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Volumn 42, Issue 12, 2004, Pages 979-988

Digging deeper into the plant cell wall proteome

Author keywords

Apoplast; Extracellular; Plant cell wall; Proteome; Secreted; Signal sequence

Indexed keywords


EID: 13444283501     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2004.10.014     Document Type: Short Survey
Times cited : (95)

References (92)
  • 1
    • 0036840832 scopus 로고    scopus 로고
    • Subcellular localization of peroxidase in tomato fruit skin and the possible implications for the regulation of fruit growth
    • J. Andrews, S.R. Adams, K.S. Burton, and C.E. Evered Subcellular localization of peroxidase in tomato fruit skin and the possible implications for the regulation of fruit growth J. Exp. Bot. 53 2002 2185 2191
    • (2002) J. Exp. Bot. , vol.53 , pp. 2185-2191
    • Andrews, J.1    Adams, S.R.2    Burton, K.S.3    Evered, C.E.4
  • 2
    • 0036187913 scopus 로고    scopus 로고
    • Extensive feature detection of N-terminal protein sorting signals
    • H. Bannai, Y. Tamada, O. Maruyama, K. Nakai, and S. Miyano Extensive feature detection of N-terminal protein sorting signals Bioinformatics 18 2002 298 305
    • (2002) Bioinformatics , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 3
    • 3142613719 scopus 로고    scopus 로고
    • Plasmodesmata in Arabidopsis thaliana suspension cells
    • E. Bayer, C.L. Thjomas, and A.J. Maule Plasmodesmata in Arabidopsis thaliana suspension cells Protoplasma 223 2004 93 102
    • (2004) Protoplasma , vol.223 , pp. 93-102
    • Bayer, E.1    Thjomas, C.L.2    Maule, A.J.3
  • 4
    • 0242286654 scopus 로고    scopus 로고
    • A signal peptide secretion screen in Fucus distichus embryos reveals expression of glucanase, EGF domain-containing, and LRR receptor kinase-like polypeptides during asymmetric cell growth
    • K.D. Belanger, A.J. Wyman, M.N. Sudol, S.L. Sigla-Pareek, and R.S. Quatrano A signal peptide secretion screen in Fucus distichus embryos reveals expression of glucanase, EGF domain-containing, and LRR receptor kinase-like polypeptides during asymmetric cell growth Planta 217 2003 931 950
    • (2003) Planta , vol.217 , pp. 931-950
    • Belanger, K.D.1    Wyman, A.J.2    Sudol, M.N.3    Sigla-Pareek, S.L.4    Quatrano, R.S.5
  • 6
    • 0035127302 scopus 로고    scopus 로고
    • Proteomic analysis reveals a novel set of cell wall proteins in a transformed tobacco cell culture that synthesizes secondary walls as determined by biochemical and morphological parameters
    • K.A. Blee, E.R. Wheatley, V.A. Bonham, G.P. Mitchell, D. Robertson, A.R. Slabas, M.M. Burrell, P. Wojtaszek, and G.P. Bolwell Proteomic analysis reveals a novel set of cell wall proteins in a transformed tobacco cell culture that synthesizes secondary walls as determined by biochemical and morphological parameters Planta 212 2001 404 415
    • (2001) Planta , vol.212 , pp. 404-415
    • Blee, K.A.1    Wheatley, E.R.2    Bonham, V.A.3    Mitchell, G.P.4    Robertson, D.5    Slabas, A.R.6    Burrell, M.M.7    Wojtaszek, P.8    Bolwell, G.P.9
  • 7
    • 0030867678 scopus 로고    scopus 로고
    • De novo synthesis and accumulation of apoplastic proteins in leaves of heavy metal-exposed barley seedlings
    • A. Blinda, B. Koch, S. Ramanjulu, and K.-J. Dietz De novo synthesis and accumulation of apoplastic proteins in leaves of heavy metal-exposed barley seedlings Plant Cell Environ. 20 1997 969 981
    • (1997) Plant Cell Environ. , vol.20 , pp. 969-981
    • Blinda, A.1    Koch, B.2    Ramanjulu, S.3    Dietz, K.-J.4
  • 9
    • 0037783246 scopus 로고    scopus 로고
    • Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis
    • G.H.H. Borner, K.S. Lilley, T.J. Stevens, and P. Dupree Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis Plant Physiol. 132 2003 568 577
    • (2003) Plant Physiol. , vol.132 , pp. 568-577
    • Borner, G.H.H.1    Lilley, K.S.2    Stevens, T.J.3    Dupree, P.4
  • 10
    • 0031458519 scopus 로고    scopus 로고
    • Sugar uptake by protoplasts isolated from tomato fruit tissues during various stages of fruit growth
