메뉴 건너뛰기




Volumn 355, Issue 1, 2007, Pages 89-96

Plant protein phosphorylation monitored by capillary liquid chromatography-element mass spectrometry

Author keywords

Algae; Arabidopsis thaliana; Chlamydomonas reinhardtii; Element mass spectrometry; Enrichment; HPLC; ICP MS; MOAC; Phosphoprotein; Phosphorus; Phosphorylation; Plant; Protein; Proteomics; Sulfur

Indexed keywords

PHOSPHOPROTEIN; PHOSPHORUS; SULFUR; VEGETABLE PROTEIN;

EID: 33847234310     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.01.108     Document Type: Article
Times cited : (28)

References (37)
  • 1
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation-a 25 year update
    • Cohen P. The regulation of protein function by multisite phosphorylation-a 25 year update. Trends Biochem. Sci. 25 (2000) 596-601
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 3
    • 33748573639 scopus 로고    scopus 로고
    • Charging it up: global analysis of protein phosphorylation
    • Ptacek J., and Snyder M. Charging it up: global analysis of protein phosphorylation. Trends Genet. 22 (2006) 545-554
    • (2006) Trends Genet. , vol.22 , pp. 545-554
    • Ptacek, J.1    Snyder, M.2
  • 4
    • 3042634240 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors in cancer therapy
    • Madhusudan S., and Ganesan T.S. Tyrosine kinase inhibitors in cancer therapy. Clin. Biochem. 37 (2004) 618-635
    • (2004) Clin. Biochem. , vol.37 , pp. 618-635
    • Madhusudan, S.1    Ganesan, T.S.2
  • 5
    • 1342324700 scopus 로고    scopus 로고
    • Characterization of phosphorus content of biological samples by ICP-DRC-MS: potential tool for cancer research
    • Bandura D.R., Ornatsky O.I., and Liao L. Characterization of phosphorus content of biological samples by ICP-DRC-MS: potential tool for cancer research. J. Anal. At. Spectrom. 19 (2004) 96-100
    • (2004) J. Anal. At. Spectrom. , vol.19 , pp. 96-100
    • Bandura, D.R.1    Ornatsky, O.I.2    Liao, L.3
  • 6
    • 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., and Vierstra R.D. Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana. J. Biol. Chem. 276 (2001) 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
  • 7
    • 0037458032 scopus 로고    scopus 로고
    • A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
    • Carlberg I., Hansson M., Kieselbach T., Schroder W.P., Andersson B., and Vener A.V. A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes. Proc. Natl. Acad. Sci. USA 100 (2003) 757-762
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 757-762
    • Carlberg, I.1    Hansson, M.2    Kieselbach, T.3    Schroder, W.P.4    Andersson, B.5    Vener, A.V.6
  • 8
  • 9
    • 15944373459 scopus 로고    scopus 로고
    • Mass spectrometric contributions to the practice of phosphorylation site mapping through 2003-A literature review
    • Loyet K.M., Stults J.T., and Arnott D. Mass spectrometric contributions to the practice of phosphorylation site mapping through 2003-A literature review. Mol. Cell. Proteomics 4 (2005) 235-242
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 235-242
    • Loyet, K.M.1    Stults, J.T.2    Arnott, D.3
  • 10
    • 28444487185 scopus 로고    scopus 로고
    • Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC)
    • Wolschin F., Wienkoop S., and Weckwerth W. Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC). Proteomics 5 (2005) 4389-4397
    • (2005) Proteomics , vol.5 , pp. 4389-4397
    • Wolschin, F.1    Wienkoop, S.2    Weckwerth, W.3
  • 11
    • 84890499160 scopus 로고    scopus 로고
    • Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo protein phosphorylation sites
    • Wolschin F., and Weckwerth W. Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo protein phosphorylation sites. Plant Methods 1 (2005) 9
    • (2005) Plant Methods , vol.1 , pp. 9
    • Wolschin, F.1    Weckwerth, W.2
  • 12
    • 0022541790 scopus 로고
    • Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography
    • Andersson L., and Porath J. Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. Anal. Biochem. 154 (1986) 250-254
    • (1986) Anal. Biochem. , vol.154 , pp. 250-254
    • Andersson, L.1    Porath, J.2
  • 13
    • 1842427490 scopus 로고    scopus 로고
    • Chemo-affinity of titania for the column-switching HPLC analysis of phosphopeptides
    • Sano A., and Nakamura H. Chemo-affinity of titania for the column-switching HPLC analysis of phosphopeptides. Anal. Sci. 20 (2004) 565-566
    • (2004) Anal. Sci. , vol.20 , pp. 565-566
    • Sano, A.1    Nakamura, H.2
  • 14
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-nanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse M.W.H., Uitto P.M., Hilhorst M.J., Ooms B., and Heck A.J.R. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-nanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 76 (2004) 3935-3943
