메뉴 건너뛰기




Volumn 171, Issue 4, 2006, Pages 488-496

Phosphoproteomic profiling of wheat callus labelled in vivo

Author keywords

Callus; Mass spectrometry; Phosphoproteomics; Somatic embryogenesis; Wali7

Indexed keywords

BIOCHEMISTRY; ELECTROPHORESIS; MASS SPECTROMETRY; PROTEINS; TISSUE CULTURE;

EID: 33746777804     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2006.05.010     Document Type: Article
Times cited : (8)

References (34)
  • 1
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome
    • Mann M., Ong S., Grønborg M., Steen H., Jensen O.N., and Pandey A. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. TiBtechniques 20 (2002) 261-268
    • (2002) TiBtechniques , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.2    Grønborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 2
    • 0036652968 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies
    • Grønborg M., Kristiansen T.Z., Stensballe A., Andersen J.S., Ohara M., Mann M., Jensen O.N., and Pandey A. A mass spectrometry-based proteomic approach for identification of serine/threonine-phosphorylated proteins by enrichment with phospho-specific antibodies. Mol. Cell. Proteomics 1.7 (2002) 517-527
    • (2002) Mol. Cell. Proteomics , vol.1 7 , pp. 517-527
    • Grønborg, M.1    Kristiansen, T.Z.2    Stensballe, A.3    Andersen, J.S.4    Ohara, M.5    Mann, M.6    Jensen, O.N.7    Pandey, A.8
  • 3
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou Z., Watts J.D., and Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat. Biotechnol. 19 (2001) 375-378
    • (2001) Nat. Biotechnol. , vol.19 , pp. 375-378
    • Zhou, Z.1    Watts, J.D.2    Aebersold, R.3
  • 5
    • 28444487185 scopus 로고    scopus 로고
    • Enrichment of phosphorylated proteins and peptides from complex mixtures using metal oxide/hydroxide affinity chromatography (MOAC)
    • Wolschin F., Weinkoop 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    Weinkoop, S.2    Weckwerth, W.3
  • 6
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art phosphoproteomics
    • Reinders J., and Sickmann A. State-of-the-art phosphoproteomics. Proteomics 5 (2005) 4052-4461
    • (2005) Proteomics , vol.5 , pp. 4052-4461
    • Reinders, J.1    Sickmann, A.2
  • 7
    • 0034954952 scopus 로고    scopus 로고
    • Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors
    • Peck S.C., Nühse T.S., Hess D., Iglesias A., Meins F., and Boller T. Directed proteomics identifies a plant-specific protein rapidly phosphorylated in response to bacterial and fungal elicitors. Plant Cell 13 (2001) 1467-1475
    • (2001) Plant Cell , vol.13 , pp. 1467-1475
    • Peck, S.C.1    Nühse, T.S.2    Hess, D.3    Iglesias, A.4    Meins, F.5    Boller, T.6
  • 8
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • Schulenberg B., Aggeler R., Beechem J.M., Capaldi R.A., and Patton W.F. Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278 (2003) 27251-27255
    • (2003) J. Biol. Chem. , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 9
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann M., Hendrickson R.C., and Pandey A. Analysis of proteins and proteomes by mass spectrometry. Annu. Rev. Biochem. 70 (2001) 437-473
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 10
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., and Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20 (1999) 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 11
    • 0035298820 scopus 로고    scopus 로고
    • Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole tof mass spectrometry in positive ion mode
    • Steen H., Küster B., Fernandez M., Pandey A., and Mann M. Detection of tyrosine phosphorylated peptides by precursor ion scanning quadrupole tof mass spectrometry in positive ion mode. Anal. Chem. 73 (2001) 1440-1448
    • (2001) Anal. Chem. , vol.73 , pp. 1440-1448
    • Steen, H.1    Küster, B.2    Fernandez, M.3    Pandey, A.4    Mann, M.5
  • 14
  • 15
    • 0033946976 scopus 로고    scopus 로고
    • Embryogenic cells in Dactylis glomerata L. (Poaceae) explants identified by cell tracking and SERK expression
    • Somleva M.N., Schmidt E., and de Vries S.C. Embryogenic cells in Dactylis glomerata L. (Poaceae) explants identified by cell tracking and SERK expression. Plant Cell Rep. 19 (2000) 718-726
    • (2000) Plant Cell Rep. , vol.19 , pp. 718-726
    • Somleva, M.N.1    Schmidt, E.2    de Vries, S.C.3
  • 16
    • 0037560022 scopus 로고    scopus 로고
    • cdc2 protein kinase (cdc2Pa) genes during somatic embryogenesis in Norway spruce (Picea abies [L.] Karst)