    • M.M. Brown, J.L. Hall, and L.C. Ho Sugar uptake by protoplasts isolated from tomato fruit tissues during various stages of fruit growth Physiol. Plant. 101 1997 533 539
    • (1997) Physiol. Plant. , vol.101 , pp. 533-539
    • Brown, M.M.1    Hall, J.L.2    Ho, L.C.3
  • 11
    • 0041423537 scopus 로고    scopus 로고
    • Root-specific CLE19 overexpression and the sol1/2 suppressors implicate a CLV-like pathway in the control of Arabidopsis root meristem maintenance
    • E. Casamitjana-Martinez, H.F. Hofhuis, J. Xu, C.M. Liu, R. Heidstra, and B. Scheres Root-specific CLE19 overexpression and the sol1/2 suppressors implicate a CLV-like pathway in the control of Arabidopsis root meristem maintenance Curr. Biol. 13 2003 1435 1441
    • (2003) Curr. Biol. , vol.13 , pp. 1435-1441
    • Casamitjana-Martinez, E.1    Hofhuis, H.F.2    Xu, J.3    Liu, C.M.4    Heidstra, R.5    Scheres, B.6
  • 13
    • 3543008404 scopus 로고    scopus 로고
    • Role of the apoplast in the control of assimilate transport, photosynthesis and plant productivity
    • V.I. Chikov, and G.G. Bakirova Role of the apoplast in the control of assimilate transport, photosynthesis and plant productivity Russ. J. Plant Physiol. 51 2004 420 431
    • (2004) Russ. J. Plant Physiol. , vol.51 , pp. 420-431
    • Chikov, V.I.1    Bakirova, G.G.2
  • 15
    • 0032187921 scopus 로고    scopus 로고
    • Cell wall loosening by expansins
    • D.J. Cosgrove Cell wall loosening by expansins Plant Physiol. 118 1998 333 339
    • (1998) Plant Physiol. , vol.118 , pp. 333-339
    • Cosgrove, D.J.1
  • 16
    • 2442442977 scopus 로고    scopus 로고
    • Expansion of the plant cell wall
    • J.K.C. Rose Blackwell Publishing Ltd., Oxford, UK and CRC Press Boca Raton, FL
    • D.J. Cosgrove Expansion of the plant cell wall J.K.C. Rose The Plant Cell Wall, Annual Plant Reviews, vol. 8 2003 Blackwell Publishing Ltd., Oxford, UK and CRC Press Boca Raton, FL 237 263
    • (2003) The Plant Cell Wall, Annual Plant Reviews, Vol. 8 , pp. 237-263
    • Cosgrove, D.J.1
  • 17
    • 0034724178 scopus 로고    scopus 로고
    • Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency
    • S.R. Cutler, D.W. Ehrhardt, J.S. Griffitts, and C.R. Somerville Random GFP::cDNA fusions enable visualization of subcellular structures in cells of Arabidopsis at a high frequency Proc. Natl. Acad. Sci. USA 97 2000 3718 3723
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3718-3723
    • Cutler, S.R.1    Ehrhardt, D.W.2    Griffitts, J.S.3    Somerville, C.R.4
  • 18
    • 0036017855 scopus 로고    scopus 로고
    • Polygalacturonase-inhibiting proteins in defense against phytopathogenic fungi
    • G. De Lorenzo, and S. Ferrari Polygalacturonase-inhibiting proteins in defense against phytopathogenic fungi Curr. Opin. Plant Biol. 5 2002 295 299
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 295-299
    • De Lorenzo, G.1    Ferrari, S.2
  • 19
    • 0000260623 scopus 로고    scopus 로고
    • Functions and responses of the leaf apoplast under stress
    • K.J. Dietz Functions and responses of the leaf apoplast under stress Prog. Bot. 58 1996 221 254
    • (1996) Prog. Bot. , vol.58 , pp. 221-254
    • Dietz, K.J.1
  • 20
    • 0346245905 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol lipid anchoring of plant proteins. Sensitive prediction from sequence- and genome-wide studies for Arabidopsis and rice
    • B. Eisenhaber, M. Wildpaner, C.J. Schultz, G.H. Borner, P. Dupree, and F. Eisenhaber Glycosylphosphatidylinositol lipid anchoring of plant proteins. Sensitive prediction from sequence- and genome-wide studies for Arabidopsis and rice Plant Physiol. 133 2003 1691 1701
    • (2003) Plant Physiol. , vol.133 , pp. 1691-1701
    • Eisenhaber, B.1    Wildpaner, M.2    Schultz, C.J.3    Borner, G.H.4    Dupree, P.5    Eisenhaber, F.6
  • 21
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • O. Emanuelsson, H. Nielsen, S. Brunak, and G. Von Heijne Predicting subcellular localization of proteins based on their N-terminal amino acid sequence J. Mol. Biol. 300 2000 1005 1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 22
