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Volumn 91, Issue , 2013, Pages 172-187

Comparative proteomics analysis of developing peanut aerial and subterranean pods identifies pod swelling related proteins

Author keywords

Aerial and subterranean pods; Peanut; Plant proteome; Pod development

Indexed keywords

LIGNIN; MESSENGER RNA; PROTEASOME; PROTEIN; TRANSCRIPTOME; UBIQUITIN;

EID: 84881520623     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.07.002     Document Type: Article
Times cited : (24)

References (88)
  • 1
    • 84871695159 scopus 로고    scopus 로고
    • Deep sequencing analysis of the transcriptomes of peanut aerial and subterranean young pods identifies candidate genes related to early embryo abortion
    • Chen X.P., Zhu W., Azam S., Li H.Y., Zhu F.H., Li H.F., et al. Deep sequencing analysis of the transcriptomes of peanut aerial and subterranean young pods identifies candidate genes related to early embryo abortion. Plant Biotechnol J 2013, 11:115-127.
    • (2013) Plant Biotechnol J , vol.11 , pp. 115-127
    • Chen, X.P.1    Zhu, W.2    Azam, S.3    Li, H.Y.4    Zhu, F.H.5    Li, H.F.6
  • 2
    • 0033402055 scopus 로고    scopus 로고
    • The role of amyloplasts during gravity perception in gynophores of the peanut plant
    • Moctezuma E., Feldman L.J. The role of amyloplasts during gravity perception in gynophores of the peanut plant. Ann Bot 1999, 84:709-714.
    • (1999) Ann Bot , vol.84 , pp. 709-714
    • Moctezuma, E.1    Feldman, L.J.2
  • 3
    • 3142520551 scopus 로고
    • Arachis hypogaea plant recovery through in vitro culture of peg tips
    • Feng Q.L., Stalker H.T., Pattee H.E., Isleib T.G. Arachis hypogaea plant recovery through in vitro culture of peg tips. Peanut Sci 1995, 22:129-135.
    • (1995) Peanut Sci , vol.22 , pp. 129-135
    • Feng, Q.L.1    Stalker, H.T.2    Pattee, H.E.3    Isleib, T.G.4
  • 4
    • 0038455058 scopus 로고    scopus 로고
    • The peanut gynophore: a developmental and physiological perspective
    • Moctezuma E. The peanut gynophore: a developmental and physiological perspective. Can J Bot 2003, 81:183-190.
    • (2003) Can J Bot , vol.81 , pp. 183-190
    • Moctezuma, E.1
  • 5
    • 77956983635 scopus 로고
    • Geotropic responses and pod development in gynophore explants of peanut (Arachis hypogaea L.) cultured in vitro
    • Ziv M., Zamskj E. Geotropic responses and pod development in gynophore explants of peanut (Arachis hypogaea L.) cultured in vitro. Ann Bot 1975, 39:579-583.
    • (1975) Ann Bot , vol.39 , pp. 579-583
    • Ziv, M.1    Zamskj, E.2
  • 6
    • 0001092689 scopus 로고
    • Pod formation and its geotropic orientation in the peanut, Aruchis hypogaea L., in relation to light and mechanical stimulus
    • Zamski E., Ziv M. Pod formation and its geotropic orientation in the peanut, Aruchis hypogaea L., in relation to light and mechanical stimulus. Ann Bot 1976, 40:63l-636l.
    • (1976) Ann Bot , vol.40
    • Zamski, E.1    Ziv, M.2
  • 7
    • 84871687498 scopus 로고
    • Photocontrol of peanut (Arachis hypogaea L.) embryo and ovule development in vitro
    • Thompson L.K., Ziv M., Deitzer G.F. Photocontrol of peanut (Arachis hypogaea L.) embryo and ovule development in vitro. Plant Physiol 1985, 78:370-373.
    • (1985) Plant Physiol , vol.78 , pp. 370-373
    • Thompson, L.K.1    Ziv, M.2    Deitzer, G.F.3
  • 8
    • 0000518152 scopus 로고
    • Growth of the gynophore of the peanut Arachis hypogaea L. intact and decapitated gynophores
    • Shushu D.D., Cutter E.G. Growth of the gynophore of the peanut Arachis hypogaea L. intact and decapitated gynophores. Can J Bot 1990, 68:955-964.
    • (1990) Can J Bot , vol.68 , pp. 955-964
    • Shushu, D.D.1    Cutter, E.G.2
  • 9
    • 0007205665 scopus 로고
    • Auxin relationships in an intercalary meristem: further studies on the gynophore of Arachis hypogaea L
    • Jacobs W. Auxin relationships in an intercalary meristem: further studies on the gynophore of Arachis hypogaea L. Am J Bot 1951, 38:307-310.
    • (1951) Am J Bot , vol.38 , pp. 307-310
    • Jacobs, W.1
  • 10
    • 0007279712 scopus 로고    scopus 로고
    • IAA redistributes to the upper side of gravistimulated peanut (Arachis hypogaea) gynophores
    • Moctezuma E., Feldman L.J. IAA redistributes to the upper side of gravistimulated peanut (Arachis hypogaea) gynophores. Plant Physiol 1996, 111:S73.
