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Volumn 161, Issue 4, 2013, Pages 1706-1721

Distribution of transglutaminase in pear pollen tubes in relation to cytoskeleton and membrane dynamics

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EID: 84875742070     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.112.212225     Document Type: Article
Times cited : (24)

References (74)
  • 1
    • 79251631214 scopus 로고    scopus 로고
    • Plasma membrane factor XIIIA transglutaminase activity regulates osteoblast matrix secretion and deposition by affecting microtubule dynamics
    • Al-Jallad HF, Myneni VD, Piercy-Kotb SA, Chabot N, Mulani A, Keillor JW, Kaartinen MT (2011) Plasma membrane factor XIIIA transglutaminase activity regulates osteoblast matrix secretion and deposition by affecting microtubule dynamics. PLoS ONE 6: e15893
    • (2011) PLoS ONE , vol.6
    • Al-Jallad, H.F.1    Myneni, V.D.2    Piercy-Kotb, S.A.3    Chabot, N.4    Mulani, A.5    Keillor, J.W.6    Kaartinen, M.T.7
  • 2
    • 0035937106 scopus 로고    scopus 로고
    • Phospholipase Cdelta1 is a guanine nucleotide exchanging factor for transglutaminase II (Galpha h) and promotes alpha 1B-adrenoreceptor-mediated GTP binding and intracellular calcium release
    • Baek KJ, Kang S, Damron D, Im M (2001) Phospholipase Cdelta1 is a guanine nucleotide exchanging factor for transglutaminase II (Galpha h) and promotes alpha 1B-adrenoreceptor-mediated GTP binding and intracellular calcium release. J Biol Chem 276: 5591-5597
    • (2001) J Biol Chem , vol.276 , pp. 5591-5597
    • Baek, K.J.1    Kang, S.2    Damron, D.3    Im, M.4
  • 3
    • 0000364270 scopus 로고
    • RNA, proteins and polyamines during tube growth in germinating apple pollen
    • Bagni N, Adamo P, Serafini-Fracassini D (1981) RNA, proteins and polyamines during tube growth in germinating apple pollen. Plant Physiol 68: 727-730
    • (1981) Plant Physiol , vol.68 , pp. 727-730
    • Bagni, N.1    Adamo, P.2    Serafini-Fracassini, D.3
  • 4
    • 62949123361 scopus 로고    scopus 로고
    • An overview of the first 50 years of transglutaminase research
    • Beninati S, Bergamini CM, Piacentini M (2009) An overview of the first 50 years of transglutaminase research. Amino Acids 36: 591-598
    • (2009) Amino Acids , vol.36 , pp. 591-598
    • Beninati, S.1    Bergamini, C.M.2    Piacentini, M.3
  • 5
    • 84871943544 scopus 로고    scopus 로고
    • Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apices
    • Beninati S, Iorio RA, Tasco G, Serafini-Fracassini D, Casadio R, Del Duca S (2013) Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apices. Amino Acids 44: 271-283
    • (2013) Amino Acids , vol.44 , pp. 271-283
    • Beninati, S.1    Iorio, R.A.2    Tasco, G.3    Serafini-Fracassini, D.4    Casadio, R.5    Del Duca, S.6
  • 6
    • 0017144469 scopus 로고
    • Differential transglutaminase distribution in normal rat liver and rat hepatoma
    • Birckbichler PJ, Orr GR, Patterson MK Jr (1976) Differential transglutaminase distribution in normal rat liver and rat hepatoma. Cancer Res 36: 2911-2914
    • (1976) Cancer Res , vol.36 , pp. 2911-2914
    • Birckbichler, P.J.1    Orr, G.R.2    Patterson Jr., M.K.3
  • 7
    • 79952295573 scopus 로고    scopus 로고
    • Distribution of callose synthase, cellulose synthase, and sucrose synthase in tobacco pollen tube is controlled in dissimilar ways by actin filaments and microtubules
