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Volumn 451, Issue , 2008, Pages 339-359

Phosphorylation analysis of plant viral proteins

Author keywords

Kinase identification; Phosphorylation site mapping; Plant virus infection; Plant virus protein; Protein phosphorylation

Indexed keywords


EID: 84934434598     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-102-4_24     Document Type: Article
Times cited : (3)

References (18)
  • 1
    • 0036582580 scopus 로고    scopus 로고
    • Towards genomic and proteomic studies of protein phosphorylation in plant-pathogen interactions
    • Xing, T., Quellet, T., and Miki, B.L. (2002) Towards genomic and proteomic studies of protein phosphorylation in plant-pathogen interactions. Trends Plant Sci. 7, 224-230.
    • (2002) Trends Plant Sci , vol.7 , pp. 224-230
    • Xing, T.1    Quellet, T.2    Miki, B.L.3
  • 2
    • 0037302253 scopus 로고    scopus 로고
    • Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication
    • Law, L.M.J., Everitt, J.C., Beatch, M.D., Holmes, C.F.B., and Hobman, T.C. (2003) Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication. J. Virol. 77, 1764-1771.
    • (2003) J. Virol , vol.77 , pp. 1764-1771
    • Law, L.M.J.1    Everitt, J.C.2    Beatch, M.D.3    Holmes, C.F.B.4    Hobman, T.C.5
  • 3
    • 0031816798 scopus 로고    scopus 로고
    • Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument
    • Morrison, E.E., Wang, Y., and Meredith, D.M. (1998) Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument. J. Virol. 72, 7108-7114.
    • (1998) J. Virol , vol.72 , pp. 7108-7114
    • Morrison, E.E.1    Wang, Y.2    Meredith, D.M.3
  • 4
    • 0035006310 scopus 로고    scopus 로고
    • Phosphorylation of viral movement proteins: Regulation of cell-to-cell trafficking
    • Lee, J., and Lucas, W.J. (2001) Phosphorylation of viral movement proteins: regulation of cell-to-cell trafficking. Trends Microbiol. 9, 5-8.
    • (2001) Trends Microbiol , vol.9 , pp. 5-8
    • Lee, J.1    Lucas, W.J.2
  • 5
    • 0034665471 scopus 로고    scopus 로고
    • Regulation of plasmodesmal transport by phosphorylation of tobacco mosaic virus cell-to-cell movement protein
    • Waigmann, E., Chen, M.H., Bachmaier, R., Ghoshroy, R., and Citovsky, V. (2000) Regulation of plasmodesmal transport by phosphorylation of tobacco mosaic virus cell-to-cell movement protein. EMBO J. 19, 4875-4884.
    • (2000) EMBO J , vol.19 , pp. 4875-4884
    • Waigmann, E.1    Chen, M.H.2    Bachmaier, R.3    Ghoshroy, R.4    Citovsky, V.5
  • 7
    • 0001621536 scopus 로고    scopus 로고
    • High-resolution two dimensional electrophoresis of proteins using immobilized pH gradients
    • Second edition Celis, J.E, ed, Academic press
    • Görg, A. and Weiss, W. (1998) High-resolution two dimensional electrophoresis of proteins using immobilized pH gradients, in Cell biology: a laboratory handbook, Second edition (Celis, J.E., ed.), Academic press, vol. 4, 386-396.
    • (1998) Cell biology: A laboratory handbook , vol.4 , pp. 386-396
    • Görg, A.1    Weiss, W.2
  • 8
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W.J., van der Geer, P., and Hunter, T. (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 110-149.
    • (1991) Methods Enzymol , vol.201 , pp. 110-149
    • Boyle, W.J.1    van der Geer, P.2    Hunter, T.3
  • 9
    • 85069242163 scopus 로고    scopus 로고
    • Sefton, B.M. (1997) Phosphopeptide mapping and identification of phosphorylation sites, in Current protocols in molecular biology (Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith J.A., Struhl, K., eds.), Wiley, Hoboken, NJ, p. 18.9.10.
    • Sefton, B.M. (1997) Phosphopeptide mapping and identification of phosphorylation sites, in Current protocols in molecular biology (Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith J.A., Struhl, K., eds.), Wiley, Hoboken, NJ, p. 18.9.10.
  • 10
    • 30544452187 scopus 로고    scopus 로고
    • Mapping posttranslational modifications of proteins by MS-based selective detection: Application to phosphoproteomics
    • Carr, S.A., Annan, R.S., and Huddleston, M.J. (2005) Mapping posttranslational modifications of proteins by MS-based selective detection: application to phosphoproteomics. Methods Enzymol. 405, 82-115.
    • (2005) Methods Enzymol , vol.405 , pp. 82-115
    • Carr, S.A.1    Annan, R.S.2    Huddleston, M.J.3
  • 11
    • 30544443201 scopus 로고    scopus 로고
    • Identification of phosphorylation sites using microimmobilized metal affinity chromatography
    • Corthals, G.L., Aebersold, R., and Goodlett, D.R. (2005) Identification of phosphorylation sites using microimmobilized metal affinity chromatography. Methods Enzymol. 405, 66-81.
    • (2005) Methods Enzymol , vol.405 , pp. 66-81
    • Corthals, G.L.1    Aebersold, R.2    Goodlett, D.R.3
  • 12
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M.R., Thingholm, T.E., Jensen, O.N., Roepstorff, P., and Jørgensen T.J.D. (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 4, 873-886.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.D.5
  • 13
    • 0034868043 scopus 로고    scopus 로고
    • Selective analysis of phosphopeptides within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry
    • Adamczyk, M., Gebler, J.C., and Wu, J. (2001) Selective analysis of phosphopeptides within a protein mixture by chemical modification, reversible biotinylation and mass spectrometry. Rapid Commun. Mass Spectrom. 15, 1481-1488.
    • (2001) Rapid Commun. Mass Spectrom , vol.15 , pp. 1481-1488
    • Adamczyk, M.1    Gebler, J.C.2    Wu, J.3
  • 14
    • 0037044198 scopus 로고    scopus 로고
    • Wooten M.W. (2002) In-gel kinase assay as a method to identify kinase substrates. Sci. STKE 15.
    • Wooten M.W. (2002) In-gel kinase assay as a method to identify kinase substrates. Sci. STKE 15.
  • 15
    • 0025002460 scopus 로고
    • Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase
    • Dean, A.M., and Koshland, D.E. (1990) Electrostatic and steric contributions to regulation at the active site of isocitrate dehydrogenase. Science 249, 1044-1046.
    • (1990) Science , vol.249 , pp. 1044-1046
    • Dean, A.M.1    Koshland, D.E.2
  • 16
    • 0038725902 scopus 로고    scopus 로고
    • Constructs and methods for high-throughput gene silencing in plants
    • Helliwell, C. and Waterhouse, P. (2003) Constructs and methods for high-throughput gene silencing in plants. Methods 30, 289-95.
    • (2003) Methods , vol.30 , pp. 289-295
    • Helliwell, C.1    Waterhouse, P.2
  • 17
    • 0035144638 scopus 로고    scopus 로고
    • Tobacco rattle virus as a vector for analysis of gene function by silencing
    • Ratcliff, F., Martin-Hernandez, A.M., and Baulcombe, D.C. (2001) Tobacco rattle virus as a vector for analysis of gene function by silencing. Plant J. 25, 237-245.
    • (2001) Plant J , vol.25 , pp. 237-245
    • Ratcliff, F.1    Martin-Hernandez, A.M.2    Baulcombe, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.