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Volumn 72, Issue 10, 2011, Pages 1308-1315

Agricultural recovery of a formerly radioactive area: I. Establishment of high-resolution quantitative protein map of mature flax seeds harvested from the remediated Chernobyl area

Author keywords

Chernobyl; Flax; Linum usitatissimum L.; Mass spectrometry; Protein map; Proteomics; Radiation; Remediation

Indexed keywords

VEGETABLE PROTEIN;

EID: 79958147842     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2010.11.010     Document Type: Article
Times cited : (15)

References (49)
  • 1
    • 33751401609 scopus 로고    scopus 로고
    • Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape
    • DOI 10.1074/mcp.M600084-MCP200
    • G.K. Agrawal, and J.J. Thelen Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape Mol. Cell Proteomics 5 2006 2044 2059 (Pubitemid 44817017)
    • (2006) Molecular and Cellular Proteomics , vol.5 , Issue.11 , pp. 2044-2059
    • Agrawal, G.K.1    Thelen, J.J.2
  • 2
    • 40849102458 scopus 로고    scopus 로고
    • Structure and function of plant acyl-CoA oxidases
    • S. Arent, V.E. Pye, and A. Henriksen Structure and function of plant acyl-CoA oxidases Plant Physiol. Biochem. 46 2008 292 301
    • (2008) Plant Physiol. Biochem. , vol.46 , pp. 292-301
    • Arent, S.1    Pye, V.E.2    Henriksen, A.3
  • 3
    • 37348999896 scopus 로고    scopus 로고
    • Third annual Warren K. Sinclair keynote address: Retrospective analysis of impacts of the chernobyl accident
    • DOI 10.1097/01.HP.0000282109.20364.37, PII 0000403220071100000005
    • M. Balonov Third annual Warren K. Sinclair keynote address: retrospective analysis of impacts of the Chernobyl accident Health Phys. 93 2007 383 409 (Pubitemid 350287263)
    • (2007) Health Physics , vol.93 , Issue.5 , pp. 383-409
    • Balonov, M.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0029169501 scopus 로고
    • Tansley review No. 80. Biochemistry and molecular biology of lignification
    • A.M. Boudet, C. Lapierre, and J. Grima-Pettenati Tansley review No. 80. Biochemistry and molecular biology of lignification New Phytol. 129 1995 203 236
    • (1995) New Phytol. , vol.129 , pp. 203-236
    • Boudet, A.M.1    Lapierre, C.2    Grima-Pettenati, J.3
  • 8
    • 67349277418 scopus 로고    scopus 로고
    • Development and analysis of EST-SSRs for flax (Linum usitatissimum L.)
    • S. Cloutier, Z. Niu, R. Datla, and S. Duguid Development and analysis of EST-SSRs for flax (Linum usitatissimum L.) Theor. Appl. Genet. 119 2009 53 63
    • (2009) Theor. Appl. Genet. , vol.119 , pp. 53-63
    • Cloutier, S.1    Niu, Z.2    Datla, R.3    Duguid, S.4
  • 9
    • 4644306812 scopus 로고    scopus 로고
    • Isolation and structural characterization of the major protein fraction from NorMan flaxseed (Linum usitatissimum L.)