    • Cai G, Faleri C, Del Casino C, Emons AMC, Cresti M (2011) Distribution of callose synthase, cellulose synthase, and sucrose synthase in tobacco pollen tube is controlled in dissimilar ways by actin filaments and microtubules. Plant Physiol 155: 1169-1190
    • (2011) Plant Physiol , vol.155 , pp. 1169-1190
    • Cai, G.1    Faleri, C.2    Del Casino, C.3    Emons, A.M.C.4    Cresti, M.5
  • 8
    • 48549104131 scopus 로고    scopus 로고
    • Pollen tube growth oscillations and intracellular calcium levels are reversibly modulated by actin polymerization
    • Cárdenas L, Lovy-Wheeler A, Kunkel JG, Hepler PK (2008) Pollen tube growth oscillations and intracellular calcium levels are reversibly modulated by actin polymerization. Plant Physiol 146: 1611-1621
    • (2008) Plant Physiol , vol.146 , pp. 1611-1621
    • Cárdenas, L.1    Lovy-Wheeler, A.2    Kunkel, J.G.3    Hepler, P.K.4
  • 10
    • 44949226058 scopus 로고    scopus 로고
    • Structural and signaling networks for the polar cell growth machinery in pollen tubes
    • Cheung AY, Wu HM (2008) Structural and signaling networks for the polar cell growth machinery in pollen tubes. Annu Rev Plant Biol 59: 547-572
    • (2008) Annu Rev Plant Biol , vol.59 , pp. 547-572
    • Cheung, A.Y.1    Wu, H.M.2
  • 11
    • 0031585857 scopus 로고    scopus 로고
    • Colocalization of tissue transglutaminase and stress fibers in human vascular smooth muscle cells and human umbilical vein endothelial cells
    • Chowdhury ZA, Barsigian C, Chalupowicz GD, Bach TL, Garcia-Manero G, Martinez J (1997) Colocalization of tissue transglutaminase and stress fibers in human vascular smooth muscle cells and human umbilical vein endothelial cells. Exp Cell Res 231: 38-49
    • (1997) Exp Cell Res , vol.231 , pp. 38-49
    • Chowdhury, Z.A.1    Barsigian, C.2    Chalupowicz, G.D.3    Bach, T.L.4    Garcia-Manero, G.5    Martinez, J.6
  • 13
    • 34548390229 scopus 로고    scopus 로고
    • Transglutaminase activity changes during the hypersensitive reaction, a typical defense response of tobacco NN plants to TMV
    • Del Duca S, Betti L, Trebbi G, Serafini-Fracassini D, Torrigiani P (2007) Transglutaminase activity changes during the hypersensitive reaction, a typical defense response of tobacco NN plants to TMV. Physiol Plant 131: 241-250
    • (2007) Physiol Plant , vol.131 , pp. 241-250
    • Del Duca, S.1    Betti, L.2    Trebbi, G.3    Serafini-Fracassini, D.4    Torrigiani, P.5
  • 14
    • 0030905623 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed modification of cytoskeletal proteins by polyamines during the germination of Malus domestica pollen
    • Del Duca S, Bregoli AM, Bergamini C, Serafini-Fracassini D (1997) Transglutaminase-catalyzed modification of cytoskeletal proteins by polyamines during the germination of Malus domestica pollen. Sex Plant Reprod 10: 89-95
    • (1997) Sex Plant Reprod , vol.10 , pp. 89-95
    • Del Duca, S.1    Bregoli, A.M.2    Bergamini, C.3    Serafini-Fracassini, D.4
  • 15
    • 77953079215 scopus 로고    scopus 로고
    • Compatible and self-incompatible pollination in Pyrus communis displays different polyamine levels and transglutaminase activity
    • Del Duca S, Cai G, Di Sandro A, Serafini-Fracassini D (2010) Compatible and self-incompatible pollination in Pyrus communis displays different polyamine levels and transglutaminase activity. Amino Acids 38: 659-667
    • (2010) Amino Acids , vol.38 , pp. 659-667
    • Del Duca, S.1    Cai, G.2    Di Sandro, A.3    Serafini-Fracassini, D.4
  • 16
    • 18344396836 scopus 로고    scopus 로고
    • Transglutaminases of higher, lower plants and fungi