    • (1996) Plant Physiol , vol.111
    • Moctezuma, E.1    Feldman, L.J.2
  • 11
    • 38249029620 scopus 로고
    • The role of the peanut (Araschis hypogaea) ovular tissue in the photo-morphogenetic response of the embryo
    • Ziv M., Kahana O. The role of the peanut (Araschis hypogaea) ovular tissue in the photo-morphogenetic response of the embryo. Plant Sci 1988, 57:159-164.
    • (1988) Plant Sci , vol.57 , pp. 159-164
    • Ziv, M.1    Kahana, O.2
  • 12
    • 0029137816 scopus 로고
    • Light, dark and growth regulator involvement in groundnut (Arachis hypogaea L.) pod development
    • Shlamovitz N., Ziv M., Zamski E. Light, dark and growth regulator involvement in groundnut (Arachis hypogaea L.) pod development. Plant Growth Regul 1995, 16:37-42.
    • (1995) Plant Growth Regul , vol.16 , pp. 37-42
    • Shlamovitz, N.1    Ziv, M.2    Zamski, E.3
  • 13
    • 0032981957 scopus 로고    scopus 로고
    • Changes in auxin patterns in developing gynophores of the peanut plant (Arachis hypogaea L.)
    • Moctezuma E. Changes in auxin patterns in developing gynophores of the peanut plant (Arachis hypogaea L.). Ann Bot 1999, 83:235-242.
    • (1999) Ann Bot , vol.83 , pp. 235-242
    • Moctezuma, E.1
  • 14
    • 0038288699 scopus 로고
    • Localization of phytochrome during peanut (Arachis hypogaea) gynophore and ovule development
    • Thompson L.K., Burgess C.L., Skinner E.N. Localization of phytochrome during peanut (Arachis hypogaea) gynophore and ovule development. Am J Bot 1992, 79:828-832.
    • (1992) Am J Bot , vol.79 , pp. 828-832
    • Thompson, L.K.1    Burgess, C.L.2    Skinner, E.N.3
  • 15
    • 0007745184 scopus 로고
    • Soil physical factors affecting peanut pod development
    • Underwood C.V., Taylor H.M., Hoveland C.S. Soil physical factors affecting peanut pod development. Agron J 1971, 63:953-954.
    • (1971) Agron J , vol.63 , pp. 953-954
    • Underwood, C.V.1    Taylor, H.M.2    Hoveland, C.S.3
  • 16
    • 67650373888 scopus 로고    scopus 로고
    • Expressed sequence tags of the peanut pod nematode Ditylenchus africanus: the first transcriptome analysis of an Anguinid nematode
    • Haegeman A., Jacob J., Vanholme B., Kyndt T., Mitreva M., Gheysen G. Expressed sequence tags of the peanut pod nematode Ditylenchus africanus: the first transcriptome analysis of an Anguinid nematode. Mol Biochem Parasitol 2009, 167:32-40.
    • (2009) Mol Biochem Parasitol , vol.167 , pp. 32-40
    • Haegeman, A.1    Jacob, J.2    Vanholme, B.3    Kyndt, T.4    Mitreva, M.5    Gheysen, G.6
  • 17
    • 78650095218 scopus 로고    scopus 로고
    • EST sequencing and gene expression profiling of cultivated peanut (Arachis hypogaea)
    • Bi Y.P., Liu W., Xia H., Su L., Zhao Z.C., Wan S.B., et al. EST sequencing and gene expression profiling of cultivated peanut (Arachis hypogaea). Genome 2010, 53:832-839.
    • (2010) Genome , vol.53 , pp. 832-839
    • Bi, Y.P.1    Liu, W.2    Xia, H.3    Su, L.4    Zhao, Z.C.5    Wan, S.B.6
  • 18
    • 79251601217 scopus 로고    scopus 로고
    • Differential gene expression in roots of nematode-resistant and -susceptible peanut (Arachis hypogaea L.) cultivars in response to early stages of peanut root-knot nematode (Meloidogyne arenaria) parasitization
    • Tirumalaraju S.V., Jain M., Gallo M. Differential gene expression in roots of nematode-resistant and -susceptible peanut (Arachis hypogaea L.) cultivars in response to early stages of peanut root-knot nematode (Meloidogyne arenaria) parasitization. Plant Physiol 2011, 168:481-492.
    • (2011) Plant Physiol , vol.168 , pp. 481-492
    • Tirumalaraju, S.V.1    Jain, M.2    Gallo, M.3
  • 19
    • 67649708611 scopus 로고    scopus 로고
    • Gene expression profiling in peanut using high density oligonucleotide microarrays
    • Payton P., Kottapalli K.R., Rowland D., Faircloth W., Guo B.Z., Burow M., et al. Gene expression profiling in peanut using high density oligonucleotide microarrays. BMC Genomics 2009, 10:265-276.
    • (2009) BMC Genomics , vol.10 , pp. 265-276
    • Payton, P.1    Kottapalli, K.R.2    Rowland, D.3    Faircloth, W.4    Guo, B.Z.5    Burow, M.6
  • 20
    • 84862825018 scopus 로고    scopus 로고
    • De novo assembly and characterization of the transcriptome during seed development, and generation of genic-SSR markers in peanut (Arachis hypogaea L.)
