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Volumn 3, Issue JAN, 2013, Pages

Quantitation, networking, and function of protein phosphorylation in plant cell

Author keywords

AQUIP; Cell signaling and regulation; Mass spectrometry based interactomics; Plant; Post translational modification; Quantitative proteomics; SILIA

Indexed keywords


EID: 84900869581     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2012.00302     Document Type: Review
Times cited : (8)

References (56)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R., and Mann, M. (2003). Mass spectrometry-based proteomics. Nature 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L., and Hunter, C. L. (2006). Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 5, 573-588.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 3
    • 84856702955 scopus 로고    scopus 로고
    • The use of heavy nitrogen in quantitative proteomics experiments in plants
    • Arsova, B., Kierszniowska, S., and Schulze, W. X. (2012). The use of heavy nitrogen in quantitative proteomics experiments in plants. Trends Plant Sci. 17, 102-112.
    • (2012) Trends Plant Sci. , vol.17 , pp. 102-112
    • Arsova, B.1    Kierszniowska, S.2    Schulze, W.X.3
  • 5
    • 4444301306 scopus 로고    scopus 로고
    • Absolute quantification of the model biomarker prostate-specific antigen in serum by LC-Ms/MS using protein cleavage and isotope dilution mass spectrometry
    • Barnidge, D. R., Goodmanson, M. K., Klee, G. G., and Muddiman, D. C. (2004). Absolute quantification of the model biomarker prostate-specific antigen in serum by LC-Ms/MS using protein cleavage and isotope dilution mass spectrometry. J. Proteome Res. 3, 644-652.
    • (2004) J. Proteome Res. , vol.3 , pp. 644-652
    • Barnidge, D.R.1    Goodmanson, M.K.2    Klee, G.G.3    Muddiman, D.C.4
  • 7
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • Beynon, R. J., Doherty, M. K., Pratt, J. M., and Gaskell, S. J. (2005). Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Nat. Methods 2, 587-589.
    • (2005) Nat. Methods , vol.2 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 8
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics: An oxidative stress case study
    • Bindschedler, L. V., Palmblada, M., and Cramera, R. (2008). Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics: an oxidative stress case study. Phytochemistry 69, 1962-1972.
    • (2008) Phytochemistry , vol.69 , pp. 1962-1972
    • Bindschedler, L.V.1    Palmblada, M.2    Cramera, R.3
  • 9
  • 10
    • 33750588336 scopus 로고    scopus 로고
    • Advances in plant proteomics
    • Chen, S., and Harmon, A. C. (2006). Advances in plant proteomics. Proteomics 6, 5504-5516.
    • (2006) Proteomics , vol.6 , pp. 5504-5516
    • Chen, S.1    Harmon, A.C.2
  • 11
    • 80052510197 scopus 로고    scopus 로고
    • Proteomic screening method for phosphopeptide motif binding proteins using peptide libraries
    • Christofk, H. R., Wu, N., Cantley, L. C., and Asara, J. M. (2011). Proteomic screening method for phosphopeptide motif binding proteins using peptide libraries. J. Proteome Res. 10, 4158-4164.
    • (2011) J. Proteome Res. , vol.10 , pp. 4158-4164
    • Christofk, H.R.1    Wu, N.2    Cantley, L.C.3    Asara, J.M.4
  • 12
    • 0028362176 scopus 로고
    • Molecular characterization of human stathmin expressed in Escherichia coli site-directed mutagenesis of 2 phosphorylatable serines (Ser-25 and Ser-63)
    • Curmi, P. A., Maucuer, A., Asselin, S., Lecourtois, M., Chaffotte, A., Schmitter, J. M., et al. (1994). Molecular characterization of human stathmin expressed in Escherichia coli site-directed mutagenesis of 2 phosphorylatable serines (Ser-25 and Ser-63). Biochem. J. 300, 331-338.
    • (1994) Biochem. J. , vol.300 , pp. 331-338
    • Curmi, P.A.1    Maucuer, A.2    Asselin, S.3    Lecourtois, M.4    Chaffotte, A.5    Schmitter, J.M.6
  • 13
    • 55849107369 scopus 로고    scopus 로고
    • Towards functional phosphoproteomics by mapping differential phosphorylation events in signaling networks
    • de la Fuente van Bentem, S., Mentzen, W. I., de la Fuente, A., and Hirt, H. (2008). Towards functional phosphoproteomics by mapping differential phosphorylation events in signaling networks. Proteomics 8, 4453-4465.