    • Del Duca S, Serafini-Fracassini D (2005) Transglutaminases of higher, lower plants and fungi. Prog Exp Tumor Res 38: 223-247
    • (2005) Prog Exp Tumor Res , vol.38 , pp. 223-247
    • Del Duca, S.1    Serafini-Fracassini, D.2
  • 17
    • 62149146855 scopus 로고    scopus 로고
    • Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments
    • Del Duca S, Serafini-Fracassini D, Bonner PL, Cresti M, Cai G (2009) Effects of post-translational modifications catalysed by pollen transglutaminase on the functional properties of microtubules and actin filaments. Biochem J 418: 651-664
    • (2009) Biochem J , vol.418 , pp. 651-664
    • Del Duca, S.1    Serafini-Fracassini, D.2    Bonner, P.L.3    Cresti, M.4    Cai, G.5
  • 19
    • 34250683461 scopus 로고    scopus 로고
    • The acropetal wave of developmental cell death of tobacco corolla is preceded by activation of transglutaminase in different cell compartments
    • Della Mea M, De Filippis F, Genovesi V, Serafini Fracassini D, Del Duca S (2007) The acropetal wave of developmental cell death of tobacco corolla is preceded by activation of transglutaminase in different cell compartments. Plant Physiol 144: 1211-1222
    • (2007) Plant Physiol , vol.144 , pp. 1211-1222
    • della Mea, M.1    de Filippis, F.2    Genovesi, V.3    Serafini, F.D.4    Del Duca, S.5
  • 23
    • 84866176153 scopus 로고    scopus 로고
    • Beta-actin is a target for transglutaminase activity at synaptic endings in chicken telencephalic cell cultures
    • Dolge L, Aufenvenne K, Traupe H, Baumgartner W (2012) Beta-actin is a target for transglutaminase activity at synaptic endings in chicken telencephalic cell cultures. J Mol Neurosci 46: 410-419
    • (2012) J Mol Neurosci , vol.46 , pp. 410-419
    • Dolge, L.1    Aufenvenne, K.2    Traupe, H.3    Baumgartner, W.4
  • 24
    • 0019783299 scopus 로고
    • Degradation of unsaturated fatty acids in peroxisomes: Existence of a 2,4-dienoyl-CoA reductase pathway
    • Dommes V, Baumgart C, Kunau WH (1981) Degradation of unsaturated fatty acids in peroxisomes: existence of a 2,4-dienoyl-CoA reductase pathway. J Biol Chem 256: 8259-8262
    • (1981) J Biol Chem , vol.256 , pp. 8259-8262
    • Dommes, V.1    Baumgart, C.2    Kunau, W.H.3
  • 25
    • 0023652785 scopus 로고
    • In vitro interactions between polyamines and pectic substances
    • D'Orazi D, Bagni N (1987) In vitro interactions between polyamines and pectic substances. Biochem Biophys Res Commun 148: 1259-1263
    • (1987) Biochem Biophys Res Commun , vol.148 , pp. 1259-1263
    • D'Orazi, D.1    Bagni, N.2
  • 27
    • 14644430344 scopus 로고    scopus 로고
    • Sequential extraction and quantitative recovery of gliadins, glutenins, and other proteins from small samples of wheat flour
    • DuPont FM, Chan R, Lopez R, Vensel WH (2005) Sequential extraction and quantitative recovery of gliadins, glutenins, and other proteins from small samples of wheat flour. J Agric Food Chem 53: 1575-1584
    • (2005) J Agric Food Chem , vol.53 , pp. 1575-1584
    • Dupont, F.M.1    Chan, R.2    Lopez, R.3    Vensel, W.H.4
  • 28
    • 0033535048 scopus 로고    scopus 로고
    • Growing pollen tubes possess a constitutive alkaline band in the clear zone and a growth-dependent acidic tip
    • Feijó JA, Sainhas J, Hackett GR, Kunkel JG, Hepler PK (1999) Growing pollen tubes possess a constitutive alkaline band in the clear zone and a growth-dependent acidic tip. J Cell Biol 144: 483-496
    • (1999) J Cell Biol , vol.144 , pp. 483-496
    • Feijó, J.A.1    Sainhas, J.2    Hackett, G.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 29
