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Volumn 74, Issue 2, 2011, Pages 262-267

2-DE-based proteomic analysis of common bean (Phaseolus vulgaris L.) seeds

Author keywords

Mass spectrometry; Phaseolus vulgaris; Protein extraction methods; Seed proteome; Two dimensional electrophoresis

Indexed keywords

AMYLASE INHIBITOR; PHASEOLINONE; PHYTOHEMAGGLUTININ; SEED STORAGE PROTEIN;

EID: 78650308562     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2010.10.004     Document Type: Article
Times cited : (40)

References (32)
  • 1
    • 33846558837 scopus 로고    scopus 로고
    • A Dietary supplement containing standardized Phaseolus vulgaris extract influences body composition of overweight men and women
    • Celleno L., Tolaini M.V., D'Amore A., Perricone N.V., Preuss H.G. A Dietary supplement containing standardized Phaseolus vulgaris extract influences body composition of overweight men and women. Int J Med Sci 2007, 4:45-52.
    • (2007) Int J Med Sci , vol.4 , pp. 45-52
    • Celleno, L.1    Tolaini, M.V.2    D'Amore, A.3    Perricone, N.V.4    Preuss, H.G.5
  • 2
    • 77953059409 scopus 로고    scopus 로고
    • Beans and diabetes: Phaseolus vulgaris preparations as antihyperglycemic agents
    • Helmstädter A. Beans and diabetes: Phaseolus vulgaris preparations as antihyperglycemic agents. J Med Food 2010, 13:251-254.
    • (2010) J Med Food , vol.13 , pp. 251-254
    • Helmstädter, A.1
  • 3
    • 78650304000 scopus 로고    scopus 로고
    • Phaseolus vulgaris: a diploid model for soybean
    • Springer, G. Stacey (Ed.) Genetics and genomics of soybean
    • McClean P.E., Lavin M., Gepts P., Jackson S.A. Phaseolus vulgaris: a diploid model for soybean. Plant genetics/Genomics 2008, 2. Springer. G. Stacey (Ed.).
    • (2008) Plant genetics/Genomics , vol.2
    • McClean, P.E.1    Lavin, M.2    Gepts, P.3    Jackson, S.A.4
  • 5
    • 16244403005 scopus 로고    scopus 로고
    • Domestication patterns in common bean (Phaseolus vulgaris L.) and the origin of the Mesoamerican and Andean cultivated races
    • Chacón M.I., Pickersgill S.B., Debouck D.G. Domestication patterns in common bean (Phaseolus vulgaris L.) and the origin of the Mesoamerican and Andean cultivated races. Theor Appl Genet 2005, 110:432-444.
    • (2005) Theor Appl Genet , vol.110 , pp. 432-444
    • Chacón, M.I.1    Pickersgill, S.B.2    Debouck, D.G.3
  • 6
    • 61649095160 scopus 로고    scopus 로고
    • Structure of genetic diversity in the two major gene pools of common bean (Phaseolus vulgaris L., Fabaceae)
    • Kwak M., Gepts P. Structure of genetic diversity in the two major gene pools of common bean (Phaseolus vulgaris L., Fabaceae). Theor Appl Genet 2009, 118:979-992.
    • (2009) Theor Appl Genet , vol.118 , pp. 979-992
    • Kwak, M.1    Gepts, P.2
  • 7
    • 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., Le Signor C., Vandekerckhove J., Thompson R.D., Burstin J. 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    Le Signor, C.2    Vandekerckhove, J.3    Thompson, R.D.4    Burstin, J.5
  • 10
    • 67949108131 scopus 로고    scopus 로고
    • Differential expression proteomics to investigate responses and resistance to Orobanche crenata in Medicago truncatula
    • Castillejo M.A., Maldonado A.M., Dumas-Gaudot E., Fernández-Aparicio M., Susín R., Diego R., et al. Differential expression proteomics to investigate responses and resistance to Orobanche crenata in Medicago truncatula. BMC Genomics 2009, 10:294.
    • (2009) BMC Genomics , vol.10 , pp. 294
    • Castillejo, M.A.1    Maldonado, A.M.2    Dumas-Gaudot, E.3    Fernández-Aparicio, M.4    Susín, R.5    Diego, R.6
  • 12
    • 4444271855 scopus 로고    scopus 로고
    • Proteome reference maps of vegetative tissues in pea. An investigation of nitrogen mobilization from leaves during seed filling
    • Schiltz S., Gallardo K., Huart M., Negroni L., Sommerer N., Burstin J. Proteome reference maps of vegetative tissues in pea. An investigation of nitrogen mobilization from leaves during seed filling. Plant Physiol 2004, 35:2241-2260.
    • (2004) Plant Physiol , vol.35 , pp. 2241-2260
    • Schiltz, S.1    Gallardo, K.2    Huart, M.3    Negroni, L.4    Sommerer, N.5    Burstin, J.6
  • 14