    • 0038381715 scopus 로고    scopus 로고
    • High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata
    • N.M. Escobar, S. Haupt, G. Thow, P. Boevink, S. Chapman, and K. Oparka High-throughput viral expression of cDNA-green fluorescent protein fusions reveals novel subcellular addresses and identifies unique proteins that interact with plasmodesmata Plant Cell 15 2003 1507 1523
    • (2003) Plant Cell , vol.15 , pp. 1507-1523
    • Escobar, N.M.1    Haupt, S.2    Thow, G.3    Boevink, P.4    Chapman, S.5    Oparka, K.6
  • 24
    • 0346306083 scopus 로고    scopus 로고
    • Gametophytic self-incompatibility inhibits pollen tube growth using different mechanisms
    • V.E. Franklin-Tong, and F.C.H. Franklin Gametophytic self-incompatibility inhibits pollen tube growth using different mechanisms Trends Plant Sci. 8 2003 598 605
    • (2003) Trends Plant Sci. , vol.8 , pp. 598-605
    • Franklin-Tong, V.E.1    Franklin, F.C.H.2
  • 25
    • 0028878632 scopus 로고
    • Polysaccharide-modifying enzymes in the plant cell wall
    • S.C. Fry Polysaccharide-modifying enzymes in the plant cell wall Annu. Rev. Plant Physiol. Plant Mol. Biol. 46 1995 497 520
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 497-520
    • Fry, S.C.1
  • 26
    • 0345148433 scopus 로고    scopus 로고
    • Selection of Arabidopsis genes encoding secreted and plasma membrane proteins
    • J.H. Goo, A.R. Park, W.J. Park, and O.K. Park Selection of Arabidopsis genes encoding secreted and plasma membrane proteins Plant Mol. Biol. 41 1999 415 423
    • (1999) Plant Mol. Biol. , vol.41 , pp. 415-423
    • Goo, J.H.1    Park, A.R.2    Park, W.J.3    Park, O.K.4
  • 28
    • 0141638533 scopus 로고    scopus 로고
    • Identification of guttation fluid proteins: The presence of pathogenesis-related proteins in non-infected barley plants
    • I. Grunwald, I. Rupprecht, G. Schuster, and K. Kloppstech Identification of guttation fluid proteins: the presence of pathogenesis-related proteins in non-infected barley plants Physiol. Plant. 119 2003 192 202
    • (2003) Physiol. Plant. , vol.119 , pp. 192-202
    • Grunwald, I.1    Rupprecht, I.2    Schuster, G.3    Kloppstech, K.4
  • 30
    • 3142734925 scopus 로고    scopus 로고
    • Switching desaturase enzyme specificity by alternate subcellular targeting
    • I. Heilmann, M.S. Pidkowich, T. Girke, and J. Shanklin Switching desaturase enzyme specificity by alternate subcellular targeting Proc. Natl. Acad. Sci. USA 101 2004 10266 10271
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10266-10271
    • Heilmann, I.1    Pidkowich, M.S.2    Girke, T.3    Shanklin, J.4
  • 32
    • 0036834966 scopus 로고    scopus 로고
    • Comparison of peptides in the phloem sap of flowering and non-flowering Perilla and lupine plants using microbore HPLC followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • S. Hoffmann-Benning, D.A. Gage, L. McIntosh, H. Kende, and J.A.D. Zeevaart Comparison of peptides in the phloem sap of flowering and non-flowering Perilla and lupine plants using microbore HPLC followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry Planta 216 2002 140 147
    • (2002) Planta , vol.216 , pp. 140-147
    • Hoffmann-Benning, S.1    Gage, D.A.2    McIntosh, L.3    Kende, H.4    Zeevaart, J.A.D.5
  • 33
    • 0032013898 scopus 로고    scopus 로고
    • Apoplast as the site of response to environmental signals
    • T. Hoson Apoplast as the site of response to environmental signals J. Plant Res. 111 1998 167 177
    • (1998) J. Plant Res. , vol.111 , pp. 167-177
    • Hoson, T.1
  • 34
    • 1342287271 scopus 로고    scopus 로고
    • Coordinated regulation of genes for secretion in tobacco at late developmental stages: Association with resistance against oomycetes
    • K. Hugot, M.P. Riviere, C. Moreilhon, M.A. Dayem, J. Cozzitorto, G. Arbiol, P. Barbry, C. Weiss, and E. Galiana Coordinated regulation of genes for secretion in tobacco at late developmental stages: association with resistance against oomycetes Plant Physiol. 134 2004 858 870
    • (2004) Plant Physiol. , vol.134 , pp. 858-870
