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Volumn 49, Issue 2, 2017, Pages 186-201

Different Golgi ultrastructure across species and tissues: Implications under functional and pathological conditions, and an attempt at classification

Author keywords

Clathrin; COPI; COPII; Golgi classification; Golgi complex; Golgi structure; Intracellular transport; TGN

Indexed keywords

CLASSIFICATION; GOLGI COMPLEX; HUMAN; INTRACELLULAR TRANSPORT; LIPID TRANSPORT; MORPHOLOGY; NONHUMAN; PROTEIN GLYCOSYLATION; PROTEIN TARGETING; REVIEW; SECRETORY PATHWAY; ULTRASTRUCTURE; ANIMAL; ANTIBODY SPECIFICITY; GENETICS; MOLECULAR EVOLUTION; PATHOLOGY; SPECIES DIFFERENCE;

EID: 85008413093     PISSN: 00408166     EISSN: 15323072     Source Type: Journal    
DOI: 10.1016/j.tice.2016.12.002     Document Type: Review
Times cited : (26)

References (179)
  • 2
    • 0033548165 scopus 로고    scopus 로고
    • Cargo can modulate COPII vesicle formation from the endoplasmic reticulum
    • Aridor, M., Bannykh, S.I., Rowe, T., Balch, W.E., Cargo can modulate COPII vesicle formation from the endoplasmic reticulum. J. Biol. Chem. 274 (1999), 4389–4399.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4389-4399
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 4
    • 84920587931 scopus 로고    scopus 로고
    • Golgi apparatus and protein trafficking in Alzheimer's disease
    • Baloyannis, S.J., Golgi apparatus and protein trafficking in Alzheimer's disease. J. Alzheimers Dis. 42:Suppl. 3 (2014), S153–162.
    • (2014) J. Alzheimers Dis. , vol.42 , pp. S153-162
    • Baloyannis, S.J.1
  • 5
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • Bannykh, S.I., Rowe, T., Balch, W.E., The organization of endoplasmic reticulum export complexes. J. Cell Biol. 135 (1996), 19–35.
    • (1996) J. Cell Biol. , vol.135 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 7
    • 84944454078 scopus 로고    scopus 로고
    • Endomembrane control of cell polarity: relevance to cancer
    • Baschieri, F., Farhan, H., Endomembrane control of cell polarity: relevance to cancer. Small GT Pases 6:2 (2015), 104–107.
    • (2015) Small GT Pases , vol.6 , Issue.2 , pp. 104-107
    • Baschieri, F.1    Farhan, H.2
  • 8
    • 84928036492 scopus 로고    scopus 로고
    • Loss of GM130 in breast cancer cells and its effects on cell migration, invasion and polarity
    • Baschieri, F., Uetz-von Allmen, E., Legler, D.F., Farhan, H., Loss of GM130 in breast cancer cells and its effects on cell migration, invasion and polarity. ABBV Cell Cycle 14:8 (2015), 1139–1147.
    • (2015) ABBV Cell Cycle , vol.14 , Issue.8 , pp. 1139-1147
    • Baschieri, F.1    Uetz-von Allmen, E.2    Legler, D.F.3    Farhan, H.4
  • 9
    • 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. 60 (1996), 697–721.
    • (1996) Microbiol. Rev. , vol.60 , pp. 697-721
    • Becker, B.1    Melkonian, M.2
  • 10
    • 33750332048 scopus 로고    scopus 로고
    • Golgi structural stability and biogenesis depend on associated PKA activity
    • Bejarano, E., Cabrera, M., Vega, L., Hidalgo, J., Velasco, A., Golgi structural stability and biogenesis depend on associated PKA activity. J. Cell Sci. 119 (2006), 3764–3775.
    • (2006) J. Cell Sci. , vol.119 , pp. 3764-3775
    • Bejarano, E.1    Cabrera, M.2    Vega, L.3    Hidalgo, J.4    Velasco, A.5
  • 11
    • 0034814332 scopus 로고    scopus 로고
    • Structure and division of the Golgi complex in Trichomonas vaginalis and Tritrichomonas foetus
    • Benchimol, M., Ribeiro, K.C., Mariante, R.M., Alderete, J.F., Structure and division of the Golgi complex in Trichomonas vaginalis and Tritrichomonas foetus. Eur. J. Cell Biol. 80:9 (2001), 593–607.
    • (2001) Eur. J. Cell Biol. , vol.80 , Issue.9 , pp. 593-607
    • Benchimol, M.1    Ribeiro, K.C.2    Mariante, R.M.3    Alderete, J.F.4
  • 12
    • 0036828838 scopus 로고    scopus 로고
    • Models of intracellular transport and evolution of the Golgi complex
    • Beznoussenko, G.V., Mironov, A.A., Models of intracellular transport and evolution of the Golgi complex. Anat. Rec. 268 (2002), 226–238.
    • (2002) Anat. Rec. , vol.268 , pp. 226-238
    • Beznoussenko, G.V.1    Mironov, A.A.2
  • 16
    • 84984919831 scopus 로고    scopus 로고
    • Three-dimensional and immune electron microscopic analysis of the secretory pathway in Saccharomyces cerevisiae
    • Beznoussenko, G.V., Ragnini-Wilson, A., Wilson, C., Mironov, A.A., Three-dimensional and immune electron microscopic analysis of the secretory pathway in Saccharomyces cerevisiae. Histochem. Cell Biol. Sep., 3, 2016.
