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Volumn 15, Issue 5-6, 2015, Pages 1127-1141

Recent advances and challenges in plant phosphoproteomics

Author keywords

MS; Phosphopeptide enrichment; Phosphoproteomics; Plant proteomics; PTM network

Indexed keywords

METAL ION; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; STABLE ISOTOPE; VEGETABLE PROTEIN; PROTEOME;

EID: 84924660339     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201400410     Document Type: Review
Times cited : (109)

References (126)
  • 1
    • 33750588336 scopus 로고    scopus 로고
    • Advances in plant proteomics
    • Chen, S., Harmon, A. C., Advances in plant proteomics. Proteomics 2006, 6, 5504-5516.
    • (2006) Proteomics , vol.6 , pp. 5504-5516
    • Chen, S.1    Harmon, A.C.2
  • 2
    • 84901354464 scopus 로고    scopus 로고
    • Electrochemical methods for detection of post-translational modifications of proteins
    • Shumyantseva, V. V., Suprun, E. V., Bulko, T. V., Archakov, A. I., Electrochemical methods for detection of post-translational modifications of proteins. Biosens. Bioelectron. 2014, 61, 131-139.
    • (2014) Biosens. Bioelectron. , vol.61 , pp. 131-139
    • Shumyantseva, V.V.1    Suprun, E.V.2    Bulko, T.V.3    Archakov, A.I.4
  • 4
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., Jensen, O. N., Proteomic analysis of post-translational modifications. Nat. Biotechnol. 2003, 21, 255-261.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 5
    • 84924682207 scopus 로고    scopus 로고
    • The Association of Biotechnological Resources Facilities
    • Delta mass: A Database of Protein Post Translational Modifications.,
    • The Association of Biotechnological Resources Facilities. Delta mass: A Database of Protein Post Translational Modifications. 2014, http://www.abrf.org/index.cfm/dm.home?AvgMass=all.
    • (2014)
  • 6
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann, M., Ong, S. E., Grønborg, M., Steen, H. et al., Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 2002, 20, 261-268.
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Grønborg, M.3    Steen, H.4
  • 10
    • 84856087985 scopus 로고    scopus 로고
    • Platforms for enrichment of phosphorylated proteins and peptides in proteomics
    • Batalha, I. L., Lowe, C. R., Roque, A. C., Platforms for enrichment of phosphorylated proteins and peptides in proteomics. Trends Biotechnol. 2012, 30, 100-110.
    • (2012) Trends Biotechnol. , vol.30 , pp. 100-110
    • Batalha, I.L.1    Lowe, C.R.2    Roque, A.C.3
  • 11
    • 0029328357 scopus 로고
    • Seed storage proteins: structures and biosynthesis
    • Shewry, P. R., Napier, J. A., Tatham, A. S. Seed storage proteins: structures and biosynthesis. Plant Cell 1995, 7, 945-956.
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 12
    • 84900869581 scopus 로고    scopus 로고
    • Quantitation, networking, and function of protein phosphorylation in plant cell
    • Zhu, L., Li, N., Quantitation, networking, and function of protein phosphorylation in plant cell. Front Plant Sci. 2013, 3, 302.
    • (2013) Front Plant Sci. , vol.3 , pp. 302
    • Zhu, L.1    Li, N.2
  • 13
    • 84903795865 scopus 로고    scopus 로고
    • Basics and recent advances of two dimensional- polyacrylamide gel electrophoresis
    • Magdeldin, S., Enany, S., Yoshida, Y., Xu, B. et al., Basics and recent advances of two dimensional- polyacrylamide gel electrophoresis. Clin. Proteomics 2014, 11, 16.
    • (2014) Clin. Proteomics , vol.11 , pp. 16
    • Magdeldin, S.1    Enany, S.2    Yoshida, Y.3    Xu, B.4
  • 14
    • 33751401609 scopus 로고    scopus 로고
    • Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape
    • Agrawal, G. K., Thelen, J. J., Large scale identification and quantitative profiling of phosphoproteins expressed during seed filling in oilseed rape. Mol. Cell Proteomics 2006, 5, 2044-2059.
    • (2006) Mol. Cell Proteomics , vol.5 , pp. 2044-2059
    • Agrawal, G.K.1    Thelen, J.J.2
  • 15
    • 65349083749 scopus 로고    scopus 로고
    • A high-resolution two dimensional Gel- and Pro-Q DPS-based proteomics workflow for phosphoprotein identification and quantitative profiling
    • ix.
    • Agrawal, G. K., Thelen, J. J., A high-resolution two dimensional Gel- and Pro-Q DPS-based proteomics workflow for phosphoprotein identification and quantitative profiling. Methods Mol. Biol. 2009, 527, 3-19, ix.
    • (2009) Methods Mol. Biol. , vol.527 , pp. 3-19
    • Agrawal, G.K.1    Thelen, J.J.2
  • 16
    • 79958125680 scopus 로고    scopus 로고
    • Using multiplex-staining to study changes in the maize leaf phosphoproteome in response to mechanical wounding
    • Lewandowska-Gnatowska, E., Johnston, M. L., Antoine, W., Szczegielniak, J. et al., Using multiplex-staining to study changes in the maize leaf phosphoproteome in response to mechanical wounding. Phytochemistry 2011, 72, 1285-1292.
    • (2011) Phytochemistry , vol.72 , pp. 1285-1292
    • Lewandowska-Gnatowska, E.1    Johnston, M.L.2    Antoine, W.3    Szczegielniak, J.4
  • 17
    • 79951999099 scopus 로고    scopus 로고
    • The phosphoproteome of Arabidopsis plants lacking the oxidative signal-inducible1 (OXI1) protein kinase
    • Howden, A. J., Salek, M., Miguet, L., Pullen, M. et al., The phosphoproteome of Arabidopsis plants lacking the oxidative signal-inducible1 (OXI1) protein kinase. New Phytol. 2011, 190, 49-56.
    • (2011) New Phytol. , vol.190 , pp. 49-56
    • Howden, A.J.1    Salek, M.2    Miguet, L.3    Pullen, M.4
  • 18
    • 84891525422 scopus 로고    scopus 로고
    • Proteomic and phosphoproteomic analysis of polyethylene glycol-induced osmotic stress in root tips of common bean (Phaseolus vulgaris L.)
    • Yang, Z. B., Eticha, D., Führs, H., Heintz, D. et al., Proteomic and phosphoproteomic analysis of polyethylene glycol-induced osmotic stress in root tips of common bean (Phaseolus vulgaris L.). J. Exp. Bot. 2013, 64, 5569-5586.
    • (2013) J. Exp. Bot. , vol.64 , pp. 5569-5586
    • Yang, Z.B.1    Eticha, D.2    Führs, H.3    Heintz, D.4
  • 19
    • 84861161220 scopus 로고    scopus 로고
    • PTMScan direct: identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS/MS
    • Stokes, M. P., Farnsworth, C. L., Moritz, A., Silva, J. C. et al., PTMScan direct: identification and quantification of peptides from critical signaling proteins by immunoaffinity enrichment coupled with LC-MS/MS. Mol. Cell Proteomics 2012, 11, 187-201.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 187-201
    • Stokes, M.P.1    Farnsworth, C.L.2    Moritz, A.3    Silva, J.C.4
  • 20
    • 57749098543 scopus 로고    scopus 로고
    • Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells
    • Ghelis, T., Bolbach, G., Clodic, G., Habricot, Y. et al., Protein tyrosine kinases and protein tyrosine phosphatases are involved in abscisic acid-dependent processes in Arabidopsis seeds and suspension cells. Plant Physiol. 2008, 148, 1668-1680.