    • (2008) Proteomics , vol.8 , pp. 4453-4465
    • de la Fuente van Bentem, S.1    Mentzen, W.I.2    de la Fuente, A.3    Hirt, H.4
  • 16
    • 36549015311 scopus 로고    scopus 로고
    • Metabolic labeling of plant cell cultures with K(15)NO3 as a tool for quantitative analysis of proteins and metabolites
    • Engelsberger, W. R., Erban, A., Kopka, J., and Schulze, W. X. (2006). Metabolic labeling of plant cell cultures with K(15)NO3 as a tool for quantitative analysis of proteins and metabolites. Plant Methods 2, 14.
    • (2006) Plant Methods , vol.2 , pp. 14
    • Engelsberger, W.R.1    Erban, A.2    Kopka, J.3    Schulze, W.X.4
  • 17
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., and Gygi, S. P. (2003). Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. U.S.A. 100, 6940-6945.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 19
    • 76649083593 scopus 로고    scopus 로고
    • Quantitative proteomics by metabolic labeling of model organisms
    • Gouw, J. W., Krijgsveld, J., and Heck, A. J. (2010). Quantitative proteomics by metabolic labeling of model organisms. Mol. Cell. Proteomics 9, 11-24.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 11-24
    • Gouw, J.W.1    Krijgsveld, J.2    Heck, A.J.3
  • 20
    • 79958150765 scopus 로고    scopus 로고
    • Relative and accurate measurement of protein abundance using 15N stable isotope labeling in Arabidopsis (SILIA)
    • Guo, G., and Li, N. (2011). Relative and accurate measurement of protein abundance using 15N stable isotope labeling in Arabidopsis (SILIA). Phytochemistry 72, 1028-1039.
    • (2011) Phytochemistry , vol.72 , pp. 1028-1039
    • Guo, G.1    Li, N.2
  • 21
    • 2642569251 scopus 로고    scopus 로고
    • Absolute quantification of proteins in solutions and in polyacrylamide gels by mass spectrometry
    • Havlis, J., and Shevchenko, A. (2004). Absolute quantification of proteins in solutions and in polyacrylamide gels by mass spectrometry. Anal. Chem. 76, 3029-3036.
    • (2004) Anal. Chem. , vol.76 , pp. 3029-3036
    • Havlis, J.1    Shevchenko, A.2
  • 22
    • 38549127781 scopus 로고    scopus 로고
    • PhosPhAt: A database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor
    • Heazlewood, J. L., Durek, P., Hummel, J., Selbig, J., Weckwerth, W., Walther, D., et al. (2008). PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor. Nucleic Acids Res. 36, D1015-D1021.
    • (2008) Nucleic Acids Res. , vol.36
    • Heazlewood, J.L.1    Durek, P.2    Hummel, J.3    Selbig, J.4    Weckwerth, W.5    Walther, D.6
  • 23
    • 39049154321 scopus 로고    scopus 로고
    • Study of early leaf senescence in Arabidopsis thaliana by quantitative proteomics using reciprocal 14N/15N labeling and difference gel electrophoresis
    • Hebeler, R., Oeljeklaus, S., Reidegeld, K. A., Eisenacher, M., Stephan, C., Sitek, B., et al. (2008). Study of early leaf senescence in Arabidopsis thaliana by quantitative proteomics using reciprocal 14N/15N labeling and difference gel electrophoresis. Mol. Cell. Proteomics 7, 108-120.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 108-120
    • Hebeler, R.1    Oeljeklaus, S.2    Reidegeld, K.A.3    Eisenacher, M.4    Stephan, C.5    Sitek, B.6
  • 24
    • 3042554224 scopus 로고    scopus 로고
    • Identification of a new motif for CDPK phosphorylation in vitro that suggests ACC synthase may be a CDPK substrate
    • Hernandez, S. C., Hardin, S. C., Clouse, S. D., Kieber, J. J., and Huber, S. C. (2004). Identification of a new motif for CDPK phosphorylation in vitro that suggests ACC synthase may be a CDPK substrate. Arch. Biochem. Biophys. 428, 81-91.
