메뉴 건너뛰기




Volumn 138, Issue 3, 2005, Pages 1334-1346

Pectin methylesterase, a regulator of pollen tube growth

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; ESTERS; PLANT CELL CULTURE; POLYSACCHARIDES; RHEOLOGY;

EID: 27244457265     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.105.059865     Document Type: Article
Times cited : (317)

References (62)
  • 1
    • 0026148980 scopus 로고
    • A gene showing sequence similarity to pectin esterase is specifically expressed in developing pollen of Brassica napus. Sequences in its 5′ flanking region are conserved in other pollen-specific promoters
    • Albani D, Altosaar I, Arnison PG, Fabijanski SF (1991) A gene showing sequence similarity to pectin esterase is specifically expressed in developing pollen of Brassica napus. Sequences in its 5′ flanking region are conserved in other pollen-specific promoters. Plant Mol Biol 16: 501-513
    • (1991) Plant Mol Biol , vol.16 , pp. 501-513
    • Albani, D.1    Altosaar, I.2    Arnison, P.G.3    Fabijanski, S.F.4
  • 2
    • 0025134781 scopus 로고
    • A glycoprotein inhibitor of pectin methylesterase in kiwi fruit (Actinidia chinensis)
    • Balestrieri C, Castaldo D, Giovane A, Quagliuolo L, Servillo L (1990) A glycoprotein inhibitor of pectin methylesterase in kiwi fruit (Actinidia chinensis). Eur J Biochem 193: 183-187
    • (1990) Eur J Biochem , vol.193 , pp. 183-187
    • Balestrieri, C.1    Castaldo, D.2    Giovane, A.3    Quagliuolo, L.4    Servillo, L.5
  • 3
    • 0142152461 scopus 로고    scopus 로고
    • Transcriptional profiling of Arabidopsis tissues reveals the unique characteristics of the pollen transcriptome
    • Becker JD, Boavida LC, Carneiro J, Haury M, Feijo JA (2003) Transcriptional profiling of Arabidopsis tissues reveals the unique characteristics of the pollen transcriptome. Plant Physiol 133: 713-725
    • (2003) Plant Physiol , vol.133 , pp. 713-725
    • Becker, J.D.1    Boavida, L.C.2    Carneiro, J.3    Haury, M.4    Feijo, J.A.5
  • 4
    • 0000057919 scopus 로고    scopus 로고
    • Analysis of pectin methyl esterases
    • HF Linskens, JF Jackson, eds, Springer-Verlag, Berlin
    • Bordenave M (1996) Analysis of pectin methyl esterases. In HF Linskens, JF Jackson, eds, Plant Cell Wall Analysis, Vol 17. Springer-Verlag, Berlin, pp 165-180
    • (1996) Plant Cell Wall Analysis , vol.17 , pp. 165-180
    • Bordenave, M.1
  • 5
    • 2142750167 scopus 로고    scopus 로고
    • GFP is the way to glow: Bioimaging of the plant endomembrane system
    • Brandizzi F, Irons SL, Johansen J, Kotzer A, Neumann U (2004) GFP is the way to glow: bioimaging of the plant endomembrane system. J Microsc 214: 138-158
    • (2004) J Microsc , vol.214 , pp. 138-158
    • Brandizzi, F.1    Irons, S.L.2    Johansen, J.3    Kotzer, A.4    Neumann, U.5
  • 6
    • 0012888474 scopus 로고    scopus 로고
    • Kiwi protein inhibitor of pectin methylesterase - Amino-acid sequence and structural importance of two disulfide bridges
    • Camardella L, Carratore V, Ciardiello MA, Servillo L, Balestrieri C, Giovane A (2000) Kiwi protein inhibitor of pectin methylesterase - amino-acid sequence and structural importance of two disulfide bridges. Eur J Biochem 267: 4561-4565
    • (2000) Eur J Biochem , vol.267 , pp. 4561-4565
    • Camardella, L.1    Carratore, V.2    Ciardiello, M.A.3    Servillo, L.4    Balestrieri, C.5    Giovane, A.6
  • 7
    • 0032509207 scopus 로고    scopus 로고
    • Investigation of the action patterns of pectinmethylesterase isoforms through kinetic analyses and NMR spectroscopy - Implications in cell wall expansion
