메뉴 건너뛰기




Volumn 13, Issue 12-13, 2013, Pages 2016-2030

Development and optimisation of a label-free quantitative proteomic procedure and its application in the assessment of genetically modified tomato fruit

Author keywords

Food safety; Genetic modification; Label free quantitation; Plant proteomics; Tomato

Indexed keywords

PROTEOME;

EID: 84880097658     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201200480     Document Type: Article
Times cited : (30)

References (40)
  • 1
    • 79953700284 scopus 로고    scopus 로고
    • iTRAQ analysis reveals mechanisms of growth defects due to excess zinc in Arabidopsis
    • Fukao, Y., Ferjani, A., Tomioka, R., Nagasaki, N. et al., iTRAQ analysis reveals mechanisms of growth defects due to excess zinc in Arabidopsis. Plant Physiol. 2011, 155, 1893-1907.
    • (2011) Plant Physiol. , vol.155 , pp. 1893-1907
    • Fukao, Y.1    Ferjani, A.2    Tomioka, R.3    Nagasaki, N.4
  • 2
    • 79551697131 scopus 로고    scopus 로고
    • iTRAQ protein profile analysis of Arabidopsis roots reveals new aspects critical for uron homeostasis
    • Lan, P., Li, W. F., Wen, T. N., Shiau, J. Y. et al., iTRAQ protein profile analysis of Arabidopsis roots reveals new aspects critical for uron homeostasis. Plant Physiol. 2011, 155, 821-834.
    • (2011) Plant Physiol. , vol.155 , pp. 821-834
    • Lan, P.1    Li, W.F.2    Wen, T.N.3    Shiau, J.Y.4
  • 3
    • 84860641713 scopus 로고    scopus 로고
    • Performance of isobaric and isotopic labeling in quantitative plant proteomics
    • Nogueira, F. C. S., Palmisano, G., Schwammle, V., Campos, F. A. P. et al., Performance of isobaric and isotopic labeling in quantitative plant proteomics. J. Proteome Res. 2012, 11, 3046-3052.
    • (2012) J. Proteome Res. , vol.11 , pp. 3046-3052
    • Nogueira, F.C.S.1    Palmisano, G.2    Schwammle, V.3    Campos, F.A.P.4
  • 4
    • 84855895599 scopus 로고    scopus 로고
    • Proteomics investigation of endogenous S-nitrosylation in Arabidopsis
    • Fares, A., Rossignol, M., Peltier, J. B., Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem. Biophys. Res. Commun. 2011, 416, 331-336.
    • (2011) Biochem. Biophys. Res. Commun. , vol.416 , pp. 331-336
    • Fares, A.1    Rossignol, M.2    Peltier, J.B.3
  • 5
    • 79959849574 scopus 로고    scopus 로고
    • Extending SILAC to proteomics of plant cell lines
    • Schutz, W., Hausmann, N., Krug, K., Hampp, R., Macek, B., Extending SILAC to proteomics of plant cell lines. Plant Cell 2011, 23, 1701-1705.
    • (2011) Plant Cell , vol.23 , pp. 1701-1705
    • Schutz, W.1    Hausmann, N.2    Krug, K.3    Hampp, R.4    Macek, B.5
  • 6
    • 77957764188 scopus 로고    scopus 로고
    • Mass spectrometry in plant proteomic analysis
    • Colas, I., Koroleva, O., Shaw, P. J., Mass spectrometry in plant proteomic analysis. Plant Biosyst. 2010, 144, 703-714.
    • (2010) Plant Biosyst. , vol.144 , pp. 703-714
    • Colas, I.1    Koroleva, O.2    Shaw, P.J.3
  • 7
    • 34248161925 scopus 로고    scopus 로고
    • Implications of 15N-metabolic labeling for automated peptide identification in Arabidopsis thaliana
    • Nelson, C. J., Huttlin, E. L., Hegeman, A. D., Harms, A. C., Sussman M. R., Implications of 15N-metabolic labeling for automated peptide identification in Arabidopsis thaliana. Proteomics 2007, 7, 1279-1292.
