메뉴 건너뛰기




Volumn 11, Issue 8, 2011, Pages 1530-1544

Towards characterization of the glycoproteome of tomato (Solanum lycopersicum) fruit using Concanavalin A lectin affinity chromatography and LC-MALDI-MS/MS analysis

Author keywords

Cell wall; Fruit development; Lectin affinity; Plant proteomics; Secretome; Tomato

Indexed keywords

CELL MEMBRANE PROTEIN; CONCANAVALIN A; GLYCOPROTEIN; PROTEOME; VEGETABLE PROTEIN;

EID: 79953703697     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000424     Document Type: Article
Times cited : (66)

References (67)
  • 1
    • 77953195874 scopus 로고    scopus 로고
    • Straying off the highway: trafficking of secreted plant proteins and complexity in the plant cell wall proteome
    • Rose, J. K. C., Lee, S.-J., Straying off the highway: trafficking of secreted plant proteins and complexity in the plant cell wall proteome. Plant Physiol. 2010, 153, 433-436.
    • (2010) Plant Physiol. , vol.153 , pp. 433-436
    • Rose, J.K.C.1    Lee, S.-J.2
  • 3
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database
    • Friso, G., Giacomelli, L., Ytterberg, A. J., Peltier, J. B. et al., In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Plant Cell 2004, 16, 478-499.
    • (2004) Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Giacomelli, L.2    Ytterberg, A.J.3    Peltier, J.B.4
  • 4
    • 1842432608 scopus 로고    scopus 로고
    • The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions
    • Kleffmann, T., Russenberger, D., von Zychlinski, A., Christopher, W. et al., The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. Curr. Biol. 2004, 14, 354-362.
    • (2004) Curr. Biol. , vol.14 , pp. 354-362
    • Kleffmann, T.1    Russenberger, D.2    von Zychlinski, A.3    Christopher, W.4
  • 8
    • 40549121251 scopus 로고    scopus 로고
    • Recent advances in plant cell wall proteomics
    • Jamet, E., Albenne, C., Boudart, G., Irshad, M. et al., Recent advances in plant cell wall proteomics. Proteomics 2008, 8, 893-908.
    • (2008) Proteomics , vol.8 , pp. 893-908
    • Jamet, E.1    Albenne, C.2    Boudart, G.3    Irshad, M.4
  • 9
    • 9144258397 scopus 로고    scopus 로고
    • Proteomics of loosely bound cell wall proteins of Arabidopsis thaliana cell suspension cultures: a critical analysis
    • Borderies, G., Jamet, E., Lafitte, C., Rossignol, M. et al., Proteomics of loosely bound cell wall proteins of Arabidopsis thaliana cell suspension cultures: a critical analysis. Electrophoresis 2003, 24, 3421-3432.
    • (2003) Electrophoresis , vol.24 , pp. 3421-3432
    • Borderies, G.1    Jamet, E.2    Lafitte, C.3    Rossignol, M.4
  • 10
    • 3042515236 scopus 로고    scopus 로고
    • Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations
    • Slabas, A. R., Ndimba, B., Simon, W. J., Chivasa, S., Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations. Biochem. Soc. Trans. 2004, 32, 524-528.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 524-528
    • Slabas, A.R.1    Ndimba, B.2    Simon, W.J.3    Chivasa, S.4
  • 12
    • 24644494802 scopus 로고    scopus 로고
    • A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells
    • Kwon, H. K., Yokoyama, R., Nishitani, K., A proteomic approach to apoplastic proteins involved in cell wall regeneration in protoplasts of Arabidopsis suspension-cultured cells. Plant Cell Physiol. 2005, 46, 843-857.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 843-857
    • Kwon, H.K.1    Yokoyama, R.2    Nishitani, K.3
  • 13
    • 31344473515 scopus 로고    scopus 로고
    • Arabidopsis cell wall proteome defined using multidimensional protein identification technology
    • Bayer, E. M., Bottrill, A. R., Walshaw, J., Vigouroux, M. et al., Arabidopsis cell wall proteome defined using multidimensional protein identification technology. Proteomics 2006, 6, 301-311.