    • Catoire L, Pierron M, Morvan C, du Penhoat CH, Goldberg R (1998) Investigation of the action patterns of pectinmethylesterase isoforms through kinetic analyses and NMR spectroscopy - implications in cell wall expansion. J Biol Chem 273: 33150-33156
    • (1998) J Biol Chem , vol.273 , pp. 33150-33156
    • Catoire, L.1    Pierron, M.2    Morvan, C.3    Du Penhoat, C.H.4    Goldberg, R.5
  • 8
    • 0026516234 scopus 로고
    • Regulation of plant cell-wall pectin methyl esterase by polyamines - Interactions with the effects of metal-ions
    • Charnay D, Nari J, Noat G (1992) Regulation of plant cell-wall pectin methyl esterase by polyamines - interactions with the effects of metal-ions. Eur J Biochem 205: 711-714
    • (1992) Eur J Biochem , vol.205 , pp. 711-714
    • Charnay, D.1    Nari, J.2    Noat, G.3
  • 9
    • 0036741550 scopus 로고    scopus 로고
    • The regulation of actin organization by actin-depolymerizing factor in elongating pollen tubes
    • Chen CY, Wong EI, Vidali L, Estavillo A, Hepler PK, Wu HM, Cheung AY (2002) The regulation of actin organization by actin-depolymerizing factor in elongating pollen tubes. Plant Cell 14: 2175-2190
    • (2002) Plant Cell , vol.14 , pp. 2175-2190
    • Chen, C.Y.1    Wong, E.I.2    Vidali, L.3    Estavillo, A.4    Hepler, P.K.5    Wu, H.M.6    Cheung, A.Y.7
  • 10
    • 0041565063 scopus 로고    scopus 로고
    • Systemic movement of a tobamovirus requires host cell pectin methylesterase
    • Chen MH, Citovsky V (2003) Systemic movement of a tobamovirus requires host cell pectin methylesterase. Plant J 35: 386-392
    • (2003) Plant J , vol.35 , pp. 386-392
    • Chen, M.H.1    Citovsky, V.2
  • 11
    • 0041342982 scopus 로고    scopus 로고
    • Synthetic methyl hexagalacturonate hapten inhibitors of anti-homogalacturonan monoclonal antibodies LM7, JIM5 and JIM7
    • Clausen MH, Willats WGT, Knox JP (2003) Synthetic methyl hexagalacturonate hapten inhibitors of anti-homogalacturonan monoclonal antibodies LM7, JIM5 and JIM7. Carbohydr Res 338: 1797-1800
    • (2003) Carbohydr Res , vol.338 , pp. 1797-1800
    • Clausen, M.H.1    Willats, W.G.T.2    Knox, J.P.3
  • 12
    • 0344118134 scopus 로고    scopus 로고
    • Tomato pectin methylesterase: Modeling, fluorescence, and inhibitor interaction studies - Comparison with the bacterial (Erwinia chrysanthemi) enzyme
    • D'Avino R, Camardella L, Christensen T, Giovane A, Servillo L (2003) Tomato pectin methylesterase: modeling, fluorescence, and inhibitor interaction studies - comparison with the bacterial (Erwinia chrysanthemi) enzyme. Proteins 53: 830-839
    • (2003) Proteins , vol.53 , pp. 830-839
    • D'Avino, R.1    Camardella, L.2    Christensen, T.3    Giovane, A.4    Servillo, L.5
  • 13
    • 0028831192 scopus 로고
    • Quantitative analysis of the distribution of organelles in tobacco pollen tubes: Implications for exocytosis and endocytosis
    • Derksen J, Rutten T, Lichtscheidl IK, de Win AHN, Pierson ES, Rongen G (1995) Quantitative analysis of the distribution of organelles in tobacco pollen tubes: implications for exocytosis and endocytosis. Protoplasma 188: 267-276
    • (1995) Protoplasma , vol.188 , pp. 267-276
    • Derksen, J.1    Rutten, T.2    Lichtscheidl, I.K.3    De Win, A.H.N.4    Pierson, E.S.5    Rongen, G.6
  • 14
    • 3542995708 scopus 로고    scopus 로고
    • Identification and characterization of stretch-activated ion channels in pollen protoplasts