    • (2007) Proteomics , vol.7 , pp. 1279-1292
    • Nelson, C.J.1    Huttlin, E.L.2    Hegeman, A.D.3    Harms, A.C.4    Sussman, M.R.5
  • 8
    • 35348939574 scopus 로고    scopus 로고
    • Quantitative proteomics using uniform 15N-labeling, MASCOT, and the trans-proteomic pipeline
    • Palmblad, M, Bindschedler, L.V., Cramer, R., Quantitative proteomics using uniform 15N-labeling, MASCOT, and the trans-proteomic pipeline. Proteomics 2007, 7, 3462-3469.
    • (2007) Proteomics , vol.7 , pp. 3462-3469
    • Palmblad, M.1    Bindschedler, L.V.2    Cramer, R.3
  • 9
    • 84861672042 scopus 로고    scopus 로고
    • Label-free quantitative proteomics reveals differentially regulated proteins in the latex of sticky diseased Carica papaya L. plants
    • Rodrigues, S. P., Ventura, J. A., Aguilar, C., Nakayasu, E. S. et al., Label-free quantitative proteomics reveals differentially regulated proteins in the latex of sticky diseased Carica papaya L. plants. J. Proteomics 2012, 75, 3191-3198.
    • (2012) J. Proteomics , vol.75 , pp. 3191-3198
    • Rodrigues, S.P.1    Ventura, J.A.2    Aguilar, C.3    Nakayasu, E.S.4
  • 10
    • 74049115774 scopus 로고    scopus 로고
    • Mass spectrometry-based label-free quantitative proteomics
    • Zhu, W. H., Smith, J. W., Huang, C. M., Mass spectrometry-based label-free quantitative proteomics. J. Biomed. Biotechnol. 2009, 2010, 840518.
    • (2009) J. Biomed. Biotechnol. , vol.2010 , pp. 840518
    • Zhu, W.H.1    Smith, J.W.2    Huang, C.M.3
  • 11
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study
    • Bindschedler, L., Palmblad, M., Cramer, R., Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. Phytochemistry 2008, 69, 1962-1972.
    • (2008) Phytochemistry , vol.69 , pp. 1962-1972
    • Bindschedler, L.1    Palmblad, M.2    Cramer, R.3
  • 12
    • 79959687700 scopus 로고    scopus 로고
    • Differential proteomic response of rice (Oryza sativa) leaves exposed to high- and low-temperature stress
    • Gammulla, C. G., Pascovici, D., Atwell, B. J., Haynes, P. A., Differential proteomic response of rice (Oryza sativa) leaves exposed to high- and low-temperature stress. Proteomics 2011, 11, 2839-2850.
    • (2011) Proteomics , vol.11 , pp. 2839-2850
    • Gammulla, C.G.1    Pascovici, D.2    Atwell, B.J.3    Haynes, P.A.4
  • 13
    • 39749105466 scopus 로고    scopus 로고
    • Heat-shock response in Arabidopsis thaliana explored by multiplexed quantitative proteomics using differential metabolic labeling
    • Palmblad, M., Mills, D. J., Bindschedler, L. V., Heat-shock response in Arabidopsis thaliana explored by multiplexed quantitative proteomics using differential metabolic labeling. J. Proteome Res. 2008, 7, 780-785.
