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Volumn 14, Issue 5, 2013, Pages 551-567

Cis-Golgi Cisternal Assembly and Biosynthetic Activation Occur Sequentially in Plants and Algae

Author keywords

Arabidopsis; Cisternal assembly; COPI; COPII; Electron tomography; ER export sites; ER to Golgi transport; ERGIC; Golgi apparatus; P115 scaffold

Indexed keywords

ALPHA MANNOSIDASE; ALPHA MANNOSIDASE I; ENZYME; UNCLASSIFIED DRUG;

EID: 84876106182     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12052     Document Type: Article
Times cited : (70)

References (86)
  • 1
    • 0032433851 scopus 로고    scopus 로고
    • The curious state of the Golgi apparatus
    • Glick BS, Malhorta V. The curious state of the Golgi apparatus. Cell 1998;95:883.
    • (1998) Cell , vol.95 , pp. 883
    • Glick, B.S.1    Malhorta, V.2
  • 3
    • 70450223698 scopus 로고    scopus 로고
    • The plant Golgi apparatus: last 10 years of answered and open questions
    • Faso C, Boulaflous A, Brandizzi F. The plant Golgi apparatus: last 10 years of answered and open questions. FEBS Lett 2009;583:3752-3757.
    • (2009) FEBS Lett , vol.583 , pp. 3752-3757
    • Faso, C.1    Boulaflous, A.2    Brandizzi, F.3
  • 5
    • 77949532806 scopus 로고    scopus 로고
    • New insights into the structural mechanisms of the COPII coat
    • Russell C, Stagg SM. New insights into the structural mechanisms of the COPII coat. Traffic 2010;11:303-310.
    • (2010) Traffic , vol.11 , pp. 303-310
    • Russell, C.1    Stagg, S.M.2
  • 6
    • 0002278346 scopus 로고    scopus 로고
    • The plant Golgi apparatus: structural organization and functional properties
    • Berger EG, Roth J, editors. Basel: Birkhäuser Verlag
    • Driouich A, Staehelin LA. The plant Golgi apparatus: structural organization and functional properties. In: Berger EG, Roth J, editors. The Golgi Apparatus. Basel: Birkhäuser Verlag; 1997, pp. 275-301.
    • (1997) The Golgi Apparatus , pp. 275-301
    • Driouich, A.1    Staehelin, L.A.2
  • 7
    • 73749085462 scopus 로고    scopus 로고
    • Localization of Golgi-resident glycosyltransferases
    • Tu LN, Banfield DK. Localization of Golgi-resident glycosyltransferases. Cell Mol Life Sci 2010;67:29-41.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 29-41
    • Tu, L.N.1    Banfield, D.K.2
  • 8
    • 0001469528 scopus 로고
    • Functional compartmentation of the Golgi apparatus of plant cells. Immunocytochemical analysis of high-pressure frozen- and freeze-substituted sycamore maple suspension culture cells
    • Zhang GF, Staehelin LA. Functional compartmentation of the Golgi apparatus of plant cells. Immunocytochemical analysis of high-pressure frozen- and freeze-substituted sycamore maple suspension culture cells. Plant Physiol 1992;99:1070-1083.
    • (1992) Plant Physiol , vol.99 , pp. 1070-1083
    • Zhang, G.F.1    Staehelin, L.A.2
  • 10
    • 79751495582 scopus 로고    scopus 로고
    • Electron tomography of RabA4b-and PI-4K beta 1-labeled trans golgi network compartments in Arabidopsis
    • Kang BH, Nielsen E, Preuss ML, Mastronarde D, Staehelin LA. Electron tomography of RabA4b-and PI-4K beta 1-labeled trans golgi network compartments in Arabidopsis. Traffic 2011;12:313-329.
    • (2011) Traffic , vol.12 , pp. 313-329
    • Kang, B.H.1    Nielsen, E.2    Preuss, M.L.3    Mastronarde, D.4    Staehelin, L.A.5
  • 12
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • Bard F, Malhotra V. The formation of TGN-to-plasma-membrane transport carriers. Annu Rev Cell Dev Biol 2006;22:439-455.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 17
    • 0036799651 scopus 로고    scopus 로고
    • De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
    • Bevis BJ, Hammond AT, Reinke CA, Glick BS. De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat Cell Biol 2002;4:750-756.
