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Volumn 7, Issue 20, 2007, Pages 3788-3799

Alternative and effective proteomic analysis in Arabidopsis

Author keywords

2 DE; Mass spectrometry; Protein profile; Proteolysis

Indexed keywords

ARABIDOPSIS; ARTICLE; CHEMICAL ANALYSIS; CONTROLLED STUDY; FRACTIONATION; GENOMICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEOMICS;

EID: 35649013698     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700346     Document Type: Article
Times cited : (28)

References (32)
  • 1
    • 0037265724 scopus 로고    scopus 로고
    • Extraction of proteins from plant tissues for two-dimensional electrophoresis analysis
    • Giavalisco, P., Nordhoff, E., Lehrach, H., Gobom, J., Klose, J., Extraction of proteins from plant tissues for two-dimensional electrophoresis analysis. Electrophoresis 2003, 24, 207-216.
    • (2003) Electrophoresis , vol.24 , pp. 207-216
    • Giavalisco, P.1    Nordhoff, E.2    Lehrach, H.3    Gobom, J.4    Klose, J.5
  • 2
    • 1642569324 scopus 로고    scopus 로고
    • Proteomic studies in plants
    • Park, O. K., Proteomic studies in plants. J. Biochem. Mol. Biol. 2004, 37, 133-138.
    • (2004) J. Biochem. Mol. Biol , vol.37 , pp. 133-138
    • Park, O.K.1
  • 3
    • 4544265213 scopus 로고    scopus 로고
    • Tackling the plant proteome: Practical approaches, hurdles and experimental tools
    • Rose, J. K., Bashir, S., Giovannoni, J. J., Jahn, M. M., Saravanan, R. S., Tackling the plant proteome: Practical approaches, hurdles and experimental tools. Plant J. 2004, 39, 715-733.
    • (2004) Plant J , vol.39 , pp. 715-733
    • Rose, J.K.1    Bashir, S.2    Giovannoni, J.J.3    Jahn, M.M.4    Saravanan, R.S.5
  • 4
    • 0034931862 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of rice proteins by polyethylene glycol fractionation for protein arrays
    • Kim, S. T., Cho, K. S., Jang, Y. S., Kang, K. Y., Two-dimensional electrophoretic analysis of rice proteins by polyethylene glycol fractionation for protein arrays. Electrophoresis 2001, 22, 2103-2109.
    • (2001) Electrophoresis , vol.22 , pp. 2103-2109
    • Kim, S.T.1    Cho, K.S.2    Jang, Y.S.3    Kang, K.Y.4
  • 5
    • 1442282913 scopus 로고    scopus 로고
    • Prefractionation of protein samples for proteome analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Kim, S. T., Kim, H. S., Kim, H. J., Kim, S. G. et al., Prefractionation of protein samples for proteome analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Mol. Cells 2003, 16, 316-322.
    • (2003) Mol. Cells , vol.16 , pp. 316-322
    • Kim, S.T.1    Kim, H.S.2    Kim, H.J.3    Kim, S.G.4
  • 6
    • 0037398378 scopus 로고    scopus 로고
    • Fractionation of cytosolic proteins on an immobilized heparin column
    • Shefcheck, K., Yao, X., Fenselau, C., Fractionation of cytosolic proteins on an immobilized heparin column. Anal. Chem. 2003, 75, 1691-1698.
    • (2003) Anal. Chem , vol.75 , pp. 1691-1698
    • Shefcheck, K.1    Yao, X.2    Fenselau, C.3
  • 7
    • 18844427007 scopus 로고    scopus 로고
    • Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry
    • Giavalisco, P., Nordhoff, E., Kreitler, T., Kloppel, K. D. et al., Proteome analysis of Arabidopsis thaliana by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry. Proteomics 2005, 5, 1902-1913.
    • (2005) Proteomics , vol.5 , pp. 1902-1913
    • Giavalisco, P.1    Nordhoff, E.2    Kreitler, T.3    Kloppel, K.D.4
  • 9
    • 0348206867 scopus 로고
    • Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins
    • Damerval, C., De Vienne, D., Zivy, M., Thiellement, H., Technical improvements in two-dimensional electrophoresis increase the level of genetic variation detected in wheat-seedling proteins. Electrophoresis 1986, 7, 52-54.
    • (1986) Electrophoresis , vol.7 , pp. 52-54
    • Damerval, C.1    De Vienne, D.2    Zivy, M.3    Thiellement, H.4
  • 10
    • 35649014585 scopus 로고    scopus 로고
    • Total protein extraction with TCA-acetone