    • Zhang J., Liang S., Duan J., Wang J., Chen S., Cheng Z., et al. De novo assembly and characterization of the transcriptome during seed development, and generation of genic-SSR markers in peanut (Arachis hypogaea L.). BMC Genomics 2012, 13:90.
    • (2012) BMC Genomics , vol.13 , pp. 90
    • Zhang, J.1    Liang, S.2    Duan, J.3    Wang, J.4    Chen, S.5    Cheng, Z.6
  • 21
    • 40049096795 scopus 로고    scopus 로고
    • Peanut gene expression profiling in developing seeds at different reproduction stages during Aspergillus parasiticus infection
    • Guo B.Z., Chen X.P., Dang P., Scully B.T., Liang X.Q., Holbrook C.C., et al. Peanut gene expression profiling in developing seeds at different reproduction stages during Aspergillus parasiticus infection. BMC Dev Biol 2008, 8:12-28.
    • (2008) BMC Dev Biol , vol.8 , pp. 12-28
    • Guo, B.Z.1    Chen, X.P.2    Dang, P.3    Scully, B.T.4    Liang, X.Q.5    Holbrook, C.C.6
  • 22
    • 84877155319 scopus 로고    scopus 로고
    • Transcriptome identification of the resistance-associated genes (RAGs) to Aspergillus flavus infection in pre-harvested peanut (Arachis hypogaea)
    • Wang T., Chen X.P., Li H.F., Liu H.Y., Hong Y.B., Yang Q.L., et al. Transcriptome identification of the resistance-associated genes (RAGs) to Aspergillus flavus infection in pre-harvested peanut (Arachis hypogaea). Funct Plant Biol 2012, 10.1071/FP12143.
    • (2012) Funct Plant Biol
    • Wang, T.1    Chen, X.P.2    Li, H.F.3    Liu, H.Y.4    Hong, Y.B.5    Yang, Q.L.6
  • 23
    • 81155134417 scopus 로고    scopus 로고
    • Identification and characterization of microRNAs from peanut (Arachis hypogaea L.) by high-throughput sequencing
    • Chi X., Yang Q., Chen X., Wang J., Pan L., Chen M., et al. Identification and characterization of microRNAs from peanut (Arachis hypogaea L.) by high-throughput sequencing. PLoS One 2011, 6(11):e27530.
    • (2011) PLoS One , vol.6 , Issue.11
    • Chi, X.1    Yang, Q.2    Chen, X.3    Wang, J.4    Pan, L.5    Chen, M.6
  • 24
    • 78649483609 scopus 로고    scopus 로고
    • Identification of seed proteins associated with resistance to pre-harvested aflatoxin contamination in peanut (Arachis hypogaea L.)
    • Wang T., Zhang E.H., Chen X.P., Li L., Liang X.Q. Identification of seed proteins associated with resistance to pre-harvested aflatoxin contamination in peanut (Arachis hypogaea L.). BMC Plant Biol 2010, 10:267-278.
    • (2010) BMC Plant Biol , vol.10 , pp. 267-278
    • Wang, T.1    Zhang, E.H.2    Chen, X.P.3    Li, L.4    Liang, X.Q.5
  • 25
    • 84870665032 scopus 로고    scopus 로고
    • Quantitative proteomic analysis reveals that antioxidation mechanisms contribute to cold tolerance in plantain (Musa paradisiaca L.) seedlings
    • Yang Q.S., Wu J.H., Li C.Y., Wei Y.R., Sheng O., Hu C.H., et al. Quantitative proteomic analysis reveals that antioxidation mechanisms contribute to cold tolerance in plantain (Musa paradisiaca L.) seedlings. Mol Cell Proteomics 2012, 11:1853-1869.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 1853-1869
    • Yang, Q.S.1    Wu, J.H.2    Li, C.Y.3    Wei, Y.R.4    Sheng, O.5    Hu, C.H.6
  • 28
    • 0142214654 scopus 로고    scopus 로고
    • Proteomics of Medicago truncatula seed development establishes the time frame of diverse metabolic processes related to reserve accumulation
    • Gallardo K., Signor C.L., Vandekerckhove J., Thompson R.D., Burstin J., et al. Proteomics of Medicago truncatula seed development establishes the time frame of diverse metabolic processes related to reserve accumulation. Plant Physiol 2003, 133:664-682.
    • (2003) Plant Physiol , vol.133 , pp. 664-682
    • Gallardo, K.1    Signor, C.L.2    Vandekerckhove, J.3    Thompson, R.D.4    Burstin, J.5
  • 29
  • 30
    • 20444449370 scopus 로고    scopus 로고
    • A systematic proteomic study of seed filling in soybean establishment of high-resolution two-dimensional reference maps, expression profiles, and an interactive proteome database
    • Hajduch M., Ganapathy A., Stein J.W., Thelen J.J. A systematic proteomic study of seed filling in soybean establishment of high-resolution two-dimensional reference maps, expression profiles, and an interactive proteome database. Plant Physiol 2005, 137:1397-1419.