    • (2002) Nat Cell Biol , vol.4 , pp. 750-756
    • Bevis, B.J.1    Hammond, A.T.2    Reinke, C.A.3    Glick, B.S.4
  • 18
    • 0000401129 scopus 로고
    • Golgi-apparatus activity and membrane flow during scale biogenesis in the green flagellate Scherffelia-Dubia (Prasinophyceae).1. Flagellar regeneration
    • Mcfadden GI, Melkonian M. Golgi-apparatus activity and membrane flow during scale biogenesis in the green flagellate Scherffelia-Dubia (Prasinophyceae).1. Flagellar regeneration. Protoplasma 1986;130:186-198.
    • (1986) Protoplasma , vol.130 , pp. 186-198
    • Mcfadden, G.I.1    Melkonian, M.2
  • 20
    • 0031935129 scopus 로고    scopus 로고
    • Effects of brefeldin A on the Golgi apparatus, the nuclear envelope, and the endoplasmic reticulum in a green alga, Scenedesmus acutus
    • Noguchi T, Watanabe H, Suzuki R. Effects of brefeldin A on the Golgi apparatus, the nuclear envelope, and the endoplasmic reticulum in a green alga, Scenedesmus acutus. Protoplasma 1998;201:202-212.
    • (1998) Protoplasma , vol.201 , pp. 202-212
    • Noguchi, T.1    Watanabe, H.2    Suzuki, R.3
  • 22
    • 26844472700 scopus 로고    scopus 로고
    • Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites
    • Yang YD, Elamawi R, Bubeck J, Pepperkok R, Ritzenthaler C, Robinson DG. Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites. Plant Cell 2005;17:1513-1531.
    • (2005) Plant Cell , vol.17 , pp. 1513-1531
    • Yang, Y.D.1    Elamawi, R.2    Bubeck, J.3    Pepperkok, R.4    Ritzenthaler, C.5    Robinson, D.G.6
  • 23
    • 29444448243 scopus 로고    scopus 로고
    • Cell cycle-dependent changes in Golgi stacks, vacuoles, clathrin-coated vesicles and multivesicular bodies in meristematic cells of Arabidopsis thaliana: a quantitative and spatial analysis
    • Segui-Simarro JM, Staehelin LA. Cell cycle-dependent changes in Golgi stacks, vacuoles, clathrin-coated vesicles and multivesicular bodies in meristematic cells of Arabidopsis thaliana: a quantitative and spatial analysis. Planta 2006;223:223-236.
    • (2006) Planta , vol.223 , pp. 223-236
    • Segui-Simarro, J.M.1    Staehelin, L.A.2
  • 26
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • DaSilva LLP, Snapp EL, Denecke J, Lippincott-Schwartz J, Hawes C, Brandizzi F. Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 2004;16:1753-1771.
    • (2004) Plant Cell , vol.16 , pp. 1753-1771
    • DaSilva, L.L.P.1    Snapp, E.L.2    Denecke, J.3    Lippincott-Schwartz, J.4    Hawes, C.5    Brandizzi, F.6
  • 29
    • 57249095874 scopus 로고    scopus 로고
    • ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix
    • Kang BH, Staehelin LA. ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix. Protoplasma 2008;234:51-64.
    • (2008) Protoplasma , vol.234 , pp. 51-64
    • Kang, B.H.1    Staehelin, L.A.2
  • 30
    • 53749093685 scopus 로고    scopus 로고
    • Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography
    • Staehelin LA, Kang BH. Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography. Plant Physiol 2008;147:1454-1468.
    • (2008) Plant Physiol , vol.147 , pp. 1454-1468
    • Staehelin, L.A.1    Kang, B.H.2
  • 31
    • 0033552616 scopus 로고    scopus 로고
    • ER to Golgi transport: requirement for p115 at a pre-Golgi VTC stage
    • Alvarez C, Fujita H, Hubbard A, Sztul E. ER to Golgi transport: requirement for p115 at a pre-Golgi VTC stage. J Cell Biol 1999;147:1205-1221.