    • (2004) Arch. Biochem. Biophys. , vol.428 , pp. 81-91
    • Hernandez, S.C.1    Hardin, S.C.2    Clouse, S.D.3    Kieber, J.J.4    Huber, S.C.5
  • 25
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter, T. (2000). Signaling-2000 and beyond. Cell 100, 113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 26
    • 34249650777 scopus 로고    scopus 로고
    • Comparison of full versus partial metabolic labeling for quantitative proteomics analysis in Arabidopsis thaliana
    • Huttlin, E. L., Hegeman, A. D., Harms, A. C., and Sussman, M. R. (2007). Comparison of full versus partial metabolic labeling for quantitative proteomics analysis in Arabidopsis thaliana. Mol. Cell. Proteomics 6, 860-881.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 860-881
    • Huttlin, E.L.1    Hegeman, A.D.2    Harms, A.C.3    Sussman, M.R.4
  • 27
    • 44249108848 scopus 로고    scopus 로고
    • Directional and quantitative phosphorylation networks
    • Jorgensen, C., and Linding, R. (2008). Directional and quantitative phosphorylation networks. Brief. Funct. Genomics Proteomics 7, 17-26.
    • (2008) Brief. Funct. Genomics Proteomics , vol.7 , pp. 17-26
    • Jorgensen, C.1    Linding, R.2
  • 28
    • 0034438283 scopus 로고    scopus 로고
    • The efficacy of RNAi in the study of the plant cytoskeleton
    • Klink, V. P., and Wolniak, S. M. (2000). The efficacy of RNAi in the study of the plant cytoskeleton. J. Plant Growth Regul. 19, 371-384.
    • (2000) J. Plant Growth Regul. , vol.19 , pp. 371-384
    • Klink, V.P.1    Wolniak, S.M.2
  • 29
    • 79958099698 scopus 로고    scopus 로고
    • Advances in qualitative and quantitative plant membrane proteomics
    • Kota, U., and Goshe, M. B. (2011). Advances in qualitative and quantitative plant membrane proteomics. Phytochemistry 72, 1040-1060.
    • (2011) Phytochemistry , vol.72 , pp. 1040-1060
    • Kota, U.1    Goshe, M.B.2
  • 31
    • 0033391482 scopus 로고    scopus 로고
    • T-DNA as an insertional mutagen in Arabidopsis
    • Krysan, P. J., Young, J. C., and Sussman, M. R. (1999). T-DNA as an insertional mutagen in Arabidopsis. Plant Cell 11, 2283-2290.
    • (1999) Plant Cell , vol.11 , pp. 2283-2290
    • Krysan, P.J.1    Young, J.C.2    Sussman, M.R.3
  • 32
    • 0026701313 scopus 로고
    • Rat-liver 6-phosphofructo-2-kinase fructose-2, 6-bisphosphatase-properties of phospho-forms and dephospho-forms and of 2 mutants in which Ser32 has been changed by site-directed mutagenesis
    • Kurland, I. J., Elmaghrabi, M. R., Correia, J. J., and Pilkis, S. J. (1992). Rat-liver 6-phosphofructo-2-kinase fructose-2, 6-bisphosphatase-properties of phospho-forms and dephospho-forms and of 2 mutants in which Ser32 has been changed by site-directed mutagenesis. J. Biol. Chem. 267, 4416-4423.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4416-4423
    • Kurland, I.J.1    Elmaghrabi, M.R.2    Correia, J.J.3    Pilkis, S.J.4
  • 33
    • 80052389537 scopus 로고    scopus 로고
    • Production and use of stable isotope-labeled proteins for absolute quantitative proteomics
    • Lebert, D., Dupuis, A., Garin, J., Bruley, C., and Brun, V. (2011). Production and use of stable isotope-labeled proteins for absolute quantitative proteomics. Methods Mol. Biol. 753, 93-115.
    • (2011) Methods Mol. Biol. , vol.753 , pp. 93-115
    • Lebert, D.1    Dupuis, A.2    Garin, J.3    Bruley, C.4    Brun, V.5
  • 34
    • 63049130982 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer
    • Li, H., Wong, W. S., Zhu, L., Guo, H. W., Ecker, J., and Li, N. (2009). Phosphoproteomic analysis of ethylene-regulated protein phosphorylation in etiolated seedlings of Arabidopsis mutant ein2 using two-dimensional separations coupled with a hybrid quadrupole time-of-flight mass spectrometer. Proteomics 9, 1646-1661.