    • 0018816617 scopus 로고
    • Transglutaminases
    • Folk JE (1980) Transglutaminases. Annu Rev Biochem 49: 517-531
    • (1980) Annu Rev Biochem , vol.49 , pp. 517-531
    • Folk, J.E.1
  • 31
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: nature's biological glues. Biochem J 368: 377-396
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 34
    • 47649092897 scopus 로고    scopus 로고
    • Visualisation of transglutaminase-mediated crosslinking activity in germinating pollen by laser confocal microscopy
    • Iorio RA, Di Sandro A, Scarpellini A, Del Duca S, Serafini-Fracassini D, Verderio E (2008) Visualisation of transglutaminase-mediated crosslinking activity in germinating pollen by laser confocal microscopy. Plant Biosyst 142: 360-365
    • (2008) Plant Biosyst , vol.142 , pp. 360-365
    • Iorio, R.A.1    Di Sandro, A.2    Scarpellini, A.3    Del Duca, S.4    Serafini-Fracassini, D.5    Verderio, E.6
  • 35
    • 0021181552 scopus 로고
    • Presence of a transglutaminase activity in rat liver lysosomes
    • Juprelle-Soret M, Wattiaux-De Coninck S, Wattiaux R (1984) Presence of a transglutaminase activity in rat liver lysosomes. Eur J Cell Biol 34: 271-274
    • (1984) Eur J Cell Biol , vol.34 , pp. 271-274
    • Juprelle-Soret, M.1    Wattiaux-De, C.S.2    Wattiaux, R.3
  • 36
    • 0030583141 scopus 로고    scopus 로고
    • Purification and properties of transglutaminase from soybean (Glycine max) leaves
    • Kang H, Cho YD (1996) Purification and properties of transglutaminase from soybean (Glycine max) leaves. Biochem Biophys Res Commun 223: 288-292
    • (1996) Biochem Biophys Res Commun , vol.223 , pp. 288-292
    • Kang, H.1    Cho, Y.D.2
  • 37
    • 82755161784 scopus 로고    scopus 로고
    • 2+-dependent action of a multifunctional protein
    • 2+-dependent action of a multifunctional protein. FEBS J 278: 4717-4739
    • (2011) FEBS J , vol.278 , pp. 4717-4739
    • Király, R.1    Demény, M.2    Fésüs, L.3
  • 38
    • 70350037669 scopus 로고    scopus 로고
    • Microfilament orientation constrains vesicle flow and spatial distribution in growing pollen tubes
    • Kroeger JH, Daher FB, Grant M, Geitmann A (2009) Microfilament orientation constrains vesicle flow and spatial distribution in growing pollen tubes. Biophys J 97: 1822-1831
    • (2009) Biophys J , vol.97 , pp. 1822-1831
    • Kroeger, J.H.1    Daher, F.B.2    Grant, M.3    Geitmann, A.4
  • 39
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 40
    • 55249116526 scopus 로고    scopus 로고
    • Pollen proteins bind to the Cterminal domain of Nicotiana alata pistil arabinogalactan proteins
    • Lee CB, Swatek KN, McClure B (2008) Pollen proteins bind to the Cterminal domain of Nicotiana alata pistil arabinogalactan proteins. J Biol Chem 283: 26965-26973
    • (2008) J Biol Chem , vol.283 , pp. 26965-26973
    • Lee, C.B.1    Swatek, K.N.2    McClure, B.3
  • 41
    • 56349141069 scopus 로고    scopus 로고
    • Tip growth: Signaling in the apical dome
    • Lee YJ, Yang Z (2008) Tip growth: signaling in the apical dome. Curr Opin Plant Biol 11: 662-671
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 662-671
    • Lee, Y.J.1    Yang, Z.2
  • 42
    • 0029187853 scopus 로고
    • Immunogold localization of arabinogalactan proteins, unesterified and esterified pectins in pollen grains and pollen tubes of Nicotiana tabacum L
    • Li Y-Q, Faleri C, Geitmann A, Zhang HQ, Cresti M (1995a) 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
  • 43
    • 0010257285 scopus 로고