    • (2006) Proteomics , vol.6 , pp. 301-311
    • Bayer, E.M.1    Bottrill, A.R.2    Walshaw, J.3    Vigouroux, M.4
  • 14
    • 55749101133 scopus 로고    scopus 로고
    • Proteomic analysis of alterations in the secretome of Arabidopsis thaliana suspension cells subjected to nutritional phosphate deficiency
    • Tran, H. T., Plaxton, W. C., Proteomic analysis of alterations in the secretome of Arabidopsis thaliana suspension cells subjected to nutritional phosphate deficiency. Proteomics 2008, 8, 4317-4326.
    • (2008) Proteomics , vol.8 , pp. 4317-4326
    • Tran, H.T.1    Plaxton, W.C.2
  • 15
    • 34247261617 scopus 로고    scopus 로고
    • Extracellular proteins in pea root tip and border cell exudates
    • Wen, F., VanEtten, H. D., Tsaprailis, G., Hawes, M. C., Extracellular proteins in pea root tip and border cell exudates. Plant Physiol. 2007, 143, 773-783.
    • (2007) Plant Physiol. , vol.143 , pp. 773-783
    • Wen, F.1    VanEtten, H.D.2    Tsaprailis, G.3    Hawes, M.C.4
  • 16
    • 61349161763 scopus 로고    scopus 로고
    • Systematic secretome analyses of rice leaf and seed callus suspension-cultured cells: workflow development and establishment of high-density two-dimensional gel reference maps
    • Jung, Y. H., Jeong, S. H., Kim, S. H., Singh, R. et al., Systematic secretome analyses of rice leaf and seed callus suspension-cultured cells: workflow development and establishment of high-density two-dimensional gel reference maps. J. Proteome Res. 2008, 7, 5187-5210.
    • (2008) J. Proteome Res. , vol.7 , pp. 5187-5210
    • Jung, Y.H.1    Jeong, S.H.2    Kim, S.H.3    Singh, R.4
  • 17
    • 38949120694 scopus 로고    scopus 로고
    • Identification by 2-D DIGE of apoplastic proteins regulated by oligogalacturonides in Arabidopsis thaliana
    • Casasoli, M., Spadoni, S., Lilley, K. S., Cervone, F. et al., Identification by 2-D DIGE of apoplastic proteins regulated by oligogalacturonides in Arabidopsis thaliana. Proteomics 2008, 8, 1042-1054.
    • (2008) Proteomics , vol.8 , pp. 1042-1054
    • Casasoli, M.1    Spadoni, S.2    Lilley, K.S.3    Cervone, F.4
  • 18
    • 37249082491 scopus 로고    scopus 로고
    • Cell wall proteome in the maize primary root elongation zone. II. Region-specific changes in water soluble and lightly ionically bound proteins under water deficit
    • Zhu, J., Alvarez, S., Marsh, E. L., Lenoble, M. E. et al., Cell wall proteome in the maize primary root elongation zone. II. Region-specific changes in water soluble and lightly ionically bound proteins under water deficit. Plant Physiol. 2007, 145, 1533-1548.
    • (2007) Plant Physiol. , vol.145 , pp. 1533-1548
    • Zhu, J.1    Alvarez, S.2    Marsh, E.L.3    Lenoble, M.E.4
  • 19
    • 13244266980 scopus 로고    scopus 로고
    • Cell wall proteins in apoplastic fluids of Arabidopsis thaliana rosettes: identification by mass spectrometry and bioinformatics
    • Boudart, G., Jamet, E., Rossignol, M., Lafitte, C. et al., Cell wall proteins in apoplastic fluids of Arabidopsis thaliana rosettes: identification by mass spectrometry and bioinformatics. Proteomics 2005, 5, 212-221.
    • (2005) Proteomics , vol.5 , pp. 212-221
    • Boudart, G.1    Jamet, E.2    Rossignol, M.3    Lafitte, C.4
  • 20
    • 33751072654 scopus 로고    scopus 로고
    • The Arabidopsis unannotated secreted peptide database, a resource for plant peptidomics
    • Lease, K. A., Walker, J. C., The Arabidopsis unannotated secreted peptide database, a resource for plant peptidomics. Plant Physiol. 2006, 142, 831-838.
    • (2006) Plant Physiol. , vol.142 , pp. 831-838
    • Lease, K.A.1    Walker, J.C.2
  • 21
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson, O., Brunak, S., von Heijne, G., Nielsen, H., Locating proteins in the cell using TargetP, SignalP and related tools. Nat. Protoc. 2007, 2, 953-971.
