메뉴 건너뛰기




Volumn 77, Issue , 2012, Pages 68-86

Proteomic analysis of embryonic axis of Pisum sativum seeds during germination and identification of proteins associated with loss of desiccation tolerance

Author keywords

Calcium ions; Desiccation tolerance; Embryonic axis of Pisum sativum seed; Germination; Methylviologen; Proteomics

Indexed keywords

CONVICILIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEIN CPN60; PROTEIN P54; PROTEIN SBP65; PROTEOME; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; VICILIN;

EID: 84870392796     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.07.005     Document Type: Article
Times cited : (74)

References (96)
  • 1
    • 0031420258 scopus 로고    scopus 로고
    • Seed germination and dormancy
    • Bewley J.D. Seed germination and dormancy. Plant Cell 1997, 9:1055-1066.
    • (1997) Plant Cell , vol.9 , pp. 1055-1066
    • Bewley, J.D.1
  • 2
    • 0002372534 scopus 로고
    • Physiological and metabolic study of the germination phases in apple embryo
    • Perino C., Côme D. Physiological and metabolic study of the germination phases in apple embryo. Seed Sci Technol 1991, 19:1-14.
    • (1991) Seed Sci Technol , vol.19 , pp. 1-14
    • Perino, C.1    Côme, D.2
  • 3
    • 84948074464 scopus 로고    scopus 로고
    • Mechanisms and genes involved in germination sensu stricto
    • Blackwell Publishing, Oxford, K.J. Bradford, H. Nonogaki (Eds.)
    • Nonogaki H., Chen F., Bradford K.J. Mechanisms and genes involved in germination sensu stricto. Seed development, dormancy and germination 2007, 264-304. Blackwell Publishing, Oxford. K.J. Bradford, H. Nonogaki (Eds.).
    • (2007) Seed development, dormancy and germination , pp. 264-304
    • Nonogaki, H.1    Chen, F.2    Bradford, K.J.3
  • 5
    • 0030301921 scopus 로고    scopus 로고
    • The effects of manure, genotype, seed priming, depth and date of sowing on the emergence and early growth of Sorghum bicolor (L) Moench in semi-arid Botswana
    • Harris D. The effects of manure, genotype, seed priming, depth and date of sowing on the emergence and early growth of Sorghum bicolor (L) Moench in semi-arid Botswana. Soil Till Res 1996, 40:73-88.
    • (1996) Soil Till Res , vol.40 , pp. 73-88
    • Harris, D.1
  • 7
    • 0034489196 scopus 로고    scopus 로고
    • The evolution of vegetative desiccation tolerance in land plants
    • Oliver M.J., Tuba Z., Mishler B.D. The evolution of vegetative desiccation tolerance in land plants. Plant Ecol 2000, 151:85-100.
    • (2000) Plant Ecol , vol.151 , pp. 85-100
    • Oliver, M.J.1    Tuba, Z.2    Mishler, B.D.3
  • 9
    • 0003127213 scopus 로고
    • Acquisition and loss of desiccation tolerance
    • Marcel Dekker Inc., New York, J. Kigel, G. Galili (Eds.)
    • Vertucci C.W., Farrant J.M. Acquisition and loss of desiccation tolerance. Seed development and germination 1995, 149-184. Marcel Dekker Inc., New York. J. Kigel, G. Galili (Eds.).
    • (1995) Seed development and germination , pp. 149-184
    • Vertucci, C.W.1    Farrant, J.M.2
  • 10
    • 0002658365 scopus 로고    scopus 로고
    • Desiccation sensitivity in orthodox and recalcitrant seeds in relation to development
    • CABI Publishing, Oxon, M. Black, H.W. Pritchard (Eds.)
    • Kermode A., Finch-Savage W.E. Desiccation sensitivity in orthodox and recalcitrant seeds in relation to development. Desiccation and Survival in Plants: Drying without Dying 2002, 149-184. CABI Publishing, Oxon. M. Black, H.W. Pritchard (Eds.).
    • (2002) Desiccation and Survival in Plants: Drying without Dying , pp. 149-184
    • Kermode, A.1    Finch-Savage, W.E.2
  • 11
    • 0001061134 scopus 로고
    • Desiccation-tolerant and desiccation-intolerant stages during the development and germination of Phaseolus vulgaris seeds
    • Dasgupta J., Bewley J.D., Yeung E.C. Desiccation-tolerant and desiccation-intolerant stages during the development and germination of Phaseolus vulgaris seeds. J Exp Bot 1982, 33:1045-1057.
    • (1982) J Exp Bot , vol.33 , pp. 1045-1057
    • Dasgupta, J.1    Bewley, J.D.2    Yeung, E.C.3
  • 12
    • 0000830034 scopus 로고
    • Dehydration injury in germinating soybean (Glycine max (L.) Merr.) seeds
    • Senaratna T., McKersie B.D. Dehydration injury in germinating soybean (Glycine max (L.) Merr.) seeds. Plant Physiol 1983, 72:620-624.