    • 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
  • 15
    • 74349083247 scopus 로고    scopus 로고
    • Proteomic analysis of soybean [Glycine max (L.) Meer.] seeds during imbibition at chilling temperature
    • Cheng L., Gao X., Li S., Shi M., Javeed H., Jing X., et al. Proteomic analysis of soybean [Glycine max (L.) Meer.] seeds during imbibition at chilling temperature. Mol Breed 2010, 26:1-17.
    • (2010) Mol Breed , vol.26 , pp. 1-17
    • Cheng, L.1    Gao, X.2    Li, S.3    Shi, M.4    Javeed, H.5    Jing, X.6
  • 16
    • 67249096149 scopus 로고    scopus 로고
    • Proteome analysis of Pithecellobium dulce seeds using two-dimensional gel electrophoresis and tandem mass spectrometry
    • Sawasdipuksa N., Sumner L.L.W., Leib Z., Sangvanich P. Proteome analysis of Pithecellobium dulce seeds using two-dimensional gel electrophoresis and tandem mass spectrometry. J Sci Food Agric 2009, 89:1284-1291.
    • (2009) J Sci Food Agric , vol.89 , pp. 1284-1291
    • Sawasdipuksa, N.1    Sumner, L.L.W.2    Leib, Z.3    Sangvanich, P.4
  • 17
    • 33845970196 scopus 로고    scopus 로고
    • Proteome analysis of plant-virus interactome: comprehensive data of virus multiplication inside their hosts
    • Brizard J.P., Carapito C., Delalande F., Van Dorsselaer A., Brugidou C. Proteome analysis of plant-virus interactome: comprehensive data of virus multiplication inside their hosts. Mol Cell Proteomics 2006, 5:2279-2297.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2279-2297
    • Brizard, J.P.1    Carapito, C.2    Delalande, F.3    Van Dorsselaer, A.4    Brugidou, C.5
  • 18
    • 78650310260 scopus 로고    scopus 로고
    • Aplicación de la proteómica comparativa para la identificación de proteínas en Phaseolus vulgaris asociadas a resistencia a plagas
    • Bernal C., Galindo I., Pérez D., Diez N. Aplicación de la proteómica comparativa para la identificación de proteínas en Phaseolus vulgaris asociadas a resistencia a plagas. Agronomía Trop 2006, 56:555-559.
    • (2006) Agronomía Trop , vol.56 , pp. 555-559
    • Bernal, C.1    Galindo, I.2    Pérez, D.3    Diez, N.4
  • 19
    • 59149105426 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of bean plants infected by a virulent and avirulent obligate rust fungus
    • Lee J., Feng J., Campbell K.B., Scheffler B.E., Garret W.M., Thibivilliers S., et al. Quantitative proteomic analysis of bean plants infected by a virulent and avirulent obligate rust fungus. Mol Cell Proteomics 2009, 8:19-31.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 19-31
    • Lee, J.1    Feng, J.2    Campbell, K.B.3    Scheffler, B.E.4    Garret, W.M.5    Thibivilliers, S.6
  • 20
    • 77953121743 scopus 로고    scopus 로고
    • Proteomic analysis of common bean seed with storage protein deficiency reveals up-regulation of sulfur-rich proteins and starch and raffinose metabolic enzymes and down-regulation of the secretory pathway
    • Marsolais F., Pajak A., Yin F., Taylor M., Gabriel M., Merino D.M., et al. Proteomic analysis of common bean seed with storage protein deficiency reveals up-regulation of sulfur-rich proteins and starch and raffinose metabolic enzymes and down-regulation of the secretory pathway. J Proteomics 2010, 73:1587-1600.
    • (2010) J Proteomics , vol.73 , pp. 1587-1600
    • Marsolais, F.1    Pajak, A.2    Yin, F.3    Taylor, M.4    Gabriel, M.5    Merino, D.M.6
  • 22
    • 0028066050 scopus 로고
    • Use of 2-dimensional protein-pattern analysis for the characterization of Arabidopsis thaliana mutants
    • Santoni V., Bellini C., Caboche M. Use of 2-dimensional protein-pattern analysis for the characterization of Arabidopsis thaliana mutants. Planta 1994, 192:557-566.
    • (1994) Planta , vol.192 , pp. 557-566
    • Santoni, V.1    Bellini, C.2    Caboche, M.3
  • 23
    • 4444237731 scopus 로고    scopus 로고
    • A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues
    • Saravanan R.S., Rose J.K.C. A critical evaluation of sample extraction techniques for enhanced proteomic analysis of recalcitrant plant tissues. Proteomics 2004, 4:2522-2532.
    • (2004) Proteomics , vol.4 , pp. 2522-2532
    • Saravanan, R.S.1    Rose, J.K.C.2
  • 24
    • 22044456721 scopus 로고    scopus 로고
    • Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis
    • Carpentier S.C., Witters E., Laukens K., Deckers P., Swennen R., Panis B. Preparation of protein extracts from recalcitrant plant tissues: an evaluation of different methods for two-dimensional gel electrophoresis analysis. Proteomics 2005, 5:2497-2507.
    • (2005) Proteomics , vol.5 , pp. 2497-2507
    • Carpentier, S.C.1    Witters, E.2    Laukens, K.3    Deckers, P.4    Swennen, R.5    Panis, B.6
  • 25
    • 35948954213 scopus 로고    scopus 로고
    • A protein extraction method compatible with proteomic analysis for the euhalophyte Salicornia europaea
    • Wang X.C., Li X.F., Deng X., Han H.P., Shi W.L., Li Y.X. A protein extraction method compatible with proteomic analysis for the euhalophyte Salicornia europaea. Electrophoresis 2007, 28:3976-3987.
    • (2007) Electrophoresis , vol.28 , pp. 3976-3987
    • Wang, X.C.1    Li, X.F.2    Deng, X.3    Han, H.P.4    Shi, W.L.5    Li, Y.X.6
  • 26
    • 63149114267 scopus 로고    scopus 로고
    • Protein extraction methods compatible with proteomic analysis for the cotton seedling
    • Xie C., Wang D., Yang X. Protein extraction methods compatible with proteomic analysis for the cotton seedling. Crop Sci 2009, 49:395-402.
    • (2009) Crop Sci , vol.49 , pp. 395-402
    • Xie, C.1    Wang, D.2    Yang, X.3
  • 27
    • 0022432415 scopus 로고
    • Nucleotide sequences from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families
    • Slightom J.L., Drong R.F., Klassy R.C., Hoffman L.M. Nucleotide sequences from phaseolin cDNA clones: the major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucleic Acids Res 1985, 13:6483-6498.
    • (1985) Nucleic Acids Res , vol.13 , pp. 6483-6498
    • Slightom, J.L.1    Drong, R.F.2    Klassy, R.C.3    Hoffman, L.M.4
  • 28
    • 0023645611 scopus 로고
    • Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin
    • Sturm A., Van Kuik J.A., Vliegenthart J.F.G., Chrispeels M.J. Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin. J Bio Chem 1987, 262:13392-13403.
    • (1987) J Bio Chem , vol.262 , pp. 13392-13403
    • Sturm, A.1    Van Kuik, J.A.2    Vliegenthart, J.F.G.3    Chrispeels, M.J.4
  • 29
    • 0000434454 scopus 로고
    • Purification of an endonuclease involved with storage-protein degradation in Phaseolus vulgaris L. cotyledons
    • Boylan M.T., Sussex I.M. Purification of an endonuclease involved with storage-protein degradation in Phaseolus vulgaris L. cotyledons. Planta 1987, 170:343-352.
    • (1987) Planta , vol.170 , pp. 343-352
    • Boylan, M.T.1    Sussex, I.M.2
  • 30
    • 0001421463 scopus 로고
    • Lectin-like proteins accumulate as fragmentation products in bean seed protein bodies
    • Ceriotti A., Vitale A., Bollini R. Lectin-like proteins accumulate as fragmentation products in bean seed protein bodies. FEBS Lett 1989, 250:157-160.
    • (1989) FEBS Lett , vol.250 , pp. 157-160
    • Ceriotti, A.1    Vitale, A.2    Bollini, R.3
  • 31
    • 63349090096 scopus 로고    scopus 로고
    • Proteomic approaches to study structure, functions and toxicity of legume seeds lectins. Perspectives for the assessment of food quality and safety
    • Nasi A., Picariello G., Ferranti P. Proteomic approaches to study structure, functions and toxicity of legume seeds lectins. Perspectives for the assessment of food quality and safety. J Proteomics 2009, 72:527-538.
    • (2009) J Proteomics , vol.72 , pp. 527-538
    • Nasi, A.1    Picariello, G.2    Ferranti, P.3
  • 32
    • 33947573571 scopus 로고    scopus 로고
    • Qualitative and quantitative evaluation of protein extraction protocols for apple and strawberry fruit suitable for two-dimensional electrophoresis and mass spectrometry analysis
    • Zheng Q., Song J., Doncaster K., Rowland E., Byers D.M. Qualitative and quantitative evaluation of protein extraction protocols for apple and strawberry fruit suitable for two-dimensional electrophoresis and mass spectrometry analysis. J Agric Food Chem 2007, 55:1663-1673.
    • (2007) J Agric Food Chem , vol.55 , pp. 1663-1673
    • Zheng, Q.1    Song, J.2    Doncaster, K.3    Rowland, E.4    Byers, D.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.