    • (2005) Plant Physiol , vol.137 , pp. 1397-1419
    • Hajduch, M.1    Ganapathy, A.2    Stein, J.W.3    Thelen, J.J.4
  • 31
    • 0035983965 scopus 로고    scopus 로고
    • Proteome analysis of grain filling and seed maturation in barley
    • Finnie C., Melchior S., Roepstorff P., Svensson B. Proteome analysis of grain filling and seed maturation in barley. Plant Physiol 2002, 129:1308-1319.
    • (2002) Plant Physiol , vol.129 , pp. 1308-1319
    • Finnie, C.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 32
    • 34250678462 scopus 로고    scopus 로고
    • Major proteome variations associated with berry tomato pericarp development and ripening
    • Faurobert M., Mihr C., Bertin N., Pawlowski T., Negroni L., Sommerer N., et al. Major proteome variations associated with berry tomato pericarp development and ripening. Plant Physiol 2007, 143:1327-1346.
    • (2007) Plant Physiol , vol.143 , pp. 1327-1346
    • Faurobert, M.1    Mihr, C.2    Bertin, N.3    Pawlowski, T.4    Negroni, L.5    Sommerer, N.6
  • 33
    • 34247237057 scopus 로고    scopus 로고
    • Analysis of protein changes during grape berry ripening by 2-DE and MALDI-TOF
    • Giribaldi M., Perugini L., Sauvage F.X., Schubert A. Analysis of protein changes during grape berry ripening by 2-DE and MALDI-TOF. Proteomics 2007, 7:3l54-3170.
    • (2007) Proteomics , vol.7
    • Giribaldi, M.1    Perugini, L.2    Sauvage, F.X.3    Schubert, A.4
  • 34
    • 79952809064 scopus 로고    scopus 로고
    • Resolubilization of TCA precipitated plant proteins for 2-D electrophoresis
    • Zhang E.H., Chen X.P., Liang X.Q. Resolubilization of TCA precipitated plant proteins for 2-D electrophoresis. Electrophoresis 2011, 32:696-698.
    • (2011) Electrophoresis , vol.32 , pp. 696-698
    • Zhang, E.H.1    Chen, X.P.2    Liang, X.Q.3
  • 35
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan X.J., Wait R., Berkeiman T., Harry R.A., Westbrook J.A., Wheeler C.H., et al. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 2000, 21:3666-3672.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, X.J.1    Wait, R.2    Berkeiman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6
  • 36
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang S., Puryear J., Cairney J. A simple and efficient method for isolating RNA from pine trees. Plant Mol Biol Report 1993, 11:113-116.
    • (1993) Plant Mol Biol Report , vol.11 , pp. 113-116
    • Chang, S.1    Puryear, J.2    Cairney, J.3
  • 38
    • 44649135348 scopus 로고    scopus 로고
    • Regulation of Rubisco activase and its interaction with Rubisco
    • Portis J.A.R., Li C., Wang D., Salvucci M.E. Regulation of Rubisco activase and its interaction with Rubisco. J Exp Bot 2008, 59:1597-1604.
    • (2008) J Exp Bot , vol.59 , pp. 1597-1604
    • Portis, J.A.R.1    Li, C.2    Wang, D.3    Salvucci, M.E.4
  • 39
    • 0030870674 scopus 로고    scopus 로고
    • Novel aspects of chlorophyll a/b-binding proteins
    • Bassi R., Sandona D., Croce R. Novel aspects of chlorophyll a/b-binding proteins. Physiol Plant 1997, 100:769-779.
    • (1997) Physiol Plant , vol.100 , pp. 769-779
    • Bassi, R.1    Sandona, D.2    Croce, R.3
  • 40
    • 0023286729 scopus 로고
    • Expression of the nuclear encoded OEE1 protein is required for oxygen evolution and stability of photosystem II particles in Chlamydomonas reinhardtii
    • Mayfield S.P., Bennoun P., Rochaix J.D. Expression of the nuclear encoded OEE1 protein is required for oxygen evolution and stability of photosystem II particles in Chlamydomonas reinhardtii. EMBO J 1987, 6:313-318.
    • (1987) EMBO J , vol.6 , pp. 313-318
    • Mayfield, S.P.1    Bennoun, P.2    Rochaix, J.D.3
  • 41
    • 0023292452 scopus 로고
    • Expression of the nuclear OEE2 gene is required for high levels of photosynthetic oxygen evolution in Chlamydomonas reinhardtii
    • Mayfield S.P., Rahire M., Frank G., Zuber H., Rochaix J.D. Expression of the nuclear OEE2 gene is required for high levels of photosynthetic oxygen evolution in Chlamydomonas reinhardtii. Proc Natl Acad Sci U S A 1987, 84:749-753.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 749-753
    • Mayfield, S.P.1    Rahire, M.2    Frank, G.3    Zuber, H.4    Rochaix, J.D.5
  • 42
    • 0032520957 scopus 로고    scopus 로고
    • The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics
    • Ubbink M., Ejdeback M., Karlsson B.G., Bendall D.S. The structure of the complex of plastocyanin and cytochrome f, determined by paramagnetic NMR and restrained rigid-body molecular dynamics. Structure 1998, 6:323-335.