    • (1983) Plant Physiol , vol.72 , pp. 620-624
    • Senaratna, T.1    McKersie, B.D.2
  • 13
    • 85032068559 scopus 로고
    • Sugars and desiccation tolerance in seeds
    • Koster K.L., Leopold A.C. Sugars and desiccation tolerance in seeds. Plant Physiol 1988, 88:829-832.
    • (1988) Plant Physiol , vol.88 , pp. 829-832
    • Koster, K.L.1    Leopold, A.C.2
  • 14
    • 0032955045 scopus 로고    scopus 로고
    • Progressive loss of desiccation tolerance in germinating pea (Pisum sativum) seeds
    • Reisdorph N.A., Koster K.L. Progressive loss of desiccation tolerance in germinating pea (Pisum sativum) seeds. Physiol Plant 1999, 105:266-271.
    • (1999) Physiol Plant , vol.105 , pp. 266-271
    • Reisdorph, N.A.1    Koster, K.L.2
  • 15
    • 33745476713 scopus 로고    scopus 로고
    • Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance
    • Boudet J., Buitink J., Hoekstra F.A., Rogniaux H., Larre C., Satour P., et al. Comparative analysis of the heat stable proteome of radicles of Medicago truncatula seeds during germination identifies late embryogenesis abundant proteins associated with desiccation tolerance. Plant Physiol 2006, 140:1418-1436.
    • (2006) Plant Physiol , vol.140 , pp. 1418-1436
    • Boudet, J.1    Buitink, J.2    Hoekstra, F.A.3    Rogniaux, H.4    Larre, C.5    Satour, P.6
  • 18
    • 70350676694 scopus 로고    scopus 로고
    • Post-genomics studies of developmental processes in legume seeds
    • Thompson R., Burstin J., Gallardo K. Post-genomics studies of developmental processes in legume seeds. Plant Physiol 2009, 151:1023-1029.
    • (2009) Plant Physiol , vol.151 , pp. 1023-1029
    • Thompson, R.1    Burstin, J.2    Gallardo, K.3
  • 19
    • 80054724606 scopus 로고    scopus 로고
    • Proteomics and posttranslational proteomics of seed dormancy and germination
    • Rajjou L., Belghazi M., Catusse J., Ogè L., Arc E., Godin B., et al. Proteomics and posttranslational proteomics of seed dormancy and germination. Methods Mol Biol 2011, 773:215-236.
    • (2011) Methods Mol Biol , vol.773 , pp. 215-236
    • Rajjou, L.1    Belghazi, M.2    Catusse, J.3    Ogè, L.4    Arc, E.5    Godin, B.6
  • 21
    • 0035983666 scopus 로고    scopus 로고
    • Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds
    • Gallardo K., Job C., Groot S.P.C., Puype M., Demol H., Vandekerckhove J., et al. Proteomics of Arabidopsis seed germination. A comparative study of wild-type and gibberellin-deficient seeds. Plant Physiol 2002, 129:823-837.
    • (2002) Plant Physiol , vol.129 , pp. 823-837
    • Gallardo, K.1    Job, C.2    Groot, S.P.C.3    Puype, M.4    Demol, H.5    Vandekerckhove, J.6
  • 22
    • 3543141896 scopus 로고    scopus 로고
    • Proteome analysis of barley seeds: Identification of major proteins from two-dimensional gels (pI 4-7)
    • Østergaard O., Finnie C., Laugesen S., Roepstorff P., Svensson B. Proteome analysis of barley seeds: Identification of major proteins from two-dimensional gels (pI 4-7). Proteomics 2004, 4:2437-2447.
    • (2004) Proteomics , vol.4 , pp. 2437-2447
    • Østergaard, O.1    Finnie, C.2    Laugesen, S.3    Roepstorff, P.4    Svensson, B.5
  • 23
    • 38049070264 scopus 로고    scopus 로고
    • Spatio-temporal changes in germination and radical elongation of barley seeds tracked by proteome analysis of dissected embryo, aleurone layer, and endosperm tissues
    • Bønsager B.C., Finnie C., Roepstorff P., Svensson B. Spatio-temporal changes in germination and radical elongation of barley seeds tracked by proteome analysis of dissected embryo, aleurone layer, and endosperm tissues. Proteomics 2007, 7:4528-4540.
    • (2007) Proteomics , vol.7 , pp. 4528-4540
    • Bønsager, B.C.1    Finnie, C.2    Roepstorff, P.3    Svensson, B.4
  • 24
    • 25844437437 scopus 로고    scopus 로고
    • Proteome analysis of embryo and endosperm from germinating tomato seeds
    • Sheoran I.S., Olson D.J.H., Ross A.R.S., Sawhney V.K. Proteome analysis of embryo and endosperm from germinating tomato seeds. Proteomics 2005, 5:3752-3764.
    • (2005) Proteomics , vol.5 , pp. 3752-3764
    • Sheoran, I.S.1    Olson, D.J.H.2    Ross, A.R.S.3    Sawhney, V.K.4
  • 25
    • 34948864529 scopus 로고    scopus 로고
    • Proteomic analysis of rice (Oryza sativa) seeds during germination
    • Yang P.F., Li X.J., Wang X.Q., Chen H., Chen F., Shen S.H. Proteomic analysis of rice (Oryza sativa) seeds during germination. Proteomics 2007, 7:3358-3368.