    • Hugot, K.1    Riviere, M.P.2    Moreilhon, C.3    Dayem, M.A.4    Cozzitorto, J.5    Arbiol, G.6    Barbry, P.7    Weiss, C.8    Galiana, E.9
  • 36
    • 1042278906 scopus 로고    scopus 로고
    • Plant innate immunity - Direct and indirect recognition of general and specific pathogen-associated molecules
    • D.A. Jones, and D. Takemoto Plant innate immunity - direct and indirect recognition of general and specific pathogen-associated molecules Curr. Opin. Immunol. 16 2004 48 62
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 48-62
    • Jones, D.A.1    Takemoto, D.2
  • 37
    • 1242269749 scopus 로고    scopus 로고
    • Identification of a novel pathogen-induced gene encoding a leucine-rich repeat protein expressed in phloem cells of Capsicum annuum
    • E.H. Jung, H.W. Jung, S.C. Lee, S.W. Han, S. Heu, and B.K. Hwang Identification of a novel pathogen-induced gene encoding a leucine-rich repeat protein expressed in phloem cells of Capsicum annuum Biochim. Biophys. Acta 1676 2004 211 222
    • (2004) Biochim. Biophys. Acta , vol.1676 , pp. 211-222
    • Jung, E.H.1    Jung, H.W.2    Lee, S.C.3    Han, S.W.4    Heu, S.5    Hwang, B.K.6
  • 38
    • 0035823245 scopus 로고    scopus 로고
    • Allele-specific receptor-ligand interactions in Brassica self-incompatibility
    • A. Kachroo, C.R. Schopfer, M.E. Nasrallah, and J.B. Nasrallah Allele-specific receptor-ligand interactions in Brassica self-incompatibility Science 293 2001 1824 1826
    • (2001) Science , vol.293 , pp. 1824-1826
    • Kachroo, A.1    Schopfer, C.R.2    Nasrallah, M.E.3    Nasrallah, J.B.4
  • 40
    • 0038018230 scopus 로고    scopus 로고
    • The decrease of extracted apoplast protein in soybean root tip- by aluminium treatment
    • T. Kataoka, J. Furukawa, and T.M. Nakanishi The decrease of extracted apoplast protein in soybean root tip- by aluminium treatment Biol. Plant. 36 2003 445 449
    • (2003) Biol. Plant. , vol.36 , pp. 445-449
    • Kataoka, T.1    Furukawa, J.2    Nakanishi, T.M.3
  • 41
    • 0030561540 scopus 로고    scopus 로고
    • Signal sequence trap to clone cDNA encoding secreted or membrane-associated plant proteins
    • P. Kristoffersen, T. Teichmann, R. Stracke, and K. Palme Signal sequence trap to clone cDNA encoding secreted or membrane-associated plant proteins Anal. Biochem. 243 1996 127 132
    • (1996) Anal. Biochem. , vol.243 , pp. 127-132
    • Kristoffersen, P.1    Teichmann, T.2    Stracke, R.3    Palme, K.4
  • 42
    • 0000651436 scopus 로고
    • The protein component of primary cell walls
    • D.T.A. Lamport The protein component of primary cell walls Adv. Bot. Res. 2 1965 151 218
    • (1965) Adv. Bot. Res. , vol.2 , pp. 151-218
    • Lamport, D.T.A.1
  • 43
    • 0002426192 scopus 로고
    • Ion distribution in cereal leaves: Pathways and mechanisms
    • R.A. Leigh, and A.D. Tomos Ion distribution in cereal leaves: pathways and mechanisms Phil. Trans. Royal Soc. Lond. B 341 1993 75 86
    • (1993) Phil. Trans. Royal Soc. Lond. B , vol.341 , pp. 75-86
    • Leigh, R.A.1    Tomos, A.D.2
  • 44
    • 1542580426 scopus 로고    scopus 로고
    • The elongation defective 1 mutant of Arabidopsis is impaired in the gene encoding a serine-rich secreted protein
    • K. Lertpiriyapong, and Z.R. Sung The elongation defective 1 mutant of Arabidopsis is impaired in the gene encoding a serine-rich secreted protein Plant Mol. Biol. 53 2003 581 595
    • (2003) Plant Mol. Biol. , vol.53 , pp. 581-595
    • Lertpiriyapong, K.1    Sung, Z.R.2
  • 45
    • 0006926756 scopus 로고
    • Soluble and bound apoplastic proteins and isozymes of peroxidase, esterase and malate dehydrogenase in oat primary leaves
    • Z.-C. Li, and J.W. McClure Soluble and bound apoplastic proteins and isozymes of peroxidase, esterase and malate dehydrogenase in oat primary leaves J. Plant Physiol. 136 1990 398 403
    • (1990) J. Plant Physiol. , vol.136 , pp. 398-403
    • Li, Z.-C.1    McClure, J.W.2
  • 46
    • 84989665769 scopus 로고
    • Proteins accumulate in the apoplast of winter rye leaves during cold acclimation