    • (2008) Plant Physiol. , vol.148 , pp. 1668-1680
    • Ghelis, T.1    Bolbach, G.2    Clodic, G.3    Habricot, Y.4
  • 21
    • 84867036962 scopus 로고    scopus 로고
    • Enrichment techniques employed in phosphoproteomics
    • Fíla, J., Honys, D., Enrichment techniques employed in phosphoproteomics. Amino Acids 2012, 43, 1025-1047.
    • (2012) Amino Acids , vol.43 , pp. 1025-1047
    • Fíla, J.1    Honys, D.2
  • 22
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H., Horn, D. M., Tang, N., Mathivanan, S., Pandey, A., Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. USA 2007, 104, 2199-2204.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 23
    • 1942437647 scopus 로고    scopus 로고
    • Phosphorylation of the amino terminus of maize sucrose synthase in relation to membrane association and enzyme activity
    • Hardin, S. C., Winter, H., Huber, S. C., Phosphorylation of the amino terminus of maize sucrose synthase in relation to membrane association and enzyme activity. Plant Physiol. 2004, 134, 1427-1438.
    • (2004) Plant Physiol. , vol.134 , pp. 1427-1438
    • Hardin, S.C.1    Winter, H.2    Huber, S.C.3
  • 24
    • 17144412237 scopus 로고    scopus 로고
    • Isolation of phosphorylated and dephosphorylated forms of the CP43 internal antenna of photosystem II in Hordeum vulgare L
    • Andreucci, F., Barbato, R., Picollo, C., Segalla, A., Isolation of phosphorylated and dephosphorylated forms of the CP43 internal antenna of photosystem II in Hordeum vulgare L. J. Exp. Bot. 2005, 56, 1239-1244.
    • (2005) J. Exp. Bot. , vol.56 , pp. 1239-1244
    • Andreucci, F.1    Barbato, R.2    Picollo, C.3    Segalla, A.4
  • 25
    • 84881101018 scopus 로고    scopus 로고
    • Systems-wide analysis of K-Ras, Cdc42, and PAK4 signaling by quantitative phosphoproteomics
    • Gnad, F., Young, A., Zhou, W., Lyle, K. et al., Systems-wide analysis of K-Ras, Cdc42, and PAK4 signaling by quantitative phosphoproteomics. Mol. Cell Proteomics 2013, 12, 2070-2080.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 2070-2080
    • Gnad, F.1    Young, A.2    Zhou, W.3    Lyle, K.4
  • 26
    • 84875116092 scopus 로고    scopus 로고
    • Epidermal growth factor stimulates extracellular-signal regulated kinase phosphorylation of a novel site on cytoplasmic Dynein intermediate chain 2
    • Pullikuth, A. K., Ozdemir, A., Cardenas, D., Bailey, E. et al., Epidermal growth factor stimulates extracellular-signal regulated kinase phosphorylation of a novel site on cytoplasmic Dynein intermediate chain 2. Int. J. Mol. Sci. 2013, 14, 3595-3620.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 3595-3620
    • Pullikuth, A.K.1    Ozdemir, A.2    Cardenas, D.3    Bailey, E.4
  • 28
    • 77956875232 scopus 로고    scopus 로고
    • Comparison of metal and metal oxide media for phosphopeptide enrichment prior to mass spectrometric analyses
    • Gates, M. B., Tomer, K. B., Deterding, L. J., Comparison of metal and metal oxide media for phosphopeptide enrichment prior to mass spectrometric analyses. J. Am. Soc. Mass Spectrom. 2010, 21, 1649-1659.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1649-1659
    • Gates, M.B.1    Tomer, K.B.2    Deterding, L.J.3
  • 29
    • 84899572145 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of the non-seed vascular plant model Selaginella moellendorffii
    • Chen, X., Chan, W. L., Zhu, F. Y., Lo, C., Phosphoproteomic analysis of the non-seed vascular plant model Selaginella moellendorffii. Proteome Sci. 2014, 12, 16.
    • (2014) Proteome Sci. , vol.12 , pp. 16
    • Chen, X.1    Chan, W.L.2    Zhu, F.Y.3    Lo, C.4
  • 31
    • 84901711349 scopus 로고    scopus 로고
    • Phosphorylation of Arabidopsis ubiquitin ligase ATL31 is critical for plant carbon/nitrogen nutrient balance response and controls the stability of 14-3-3 proteins
    • Yasuda, S., Sato, T., Maekawa, S., Aoyama, S. et al., Phosphorylation of Arabidopsis ubiquitin ligase ATL31 is critical for plant carbon/nitrogen nutrient balance response and controls the stability of 14-3-3 proteins. J. Biol. Chem. 2014, 289, 15179-15193.
    • (2014) J. Biol. Chem. , vol.289 , pp. 15179-15193
    • Yasuda, S.1    Sato, T.2    Maekawa, S.3    Aoyama, S.4
  • 32
    • 42649139982 scopus 로고    scopus 로고
    • SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides
    • Thingholm, T. E., Jensen, O. N., Robinson, P. J., Larsen, M. R., SIMAC (sequential elution from IMAC), a phosphoproteomics strategy for the rapid separation of monophosphorylated from multiply phosphorylated peptides. Mol. Cell Proteomics 2008, 7, 661-671.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 661-671
    • Thingholm, T.E.1    Jensen, O.N.2    Robinson, P.J.3    Larsen, M.R.4
  • 34
    • 84867041794 scopus 로고    scopus 로고
    • Advances in phosphopeptide enrichment techniques for phosphoproteomics
    • Beltran, L., Cutillas, P. R., Advances in phosphopeptide enrichment techniques for phosphoproteomics. Amino Acids 2012, 43, 1009-1024.
    • (2012) Amino Acids , vol.43 , pp. 1009-1024
    • Beltran, L.1    Cutillas, P.R.2
  • 35
    • 84860549883 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean
    • Meyer, L. J., Gao, J., Xu, D., Thelen, J. J., Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean. Plant Physiol. 2012, 159, 517-528.
    • (2012) Plant Physiol. , vol.159 , pp. 517-528
    • Meyer, L.J.1    Gao, J.2    Xu, D.3    Thelen, J.J.4
  • 36
    • 33846643023 scopus 로고    scopus 로고
    • Rapid enrichment of phosphopeptides and phosphoproteins from complex samples using magnetic particles coated with alumina as the concentrating probes for MALDI MS analysis
    • Chen, C. T., Chen, W. Y., Tsai, P. J., Chien, K. Y. et al., Rapid enrichment of phosphopeptides and phosphoproteins from complex samples using magnetic particles coated with alumina as the concentrating probes for MALDI MS analysis. J. Proteome Res. 2007, 6, 316-325.