    • (2007) Proteomics , vol.7 , pp. 3358-3368
    • Yang, P.F.1    Li, X.J.2    Wang, X.Q.3    Chen, H.4    Chen, F.5    Shen, S.H.6
  • 26
    • 79954988552 scopus 로고    scopus 로고
    • Proteomics reveals potential biomarkers of seed vigor in sugarbeet
    • Job D., Catusse J., Meinhard J., Job C., Strub J.M., Fischer U., et al. Proteomics reveals potential biomarkers of seed vigor in sugarbeet. Proteomics 2011, 11:1569-1580.
    • (2011) Proteomics , vol.11 , pp. 1569-1580
    • Job, D.1    Catusse, J.2    Meinhard, J.3    Job, C.4    Strub, J.M.5    Fischer, U.6
  • 27
    • 80052481465 scopus 로고    scopus 로고
    • Toward characterizing seed vigor in alfalfa through proteomic analysis of germination and priming
    • Yacoubi R., Job C., Belghazi M., Chaibi W., Job D. Toward characterizing seed vigor in alfalfa through proteomic analysis of germination and priming. J Proteome Res 2011, 10:3891-3903.
    • (2011) J Proteome Res , vol.10 , pp. 3891-3903
    • Yacoubi, R.1    Job, C.2    Belghazi, M.3    Chaibi, W.4    Job, D.5
  • 28
    • 84855875396 scopus 로고    scopus 로고
    • Proteomics of desiccation tolerance during development and germination of maize embryos
    • Huang H., Møller I.M., Song S.Q. Proteomics of desiccation tolerance during development and germination of maize embryos. J Proteomics 2012, 75:1247-1262.
    • (2012) J Proteomics , vol.75 , pp. 1247-1262
    • Huang, H.1    Møller, I.M.2    Song, S.Q.3
  • 29
    • 78049270809 scopus 로고    scopus 로고
    • Desiccation tolerance: from genomics to the field
    • Leprince O., Buitink J. Desiccation tolerance: from genomics to the field. Plant Sci 2010, 179:554-564.
    • (2010) Plant Sci , vol.179 , pp. 554-564
    • Leprince, O.1    Buitink, J.2
  • 30
    • 0029108889 scopus 로고
    • Induction of desiccation tolerance in germinated seeds
    • Bruggink T., Vandertoorn P. Induction of desiccation tolerance in germinated seeds. Seed Sci Res 1995, 5:1-4.
    • (1995) Seed Sci Res , vol.5 , pp. 1-4
    • Bruggink, T.1    Vandertoorn, P.2
  • 31
    • 83355170724 scopus 로고    scopus 로고
    • The re-establishment of desiccation tolerance in germinated Arabidopsis thaliana seeds and its associated transcriptome
    • Maia J., Dekkers B.J.W., Provart N.J., Ligterink W., Hilhorst H.W.M. The re-establishment of desiccation tolerance in germinated Arabidopsis thaliana seeds and its associated transcriptome. PLoS One 2011, 6. 10.1371/journal.pone.0029123.
    • (2011) PLoS One , pp. 6
    • Maia, J.1    Dekkers, B.J.W.2    Provart, N.J.3    Ligterink, W.4    Hilhorst, H.W.M.5
  • 32
    • 83555174461 scopus 로고    scopus 로고
    • The role of recovery of mitochondrial structure and function in desiccation tolerance of pea seeds
    • Wang W.Q., Cheng H.Y., Møller I.M., Song S.Q. The role of recovery of mitochondrial structure and function in desiccation tolerance of pea seeds. Physiol Plant 2012, 144:20-34.
    • (2012) Physiol Plant , vol.144 , pp. 20-34
    • Wang, W.Q.1    Cheng, H.Y.2    Møller, I.M.3    Song, S.Q.4
  • 33
    • 60349108930 scopus 로고    scopus 로고
    • Dissecting the proteome of pea mature seeds reveals the phenotypic plasticity of seed protein composition
    • Bourgeois M., Jacquin F., Savois V., Sommerer N., Labas V., Henry C., et al. Dissecting the proteome of pea mature seeds reveals the phenotypic plasticity of seed protein composition. Proteomics 2009, 9:254-271.
    • (2009) Proteomics , vol.9 , pp. 254-271
    • Bourgeois, M.1    Jacquin, F.2    Savois, V.3    Sommerer, N.4    Labas, V.5    Henry, C.6
  • 35
    • 0003181490 scopus 로고    scopus 로고
    • International rules for seed testing
    • International Seed Testing Association
    • International Seed Testing Association International rules for seed testing. Seed Sci Technol 1999, 27(Suppl.):47-50.
    • (1999) Seed Sci Technol , vol.27 , Issue.SUPPL. , pp. 47-50
  • 36
    • 0001510436 scopus 로고
    • Solubilization of plant membrane-proteins for analysis by two-dimensional gel electrophoresis
    • Hurkman W.J., Tanaka C.K. Solubilization of plant membrane-proteins for analysis by two-dimensional gel electrophoresis. Plant Physiol 1986, 81:802-806.