    • Dutta R, Robinson KR (2004) Identification and characterization of stretch-activated ion channels in pollen protoplasts. Plant Physiol 135: 1398-1406
    • (2004) Plant Physiol , vol.135 , pp. 1398-1406
    • Dutta, R.1    Robinson, K.R.2
  • 15
    • 0001239795 scopus 로고
    • Ion dynamics and its possible role during in-vitro pollen germination and tube growth
    • Feijo JA, Malho R, Obermeyer G (1995) Ion dynamics and its possible role during in-vitro pollen germination and tube growth. Protoplasma 187: 155-167
    • (1995) Protoplasma , vol.187 , pp. 155-167
    • Feijo, J.A.1    Malho, R.2    Obermeyer, G.3
  • 16
    • 0031668983 scopus 로고    scopus 로고
    • Location of cellulose and callose in pollen tubes and grains of Nicotiana tabacum
    • Ferguson C, Teeri TT, Siika AM, Read SM, Bacic A (1998) Location of cellulose and callose in pollen tubes and grains of Nicotiana tabacum. Planta 206: 452-460
    • (1998) Planta , vol.206 , pp. 452-460
    • Ferguson, C.1    Teeri, T.T.2    Siika, A.M.3    Read, S.M.4    Bacic, A.5
  • 17
    • 0028095816 scopus 로고
    • Pectin methylesterase isoforms in tomato (Lycopersicon esculentum) tissues - Effects of expression of a pectin methylesterase antisense gene
    • Gaffe J, Tieman DM, Handa AK (1994) Pectin methylesterase isoforms in tomato (Lycopersicon esculentum) tissues - effects of expression of a pectin methylesterase antisense gene. Plant Physiol 105: 199-203
    • (1994) Plant Physiol , vol.105 , pp. 199-203
    • Gaffe, J.1    Tieman, D.M.2    Handa, A.K.3
  • 18
    • 0031200827 scopus 로고    scopus 로고
    • Characterization and functional expression of a ubiquitously expressed tomato pectin methylesterase
    • Gaffe J, Tiznado ME, Handa AK (1997) Characterization and functional expression of a ubiquitously expressed tomato pectin methylesterase. Plant Physiol 114: 1547-1556
    • (1997) Plant Physiol , vol.114 , pp. 1547-1556
    • Gaffe, J.1    Tiznado, M.E.2    Handa, A.K.3
  • 19
    • 0007983349 scopus 로고
    • Ultrastructural immunolocalization of periodic pectin depositions in the cell wall of Nicotiana tabacum pollen tubes
    • Geitmann A, Li YQ, Cresti M (1995) Ultrastructural immunolocalization of periodic pectin depositions in the cell wall of Nicotiana tabacum pollen tubes. Protoplasma 187: 168-171
    • (1995) Protoplasma , vol.187 , pp. 168-171
    • Geitmann, A.1    Li, Y.Q.2    Cresti, M.3
  • 20
    • 0028808263 scopus 로고
    • A glycoprotein inhibitor of pectin methylesterase in kiwi fruit-purification by affinity-chromatography and evidence of a ripening-related precursor
    • Giovane A, Balestrieri C, Quagliuolo L, Castaldo D, Servillo L (1995) A glycoprotein inhibitor of pectin methylesterase in kiwi fruit-purification by affinity-chromatography and evidence of a ripening-related precursor. Eur J Biochem 233: 926-929
    • (1995) Eur J Biochem , vol.233 , pp. 926-929
    • Giovane, A.1    Balestrieri, C.2    Quagliuolo, L.3    Castaldo, D.4    Servillo, L.5
  • 22
    • 77957175484 scopus 로고
    • Composition, properties and localization of pectins in young and mature cells of the mung bean hypocotyl
    • Goldberg R, Morvan C, Roland JC (1986) Composition, properties and localization of pectins in young and mature cells of the mung bean hypocotyl. Plant Cell Physiol 27: 417-429
    • (1986) Plant Cell Physiol , vol.27 , pp. 417-429
    • Goldberg, R.1    Morvan, C.2    Roland, J.C.3
  • 23
    • 0031412197 scopus 로고    scopus 로고
    • Pollen tube growth and the intracellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed
    • Holdaway-Clarke TL, Feijo JA, Hackett GR, Kunkel JG, Hepler PK (1997) Pollen tube growth and the intracellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed. Plant Cell 9: 1999-2010
    • (1997) Plant Cell , vol.9 , pp. 1999-2010
    • Holdaway-Clarke, T.L.1    Feijo, J.A.2    Hackett, G.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 24
    • 0041966088 scopus 로고    scopus 로고
    • Control of pollen tube growth: Role of ion gradients and fluxes
    • Holdaway-Clarke TL, Hepler PK (2003) Control of pollen tube growth: role of ion gradients and fluxes. New Phytol 159: 539-563
    • (2003) New Phytol , vol.159 , pp. 539-563
    • Holdaway-Clarke, T.L.1    Hepler, P.K.2
  • 26
    • 0038120839 scopus 로고    scopus 로고
    • Comparative analysis of the Arabidopsis pollen transcriptome
    • Honys D, Twell D (2003) Comparative analysis of the Arabidopsis pollen transcriptome. Plant Physiol 132: 640-652
    • (2003) Plant Physiol , vol.132 , pp. 640-652
    • Honys, D.1    Twell, D.2
  • 27
    • 17844410215 scopus 로고    scopus 로고
    • Transcriptome analysis of haploid male gametophyte development in Arabidopsis
    • Honys D, Twell D (2004) Transcriptome analysis of haploid male gametophyte development in Arabidopsis. Genome Biol 5: R85
    • (2004) Genome Biol , vol.5
    • Honys, D.1    Twell, D.2
  • 28
    • 0031863410 scopus 로고    scopus 로고
    • Activity staining of pectinesterase on polyacrylamide gels after acidic or sodium dodecyl sulfate electrophoresis
    • Hou WC, Lin YH (1998) Activity staining of pectinesterase on polyacrylamide gels after acidic or sodium dodecyl sulfate electrophoresis. Electrophoresis 19: 692-694
    • (1998) Electrophoresis , vol.19 , pp. 692-694
    • Hou, W.C.1    Lin, Y.H.2
  • 29
    • 0035951291 scopus 로고    scopus 로고
    • Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site
    • Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW (2001) Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site. J Mol Biol 305: 951-960
    • (2001) J Mol Biol , vol.305 , pp. 951-960
    • Jenkins, J.1    Mayans, O.2    Smith, D.3    Worboys, K.4    Pickersgill, R.W.5
  • 30
    • 27744577989 scopus 로고    scopus 로고
    • VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth in the Arabidopsis style and transmitting tract
    • Jiang L, Yang S-L, Xie L-F, Puah CS, Zhang X-Q, Yang W-C, Sundaresan V, Ye D (2005) VANGUARD1 encodes a pectin methylesterase that enhances pollen tube growth in the Arabidopsis style and transmitting tract. Plant Cell 17: 584-596
    • (2005) Plant Cell , vol.17 , pp. 584-596
    • Jiang, L.1    Yang, S.-L.2    Xie, L.-F.3    Puah, C.S.4    Zhang, X.-Q.5    Yang, W.-C.6    Sundaresan, V.7    Ye, D.8
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the heads of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during assembly of the heads of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0028078140 scopus 로고
    • Distribution of unesterified and esterified pectins in cell walls of pollen tubes of flowering plants
    • Li YQ, Chen F, Linskens HF, Cresti M (1994) Distribution of unesterified and esterified pectins in cell walls of pollen tubes of flowering plants. Sex Plant Reprod 7: 145-152
    • (1994) Sex Plant Reprod , vol.7 , pp. 145-152
    • Li, Y.Q.1    Chen, F.2    Linskens, H.F.3    Cresti, M.4
  • 34
    • 0029187853 scopus 로고
    • Immunogold localization of arabinogalactan proteins, unesterified and esterified pectins in pollen grains and pollen tubes of Nicotiana tabacum L.