    • (2007) J. Proteome Res. , vol.6 , pp. 316-325
    • Chen, C.T.1    Chen, W.Y.2    Tsai, P.J.3    Chien, K.Y.4
  • 37
    • 80051672948 scopus 로고    scopus 로고
    • Tools for analyzing the phosphoproteome and other phosphorylated biomolecules: a review
    • Leitner, A., Sturm, M., Lindner, W., Tools for analyzing the phosphoproteome and other phosphorylated biomolecules: a review. Anal. Chim. Acta 2011, 703, 19-30.
    • (2011) Anal. Chim. Acta , vol.703 , pp. 19-30
    • Leitner, A.1    Sturm, M.2    Lindner, W.3
  • 38
    • 84858809599 scopus 로고    scopus 로고
    • Ultra acidic strong cation exchange enabling the efficient enrichment of basic phosphopeptides
    • Hennrich, M. L., van den Toorn, H. W., Groenewold, V., Heck, A. J., Mohammed, S., Ultra acidic strong cation exchange enabling the efficient enrichment of basic phosphopeptides. Anal. Chem. 2012, 84, 1804-1808.
    • (2012) Anal. Chem. , vol.84 , pp. 1804-1808
    • Hennrich, M.L.1    van den Toorn, H.W.2    Groenewold, V.3    Heck, A.J.4    Mohammed, S.5
  • 39
    • 40549130385 scopus 로고    scopus 로고
    • Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography
    • Han, G., Ye, M., Zhou, H., Jiang, X. et al., Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics 2008, 8, 1346-1361.
    • (2008) Proteomics , vol.8 , pp. 1346-1361
    • Han, G.1    Ye, M.2    Zhou, H.3    Jiang, X.4
  • 40
    • 84884388035 scopus 로고    scopus 로고
    • Battle through signaling between wheat and the fungal pathogen Septoria tritici revealed by proteomics and phosphoproteomics
    • Yang, F., Melo-Braga, M. N., Larsen, M. R., Jørgensen, H. J., Palmisano, G., Battle through signaling between wheat and the fungal pathogen Septoria tritici revealed by proteomics and phosphoproteomics. Mol. Cell Proteomics 2013, 12, 2497-2508.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 2497-2508
    • Yang, F.1    Melo-Braga, M.N.2    Larsen, M.R.3    Jørgensen, H.J.4    Palmisano, G.5
  • 41
    • 58149387660 scopus 로고    scopus 로고
    • A comparative study of electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) versus SCX-IMAC-based methods for phosphopeptide isolation/enrichment
    • Gan, C. S., Guo, T., Zhang, H., Lim, S. K., Sze, S. K., A comparative study of electrostatic repulsion-hydrophilic interaction chromatography (ERLIC) versus SCX-IMAC-based methods for phosphopeptide isolation/enrichment. J. Proteome Res. 2008, 7, 4869-4877.
    • (2008) J. Proteome Res. , vol.7 , pp. 4869-4877
    • Gan, C.S.1    Guo, T.2    Zhang, H.3    Lim, S.K.4    Sze, S.K.5
  • 42
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • Vener, A. V., Harms, A., Sussman, M. R., Vierstra, R. D., Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana. J. Biol. Chem. 2001, 276, 6959-6966.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 43
    • 0037932398 scopus 로고    scopus 로고
    • Stable isotope labeling of phosphopeptides for multiparallel kinase target analysis and identification of phosphorylation sites
    • Glinski, M., Romeis, T., Witte, C. P., Wienkoop, S., Weckwerth, W., Stable isotope labeling of phosphopeptides for multiparallel kinase target analysis and identification of phosphorylation sites. Rapid Commun. Mass Spectrom. 2003, 17, 1579-1584.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1579-1584
    • Glinski, M.1    Romeis, T.2    Witte, C.P.3    Wienkoop, S.4    Weckwerth, W.5
  • 44
    • 27644593240 scopus 로고    scopus 로고
    • Differential multisite phosphorylation of the trehalose-6-phosphate synthase gene family in Arabidopsis thaliana: a mass spectrometry-based process for multiparallel peptide library phosphorylation analysis
    • Glinski, M., Weckwerth, W., Differential multisite phosphorylation of the trehalose-6-phosphate synthase gene family in Arabidopsis thaliana: a mass spectrometry-based process for multiparallel peptide library phosphorylation analysis. Mol. Cell Proteomics 2005, 4, 1614-1625.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1614-1625
    • Glinski, M.1    Weckwerth, W.2
  • 45
    • 25844479829 scopus 로고    scopus 로고
    • STN8 protein kinase in Arabidopsis thaliana is specific in phosphorylation of photosystem II core proteins
    • Vainonen, J. P., Hansson, M., Vener, A. V., STN8 protein kinase in Arabidopsis thaliana is specific in phosphorylation of photosystem II core proteins. J. Biol. Chem. 2005, 280, 33679-33686.
    • (2005) J. Biol. Chem. , vol.280 , pp. 33679-33686
    • Vainonen, J.P.1    Hansson, M.2    Vener, A.V.3
  • 46
    • 34547110110 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis
    • Benschop, J. J., Mohammed, S., O'Flaherty, M., Heck, A. J. et al., Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis. Mol. Cell Proteomics 2007, 6, 1198-1214.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1198-1214
    • Benschop, J.J.1    Mohammed, S.2    O'Flaherty, M.3    Heck, A.J.4
  • 48
    • 35648996970 scopus 로고    scopus 로고
    • Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis
    • Niittylä, T., Fuglsang, A. T., Palmgren, M. G., Frommer, W. B., Schulze, W. X., Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis. Mol. Cell Proteomics 2007, 6, 1711-1726.
    • (2007) Mol. Cell Proteomics , vol.6 , pp. 1711-1726
    • Niittylä, T.1    Fuglsang, A.T.2    Palmgren, M.G.3    Frommer, W.B.4    Schulze, W.X.5
  • 49
    • 46749099449 scopus 로고    scopus 로고
    • Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt stress
    • Prak, S., Hem, S., Boudet, J., Viennois, G. et al., Multiple phosphorylations in the C-terminal tail of plant plasma membrane aquaporins: role in subcellular trafficking of AtPIP2;1 in response to salt stress. Mol. Cell Proteomics 2008, 7, 1019-1030.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 1019-1030
    • Prak, S.1    Hem, S.2    Boudet, J.3    Viennois, G.4
  • 50
    • 51749100872 scopus 로고    scopus 로고
    • Absolute quantification of Medicago truncatula sucrose synthase isoforms and N-metabolism enzymes in symbiotic root nodules and the detection of novel nodule phosphoproteins by mass spectrometry
    • Wienkoop, S., Larrainzar, E., Glinski, M., González, E. M. et al., Absolute quantification of Medicago truncatula sucrose synthase isoforms and N-metabolism enzymes in symbiotic root nodules and the detection of novel nodule phosphoproteins by mass spectrometry. J. Exp. Bot. 2008, 59, 3307-3315.
    • (2008) J. Exp. Bot. , vol.59 , pp. 3307-3315
    • Wienkoop, S.1    Larrainzar, E.2    Glinski, M.3    González, E.M.4
  • 51
    • 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. et al., 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 2009, 9, 1646-1661.