    • DOI 10.1016/j.foodchem.2003.07.038, PII S030881460400319X
    • M.W.Y. Chung, B. Lei, and E.C.Y. Li-Chan Isolation and structural characterization of the major protein fraction from NorMan flaxseed (Linum usitatissimum L.) Food Chem. 90 2005 271 279 (Pubitemid 39298811)
    • (2005) Food Chemistry , vol.90 , Issue.1-2 , pp. 271-279
    • Chung, M.W.Y.1    Lei, B.2    Li-Chan, E.C.Y.3
  • 10
    • 34247522742 scopus 로고    scopus 로고
    • Engineering oilseed plants for a sustainable, land-based source of long chain polyunsaturated fatty acids
    • DOI 10.1007/s11745-007-3049-1
    • H.G. Damude, and A.J. Kinney Engineering oilseed plants for a sustainable, land-based source of long chain polyunsaturated fatty acids Lipids 42 2007 179 185 (Pubitemid 46651413)
    • (2007) Lipids , vol.42 , Issue.3 , pp. 179-185
    • Damude, H.G.1    Kinney, A.J.2
  • 11
    • 67049095500 scopus 로고    scopus 로고
    • Proteomic analysis of mature soybean seeds from the Chernobyl area suggests plant adaptation to the contaminated environment
    • M. Danchenko, L. Skultety, N. Rashydov, V. Berezhna, L. Matel, T. Salaj, A. Pretova, and M. Hajduch Proteomic analysis of mature soybean seeds from the Chernobyl area suggests plant adaptation to the contaminated environment J. Proteome Res. 8 2009 2915 2922
    • (2009) J. Proteome Res. , vol.8 , pp. 2915-2922
    • Danchenko, M.1    Skultety, L.2    Rashydov, N.3    Berezhna, V.4    Matel, L.5    Salaj, T.6    Pretova, A.7    Hajduch, M.8
  • 12
    • 26444552100 scopus 로고    scopus 로고
    • Lignification in the flax stem: Evidence for an unusual lignin in bast fibers
    • DOI 10.1007/s00425-005-1537-1
    • A. Day, K. Ruel, G. Neutelings, D. Crônier, H. David, S. Hawkins, and B. Chabbert Lignification in the flax stem: evidence for an unusual lignin in bast fibers Planta 222 2005 234 245 (Pubitemid 41429381)
    • (2005) Planta , vol.222 , Issue.2 , pp. 234-245
    • Day, A.1    Ruel, K.2    Neutelings, G.3    Cronier, D.4    David, H.5    Hawkins, S.6    Chabbert, B.7
  • 14
    • 7244237725 scopus 로고
    • Fatty acid accumulation in maturing flaxseeds as influenced by environment
    • C.D. Dybing, and D.C. Zimmerman Fatty acid accumulation in maturing flaxseeds as influenced by environment Plant Physiol. 41 1966 1465 1470
    • (1966) Plant Physiol. , vol.41 , pp. 1465-1470
    • Dybing, C.D.1    Zimmerman, D.C.2
  • 15
    • 0035983965 scopus 로고    scopus 로고
    • Proteome analysis of grain filling and seed maturation in barley
    • DOI 10.1104/pp.003681
    • C. Finnie, S. Melchior, P. Roepstorff, and B. Svensson Proteome analysis of grain filling and seed maturation in barley Plant Physiol. 129 2002 1308 1319 (Pubitemid 34801099)
    • (2002) Plant Physiology , vol.129 , Issue.3 , pp. 1308-1319
    • Finnie, C.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 17
    • 0142214654 scopus 로고    scopus 로고
    • Proteomics of Medicago truncatula Seed Development Establishes the Time Frame of Diverse Metabolic Processes Related to Reserve Accumulation
    • DOI 10.1104/pp.103.025254
    • K. Gallardo, C. Le Signor, J. Vandekerckhove, R.D. Thompson, and J. Burstin Proteomics of Medicago truncatula seed development establishes the time frame of diverse metabolic processes related to reserve accumulation Plant Physiol. 133 2003 664 682 (Pubitemid 37325678)
    • (2003) Plant Physiology , vol.133 , Issue.2 , pp. 664-682
    • Gallardo, K.1    Le Signor, C.2    Vandekerckhove, J.3    Thompson, R.D.4    Burstin, J.5
  • 18
    • 38349082659 scopus 로고    scopus 로고
    • A combined proteome and transcriptome analysis of developing Medicago truncatula seeds: Evidence for metabolic specialization of maternal and filial tissues