    • (2016) Histochem. Cell Biol. Sep. , vol.3
    • Beznoussenko, G.V.1    Ragnini-Wilson, A.2    Wilson, C.3    Mironov, A.A.4
  • 17
    • 39049174400 scopus 로고    scopus 로고
    • Electron-tomographic analysis of the Golgi complex structure in cultured cells
    • Beznusenko, G.V., Sesorova, I.S., Banin, V.V., Electron-tomographic analysis of the Golgi complex structure in cultured cells. Morfologiia 129:3 (2006), 41–44.
    • (2006) Morfologiia , vol.129 , Issue.3 , pp. 41-44
    • Beznusenko, G.V.1    Sesorova, I.S.2    Banin, V.V.3
  • 18
    • 33645424953 scopus 로고
    • Anatomy, ultrastructure and morphometry of the liver
    • H. Glaumann T. Peters C. Redman Academic New York
    • Blouin, A., Anatomy, ultrastructure and morphometry of the liver. Glaumann, H., Peters, T., Redman, C., (eds.) Plasma Protein Secretion by the Liver, 1983, Academic, New York, 31–53.
    • (1983) Plasma Protein Secretion by the Liver , pp. 31-53
    • Blouin, A.1
  • 22
    • 84923169332 scopus 로고    scopus 로고
    • GOLPH3 links the Golgi, DNA damage, and cancer
    • Buschman, M.D., Rahajeng, J., Field, S.J., GOLPH3 links the Golgi, DNA damage, and cancer. Cancer Res. 75:4 (2015), 624–627.
    • (2015) Cancer Res. , vol.75 , Issue.4 , pp. 624-627
    • Buschman, M.D.1    Rahajeng, J.2    Field, S.J.3
  • 23
    • 75449112263 scopus 로고    scopus 로고
    • Aiming for invadopodia: organizing polarized delivery at sites of invasion
    • Caldieri, G., Buccione, R., Aiming for invadopodia: organizing polarized delivery at sites of invasion. Trends Cell Biol. 20:2 (2010), 64–70.
    • (2010) Trends Cell Biol. , vol.20 , Issue.2 , pp. 64-70
    • Caldieri, G.1    Buccione, R.2
  • 24
    • 0033744835 scopus 로고    scopus 로고
    • Ultrastructural evidence of smooth endoplasmic reticulum and golgi-like elements in Entamoeba histolytica and Entamoeba dispar
    • Chávez-Munguía, B., Espinosa-Cantellano, M., Castañón, G., Martínez-Palomo, A., Ultrastructural evidence of smooth endoplasmic reticulum and golgi-like elements in Entamoeba histolytica and Entamoeba dispar. Arch. Med. Res. 31:4 Suppl (2000), S165–167.
    • (2000) Arch. Med. Res. , vol.31 , Issue.4 , pp. S165-167
    • Chávez-Munguía, B.1    Espinosa-Cantellano, M.2    Castañón, G.3    Martínez-Palomo, A.4
  • 25
    • 0029946280 scopus 로고    scopus 로고
    • Organization of the endoplasmic reticulum-Golgi system is related to the state of enterocytic differentiation of human HT-29 cells
    • Chazaud, B., Muriel, M.P., Aubery, M., Decastel, M., Organization of the endoplasmic reticulum-Golgi system is related to the state of enterocytic differentiation of human HT-29 cells. Differentiation 60:3 (1996), 179–191.
    • (1996) Differentiation , vol.60 , Issue.3 , pp. 179-191
    • Chazaud, B.1    Muriel, M.P.2    Aubery, M.3    Decastel, M.4
  • 26
    • 0028081835 scopus 로고
    • Connections between the various elements of the cis- and mid-compartments of the Golgi apparatus of early rat spermatids
    • Clermont, Y., Rambourg, A., Hermo, L., Connections between the various elements of the cis- and mid-compartments of the Golgi apparatus of early rat spermatids. Anat. Rec. 240:4 (1994), 469–480.
    • (1994) Anat. Rec. , vol.240 , Issue.4 , pp. 469-480
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 27
    • 0029040979 scopus 로고
    • Trans-Golgi network (TGN) of different cell types, three-dimensional structural characteristics and variability
    • Clermont, Y., Rambourg, A., Hermo, L., Trans-Golgi network (TGN) of different cell types, three-dimensional structural characteristics and variability. Anat. Rec. 242:3 (1995), 289–301.
    • (1995) Anat. Rec. , vol.242 , Issue.3 , pp. 289-301
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 28
    • 34249065537 scopus 로고    scopus 로고
    • The Golgi mitotic checkpoint is controlled by BARS-dependent fission of the Golgi ribbon into separate stacks in G2
    • Colanzi, A., Hidalgo Carcedo, C., Persico, A., Cericola, C., Turacchio, G., Bonazzi, M., Luini, A., Corda, D., The Golgi mitotic checkpoint is controlled by BARS-dependent fission of the Golgi ribbon into separate stacks in G2. EMBO J. 26 (2007), 2465–2476.
    • (2007) EMBO J. , vol.26 , pp. 2465-2476
    • Colanzi, A.1    Hidalgo Carcedo, C.2    Persico, A.3    Cericola, C.4    Turacchio, G.5    Bonazzi, M.6    Luini, A.7    Corda, D.8
  • 29
    • 74349098417 scopus 로고    scopus 로고
    • The ultrastructure of malpighian tubules and the chemical composition of the cocoon of Aeolothrips intermedius Bagnall (Thysanoptera)
    • Conti, B., Berti, F., Mercati, D., Giusti, F., Dallai, R., The ultrastructure of malpighian tubules and the chemical composition of the cocoon of Aeolothrips intermedius Bagnall (Thysanoptera). J. Morphol. 271:2 (2010), 244–254.