    • (1986) Plant Physiol , vol.81 , pp. 802-806
    • Hurkman, W.J.1    Tanaka, C.K.2
  • 37
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Analyt Chem 1996, 68:850-858.
    • (1996) Analyt Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 40
    • 84859820774 scopus 로고    scopus 로고
    • Mobilization of seed protein reserves
    • Tan-Wilson A.L., Wilson K.A. Mobilization of seed protein reserves. Physiol Plant 2012, 145:140-153.
    • (2012) Physiol Plant , vol.145 , pp. 140-153
    • Tan-Wilson, A.L.1    Wilson, K.A.2
  • 42
    • 1942469546 scopus 로고    scopus 로고
    • The effect of alpha-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 alpha-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
  • 43
    • 79953721157 scopus 로고    scopus 로고
    • Translation initiation: variations in the mechanism can be anticipated
    • Malys N., McCarthy J.E.G. Translation initiation: variations in the mechanism can be anticipated. Cell Mol Life Sci 2011, 68:991-1003.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 991-1003
    • Malys, N.1    McCarthy, J.E.G.2
  • 44
    • 0032560569 scopus 로고    scopus 로고
    • The specific features of methionine biosynthesis and metabolism in plants
    • Ravanel S., Gakière B., Job D., Douce R. The specific features of methionine biosynthesis and metabolism in plants. Proc Natl Acad Sci USA 1998, 95:7805-7812.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7805-7812
    • Ravanel, S.1    Gakière, B.2    Job, D.3    Douce, R.4
  • 45
    • 0036789354 scopus 로고    scopus 로고
    • Importance of methionine biosynthesis for Arabidopsis seed germination and seedling growth
    • Gallardo K., Job C., Groot S.P.C., Puype M., Demol H., Vandekerckhove J., et al. Importance of methionine biosynthesis for Arabidopsis seed germination and seedling growth. Physiol Plant 2002, 116:238-247.
    • (2002) Physiol Plant , vol.116 , pp. 238-247
    • Gallardo, K.1    Job, C.2    Groot, S.P.C.3    Puype, M.4    Demol, H.5    Vandekerckhove, J.6
  • 46
    • 14844337487 scopus 로고    scopus 로고
    • Genome-wide profiling of stored mRNA in Arabidopsis thaliana seed germination: epigenetic and genetic regulation of transcription in seed
    • Nakabayashi K., Okamoto M., Koshiba T., Kamiya Y., Nambara E. Genome-wide profiling of stored mRNA in Arabidopsis thaliana seed germination: epigenetic and genetic regulation of transcription in seed. Plant J 2005, 41:697-709.
    • (2005) Plant J , vol.41 , pp. 697-709
    • Nakabayashi, K.1    Okamoto, M.2    Koshiba, T.3    Kamiya, Y.4    Nambara, E.5
  • 47
    • 48549089299 scopus 로고    scopus 로고
    • Barley grain maturation and germination: metabolic pathway and regulatory network commonalities and differences highlighted by new MapMan/PageMan profiling tools
    • Sreenivasulu N., Usadel B., Winter A., Radchuk V., Scholz U., Stein N., et al. Barley grain maturation and germination: metabolic pathway and regulatory network commonalities and differences highlighted by new MapMan/PageMan profiling tools. Plant Physiol 2008, 146:1738-1758.
    • (2008) Plant Physiol , vol.146 , pp. 1738-1758
    • Sreenivasulu, N.1    Usadel, B.2    Winter, A.3    Radchuk, V.4    Scholz, U.5    Stein, N.6
  • 48
    • 60249086736 scopus 로고    scopus 로고
    • Mapping metabolic and transcript temporal switches during germination in rice highlights specific transcription factors and the role of RNA instability in the germination process
    • Howell K.A., Narsai R., Carroll A., Ivanova A., Lohse M., Usadel B., et al. Mapping metabolic and transcript temporal switches during germination in rice highlights specific transcription factors and the role of RNA instability in the germination process. Plant Physiol 2009, 149:961-980.
    • (2009) Plant Physiol , vol.149 , pp. 961-980
    • Howell, K.A.1    Narsai, R.2    Carroll, A.3    Ivanova, A.4    Lohse, M.5    Usadel, B.6
  • 50
    • 0036742742 scopus 로고    scopus 로고
    • Sterol C-24 methyltransferase type 1 controls the flux of carbon into sterol biosynthesis in tobacco seed
    • Holmberg N., Harker M., Gibbard C.L., Wallace A.D., Clayton J.C., Rawlins S., et al. Sterol C-24 methyltransferase type 1 controls the flux of carbon into sterol biosynthesis in tobacco seed. Plant Physiol 2002, 130:303-311.
    • (2002) Plant Physiol , vol.130 , pp. 303-311
    • Holmberg, N.1    Harker, M.2    Gibbard, C.L.3    Wallace, A.D.4    Clayton, J.C.5    Rawlins, S.6
  • 51
    • 0031470336 scopus 로고    scopus 로고
    • Cloning of cDNAs or genes encoding enzymes of sterol biosynthesis from plants and other eukaryotes: heterologous expression and complementation analysis of mutations for functional characterization
    • Bach T.J., Benveniste P. Cloning of cDNAs or genes encoding enzymes of sterol biosynthesis from plants and other eukaryotes: heterologous expression and complementation analysis of mutations for functional characterization. Prog Lipid Res 1997, 36:197-226.