    • (2009) Proteomics , vol.9 , pp. 1646-1661
    • Li, H.1    Wong, W.S.2    Zhu, L.3    Guo, H.W.4
  • 52
    • 65249173459 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics of tomato mounting a hypersensitive response reveals a swift suppression of photosynthetic activity and a differential role for hsp90 isoforms
    • Stulemeijer, I. J., Joosten, M. H., Jensen, O. N., Quantitative phosphoproteomics of tomato mounting a hypersensitive response reveals a swift suppression of photosynthetic activity and a differential role for hsp90 isoforms. J. Proteome Res. 2009, 8, 1168-1182.
    • (2009) J. Proteome Res. , vol.8 , pp. 1168-1182
    • Stulemeijer, I.J.1    Joosten, M.H.2    Jensen, O.N.3
  • 53
    • 77957682118 scopus 로고    scopus 로고
    • In planta changes in protein phosphorylation induced by the plant hormone abscisic acid
    • Kline, K. G., Barrett-Wilt, G. A., Sussman, M. R., In planta changes in protein phosphorylation induced by the plant hormone abscisic acid. Proc. Natl. Acad. Sci. USA 2010, 107, 15986-15991.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 15986-15991
    • Kline, K.G.1    Barrett-Wilt, G.A.2    Sussman, M.R.3
  • 54
    • 79961220621 scopus 로고    scopus 로고
    • Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF)
    • Reiland, S., Finazzi, G., Endler, A., Willig, A. et al., Comparative phosphoproteome profiling reveals a function of the STN8 kinase in fine-tuning of cyclic electron flow (CEF). Proc. Natl. Acad. Sci. USA 2011, 108, 12955-12960.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 12955-12960
    • Reiland, S.1    Finazzi, G.2    Endler, A.3    Willig, A.4
  • 55
    • 83455182145 scopus 로고    scopus 로고
    • Differential phosphorylation of ribosomal proteins in Arabidopsis thaliana plants during day and night
    • Turkina, M. V., Klang Årstrand, H., Vener, A. V., Differential phosphorylation of ribosomal proteins in Arabidopsis thaliana plants during day and night. PLoS One 2011, 6, e29307.
    • (2011) PLoS One , vol.6 , pp. e29307
    • Turkina, M.V.1    Klang Årstrand, H.2    Vener, A.V.3
  • 56
    • 84867168886 scopus 로고    scopus 로고
    • Phosphoproteome dynamics upon changes in plant water status reveal early events associated with rapid growth adjustment in maize leaves
    • Bonhomme, L., Valot, B., Tardieu, F., Zivy, M., Phosphoproteome dynamics upon changes in plant water status reveal early events associated with rapid growth adjustment in maize leaves. Mol. Cell Proteomics 2012, 11, 957-972.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 957-972
    • Bonhomme, L.1    Valot, B.2    Tardieu, F.3    Zivy, M.4
  • 57
    • 84861357104 scopus 로고    scopus 로고
    • The cyclic nucleotide cGMP is involved in plant hormone signalling and alters phosphorylation of Arabidopsis thaliana root proteins
    • Isner, J. C., Nühse, T., Maathuis, F. J., The cyclic nucleotide cGMP is involved in plant hormone signalling and alters phosphorylation of Arabidopsis thaliana root proteins. J. Exp. Bot. 2012, 63, 3199-3205.
    • (2012) J. Exp. Bot. , vol.63 , pp. 3199-3205
    • Isner, J.C.1    Nühse, T.2    Maathuis, F.J.3
  • 58
    • 84860576195 scopus 로고    scopus 로고
    • Quantitative phosphoproteome profiling of iron-deficient Arabidopsis roots
    • Lan, P., Li, W., Wen, T. N., Schmidt, W., Quantitative phosphoproteome profiling of iron-deficient Arabidopsis roots. Plant Physiol. 2012, 159, 403-417.
    • (2012) Plant Physiol. , vol.159 , pp. 403-417
    • Lan, P.1    Li, W.2    Wen, T.N.3    Schmidt, W.4
  • 59
    • 84867176464 scopus 로고    scopus 로고
    • Modulation of protein phosphorylation, N-glycosylation and Lys-acetylation in grape (Vitis vinifera) mesocarp and exocarp owing to Lobesia botrana infection
    • Melo-Braga, M. N., Verano-Braga, T., León, I. R., Antonacci, D. et al., Modulation of protein phosphorylation, N-glycosylation and Lys-acetylation in grape (Vitis vinifera) mesocarp and exocarp owing to Lobesia botrana infection. Mol. Cell Proteomics 2012, 11, 945-956.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 945-956
    • Melo-Braga, M.N.1    Verano-Braga, T.2    León, I.R.3    Antonacci, D.4
  • 60
    • 84869206637 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of soybean root hairs inoculated with Bradyrhizobium japonicum
    • Nguyen, T. H., Brechenmacher, L., Aldrich, J. T., Clauss, T. R. et al., Quantitative phosphoproteomic analysis of soybean root hairs inoculated with Bradyrhizobium japonicum. Mol. Cell Proteomics 2012, 11, 1140-1155.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 1140-1155
    • Nguyen, T.H.1    Brechenmacher, L.2    Aldrich, J.T.3    Clauss, T.R.4
  • 61
    • 84865778296 scopus 로고    scopus 로고
    • Rapid phosphoproteomic and transcriptomic changes in the rhizobia-legume symbiosis
    • Rose, C. M., Venkateshwaran, M., Volkening, J. D., Grimsrud, P. A. et al., Rapid phosphoproteomic and transcriptomic changes in the rhizobia-legume symbiosis. Mol. Cell Proteomics 2012, 11, 724-744.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 724-744
    • Rose, C.M.1    Venkateshwaran, M.2    Volkening, J.D.3    Grimsrud, P.A.4
  • 62
    • 84884688563 scopus 로고    scopus 로고
    • Parallel proteomic and phosphoproteomic analyses of successive stages of maize leaf development
    • Facette, M. R., Shen, Z., Björnsdóttir, F. R., Briggs, S. P., Smith, L. G., Parallel proteomic and phosphoproteomic analyses of successive stages of maize leaf development. Plant Cell 2013, 25, 2798-2812.
    • (2013) Plant Cell , vol.25 , pp. 2798-2812
    • Facette, M.R.1    Shen, Z.2    Björnsdóttir, F.R.3    Briggs, S.P.4    Smith, L.G.5
  • 63
    • 84874092435 scopus 로고    scopus 로고
    • Identification of novel in vivo MAP kinase substrates in Arabidopsis thaliana through use of tandem metal oxide affinity chromatography
    • Hoehenwarter, W., Thomas, M., Nukarinen, E., Egelhofer, V. et al., Identification of novel in vivo MAP kinase substrates in Arabidopsis thaliana through use of tandem metal oxide affinity chromatography. Mol. Cell Proteomics 2013, 12, 369-380.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 369-380
    • Hoehenwarter, W.1    Thomas, M.2    Nukarinen, E.3    Egelhofer, V.4
  • 64
    • 84876121995 scopus 로고    scopus 로고
    • Genetics and phosphoproteomics reveal a protein phosphorylation network in the abscisic acid signaling pathway in Arabidopsis thaliana
    • Rs8
    • Umezawa, T., Sugiyama, N., Takahashi, F., Anderson, J. C. et al., Genetics and phosphoproteomics reveal a protein phosphorylation network in the abscisic acid signaling pathway in Arabidopsis thaliana. Sci. Signal 2013, 6, rs8.