    • Li YQ, Faleri C, Geitmann A, Zhang HQ, Cresti M (1995) Immunogold localization of arabinogalactan proteins, unesterified and esterified pectins in pollen grains and pollen tubes of Nicotiana tabacum L. Protoplasma 189: 26-36
    • (1995) Protoplasma , vol.189 , pp. 26-36
    • Li, Y.Q.1    Faleri, C.2    Geitmann, A.3    Zhang, H.Q.4    Cresti, M.5
  • 35
    • 0347613014 scopus 로고    scopus 로고
    • Detection and localization of pectin methylesterase isoforms in pollen tubes of Nicotiana tabacum L.
    • Li YQ, Mareck A, Faleri C, Moscatelli A, Liu Q, Cresti M (2002) Detection and localization of pectin methylesterase isoforms in pollen tubes of Nicotiana tabacum L. Planta 214: 734-740
    • (2002) Planta , vol.214 , pp. 734-740
    • Li, Y.Q.1    Mareck, A.2    Faleri, C.3    Moscatelli, A.4    Liu, Q.5    Cresti, M.6
  • 36
    • 0028812280 scopus 로고
    • Calcium-channel activity during pollen-tube growth and reorientation
    • Malho R, Read ND, Trewavas AJ, Pais MS (1995) Calcium-channel activity during pollen-tube growth and reorientation. Plant Cell 7: 1173-1184
    • (1995) Plant Cell , vol.7 , pp. 1173-1184
    • Malho, R.1    Read, N.D.2    Trewavas, A.J.3    Pais, M.S.4
  • 37
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Marchler-Bauer A, Bryant SH (2004) CD-Search: protein domain annotations on the fly. Nucleic Acids Res 32: W327-W331
    • (2004) Nucleic Acids Res , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 38
    • 0035212734 scopus 로고    scopus 로고
    • Pectin methylesterases: Cell wall enzymes with important roles in plant physiology
    • Micheli F (2001) Pectin methylesterases: cell wall enzymes with important roles in plant physiology. Trends Plant Sci 6: 414-419
    • (2001) Trends Plant Sci , vol.6 , pp. 414-419
    • Micheli, F.1
  • 39
    • 0033829448 scopus 로고    scopus 로고
    • Radial distribution pattern of pectin methylesterases across the cambial region of hybrid aspen at activity and dormancy
    • Micheli F, Sundberg B, Goldberg R, Richard L (2000) Radial distribution pattern of pectin methylesterases across the cambial region of hybrid aspen at activity and dormancy. Plant Physiol 124: 191-199
    • (2000) Plant Physiol , vol.124 , pp. 191-199
    • Micheli, F.1    Sundberg, B.2    Goldberg, R.3    Richard, L.4
  • 40
    • 0026005037 scopus 로고
    • Pectin methylesterase, metal-ions and plant cell-wall extension - The role of metal-ions in plant cell-wall extension
    • Moustacas AM, Nari J, Borel M, Noat G, Ricard J (1991) Pectin methylesterase, metal-ions and plant cell-wall extension - the role of metal-ions in plant cell-wall extension. Biochem J 279: 351-354
    • (1991) Biochem J , vol.279 , pp. 351-354
    • Moustacas, A.M.1    Nari, J.2    Borel, M.3    Noat, G.4    Ricard, J.5
  • 41
    • 0028449399 scopus 로고
    • Characterization of a pollen-expressed gene encoding a putative pectin esterase of Petunia inflata
    • Mu JH, Stains JP, Kao TH (1994) Characterization of a pollen-expressed gene encoding a putative pectin esterase of Petunia inflata. Plant Mol Biol 25: 539-544
    • (1994) Plant Mol Biol , vol.25 , pp. 539-544
    • Mu, J.H.1    Stains, J.P.2    Kao, T.H.3
  • 42
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, Von-Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10: 1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von-Heijne, G.4
  • 43
    • 14644408804 scopus 로고    scopus 로고
    • Pectin and the role of the physical properties of the cell wall in pollen tube growth of Solanum chacoense