    • (2004) Anal. Chem. , vol.76 , pp. 3935-3943
    • Pinkse, M.W.H.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.R.5
  • 15
    • 13844299238 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by mass spectrometry
    • Garcia B.A., Shabanowitz J., and Hunt D.F. Analysis of protein phosphorylation by mass spectrometry. Methods 35 (2005) 256-264
    • (2005) Methods , vol.35 , pp. 256-264
    • Garcia, B.A.1    Shabanowitz, J.2    Hunt, D.F.3
  • 16
    • 20644448582 scopus 로고    scopus 로고
    • Iodoacetamide-alkylated methionine can mimic neutral loss of phosphoric acid from phosphopeptides as exemplified by nano-electrospray ionization quadrupole time-of-flight parent ion scanning
    • Krüger R., Hung C.-W., Edelson-Averbukh M., and Lehmann W.D. Iodoacetamide-alkylated methionine can mimic neutral loss of phosphoric acid from phosphopeptides as exemplified by nano-electrospray ionization quadrupole time-of-flight parent ion scanning. Rapid Commun. Mass Spectrom. 19 (2005) 1709-1716
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 1709-1716
    • Krüger, R.1    Hung, C.-W.2    Edelson-Averbukh, M.3    Lehmann, W.D.4
  • 17
    • 33747519970 scopus 로고    scopus 로고
    • Methionine oxidation in peptides-a source for false positive phosphopeptide identification in neutral loss driven MS3
    • Wolschin F., and Weckwerth W. Methionine oxidation in peptides-a source for false positive phosphopeptide identification in neutral loss driven MS3. Rapid Commun. Mass Spectrom. 20 (2006) 2516-2518
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 2516-2518
    • Wolschin, F.1    Weckwerth, W.2
  • 18
    • 0035478709 scopus 로고    scopus 로고
    • Analysis of phosphorylated proteins and peptides by mass spectrometry
    • McLachlin D.T., and Chait B.T. Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr. Opin. Chem. Biol. 5 (2001) 591-602
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 591-602
    • McLachlin, D.T.1    Chait, B.T.2
  • 19
    • 0037417791 scopus 로고    scopus 로고
    • Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labelling and mass spectrometry
    • Bonenfant D., Schmelzle T., Jacinto E., Crespo J.L., Mini T., Hall M.N., and Jenoe M.P. Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labelling and mass spectrometry. Proc. Nat. Acad. Sci. USA 100 (2003) 880-885
    • (2003) Proc. Nat. Acad. Sci. USA , vol.100 , pp. 880-885
    • Bonenfant, D.1    Schmelzle, T.2    Jacinto, E.3    Crespo, J.L.4    Mini, T.5    Hall, M.N.6    Jenoe, M.P.7
  • 20
    • 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. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc. Natl. Acad. Sci. USA 100 (2003) 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
  • 22
    • 15344341157 scopus 로고    scopus 로고
    • Stable isotope-free relative and absolute quantitation of protein phosphorylation stoichiometry by mass spectrometry
    • Steen H., Jebanathirajah J.A., Springer M., and Kirschner M.W. Stable isotope-free relative and absolute quantitation of protein phosphorylation stoichiometry by mass spectrometry. Proc. Natl. Acad. Sci. USA 102 (2005) 3948-3953
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3948-3953
    • Steen, H.1    Jebanathirajah, J.A.2    Springer, M.3    Kirschner, M.W.4
  • 23
    • 0035173651 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation by capillary liquid chromatography coupled to element plasma mass spectrometry with 31P detection and to electrospray mass spectrometry
    • Wind M., Edler M., Jakubowski N., Linscheid M., Wesch H., and Lehmann W.D. Analysis of protein phosphorylation by capillary liquid chromatography coupled to element plasma mass spectrometry with 31P detection and to electrospray mass spectrometry. Anal. Chem. 73 (2001) 29-35
    • (2001) Anal. Chem. , vol.73 , pp. 29-35
    • Wind, M.1    Edler, M.2    Jakubowski, N.3    Linscheid, M.4    Wesch, H.5    Lehmann, W.D.6
  • 24
    • 0035387929 scopus 로고    scopus 로고
    • Protein phosphorylation degree: determination by capillary liquid chromatography and inductively coupled plasma mass spectrometry
    • Wind M., Wesch H., and Lehmann W.D. Protein phosphorylation degree: determination by capillary liquid chromatography and inductively coupled plasma mass spectrometry. Anal. Chem. 73 (2001) 3006-3020
    • (2001) Anal. Chem. , vol.73 , pp. 3006-3020
    • Wind, M.1    Wesch, H.2    Lehmann, W.D.3
  • 25
    • 0036857507 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in the polo-like kinases Plx1 and Plk1 by a novel strategy based on element and electrospray high resolution mass spectrometry