    • (1997) Prog Lipid Res , vol.36 , pp. 197-226
    • Bach, T.J.1    Benveniste, P.2
  • 52
    • 0033999195 scopus 로고    scopus 로고
    • Abscisic acid inhibition of radicle emergence but not seedling growth is suppressed by sugars
    • Finkelstein R.R., Lynch T.J. Abscisic acid inhibition of radicle emergence but not seedling growth is suppressed by sugars. Plant Physiol 2000, 122:1179-1186.
    • (2000) Plant Physiol , vol.122 , pp. 1179-1186
    • Finkelstein, R.R.1    Lynch, T.J.2
  • 53
    • 84948098396 scopus 로고    scopus 로고
    • Sugar and abscisic acid regulation of germination and transition to seedling growth
    • Blackwell Publishing, Oxford, K.J. Bradford, H. Nonogaki (Eds.)
    • Dekkers B.J.W., Smeekens S.C.M. Sugar and abscisic acid regulation of germination and transition to seedling growth. Seed Development, Dormancy and Germination 2007, 305-327. Blackwell Publishing, Oxford. K.J. Bradford, H. Nonogaki (Eds.).
    • (2007) Seed Development, Dormancy and Germination , pp. 305-327
    • Dekkers, B.J.W.1    Smeekens, S.C.M.2
  • 54
    • 0031430935 scopus 로고    scopus 로고
    • Ethylene in seed dormancy and germination
    • Kepczynski J., Kepczynska E. Ethylene in seed dormancy and germination. Physiol Plant 1997, 101:720-726.
    • (1997) Physiol Plant , vol.101 , pp. 720-726
    • Kepczynski, J.1    Kepczynska, E.2
  • 55
    • 0033937171 scopus 로고    scopus 로고
    • Ethylene promotes ethylene biosynthesis during pea seed germination by positive feedback regulation of 1-aminocyclopropane-1-carboxylic acid oxidase
    • Petruzzelli L., Coraggio I., Leubner-Metzger G. Ethylene promotes ethylene biosynthesis during pea seed germination by positive feedback regulation of 1-aminocyclopropane-1-carboxylic acid oxidase. Planta 2000, 211:144-149.
    • (2000) Planta , vol.211 , pp. 144-149
    • Petruzzelli, L.1    Coraggio, I.2    Leubner-Metzger, G.3
  • 56
    • 0344417107 scopus 로고    scopus 로고
    • Rac homologues and compartmentalized phosphatidylinositol 4,5-bisphosphate act in a common pathway to regulate polar pollen tube growth
    • Kost B., Lemichez E., Spielhofer P., Hong Y., Tolias K., Carpenter C., et al. Rac homologues and compartmentalized phosphatidylinositol 4,5-bisphosphate act in a common pathway to regulate polar pollen tube growth. J Cell Biol 1999, 145:317-330.
    • (1999) J Cell Biol , vol.145 , pp. 317-330
    • Kost, B.1    Lemichez, E.2    Spielhofer, P.3    Hong, Y.4    Tolias, K.5    Carpenter, C.6
  • 57
    • 33745628866 scopus 로고    scopus 로고
    • Control of the actin cytoskeleton in plant cell growth
    • Hussey P.J., Ketelaar T., Deeks M.J. Control of the actin cytoskeleton in plant cell growth. Annu Rev Plant Biol 2006, 57:109-125.
    • (2006) Annu Rev Plant Biol , vol.57 , pp. 109-125
    • Hussey, P.J.1    Ketelaar, T.2    Deeks, M.J.3
  • 58
    • 44349105297 scopus 로고    scopus 로고
    • Actin depolymerizing factor is essential for viability in plants, and its phosphoregulation is important for tip growth
    • Augustine R.C., Vidali L., Kleinman K.P., Bezanilla M. Actin depolymerizing factor is essential for viability in plants, and its phosphoregulation is important for tip growth. Plant J 2008, 54:863-875.
    • (2008) Plant J , vol.54 , pp. 863-875
    • Augustine, R.C.1    Vidali, L.2    Kleinman, K.P.3    Bezanilla, M.4
  • 59
    • 0028000960 scopus 로고
    • Accumulation of reactive oxygen species and oxidation of cytokinin in germinating soybean seeds
    • Gidrol X., Lin W.S., Degousee N., Yip S.F., Kush A. Accumulation of reactive oxygen species and oxidation of cytokinin in germinating soybean seeds. Eur J Biochem 1994, 224:21-28.
    • (1994) Eur J Biochem , vol.224 , pp. 21-28
    • Gidrol, X.1    Lin, W.S.2    Degousee, N.3    Yip, S.F.4    Kush, A.5
  • 60
    • 0035030687 scopus 로고    scopus 로고
    • Release of reactive oxygen intermediates (superoxide radicals, hydrogen peroxide, and hydroxyl radicals) and peroxidase in germinating radish seeds controlled by light, gibberellin, and abscisic acid
    • Schopfer P., Plachy C., Frahry G. Release of reactive oxygen intermediates (superoxide radicals, hydrogen peroxide, and hydroxyl radicals) and peroxidase in germinating radish seeds controlled by light, gibberellin, and abscisic acid. Plant Physiol 2001, 125:1591-1602.