    • (2010) J. Morphol. , vol.271 , Issue.2 , pp. 244-254
    • Conti, B.1    Berti, F.2    Mercati, D.3    Giusti, F.4    Dallai, R.5
  • 30
    • 84878155422 scopus 로고    scopus 로고
    • Silencing of the mammalian Sar1 isoforms reveals COPII-independent protein sorting and transport
    • Cutrona, M.B., Beznoussenko, G.V., Fusella, A., Martella, O., Moral, P., Mironov, A.A., Silencing of the mammalian Sar1 isoforms reveals COPII-independent protein sorting and transport. Traffic 14:6 (2013), 691–708.
    • (2013) Traffic , vol.14 , Issue.6 , pp. 691-708
    • Cutrona, M.B.1    Beznoussenko, G.V.2    Fusella, A.3    Martella, O.4    Moral, P.5    Mironov, A.A.6
  • 33
    • 33645515267 scopus 로고    scopus 로고
    • Physical factors that affect the number and size of Golgi cisternae
    • Derganc, J., Mironov, A.A., Svetina, S., Physical factors that affect the number and size of Golgi cisternae. Traffic 7:1 (2006), 85–96.
    • (2006) Traffic , vol.7 , Issue.1 , pp. 85-96
    • Derganc, J.1    Mironov, A.A.2    Svetina, S.3
  • 34
  • 35
    • 33846041607 scopus 로고    scopus 로고
    • Identification and characterization of COPIa- and COPIb-type vesicle classes associated with plant and algal Golgi
    • Donohoe, B.S., Kang, B.-H., Staehelin, L.A., Identification and characterization of COPIa- and COPIb-type vesicle classes associated with plant and algal Golgi. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 163–168.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 163-168
    • Donohoe, B.S.1    Kang, B.-H.2    Staehelin, L.A.3
  • 36
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • da Silva, L.L., Snapp, E.L., 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 16 (2004), 1753–1771.
    • (2004) Plant Cell , vol.16 , pp. 1753-1771
    • da Silva, L.L.1    Snapp, E.L.2    Denecke, J.3    Lippincott-Schwartz, J.4    Hawes, C.5    Brandizzi, F.6
  • 37
    • 84862303678 scopus 로고    scopus 로고
    • The structures of COPI-coated vesicles reveal alternate coatomer conformations and interactions
    • Faini, M., Prinz, S., Beck, R., Schorb, M., Riches, J.D., Bacia, K., Brügger, B., Wieland, F.T., Briggs, J.A., The structures of COPI-coated vesicles reveal alternate coatomer conformations and interactions. Science 336:6087 (2012), 1451–1454.
    • (2012) Science , vol.336 , Issue.6087 , pp. 1451-1454
    • Faini, M.1    Prinz, S.2    Beck, R.3    Schorb, M.4    Riches, J.D.5    Bacia, K.6    Brügger, B.7    Wieland, F.T.8    Briggs, J.A.9
  • 38
    • 79952709066 scopus 로고    scopus 로고
    • Membrane trafficking and organelle biogenesis in Giardia lamblia, use it or lose it
    • Faso, C., Hehl, A.B., Membrane trafficking and organelle biogenesis in Giardia lamblia, use it or lose it. Int. J. Parasitol. 41:5 (2011), 471–480.
    • (2011) Int. J. Parasitol. , vol.41 , Issue.5 , pp. 471-480
    • Faso, C.1    Hehl, A.B.2
  • 39
    • 0028019867 scopus 로고
    • Kinesin-mediated organelle translocation revealed by specific cellular manipulations
    • Feiguin, F., Ferreira, A., Kosik, K.S., Caceres, A., Kinesin-mediated organelle translocation revealed by specific cellular manipulations. J. Cell Biol. 127:4 (1994), 1021–1039.
    • (1994) J. Cell Biol. , vol.127 , Issue.4 , pp. 1021-1039
    • Feiguin, F.1    Ferreira, A.2    Kosik, K.S.3    Caceres, A.4
  • 41
    • 84872870355 scopus 로고    scopus 로고
    • Small molecule targeting Cdc42-intersectin interaction disrupts Golgi organization and suppresses cell motility
    • Friesland, A., Zhao, Y., Chen, Y.H., Wang, L., Zhou, H., Lu, Q., Small molecule targeting Cdc42-intersectin interaction disrupts Golgi organization and suppresses cell motility. Proc. Natl. Acad. Sci. U. S. A. 110:4 (2013), 1261–1266.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , Issue.4 , pp. 1261-1266
    • Friesland, A.1    Zhao, Y.2    Chen, Y.H.3    Wang, L.4    Zhou, H.5    Lu, Q.6
  • 42
    • 84876116739 scopus 로고    scopus 로고
    • Segregation of the Qb-SNAREs GS27 and GS28 into Golgi vesicles regulates intra-Golgi transport
    • Fusella, A., Micaroni, M., Di Giandomenico, D., Mironov, A.A., Beznoussenko, G.V., Segregation of the Qb-SNAREs GS27 and GS28 into Golgi vesicles regulates intra-Golgi transport. Traffic 14:5 (2013), 568–584.
    • (2013) Traffic , vol.14 , Issue.5 , pp. 568-584
    • Fusella, A.1    Micaroni, M.2    Di Giandomenico, D.3    Mironov, A.A.4    Beznoussenko, G.V.5
  • 43
    • 0004165783 scopus 로고
    • Ultrastructural Pathology of the Cell and Matrix
    • Butterworths London et al
    • Ghadialli, F.N., Ultrastructural Pathology of the Cell and Matrix. 1982, Butterworths, London et al.