    • (1999) J Cell Biol , vol.147 , pp. 1205-1221
    • Alvarez, C.1    Fujita, H.2    Hubbard, A.3    Sztul, E.4
  • 32
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese OW, Soderholm J, Bevis BJ, Sears IB, O'Connor J, Williamson EK, Glick BS. Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J Cell Biol 1999;145:69-81.
    • (1999) J Cell Biol , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 33
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog C, Hauri HP. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci 2006;119:2173-2183.
    • (2006) J Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 36
    • 0021905438 scopus 로고
    • Attachment of terminal N-acetylglucosamine to asparagine-linked oligosaccharides occurs in central cisternae of the Golgi stack
    • Dunphy WG, Brands R, Rothman JE. Attachment of terminal N-acetylglucosamine to asparagine-linked oligosaccharides occurs in central cisternae of the Golgi stack. Cell 1985;40:463-472.
    • (1985) Cell , vol.40 , pp. 463-472
    • Dunphy, W.G.1    Brands, R.2    Rothman, J.E.3
  • 37
    • 0019769965 scopus 로고
    • The Golgi apparatus (complex) - (1954-1981) - from artifact to center stage
    • Farquhar MG, Palade GE. The Golgi apparatus (complex) - (1954-1981) - from artifact to center stage. J Cell Biol 1981;91:775-1035.
    • (1981) J Cell Biol , vol.91 , pp. 775-1035
    • Farquhar, M.G.1    Palade, G.E.2
  • 38
    • 70350230237 scopus 로고    scopus 로고
    • Membrane traffic within the Golgi apparatus
    • Glick BS, Nakano A. Membrane traffic within the Golgi apparatus. Annu Rev Cell Dev Biol 2009;25:113-132.
    • (2009) Annu Rev Cell Dev Biol , vol.25 , pp. 113-132
    • Glick, B.S.1    Nakano, A.2
  • 39
    • 0000122262 scopus 로고
    • Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles
    • Becker B, Bölinger B, Melkonian M. Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles. Trends Cell Biol 1995;5:305-307.
    • (1995) Trends Cell Biol , vol.5 , pp. 305-307
    • Becker, B.1    Bölinger, B.2    Melkonian, M.3
  • 41
    • 1842681953 scopus 로고    scopus 로고
    • Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells
    • Marsh BJ, Volkmann N, McIntosh JR, Howell KE. Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells. Proc Natl Acad Sci USA 2004;101:5565-5570.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5565-5570
    • Marsh, B.J.1    Volkmann, N.2    McIntosh, J.R.3    Howell, K.E.4
  • 42
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman JE, Wieland FT. Protein sorting by transport vesicles. Science 1996;272:227-234.
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 43
    • 84859606183 scopus 로고    scopus 로고
    • Electron tomography reveals Rab6 is essential to the trafficking of trans-Golgi clathrin and COPI-coated vesicles and the maintenance of Golgi cisternal number
    • Storrie B, Micaroni M, Morgan GP, Jones N, Kamykowski JA, Wilkins N, Pan TH, Marsh BJ. Electron tomography reveals Rab6 is essential to the trafficking of trans-Golgi clathrin and COPI-coated vesicles and the maintenance of Golgi cisternal number. Traffic 2012;13:727-744.
    • (2012) Traffic , vol.13 , pp. 727-744
    • Storrie, B.1    Micaroni, M.2    Morgan, G.P.3    Jones, N.4    Kamykowski, J.A.5    Wilkins, N.6    Pan, T.H.7    Marsh, B.J.8
  • 44
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: functional insights from the normal rat kidney cell
    • Ladinsky MS, Mastronarde DN, McIntosh JR, Howell KE. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J Cell Biol 1999;144:1-16.
    • (1999) J Cell Biol , vol.144 , pp. 1-16
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4
  • 45
    • 33846041607 scopus 로고    scopus 로고
    • Identification and characterization of COPla- and COPlb-type vesicle classes associated with plant and algal Golgi
    • Donohoe BS, Kang BH, Staehelin LA. Identification and characterization of COPla- and COPlb-type vesicle classes associated with plant and algal Golgi. Proc Natl Acad Sci USA 2007;104:163-168.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 163-168
    • Donohoe, B.S.1    Kang, B.H.2    Staehelin, L.A.3
  • 48
    • 0034802410 scopus 로고    scopus 로고
    • Three-dimensional analysis of syncytial-type cell plates during endosperm cellularization visualized by high resolution electron tomography
    • Otegui MS, Mastronarde DN, Kang BH, Bednarek SY, Staehelin LA. Three-dimensional analysis of syncytial-type cell plates during endosperm cellularization visualized by high resolution electron tomography. Plant Cell 2001;13:2033-2051.