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 22
    • 24944480447 scopus 로고    scopus 로고
    • A coupled yeast signal sequence trap and transient plant expression strategy to identify genes encoding secreted proteins from peach pistils
    • Yamane, H., Lee, S. J., Kim, B. D., Tao, R., Rose, J. K. C., A coupled yeast signal sequence trap and transient plant expression strategy to identify genes encoding secreted proteins from peach pistils. J. Exp. Bot. 2005, 56, 2229-2238.
    • (2005) J. Exp. Bot. , vol.56 , pp. 2229-2238
    • Yamane, H.1    Lee, S.J.2    Kim, B.D.3    Tao, R.4    Rose, J.K.C.5
  • 23
    • 34548825632 scopus 로고    scopus 로고
    • Identification of eukaryotic secreted and cell surface proteins using the yeast secretion trap screen
    • Lee, S. J., Kim, B. D., Rose, J. K., Identification of eukaryotic secreted and cell surface proteins using the yeast secretion trap screen. Nat. Protoc. 2006, 1, 2439-2447.
    • (2006) Nat. Protoc. , vol.1 , pp. 2439-2447
    • Lee, S.J.1    Kim, B.D.2    Rose, J.K.3
  • 24
    • 0034351416 scopus 로고    scopus 로고
    • Glycosylation and protein transport
    • Scheiffele, P., Fullekrug, J., Glycosylation and protein transport. Essays Biochem. 2000, 36, 27-35.
    • (2000) Essays Biochem. , vol.36 , pp. 27-35
    • Scheiffele, P.1    Fullekrug, J.2
  • 25
    • 14744298421 scopus 로고    scopus 로고
    • Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming
    • Faye, L., Boulaflous, A., Benchabane, M., Gomord, V., Michaud, D., Protein modifications in the plant secretory pathway: current status and practical implications in molecular pharming. Vaccine 2005, 23, 1770-1778.
    • (2005) Vaccine , vol.23 , pp. 1770-1778
    • Faye, L.1    Boulaflous, A.2    Benchabane, M.3    Gomord, V.4    Michaud, D.5
  • 26
    • 33845762779 scopus 로고    scopus 로고
    • Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
    • Saint-Jore-Dupas, C., Nebenfuhr, A., Boulaflous, A., Follet-Gueye, M. L. et al., Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway. Plant Cell 2006, 18, 3182-3200.
    • (2006) Plant Cell , vol.18 , pp. 3182-3200
    • Saint-Jore-Dupas, C.1    Nebenfuhr, A.2    Boulaflous, A.3    Follet-Gueye, M.L.4
  • 27
    • 0037685263 scopus 로고    scopus 로고
    • Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins
    • Kaji, H., Saito, H., Yamauchi, Y., Shinkawa, T. et al., Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins. Nat. Biotechnol. 2003, 21, 667-672.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 667-672
    • Kaji, H.1    Saito, H.2    Yamauchi, Y.3    Shinkawa, T.4
  • 28
    • 33750620940 scopus 로고    scopus 로고
    • Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers
    • Drake, R. R., Schwegler, E. E., Malik, G., Diaz, J. et al., Lectin capture strategies combined with mass spectrometry for the discovery of serum glycoprotein biomarkers. Mol. Cell. Proteomics 2006, 5, 1957-1967.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1957-1967
    • Drake, R.R.1    Schwegler, E.E.2    Malik, G.3    Diaz, J.4
  • 29
    • 33751521664 scopus 로고    scopus 로고
    • A method for the identification of glycoproteins from human serum by a combination of lectin affinity chromatography along with anion exchange and Cu-IMAC selection of tryptic peptides
    • Qiu, R., Zhang, X., Regnier, F. E., A method for the identification of glycoproteins from human serum by a combination of lectin affinity chromatography along with anion exchange and Cu-IMAC selection of tryptic peptides. J. Chromatogr. B 2007, 845, 143-150.
    • (2007) J. Chromatogr. B , vol.845 , pp. 143-150
    • Qiu, R.1    Zhang, X.2    Regnier, F.E.3
  • 30
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • Yang, Z., Hancock, W. S., Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J. Chromatogr. A 2004, 1053, 79-88.