    • (1982)
    • Ghadialli, F.N.1
  • 44
    • 84872184210 scopus 로고    scopus 로고
    • On the ultrastructural organization of Trypanosoma cruzi using cryopreparation methods and electron tomography
    • Girard-Dias, W., Alcântara, C.L., Cunha-E-Silva, N., de Souza, W., Miranda, K., On the ultrastructural organization of Trypanosoma cruzi using cryopreparation methods and electron tomography. Histochem. Cell Biol. 138:6 (2012), 821–831.
    • (2012) Histochem. Cell Biol. , vol.138 , Issue.6 , pp. 821-831
    • Girard-Dias, W.1    Alcântara, C.L.2    Cunha-E-Silva, N.3    de Souza, W.4    Miranda, K.5
  • 45
    • 84862492324 scopus 로고    scopus 로고
    • Models for Golgi traffic, a critical assessment
    • (pii)
    • Glick, B.S., Luini, A., Models for Golgi traffic, a critical assessment. Cold Spring Harb. Perspect. Biol., 3(11), 2011, a005215 (pii).
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , Issue.11 , pp. a005215
    • Glick, B.S.1    Luini, A.2
  • 46
    • 70350230237 scopus 로고    scopus 로고
    • Membrane traffic within the Golgi apparatus
    • Glick, B.S., Nakano, A., Membrane traffic within the Golgi apparatus. Annu. Rev. Cell Dev. Biol. 25 (2009), 113–132.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 113-132
    • Glick, B.S.1    Nakano, A.2
  • 47
    • 0022975133 scopus 로고
    • The trans Golgi network, sorting at the exit site of the Golgi complex
    • Griffiths, G., Simons, K., The trans Golgi network, sorting at the exit site of the Golgi complex. Science 34 (1986), 438–443.
    • (1986) Science , vol.34 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 49
    • 0028984235 scopus 로고
    • Immunocytochemical localization of beta-COP to the ER-Golgi boundary and the TGN
    • Griffiths, G., Pepperkok, R., Locker, J.K., Kreis, T.E., Immunocytochemical localization of beta-COP to the ER-Golgi boundary and the TGN. J. Cell Sci. 108:Pt. 8 (1995), 2839–2856.
    • (1995) J. Cell Sci. , vol.108 , pp. 2839-2856
    • Griffiths, G.1    Pepperkok, R.2    Locker, J.K.3    Kreis, T.E.4
  • 50
    • 0032845689 scopus 로고    scopus 로고
    • The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii
    • Hager, K.M., Striepen, B., Tilney, L.G., Roos, D.S., The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii. J. Cell Sci. 112:Pt. 16 (1999), 2631–2638.
    • (1999) J. Cell Sci. , vol.112 , pp. 2631-2638
    • Hager, K.M.1    Striepen, B.2    Tilney, L.G.3    Roos, D.S.4
  • 51
    • 3142518032 scopus 로고    scopus 로고
    • Secretory protein trafficking in Giardia intestinalis
    • Hehl, A.B., Marti, M., Secretory protein trafficking in Giardia intestinalis. Mol. Microbiol. 53 (2004), 19–28.
    • (2004) Mol. Microbiol. , vol.53 , pp. 19-28
    • Hehl, A.B.1    Marti, M.2
  • 52
    • 40349094722 scopus 로고    scopus 로고
    • 3-D ultrastructure of O. tauri: electron cryotomography of an entire eukaryotic cell
    • Henderson, G.P., Gan, L., Jensen, G.J., 3-D ultrastructure of O. tauri: electron cryotomography of an entire eukaryotic cell. PLoS One, 2(8), 2007, e749.
    • (2007) PLoS One , vol.2 , Issue.8 , pp. e749
    • Henderson, G.P.1    Gan, L.2    Jensen, G.J.3
  • 53
    • 0031809401 scopus 로고    scopus 로고
    • The structure of the Golgi apparatus: a sperm's eye view in principal epithelial cells of the rat epididymis
    • Hermo, L., Smith, C.E., The structure of the Golgi apparatus: a sperm's eye view in principal epithelial cells of the rat epididymis. Histochem. Cell Biol. 109:5–6 (1998), 431–447.
    • (1998) Histochem. Cell Biol. , vol.109 , Issue.5-6 , pp. 431-447
    • Hermo, L.1    Smith, C.E.2
  • 54
    • 0026034932 scopus 로고
    • Golgi apparatus of epithelial principal cells of the epididymal initial segment of the rat: structure, relationship with endoplasmic reticulum, and role in the formation of secretory vesicles
    • Hermo, L., Green, H., Clermont, Y., Golgi apparatus of epithelial principal cells of the epididymal initial segment of the rat: structure, relationship with endoplasmic reticulum, and role in the formation of secretory vesicles. Anat. Rec. 229:2 (1991), 159–176.
    • (1991) Anat. Rec. , vol.229 , Issue.2 , pp. 159-176
    • Hermo, L.1    Green, H.2    Clermont, Y.3
  • 56
    • 0033214664 scopus 로고    scopus 로고
    • Three-dimensional structure of the Golgi apparatus in mouse spermatids, a scanning electron microscopic study
    • Ho, H.C., Tang, C.Y., Suarez, S.S., Three-dimensional structure of the Golgi apparatus in mouse spermatids, a scanning electron microscopic study. Anat. Rec. 256:2 (1999), 189–194.
    • (1999) Anat. Rec. , vol.256 , Issue.2 , pp. 189-194
    • Ho, H.C.1    Tang, C.Y.2    Suarez, S.S.3
  • 58
    • 0038382300 scopus 로고    scopus 로고
    • Dual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging
    • Horton, A.C., Ehlers, M.D., Dual modes of endoplasmic reticulum-to-Golgi transport in dendrites revealed by live-cell imaging. J. Neurosci. 23:15 (2003), 6188–6199.