    • (1998) Structure , vol.6 , pp. 323-335
    • Ubbink, M.1    Ejdeback, M.2    Karlsson, B.G.3    Bendall, D.S.4
  • 43
    • 0027954821 scopus 로고
    • Manipulation of lignin quality by down regulation of cinnamyl alcohol dehydrogenase
    • Halpin C., Knight M.E., Foxon G.A., Campbell M.M., Boudet A.M., Boon J.J., et al. Manipulation of lignin quality by down regulation of cinnamyl alcohol dehydrogenase. Plant J 1994, 6:339-350.
    • (1994) Plant J , vol.6 , pp. 339-350
    • Halpin, C.1    Knight, M.E.2    Foxon, G.A.3    Campbell, M.M.4    Boudet, A.M.5    Boon, J.J.6
  • 44
    • 1242274657 scopus 로고    scopus 로고
    • Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis
    • Kim S.J., Kim M.R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L., Davin L.B., et al. Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis. Proc Natl Acad Sci U S A 2004, 101:1455-1460.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 1455-1460
    • Kim, S.J.1    Kim, M.R.2    Bedgar, D.L.3    Moinuddin, S.G.A.4    Cardenas, C.L.5    Davin, L.B.6
  • 45
    • 0035983842 scopus 로고    scopus 로고
    • Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase
    • Zubieta C., Kota P., Ferrer J.L., Dixon R.A., Noel J.P. Structural basis for the modulation of lignin monomer methylation by caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase. Plant Cell 2002, 14:1265-1277.
    • (2002) Plant Cell , vol.14 , pp. 1265-1277
    • Zubieta, C.1    Kota, P.2    Ferrer, J.L.3    Dixon, R.A.4    Noel, J.P.5
  • 46
    • 17444420139 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and plant development
    • Moon J., Parry G., Estelle1 M. The ubiquitin-proteasome pathway and plant development. Plant Cell 2004, 16:3181-3195.
    • (2004) Plant Cell , vol.16 , pp. 3181-3195
    • Moon, J.1    Parry, G.2    Estelle1, M.3
  • 47
    • 3142732890 scopus 로고    scopus 로고
    • Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein degradation
    • Feng S., Shen Y., Sullivan J.A., Rubio V., Xiong Y., Sun T.P., et al. Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein degradation. Plant Cell 2004, 16:1870-1882.
    • (2004) Plant Cell , vol.16 , pp. 1870-1882
    • Feng, S.1    Shen, Y.2    Sullivan, J.A.3    Rubio, V.4    Xiong, Y.5    Sun, T.P.6
  • 48
    • 0037008512 scopus 로고    scopus 로고
    • Plant development: regulation by protein degradation
    • Hellmann H., Estelle M. Plant development: regulation by protein degradation. Science 2002, 297:793-797.
    • (2002) Science , vol.297 , pp. 793-797
    • Hellmann, H.1    Estelle, M.2
  • 49
    • 0012810697 scopus 로고    scopus 로고
    • The ubiquitinproteasome pathway of intracellular proteolysis
    • Doherty F.J., Dawson S., Mayer R.J. The ubiquitinproteasome pathway of intracellular proteolysis. Essays Biochem 2002, 38:51-63.
    • (2002) Essays Biochem , vol.38 , pp. 51-63
    • Doherty, F.J.1    Dawson, S.2    Mayer, R.J.3
  • 50
    • 38749106247 scopus 로고    scopus 로고
    • Structure, function and regulation of plant proteasomes
    • Kurepa J., Smalle J.A. Structure, function and regulation of plant proteasomes. Biochimie 2008, 90:324-335.
    • (2008) Biochimie , vol.90 , pp. 324-335
    • Kurepa, J.1    Smalle, J.A.2
  • 51
    • 0141818068 scopus 로고    scopus 로고
    • Hormonal interactions in fruit development
    • Ozga J.A., Reinecke D.M. Hormonal interactions in fruit development. J Plant Growth Regul 2003, 22:73-81.
    • (2003) J Plant Growth Regul , vol.22 , pp. 73-81
    • Ozga, J.A.1    Reinecke, D.M.2
  • 52
    • 0033041152 scopus 로고    scopus 로고
    • Sequences within both the N- and C-terminal domains of phytochrome A are required for Pfr ubiquitination and degradation
    • Clough R.C., Beebe E.T.J., Lohman K.N., Marita J.M., Walker J.M., Gatz C., et al. Sequences within both the N- and C-terminal domains of phytochrome A are required for Pfr ubiquitination and degradation. Plant J 1999, 17:155-167.
    • (1999) Plant J , vol.17 , pp. 155-167
    • Clough, R.C.1    Beebe, E.T.J.2    Lohman, K.N.3    Marita, J.M.4    Walker, J.M.5    Gatz, C.6
  • 53
    • 0034713297 scopus 로고    scopus 로고
    • Targeted destabilization of HY5 during light-regulated development of Arabidopsis
    • Osterlund M.T., Hardtke C.S., Wei N., Deng X.W. Targeted destabilization of HY5 during light-regulated development of Arabidopsis. Nature 2000, 405:462-466.