    • Presumed phylogenetic basis of the correlation of pectin deposition pattern in pollen tube walls and the stylar structure of angiosperms
    • Li Y-Q, Fang C, Faleri C, Ciampolini F, Linskens HF, Cresti M (1995b) Presumed phylogenetic basis of the correlation of pectin deposition pattern in pollen tube walls and the stylar structure of angiosperms. Proc Kon Ned Akad Wetensch 98: 39-44
    • (1995) Proc Kon Ned Akad Wetensch , vol.98 , pp. 39-44
    • Li, Y.-Q.1    Fang, C.2    Faleri, C.3    Ciampolini, F.4    Linskens, H.F.5    Cresti, M.6
  • 44
    • 0001653786 scopus 로고    scopus 로고
    • Detection of Ca2+-dependent transglutaminase activity in root and leaf tissue of monocotyledonous and dicotyledonous plants
    • Lilley GR, Skill J, Griffin M, Bonner PL (1998) Detection of Ca2+-dependent transglutaminase activity in root and leaf tissue of monocotyledonous and dicotyledonous plants. Plant Physiol 117: 1115-1123
    • (1998) Plant Physiol , vol.117 , pp. 1115-1123
    • Lilley, G.R.1    Skill, J.2    Griffin, M.3    Bonner, P.L.4
  • 45
    • 38049086320 scopus 로고    scopus 로고
    • Pyrus pyrifolia stylar S-RNase induces alterations in the actin cytoskeleton in self-pollen and tubes in vitro
    • Liu ZQ, Xu GH, Zhang SL (2007) Pyrus pyrifolia stylar S-RNase induces alterations in the actin cytoskeleton in self-pollen and tubes in vitro. Protoplasma 232: 61-67
    • (2007) Protoplasma , vol.232 , pp. 61-67
    • Liu, Z.Q.1    Xu, G.H.2    Zhang, S.L.3
  • 46
    • 18044372483 scopus 로고    scopus 로고
    • Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube
    • Lovy-Wheeler A, Wilsen KL, Baskin TI, Hepler PK (2005) Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube. Planta 221: 95-104
    • (2005) Planta , vol.221 , pp. 95-104
    • Lovy-Wheeler, A.1    Wilsen, K.L.2    Baskin, T.I.3    Hepler, P.K.4
  • 47
    • 0033768668 scopus 로고    scopus 로고
    • The multiple roles of arabinogalactan proteins in plant development
    • Majewska-Sawka A, Nothnagel EA (2000) The multiple roles of arabinogalactan proteins in plant development. Plant Physiol 122: 3-10
    • (2000) Plant Physiol , vol.122 , pp. 3-10
    • Majewska-Sawka, A.1    Nothnagel, E.A.2
  • 50
    • 32844467408 scopus 로고    scopus 로고
    • Tissue transglutaminase: From biological glue to cell survival cues
    • Mehta K, Fok JY, Mangala LS (2006) Tissue transglutaminase: from biological glue to cell survival cues. Front Biosci 11: 173-185
    • (2006) Front Biosci , vol.11 , pp. 173-185
    • Mehta, K.1    Fok, J.Y.2    Mangala, L.S.3
  • 51
    • 0036008291 scopus 로고    scopus 로고
    • Arabinogalactan proteins, pollen tube growth, and the reversible effects of Yariv phenylglycoside
    • Mollet JC, Kim S, Jauh GY, Lord EM (2002) Arabinogalactan proteins, pollen tube growth, and the reversible effects of Yariv phenylglycoside. Protoplasma 219: 89-98
    • (2002) Protoplasma , vol.219 , pp. 89-98
    • Mollet, J.C.1    Kim, S.2    Jauh, G.Y.3    Lord, E.M.4
  • 52
    • 0036851186 scopus 로고    scopus 로고
    • Brefeldin A: Deciphering an enigmatic inhibitor of secretion
    • Nebenführ A, Ritzenthaler C, Robinson DG (2002) Brefeldin A: deciphering an enigmatic inhibitor of secretion. Plant Physiol 130: 1102-1108
    • (2002) Plant Physiol , vol.130 , pp. 1102-1108
    • Nebenführ, A.1    Ritzenthaler, C.2    Robinson, D.G.3
  • 53
    • 77956916373 scopus 로고    scopus 로고
    • Transglutaminase 2: A multi-functional protein in multiple subcellular compartments