    • (2003) J. Neurosci. , vol.23 , Issue.15 , pp. 6188-6199
    • Horton, A.C.1    Ehlers, M.D.2
  • 59
    • 34547961491 scopus 로고    scopus 로고
    • Brefeldin A action and recovery in Chlamydomonas are rapid and involve fusion and fission of Golgi cisternae
    • Hummel, E., Schmickl, R., Hinz, G., Hillmer, S., Robinson, D.G., Brefeldin A action and recovery in Chlamydomonas are rapid and involve fusion and fission of Golgi cisternae. Plant Biol. (Stuttg) 9:4 (2007), 489–501.
    • (2007) Plant Biol. (Stuttg) , vol.9 , Issue.4 , pp. 489-501
    • Hummel, E.1    Schmickl, R.2    Hinz, G.3    Hillmer, S.4    Robinson, D.G.5
  • 60
    • 0027017236 scopus 로고
    • Complementary scanning electron microscopy, technical notes and applications
    • Inoue, T., Complementary scanning electron microscopy, technical notes and applications. Arch. Histol. Cytol. 55:suppl (1992), 45–51.
    • (1992) Arch. Histol. Cytol. , vol.55 , pp. 45-51
    • Inoue, T.1
  • 61
    • 84988418466 scopus 로고    scopus 로고
    • COPI is essential for Golgi cisternal maturation and dynamics
    • Ishii, M., Suda, Y., Kurokawa, K., Nakano, A., COPI is essential for Golgi cisternal maturation and dynamics. J. Cell Sci. 129:17 (2016), 3251–3261.
    • (2016) J. Cell Sci. , vol.129 , Issue.17 , pp. 3251-3261
    • Ishii, M.1    Suda, Y.2    Kurokawa, K.3    Nakano, A.4
  • 62
    • 84903363332 scopus 로고    scopus 로고
    • Golgin-84-associated Golgi fragmentation triggers tau hyperphosphorylation by activation of cyclin-dependent kinase-5 and extracellular signal-regulated kinase
    • Jiang, Q., Wang, L., Guan, Y., Xu, H., Niu, Y., Han, L., Wei, Y.P., Lin, L., Chu, J., Wang, Q., Yang, Y., Pei, L., Wang, J.Z., Tian, Q., Golgin-84-associated Golgi fragmentation triggers tau hyperphosphorylation by activation of cyclin-dependent kinase-5 and extracellular signal-regulated kinase. Neurobiol. Aging 35:6 (2014), 1352–1363.
    • (2014) Neurobiol. Aging , vol.35 , Issue.6 , pp. 1352-1363
    • Jiang, Q.1    Wang, L.2    Guan, Y.3    Xu, H.4    Niu, Y.5    Han, L.6    Wei, Y.P.7    Lin, L.8    Chu, J.9    Wang, Q.10    Yang, Y.11    Pei, L.12    Wang, J.Z.13    Tian, Q.14
  • 63
    • 0037051978 scopus 로고    scopus 로고
    • Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH
    • Kellokumpu, S., Sormunen, R., Kellokumpu, I., Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH. FEBS Lett. 516 (2002), 217–224.
    • (2002) FEBS Lett. , vol.516 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 64
    • 77956038457 scopus 로고    scopus 로고
    • Tyrosylprotein sulfotransferase regulates collagen secretion in Caenorhabditis elegans
    • Kim, T.H., Kim do, H., Nam, H.W., Park, S.Y., Shim, J., Cho, J.W., Tyrosylprotein sulfotransferase regulates collagen secretion in Caenorhabditis elegans. Mol. Cells 29:4 (2010), 413–418.
    • (2010) Mol. Cells , vol.29 , Issue.4 , pp. 413-418
    • Kim, T.H.1    Kim do, H.2    Nam, H.W.3    Park, S.Y.4    Shim, J.5    Cho, J.W.6
  • 65
    • 0026561901 scopus 로고
    • Brefeldin A: insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., Donaldson, J.G., Lippincott-Schwartz, J., Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116 (1992), 1071–1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 67
    • 33947096851 scopus 로고    scopus 로고
    • Three-dimensional ultrastructure of the Golgi apparatus in different cells, high-resolution scanning electron microscopy of osmium-macerated tissues
    • Koga, D., Ushiki, T., Three-dimensional ultrastructure of the Golgi apparatus in different cells, high-resolution scanning electron microscopy of osmium-macerated tissues. Arch. Histol. Cytol. 69:5 (2006), 357–374.
    • (2006) Arch. Histol. Cytol. , vol.69 , Issue.5 , pp. 357-374
    • Koga, D.1    Ushiki, T.2
  • 69
    • 0042672956 scopus 로고    scopus 로고
    • A novel role for dp115 in the organization of tER sites in Drosophila
    • Kondylis, V., Rabouille, C., A novel role for dp115 in the organization of tER sites in Drosophila. J. Cell Biol. 162 (2003), 185–198.
    • (2003) J. Cell Biol. , vol.162 , pp. 185-198
    • Kondylis, V.1    Rabouille, C.2
  • 70
    • 70450223327 scopus 로고    scopus 로고
    • The golgi apparatus: lessons from drosophila
    • Kondylis, V., Rabouille, C., The golgi apparatus: lessons from drosophila. FEBS Lett. 583:23 (2009), 3827–3838.
    • (2009) FEBS Lett. , vol.583 , Issue.23 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 71
    • 84875327132 scopus 로고    scopus 로고
    • The golgin tether giantin regulates the secretory pathway by controlling stack organization within Golgi apparatus
    • Koreishi, M., Gniadek, T.J., Yu, S., Masuda, J., Honjo, Y., Satoh, A., The golgin tether giantin regulates the secretory pathway by controlling stack organization within Golgi apparatus. PLoS One, 8, 2013, e59821.