    • Mechin, V., Damerval, C., Zivy, M., Total protein extraction with TCA-acetone. Methods Mol. Biol. 2007, 355, 1-8.
    • (2007) Methods Mol. Biol , vol.355 , pp. 1-8
    • Mechin, V.1    Damerval, C.2    Zivy, M.3
  • 11
    • 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. et al., 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
  • 12
    • 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., 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.2
  • 13
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • Giglione, C., Serero, A., Pierre, M., Boisson, B., Meinnel, T., Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J. 2000, 19, 5916-5929.
    • (2000) EMBO J , vol.19 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 14
    • 19044396327 scopus 로고    scopus 로고
    • Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis
    • Ross, S., Giglione, C., Pierre, M., Espagne, C., Meinnel, T., Functional and developmental impact of cytosolic protein N-terminal methionine excision in Arabidopsis. Plant Physiol. 2005, 137, 623-637.
    • (2005) Plant Physiol , vol.137 , pp. 623-637
    • Ross, S.1    Giglione, C.2    Pierre, M.3    Espagne, C.4    Meinnel, T.5
  • 15
    • 0035787060 scopus 로고    scopus 로고
    • Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells
    • Pauly, M., Eberhard, S., Albersheim, P., Darvill, A., York, W. S., Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells. Planta 2001, 214, 67-74.
    • (2001) Planta , vol.214 , pp. 67-74
    • Pauly, M.1    Eberhard, S.2    Albersheim, P.3    Darvill, A.4    York, W.S.5
  • 16
    • 84980140250 scopus 로고
    • Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco
    • Jouanneau, J. P., Peaud-Lenoel, C., Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco. Physiologia Plantarum 1967, 20, 834-850.
    • (1967) Physiologia Plantarum , vol.20 , pp. 834-850
    • Jouanneau, J.P.1    Peaud-Lenoel, C.2
  • 17
    • 35649026115 scopus 로고    scopus 로고
    • Visible and fluorescent staining of two-dimensional gels
    • Chevalier, F., Rofidal, V., Rossignol, M., Visible and fluorescent staining of two-dimensional gels. Methods Mol. Biol. 2007, 355, 145-156.
    • (2007) Methods Mol. Biol , vol.355 , pp. 145-156
    • Chevalier, F.1    Rofidal, V.2    Rossignol, M.3
  • 18
    • 33644788986 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis of total yeast proteins
    • Boucherie, H., Monribot-Espagne, C., Two-dimensional gel electrophoresis of total yeast proteins. Methods Mol. Biol. 2006, 313, 47-64.
    • (2006) Methods Mol. Biol , vol.313 , pp. 47-64
    • Boucherie, H.1    Monribot-Espagne, C.2
  • 19
    • 0034633273 scopus 로고    scopus 로고
    • A method for global analysis of complex proteomes using sample prefractionation by solution isoelectrofocusing prior to two-dimensional electrophoresis
    • Zuo, X., Speicher, D. W., A method for global analysis of complex proteomes using sample prefractionation by solution isoelectrofocusing prior to two-dimensional electrophoresis. Anal. Biochem. 2000, 284, 266-278.
    • (2000) Anal. Biochem , vol.284 , pp. 266-278
    • Zuo, X.1    Speicher, D.W.2
  • 20
    • 0036208704 scopus 로고    scopus 로고
    • Differential gel exposure, a new methodology for the two-dimensional comparison of protein samples
    • Monribot-Espagne, C., Boucherie, H., Differential gel exposure, a new methodology for the two-dimensional comparison of protein samples. Proteomics 2002, 2, 229-240.
    • (2002) Proteomics , vol.2 , pp. 229-240
    • Monribot-Espagne, C.1    Boucherie, H.2
  • 21
    • 33645823426 scopus 로고    scopus 로고
    • Distinct roles of the first introns on the expression of Arabidopsis profilin gene family members
    • Jeong, Y. M., Mun, J. H., Lee, I., Woo, J. C. et al., Distinct roles of the first introns on the expression of Arabidopsis profilin gene family members. Plant Physiol. 2006, 140, 196-209.
    • (2006) Plant Physiol , vol.140 , pp. 196-209
    • Jeong, Y.M.1    Mun, J.H.2    Lee, I.3    Woo, J.C.4
  • 22