    • Parre E, Geitmann A (2005) Pectin and the role of the physical properties of the cell wall in pollen tube growth of Solanum chacoense. Planta 220: 582-592
    • (2005) Planta , vol.220 , pp. 582-592
    • Parre, E.1    Geitmann, A.2
  • 44
    • 0038783280 scopus 로고    scopus 로고
    • Pollen tubes exhibit regular periodic membrane trafficking events in the absence of apical extension
    • Parton RM, Fischer-Parton S, Trewavas AJ, Watahiki MK (2003) Pollen tubes exhibit regular periodic membrane trafficking events in the absence of apical extension. J Cell Sci 116: 2707-2719
    • (2003) J Cell Sci , vol.116 , pp. 2707-2719
    • Parton, R.M.1    Fischer-Parton, S.2    Trewavas, A.J.3    Watahiki, M.K.4
  • 45
    • 0028675663 scopus 로고
    • Pollen tube growth is coupled to the extracellular calcium ion flux and the intracellular calcium gradient: Effect of BAPTA-type buffers and hypertonic media
    • Pierson ES, Miller DD, Callaham DA, Shipley AM, Rivers BA, Cresti M, Hepler P (1994) Pollen tube growth is coupled to the extracellular calcium ion flux and the intracellular calcium gradient: effect of BAPTA-type buffers and hypertonic media. Plant Cell 6: 1815-1828
    • (1994) Plant Cell , vol.6 , pp. 1815-1828
    • Pierson, E.S.1    Miller, D.D.2    Callaham, D.A.3    Shipley, A.M.4    Rivers, B.A.5    Cresti, M.6    Hepler, P.7
  • 47
    • 26944493068 scopus 로고    scopus 로고
    • Gene family analysis of the Arabidopsis pollen transcriptome reveals biological implications for cell growth, division control, and gene expression regulation
    • Pina C, Pinto F, Feijo JA, Becker JD (2005) Gene family analysis of the Arabidopsis pollen transcriptome reveals biological implications for cell growth, division control, and gene expression regulation. Plant Physiol 138: 744-756
    • (2005) Plant Physiol , vol.138 , pp. 744-756
    • Pina, C.1    Pinto, F.2    Feijo, J.A.3    Becker, J.D.4
  • 49
    • 1042266305 scopus 로고    scopus 로고
    • Plant protein inhibitors of invertases
    • Rausch T, Greiner S (2004) Plant protein inhibitors of invertases. BBA-Proteins Proteom 1696: 253-261
    • (2004) BBA-Proteins Proteom , vol.1696 , pp. 253-261
    • Rausch, T.1    Greiner, S.2
  • 50
    • 0033833818 scopus 로고    scopus 로고
    • An increase in pectin methyl esterase activity accompanies dormancy breakage and germination of yellow cedar seeds
    • Ren CW, Kermode AR (2000) An increase in pectin methyl esterase activity accompanies dormancy breakage and germination of yellow cedar seeds. Plant Physiol 124: 231-242
    • (2000) Plant Physiol , vol.124 , pp. 231-242
    • Ren, C.W.1    Kermode, A.R.2
  • 51
    • 0032882758 scopus 로고    scopus 로고
    • Uncoupling secretion and tip growth in lily pollen tubes: Evidence for the role of calcium in exocytosis
    • Roy SJ, Holdaway CT, Hackett GR, Kunkel JG, Lord EM, Hepler PK (1999) Uncoupling secretion and tip growth in lily pollen tubes: evidence for the role of calcium in exocytosis. Plant J 19: 379-386
    • (1999) Plant J , vol.19 , pp. 379-386
    • Roy, S.J.1    Holdaway, C.T.2    Hackett, G.R.3    Kunkel, J.G.4    Lord, E.M.5    Hepler, P.K.6
  • 52
    • 0028855261 scopus 로고
    • The plant Golgi-apparatus - Structure, functional organization and trafficking mechanisms
    • Staehelin LA, Moore I (1995) The plant Golgi-apparatus - structure, functional organization and trafficking mechanisms. Annu Rev Plant Physiol 46: 261-288
    • (1995) Annu Rev Plant Physiol , vol.46 , pp. 261-288