    • (2000) Nature , vol.405 , pp. 462-466
    • Osterlund, M.T.1    Hardtke, C.S.2    Wei, N.3    Deng, X.W.4
  • 54
    • 0037712997 scopus 로고    scopus 로고
    • The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins
    • Vierstra R.D. The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins. Trends Plant Sci 2003, 8:1360-1385.
    • (2003) Trends Plant Sci , vol.8 , pp. 1360-1385
    • Vierstra, R.D.1
  • 55
    • 0036500015 scopus 로고    scopus 로고
    • Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis
    • Suzuki G., Yanagawa Y., Kwok S.F., Matsui M., Deng X.W. Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis. Genes Dev 2002, 16:554-559.
    • (2002) Genes Dev , vol.16 , pp. 554-559
    • Suzuki, G.1    Yanagawa, Y.2    Kwok, S.F.3    Matsui, M.4    Deng, X.W.5
  • 56
    • 77950401024 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates plant hormone signaling
    • Santner A., Estelle M. The ubiquitin-proteasome system regulates plant hormone signaling. Plant J 2010, 61:1029-1040.
    • (2010) Plant J , vol.61 , pp. 1029-1040
    • Santner, A.1    Estelle, M.2
  • 57
    • 0036269779 scopus 로고    scopus 로고
    • Ubiquitination and auxin signaling: a degrading story
    • Kepinski S., Leyser O. Ubiquitination and auxin signaling: a degrading story. Plant Cell 2002, 14:S81-S95.
    • (2002) Plant Cell , vol.14
    • Kepinski, S.1    Leyser, O.2
  • 58
    • 0035999461 scopus 로고    scopus 로고
    • The role of regulated protein degradation in auxin response
    • Dharmasiri S., Estelle M. The role of regulated protein degradation in auxin response. Plant Mol Biol 2002, 49:401-409.
    • (2002) Plant Mol Biol , vol.49 , pp. 401-409
    • Dharmasiri, S.1    Estelle, M.2
  • 59
    • 0034756346 scopus 로고    scopus 로고
    • Rapid degradation of auxin/indoleacetic acid proteins requires conserved amino acids of domain II and is proteasome dependent
    • Ramos J.A., Zenser N., Leyser O., Callis J. Rapid degradation of auxin/indoleacetic acid proteins requires conserved amino acids of domain II and is proteasome dependent. Plant Cell 2001, 13:2349-2360.
    • (2001) Plant Cell , vol.13 , pp. 2349-2360
    • Ramos, J.A.1    Zenser, N.2    Leyser, O.3    Callis, J.4
  • 60
    • 0037390990 scopus 로고    scopus 로고
    • The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis thaliana growth and development supports a substrate specific function in abscisic acid signaling
    • Smalle J., Kurepa J., Yang P., Emborg T.J., Babyichuk E., Kushnir S., et al. The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis thaliana growth and development supports a substrate specific function in abscisic acid signaling. Plant Cell 2003, 15:965-980.
    • (2003) Plant Cell , vol.15 , pp. 965-980
    • Smalle, J.1    Kurepa, J.2    Yang, P.3    Emborg, T.J.4    Babyichuk, E.5    Kushnir, S.6
  • 61
    • 0036910333 scopus 로고    scopus 로고
    • Gibberellin mediated proteasome-dependent degradation of the barley DELLA protein SLN1 repressor
    • Fu X.D., Richards D.E., Ait-Ali T., Hynes L.W., Ougham H., Peng J., et al. Gibberellin mediated proteasome-dependent degradation of the barley DELLA protein SLN1 repressor. Plant Cell 2002, 14:3191-3200.
    • (2002) Plant Cell , vol.14 , pp. 3191-3200
    • Fu, X.D.1    Richards, D.E.2    Ait-Ali, T.3    Hynes, L.W.4    Ougham, H.5    Peng, J.6
  • 62
    • 0036007963 scopus 로고    scopus 로고
    • Cytokinin growth responses in Arabidopsis involve the 26S proteasome subunit RPN12a
    • Smalle J., Kurepa J., Yang P., Babiychuk E., Kushnir S., Durski A., et al. Cytokinin growth responses in Arabidopsis involve the 26S proteasome subunit RPN12a. Plant Cell 2002, 14:17-32.
    • (2002) Plant Cell , vol.14 , pp. 17-32
    • Smalle, J.1    Kurepa, J.2    Yang, P.3    Babiychuk, E.4    Kushnir, S.5    Durski, A.6
  • 63
    • 17944366393 scopus 로고    scopus 로고
    • SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase
    • Farras R., Ferrando A., Jasik J., Kleinow T., Okresz L., Tiburcio A., et al. SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase. EMBO J 2001, 20:2742-2756.
    • (2001) EMBO J , vol.20 , pp. 2742-2756
    • Farras, R.1    Ferrando, A.2    Jasik, J.3    Kleinow, T.4    Okresz, L.5    Tiburcio, A.6
  • 64
    • 0035983333 scopus 로고    scopus 로고
    • Cell cycle dependent dynamic change of 26S proteasome distribution in tobacco BY-2 cells
    • Yanagawa Y., Hasezawa S., Kumagai F., Oka M., Fujimuro M., Naito T., et al. Cell cycle dependent dynamic change of 26S proteasome distribution in tobacco BY-2 cells. Plant Cell Physiol 2002, 43:604-613.