    • (2009) Proteomics , vol.9 , pp. 1646-1661
    • Li, H.1    Wong, W.S.2    Zhu, L.3    Guo, H.W.4    Ecker, J.5    Li, N.6
  • 35
    • 84864805482 scopus 로고    scopus 로고
    • AQUIP: Absolute quantitation of isoforms of post-translationally modified proteins in transgenic organism
    • Li, Y., Shu, Y., Peng, C., Zhu, L., Guo, G., and Li, N. (2012). AQUIP: absolute quantitation of isoforms of post-translationally modified proteins in transgenic organism. Mol. Cell. Proteomics 11, 272-285.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 272-285
    • Li, Y.1    Shu, Y.2    Peng, C.3    Zhu, L.4    Guo, G.5    Li, N.6
  • 36
    • 16344390469 scopus 로고    scopus 로고
    • Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by MPK6, a stress-responsive mitogen-activated protein kinase, induces ethylene biosynthesis in Arabidopsis
    • Liu, Y. D., and Zhang, S. Q. (2004). Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by MPK6, a stress-responsive mitogen-activated protein kinase, induces ethylene biosynthesis in Arabidopsis. Plant Cell 16, 3386-3399.
    • (2004) Plant Cell , vol.16 , pp. 3386-3399
    • Liu, Y.D.1    Zhang, S.Q.2
  • 37
    • 33745621292 scopus 로고    scopus 로고
    • Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: Determination of inhibitory phosphorylation status of cyclin-dependent kinases
    • Mayya, V., Rezual, K., Wu, L., Fong, M. B., and Han, D. K. (2006). Absolute quantification of multisite phosphorylation by selective reaction monitoring mass spectrometry: determination of inhibitory phosphorylation status of cyclin-dependent kinases. Mol. Cell. Proteomics 5, 1146-1157.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1146-1157
    • Mayya, V.1    Rezual, K.2    Wu, L.3    Fong, M.B.4    Han, D.K.5
  • 38
    • 77952986553 scopus 로고    scopus 로고
    • Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs
    • Mok, J., Kim, P. M., Lam, H. Y., Piccirillo, S., Zhou, X., Jeschke, G. R., et al. (2010). Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Sci. Signal. 3, ra12.
    • (2010) Sci. Signal. , vol.3
    • Mok, J.1    Kim, P.M.2    Lam, H.Y.3    Piccirillo, S.4    Zhou, X.5    Jeschke, G.R.6
  • 39
    • 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., and Sussman, M. R. (2007). Implications of 15N-metabolic labeling for automated peptide identification in Arabidopsis thaliana. Proteomics 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
  • 40
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda, Y., Huang, K., Cross, F. R., Cowburn, D., and Chait, B. T. (1999). Accurate quantitation of protein expression and site-specific phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 96, 6591-6596.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 41
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., et al. (2002). Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 42
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and Mann, M. (2005). Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 43
    • 33847179916 scopus 로고    scopus 로고
    • Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes
    • Pratt, J. M., Simpson, D. M., Doherty, M. K., Rivers, J., Gaskell, S. J., and Beynon, R. J. (2006). Multiplexed absolute quantification for proteomics using concatenated signature peptides encoded by QconCAT genes. Nat. Protoc. 1, 1029-1043.
    • (2006) Nat. Protoc. , vol.1 , pp. 1029-1043
    • Pratt, J.M.1    Simpson, D.M.2    Doherty, M.K.3    Rivers, J.4    Gaskell, S.J.5    Beynon, R.J.6
  • 44
    • 34548427053 scopus 로고    scopus 로고
    • Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT
    • Rivers, J., Simpson, D. M., Robertson, D. H., Gaskell, S. J., and Beynon, R. J. (2007). Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT. Mol. Cell. Proteomics 6, 1416-1427.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1416-1427
    • Rivers, J.1    Simpson, D.M.2    Robertson, D.H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 45
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B., Parker, K., Hattan, S., et al. (2004). Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattan, S.6
  • 46
    • 57649093858 scopus 로고    scopus 로고
    • SILIP: A novel stable isotope labeling method for in planta quantitative proteomic analysis
    • Schaff, J. E., Mbeunkui, F., Blackburn, K., Bird, D. M., and Goshe, M. B. (2008). SILIP: a novel stable isotope labeling method for in planta quantitative proteomic analysis. Plant J. 56, 840-854.
    • (2008) Plant J. , vol.56 , pp. 840-854
    • Schaff, J.E.1    Mbeunkui, F.2    Blackburn, K.3    Bird, D.M.4    Goshe, M.B.5
  • 47
    • 33746730389 scopus 로고    scopus 로고
    • Phosphoproteomic approaches to elucidate cellular signaling networks
    • Schmelzle, K., and White, F. M. (2006). Phosphoproteomic approaches to elucidate cellular signaling networks. Curr. Opin. Biotechnol. 17, 406-414.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 406-414
    • Schmelzle, K.1    White, F.M.2
  • 49
    • 77955873040 scopus 로고    scopus 로고
    • Proteomics approaches to understand protein phosphorylation in pathway modulation
    • Schulze, W. X. (2010). Proteomics approaches to understand protein phosphorylation in pathway modulation. Curr. Opin. Plant Biol. 13, 280-287.