    • (2001) Plant Cell , vol.13 , pp. 2033-2051
    • Otegui, M.S.1    Mastronarde, D.N.2    Kang, B.H.3    Bednarek, S.Y.4    Staehelin, L.A.5
  • 49
    • 33750988212 scopus 로고    scopus 로고
    • The proteolytic processing of seed storage proteins in Arabidopsis embryo cells starts in the multivesicular bodies
    • Otegui MS, Herder R, Schulze J, Jung R, Staehelin LA. The proteolytic processing of seed storage proteins in Arabidopsis embryo cells starts in the multivesicular bodies. Plant Cell 2006;18:2567-2581.
    • (2006) Plant Cell , vol.18 , pp. 2567-2581
    • Otegui, M.S.1    Herder, R.2    Schulze, J.3    Jung, R.4    Staehelin, L.A.5
  • 50
    • 0029808891 scopus 로고    scopus 로고
    • The secretory pathway of protists: spatial and functional organization and evolution
    • Becker B, Melkonian M. The secretory pathway of protists: spatial and functional organization and evolution. Microbiol Rev 1996;60:697-721.
    • (1996) Microbiol Rev , vol.60 , pp. 697-721
    • Becker, B.1    Melkonian, M.2
  • 51
    • 0022163967 scopus 로고
    • Progress in unraveling pathways of Golgi traffic
    • Farquhar MG. Progress in unraveling pathways of Golgi traffic. Annu Rev Cell Biol 1985;1:447-488.
    • (1985) Annu Rev Cell Biol , vol.1 , pp. 447-488
    • Farquhar, M.G.1
  • 52
    • 0014782559 scopus 로고
    • Scale formation in Chrysophycean Algae .1. Cellulosic and noncellulosic wall components made by Golgi apparatus
    • Brown RM, Franke WW, Kleinig H, Falk H, Sitte P. Scale formation in Chrysophycean Algae .1. Cellulosic and noncellulosic wall components made by Golgi apparatus. J Cell Biol 1970;45:246.
    • (1970) J Cell Biol , vol.45 , pp. 246
    • Brown, R.M.1    Franke, W.W.2    Kleinig, H.3    Falk, H.4    Sitte, P.5
  • 53
    • 0000401130 scopus 로고
    • Golgi-apparatus activity and membrane flow during scale biogenesis in the green flagellate Scherffelia-Dubia (Prasinophyceae). 2. Cell-wall secretion and assembly
    • Mcfadden GI, Preisig HR, Melkonian M. Golgi-apparatus activity and membrane flow during scale biogenesis in the green flagellate Scherffelia-Dubia (Prasinophyceae). 2. Cell-wall secretion and assembly. Protoplasma 1986;131:174-184.
    • (1986) Protoplasma , vol.131 , pp. 174-184
    • Mcfadden, G.I.1    Preisig, H.R.2    Melkonian, M.3
  • 54
    • 84981656290 scopus 로고
    • A light and electron-microscopic study of Scherffelia-Dubia, a new member of the scaly green flagellates (Prasinophyceae)
    • Melkonian M, Preisig HR. A light and electron-microscopic study of Scherffelia-Dubia, a new member of the scaly green flagellates (Prasinophyceae). Nord J Bot 1986;6:235-256.
    • (1986) Nord J Bot , vol.6 , pp. 235-256
    • Melkonian, M.1    Preisig, H.R.2
  • 55
    • 0025697919 scopus 로고
    • Macromolecular differentiation of Golgi stacks in root tips of Arabidopsis and Nicotiana seedlings as visualized in high pressure frozen and freeze-substituted samples
    • Staehelin LA, Giddings TH, Kiss JZ, Sack FD. Macromolecular differentiation of Golgi stacks in root tips of Arabidopsis and Nicotiana seedlings as visualized in high pressure frozen and freeze-substituted samples. Protoplasma 1990;157:75-91.