    • (2004) J. Chromatogr. A , vol.1053 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 31
    • 75749150176 scopus 로고    scopus 로고
    • Automated platform for fractionation of human plasma glycoproteome in clinical proteomics
    • Kulloli, M., Hancock, W. S., Hincapie, M., Automated platform for fractionation of human plasma glycoproteome in clinical proteomics. Anal. Chem. 2010, 82, 115-120.
    • (2010) Anal. Chem. , vol.82 , pp. 115-120
    • Kulloli, M.1    Hancock, W.S.2    Hincapie, M.3
  • 32
    • 34548442008 scopus 로고    scopus 로고
    • A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases
    • Minic, Z., Jamet, E., Negroni, L., Arsene der Garabedian, P. et al., A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases. J. Exp. Bot. 2007, 58, 2503-2512.
    • (2007) J. Exp. Bot. , vol.58 , pp. 2503-2512
    • Minic, Z.1    Jamet, E.2    Negroni, L.3    Arsene der Garabedian, P.4
  • 33
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates, J. R., 3rd, Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 2001, 19, 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates 3rd, J.R.3
  • 34
    • 33748808698 scopus 로고    scopus 로고
    • Extracellular proteomes of Arabidopsis thaliana and Brassica napus roots: analysis and comparison by MudPIT and LC-MS/MS
    • Basu, U., Francis, J. L., Whittal, R. M., Stephens, J. L. et al., Extracellular proteomes of Arabidopsis thaliana and Brassica napus roots: analysis and comparison by MudPIT and LC-MS/MS. Plant Soil 2006, 286, 357-376.
    • (2006) Plant Soil , vol.286 , pp. 357-376
    • Basu, U.1    Francis, J.L.2    Whittal, R.M.3    Stephens, J.L.4
  • 35
    • 0037015065 scopus 로고    scopus 로고
    • Plant proteomics: BLASTing out of a MudPIT
    • Whitelegge, J. P., Plant proteomics: BLASTing out of a MudPIT. Proc. Natl. Acad. Sci. USA 2002, 99, 11564-11566.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11564-11566
    • Whitelegge, J.P.1
  • 37
    • 2942690153 scopus 로고    scopus 로고
    • Genetic regulation of fruit development and ripening
    • Giovannoni, J. J., Genetic regulation of fruit development and ripening. Plant Cell 2004, 16, S170-S180.
    • (2004) Plant Cell , vol.16
    • Giovannoni, J.J.1
  • 38
    • 38949099113 scopus 로고    scopus 로고
    • The intersection between cell wall disassembly, ripening, and fruit susceptibility to Botrytis cinerea
    • Cantu, D., Vicente, A. R., Greve, L. C., Dewey, F. M. et al., The intersection between cell wall disassembly, ripening, and fruit susceptibility to Botrytis cinerea. Proc. Natl. Acad. Sci. USA, 2008, 105, 859-864.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 859-864
    • Cantu, D.1    Vicente, A.R.2    Greve, L.C.3    Dewey, F.M.4
  • 39
    • 67650175507 scopus 로고    scopus 로고
    • RNA interference of LIN5 in tomato confirms its role in controlling Brix content, uncovers the influence of sugars on the levels of fruit hormones, and demonstrates the importance of sucrose cleavage for normal fruit development and fertility
    • Zanor, M. I., Osorio, S., Nunes-Nesi, A., Carrari, F. et al., RNA interference of LIN5 in tomato confirms its role in controlling Brix content, uncovers the influence of sugars on the levels of fruit hormones, and demonstrates the importance of sucrose cleavage for normal fruit development and fertility. Plant Physiol. 2009, 150, 1204-1218.
    • (2009) Plant Physiol. , vol.150 , pp. 1204-1218
    • Zanor, M.I.1    Osorio, S.2    Nunes-Nesi, A.3    Carrari, F.4
  • 40
    • 32144446968 scopus 로고    scopus 로고
    • Alignment and statistical difference analysis of complex peptide data sets generated by multidimensional LC-MS
    • America, A. H., Cordewener, J. H., van Geffen, M. H., Lommen, A. et al., Alignment and statistical difference analysis of complex peptide data sets generated by multidimensional LC-MS. Proteomics 2006, 6, 641-653.