    • Wind M., Kelm O., Nigg E.A., and Lehmann W.D. Identification of phosphorylation sites in the polo-like kinases Plx1 and Plk1 by a novel strategy based on element and electrospray high resolution mass spectrometry. Proteomics 2 (2002) 1516-1523
    • (2002) Proteomics , vol.2 , pp. 1516-1523
    • Wind, M.1    Kelm, O.2    Nigg, E.A.3    Lehmann, W.D.4
  • 26
    • 0242501532 scopus 로고    scopus 로고
    • Stable isotope phospho-profiling of fibrinogen and fetuin subunits by element mass spectrometry coupled to capillary liquid chromatography
    • Wind M., Gosenca D., Kübler D., and Lehmann W.D. Stable isotope phospho-profiling of fibrinogen and fetuin subunits by element mass spectrometry coupled to capillary liquid chromatography. Anal. Biochem. 317 (2003) 26-33
    • (2003) Anal. Biochem. , vol.317 , pp. 26-33
    • Wind, M.1    Gosenca, D.2    Kübler, D.3    Lehmann, W.D.4
  • 27
    • 33645212811 scopus 로고    scopus 로고
    • Protein and proteome phosphorylation stoichiometry analysis by element mass spectrometry
    • Krüger R., Kübler D., Pallissé R., Burkovski A., and Lehmann W.D. Protein and proteome phosphorylation stoichiometry analysis by element mass spectrometry. Anal. Chem. 78 (2006) 1987-1994
    • (2006) Anal. Chem. , vol.78 , pp. 1987-1994
    • Krüger, R.1    Kübler, D.2    Pallissé, R.3    Burkovski, A.4    Lehmann, W.D.5
  • 29
    • 84980140250 scopus 로고
    • Croissance et synthese des proteines de suspensions cellulaires de Tabac sensibles à la kinétine (Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco)
    • Jouanneau J.P., and Peaud-Lenoel C. Croissance et synthese des proteines de suspensions cellulaires de Tabac sensibles à la kinétine (Growth and synthesis of proteins in cell suspensions of a kinetin dependent tobacco). Physiologia Plantarum 20 (1967) 834-850
    • (1967) Physiologia Plantarum , vol.20 , pp. 834-850
    • Jouanneau, J.P.1    Peaud-Lenoel, C.2
  • 30
    • 0035787060 scopus 로고    scopus 로고
    • Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells
    • Pauly M., Eberhard S., Albersheim P., Darvill A., and York W.S. Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells. Planta 214 (2001) 67-74
    • (2001) Planta , vol.214 , pp. 67-74
    • Pauly, M.1    Eberhard, S.2    Albersheim, P.3    Darvill, A.4    York, W.S.5
  • 31
    • 33847206778 scopus 로고    scopus 로고
    • Available at: http://www.ebi.ac.uk/integr8/EBI-Integr8-HomePage.do (A. thaliana) and www.chlamy.org (C. reinhardtii).
  • 32
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signaling systems
    • West A.H., and Stock A.M. Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem. Sci. 6 (2001) 369-376
    • (2001) Trends Biochem. Sci. , vol.6 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 33
    • 29344438034 scopus 로고    scopus 로고
    • Two-component phosphorelay signal transduction systems in plants: From hormone responses to circadian rhythms
    • Mizuno T. Two-component phosphorelay signal transduction systems in plants: From hormone responses to circadian rhythms. Biosci. Biotechnol. Biochem. 69 (2005) 2263-2276
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 2263-2276
    • Mizuno, T.1
  • 34
    • 0142092466 scopus 로고    scopus 로고
    • Phenotypic, genetic and molecular characterization of a maize low phytic acid mutant (lpa241)
    • Pilu R., Panzeri D., Gavazzi G., Rasmussen S.K., Consonni G., and Nielsen E. Phenotypic, genetic and molecular characterization of a maize low phytic acid mutant (lpa241). Theor. Appl. Genet. 107 (2003) 980-987
    • (2003) Theor. Appl. Genet. , vol.107 , pp. 980-987
    • Pilu, R.1    Panzeri, D.2    Gavazzi, G.3    Rasmussen, S.K.4    Consonni, G.5    Nielsen, E.6
  • 35
    • 0024329482 scopus 로고
    • Protein phosphorylation: the second messenger signal transducer of flagellar motility
    • Tash J.S. Protein phosphorylation: the second messenger signal transducer of flagellar motility. Cell Motil. Cytoskeleton 14 (1989) 332-339
    • (1989) Cell Motil. Cytoskeleton , vol.14 , pp. 332-339
    • Tash, J.S.1
  • 36
    • 0034833751 scopus 로고    scopus 로고
    • Dynein motors of the Chlamydomonas flagellum
    • DiBella L.M., and King S.M. Dynein motors of the Chlamydomonas flagellum. Int. Rev. Cytol. 210 (2001) 227-268
    • (2001) Int. Rev. Cytol. , vol.210 , pp. 227-268
    • DiBella, L.M.1    King, S.M.2
  • 37
    • 33645068852 scopus 로고    scopus 로고
    • Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways
    • Wagner V., Gessner G., Heiland I., Kaminski M., Hawat S., Scheffler K., and Mittag M. Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways. Eukaryot. Cell 5 (2006) 457-468
    • (2006) Eukaryot. Cell , vol.5 , pp. 457-468
    • Wagner, V.1    Gessner, G.2    Heiland, I.3    Kaminski, M.4    Hawat, S.5    Scheffler, K.6    Mittag, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.