    • K. Gallardo, C. Firnhaber, H. Zuber, D. Héricher, M. Belghazi, C. Henry, H. Küster, and R. Thompson A combined proteome and transcriptome analysis of developing Medicago truncatula seeds: evidence for metabolic specialization of maternal and filial tissues Mol. Cell. Proteomics 6 2007 2165 2179
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2165-2179
    • Gallardo, K.1    Firnhaber, C.2    Zuber, H.3    Héricher, D.4    Belghazi, M.5    Henry, C.6    Küster, H.7    Thompson, R.8
  • 19
    • 0035105233 scopus 로고    scopus 로고
    • Downregulation of caffeic acid 3-O-methyltransferase and caffeoyl CoA 3-O-methyltransferase in transgenic alfalfa: Impacts on lignin structure and implications for the biosynthesis of G and S lignin
    • DOI 10.1105/tpc.13.1.73
    • D. Guo, F. Chen, K. Inoue, J.W. Blount, and R.A. Dixon Downregulation of caffeic acid 3-O-methyltransferase and caffeoyl CoA 3-O-methyltransferase in transgenic alfalfa. Impacts on lignin structure and implications for the biosynthesis of G and S lignin Plant Cell 13 2001 73 88 (Pubitemid 32177034)
    • (2001) Plant Cell , vol.13 , Issue.1 , pp. 73-88
    • Guo, D.1    Chen, F.2    Inoue, K.3    Blount, J.W.4    Dixon, R.A.5
  • 20
    • 33745462558 scopus 로고    scopus 로고
    • Proteomic analysis of seed filling in Brassica napus. Developmental characterization of metabolic isozymes using high-resolution two-dimensional gel electrophoresis
    • DOI 10.1104/pp.105.075390
    • M. Hajduch, J.E. Casteel, K.E. Hurrelmeyer, Z. Song, G.K. Agrawal, and J.J. Thelen Proteomic analysis of seed filling in Brassica napus. Developmental characterization of metabolic isozymes using high-resolution two-dimensional gel electrophoresis Plant Physiol. 141 2006 32 46 (Pubitemid 43956180)
    • (2006) Plant Physiology , vol.141 , Issue.1 , pp. 32-46
    • Hajduch, M.1    Casteel, J.E.2    Hurrelmeyer, K.E.3    Song, Z.4    Agrawal, G.K.5    Thelen, J.J.6
  • 21
    • 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
    • DOI 10.1104/pp.104.056614
    • M. Hajduch, A. Ganapathy, J.W. Stein, and J.J. Thelen 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. 137 2005 1397 1419 (Pubitemid 43119338)
    • (2005) Plant Physiology , vol.137 , Issue.4 , pp. 1397-1419
    • Hajduch, M.1    Ganapathy, A.2    Stein, J.W.3    Thelen, J.J.4
  • 22
    • 77950524249 scopus 로고    scopus 로고
    • Systems analysis of seed filling in Arabidopsis: Using general linear modeling to assess concordance of transcript and protein expression
    • M. Hajduch, L.B. Hearne, J.A. Miernyk, J.E. Casteel, T. Joshi, G.K. Agrawal, Z. Song, M. Zhou, D. Xu, and J.J. Thelen Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression Plant Physiol. 152 2010 2078 2087
    • (2010) Plant Physiol. , vol.152 , pp. 2078-2087
    • Hajduch, M.1    Hearne, L.B.2    Miernyk, J.A.3    Casteel, J.E.4    Joshi, T.5    Agrawal, G.K.6    Song, Z.7    Zhou, M.8    Xu, D.9    Thelen, J.J.10
  • 23
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • DOI 10.1146/annurev.biochem.66.1.315
    • G.W. Hart Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins Annu. Rev. Biochem. 66 1997 315 335 (Pubitemid 27274659)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 24
    • 0036021405 scopus 로고    scopus 로고
    • Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh. Have overlapping functions necessary for gamete and seed development
    • L.M. Hartweck, C.L. Scott, and N.E. Olszewski Two O-linked N-acetylglucosamine transferase genes of Arabidopsis thaliana L. Heynh have overlapping functions necessary for gamete and seed development Genetics 161 2002 1279 1291 (Pubitemid 34831451)