    • (2006) Proteomics , vol.6 , pp. 641-653
    • America, A.H.1    Cordewener, J.H.2    van Geffen, M.H.3    Lommen, A.4
  • 41
    • 33746030032 scopus 로고    scopus 로고
    • Proteomic analysis of tomato fruits from two ecotypes during ripening
    • Rocco, M., D'Ambrosio, C., Arena, S., Faurobert, M. et al., Proteomic analysis of tomato fruits from two ecotypes during ripening. Proteomics 2006, 6, 3781-3791.
    • (2006) Proteomics , vol.6 , pp. 3781-3791
    • Rocco, M.1    D'Ambrosio, C.2    Arena, S.3    Faurobert, M.4
  • 42
    • 34250678462 scopus 로고    scopus 로고
    • Major proteome variations associated with cherry tomato pericarp development and ripening
    • Faurobert, M., Mihr, C., Bertin, N., Pawlowski, T. et al., Major proteome variations associated with cherry tomato pericarp development and ripening. Plant Physiol. 2007, 143, 1327-1346.
    • (2007) Plant Physiol. , vol.143 , pp. 1327-1346
    • Faurobert, M.1    Mihr, C.2    Bertin, N.3    Pawlowski, T.4
  • 43
    • 0030995515 scopus 로고    scopus 로고
    • Expression of a divergent expansin gene is fruit-specific and ripening-regulated
    • Rose, J. K. C., Lee, H. H., Bennett, A. B., Expression of a divergent expansin gene is fruit-specific and ripening-regulated. Proc. Natl. Acad. Sci. USA 1997, 94, 5955-5960.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5955-5960
    • Rose, J.K.C.1    Lee, H.H.2    Bennett, A.B.3
  • 44
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., Horton, P., PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 1999, 24, 34-36.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 45
    • 1542400030 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins using machine-learned classifiers
    • Lu, Z., Szafron, D., Greiner, R., Lu, P. et al., Predicting subcellular localization of proteins using machine-learned classifiers. Bioinformatics 2004, 20, 547-556.
    • (2004) Bioinformatics , vol.20 , pp. 547-556
    • Lu, Z.1    Szafron, D.2    Greiner, R.3    Lu, P.4
  • 46
    • 33646861792 scopus 로고    scopus 로고
    • MultiLoc: prediction of protein subcellular localization using N-terminal targeting sequences, sequence motifs and amino acid composition
    • Hoglund, A., Donnes, P., Blum, T., Adolph, H. W., Kohlbacher, O., MultiLoc: prediction of protein subcellular localization using N-terminal targeting sequences, sequence motifs and amino acid composition. Bioinformatics 2006, 22, 1158-1165.
    • (2006) Bioinformatics , vol.22 , pp. 1158-1165
    • Hoglund, A.1    Donnes, P.2    Blum, T.3    Adolph, H.W.4    Kohlbacher, O.5
  • 47
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • Krogh, A., Larsson, B., von Heijne, G., Sonnhammer, E. L., Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305, 567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 48
    • 0346245905 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol lipid anchoring of plant proteins. Sensitive prediction from sequence- and genome-wide studies for Arabidopsis and rice
    • Eisenhaber, B., Wildpaner, M., Schultz, C. J., Borner, G. H. et al., Glycosylphosphatidylinositol lipid anchoring of plant proteins. Sensitive prediction from sequence- and genome-wide studies for Arabidopsis and rice. Plant Physiol. 2003, 133, 1691-1701.
    • (2003) Plant Physiol. , vol.133 , pp. 1691-1701
    • Eisenhaber, B.1    Wildpaner, M.2    Schultz, C.J.3    Borner, G.H.4
  • 49
    • 0037783246 scopus 로고    scopus 로고
    • Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis
    • Borner, G. H., Lilley, K. S., Stevens, T. J., Dupree, P., Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis. Plant Physiol. 2003, 132, 568-577.
    • (2003) Plant Physiol. , vol.132 , pp. 568-577
    • Borner, G.H.1    Lilley, K.S.2    Stevens, T.J.3    Dupree, P.4
  • 50
    • 0002473750 scopus 로고
    • Molecular cloning of tomato pectin methylesterase gene and its expression in Rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits
    • Harriman, R. W., Tieman, D. M., Handa, A. K., Molecular cloning of tomato pectin methylesterase gene and its expression in Rutgers, ripening inhibitor, nonripening, and never ripe tomato fruits. Plant Physiol. 1991, 97, 80-87.