    • (2010) Curr. Opin. Plant Biol. , vol.13 , pp. 280-287
    • Schulze, W.X.1
  • 50
    • 77952538049 scopus 로고    scopus 로고
    • Quantitation in mass-spectrometry-based proteomics
    • Schulze, W. X., and Usadel, B. (2010). Quantitation in mass-spectrometry-based proteomics. Annu. Rev. Plant Biol. 61, 491-516.
    • (2010) Annu. Rev. Plant Biol. , vol.61 , pp. 491-516
    • Schulze, W.X.1    Usadel, B.2
  • 51
    • 43149125189 scopus 로고    scopus 로고
    • Different phosphorylation states of the anaphase promoting complex in response to antimitotic drugs: A quantitative proteomic analysis
    • Steen, J. A., Steen, H., Georgi, A., Parker, K., Springer, M., Kirchner, M., et al. (2008). Different phosphorylation states of the anaphase promoting complex in response to antimitotic drugs: a quantitative proteomic analysis. Proc. Natl. Acad. Sci. U.S.A. 105, 6069-6074.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6069-6074
    • Steen, J.A.1    Steen, H.2    Georgi, A.3    Parker, K.4    Springer, M.5    Kirchner, M.6
  • 52
    • 84863338106 scopus 로고    scopus 로고
    • Calcium/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr-348 and Ser-500 to regulate its activity and calcium dependence
    • Tavares, C. D. J., O'Brien, J. P., Abramczyk, O., Devkota, A. K., Shores, K. S., Ferguson, S. B., et al. (2012). Calcium/calmodulin stimulates the autophosphorylation of elongation factor 2 kinase on Thr-348 and Ser-500 to regulate its activity and calcium dependence. Biochemistry 51, 2232-2245.
    • (2012) Biochemistry , vol.51 , pp. 2232-2245
    • Tavares, C.D.J.1    O'Brien, J.P.2    Abramczyk, O.3    Devkota, A.K.4    Shores, K.S.5    Ferguson, S.B.6
  • 53
    • 37849025862 scopus 로고    scopus 로고
    • Quantitative proteomics in plants: Choices in abundance
    • Thelen, J. J., and Peck, S. C. (2007). Quantitative proteomics in plants: choices in abundance. Plant Cell 19, 3339-3346.
    • (2007) Plant Cell , vol.19 , pp. 3339-3346
    • Thelen, J.J.1    Peck, S.C.2
  • 54
    • 79960979428 scopus 로고    scopus 로고
    • A large-scale method to measure absolute protein phosphorylation stoichiometries
    • Wu, R., Haas, W., Dephoure, N., Huttlin, E. L., Zhai, B., Sowa, M. E., et al. (2011). A large-scale method to measure absolute protein phosphorylation stoichiometries. Nat. Methods 8, 677-683.
    • (2011) Nat. Methods , vol.8 , pp. 677-683
    • Wu, R.1    Haas, W.2    Dephoure, N.3    Huttlin, E.L.4    Zhai, B.5    Sowa, M.E.6
  • 55
    • 39149095565 scopus 로고    scopus 로고
    • Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4 signalling
    • U789-U781
    • Yoo, S. D., Cho, Y. H., Tena, G., Xiong, Y., and Sheen, J. (2008). Dual control of nuclear EIN3 by bifurcate MAPK cascades in C2H4 signalling. Nature 451, U789-U781.
    • (2008) Nature , vol.451
    • Yoo, S.D.1    Cho, Y.H.2    Tena, G.3    Xiong, Y.4    Sheen, J.5
  • 56
    • 84873243295 scopus 로고    scopus 로고
    • Functional phosphoproteomic analysis reveals that a Ser62-phosphorylated isoform of ethylene response factor 110 is involved in Arabidopsis bolting
    • doi: 10.1104pp.112.204487 [Epub ahead of print]
    • Zhu, L., Liu, D. D., Li, Y. J., and Li, N. (2012). Functional phosphoproteomic analysis reveals that a Ser62-phosphorylated isoform of ethylene response factor 110 is involved in Arabidopsis bolting. Plant Physiol. doi: 10.1104pp.112.204487 [Epub ahead of print].
    • (2012) Plant Physiol.
    • Zhu, L.1    Liu, D.D.2    Li, Y.J.3    Li, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.