    • E. Marentes, M. Griffith, A. Mlynarz, and R.A. Brush Proteins accumulate in the apoplast of winter rye leaves during cold acclimation Physiol. Plant. 87 1993 499 507
    • (1993) Physiol. Plant. , vol.87 , pp. 499-507
    • Marentes, E.1    Griffith, M.2    Mlynarz, A.3    Brush, R.A.4
  • 48
    • 0032989240 scopus 로고    scopus 로고
    • Physiological relationships between auxin, cytokinin, and a peptide growth factor, phytosulfokine-α, in stimulation of asparagus cell proliferation
    • Y. Matsubayashi, A. Morita, E. Matsunaga, A. Furuya, N. Hanai, and Y. Sakagami Physiological relationships between auxin, cytokinin, and a peptide growth factor, phytosulfokine-α, in stimulation of asparagus cell proliferation Planta 207 1999 559 565
    • (1999) Planta , vol.207 , pp. 559-565
    • Matsubayashi, Y.1    Morita, A.2    Matsunaga, E.3    Furuya, A.4    Hanai, N.5    Sakagami, Y.6
  • 49
    • 0037165995 scopus 로고    scopus 로고
    • An LRR receptor kinase involved in perception of a peptide plant hormone, phytosulfokine
    • Y. Matsubayashi, M. Ogawa, A. Morita, and Y. Sakagami An LRR receptor kinase involved in perception of a peptide plant hormone, phytosulfokine Science 296 2002 1470 1472
    • (2002) Science , vol.296 , pp. 1470-1472
    • Matsubayashi, Y.1    Ogawa, M.2    Morita, A.3    Sakagami, Y.4
  • 50
    • 0033870123 scopus 로고    scopus 로고
    • A comparison of proteins from the developing xylem of compression and non-compression wood of branches of Sitka spruce (Picea sitchensis) reveals a differentially expressed laccase
    • G.J. McDougall A comparison of proteins from the developing xylem of compression and non-compression wood of branches of Sitka spruce (Picea sitchensis) reveals a differentially expressed laccase J. Exp. Bot. 51 2000 1395 1401
    • (2000) J. Exp. Bot. , vol.51 , pp. 1395-1401
    • McDougall, G.J.1
  • 51
    • 3342890632 scopus 로고    scopus 로고
    • Location, location, location: Surveying the intracellular real estate through proteomics in plants
    • A.H. Millar Location, location, location: surveying the intracellular real estate through proteomics in plants Funct. Plant Biol. 31 2004 563 571
    • (2004) Funct. Plant Biol. , vol.31 , pp. 563-571
    • Millar, A.H.1
  • 52
    • 0036107468 scopus 로고    scopus 로고
    • Identification of defence-related cell wall proteins in Phytophthora sojae-infected soybean roots by ESI-MS/MS
    • A. Mithöfer, B. Müller, G. Wanner, and L.A. Eichacker Identification of defence-related cell wall proteins in Phytophthora sojae-infected soybean roots by ESI-MS/MS Mol. Plant Pathol. 3 2002 163 166
    • (2002) Mol. Plant Pathol. , vol.3 , pp. 163-166
    • Mithöfer, A.1    Müller, B.2    Wanner, G.3    Eichacker, L.A.4
  • 53
    • 0038047058 scopus 로고    scopus 로고
    • Proteomic analysis of changes in the extracellular matrix of Arabidopsis cell suspension cultures induced by fungal elicitors
    • B.K. Ndimba, S. Chivasa, J.M. Hamilton, W.J. Simon, and A.R. Slabas Proteomic analysis of changes in the extracellular matrix of Arabidopsis cell suspension cultures induced by fungal elicitors Proteomics 3 2003 1047 1059
    • (2003) Proteomics , vol.3 , pp. 1047-1059
    • Ndimba, B.K.1    Chivasa, S.2    Hamilton, J.M.3    Simon, W.J.4    Slabas, A.R.5
  • 54
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. Von Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng. 10 1997 1 6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 55
    • 0030976353 scopus 로고    scopus 로고
    • Proteoglycans and related components in plant cells
    • E.A. Nothnagel Proteoglycans and related components in plant cells Int. Rev. Cytol. 174 1997 195 291
    • (1997) Int. Rev. Cytol. , vol.174 , pp. 195-291
    • Nothnagel, E.A.1
  • 56
    • 0032825140 scopus 로고    scopus 로고
    • Starch synthesis in tomato remains constant throughout fruit development and is dependent on sucrose supply and sucrose synthase activity
    • H. N'tchobo, N. Dali, B. Nguyen-Quoc, C. Foyer, and S. Yelle Starch synthesis in tomato remains constant throughout fruit development and is dependent on sucrose supply and sucrose synthase activity J. Exp. Bot. 338 1999 1457 1463