    • (2008) J. Proteome Res. , vol.7 , pp. 780-785
    • Palmblad, M.1    Mills, D.J.2    Bindschedler, L.V.3
  • 14
    • 84859879608 scopus 로고    scopus 로고
    • Quantitative proteomics reveals dynamic changes in the plasma membrane during Arabidopsis immune signaling
    • Elmore, J. M., Liu, J., Smith, B., Phinney, B., Coaker, G., Quantitative proteomics reveals dynamic changes in the plasma membrane during Arabidopsis immune signaling. Mol. Cell. Proteomics 2012, 11, M111.014555.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Elmore, J.M.1    Liu, J.2    Smith, B.3    Phinney, B.4    Coaker, G.5
  • 15
    • 78649531413 scopus 로고    scopus 로고
    • Isobaric tags for relative and absolute quantification-based comparative proteomics reveals the features of plasma membrane-associated proteomes of pollen grains and pollen tubes from Lilium davidii
    • Han, B., Chen, S. X., Dai, S. J., Yang, N., Wang, T., Isobaric tags for relative and absolute quantification-based comparative proteomics reveals the features of plasma membrane-associated proteomes of pollen grains and pollen tubes from Lilium davidii. J. Integr. Plant Biol. 2010, 52, 1043-1058.
    • (2010) J. Integr. Plant Biol. , vol.52 , pp. 1043-1058
    • Han, B.1    Chen, S.X.2    Dai, S.J.3    Yang, N.4    Wang, T.5
  • 16
    • 77952065773 scopus 로고    scopus 로고
    • Comparative proteomics of salt tolerance in Arabidopsis thaliana and Thellungiella halophila
    • Pang, Q. Y., Chen, S. X., Dai, S. J., Chen, Y. Z. et al., Comparative proteomics of salt tolerance in Arabidopsis thaliana and Thellungiella halophila. J. Proteome Res. 2010, 9, 2584-2599.
    • (2010) J. Proteome Res. , vol.9 , pp. 2584-2599
    • Pang, Q.Y.1    Chen, S.X.2    Dai, S.J.3    Chen, Y.Z.4
  • 17
    • 84864281039 scopus 로고    scopus 로고
    • A label-free differential quantitative proteomics analysis of a TaLEA-introduced transgenic Populus simonii x Populus nigra dwarf mutant
    • Chen, S., Yuan, H. M., Liu, G. F., Li, H. Y., Jiang, J., A label-free differential quantitative proteomics analysis of a TaLEA-introduced transgenic Populus simonii x Populus nigra dwarf mutant. Mol. Biol. Rep. 2012, 39, 7657-7664.
    • (2012) Mol. Biol. Rep. , vol.39 , pp. 7657-7664
    • Chen, S.1    Yuan, H.M.2    Liu, G.F.3    Li, H.Y.4    Jiang, J.5
  • 18
    • 84856490899 scopus 로고    scopus 로고
    • Proteomic analysis of susceptible rice plants expressing the whole plant-specific resistance against Magnaporthe oryzae: involvement of a thaumatin-like protein
    • Koga, H., Dohi, K., Nishiuchi, T., Kato, T. et al., Proteomic analysis of susceptible rice plants expressing the whole plant-specific resistance against Magnaporthe oryzae: involvement of a thaumatin-like protein. Physiol. Mol. Plant Path. 2012, 77, 60-66.
    • (2012) Physiol. Mol. Plant Path. , vol.77 , pp. 60-66
    • Koga, H.1    Dohi, K.2    Nishiuchi, T.3    Kato, T.4
  • 19
    • 79952708666 scopus 로고    scopus 로고
    • Proteomic analysis of known and candidate rice allergens between non-transgenic and transgenic plants
    • Satoh, R., Nakamura, R., Komatsu, A., Oshima, M., Teshima, R., Proteomic analysis of known and candidate rice allergens between non-transgenic and transgenic plants. Reg. Toxicol. Pharmacol. 2011, 59, 437-444.
    • (2011) Reg. Toxicol. Pharmacol. , vol.59 , pp. 437-444
    • Satoh, R.1    Nakamura, R.2    Komatsu, A.3    Oshima, M.4    Teshima, R.5
  • 20
    • 0030932384 scopus 로고    scopus 로고
    • Functional foods
    • Farr, D. R., Functional foods. Cancer Lett. 1997, 114, 59-63.