    • cdc2 protein kinase (cdc2Pa) genes during somatic embryogenesis in Norway spruce (Picea abies [L.] Karst). J. Exp. Bot. 54 (2003) 1711-1719
    • (2003) J. Exp. Bot. , vol.54 , pp. 1711-1719
    • Footitt, S.1    Ingouff, M.2    Clapham, D.3    von Arnold, S.4
  • 17
    • 0033712277 scopus 로고    scopus 로고
    • Green fluorescent protein as a visual marker for wheat transformation
    • Jordan M.C. Green fluorescent protein as a visual marker for wheat transformation. Plant Cell Rep. 19 (2000) 1069-1075
    • (2000) Plant Cell Rep. , vol.19 , pp. 1069-1075
    • Jordan, M.C.1
  • 18
    • 33645470420 scopus 로고    scopus 로고
    • Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction
    • Rampitsch C., Bykova N.V., McCallum B., Beimcik E., and Ens W. Analysis of the wheat and Puccinia triticina (leaf rust) proteomes during a susceptible host-pathogen interaction. Proteomics 6 (2006) 1897-1907
    • (2006) Proteomics , vol.6 , pp. 1897-1907
    • Rampitsch, C.1    Bykova, N.V.2    McCallum, B.3    Beimcik, E.4    Ens, W.5
  • 20
    • 0035258256 scopus 로고    scopus 로고
    • Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis
    • Stensballe A., Andersen S., and Jensen O.N. Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis. Proteomics 1 (2001) 207-218
    • (2001) Proteomics , vol.1 , pp. 207-218
    • Stensballe, A.1    Andersen, S.2    Jensen, O.N.3
  • 21
    • 0034124238 scopus 로고    scopus 로고
    • A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance
    • Loboda A.V., Krutchinsky A.N., Bromirski M., Ens W., and Standing K.G. A tandem quadrupole/time-of-flight mass spectrometer with a matrix-assisted laser desorption/ionization source: design and performance. Rapid Commun. Mass Spectrom. 14 (2000) 1047-1057
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1047-1057
    • Loboda, A.V.1    Krutchinsky, A.N.2    Bromirski, M.3    Ens, W.4    Standing, K.G.5
  • 23
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko A., Sunyaev S., Loboda A., Shevchenko A., Bork P., Ens W., and Standing K. Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal. Chem. 73 (2001) 1917-1926
    • (2001) Anal. Chem. , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Shevchenko, A.4    Bork, P.5    Ens, W.6    Standing, K.7
  • 25
    • 4444335470 scopus 로고    scopus 로고
    • The ABCs (and XYZs) of peptide sequencing
    • Steen H., and Mann M. The ABCs (and XYZs) of peptide sequencing. Nat. Rev. 5 (2004) 699-711
    • (2004) Nat. Rev. , vol.5 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 26
    • 0141884306 scopus 로고    scopus 로고
    • Peptide and protein de novo sequencing by mass spectrometry
    • Standing K.G. Peptide and protein de novo sequencing by mass spectrometry. Current Opin. Struct. Biol. 13 (2003) 595-601
    • (2003) Current Opin. Struct. Biol. , vol.13 , pp. 595-601
    • Standing, K.G.1
  • 27
    • 0033614273 scopus 로고    scopus 로고
    • Light-enhanced induction of ascorbate peroxidase in Japanese radish roots during postgerminative growth
    • Morimura Y., Iwamoto K., Ohya T., Igarashi T., Nakamura Y., Kubo A., Tanaka K., and Ikawa T. Light-enhanced induction of ascorbate peroxidase in Japanese radish roots during postgerminative growth. Plant Sci. 142 (1999) 123-132
    • (1999) Plant Sci. , vol.142 , pp. 123-132
    • Morimura, Y.1    Iwamoto, K.2    Ohya, T.3    Igarashi, T.4    Nakamura, Y.5    Kubo, A.6    Tanaka, K.7    Ikawa, T.8
  • 28
    • 0028489814 scopus 로고
    • Genes induced by aluminum in wheat (Triticum aestivum L.) roots.
    • Richards K.D., Snowden K.C., Gardner R.C., and Wali6 wali7. Genes induced by aluminum in wheat (Triticum aestivum L.) roots. Plant Physiol. 105 (1994) 1455-1456
    • (1994) Plant Physiol. , vol.105 , pp. 1455-1456
    • Richards, K.D.1    Snowden, K.C.2    Gardner, R.C.3
  • 29
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen J.V., Ong S., and Mann M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol. Cell. Proteomics 3 (2004) 608-614
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.2    Mann, M.3
  • 33
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the arabidopsis plasma membrane and a new phosphorylation site database
    • Nühse T.S., Stensballe A., Jensen O.N., and Peck S.C. Phosphoproteomics of the arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 16 (2004) 2394-2405
    • (2004) Plant Cell , vol.16 , pp. 2394-2405
    • Nühse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.