    • (1999) J. Exp. Bot. , vol.338 , pp. 1457-1463
    • N'Tchobo, H.1    Dali, N.2    Nguyen-Quoc, B.3    Foyer, C.4    Yelle, S.5
  • 57
    • 0034051713 scopus 로고    scopus 로고
    • Secreted proteins of tobacco cultured BY2 cells: Identification of a new member of pathogenesis-related proteins
    • Y. Okushima, N. Koizumi, T. Kusano, and H. Sano Secreted proteins of tobacco cultured BY2 cells: identification of a new member of pathogenesis-related proteins Plant Mol. Biol 42 2000 479 488
    • (2000) Plant Mol. Biol , vol.42 , pp. 479-488
    • Okushima, Y.1    Koizumi, N.2    Kusano, T.3    Sano, H.4
  • 58
    • 0031735853 scopus 로고    scopus 로고
    • Analysis of intercellular washing fluids of potato tubers and detection of increased proteolytic activity upon fungal infection
    • F. Olivieri, A.V. Godoy, A. Escande, and C.A. Casalongú Analysis of intercellular washing fluids of potato tubers and detection of increased proteolytic activity upon fungal infection Physiol. Plant. 104 1998 232 238
    • (1998) Physiol. Plant. , vol.104 , pp. 232-238
    • Olivieri, F.1    Godoy, A.V.2    Escande, A.3    Casalongú, C.A.4
  • 59
    • 0029846567 scopus 로고    scopus 로고
    • The elicitor-induced oxidative burst in cultured chickpea cells drives the rapid insolubilization of two cell wall structural proteins
    • O. Otte, and W. Barz The elicitor-induced oxidative burst in cultured chickpea cells drives the rapid insolubilization of two cell wall structural proteins Planta 200 1996 238 246
    • (1996) Planta , vol.200 , pp. 238-246
    • Otte, O.1    Barz, W.2
  • 60
    • 0033434090 scopus 로고    scopus 로고
    • Structure of the glycosylphosphatidylinositol anchor of an arabinogalactan protein from Pyrus communis suspension-cultured cells
    • D. Oxley, and A. Bacic Structure of the glycosylphosphatidylinositol anchor of an arabinogalactan protein from Pyrus communis suspension-cultured cells Proc. Natl. Acad. Sci. USA 96 1999 14246 14251
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14246-14251
    • Oxley, D.1    Bacic, A.2
  • 61
    • 0033777474 scopus 로고    scopus 로고
    • A proteomic approach for the study of Saccharomyces cerevisiae cell wall biogenesis
    • M. Pardo, M. Ward, S. Bains, M. Molina, W. Blackstock, C. Gil, and C. Nobela A proteomic approach for the study of Saccharomyces cerevisiae cell wall biogenesis Electrophoresis 21 2000 3396 3410
    • (2000) Electrophoresis , vol.21 , pp. 3396-3410
    • Pardo, M.1    Ward, M.2    Bains, S.3    Molina, M.4    Blackstock, W.5    Gil, C.6    Nobela, C.7
  • 62
    • 0035940404 scopus 로고    scopus 로고
    • RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development
    • G. Pearce, D.S. Moura, J. Stratmann, and C.A. Ryan Jr. RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development Proc. Natl. Acad. Sci. USA 98 2001 12843 12847
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12843-12847
    • Pearce, G.1    Moura, D.S.2    Stratmann, J.3    Ryan Jr., C.A.4
  • 64
    • 0009626978 scopus 로고
    • Detoxification of sulfur dioxide by apoplastic peroxidases
    • H. Rennenberg C.H. Brunold L.J. De Kok I. Stulen SPB Academic Publishing The Hague
    • H. Pfanz, K.-J. Dietz, I. Weinerth, and B. Oppmann Detoxification of sulfur dioxide by apoplastic peroxidases H. Rennenberg C.H. Brunold L.J. De Kok I. Stulen Sulfur Nutrition and Sulfur Assimilation in Higher Plants 1990 SPB Academic Publishing The Hague
    • (1990) Sulfur Nutrition and Sulfur Assimilation in Higher Plants
    • Pfanz, H.1    Dietz, K.-J.2    Weinerth, I.3    Oppmann, B.4
  • 65
    • 0038631572 scopus 로고    scopus 로고
    • Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome
    • A. Pitarch, M. Sánchez, C. Nombela, and C. Gil Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome Mol. Cell. Proteom. 1 12 2002 967 982
    • (2002) Mol. Cell. Proteom. , vol.1 , Issue.12 , pp. 967-982
    • Pitarch, A.1    Sánchez, M.2    Nombela, C.3    Gil, C.4
  • 68
    • 0030979341 scopus 로고    scopus 로고
    • Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants
    • D. Robertson, G.P. Mitchell, J.S. Gilroy, C. Gerrish, G.P. Bolwell, and A.R. Slabas Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants J. Biol. Chem. 1272 1997 15841 15848
    • (1997) J. Biol. Chem. , vol.1272 , pp. 15841-15848
    • Robertson, D.1    Mitchell, G.P.2    Gilroy, J.S.3    Gerrish, C.4    Bolwell, G.P.5    Slabas, A.R.6
  • 69
    • 0036016431 scopus 로고    scopus 로고
    • CLV3 is localized to the extracellular space, where it activates the Arabidopsis CLAVATA stem cell signaling pathway
    • E. Rojo, V.K. Sharma, V. Kovaleva, N.V. Raikhel, and J.C. Fletcher CLV3 is localized to the extracellular space, where it activates the Arabidopsis CLAVATA stem cell signaling pathway Plant Cell 14 2002 969 977
    • (2002) Plant Cell , vol.14 , pp. 969-977
    • Rojo, E.1    Sharma, V.K.2    Kovaleva, V.3    Raikhel, N.V.4    Fletcher, J.C.5
  • 70
    • 0033041997 scopus 로고    scopus 로고
    • Cooperative disassembly of the cellulose-xyloglucan network of plant cell walls; Parallels between cell expansion and fruit ripening
    • J.K.C. Rose, and A.B. Bennett Cooperative disassembly of the cellulose-xyloglucan network of plant cell walls; parallels between cell expansion and fruit ripening Trends Plant Sci. 4 1999 176 183
    • (1999) Trends Plant Sci. , vol.4 , pp. 176-183
    • Rose, J.K.C.1    Bennett, A.B.2
  • 72
    • 0028813495 scopus 로고
    • Non-destructive collection of apoplastic fluid from developing tomato fruit using a pressure dehydration procedure
    • Y.-L. Ruan, C. Mate, J.W. Patrick, and C.J. Brady Non-destructive collection of apoplastic fluid from developing tomato fruit using a pressure dehydration procedure Aust. J. Plant Physiol. 22 1995 761 769
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 761-769
    • Ruan, Y.-L.1    Mate, C.2    Patrick, J.W.3    Brady, C.J.4
  • 73
    • 0030038321 scopus 로고    scopus 로고
    • The composition of apoplastic fluid recovered from intact developing tomato fruit
    • Y.-L. Ruan, J.W. Patrick, and C.J. Brady The composition of apoplastic fluid recovered from intact developing tomato fruit Aust. J. Plant Physiol. 23 1996 9 13
    • (1996) Aust. J. Plant Physiol. , vol.23 , pp. 9-13
    • Ruan, Y.-L.1    Patrick, J.W.2    Brady, C.J.3
  • 74
    • 0032219547 scopus 로고    scopus 로고
    • Dynamic function and regulation of apoplast in the plant body
    • N. Sakurai Dynamic function and regulation of apoplast in the plant body J. Plant Res. 111 1998 133 148
    • (1998) J. Plant Res. , vol.111 , pp. 133-148
    • Sakurai, N.1
  • 76
    • 0027356728 scopus 로고
    • Structure and function of plant cell wall proteins
    • A.M. Showalter Structure and function of plant cell wall proteins Plant Cell 5 1993 9 23
    • (1993) Plant Cell , vol.5 , pp. 9-23
    • Showalter, A.M.1
  • 77
    • 3042515236 scopus 로고    scopus 로고
    • Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations
    • A.R. Slabas, B. Ndimba, H.W.J. Simon, and S. Chivasa Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations Biochem. Soc. Trans. 32 2004 524 528
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 524-528
    • Slabas, A.R.1    Ndimba, B.2    Simon, H.W.J.3    Chivasa, S.4
  • 81
    • 0030890351 scopus 로고    scopus 로고
    • Detection of glycosyl-phosphatidylinositol-anchored proteins on the surface of Nicotiana tabacum protoplasts
    • A.M. Takos, I.B. Dry, and K.L. Soole Detection of glycosyl- phosphatidylinositol-anchored proteins on the surface of Nicotiana tabacum protoplasts FEBS Lett. 405 1997 1 4
    • (1997) FEBS Lett. , vol.405 , pp. 1-4
    • Takos, A.M.1    Dry, I.B.2    Soole, K.L.3
  • 82
    • 3843115465 scopus 로고    scopus 로고
    • LeSTIG1, an extracellular binding partner for the pollen receptor kinases LePRK1 and LePRK2, promotes pollen tube growth in vitro
    • W. Tang, D. Kelley, I. Ezcurra, R. Cotter, and S. McCormick LeSTIG1, an extracellular binding partner for the pollen receptor kinases LePRK1 and LePRK2, promotes pollen tube growth in vitro Plant J. 39 2004 343 353