    • (1997) Cancer Lett. , vol.114 , pp. 59-63
    • Farr, D.R.1
  • 21
    • 77953194787 scopus 로고    scopus 로고
    • Integrative transcript and metabolite analysis of nutritionally enhanced DE-ETIOLATED1 down-regulated tomato fruit
    • Enfissi, E. M. A., Barneche, F., Ahmed, I., Lichtle, C. et al., Integrative transcript and metabolite analysis of nutritionally enhanced DE-ETIOLATED1 down-regulated tomato fruit. Plant Cell 2010, 22, 1190-1215.
    • (2010) Plant Cell , vol.22 , pp. 1190-1215
    • Enfissi, E.M.A.1    Barneche, F.2    Ahmed, I.3    Lichtle, C.4
  • 22
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford, M. M., Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-54.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli, U. K., Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 1970, 227, 680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 24
    • 82755198892 scopus 로고    scopus 로고
    • Label-free quantitative proteomics analysis of cotton leaf response to nitric oxide
    • Meng, Y. Y., Liu, F., Pang, C. Y., Fan, S. L. et al., Label-free quantitative proteomics analysis of cotton leaf response to nitric oxide. J. Proteome Res. 2011, 10, 5416-5432.
    • (2011) J. Proteome Res. , vol.10 , pp. 5416-5432
    • Meng, Y.Y.1    Liu, F.2    Pang, C.Y.3    Fan, S.L.4
  • 25
    • 72149105355 scopus 로고    scopus 로고
    • Label-free quantitative proteomics analysis of etiolated maize seedling leaves during greening
    • Shen, Z., Li, P., Ni, R. J., Ritchie, M. et al., Label-free quantitative proteomics analysis of etiolated maize seedling leaves during greening. Mol. Cell. Proteomics 2009, 8, 2443-2460.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2443-2460
    • Shen, Z.1    Li, P.2    Ni, R.J.3    Ritchie, M.4
  • 26
    • 33646564676 scopus 로고    scopus 로고
    • Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes
    • Wang, G., Wu, W. W., Zeng, W., Chou, C. L., Shen, R. F., Label-free protein quantification using LC-coupled ion trap or FT mass spectrometry: reproducibility, linearity, and application with complex proteomes. J. Proteome Res. 2006, 5, 1214-1223.
    • (2006) J. Proteome Res , vol.5 , pp. 1214-1223
    • Wang, G.1    Wu, W.W.2    Zeng, W.3    Chou, C.L.4    Shen, R.F.5
  • 27
    • 0344305739 scopus 로고    scopus 로고
    • Global protein identification and quantification technology using two-dimensional liquid chromatography nanospray mass spectrometry
    • Chelius, D., Zhang, T., Wang, G. H., Shen, R. F., Global protein identification and quantification technology using two-dimensional liquid chromatography nanospray mass spectrometry. Anal. Chem. 2003, 75, 6658-6665.
    • (2003) Anal. Chem. , vol.75 , pp. 6658-6665
    • Chelius, D.1    Zhang, T.2    Wang, G.H.3    Shen, R.F.4
  • 28
    • 30744459634 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of drug-induced changes in mycobacteria
    • Hughes, M. A., Silva, J. C., Geromanos, S. J., Townsend, C. A., Quantitative proteomic analysis of drug-induced changes in mycobacteria. J. Proteome Res. 2006, 5, 54-63.
    • (2006) J. Proteome Res. , vol.5 , pp. 54-63
    • Hughes, M.A.1    Silva, J.C.2    Geromanos, S.J.3    Townsend, C.A.4
  • 29
    • 20144388265 scopus 로고    scopus 로고
    • Quantitative proteomic analysis by accurate mass retention time pairs
    • Silva, J. C., Denny, R., Dorschel, C. A., Gorenstein, M. et al., Quantitative proteomic analysis by accurate mass retention time pairs. Anal. Chem. 2005, 77, 2187-2200.
    • (2005) Anal. Chem. , vol.77 , pp. 2187-2200
    • Silva, J.C.1    Denny, R.2    Dorschel, C.A.3    Gorenstein, M.4
  • 30
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang, W. X., Zhou, H. H., Lin, H., Roy, S. et al., Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal. Chem. 2003, 75, 4818-4826.