    • Park D, Choi SS, Ha KS (2010) Transglutaminase 2: a multi-functional protein in multiple subcellular compartments. Amino Acids 39: 619-631
    • (2010) Amino Acids , vol.39 , pp. 619-631
    • Park, D.1    Choi, S.S.2    Ha, K.S.3
  • 54
    • 77949772648 scopus 로고    scopus 로고
    • Changes in the accumulation of a- and b-tubulin during bud development in Vitis vinifera L
    • Parrotta L, Cai G, Cresti M (2010) Changes in the accumulation of a- and b-tubulin during bud development in Vitis vinifera L. Planta 231: 277-291
    • (2010) Planta , vol.231 , pp. 277-291
    • Parrotta, L.1    Cai, G.2    Cresti, M.3
  • 55
    • 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
  • 58
    • 48949120184 scopus 로고    scopus 로고
    • Microtubules are a target for self-incompatibility signaling in Papaver pollen
    • Poulter NS, Vatovec S, Franklin-Tong VE (2008) Microtubules are a target for self-incompatibility signaling in Papaver pollen. Plant Physiol 146: 1358-1367
    • (2008) Plant Physiol , vol.146 , pp. 1358-1367
    • Poulter, N.S.1    Vatovec, S.2    Franklin-Tong, V.E.3
  • 59
    • 0020375704 scopus 로고
    • Intracellular distribution of transglutaminase activity during rat liver regeneration
    • Remington JA, Russell DH (1982) Intracellular distribution of transglutaminase activity during rat liver regeneration. J Cell Physiol 113: 252-256
    • (1982) J Cell Physiol , vol.113 , pp. 252-256
    • Remington, J.A.1    Russell, D.H.2
  • 60
    • 0347400431 scopus 로고    scopus 로고
    • Organelle isolation
    • eds, Plant Cell Biology. Oxford University Press, Oxford
    • Robinson DG, Hinz G (2001) Organelle isolation. In C Hawes, B Satiat-Jeunemaitre, eds, Plant Cell Biology. Oxford University Press, Oxford, pp 295-323
    • (2001) C Hawes, B Satiat-Jeunemaitre , pp. 295-323
    • Robinson, D.G.1    Hinz, G.2
  • 61
    • 47649091159 scopus 로고    scopus 로고
    • Transglutaminases: Widespread cross-linking enzymes in plants
    • Serafini-Fracassini D, Del Duca S (2008) Transglutaminases: widespread cross-linking enzymes in plants. Ann Bot (Lond) 102: 145-152
    • (2008) Ann Bot (Lond) , vol.102 , pp. 145-152
    • Serafini-Fracassini, D.1    Del Duca, S.2
  • 62
    • 84960668655 scopus 로고
    • First evidence for polyamine conjugation mediated by an enzymic activity in plants
    • Serafini-Fracassini D, Del Duca S, D'Orazi D (1988) First evidence for polyamine conjugation mediated by an enzymic activity in plants. Plant Physiol 87: 757-761
    • (1988) Plant Physiol , vol.87 , pp. 757-761
    • Serafini-Fracassini, D.1    Del Duca, S.2    D'Orazi, D.3
  • 64
    • 0033739035 scopus 로고    scopus 로고
    • Integrin-like proteins in the pollen tube: Detection, localization and function
    • Sun Y, Qian H, Xu X-D, Han Y, Yen L-F, Sun D-Y (2000) Integrin-like proteins in the pollen tube: detection, localization and function. Plant Cell Physiol 41: 1136-1142
    • (2000) Plant Cell Physiol , vol.41 , pp. 1136-1142
    • Sun, Y.1    Qian, H.2    Xu, X.-D.3    Han, Y.4    Yen, L.-F.5    Sun, D.-Y.6
  • 65
    • 0023834388 scopus 로고
    • A novel actin label: A fluorescent probe at glutamine-41 and its consequences
    • Takashi R (1988) A novel actin label: a fluorescent probe at glutamine-41 and its consequences. Biochemistry 27: 938-943
    • (1988) Biochemistry , vol.27 , pp. 938-943
    • Takashi, R.1
  • 66
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 67
    • 66149165865 scopus 로고    scopus 로고
    • A mobile secretory vesicle cluster involved in mass transport from the Golgi to the plant cell exterior