    • (2013) PLoS One , vol.8 , pp. e59821
    • Koreishi, M.1    Gniadek, T.J.2    Yu, S.3    Masuda, J.4    Honjo, Y.5    Satoh, A.6
  • 72
    • 78149448259 scopus 로고    scopus 로고
    • Golgi apparatus fragmentation as a mechanism responsible for uniform delivery of uroplakins to the apical plasma membrane of uroepithelial cells
    • Kreft, M.E., Di Giandomenico, D., Beznoussenko, G.V., Resnik, N., Mironov, A.A., Jezernik, K., Golgi apparatus fragmentation as a mechanism responsible for uniform delivery of uroplakins to the apical plasma membrane of uroepithelial cells. Biol. Cell. 102:11 (2010), 593–607.
    • (2010) Biol. Cell. , vol.102 , Issue.11 , pp. 593-607
    • Kreft, M.E.1    Di Giandomenico, D.2    Beznoussenko, G.V.3    Resnik, N.4    Mironov, A.A.5    Jezernik, K.6
  • 73
    • 0020534368 scopus 로고
    • Estimation of Golgi membrane flow rates in ovary glands of aptenia cordifolia using cytochalasin B
    • Kristen, U., Lockhausen, J., Estimation of Golgi membrane flow rates in ovary glands of aptenia cordifolia using cytochalasin B. Eur. J. Cell Biol. 29:2 (1983), 262–267.
    • (1983) Eur. J. Cell Biol. , vol.29 , Issue.2 , pp. 262-267
    • Kristen, U.1    Lockhausen, J.2
  • 75
    • 0028136433 scopus 로고
    • HVEM tomography of the trans-Golgi network, structural insights and identification of a lace-like vesicle coat
    • Ladinsky, M.S., Kremer, J.R., Furcinitti, P.S., McIntosh, J.R., Howell, K.E., HVEM tomography of the trans-Golgi network, structural insights and identification of a lace-like vesicle coat. J. Cell Biol. 127:1 (1994), 29–38.
    • (1994) J. Cell Biol. , vol.127 , Issue.1 , pp. 29-38
    • Ladinsky, M.S.1    Kremer, J.R.2    Furcinitti, P.S.3    McIntosh, J.R.4    Howell, K.E.5
  • 76
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions, functional insights from the normal rat kidney cell
    • Ladinsky, M.S., Mastronarde, D.N., McIntosh, J.R., Howell, K.E., Staehelin, L.A., Golgi structure in three dimensions, functional insights from the normal rat kidney cell. J. Cell Biol. 144 (1999), 1135–1149.
    • (1999) J. Cell Biol. , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 77
    • 0036678493 scopus 로고    scopus 로고
    • Structure of the Golgi and distribution of reporter molecules at 20 °C reveals the complexity of the exit compartments
    • Ladinsky, M.S., Wu, C.C., McIntosh, S., McIntosh, J.R., Howell, K.E., Structure of the Golgi and distribution of reporter molecules at 20 °C reveals the complexity of the exit compartments. Mol. Biol. Cell. 13 (2002), 2810–2825.
    • (2002) Mol. Biol. Cell. , vol.13 , pp. 2810-2825
    • Ladinsky, M.S.1    Wu, C.C.2    McIntosh, S.3    McIntosh, J.R.4    Howell, K.E.5
  • 78
    • 71949104933 scopus 로고    scopus 로고
    • BFA-induced compartments from the Golgi apparatus and trans-Golgi network/early endosome are distinct in plant cells
    • Lam, S.K., Cai, Y., Tse, Y.C., Wang, J., Law, A.H., Pimpl, P., Chan, H.Y., Xia, J., Jiang, L., BFA-induced compartments from the Golgi apparatus and trans-Golgi network/early endosome are distinct in plant cells. Plant J. 60:5 (2009), 865–881.
    • (2009) Plant J. , vol.60 , Issue.5 , pp. 865-881
    • Lam, S.K.1    Cai, Y.2    Tse, Y.C.3    Wang, J.4    Law, A.H.5    Pimpl, P.6    Chan, H.Y.7    Xia, J.8    Jiang, L.9
  • 79
    • 17844387375 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons
    • Liazoghli, D., Perreault, S., Micheva, K.D., Desjardins, M., Leclerc, N., Fragmentation of the Golgi apparatus induced by the overexpression of wild-type and mutant human tau forms in neurons. Am. J. Pathol. 166:5 (2005), 1499–1514.
    • (2005) Am. J. Pathol. , vol.166 , Issue.5 , pp. 1499-1514
    • Liazoghli, D.1    Perreault, S.2    Micheva, K.D.3    Desjardins, M.4    Leclerc, N.5
  • 80
    • 0022370408 scopus 로고
    • The neuronal endomembrane system. I. Direct links between rough endoplasmic reticulum and the cis element of the Golgi apparatus
    • Lindsey, J.D., Ellisman, M.H., The neuronal endomembrane system. I. Direct links between rough endoplasmic reticulum and the cis element of the Golgi apparatus. J. Neurosci. 5:12 (1985), 3111–3123.
    • (1985) J. Neurosci. , vol.5 , Issue.12 , pp. 3111-3123
    • Lindsey, J.D.1    Ellisman, M.H.2
  • 81
    • 0022346474 scopus 로고
    • The neuronal endomembrane system. II. The multiple forms of the Golgi apparatus cis element
    • Lindsey, J.D., Ellisman, M.H., The neuronal endomembrane system. II. The multiple forms of the Golgi apparatus cis element. J. Neurosci. 5:12 (1985), 3124–3134.