    • (1991) Plant Physiol. , vol.97 , pp. 80-87
    • Harriman, R.W.1    Tieman, D.M.2    Handa, A.K.3
  • 51
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W., Rabouille, C., Mechanisms of regulated unconventional protein secretion. Nat. Rev. Mol. Cell Biol. 2009, 10, 148-155.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 52
    • 0034867627 scopus 로고    scopus 로고
    • Cell wall metabolism in fruit softening and quality and its manipulation in transgenic plants
    • Brummell, D. A., Harpster, M. H., Cell wall metabolism in fruit softening and quality and its manipulation in transgenic plants. Plant Mol. Biol. 2001, 47, 311-340.
    • (2001) Plant Mol. Biol. , vol.47 , pp. 311-340
    • Brummell, D.A.1    Harpster, M.H.2
  • 53
    • 0029801592 scopus 로고    scopus 로고
    • Differential expression of two endo-1,4-[beta]-glucanase genes in pericarp and locules of wild-type and mutant tomato fruit
    • Gonzalez-Bosch, C., Brummell, D. A., Bennett, A. B., Differential expression of two endo-1, 4-[beta]-glucanase genes in pericarp and locules of wild-type and mutant tomato fruit. Plant Physiol. 1996, 111, 1313-1319.
    • (1996) Plant Physiol. , vol.111 , pp. 1313-1319
    • Gonzalez-Bosch, C.1    Brummell, D.A.2    Bennett, A.B.3
  • 54
    • 0031809410 scopus 로고    scopus 로고
    • Concanavalin A binding and endoglycosidase D resistance of beta1,2-xylosylated and alpha 1,3-fucosylated plant and insect oligosaccharides
    • Wilson, B. H., Altmann, F., Concanavalin A binding and endoglycosidase D resistance of beta1, 2-xylosylated and alpha 1, 3-fucosylated plant and insect oligosaccharides. Glycoconj. J. 1998, 15, 203-206.
    • (1998) Glycoconj. J. , vol.15 , pp. 203-206
    • Wilson, B.H.1    Altmann, F.2
  • 55
    • 11844252119 scopus 로고    scopus 로고
    • A cut above the rest: the regulatory function of plant proteases
    • Schaller, A., A cut above the rest: the regulatory function of plant proteases. Planta 2004, 220, 183-197.
    • (2004) Planta , vol.220 , pp. 183-197
    • Schaller, A.1
  • 56
    • 44949258132 scopus 로고    scopus 로고
    • Plant proteases: from phenotypes to molecular mechanisms
    • van der Hoorn, R. A., Plant proteases: from phenotypes to molecular mechanisms. Annu. Rev. Plant Biol. 2008, 59, 191-223.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 191-223
    • van der Hoorn, R.A.1
  • 57
    • 0024678117 scopus 로고
    • Molecular cloning, nucleotide sequence, and abscisic acid induction of a suberization-associated highly anionic peroxidase
    • Roberts, E., Kolattukudy, P. E., Molecular cloning, nucleotide sequence, and abscisic acid induction of a suberization-associated highly anionic peroxidase. Mol. Gen. Genet. 1989, 217, 223-232.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 223-232
    • Roberts, E.1    Kolattukudy, P.E.2
  • 58
    • 33344460777 scopus 로고    scopus 로고
    • TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat
    • Pourcel, L., Routaboul, J. M., Kerhoas, L., Caboche, M. et al., TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat. Plant Cell 2005, 17, 2966-2980.
    • (2005) Plant Cell , vol.17 , pp. 2966-2980
    • Pourcel, L.1    Routaboul, J.M.2    Kerhoas, L.3    Caboche, M.4
  • 59
    • 70349861775 scopus 로고    scopus 로고
    • Cutin deficiency in the tomato fruit cuticle consistently affects resistance to microbial infection and biomechanical properties, but not transpirational water loss
    • Isaacson, T., Kosma, D. K., Matas, A. J., Buda, G. J. et al., Cutin deficiency in the tomato fruit cuticle consistently affects resistance to microbial infection and biomechanical properties, but not transpirational water loss. Plant J. 2009, 60, 363-377.