    • (2013) Sci. Signal , vol.6
    • Umezawa, T.1    Sugiyama, N.2    Takahashi, F.3    Anderson, J.C.4
  • 65
    • 84879732650 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics identifies SnRK2 protein kinase substrates and reveals the effectors of abscisic acid action
    • Wang, P., Xue, L., Batelli, G., Lee, S. et al., Quantitative phosphoproteomics identifies SnRK2 protein kinase substrates and reveals the effectors of abscisic acid action. Proc. Natl. Acad. Sci. USA 2013, 110, 11205-11210.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11205-11210
    • Wang, P.1    Xue, L.2    Batelli, G.3    Lee, S.4
  • 67
    • 84879707554 scopus 로고    scopus 로고
    • Quantitative measurement of phosphoproteome response to osmotic stress in Arabidopsis based on Library-Assisted eXtracted Ion Chromatogram (LAXIC)
    • Xue, L., Wang, P., Wang, L., Renzi, E. et al., Quantitative measurement of phosphoproteome response to osmotic stress in Arabidopsis based on Library-Assisted eXtracted Ion Chromatogram (LAXIC). Mol. Cell Proteomics 2013, 12, 2354-2369.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 2354-2369
    • Xue, L.1    Wang, P.2    Wang, L.3    Renzi, E.4
  • 68
    • 84890677480 scopus 로고    scopus 로고
    • Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins and putative substrates of constitutive triple response 1 kinase
    • Yang, Z., Guo, G., Zhang, M., Liu, C. Y. et al., Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins and putative substrates of constitutive triple response 1 kinase. Mol. Cell Proteomics 2013, 12, 3559-3582.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 3559-3582
    • Yang, Z.1    Guo, G.2    Zhang, M.3    Liu, C.Y.4
  • 69
    • 84877588949 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics after auxin-stimulated lateral root induction identifies an SNX1 protein phosphorylation site required for growth
    • Zhang, H., Zhou, H., Berke, L., Heck, A. J. et al., Quantitative phosphoproteomics after auxin-stimulated lateral root induction identifies an SNX1 protein phosphorylation site required for growth. Mol. Cell Proteomics 2013, 12, 1158-1169.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 1158-1169
    • Zhang, H.1    Zhou, H.2    Berke, L.3    Heck, A.J.4
  • 70
    • 84873243295 scopus 로고    scopus 로고
    • Functional phosphoproteomic analysis reveals that a serine-62-phosphorylated isoform of ethylene response factor110 is involved in Arabidopsis bolting
    • Zhu, L., Liu, D., Li, Y., Li, N., Functional phosphoproteomic analysis reveals that a serine-62-phosphorylated isoform of ethylene response factor110 is involved in Arabidopsis bolting. Plant Physiol. 2013, 161, 904-917.
    • (2013) Plant Physiol. , vol.161 , pp. 904-917
    • Zhu, L.1    Liu, D.2    Li, Y.3    Li, N.4
  • 71
    • 84907419348 scopus 로고    scopus 로고
    • Photosynthetic activity influences cellulose biosynthesis and phosphorylation of proteins involved therein in Arabidopsis leaves
    • Boex-Fontvieille, E., Davanture, M., Jossier, M., Zivy, M. et al., Photosynthetic activity influences cellulose biosynthesis and phosphorylation of proteins involved therein in Arabidopsis leaves. J. Exp. Bot. 2014, 65, 4997-5010.
    • (2014) J. Exp. Bot. , vol.65 , pp. 4997-5010
    • Boex-Fontvieille, E.1    Davanture, M.2    Jossier, M.3    Zivy, M.4
  • 72
    • 84903642270 scopus 로고    scopus 로고
    • Phosphoproteomic analyses reveal early signaling events in the osmotic stress response
    • E Stecker, K., Minkoff, B. B., Sussman, M. R., Phosphoproteomic analyses reveal early signaling events in the osmotic stress response. Plant Physiol. 2014, 165, 1171-1187.
    • (2014) Plant Physiol. , vol.165 , pp. 1171-1187
    • Stecker, K.B.1    Minkoff, B.B.2    Sussman, M.R.3
  • 73
    • 84856661312 scopus 로고    scopus 로고
    • Comparative phosphoproteomic analysis of microsomal fractions of Arabidopsis thaliana and Oryza sativa subjected to high salinity
    • Chang, I.F., Hsu, J.L., Hsu, P.H., Sheng, W.A. et al., Comparative phosphoproteomic analysis of microsomal fractions of Arabidopsis thaliana and Oryza sativa subjected to high salinity. Plant Sci. 2012, 185, 131-142.
    • (2012) Plant Sci. , vol.185 , pp. 131-142
    • Chang, I.F.1    Hsu, J.L.2    Hsu, P.H.3    Sheng, W.A.4
  • 74
    • 84899575143 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics analysis of nitric oxide-responsive phosphoproteins in cotton leaf
    • Fan, S., Meng, Y., Song, M., Pang, C. et al., Quantitative phosphoproteomics analysis of nitric oxide-responsive phosphoproteins in cotton leaf. PLoS One 2014, 9, e94261.
    • (2014) PLoS One , vol.9 , pp. e94261
    • Fan, S.1    Meng, Y.2    Song, M.3    Pang, C.4
  • 75
    • 84896781265 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the role of protein phosphorylation in rice embryos during early stages of germination
    • Han, C., Yang, P., Sakata, K., Komatsu, S., Quantitative proteomics reveals the role of protein phosphorylation in rice embryos during early stages of germination. J. Proteome Res. 2014, 13, 1766-1782.
    • (2014) J. Proteome Res. , vol.13 , pp. 1766-1782
    • Han, C.1    Yang, P.2    Sakata, K.3    Komatsu, S.4
  • 76
    • 84904767185 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic profiling of fiber differentiation and initiation in a fiberless mutant of cotton
    • Ma, Q., Wu, M., Pei, W., Li, H. et al., Quantitative phosphoproteomic profiling of fiber differentiation and initiation in a fiberless mutant of cotton. BMC Genomics 2014, 15, 466.
    • (2014) BMC Genomics , vol.15 , pp. 466
    • Ma, Q.1    Wu, M.2    Pei, W.3    Li, H.4
  • 77
    • 84905443201 scopus 로고    scopus 로고
    • Phosphoproteome analysis reveals new drought response and defense mechanisms of seedling leaves in bread wheat (Triticum aestivumL.)
    • Zhang, M., Lv, D., Ge, P., Bian, Y. et al., Phosphoproteome analysis reveals new drought response and defense mechanisms of seedling leaves in bread wheat (Triticum aestivumL.). J. Proteomics 2014, 109C, 290-308.
    • (2014) J. Proteomics , vol.109 C , pp. 290-308
    • Zhang, M.1    Lv, D.2    Ge, P.3    Bian, Y.4
  • 78
    • 84907820818 scopus 로고    scopus 로고
    • Comparative phosphoproteome analysis of the developing grains in bread wheat (Triticum aestivum L.) under well-watered and water-deficit conditions
    • Zhang, M., Ma, C.Y., Lv, D.W., Zhen, S.M. et al., Comparative phosphoproteome analysis of the developing grains in bread wheat (Triticum aestivum L.) under well-watered and water-deficit conditions. J. Proteome Res. 2014, 13, 4281-4297.