    • (1985) J. Neurosci. , vol.5 , Issue.12 , pp. 3124-3134
    • Lindsey, J.D.1    Ellisman, M.H.2
  • 82
    • 0022401384 scopus 로고
    • The neuronal endomembrane system. III. The origins of the axoplasmic reticulum and discrete axonal cisternae at the axon hillock
    • Lindsey, J.D., Ellisman, M.H., The neuronal endomembrane system. III. The origins of the axoplasmic reticulum and discrete axonal cisternae at the axon hillock. J. Neurosci. 5:12 (1985), 3135–3144.
    • (1985) J. Neurosci. , vol.5 , Issue.12 , pp. 3135-3144
    • Lindsey, J.D.1    Ellisman, M.H.2
  • 83
    • 0025102566 scopus 로고
    • Three-dimensional reconstruction of a plant dictyosome from series of ultrathin sections using computer image processing
    • Lockhausen, J., Kristen, U., Menhardt, W., Dallas, W., Three-dimensional reconstruction of a plant dictyosome from series of ultrathin sections using computer image processing. J. Microsc. 158 (1990), 197–205.
    • (1990) J. Microsc. , vol.158 , pp. 197-205
    • Lockhausen, J.1    Kristen, U.2    Menhardt, W.3    Dallas, W.4
  • 84
    • 0024409747 scopus 로고
    • Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway
    • Lucocq, J.M., Berger, E.G., Warren, G., Mitotic Golgi fragments in HeLa cells and their role in the reassembly pathway. J. Cell Biol. 109:2 (1989), 463–474.
    • (1989) J. Cell Biol. , vol.109 , Issue.2 , pp. 463-474
    • Lucocq, J.M.1    Berger, E.G.2    Warren, G.3
  • 86
    • 84887446957 scopus 로고    scopus 로고
    • Accommodation of large cargo within Golgi cisternae
    • Machamer, C.E., Accommodation of large cargo within Golgi cisternae. Histochem. Cell Biol. 140:3 (2013), 261–269.
    • (2013) Histochem. Cell Biol. , vol.140 , Issue.3 , pp. 261-269
    • Machamer, C.E.1
  • 87
    • 80053494001 scopus 로고    scopus 로고
    • Live-cell imaging of dual-labeled Golgi stacks in tobacco BY-2 cells reveals similar behaviors for different cisternae during movement and brefeldin A treatment
    • Madison, S.L., Nebenführ, A., Live-cell imaging of dual-labeled Golgi stacks in tobacco BY-2 cells reveals similar behaviors for different cisternae during movement and brefeldin A treatment. Mol. Plant. 4:5 (2011), 896–908.
    • (2011) Mol. Plant. , vol.4 , Issue.5 , pp. 896-908
    • Madison, S.L.1    Nebenführ, A.2
  • 88
    • 84962439323 scopus 로고    scopus 로고
    • Wine glasses and hourglasses. Non-adaptive complexity of vesicle traffic in microbial eukaryotes
    • (pii)
    • Mani, S., Thattai, M., Wine glasses and hourglasses. Non-adaptive complexity of vesicle traffic in microbial eukaryotes. Mol. Biochem. Parasitol. S0166–S6851:16 (2016), 30023–30028 (pii).
    • (2016) Mol. Biochem. Parasitol. , vol.S0166–S6851 , Issue.16 , pp. 30023-30028
    • Mani, S.1    Thattai, M.2
  • 91
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh, B.J., Mastronarde, D.N., Buttle, K.F., Howell, K.E., McIntosh, J.R., Organellar relationships in the Golgi region of pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 2399–2406.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 92
    • 1842681953 scopus 로고    scopus 로고
    • Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells
    • Marsh, B.J., Volkmann, N., McIntosh, J.R., Howell, K.E., Direct continuities between cisternae at different levels of the Golgi complex in glucose-stimulated mouse islet beta cells. Proc. Natl. Acad. Sci. U. S. A. 101:15 (2004), 5565–5570.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.15 , pp. 5565-5570
    • Marsh, B.J.1    Volkmann, N.2    McIntosh, J.R.3    Howell, K.E.4
  • 93
    • 0029860462 scopus 로고    scopus 로고
    • Identification of two types of beta-COP vesicles in the Golgi complex of rat spermatids
    • Martínez-Menárguez, J.A., Geuze, H.J., Ballesta, J., Identification of two types of beta-COP vesicles in the Golgi complex of rat spermatids. Eur. J. Cell Biol. 71:2 (1996), 137–143.
    • (1996) Eur. J. Cell Biol. , vol.71 , Issue.2 , pp. 137-143
    • Martínez-Menárguez, J.A.1    Geuze, H.J.2    Ballesta, J.3
  • 94
    • 71849112960 scopus 로고    scopus 로고
    • PKA-mediated Golgi remodeling during cAMP signal transmission
    • Mavillard, F., Hidalgo, J., Megias, D., Levitsky, K.L., Velasco, A., PKA-mediated Golgi remodeling during cAMP signal transmission. Traffic 11:1 (2010), 90–109.
    • (2010) Traffic , vol.11 , Issue.1 , pp. 90-109
    • Mavillard, F.1    Hidalgo, J.2    Megias, D.3    Levitsky, K.L.4    Velasco, A.5
  • 96
    • 79951724284 scopus 로고    scopus 로고
    • The ceramide-enriched trans-Golgi compartments reorganize together with other parts of the Golgi apparatus in response to ATP-depletion
    • Meisslitzer-Ruppitsch, C., Röhrl, C., Ranftler, C., Neumüller, J., Vetterlein, M., Ellinger, A., Pavelka, M., The ceramide-enriched trans-Golgi compartments reorganize together with other parts of the Golgi apparatus in response to ATP-depletion. Histochem. Cell Biol. 135:2 (2011), 159–171.