    • (2002) Plant Cell Physiol , vol.43 , pp. 604-613
    • Yanagawa, Y.1    Hasezawa, S.2    Kumagai, F.3    Oka, M.4    Fujimuro, M.5    Naito, T.6
  • 66
    • 3242665372 scopus 로고    scopus 로고
    • The ubiqutin 26S proteasome proteolytic pathway
    • Smalle J., Vierstra R.D. The ubiqutin 26S proteasome proteolytic pathway. Annu Rev Plant Biol 2004, 55:555-590.
    • (2004) Annu Rev Plant Biol , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 67
    • 0034867567 scopus 로고    scopus 로고
    • ORE9, an F-Box protein that regulates leaf senescence in Arabidopsis
    • Woo H.R., Chung K.M., Park J.H., Oh S.A., Ahn T., Hong S.H., et al. ORE9, an F-Box protein that regulates leaf senescence in Arabidopsis. Plant Cell 2001, 13:1779-1790.
    • (2001) Plant Cell , vol.13 , pp. 1779-1790
    • Woo, H.R.1    Chung, K.M.2    Park, J.H.3    Oh, S.A.4    Ahn, T.5    Hong, S.H.6
  • 68
    • 0037805637 scopus 로고    scopus 로고
    • Activation of the programmed cell death pathway by inhibition of proteasome function in plants
    • Kim M., Ahn J.W., Jin U.H., Choi D., Paek K.H., Pai H.S. Activation of the programmed cell death pathway by inhibition of proteasome function in plants. J Biol Chem 2003, 278:19406-19415.
    • (2003) J Biol Chem , vol.278 , pp. 19406-19415
    • Kim, M.1    Ahn, J.W.2    Jin, U.H.3    Choi, D.4    Paek, K.H.5    Pai, H.S.6
  • 69
    • 33745662408 scopus 로고    scopus 로고
    • Production and scavenging of reactive oxygen species in chloroplasts and their functions
    • Asada K. Production and scavenging of reactive oxygen species in chloroplasts and their functions. Plant Physiol 2006, 141:391-396.
    • (2006) Plant Physiol , vol.141 , pp. 391-396
    • Asada, K.1
  • 70
    • 13944284179 scopus 로고    scopus 로고
    • Singlet oxygen production in photosynthesis
    • Liszkay A.K. Singlet oxygen production in photosynthesis. J Exp Bot 2005, 56:337-346.
    • (2005) J Exp Bot , vol.56 , pp. 337-346
    • Liszkay, A.K.1
  • 71
    • 33750819157 scopus 로고    scopus 로고
    • Reactive oxygen species as signals that modulate plant stress responses and programmed cell death
    • Gechev T.S., Breusegem F.V., Stone J.M., Denev I., Laloi C. Reactive oxygen species as signals that modulate plant stress responses and programmed cell death. Bioessays 2006, 28:1091-1101.
    • (2006) Bioessays , vol.28 , pp. 1091-1101
    • Gechev, T.S.1    Breusegem, F.V.2    Stone, J.M.3    Denev, I.4    Laloi, C.5
  • 72
    • 31644451600 scopus 로고    scopus 로고
    • Reactive oxygen species and oxidative burst: Role in stress, senescence and signal transduction in plant
    • Bhattacharjee S. Reactive oxygen species and oxidative burst: Role in stress, senescence and signal transduction in plant. Curr Sci 2005, 89:1113-1121.
    • (2005) Curr Sci , vol.89 , pp. 1113-1121
    • Bhattacharjee, S.1
  • 73
    • 20044375371 scopus 로고    scopus 로고
    • Cytosolic ascorbate peroxidase is a central component of the reactive oxygen gene network of Arabidopsis
    • Davletova S., Rizhsky L., Liang H., Zhong S.Q., Oliver D.J., Coutu J., et al. Cytosolic ascorbate peroxidase is a central component of the reactive oxygen gene network of Arabidopsis. Plant Cell 2005, 17:268-281.
    • (2005) Plant Cell , vol.17 , pp. 268-281
    • Davletova, S.1    Rizhsky, L.2    Liang, H.3    Zhong, S.Q.4    Oliver, D.J.5    Coutu, J.6
  • 74
    • 84983392009 scopus 로고
    • Ascorbate peroxidase-a hydrogen peroxide-scavenging enzyme in plants
    • Asada K. Ascorbate peroxidase-a hydrogen peroxide-scavenging enzyme in plants. Physiol Plant 1992, 85:235-241.
    • (1992) Physiol Plant , vol.85 , pp. 235-241
    • Asada, K.1
  • 75
    • 0001329109 scopus 로고
    • Proteolytic enzymes and their inhibitors in plant
    • Ryan C.A. Proteolytic enzymes and their inhibitors in plant. Annu Rev Plant Physiol 1977, 24:173-196.
    • (1977) Annu Rev Plant Physiol , vol.24 , pp. 173-196
    • Ryan, C.A.1
  • 77
    • 0023715906 scopus 로고
    • Isolation of soybean trypsin inhibitors by affinity chromatography on anhydro trypsin-Sepharose 4B
    • Putzai A., Grant G., Stewart J.C., Watt W.B. Isolation of soybean trypsin inhibitors by affinity chromatography on anhydro trypsin-Sepharose 4B. Anal Biochem 1988, 172:108-112.
