopus 로고
    • Seed-specific expression of a bacterial phosphoenolpyruvate carboxylase in Vicia narbonensis increases protein content and improves carbon economy
    • Rolletschek H., Borisjuk L., Radchuk R., Miranda M., Heim U., Wobus U., et al. Seed-specific expression of a bacterial phosphoenolpyruvate carboxylase in Vicia narbonensis increases protein content and improves carbon economy. Plant Biotechnol J 2004, 2:211-219.
    • (2004) Plant Biotechnol J , vol.2 , pp. 211-219
    • Rolletschek, H.1    Borisjuk, L.2    Radchuk, R.3    Miranda, M.4    Heim, U.5    Wobus, U.6
  • 62
    • 0001221102 scopus 로고
    • Phosphoenolpyruvate carboxylase activity and concentration in the endosperm of developing and germinating castor oil seeds
    • Sangwan R.S., Singh N., Plaxton W.C. Phosphoenolpyruvate carboxylase activity and concentration in the endosperm of developing and germinating castor oil seeds. Plant Physiol 1992, 99:445-449.
    • (1992) Plant Physiol , vol.99 , pp. 445-449
    • Sangwan, R.S.1    Singh, N.2    Plaxton, W.C.3
  • 63
    • 0038485638 scopus 로고    scopus 로고
    • Structural and kinetic properties of high and low molecular mass phosphoenolpyruvate carboxylase isoforms from the endosperm of developing castor oilseeds
    • Blonde J.D., Plaxton W.C. Structural and kinetic properties of high and low molecular mass phosphoenolpyruvate carboxylase isoforms from the endosperm of developing castor oilseeds. J Biol Chem 2003, 278:11867-11873.
    • (2003) J Biol Chem , vol.278 , pp. 11867-11873
    • Blonde, J.D.1    Plaxton, W.C.2
  • 64
    • 0033214409 scopus 로고    scopus 로고
    • The sucrose-cleaving enzymes of plants are crucial for development, growth and carbon partitioning
    • Sturm A., Tang G.Q. The sucrose-cleaving enzymes of plants are crucial for development, growth and carbon partitioning. Trends Plant Sci 1999, 4:401-407.
    • (1999) Trends Plant Sci , vol.4 , pp. 401-407
    • Sturm, A.1    Tang, G.Q.2
  • 65
    • 0033984161 scopus 로고    scopus 로고
    • Regulation of sucrose metabolism in higher plants: localization and regulation of activity of key enzymes
    • Winter H., Huber S.C. Regulation of sucrose metabolism in higher plants: localization and regulation of activity of key enzymes. Crit Rev Plant Sci 2000, 19:31-67.
    • (2000) Crit Rev Plant Sci , vol.19 , pp. 31-67
    • Winter, H.1    Huber, S.C.2
  • 66
    • 0031407765 scopus 로고    scopus 로고
    • Carbohydrate content and enzyme metabolism in developing canola (Brassica napus L.) siliques
    • King S.P., Lunn J.E., Furbank R.T. Carbohydrate content and enzyme metabolism in developing canola (Brassica napus L.) siliques. Plant Physiol 1997, 114:153-160.
    • (1997) Plant Physiol , vol.114 , pp. 153-160
    • King, S.P.1    Lunn, J.E.2    Furbank, R.T.3
  • 67
    • 0037008225 scopus 로고    scopus 로고
    • The role of auxin, pH, and stress in the activation of embryogenic cell division in leaf protoplast-derived cells of Alfalfa
    • Pasternak T.P., Prinsen E., Ayaydin F., Miskolczi P., Potters G., Asard H., et al. The role of auxin, pH, and stress in the activation of embryogenic cell division in leaf protoplast-derived cells of Alfalfa. Plant Physiol 2002, 129:1807-1819.
    • (2002) Plant Physiol , vol.129 , pp. 1807-1819
    • Pasternak, T.P.1    Prinsen, E.2    Ayaydin, F.3    Miskolczi, P.4    Potters, G.5    Asard, H.6
  • 69
    • 34250014434 scopus 로고    scopus 로고
    • Pluripotent versus totipotent plant cells: dependence versus autonomy
    • Verdeil J.L., Alemanno L., Niemenak N., Tranbager T.J. Pluripotent versus totipotent plant cells: dependence versus autonomy. Trends Plant Sci 2007, 12:245-252.
    • (2007) Trends Plant Sci , vol.12 , pp. 245-252
    • Verdeil, J.L.1    Alemanno, L.2    Niemenak, N.3    Tranbager, T.J.4
  • 70
    • 0037507700 scopus 로고    scopus 로고
    • Clustring of microarray data reveals transcript patterns associated with somatic embryogenesis in soybean
    • Thibaud-Nissen F., Shealy R.T., Khanna A., Vodkin L.O. Clustring of microarray data reveals transcript patterns associated with somatic embryogenesis in soybean. Plant Physiol 2003, 132:118-136.
    • (2003) Plant Physiol , vol.132 , pp. 118-136
    • Thibaud-Nissen, F.1    Shealy, R.T.2    Khanna, A.3    Vodkin, L.O.4
  • 71
    • 0000677401 scopus 로고    scopus 로고
    • The functions and regulation of glutathione S-transferases in plants
    • Marrs K.A. The functions and regulation of glutathione S-transferases in plants. Annu Rev Plant Physiol Plant Mol Biol 1996, 47:127-158.