    • (2002) Genetics , vol.161 , Issue.3 , pp. 1279-1291
    • Hartweck, L.M.1    Scott, C.L.2    Olszewski, N.E.3
  • 25
    • 70349644993 scopus 로고    scopus 로고
    • Quantitative proteomics of seed filling in castor: Comparison with soybean and rapeseed reveals differences between photosynthetic and nonphotosynthetic seed metabolism
    • N.L. Houston, M. Hajduch, and J.J. Thelen Quantitative proteomics of seed filling in castor: comparison with soybean and rapeseed reveals differences between photosynthetic and nonphotosynthetic seed metabolism Plant Physiol. 151 2009 857 868
    • (2009) Plant Physiol. , vol.151 , pp. 857-868
    • Houston, N.L.1    Hajduch, M.2    Thelen, J.J.3
  • 29
    • 0002310038 scopus 로고
    • β-Oxidization of fatty acids by specific organelles
    • H. Kindl β-Oxidization of fatty acids by specific organelles P.K. Stumpf, The Biochemistry of Plants 1987 Academic Press New York 1 50 vol. 9
    • (1987) The Biochemistry of Plants , pp. 1-50
    • Kindl, H.1
  • 31
    • 33748944014 scopus 로고    scopus 로고
    • Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis
    • DOI 10.1007/s00425-006-0300-6
    • M. Liang, E. Davis, D. Gardner, X. Cai, and Y. Wu Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis Planta 224 2006 1185 1196 (Pubitemid 44435868)
    • (2006) Planta , vol.224 , Issue.5 , pp. 1185-1196
    • Liang, M.1    Davis, E.2    Gardner, D.3    Cai, X.4    Wu, Y.5
  • 32
    • 65849244076 scopus 로고    scopus 로고
    • How long is long-term? Reflections based on over 20 years of post-Chernobyl management in Norway
    • A. Liland, J. Lochard, and L. Skuterud How long is long-term? Reflections based on over 20 years of post-Chernobyl management in Norway J. Environ. Radioact. 100 2009 581 584
    • (2009) J. Environ. Radioact. , vol.100 , pp. 581-584
    • Liland, A.1    Lochard, J.2    Skuterud, L.3
  • 33
    • 0000073961 scopus 로고
    • Isolation and characterization of a small molecular weight protein of linseed meal
    • K.T. Madhusudhan, and N. Singh Isolation and characterization of a small molecular weight protein of linseed meal Phytochemistry 24 1985 2507 2509
    • (1985) Phytochemistry , vol.24 , pp. 2507-2509
    • Madhusudhan, K.T.1    Singh, N.2
  • 34
    • 28544450370 scopus 로고    scopus 로고
    • Advancing LC performance with smaller particles and higher pressure
    • J. Mazzeo, U. Neue, M. Kele, and R. Plumb Advancing LC performance with smaller particles and higher pressure Anal. Chem. 77 2005 460A 467A
    • (2005) Anal. Chem. , vol.77
    • Mazzeo, J.1    Neue, U.2    Kele, M.3    Plumb, R.4
  • 36
    • 0027434086 scopus 로고
    • Evolutionary relationships among group II intron-encoded proteins and identification of a conserved domain that may be related to maturase function
    • G. Mohr, P.S. Perlman, and A.M. Lambowitz Evolutionary relationships among group II intron-encoded proteins and identification of a conserved domain that may be related to maturase function Nucleic Acids Res. 21 1993 4991 4997 (Pubitemid 23342504)
    • (1993) Nucleic Acids Research , vol.21 , Issue.22 , pp. 4991-4997
    • Mohr, G.1    Perlman, P.S.2    Lambowitz, A.M.3
  • 37
    • 3242774747 scopus 로고    scopus 로고
    • High-throughput peptide mass fingerprinting of soybean seed proteins: Automated workflow and utility of UniGene expressed sequence tag databases for protein identification
    • DOI 10.1016/j.phytochem.2004.04.011, PII S0031942204001621
    • B.P. Mooney, H.B. Krishnan, and J.J. Thelen High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification Phytochemistry 65 2004 1733 1744 (Pubitemid 38969919)
    • (2004) Phytochemistry , vol.65 , Issue.12 , pp. 1733-1744