    • (2014) J. Proteome Res. , vol.13 , pp. 4281-4297
    • Zhang, M.1    Ma, C.Y.2    Lv, D.W.3    Zhen, S.M.4
  • 79
    • 84855932755 scopus 로고    scopus 로고
    • Advances in quantitative phosphoproteomics
    • Nilsson, C. L., Advances in quantitative phosphoproteomics. Anal. Chem. 2012, 84, 735-746.
    • (2012) Anal. Chem. , vol.84 , pp. 735-746
    • Nilsson, C.L.1
  • 80
    • 28644448658 scopus 로고    scopus 로고
    • Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry
    • Gruhler, A., Schulze, W. X., Matthiesen, R., Mann, M., Jensen, O. N., Stable isotope labeling of Arabidopsis thaliana cells and quantitative proteomics by mass spectrometry. Mol. Cell Proteomics 2005, 4, 1697-1709.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 1697-1709
    • Gruhler, A.1    Schulze, W.X.2    Matthiesen, R.3    Mann, M.4    Jensen, O.N.5
  • 81
    • 79959849574 scopus 로고    scopus 로고
    • Extending SILAC to proteomics of plant cell lines
    • Schütz, 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
    • Schütz, W.1    Hausmann, N.2    Krug, K.3    Hampp, R.4    Macek, B.5
  • 82
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study
    • Bindschedler, L.V., 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.V.1    Palmblad, M.2    Cramer, R.3
  • 83
    • 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., Goshe, M.B., SILIP: a novel stable isotope labeling method for in planta quantitative proteomic analysis. Plant J. 2008, 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
  • 84
    • 77953595441 scopus 로고    scopus 로고
    • Undesirable charge-enhancement of isobaric tagged phosphopeptides leads to reduced identification efficiency
    • Thingholm, T. E., Palmisano, G., Kjeldsen, F., Larsen, M. R., Undesirable charge-enhancement of isobaric tagged phosphopeptides leads to reduced identification efficiency. J Proteome Res. 2010, 9, 4045-4052.
    • (2010) J Proteome Res. , vol.9 , pp. 4045-4052
    • Thingholm, T.E.1    Palmisano, G.2    Kjeldsen, F.3    Larsen, M.R.4
  • 85
    • 79961013401 scopus 로고    scopus 로고
    • Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes
    • M111009654
    • Wu, R., Dephoure, N., Haas, W., Huttlin, E. L. et al., Correct interpretation of comprehensive phosphorylation dynamics requires normalization by protein expression changes. Mol. Cell Proteomics 2011, 10, M111.009654.
    • (2011) Mol. Cell Proteomics , vol.10
    • Wu, R.1    Dephoure, N.2    Haas, W.3    Huttlin, E.L.4
  • 86
    • 79960979428 scopus 로고    scopus 로고
    • A large-scale method to measure absolute protein phosphorylation stoichiometries
    • Wu, R., Haas, W., Dephoure, N., Huttlin, E. L. et al., A large-scale method to measure absolute protein phosphorylation stoichiometries. Nat. Methods 2011, 8, 677-683.
    • (2011) Nat. Methods , vol.8 , pp. 677-683
    • Wu, R.1    Haas, W.2    Dephoure, N.3    Huttlin, E.L.4
  • 87
    • 55849093586 scopus 로고    scopus 로고
    • Triplex protein quantification based on stable isotope labeling by peptide dimethylation applied to cell and tissue lysates
    • Boersema, P. J., Aye, T. T., van Veen, T. A., Heck, A. J., Mohammed, S., Triplex protein quantification based on stable isotope labeling by peptide dimethylation applied to cell and tissue lysates. Proteomics 2008, 8, 4624-4632.
    • (2008) Proteomics , vol.8 , pp. 4624-4632
    • Boersema, P.J.1    Aye, T.T.2    van Veen, T.A.3    Heck, A.J.4    Mohammed, S.5
  • 88
    • 77950398579 scopus 로고    scopus 로고
    • N,N-dimethyl leucines as novel isobaric tandem mass tags for quantitative proteomics and peptidomics
    • Xiang, F., Ye, H., Chen, R., Fu, Q., Li, L., N, N-dimethyl leucines as novel isobaric tandem mass tags for quantitative proteomics and peptidomics. Anal. Chem. 2010, 82, 2817-2825.
    • (2010) Anal. Chem. , vol.82 , pp. 2817-2825
    • Xiang, F.1    Ye, H.2    Chen, R.3    Fu, Q.4    Li, L.5
  • 89
    • 85027926759 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics and peptidomics for systems biology and biomarker discovery
    • Cunningham, R., Ma, D., Li, L., Mass spectrometry-based proteomics and peptidomics for systems biology and biomarker discovery. Front. Biol. (Beijing) 2012, 7, 313-335.
    • (2012) Front. Biol. (Beijing) , vol.7 , pp. 313-335
    • Cunningham, R.1    Ma, D.2    Li, L.3
  • 90
    • 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, 535-553.
    • (2011) Proteomics , vol.11 , pp. 535-553
    • Neilson, K.A.1    Ali, N.A.2    Muralidharan, S.3    Mirzaei, M.4
  • 91
    • 84857950653 scopus 로고    scopus 로고
    • The functional network of the Arabidopsis plastoglobule proteome based on quantitative proteomics and genome-wide coexpression analysis
    • Lundquist, P. K., Poliakov, A., Bhuiyan, N. H., Zybailov, B. et al., The functional network of the Arabidopsis plastoglobule proteome based on quantitative proteomics and genome-wide coexpression analysis. Plant Physiol. 2012, 158, 1172-1192.
    • (2012) Plant Physiol. , vol.158 , pp. 1172-1192
    • Lundquist, P.K.1    Poliakov, A.2    Bhuiyan, N.H.3    Zybailov, B.4
  • 92
    • 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., Gygi, S. P., Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. USA 2003, 100, 6940-6945.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 93
    • 33646251130 scopus 로고    scopus 로고
    • Relative and absolute quantitative shotgun proteomics: targeting low-abundance proteins in Arabidopsis thaliana
    • Wienkoop, S., Weckwerth, W., Relative and absolute quantitative shotgun proteomics: targeting low-abundance proteins in Arabidopsis thaliana. J. Exp. Bot. 2006, 57, 1529-1535.
    • (2006) J. Exp. Bot. , vol.57 , pp. 1529-1535
    • Wienkoop, S.1    Weckwerth, W.2
  • 94
    • 84864805482 scopus 로고    scopus 로고
    • Absolute quantitation of isoforms of post-translationally modified proteins in transgenic organism
    • Li, Y., Shu, Y., Peng, C., Zhu, L. et al., Absolute quantitation of isoforms of post-translationally modified proteins in transgenic organism. Mol. Cell Proteomics 2012, 11, 272-285.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 272-285
    • Li, Y.1    Shu, Y.2    Peng, C.3    Zhu, L.4
  • 95
    • 67649213067 scopus 로고    scopus 로고
    • Phosphopeptide fragmentation and analysis by mass spectrometry
    • Boersema, P. J., Mohammed, S., Heck, A. J., Phosphopeptide fragmentation and analysis by mass spectrometry. J. Mass Spectrom. 2009, 44, 861-878.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 861-878
    • Boersema, P.J.1    Mohammed, S.2    Heck, A.J.3
  • 96
    • 61849182590 scopus 로고    scopus 로고
    • Comparison of MS(2)-only, MSA, and MS(2)/MS(3) methodologies for phosphopeptide identification
    • Ulintz, P. J., Yocum, A. K., Bodenmiller, B., Aebersold, R. et al., Comparison of MS(2)-only, MSA, and MS(2)/MS(3) methodologies for phosphopeptide identification. J. Proteome Res. 2009, 8, 887-899.