    • (2001) Plant Physiol , vol.125 , pp. 1591-1602
    • Schopfer, P.1    Plachy, C.2    Frahry, G.3
  • 61
    • 0036217756 scopus 로고    scopus 로고
    • Changes in activities of antioxidant enzymes and lipoxygenase during growth of sunflower seedlings from seeds of different vigour
    • Bailly C., Bogatek-Leszczynska R., Côme D., Corbineau F. Changes in activities of antioxidant enzymes and lipoxygenase during growth of sunflower seedlings from seeds of different vigour. Seed Sci Res 2002, 12:47-55.
    • (2002) Seed Sci Res , vol.12 , pp. 47-55
    • Bailly, C.1    Bogatek-Leszczynska, R.2    Côme, D.3    Corbineau, F.4
  • 62
    • 0035983788 scopus 로고    scopus 로고
    • Peroxidase activity develops in the micropylar endosperm of tomato seeds prior to radicle protrusion
    • Morohashi Y. Peroxidase activity develops in the micropylar endosperm of tomato seeds prior to radicle protrusion. J Exp Bot 2002, 53:1643-1650.
    • (2002) J Exp Bot , vol.53 , pp. 1643-1650
    • Morohashi, Y.1
  • 63
    • 34250849635 scopus 로고    scopus 로고
    • Oxidative modifications to cellular components in plants
    • Møller I.M., Jensen P.E., Hansson A. Oxidative modifications to cellular components in plants. Annu Rev Plant Biol 2007, 58:459-481.
    • (2007) Annu Rev Plant Biol , vol.58 , pp. 459-481
    • Møller, I.M.1    Jensen, P.E.2    Hansson, A.3
  • 64
    • 3042850902 scopus 로고    scopus 로고
    • Active oxygen species and antioxidants in seed biology
    • Bailly C. Active oxygen species and antioxidants in seed biology. Seed Sci Res 2004, 14:93-107.
    • (2004) Seed Sci Res , vol.14 , pp. 93-107
    • Bailly, C.1
  • 65
    • 33845667960 scopus 로고    scopus 로고
    • Reactive oxygen species generation and antioxidant systems in plant mitochondria
    • Navrot N., Rouhier N., Gelhaye E., Jacquot J.P. Reactive oxygen species generation and antioxidant systems in plant mitochondria. Physiol Plant 2007, 129:185-195.
    • (2007) Physiol Plant , vol.129 , pp. 185-195
    • Navrot, N.1    Rouhier, N.2    Gelhaye, E.3    Jacquot, J.P.4
  • 66
    • 0041762551 scopus 로고    scopus 로고
    • Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance
    • Sunkar R., Bartels D., Kirch H.H. Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance. Plant J 2003, 35:452-464.
    • (2003) Plant J , vol.35 , pp. 452-464
    • Sunkar, R.1    Bartels, D.2    Kirch, H.H.3
  • 67
    • 37849036809 scopus 로고    scopus 로고
    • From avicennia to zizania: seed recalcitrance in perspective
    • Berjak P., Pammenter N.W. From avicennia to zizania: seed recalcitrance in perspective. Ann Bot 2008, 101:213-228.
    • (2008) Ann Bot , vol.101 , pp. 213-228
    • Berjak, P.1    Pammenter, N.W.2
  • 68
    • 0029587196 scopus 로고
    • Seed storage proteins of spermatophytes share a common ancestor with desiccation proteins of fungi
    • Baumlein H., Braun H., Kakhovskaya I.A., Shutov A.D. Seed storage proteins of spermatophytes share a common ancestor with desiccation proteins of fungi. J Mol Evol 1995, 41:1070-1075.
    • (1995) J Mol Evol , vol.41 , pp. 1070-1075
    • Baumlein, H.1    Braun, H.2    Kakhovskaya, I.A.3    Shutov, A.D.4
  • 69
    • 33747053339 scopus 로고    scopus 로고
    • Transcriptome profiling uncovers metabolic and regulatory processes occurring during the transition from desiccation-sensitive to desiccation-tolerant stages in Medicago truncatula seeds
    • Buitink J., Leger J.J., Guisle I., Vu B.L., Wuilleme S., Lamirault G., et al. Transcriptome profiling uncovers metabolic and regulatory processes occurring during the transition from desiccation-sensitive to desiccation-tolerant stages in Medicago truncatula seeds. Plant J 2006, 47:735-750.
    • (2006) Plant J , vol.47 , pp. 735-750
    • Buitink, J.1    Leger, J.J.2    Guisle, I.3    Vu, B.L.4    Wuilleme, S.5    Lamirault, G.6
  • 70
    • 0030857939 scopus 로고    scopus 로고
    • The solubilization of the basic subunit of sugar beetseed 11-S globulin during priming and early germination
    • Job C., Kersulec A., Ravasio L., Chareyre S., Pepin R. The solubilization of the basic subunit of sugar beetseed 11-S globulin during priming and early germination. Seed Sci Res 1997, 3:225-244.