    • Toyooka K, Goto Y, Asatsuma S, Koizumi M, Mitsui T, Matsuoka K (2009) A mobile secretory vesicle cluster involved in mass transport from the Golgi to the plant cell exterior. Plant Cell 21: 1212-1229
    • (2009) Plant Cell , vol.21 , pp. 1212-1229
    • Toyooka, K.1    Goto, Y.2    Asatsuma, S.3    Koizumi, M.4    Mitsui, T.5    Matsuoka, K.6
  • 68
    • 0035172425 scopus 로고    scopus 로고
    • Actin polymerization is essential for pollen tube growth
    • Vidali L, McKenna ST, Hepler PK (2001) Actin polymerization is essential for pollen tube growth. Mol Biol Cell 12: 2534-2545
    • (2001) Mol Biol Cell , vol.12 , pp. 2534-2545
    • Vidali, L.1    McKenna, S.T.2    Hepler, P.K.3
  • 69
    • 0033230231 scopus 로고    scopus 로고
    • A transglutaminase immunologically related to tissue transglutaminase catalyzes cross-linking of cell wall proteins in Chlamydomonas reinhardtii
    • Waffenschmidt S, Kusch T, Woessner JP (1999) A transglutaminase immunologically related to tissue transglutaminase catalyzes cross-linking of cell wall proteins in Chlamydomonas reinhardtii. Plant Physiol 121: 1003-1015
    • (1999) Plant Physiol , vol.121 , pp. 1003-1015
    • Waffenschmidt, S.1    Kusch, T.2    Woessner, J.P.3
  • 70
    • 33645015652 scopus 로고    scopus 로고
    • Effects of brefeldin A on pollen germination and tube growth: Antagonistic effects on endocytosis and secretion
    • Wang Q, Kong L, Hao H, Wang X, Lin J, Samaj J, Baluska F (2005) Effects of brefeldin A on pollen germination and tube growth: antagonistic effects on endocytosis and secretion. Plant Physiol 139: 1692-1703
    • (2005) Plant Physiol , vol.139 , pp. 1692-1703
    • Wang, Q.1    Kong, L.2    Hao, H.3    Wang, X.4    Lin, J.5    Samaj, J.6    Baluska, F.7
  • 71
    • 84860354394 scopus 로고    scopus 로고
    • Transglutaminase 2 promotes both caspase-dependent and caspase-independent apoptotic cell death via the calpain/Bax protein signaling pathway
    • Yoo JO, Lim YC, Kim YM, Ha KS (2012) Transglutaminase 2 promotes both caspase-dependent and caspase-independent apoptotic cell death via the calpain/Bax protein signaling pathway. J Biol Chem 287: 14377-14388
    • (2012) J Biol Chem , vol.287 , pp. 14377-14388
    • Yoo, J.O.1    Lim, Y.C.2    Kim, Y.M.3    Ha, K.S.4
  • 72
    • 35548939792 scopus 로고    scopus 로고
    • Cellsurface transglutaminase undergoes internalization and lysosomal degradation: An essential role for LRP1
    • Zemskov EA, Mikhailenko I, Strickland DK, Belkin AM (2007) Cellsurface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1. J Cell Sci 120: 3188-3199
    • (2007) J Cell Sci , vol.120 , pp. 3188-3199
    • Zemskov, E.A.1    Mikhailenko, I.2    Strickland, D.K.3    Belkin, A.M.4
  • 73
    • 43149115621 scopus 로고    scopus 로고
    • Vesicle trafficking dynamics and visualization of zones of exocytosis and endocytosis in tobacco pollen tubes
    • Zonia L, Munnik T (2008) Vesicle trafficking dynamics and visualization of zones of exocytosis and endocytosis in tobacco pollen tubes. J Exp Bot 59: 861-873
    • (2008) J Exp Bot , vol.59 , pp. 861-873
    • Zonia, L.1    Munnik, T.2
  • 74
    • 79959884485 scopus 로고    scopus 로고
    • Understanding pollen tube growth: The hydrodynamic model versus the cell wall model
    • Zonia L, Munnik T (2011) Understanding pollen tube growth: the hydrodynamic model versus the cell wall model. Trends Plant Sci 16: 347-352
    • (2011) Trends Plant Sci , vol.16 , pp. 347-352
    • Zonia, L.1    Munnik, T.2


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