    • (2004) Plant J. , vol.39 , pp. 343-353
    • Tang, W.1    Kelley, D.2    Ezcurra, I.3    Cotter, R.4    McCormick, S.5
  • 83
    • 0027165675 scopus 로고
    • Signal sequence trap: A cloning strategy for secreted proteins and type I membrane proteins
    • K. Tashiro, H. Tada, R. Heilker, M. Shirozu, T. Nakano, and T. Honjo Signal sequence trap: a cloning strategy for secreted proteins and type I membrane proteins Science 261 1993 600 603
    • (1993) Science , vol.261 , pp. 600-603
    • Tashiro, K.1    Tada, H.2    Heilker, R.3    Shirozu, M.4    Nakano, T.5    Honjo, T.6
  • 84
    • 1942469934 scopus 로고    scopus 로고
    • Leucine-rich repeat receptor kinases in plants: Structure, function, and signal transduction pathways
    • K.U. Torii Leucine-rich repeat receptor kinases in plants: structure, function, and signal transduction pathways Int. Rev. Cytol. 234 2004 1 46
    • (2004) Int. Rev. Cytol. , vol.234 , pp. 1-46
    • Torii, K.U.1
  • 85
    • 0030459247 scopus 로고    scopus 로고
    • Protein composition of wheat apoplastic fluid and resistance to Russian wheat aphid
    • A.J. Van der Westhuizen, and Z. Pretorius Protein composition of wheat apoplastic fluid and resistance to Russian wheat aphid Aust. J. Plant Physiol. 23 1996 645 648
    • (1996) Aust. J. Plant Physiol. , vol.23 , pp. 645-648
    • Van Der Westhuizen, A.J.1    Pretorius, Z.2
  • 86
    • 0035984051 scopus 로고    scopus 로고
    • The subtilisin-like serine protease SDD1 mediates cell-cell signaling during Arabidopsis stomatal development
    • U. Von Groll, D. Berger, and T. Altmann The subtilisin-like serine protease SDD1 mediates cell-cell signaling during Arabidopsis stomatal development Plant Cell 14 2002 1527 1539
    • (2002) Plant Cell , vol.14 , pp. 1527-1539
    • Von Groll, U.1    Berger, D.2    Altmann, T.3
  • 87
    • 1542406265 scopus 로고    scopus 로고
    • Cell wall proteomics of the green alga Haematococcus pluvialis (Chlorophyceae)
    • S.-B. Wang, Q. Hu, M. Sommerfeld, and F. Chen Cell wall proteomics of the green alga Haematococcus pluvialis (Chlorophyceae) Proteomics 4 2004 692 708
    • (2004) Proteomics , vol.4 , pp. 692-708
    • Wang, S.-B.1    Hu, Q.2    Sommerfeld, M.3    Chen, F.4
  • 89
    • 0029360730 scopus 로고
    • Specificity in the immobilisation of cell wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.)
    • P. Wojtaszek, J. Trethowan, and G.P. Bolwell Specificity in the immobilisation of cell wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.) Plant Mol. Biol. 28 1995 1075 1087
    • (1995) Plant Mol. Biol. , vol.28 , pp. 1075-1087
    • Wojtaszek, P.1    Trethowan, J.2    Bolwell, G.P.3
  • 90
    • 1942487257 scopus 로고    scopus 로고
    • 21-kDa polypeptide, a low-molecular-weight cyclophilin, is released from pollen of higher plants into the extracellular medium in vitro
    • E. Yokota, T. Ohmori, S. Muto, and T. Shimmen 21-kDa polypeptide, a low-molecular-weight cyclophilin, is released from pollen of higher plants into the extracellular medium in vitro Planta 218 2004 1008 1018
    • (2004) Planta , vol.218 , pp. 1008-1018
    • Yokota, E.1    Ohmori, T.2    Muto, S.3    Shimmen, T.4
  • 91
    • 0032803062 scopus 로고    scopus 로고
    • Extraction of apoplastic sap from plant roots by centrifugation
    • Q. Yu, C. Tang, Z. Chen, and J. Kuo Extraction of apoplastic sap from plant roots by centrifugation New Phytol. 143 1999 299 304
    • (1999) New Phytol. , vol.143 , pp. 299-304
    • Yu, Q.1    Tang, C.2    Chen, Z.3    Kuo, J.4
  • 92
    • 0036800766 scopus 로고    scopus 로고
    • Isolation of fungal cell wall degrading proteins from barley (Hordeum vulgare L.) leaves infected with Rynchosproium secalis
    • R. Zareie, D.L. Melanson, and P.J. Murphy Isolation of fungal cell wall degrading proteins from barley (Hordeum vulgare L.) leaves infected with Rynchosproium secalis Mol. Plant-Microbe Interact. 15 2002 1031 1039
    • (2002) Mol. Plant-Microbe Interact. , vol.15 , pp. 1031-1039
    • Zareie, R.1    Melanson, D.L.2    Murphy, P.J.3


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