    • (1997) Seed Sci Res , vol.3 , pp. 225-244
    • Job, C.1    Kersulec, A.2    Ravasio, L.3    Chareyre, S.4    Pepin, R.5
  • 71
    • 0033645832 scopus 로고    scopus 로고
    • Sugarbeet seed priming: effects of priming conditions on germination, solubilization of 11-S globulin and accumulation of LEA proteins
    • Capron I., Corbineau F., Dacher F., Job C., Côme D., Job D. Sugarbeet seed priming: effects of priming conditions on germination, solubilization of 11-S globulin and accumulation of LEA proteins. Seed Sci Res 2000, 10:243-254.
    • (2000) Seed Sci Res , vol.10 , pp. 243-254
    • Capron, I.1    Corbineau, F.2    Dacher, F.3    Job, C.4    Côme, D.5    Job, D.6
  • 73
    • 0033197643 scopus 로고    scopus 로고
    • A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels
    • Marcus J.P., Green J.L., Goulter K.C., Manners J.M. A family of antimicrobial peptides is produced by processing of a 7S globulin protein in Macadamia integrifolia kernels. Plant J 1999, 19:699-710.
    • (1999) Plant J , vol.19 , pp. 699-710
    • Marcus, J.P.1    Green, J.L.2    Goulter, K.C.3    Manners, J.M.4
  • 75
    • 80053892540 scopus 로고    scopus 로고
    • Plant storage proteins with antimicrobial activity: novel insights into plant defense mechanisms
    • Cândido E.D., Pinto M.F.S., Pelegrini P.B., Lima T.B., Silva O.N., Pogue R., et al. Plant storage proteins with antimicrobial activity: novel insights into plant defense mechanisms. FASEB J 2011, 25:3290-3305.
    • (2011) FASEB J , vol.25 , pp. 3290-3305
    • Cândido, E.D.1    Pinto, M.F.S.2    Pelegrini, P.B.3    Lima, T.B.4    Silva, O.N.5    Pogue, R.6
  • 76
    • 0033784133 scopus 로고    scopus 로고
    • Do legume storage proteins play a role in defending seeds against bruchids?
    • Sales M.P., Gerhardt I.R., Grossi-de-Sá M.F., Xavier J. Do legume storage proteins play a role in defending seeds against bruchids?. Plant Physiol 2000, 124:515-522.
    • (2000) Plant Physiol , vol.124 , pp. 515-522
    • Sales, M.P.1    Gerhardt, I.R.2    Grossi-de-Sá, M.F.3    Xavier, J.4
  • 77
    • 0029278045 scopus 로고
    • Molecular-cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan
    • Chang M.M., Horovitz D., Culley D., Hadwiger L.A. Molecular-cloning and characterization of a pea chitinase gene expressed in response to wounding, fungal infection and the elicitor chitosan. Plant Mol Biol 1995, 28:105-111.
    • (1995) Plant Mol Biol , vol.28 , pp. 105-111
    • Chang, M.M.1    Horovitz, D.2    Culley, D.3    Hadwiger, L.A.4
  • 78
    • 0036010840 scopus 로고    scopus 로고
    • Transgenic potatoes with enhanced levels of nematode resistance do not have altered susceptibility to nontarget aphids
    • Cowgill S.E., Wright C., Atkinson H.J. Transgenic potatoes with enhanced levels of nematode resistance do not have altered susceptibility to nontarget aphids. Mol Ecol 2002, 11:821-827.
    • (2002) Mol Ecol , vol.11 , pp. 821-827
    • Cowgill, S.E.1    Wright, C.2    Atkinson, H.J.3
  • 79
    • 0037394766 scopus 로고    scopus 로고
    • Effects of the cysteine protease inhibitor oryzacystatin (OC-I) on different aphids and reduced performance of Myzus persicae on OC-I expressing transgenic oilseed rape
    • Rahbe Y., Deraison C., Bonade-Bottino M., Girard C., Nardon C., Jouanin L. Effects of the cysteine protease inhibitor oryzacystatin (OC-I) on different aphids and reduced performance of Myzus persicae on OC-I expressing transgenic oilseed rape. Plant Sci 2003, 164:441-450.
    • (2003) Plant Sci , vol.164 , pp. 441-450
    • Rahbe, Y.1    Deraison, C.2    Bonade-Bottino, M.3    Girard, C.4    Nardon, C.5    Jouanin, L.6
  • 80
    • 45849099542 scopus 로고    scopus 로고
    • Plant protease inhibitors: a defense strategy in plants
    • Habib H., Fazili K. Plant protease inhibitors: a defense strategy in plants. Biotechnol Mol Biol Rev 2007, 22:68-85.
    • (2007) Biotechnol Mol Biol Rev , vol.22 , pp. 68-85
    • Habib, H.1    Fazili, K.2
  • 81
    • 0003006737 scopus 로고    scopus 로고
    • LEA proteins
    • Kluwer Academic Press, Dordrecht, The Netherlands, P.R. Shewry, R. Casey (Eds.)
    • Cuming A.C. LEA proteins. Seed Proteins 1999, 753-780. Kluwer Academic Press, Dordrecht, The Netherlands. P.R. Shewry, R. Casey (Eds.).