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • Santoni, V., Molloy, M., Rabilloud, T., Membrane proteins and proteomics: Un amour impossible? Electrophoresis 2000, 21, 1054-1070.
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 23
    • 0028809324 scopus 로고
    • A reactive, surface cysteine residue of the class-II fructose-1,6-bisphosphate aldolase of Escherichia coli revealed by electrospray ionisation mass spectrometry
    • Packman, L. C., Berry, A., A reactive, surface cysteine residue of the class-II fructose-1,6-bisphosphate aldolase of Escherichia coli revealed by electrospray ionisation mass spectrometry. Eur. J. Biochem. 1995, 227, 510-515.
    • (1995) Eur. J. Biochem , vol.227 , pp. 510-515
    • Packman, L.C.1    Berry, A.2
  • 24
    • 1642464018 scopus 로고    scopus 로고
    • A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells
    • Paron, I., D'Elia, A., D'Ambrosio, C., Scaloni, A. et al., A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells. Biochem. J. 2004, 378, 929-937.
    • (2004) Biochem. J , vol.378 , pp. 929-937
    • Paron, I.1    D'Elia, A.2    D'Ambrosio, C.3    Scaloni, A.4
  • 25
    • 0030714040 scopus 로고    scopus 로고
    • Allosteric communication in mammalian muscle aldolase
    • Sygusch, J., Beaudry, D., Allosteric communication in mammalian muscle aldolase. Biochem. J. 1997, 327, 717-720.
    • (1997) Biochem. J , vol.327 , pp. 717-720
    • Sygusch, J.1    Beaudry, D.2
  • 26
    • 33644682396 scopus 로고    scopus 로고
    • Stress-induced protein S-glutathionylation in Arabidopsis
    • Dixon, D. P., Skipsey, M., Grundy, N. M., Edwards, R., Stress-induced protein S-glutathionylation in Arabidopsis. Plant Physiol. 2005, 138, 2233-2244.
    • (2005) Plant Physiol , vol.138 , pp. 2233-2244
    • Dixon, D.P.1    Skipsey, M.2    Grundy, N.M.3    Edwards, R.4
  • 27
    • 22044458433 scopus 로고    scopus 로고
    • Molecular determinants of S-glutathionylation of carbonic anhydrase 3
    • Kim, G., Levine, R. L., Molecular determinants of S-glutathionylation of carbonic anhydrase 3. Antioxid. Redox Signal. 2005, 7, 849-854.
    • (2005) Antioxid. Redox Signal , vol.7 , pp. 849-854
    • Kim, G.1    Levine, R.L.2
  • 28
    • 0030805979 scopus 로고    scopus 로고
    • Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12
    • Link, A. J., Robison, K., Church, G. M., Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 1997, 18, 1259-1313.
    • (1997) Electrophoresis , vol.18 , pp. 1259-1313
    • Link, A.J.1    Robison, K.2    Church, G.M.3
  • 29
    • 0035525595 scopus 로고    scopus 로고
    • Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis
    • Mortz, E., Krogh, T. N., Vorum, H., Gorg, A., Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 2001, 1, 1359-1363.
    • (2001) Proteomics , vol.1 , pp. 1359-1363
    • Mortz, E.1    Krogh, T.N.2    Vorum, H.3    Gorg, A.4
  • 30
    • 33749529109 scopus 로고    scopus 로고
    • Polyethylene glycol fractionation improved detection of low-abundant proteins by two-dimensional electrophoresis analysis of plant proteome
    • Xi, J., Wang, X., Li, S., Zhou, X. et al., Polyethylene glycol fractionation improved detection of low-abundant proteins by two-dimensional electrophoresis analysis of plant proteome. Phytochemistry 2006, 67, 2341-2348.
    • (2006) Phytochemistry , vol.67 , pp. 2341-2348
    • Xi, J.1    Wang, X.2    Li, S.3    Zhou, X.4
  • 31
    • 33646239605 scopus 로고    scopus 로고
    • Arabidopsis thaliana proteomics: From proteome to genome
    • Baginsky, S., Gruissem, W., Arabidopsis thaliana proteomics: From proteome to genome. J. Exp. Bot. 2006, 57, 1485-1491.
    • (2006) J. Exp. Bot , vol.57 , pp. 1485-1491
    • Baginsky, S.1    Gruissem, W.2
  • 32
    • 0032935861 scopus 로고    scopus 로고
    • Emanuelsson, O., Nielsen, H., von Heijne, G., ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 1999, 8, 978-984.
    • Emanuelsson, O., Nielsen, H., von Heijne, G., ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 1999, 8, 978-984.


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