    • (2009) J. Proteome Res. , vol.8 , pp. 887-899
    • Ulintz, P.J.1    Yocum, A.K.2    Bodenmiller, B.3    Aebersold, R.4
  • 97
    • 84898860672 scopus 로고    scopus 로고
    • Confident and sensitive phosphoproteomics using combinations of collision induced dissociation and electron transfer dissociation
    • Collins, M. O., Wright, J. C., Jones, M., Rayner, J. C., Choudhary, J. S., Confident and sensitive phosphoproteomics using combinations of collision induced dissociation and electron transfer dissociation. J. Proteomics 2014, 103, 1-14.
    • (2014) J. Proteomics , vol.103 , pp. 1-14
    • Collins, M.O.1    Wright, J.C.2    Jones, M.3    Rayner, J.C.4    Choudhary, J.S.5
  • 98
    • 65549102501 scopus 로고    scopus 로고
    • Challenges and strategies for targeted phosphorylation site identification and quantification using mass spectrometry analysis
    • Blackburn, K., Goshe, M. B., Challenges and strategies for targeted phosphorylation site identification and quantification using mass spectrometry analysis. Brief Funct. Genomic Proteomic 2009, 8, 90-103.
    • (2009) Brief Funct. Genomic Proteomic , vol.8 , pp. 90-103
    • Blackburn, K.1    Goshe, M.B.2
  • 99
    • 84870656540 scopus 로고    scopus 로고
    • Targeted proteomic quantification on quadrupole-orbitrap mass spectrometer
    • Gallien, S., Duriez, E., Crone, C., Kellmann, M. et al., Targeted proteomic quantification on quadrupole-orbitrap mass spectrometer. Mol. Cell Proteomics 2012, 11, 1709-1723.
    • (2012) Mol. Cell Proteomics , vol.11 , pp. 1709-1723
    • Gallien, S.1    Duriez, E.2    Crone, C.3    Kellmann, M.4
  • 100
    • 48549096822 scopus 로고    scopus 로고
    • Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling
    • Wang, X., Kota, U., He, K., Blackburn, K. et al., Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling. Dev. Cell 2008, 15, 220-235.
    • (2008) Dev. Cell , vol.15 , pp. 220-235
    • Wang, X.1    Kota, U.2    He, K.3    Blackburn, K.4
  • 101
    • 84908073840 scopus 로고    scopus 로고
    • Probing phosphorylation-dependent protein interactions within functional domains of histone deacetylase 5 (HDAC5)
    • Guise, A. J., Mathias, R. A., Rowland, E. A., Yu, F., Cristea, I. M., Probing phosphorylation-dependent protein interactions within functional domains of histone deacetylase 5 (HDAC5). Proteomics 2014, 14, 2156-2166.
    • (2014) Proteomics , vol.14 , pp. 2156-2166
    • Guise, A.J.1    Mathias, R.A.2    Rowland, E.A.3    Yu, F.4    Cristea, I.M.5
  • 102
    • 84902031172 scopus 로고    scopus 로고
    • Evolution and functional cross-talk of protein post-translational modifications
    • Beltrao, P., Bork, P., Krogan, N. J., van Noort, V., Evolution and functional cross-talk of protein post-translational modifications. Mol. Syst. Biol. 2013, 9, 714.
    • (2013) Mol. Syst. Biol. , vol.9 , pp. 714
    • Beltrao, P.1    Bork, P.2    Krogan, N.J.3    van Noort, V.4
  • 103
    • 84879613791 scopus 로고    scopus 로고
    • Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation
    • Swaney, D. L., Beltrao, P., Starita, L., Guo, A. et al., Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nat. Methods 2013, 10, 676-682.
    • (2013) Nat. Methods , vol.10 , pp. 676-682
    • Swaney, D.L.1    Beltrao, P.2    Starita, L.3    Guo, A.4
  • 104
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary, C., Mann, M., Decoding signalling networks by mass spectrometry-based proteomics. Nat. Rev. Mol. Cell Biol. 2010, 11, 427-439.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 105
    • 82555170600 scopus 로고    scopus 로고
    • Bioinformatic analysis and post-translational modification crosstalk prediction of lysine acetylation
    • Lu, Z., Cheng, Z., Zhao, Y., Volchenboum, S. L., Bioinformatic analysis and post-translational modification crosstalk prediction of lysine acetylation. PLoS One 2011, 6, e28228.
    • (2011) PLoS One , vol.6 , pp. e28228
    • Lu, Z.1    Cheng, Z.2    Zhao, Y.3    Volchenboum, S.L.4
  • 106
    • 84874957680 scopus 로고    scopus 로고
    • PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins
    • Minguez, P., Letunic, I., Parca, L., Bork, P., PTMcode: a database of known and predicted functional associations between post-translational modifications in proteins. Nucleic Acids Res. 2013, 41, D306-311.
    • (2013) Nucleic Acids Res. , vol.41 , pp. D306-D311
    • Minguez, P.1    Letunic, I.2    Parca, L.3    Bork, P.4
  • 107
    • 84875991401 scopus 로고    scopus 로고
    • Dual coordination of post translational modifications in human protein networks
    • Woodsmith, J., Kamburov, A., Stelzl, U., Dual coordination of post translational modifications in human protein networks. PLoS Comput. Biol. 2013, 9, e1002933.
    • (2013) PLoS Comput. Biol. , vol.9 , pp. e1002933
    • Woodsmith, J.1    Kamburov, A.2    Stelzl, U.3
  • 108
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro, R. G., Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002, 12, 43R-56R.
    • (2002) Glycobiology , vol.12 , pp. 43R-56R
    • Spiro, R.G.1
  • 109
    • 84901004695 scopus 로고    scopus 로고
    • Sweet and sour: the impact of differential glycosylation in cancer cells undergoing epithelial-mesenchymal transition
    • Freire-de-Lima, L., Sweet and sour: the impact of differential glycosylation in cancer cells undergoing epithelial-mesenchymal transition. Front Oncol. 2014, 4, 59.
    • (2014) Front Oncol. , vol.4 , pp. 59
    • Freire-de-Lima, L.1
  • 110
    • 79959381299 scopus 로고    scopus 로고
    • Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
    • Hart, G. W., Slawson, C., Ramirez-Correa, G., Lagerlof, O., Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease. Annu. Rev. Biochem. 2011, 80, 825-858.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 825-858
    • Hart, G.W.1    Slawson, C.2    Ramirez-Correa, G.3    Lagerlof, O.4
  • 111
    • 0345277743 scopus 로고    scopus 로고
    • Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: a new paradigm for metabolic control of signal transduction and transcription
    • Kamemura, K., Hart, G. W., Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: a new paradigm for metabolic control of signal transduction and transcription. Prog. Nucleic Acid Res. Mol. Biol. 2003, 73, 107-136.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.73 , pp. 107-136
    • Kamemura, K.1    Hart, G.W.2
  • 112
    • 84873887641 scopus 로고    scopus 로고
    • Human 14-3-3 paralogs differences uncovered by cross-talk of phosphorylation and lysine acetylation
    • Uhart, M., Bustos, D. M., Human 14-3-3 paralogs differences uncovered by cross-talk of phosphorylation and lysine acetylation. PLoS One 2013, 8, e55703.