    • (1999) Seed Proteins , pp. 753-780
    • Cuming, A.C.1
  • 83
    • 0033948588 scopus 로고    scopus 로고
    • Protein analysis during almond embryo development. Identification and characterization of a late embryogenesis abundant protein
    • Campalans A., Pages M., Messeguer R. Protein analysis during almond embryo development. Identification and characterization of a late embryogenesis abundant protein. Plant Physiol Bioch 2000, 38:449-457.
    • (2000) Plant Physiol Bioch , vol.38 , pp. 449-457
    • Campalans, A.1    Pages, M.2    Messeguer, R.3
  • 85
    • 0028518719 scopus 로고
    • The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site
    • Duval M., Derose R.T., Job C., Faucher D., Douce R., Job D. The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site. Plant Mol Biol 1994, 26:265-273.
    • (1994) Plant Mol Biol , vol.26 , pp. 265-273
    • Duval, M.1    Derose, R.T.2    Job, C.3    Faucher, D.4    Douce, R.5    Job, D.6
  • 86
    • 0028327162 scopus 로고
    • Developmental patterns of free and protein bound biotin during maturation and germination of seeds of Pisum sativum - characterization of a novel seed-specific biotinylated protein
    • Duval M., Job C., Alban C., Douce R., Job D. Developmental patterns of free and protein bound biotin during maturation and germination of seeds of Pisum sativum - characterization of a novel seed-specific biotinylated protein. Biochem J 1994, 299:141-150.
    • (1994) Biochem J , vol.299 , pp. 141-150
    • Duval, M.1    Job, C.2    Alban, C.3    Douce, R.4    Job, D.5
  • 88
    • 0031282542 scopus 로고    scopus 로고
    • Cloning and expression of the pea gene encoding SBP65, a seed-specific biotinylated protein
    • Dehaye L., Duval M., Viguier D., Yaxley J., Job D. Cloning and expression of the pea gene encoding SBP65, a seed-specific biotinylated protein. Plant Mol Biol 1997, 35:605-621.
    • (1997) Plant Mol Biol , vol.35 , pp. 605-621
    • Dehaye, L.1    Duval, M.2    Viguier, D.3    Yaxley, J.4    Job, D.5
  • 89
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 2001, 70:603-647.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 91
    • 0028587244 scopus 로고
    • A yeast tcp-1-like protein is required for actin function in vivo
    • Vinh D.B.N., Drubin D.G. A yeast tcp-1-like protein is required for actin function in vivo. Proc Natl Acad Sci USA 1994, 91:9116-9120.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9116-9120
    • Vinh, D.B.N.1    Drubin, D.G.2
  • 92
    • 33745198422 scopus 로고    scopus 로고
    • Calcium in plant defence-signalling pathways
    • Lecourieux D., Ranjeva R., Pugin A. Calcium in plant defence-signalling pathways. New Phytol 2006, 171:249-269.
    • (2006) New Phytol , vol.171 , pp. 249-269
    • Lecourieux, D.1    Ranjeva, R.2    Pugin, A.3
  • 93
    • 77953184082 scopus 로고    scopus 로고
    • Calcium signals: the lead currency of plant information processing
    • Kudla J., Batistic O., Hashimoto K. Calcium signals: the lead currency of plant information processing. Plant Cell 2010, 22:541-563.
    • (2010) Plant Cell , vol.22 , pp. 541-563
    • Kudla, J.1    Batistic, O.2    Hashimoto, K.3
  • 94
    • 79960859588 scopus 로고    scopus 로고
    • Coping with stresses: roles of calcium- and calcium/calmodulin-regulated gene expression
    • Reddy A.S.N., Ali G.S., Celesnik H., Day I.S. Coping with stresses: roles of calcium- and calcium/calmodulin-regulated gene expression. Plant Cell 2011, 23:2010-2032.
    • (2011) Plant Cell , vol.23 , pp. 2010-2032
    • Reddy, A.S.N.1    Ali, G.S.2    Celesnik, H.3    Day, I.S.4
  • 95
    • 23044513879 scopus 로고    scopus 로고
    • Ethylene-mediated cross-talk between calcium-dependent protein kinase and MAPK signaling controls stress responses in plants
    • Ludwig A.A., Saitoh H., Felix G., Freymark G., Miersch O., Wasternack C., et al. Ethylene-mediated cross-talk between calcium-dependent protein kinase and MAPK signaling controls stress responses in plants. Proc Natl Acad Sci USA 2005, 102:10736-10741.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10736-10741
    • Ludwig, A.A.1    Saitoh, H.2    Felix, G.3    Freymark, G.4    Miersch, O.5    Wasternack, C.6
  • 96
    • 77955151773 scopus 로고    scopus 로고
    • Cross-talk between ROS and calcium in regulation of nuclear activities
    • Mazars C., Thuleau P., Lamotte O., Bourque S. Cross-talk between ROS and calcium in regulation of nuclear activities. Mol Plant 2010, 3:706-718.
    • (2010) Mol Plant , vol.3 , pp. 706-718
    • Mazars, C.1    Thuleau, P.2    Lamotte, O.3    Bourque, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.