    • (2003) Anal. Chem. , vol.75 , pp. 4818-4826
    • Wang, W.X.1    Zhou, H.H.2    Lin, H.3    Roy, S.4
  • 32
    • 49749115277 scopus 로고    scopus 로고
    • Comparison of a label-free quantitative proteomic method based on peptide ion current area to the isotope coded affinity tag method
    • Ryu, S., Gallis, B., Goo, Y. A., Shaffer, S. A. et al., Comparison of a label-free quantitative proteomic method based on peptide ion current area to the isotope coded affinity tag method. Cancer Inform. 2008, 6, 243-255.
    • (2008) Cancer Inform. , vol.6 , pp. 243-255
    • Ryu, S.1    Gallis, B.2    Goo, Y.A.3    Shaffer, S.A.4
  • 34
    • 12244270638 scopus 로고    scopus 로고
    • Differential proteomics via probabilistic peptide identification scores
    • Colinge, J., Chiappe, D., Lagache, S., Moniatte, M., Bougueleret, L., Differential proteomics via probabilistic peptide identification scores. Anal. Chem. 2005, 77, 596-606.
    • (2005) Anal. Chem. , vol.77 , pp. 596-606
    • Colinge, J.1    Chiappe, D.2    Lagache, S.3    Moniatte, M.4    Bougueleret, L.5
  • 36
    • 79551500036 scopus 로고    scopus 로고
    • Less label, more free: approaches in label-free quantitative mass spectrometry
    • Neilson, K. A., Ali, N. A., Muralidharan, S., Mirzaei, M. et al., Less label, more free: approaches in label-free quantitative mass spectrometry. Proteomics 2011, 11, 535-53.
    • (2011) Proteomics , vol.11 , pp. 535-553
    • Neilson, K.A.1    Ali, N.A.2    Muralidharan, S.3    Mirzaei, M.4
  • 37
    • 79958099698 scopus 로고    scopus 로고
    • Advances in qualitative and quantitative plant membrane proteomics
    • Kota, U., Goshe, M. B., Advances in qualitative and quantitative plant membrane proteomics. Phytochemistry 2011, 72, 1040-1060.
    • (2011) Phytochemistry , vol.72 , pp. 1040-1060
    • Kota, U.1    Goshe, M.B.2
  • 38
    • 79958093378 scopus 로고    scopus 로고
    • Recent progress in liquid chromatography-based separation and label-free quantitative plant proteomics
    • Matros, A., Kaspar, S., Witzel, K., Mock, H. P., Recent progress in liquid chromatography-based separation and label-free quantitative plant proteomics. Phytochemistry 2011, 72, 963-974.
    • (2011) Phytochemistry , vol.72 , pp. 963-974
    • Matros, A.1    Kaspar, S.2    Witzel, K.3    Mock, H.P.4
  • 39
    • 79961202534 scopus 로고    scopus 로고
    • The importance of the digest: proteolysis and absolute quantification in proteomics
    • Brownridge, P., Beynon, R. J., The importance of the digest: proteolysis and absolute quantification in proteomics. Methods 2011, 54, 351-360.
    • (2011) Methods , vol.54 , pp. 351-360
    • Brownridge, P.1    Beynon, R.J.2
  • 40
    • 84867546621 scopus 로고    scopus 로고
    • Proteome changes in tomato lines transformed with phytoene synthase-1 in the sense and antisense orientations
    • Robertson, R. P., Koistinen, K., Gerrish, C., Halket, J. M. et al., Proteome changes in tomato lines transformed with phytoene synthase-1 in the sense and antisense orientations. J. Exp. Bot. 2012, 63, 6035-6043.
    • (2012) J. Exp. Bot. , vol.63 , pp. 6035-6043
    • Robertson, R.P.1    Koistinen, K.2    Gerrish, C.3    Halket, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.