    • Mooney, B.P.1    Thelen, J.J.2
  • 38
    • 0035183275 scopus 로고    scopus 로고
    • Study of soybean seed coat components and their relationship to water absorption
    • DOI 10.1021/jf010303s
    • W.J. Mullin, and W. Xu Study of soybean seed coat components and their relationship to water absorption J. Agric. Food Chem. 49 2001 5331 5335 (Pubitemid 33089673)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.11 , pp. 5331-5335
    • Mullin, W.J.1    Xu, W.2
  • 39
    • 0027273062 scopus 로고
    • Flaxseed proteins - A review
    • B.D. Oomah, and G. Mazza Flaxseed proteins - a review Food Chem. 48 1993 109 114
    • (1993) Food Chem. , vol.48 , pp. 109-114
    • Oomah, B.D.1    Mazza, G.2
  • 41
    • 2942562280 scopus 로고    scopus 로고
    • Evolutionary relatedness between glycolytic enzymes most frequently occurring in genomes
    • A. Oslancová, and Š. Janeček Evolutionary relatedness between glycolytic enzymes most frequently occurring in genomes Folia Microbiol. 49 2004 247 258 (Pubitemid 38730189)
    • (2004) Folia Microbiologica , vol.49 , Issue.3 , pp. 247-258
    • Oslancova, A.1    Janecek, S.2
  • 42
    • 0035987498 scopus 로고    scopus 로고
    • Initial proteome analysis of mature barley seeds and malt
    • DOI 10.100 2/1615-98 61(200 206)2:6<73 3::AID-PROT 733>3.0.CO;2-E
    • O. Østergaard, S. Melchior, P. Roepstorff, and B. Svensson Initial proteome analysis of mature barley seeds and malt Proteomics 2 2002 733 739 (Pubitemid 34693575)
    • (2002) Proteomics , vol.2 , Issue.6 , pp. 733-739
    • Ostergaard, O.1    Melchior, S.2    Roepstorff, P.3    Svensson, B.4
  • 44
    • 0029328357 scopus 로고
    • Seed storage proteins: Structures and biosynthesis
    • P.R. Shewry, J.A. Napier, and A.S. Tatham Seed storage proteins: structures and biosynthesis Plant Cell 7 1995 945 956
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 45
    • 0036668065 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis investigation of short-term response of flax seedlings to a cold shock
    • M. Tafforeau, M.C. Verdus, R. Charlionet, A. Cabin-Flaman, and C. Ripoll Two-dimensional electrophoresis investigation of short-term response of flax seedlings to a cold shock Electrophoresis 23 2002 2534 2540
    • (2002) Electrophoresis , vol.23 , pp. 2534-2540
    • Tafforeau, M.1    Verdus, M.C.2    Charlionet, R.3    Cabin-Flaman, A.4    Ripoll, C.5
  • 46
    • 0037302497 scopus 로고    scopus 로고
    • Molecular analysis of flax 2S storage protein conlinin and seed specific activity of its promoter
    • DOI 10.1016/S0981-9428(02)00022-0, PII S0981942802000220
    • M. Truksa, S.L. MacKenzieb, and X. Qiu Molecular analysis of flax 2S storage protein conlinin and seed specific activity of its promoter Plant Physiol. Biochem. 41 2003 141 147 (Pubitemid 36391869)
    • (2003) Plant Physiology and Biochemistry , vol.41 , Issue.2 , pp. 141-147
    • Truksa, M.1    MacKenzie, S.L.2    Qiu, X.3
  • 47
    • 0001442232 scopus 로고
    • The nitrogenous constituents of flaxseed. II. The isolation of a purified protein fraction
    • B. Vassel, and L.L. Nesbitt The nitrogenous constituents of flaxseed. II. The isolation of a purified protein fraction J. Biol. Chem. 159 1945 571 584
    • (1945) J. Biol. Chem. , vol.159 , pp. 571-584
    • Vassel, B.1    Nesbitt, L.L.2
  • 48
    • 77954146744 scopus 로고    scopus 로고
    • The origin and evolution of lignin biosynthesis
    • J.-K. Weng, and C. Chapple The origin and evolution of lignin biosynthesis New Phytol. 187 2010 273 285
    • (2010) New Phytol. , vol.187 , pp. 273-285
    • Weng, J.-K.1    Chapple, C.2


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