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 127-158
    • Marrs, K.A.1
  • 72
    • 0001931403 scopus 로고
    • Glutathione in the metabolism and detoxification of xenobiotics in plants
    • SPB: Academic Publishing, L.J. De Kok (Ed.)
    • Lamoureux G.L., Rusness D.G. Glutathione in the metabolism and detoxification of xenobiotics in plants. Sulfur Nutrition and Assimilation in Higher Plants 1993, 221-237. SPB: Academic Publishing. L.J. De Kok (Ed.).
    • (1993) Sulfur Nutrition and Assimilation in Higher Plants , pp. 221-237
    • Lamoureux, G.L.1    Rusness, D.G.2
  • 73
    • 0034192572 scopus 로고    scopus 로고
    • Plant glutathione S-transferases: enzymes with multiple functions in sickness and in health
    • Edwards R., Dixon D.P., Walbot V. Plant glutathione S-transferases: enzymes with multiple functions in sickness and in health. Trends Plant Sci 2000, 5:193-198.
    • (2000) Trends Plant Sci , vol.5 , pp. 193-198
    • Edwards, R.1    Dixon, D.P.2    Walbot, V.3
  • 74
    • 0029107096 scopus 로고
    • Developmental stage-dependent variation of the levels of globular storage protein and aspartic endoprotease during ripening and germination of Theobroma cacao L. seeds
    • Voigt J., Kamaruddin S., Heinrichs H., Wrann D., Senyuk V., Biehl B. Developmental stage-dependent variation of the levels of globular storage protein and aspartic endoprotease during ripening and germination of Theobroma cacao L. seeds. J Plant Physiol 1995, 145:299-307.
    • (1995) J Plant Physiol , vol.145 , pp. 299-307
    • Voigt, J.1    Kamaruddin, S.2    Heinrichs, H.3    Wrann, D.4    Senyuk, V.5    Biehl, B.6
  • 75
    • 0031046559 scopus 로고    scopus 로고
    • Aspartic proteinase levels in seeds of different angiosperms
    • Voigt G., Biehl B., Heinrichs H., Voigt J. Aspartic proteinase levels in seeds of different angiosperms. Phytochemistry 1997, 44:389-392.
    • (1997) Phytochemistry , vol.44 , pp. 389-392
    • Voigt, G.1    Biehl, B.2    Heinrichs, H.3    Voigt, J.4
  • 76
    • 14144252975 scopus 로고    scopus 로고
    • Identification and characterisation of the major aspartic proteinase activity in Theobroma cacao seeds
    • Guilloteau M., Laloi M., Michaux S., Bucheli P., McCarthy J. Identification and characterisation of the major aspartic proteinase activity in Theobroma cacao seeds. J Sci Food Agric 2005, 85:549-562.
    • (2005) J Sci Food Agric , vol.85 , pp. 549-562
    • Guilloteau, M.1    Laloi, M.2    Michaux, S.3    Bucheli, P.4    McCarthy, J.5
  • 77
    • 0026166258 scopus 로고
    • Nucleic acid sequence of a 21kDa cocoa seed protein with homology to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors
    • Tai H., McHenry L., Fritz P.J., Furtek D.B. Nucleic acid sequence of a 21kDa cocoa seed protein with homology to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. Plant Mol Biol 1991, 16:913-915.
    • (1991) Plant Mol Biol , vol.16 , pp. 913-915
    • Tai, H.1    McHenry, L.2    Fritz, P.J.3    Furtek, D.B.4
  • 78
    • 6844224205 scopus 로고
    • Purification of a trypsin inhibitor secreted by embryogenic carrot cells
    • Carlberg I., Jonsson L., Bergenstråhle A., Söderhäll K. Purification of a trypsin inhibitor secreted by embryogenic carrot cells. Plant Physiol 1987, 84:197-290.
    • (1987) Plant Physiol , vol.84 , pp. 197-290
    • Carlberg, I.1    Jonsson, L.2    Bergenstråhle, A.3    Söderhäll, K.4
  • 79
    • 0034913267 scopus 로고    scopus 로고
    • Ubiquitin and proteasome dependent proteolysis in plants
    • Ingvardsen C., Veierskov B. Ubiquitin and proteasome dependent proteolysis in plants. Physiol Plant 2001, 112:451-459.
    • (2001) Physiol Plant , vol.112 , pp. 451-459
    • Ingvardsen, C.1    Veierskov, B.2
  • 80
    • 27244444230 scopus 로고    scopus 로고
    • The plant VirE2 interacting protein 1. A molecular link between the agrobacterium T-Complex and the host cell chromatin?
    • Loyter A., Rosenbluh J., Zakai N., Li J., Kozlovsky S.V., Tzfira T., et al. The plant VirE2 interacting protein 1. A molecular link between the agrobacterium T-Complex and the host cell chromatin?. Plant Physiol 2005, 138:1318-1321.
    • (2005) Plant Physiol , vol.138 , pp. 1318-1321
    • Loyter, A.1    Rosenbluh, J.2    Zakai, N.3    Li, J.4    Kozlovsky, S.V.5    Tzfira, T.6
  • 81
    • 77956283656 scopus 로고    scopus 로고
    • A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability
    • Hurov K.E., Ramusino C.C., Elledge S.J. A genetic screen identifies the Triple T complex required for DNA damage signaling and ATM and ATR stability. Genes Dev 2010, 24:1939-1950.
    • (2010) Genes Dev , vol.24 , pp. 1939-1950
    • Hurov, K.E.1    Ramusino, C.C.2    Elledge, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.