    • (2013) PLoS One , vol.8 , pp. e55703
    • Uhart, M.1    Bustos, D.M.2
  • 113
    • 84885339230 scopus 로고    scopus 로고
    • Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation
    • Rao, R., Xu, D., Thelen, J. J., Miernyk, J. A., Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation. BMC Bioinformatics 2013, 14(Suppl 14), S14.
    • (2013) BMC Bioinformatics , vol.14 , pp. S14
    • Rao, R.1    Xu, D.2    Thelen, J.J.3    Miernyk, J.A.4
  • 114
    • 84879002623 scopus 로고    scopus 로고
    • Protein SUMOylation and plant abiotic stress signaling: in silico case study of rice RLKs, heat-shock and Ca(2+)-binding proteins
    • Raorane, M. L., Mutte, S. K., Varadarajan, A. R., Pabuayon, I. M., Kohli, A., Protein SUMOylation and plant abiotic stress signaling: in silico case study of rice RLKs, heat-shock and Ca(2+)-binding proteins. Plant Cell Rep. 2013, 32, 1053-1065.
    • (2013) Plant Cell Rep. , vol.32 , pp. 1053-1065
    • Raorane, M.L.1    Mutte, S.K.2    Varadarajan, A.R.3    Pabuayon, I.M.4    Kohli, A.5
  • 115
    • 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. et al., PhosPhAt: a database of phosphorylation sites in Arabidopsis thaliana and a plant-specific phosphorylation site predictor. Nucleic Acids Res. 2008, 36, D1015-1021.
    • (2008) Nucleic Acids Res. , vol.36 , pp. D1015-D1021
    • Heazlewood, J.L.1    Durek, P.2    Hummel, J.3    Selbig, J.4
  • 116
    • 75549090366 scopus 로고    scopus 로고
    • PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update
    • Durek, P., Schmidt, R., Heazlewood, J. L., Jones, A. et al., PhosPhAt: the Arabidopsis thaliana phosphorylation site database. An update. Nucleic Acids Res. 2010, 38, D828-834.
    • (2010) Nucleic Acids Res. , vol.38 , pp. D828-D834
    • Durek, P.1    Schmidt, R.2    Heazlewood, J.L.3    Jones, A.4
  • 117
    • 84891771339 scopus 로고    scopus 로고
    • 3DB 3.0: from plant phosphorylation sites to protein networks
    • 3DB 3.0: from plant phosphorylation sites to protein networks. Nucleic Acids Res. 2014, 42, D1206-1213.
    • (2014) Nucleic Acids Res. , vol.42 , pp. D1206-D1213
    • Yao, Q.1    Ge, H.2    Wu, S.3    Zhang, N.4
  • 118
    • 84886599885 scopus 로고    scopus 로고
    • Predicting and analyzing protein phosphorylation sites in plants using musite
    • Yao, Q., Gao, J., Bollinger, C., Thelen, J. J., Xu, D., Predicting and analyzing protein phosphorylation sites in plants using musite. Front Plant Sci. 2012, 3, 186.
    • (2012) Front Plant Sci. , vol.3 , pp. 186
    • Yao, Q.1    Gao, J.2    Bollinger, C.3    Thelen, J.J.4    Xu, D.5
  • 119
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., Gygi, S.P., An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 2005, 23, 1391-1398.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 121
    • 84873736627 scopus 로고    scopus 로고
    • Medicago PhosphoProtein Database: a repository for Medicago truncatula phosphoprotein data
    • Rose, C. M., Venkateshwaran, M., Grimsrud, P. A., Westphall, M. S. et al., Medicago PhosphoProtein Database: a repository for Medicago truncatula phosphoprotein data. Front Plant Sci. 2012, 3, 122.
    • (2012) Front Plant Sci. , vol.3 , pp. 122
    • Rose, C.M.1    Venkateshwaran, M.2    Grimsrud, P.A.3    Westphall, M.S.4
  • 122
    • 79952531916 scopus 로고    scopus 로고
    • pep2pro: a new tool for comprehensive proteome data analysis to reveal information about organ-specific proteomes in Arabidopsis thaliana
    • Baerenfaller, K., Hirsch-Hoffmann, M., Svozil, J., Hull, R. et al., pep2pro: a new tool for comprehensive proteome data analysis to reveal information about organ-specific proteomes in Arabidopsis thaliana. Integr. Biol. (Camb) 2011, 3, 225-237.
    • (2011) Integr. Biol. (Camb) , vol.3 , pp. 225-237
    • Baerenfaller, K.1    Hirsch-Hoffmann, M.2    Svozil, J.3    Hull, R.4
  • 123
    • 84901024935 scopus 로고    scopus 로고
    • MASCP gator: an overview of the Arabidopsis proteomic aggregation portal
    • Mann, G. W., Calley, P. C., Joshi, H. J., Heazlewood, J. L., MASCP gator: an overview of the Arabidopsis proteomic aggregation portal. Front Plant Sci. 2013, 4, 411.
    • (2013) Front Plant Sci. , vol.4 , pp. 411
    • Mann, G.W.1    Calley, P.C.2    Joshi, H.J.3    Heazlewood, J.L.4
  • 124
    • 84904988782 scopus 로고    scopus 로고
    • Meta-analysis of Arabidopsis thaliana phosphoproteomics data reveals compartmentalization of phosphorylation motifs
    • van Wijk, K.J., Friso, G., Walther, D., Schulze, W.X., Meta-analysis of Arabidopsis thaliana phosphoproteomics data reveals compartmentalization of phosphorylation motifs. Plant Cell 2014, 26, 2367-2389.
    • (2014) Plant Cell , vol.26 , pp. 2367-2389
    • van Wijk, K.J.1    Friso, G.2    Walther, D.3    Schulze, W.X.4
  • 125
    • 84900869581 scopus 로고    scopus 로고
    • Quantitation, networking, and function of protein phosphorylation in plant cell
    • Zhu, L., Li, N., Quantitation, networking, and function of protein phosphorylation in plant cell. Front Plant Sci. 2013, 3, 302.
    • (2013) Front Plant Sci. , vol.3 , pp. 302
    • Zhu, L.1    Li, N.2
  • 126
    • 84897407251 scopus 로고    scopus 로고
    • Identification of multiple phosphorylation sites on maize endosperm starch branching enzyme IIb, a key enzyme in amylopectin biosynthesis
    • Makhmoudova, A., Williams, D., Brewer, D., Massey, S. et al., Identification of multiple phosphorylation sites on maize endosperm starch branching enzyme IIb, a key enzyme in amylopectin biosynthesis. J. Biol. Chem. 2014, 289, 9233-9246.
    • (2014) J. Biol. Chem. , vol.289 , pp. 9233-9246
    • Makhmoudova, A.1    Williams, D.2    Brewer, D.3    Massey, S.4


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