    • (1990) Protoplasma , vol.157 , pp. 75-91
    • Staehelin, L.A.1    Giddings, T.H.2    Kiss, J.Z.3    Sack, F.D.4
  • 56
    • 0036851205 scopus 로고    scopus 로고
    • Characterization of AtCDC48. Evidence for multiple membrane fusion mechanisms at the plane of cell division in plants
    • Rancour DM, Dickey CE, Park S, Bednarek SY. Characterization of AtCDC48. Evidence for multiple membrane fusion mechanisms at the plane of cell division in plants. Plant Physiol 2002;130:1241-1253.
    • (2002) Plant Physiol , vol.130 , pp. 1241-1253
    • Rancour, D.M.1    Dickey, C.E.2    Park, S.3    Bednarek, S.Y.4
  • 57
    • 0033213370 scopus 로고    scopus 로고
    • V-ATPase is a major component of the Golgi complex in the scaly green flagellate Scherffelia dubia
    • Grunow A, Rusing M, Becker B, Melkonian M. V-ATPase is a major component of the Golgi complex in the scaly green flagellate Scherffelia dubia. Protist 1999;150:265-281.
    • (1999) Protist , vol.150 , pp. 265-281
    • Grunow, A.1    Rusing, M.2    Becker, B.3    Melkonian, M.4
  • 58
    • 0029857911 scopus 로고    scopus 로고
    • Monensin-induced redistribution of enzymes and products from Golgi stacks to swollen vesicles in plant cells
    • Zhang GF, Driouich A, Staehelin LA. Monensin-induced redistribution of enzymes and products from Golgi stacks to swollen vesicles in plant cells. Eur J Cell Biol 1996;71:332-340.
    • (1996) Eur J Cell Biol , vol.71 , pp. 332-340
    • Zhang, G.F.1    Driouich, A.2    Staehelin, L.A.3
  • 59
    • 80055094003 scopus 로고    scopus 로고
    • Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells
    • Hassinen A, Pujol FM, Kokkonen N, Pieters C, Kihlstrom M, Korhonen K, Kellokumpu S. Functional organization of Golgi N- and O-glycosylation pathways involves pH-dependent complex formation that is impaired in cancer cells. J Biol Chem 2011;286:38329-38340.
    • (2011) J Biol Chem , vol.286 , pp. 38329-38340
    • Hassinen, A.1    Pujol, F.M.2    Kokkonen, N.3    Pieters, C.4    Kihlstrom, M.5    Korhonen, K.6    Kellokumpu, S.7
  • 60
    • 84968620640 scopus 로고
    • Membrane flow via the Golgi apparatus of higher plant cells
    • Robinson DG, Kristen U. Membrane flow via the Golgi apparatus of higher plant cells. Int Rev Cytol 1982;77:89-127.
    • (1982) Int Rev Cytol , vol.77 , pp. 89-127
    • Robinson, D.G.1    Kristen, U.2
  • 61
    • 0029842198 scopus 로고    scopus 로고
    • Scale-associated glycoproteins of Scherffelia dubia (Chlorophyta) form high-molecular-weight complexes between the scale layers and the flagellar membrane
    • Becker B, Perasso L, Kammann A, Salzburg N, Melkonian M. Scale-associated glycoproteins of Scherffelia dubia (Chlorophyta) form high-molecular-weight complexes between the scale layers and the flagellar membrane. Planta 1996;199:503-510.
    • (1996) Planta , vol.199 , pp. 503-510
    • Becker, B.1    Perasso, L.2    Kammann, A.3    Salzburg, N.4    Melkonian, M.5
  • 62
    • 44149113708 scopus 로고    scopus 로고
    • Golgi transporters: opening the gate to cell wall polysaccharide biosynthesis
    • Reyes F, Orellana A. Golgi transporters: opening the gate to cell wall polysaccharide biosynthesis. Curr Opin Plant Biol 2008;11:244-251.
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 244-251
    • Reyes, F.1    Orellana, A.2
  • 63
    • 0031010772 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, nucleotide sulfate and ATP in the Golgi apparatus
    • Abeijon C, Mandon EC, Hirschberg CB. Transporters of nucleotide sugars, nucleotide sulfate and ATP in the Golgi apparatus. Trends Biochem Sci 1997;22:203-207.