    • Staehelin, L.A.1    Moore, I.2
  • 53
    • 84987012975 scopus 로고
    • Tansley review no.16: Pollen tube tip growth
    • Steer MW, Steer JM (1989) Tansley review no.16: pollen tube tip growth. New Phytol 111: 323-358
    • (1989) New Phytol , vol.111 , pp. 323-358
    • Steer, M.W.1    Steer, J.M.2
  • 54
    • 0034835140 scopus 로고    scopus 로고
    • The catalytic site of the pectin biosynthetic enzyme alpha-1,4- galacturonosyltransferase is located in the lumen of the Golgi
    • Sterling JD, Quigley HF, Orellana A, Mohnen D (2001) The catalytic site of the pectin biosynthetic enzyme alpha-1,4-galacturonosyltransferase is located in the lumen of the Golgi. Plant Physiol 127: 360-371
    • (2001) Plant Physiol , vol.127 , pp. 360-371
    • Sterling, J.D.1    Quigley, H.F.2    Orellana, A.3    Mohnen, D.4
  • 55
    • 0028152337 scopus 로고
    • Reduction in pectin methylesterase activity modifies tissue integrity and cation levels in ripening tomato (Lycopersicon esculentum Mill.) fruits
    • Tieman DM, Handa AK (1994) Reduction in pectin methylesterase activity modifies tissue integrity and cation levels in ripening tomato (Lycopersicon esculentum Mill.) fruits. Plant Physiol 106: 429-436
    • (1994) Plant Physiol , vol.106 , pp. 429-436
    • Tieman, D.M.1    Handa, A.K.2
  • 56
    • 0024674809 scopus 로고
    • Isolation and expression of an anther-specific gene from tomato
    • Twell D, Wing R, Yamaguchi J, McCormick S (1989) Isolation and expression of an anther-specific gene from tomato. Mol Gen Genet 217: 240-245
    • (1989) Mol Gen Genet , vol.217 , pp. 240-245
    • Twell, D.1    Wing, R.2    Yamaguchi, J.3    McCormick, S.4
  • 57
    • 0025339859 scopus 로고
    • Pollen-specific gene expression in transgenic plants - Coordinate regulation of 2 different tomato gene promoters during microsporogenesis
    • Twell D, Yamaguchi J, Mccormick S (1990) Pollen-specific gene expression in transgenic plants - coordinate regulation of 2 different tomato gene promoters during microsporogenesis. Development 109: 705-713
    • (1990) Development , vol.109 , pp. 705-713
    • Twell, D.1    Yamaguchi, J.2    Mccormick, S.3
  • 59
    • 0033149816 scopus 로고    scopus 로고
    • Effect of pectin methylesterase gene expression on pea root development
    • Wen FS, Zhu YM, Hawes MC (1999) Effect of pectin methylesterase gene expression on pea root development. Plant Cell 11: 1129-1140
    • (1999) Plant Cell , vol.11 , pp. 1129-1140
    • Wen, F.S.1    Zhu, Y.M.2    Hawes, M.C.3
  • 61
    • 0346996707 scopus 로고    scopus 로고
    • Identification of pollen-expressed pectin methylesterase inhibitors in Arabidopsis
    • Wolf S, Grsic-Rausch S, Rausch T, Greiner S (2003) Identification of pollen-expressed pectin methylesterase inhibitors in Arabidopsis. FEBS Lett 555: 551-555
    • (2003) FEBS Lett , vol.555 , pp. 551-555
    • Wolf, S.1    Grsic-Rausch, S.2    Rausch, T.3    Greiner, S.4
  • 62
    • 0032160714 scopus 로고    scopus 로고
    • Hexose transport in growing petunia pollen tubes and characterization of a pollen-specific, putative monosaccharide transporter
    • Ylstra B, Garrido D, Busscher J, vanTunen AJ (1998) Hexose transport in growing petunia pollen tubes and characterization of a pollen-specific, putative monosaccharide transporter. Plant Physiol 118: 297-304
    • (1998) Plant Physiol , vol.118 , pp. 297-304
    • Ylstra, B.1    Garrido, D.2    Busscher, J.3    VanTunen, A.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.