    • (1988) Anal Biochem , vol.172 , pp. 108-112
    • Putzai, A.1    Grant, G.2    Stewart, J.C.3    Watt, W.B.4
  • 78
    • 33644852137 scopus 로고    scopus 로고
    • Downregulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development
    • Sin S.F., Yeung E.C., Chye M.L. Downregulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development. Plant J 2006, 45:58-70.
    • (2006) Plant J , vol.45 , pp. 58-70
    • Sin, S.F.1    Yeung, E.C.2    Chye, M.L.3
  • 79
    • 0002295661 scopus 로고
    • Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung bean
    • Baumgartmer B., Chrispeels M.J. Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung bean. Plant Physiol 1976, 58:1-6.
    • (1976) Plant Physiol , vol.58 , pp. 1-6
    • Baumgartmer, B.1    Chrispeels, M.J.2
  • 80
    • 0000679720 scopus 로고
    • A trypsin inhibitor from the water-soluble fraction of wheat kernel
    • Poerio E., Carranzo L., Garzillo A.M., Buonocore V. A trypsin inhibitor from the water-soluble fraction of wheat kernel. Phytochemistry 1989, 28:1307-1311.
    • (1989) Phytochemistry , vol.28 , pp. 1307-1311
    • Poerio, E.1    Carranzo, L.2    Garzillo, A.M.3    Buonocore, V.4
  • 81
    • 0034613548 scopus 로고    scopus 로고
    • Temporal and spatial activity of a promoter from a pea enzyme inhibitor gene and its exploitation for seed quality improvement
    • Welham T., Domoney C. Temporal and spatial activity of a promoter from a pea enzyme inhibitor gene and its exploitation for seed quality improvement. Plant Sci 2000, 159:289-299.
    • (2000) Plant Sci , vol.159 , pp. 289-299
    • Welham, T.1    Domoney, C.2
  • 82
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants
    • Solomon M., Belenghi B., Delledonne M., Menachem E., Levinea A. The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants. Plant Cell 1999, 11:431-443.
    • (1999) Plant Cell , vol.11 , pp. 431-443
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Menachem, E.4    Levinea, A.5
  • 83
    • 0036367452 scopus 로고    scopus 로고
    • Programmed cell death during flower senescence: isolation and characterization of cysteine proteinases from Sandersonia aurantiaca
    • Eason J.R., Ryan D.J., Pinkney T.T., Donoghue E.M. Programmed cell death during flower senescence: isolation and characterization of cysteine proteinases from Sandersonia aurantiaca. Funct Plant Biol 2002, 29:1055-1064.
    • (2002) Funct Plant Biol , vol.29 , pp. 1055-1064
    • Eason, J.R.1    Ryan, D.J.2    Pinkney, T.T.3    Donoghue, E.M.4
  • 84
    • 0021753882 scopus 로고
    • Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei
    • Misset O., Opperdoes F.R. Simultaneous purification of hexokinase, class-I fructose-bisphosphate aldolase, triosephosphate isomerase and phosphoglycerate kinase from Trypanosoma brucei. Eur J Biochem 1984, 144:475-483.
    • (1984) Eur J Biochem , vol.144 , pp. 475-483
    • Misset, O.1    Opperdoes, F.R.2
  • 85
    • 0032926319 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts
    • Gothel S.F., Marahiel M.A. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol Life Sci 1999, 55:423-436.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 423-436
    • Gothel, S.F.1    Marahiel, M.A.2
  • 86
    • 0034476852 scopus 로고    scopus 로고
    • Plant proteolytic enzymes: possible roles during programmed cell death
    • Beers E.P., Woffenden B.J., Zhao C.G. Plant proteolytic enzymes: possible roles during programmed cell death. Plant Mol Biol 2000, 44:399-415.
    • (2000) Plant Mol Biol , vol.44 , pp. 399-415
    • Beers, E.P.1    Woffenden, B.J.2    Zhao, C.G.3
  • 87
    • 33751401609 scopus 로고    scopus 로고
    • Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape
    • Agrawal G.K., Thelen J.J. Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol Cell Proteomics 2006, 5:2044-2059.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2044-2059
    • Agrawal, G.K.1    Thelen, J.J.2
  • 88
    • 34447130270 scopus 로고    scopus 로고
    • Functional characterization of the Arabidopsis eukaryotic translation initiation factor 5A-2 that plays a crucial role in plant growth and development by regulating cell division, cell growth, and cell death
    • Feng H.Z., Chen Q.G., Feng J., Zhang J., Yang X.H., Zuo J.R. Functional characterization of the Arabidopsis eukaryotic translation initiation factor 5A-2 that plays a crucial role in plant growth and development by regulating cell division, cell growth, and cell death. Plant Physiol 2007, 144:1531-1545.
    • (2007) Plant Physiol , vol.144 , pp. 1531-1545
    • Feng, H.Z.1    Chen, Q.G.2    Feng, J.3    Zhang, J.4    Yang, X.H.5    Zuo, J.R.6


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