    • (1997) Trends Biochem Sci , vol.22 , pp. 203-207
    • Abeijon, C.1    Mandon, E.C.2    Hirschberg, C.B.3
  • 65
    • 78650121974 scopus 로고    scopus 로고
    • Subcompartment localization of the side chain xyloglucan-synthesizing enzymes within Golgi stacks of tobacco suspension-cultured cells
    • Chevalier L, Bernard S, Ramdani Y, Lamour R, Bardor M, Lerouge P, Follet-Gueye ML, Driouich A. Subcompartment localization of the side chain xyloglucan-synthesizing enzymes within Golgi stacks of tobacco suspension-cultured cells. Plant J 2010;64:977-989.
    • (2010) Plant J , vol.64 , pp. 977-989
    • Chevalier, L.1    Bernard, S.2    Ramdani, Y.3    Lamour, R.4    Bardor, M.5    Lerouge, P.6    Follet-Gueye, M.L.7    Driouich, A.8
  • 66
    • 79953185070 scopus 로고    scopus 로고
    • Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants
    • Schoberer J, Strasser R. Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants. Mol Plant 2011;4:220-228.
    • (2011) Mol Plant , vol.4 , pp. 220-228
    • Schoberer, J.1    Strasser, R.2
  • 67
    • 0842287521 scopus 로고    scopus 로고
    • Protein localization in the plant Golgi apparatus and the trans-Golgi network
    • Saint-Jore-Dupas C, Gomord V, Paris N. Protein localization in the plant Golgi apparatus and the trans-Golgi network. Cell Mol Life Sci 2004;61:159-171.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 159-171
    • Saint-Jore-Dupas, C.1    Gomord, V.2    Paris, N.3
  • 68
    • 0026078287 scopus 로고
    • Spatial organization of the assembly pathways of glycoproteins and complex polysaccharides in the Golgi apparatus of plants
    • Moore PJ, Swords KMM, Lynch MA, Staehelin LA. Spatial organization of the assembly pathways of glycoproteins and complex polysaccharides in the Golgi apparatus of plants. J Cell Biol 1991;112:589-602.
    • (1991) J Cell Biol , vol.112 , pp. 589-602
    • Moore, P.J.1    Swords, K.M.M.2    Lynch, M.A.3    Staehelin, L.A.4
  • 69
    • 0028003272 scopus 로고
    • Secretion of cell wall polysaccharides in Vicia root hairs
    • Sherrier DJ, VandenBosch KA. Secretion of cell wall polysaccharides in Vicia root hairs. Plant J 1994;5:185-195.
    • (1994) Plant J , vol.5 , pp. 185-195
    • Sherrier, D.J.1    VandenBosch, K.A.2
  • 70
    • 0022653966 scopus 로고
    • Advances in ultra-rapid freezing for the preservation of cellular ultrastructure
    • Gilkey JC, Staehelin LA. Advances in ultra-rapid freezing for the preservation of cellular ultrastructure. J Electr Microsc Technol 1986;3:177-210.
    • (1986) J Electr Microsc Technol , vol.3 , pp. 177-210
    • Gilkey, J.C.1    Staehelin, L.A.2
  • 71
    • 70349247790 scopus 로고    scopus 로고
    • Validating the location of fluorescent protein fusions in the endomembrane system
    • Moore I, Murphy A. Validating the location of fluorescent protein fusions in the endomembrane system. Plant Cell 2009;21:1632-1636.
    • (2009) Plant Cell , vol.21 , pp. 1632-1636
    • Moore, I.1    Murphy, A.2
  • 72
    • 0023733211 scopus 로고
    • Identification, by a monoclonal-antibody, of a 53-kd protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi-apparatus
    • Schweizer A, Fransen JAM, Bachi T, Ginsel L, Hauri HP. Identification, by a monoclonal-antibody, of a 53-kd protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi-apparatus. J Cell Biol 1988;107:1643-1653.
    • (1988) J Cell Biol , vol.107 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.M.2    Bachi, T.3    Ginsel, L.4    Hauri, H.P.5
  • 73
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh SI, Rowe T, Balch WE. The organization of endoplasmic reticulum export complexes. J Cell Biol 1996;135:19-35.