    • (2009) Plant J. , vol.60 , pp. 363-377
    • Isaacson, T.1    Kosma, D.K.2    Matas, A.J.3    Buda, G.J.4
  • 60
    • 66149161763 scopus 로고    scopus 로고
    • Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid transfer protein required for export of lipids to the plant surface
    • DeBono, A., Yeats, T. H., Rose, J. K. C., Bird, D. et al., Arabidopsis LTPG is a glycosylphosphatidylinositol-anchored lipid transfer protein required for export of lipids to the plant surface. Plant Cell 2009, 21, 1230-1238.
    • (2009) Plant Cell , vol.21 , pp. 1230-1238
    • DeBono, A.1    Yeats, T.H.2    Rose, J.K.C.3    Bird, D.4
  • 61
    • 77955860805 scopus 로고    scopus 로고
    • Mining the surface proteome of tomato (Solanum lycopersicum) fruit for proteins associated with cuticle biogenesis
    • Yeats, T. H., Howe, K. J., Matas, A. J., Buda, G. J. et al., Mining the surface proteome of tomato (Solanum lycopersicum) fruit for proteins associated with cuticle biogenesis. J. Exp. Bot; 2010, 61, 3759-3771.
    • (2010) J. Exp. Bot; , vol.61 , pp. 3759-3771
    • Yeats, T.H.1    Howe, K.J.2    Matas, A.J.3    Buda, G.J.4
  • 62
    • 23644455714 scopus 로고    scopus 로고
    • Phospholipase D: a lipid centric review
    • Jenkins, G. M., Frohman, M. A., Phospholipase D: a lipid centric review. Cell Mol. Life Sci. 2005, 62, 2305-2316.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2305-2316
    • Jenkins, G.M.1    Frohman, M.A.2
  • 63
    • 46249091922 scopus 로고    scopus 로고
    • Multiple roles of phosphoinositide-specific phospholipase C isozymes
    • Suh, P. G., Park, J. I., Manzoli, L., Cocco, L. et al., Multiple roles of phosphoinositide-specific phospholipase C isozymes. BMB Rep. 2008, 41, 415-434.
    • (2008) BMB Rep. , vol.41 , pp. 415-434
    • Suh, P.G.1    Park, J.I.2    Manzoli, L.3    Cocco, L.4
  • 64
    • 77953280408 scopus 로고    scopus 로고
    • Potential role for purple acid phosphatase in the dephosphorylation of wall proteins in tobacco cells
    • Kaida, R., Serada, S., Norioka, N., Neumetzler, L. et al., Potential role for purple acid phosphatase in the dephosphorylation of wall proteins in tobacco cells. Plant Physiol. 2010, 153, 603-610.
    • (2010) Plant Physiol. , vol.153 , pp. 603-610
    • Kaida, R.1    Serada, S.2    Norioka, N.3    Neumetzler, L.4
  • 65
    • 77956014533 scopus 로고    scopus 로고
    • The lectin riddle: glycoproteins fractionated from complex mixtures have similar glycomic profiles
    • Lee, A., Nakano, M., Hincapie, M., Kolarich, D. et al., The lectin riddle: glycoproteins fractionated from complex mixtures have similar glycomic profiles. J. Integ. Biol. 2010, 14: 487-499.
    • (2010) J. Integ. Biol. , vol.14 , pp. 487-499
    • Lee, A.1    Nakano, M.2    Hincapie, M.3    Kolarich, D.4
  • 66
    • 59749086716 scopus 로고    scopus 로고
    • Specificity analysis of lectins and antibodies using remodeled glycoproteins
    • Iskratsch, T., Braun, A., Paschinger, K., Wilson, I. B. H., Specificity analysis of lectins and antibodies using remodeled glycoproteins. Anal. Biochem. 2009, 386, 133-146.
    • (2009) Anal. Biochem. , vol.386 , pp. 133-146
    • Iskratsch, T.1    Braun, A.2    Paschinger, K.3    Wilson, I.B.H.4
  • 67
    • 33750097998 scopus 로고    scopus 로고
    • The use of mass spectrometry for the proteomic analysis of glycosylation
    • Morelle, W., Canis, K., Chirat, F., Faid, V., Michalski, J.-C., The use of mass spectrometry for the proteomic analysis of glycosylation. Proteomics 2006, 6, 3993-4015.
    • (2006) Proteomics , vol.6 , pp. 3993-4015
    • Morelle, W.1    Canis, K.2    Chirat, F.3    Faid, V.4    Michalski, J.-C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.