    • (1996) J Cell Biol , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 74
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham AK, Munro S. Long coiled-coil proteins and membrane traffic. Biochim Biophys Acta 2003;1641:71-85.
    • (2003) Biochim Biophys Acta , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 75
    • 0034698202 scopus 로고    scopus 로고
    • Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion
    • Allan BB, Moyer BD, Balch WE. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science 2000;289:444-448.
    • (2000) Science , vol.289 , pp. 444-448
    • Allan, B.B.1    Moyer, B.D.2    Balch, W.E.3
  • 76
    • 21844454722 scopus 로고    scopus 로고
    • A cryptic Rab1-binding site in the p115 tethering protein
    • Beard M, Satoh A, Shorter J, Warren G. A cryptic Rab1-binding site in the p115 tethering protein. J Biol Chem 2005;280:25840-25848.
    • (2005) J Biol Chem , vol.280 , pp. 25840-25848
    • Beard, M.1    Satoh, A.2    Shorter, J.3    Warren, G.4
  • 78
    • 0035071569 scopus 로고    scopus 로고
    • Illuminating the secretory pathway: when do we need vesicles?
    • Stephens DJ, Pepperkok R. Illuminating the secretory pathway: when do we need vesicles? J Cell Sci 2001;114:1053-1059.
    • (2001) J Cell Sci , vol.114 , pp. 1053-1059
    • Stephens, D.J.1    Pepperkok, R.2
  • 79
  • 80
    • 2442640305 scopus 로고    scopus 로고
    • Predicting function from structure: 3D structure studies of the mammalian Golgi complex
    • Mogelsvang S, Marsh BJ, Ladinsky MS, Howell KE. Predicting function from structure: 3D structure studies of the mammalian Golgi complex. Traffic 2004;5:338-345.
    • (2004) Traffic , vol.5 , pp. 338-345
    • Mogelsvang, S.1    Marsh, B.J.2    Ladinsky, M.S.3    Howell, K.E.4
  • 81
    • 0027174523 scopus 로고
    • Cell-type dependent variations in the subcellular-distribution of alpha-mannosidase-I and alpha-mannosidase-II
    • Velasco A, Hendricks L, Moremen KW, Tulsiani DRP, Touster O, Farquhar MG. Cell-type dependent variations in the subcellular-distribution of alpha-mannosidase-I and alpha-mannosidase-II. J Cell Biol 1993;122:39-51.
    • (1993) J Cell Biol , vol.122 , pp. 39-51
    • Velasco, A.1    Hendricks, L.2    Moremen, K.W.3    Tulsiani, D.R.P.4    Touster, O.5    Farquhar, M.G.6
  • 82
    • 0028905820 scopus 로고
    • Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
    • Rabouille C, Hui N, Hunte F, Kieckbusch R, Berger EG, Warren G, Nilsson T. Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J Cell Sci 1995;108:1617-1627.
    • (1995) J Cell Sci , vol.108 , pp. 1617-1627
    • Rabouille, C.1    Hui, N.2    Hunte, F.3    Kieckbusch, R.4    Berger, E.G.5    Warren, G.6    Nilsson, T.7
  • 83
    • 1842813514 scopus 로고    scopus 로고
    • Electron tomographic analysis of somatic cell plate formation in meristematic cells of Arabidopsis preserved by high-pressure freezing
    • Segui-Simarro JM, Austin JR, White EA, Staehelin LA. Electron tomographic analysis of somatic cell plate formation in meristematic cells of Arabidopsis preserved by high-pressure freezing. Plant Cell 2004;16:836-856.
    • (2004) Plant Cell , vol.16 , pp. 836-856
    • Segui-Simarro, J.M.1    Austin, J.R.2    White, E.A.3    Staehelin, L.A.4
  • 84
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN. Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol 2005;152:36-51.
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 85
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: an approach with alignment methods that preserve resolution
    • Mastronarde DN. Dual-axis tomography: an approach with alignment methods that preserve resolution. J Struct Biol 1997;120:343-352.
    • (1997) J Struct Biol , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 86
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer JR, Mastronarde DN, McIntosh JR. Computer visualization of three-dimensional image data using IMOD. J Struct Biol 1996;116:71-76.
    • (1996) J Struct Biol , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.