    • (2011) Histochem. Cell Biol. , vol.135 , Issue.2 , pp. 159-171
    • Meisslitzer-Ruppitsch, C.1    Röhrl, C.2    Ranftler, C.3    Neumüller, J.4    Vetterlein, M.5    Ellinger, A.6    Pavelka, M.7
  • 100
    • 78650927923 scopus 로고    scopus 로고
    • Molecular mechanisms responsible for formation of Golgi ribbon
    • Mironov, A.A., Beznoussenko, G.V., Molecular mechanisms responsible for formation of Golgi ribbon. Histol. Histopathol. 26:1 (2011), 117–133.
    • (2011) Histol. Histopathol. , vol.26 , Issue.1 , pp. 117-133
    • Mironov, A.A.1    Beznoussenko, G.V.2
  • 101
    • 84862487904 scopus 로고    scopus 로고
    • The kiss-and-run model of intra-Golgi transport
    • Mironov, A.A., Beznoussenko, G.V., The kiss-and-run model of intra-Golgi transport. Int. J. Mol. Sci. 13:6 (2012), 6800–6819.
    • (2012) Int. J. Mol. Sci. , vol.13 , Issue.6 , pp. 6800-6819
    • Mironov, A.A.1    Beznoussenko, G.V.2
  • 102
    • 7844231673 scopus 로고    scopus 로고
    • Estimation of subcellular organelle volume from ultrathin sections through centrioles with a discretized version of vertical rotator
    • Mironov, A.A. Jr., Mironov, A.A., Estimation of subcellular organelle volume from ultrathin sections through centrioles with a discretized version of vertical rotator. J. Microsc. 192 (1998), 29–36.
    • (1998) J. Microsc. , vol.192 , pp. 29-36
    • Mironov, A.A.1    Mironov, A.A.2
  • 103
  • 104
    • 0030753006 scopus 로고    scopus 로고
    • Variations on the intracellular transport theme, maturing cisternae and trafficking tubules
    • Mironov, A.A., Weidman, A., Luini, P., Variations on the intracellular transport theme, maturing cisternae and trafficking tubules. J. Cell Biol. 138 (1997), 481–484.
    • (1997) J. Cell Biol. , vol.138 , pp. 481-484
    • Mironov, A.A.1    Weidman, A.2    Luini, P.3
  • 108
    • 84885396118 scopus 로고    scopus 로고
    • Golgi's way, a long path toward the new paradigm of the intra-Golgi transport
    • Mironov, A.A., Sesorova, I.V., Beznoussenko, G.V., Golgi's way, a long path toward the new paradigm of the intra-Golgi transport. Histochem. Cell Biol. 140:4 (2013), 383–393.
    • (2013) Histochem. Cell Biol. , vol.140 , Issue.4 , pp. 383-393
    • Mironov, A.A.1    Sesorova, I.V.2    Beznoussenko, G.V.3
  • 109
    • 0038647481 scopus 로고    scopus 로고
    • Tomographic evidence for continuous turnover of Golgi cisternae in Pichia pastoris
    • Mogelsvang, S., Gomez-Ospina, N., Soderholm, J., Glick, B.S., Staehelin, L.A., Tomographic evidence for continuous turnover of Golgi cisternae in Pichia pastoris. Mol. Biol. Cell 14:6 (2003), 2277–2291.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.6 , pp. 2277-2291
    • Mogelsvang, S.1    Gomez-Ospina, N.2    Soderholm, J.3    Glick, B.S.4    Staehelin, L.A.5
  • 110
    • 0018198592 scopus 로고
    • Structural differences contrast higher plant and animal Golgi apparatus
    • Mollenhauer, H.H., Morré, D.J., Structural differences contrast higher plant and animal Golgi apparatus. J. Cell Sci. 32 (1978), 357–362.
    • (1978) J. Cell Sci. , vol.32 , pp. 357-362
    • Mollenhauer, H.H.1    Morré, D.J.2
  • 112
    • 0028020066 scopus 로고
    • Oocyte follicle cells association during development of human ovarian follicle: a study by high resolution scanning and transmission electron microscopy
    • Motta, P.M., Makabe, S., Naguro, T., Correr, S., Oocyte follicle cells association during development of human ovarian follicle: a study by high resolution scanning and transmission electron microscopy. Arch. Histol. Cytol. 57:4 (1994), 369–394.
    • (1994) Arch. Histol. Cytol. , vol.57 , Issue.4 , pp. 369-394
    • Motta, P.M.1    Makabe, S.2    Naguro, T.3    Correr, S.4
  • 113
    • 70450224864 scopus 로고    scopus 로고
    • Evolution and diversity of the Golgi body
    • Mowbrey, K., Dacks, J.B., Evolution and diversity of the Golgi body. FEBS Lett. 583:23 (2009), 3738–3745.
    • (2009) FEBS Lett. , vol.583 , Issue.23 , pp. 3738-3745
    • Mowbrey, K.1    Dacks, J.B.2
  • 114
    • 77955050740 scopus 로고    scopus 로고
    • Passage through the golgi
    • Nakano, A., Luini, A., Passage through the golgi. Curr. Opin. Cell Biol. 22:4 (2010), 471–478.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , Issue.4 , pp. 471-478
    • Nakano, A.1    Luini, A.2
  • 115
    • 0032498607 scopus 로고    scopus 로고
    • Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons
    • Nakata, T., Terada, S., Hirokawa, N., Visualization of the dynamics of synaptic vesicle and plasma membrane proteins in living axons. J. Cell Biol. 140 (1998), 659–674.
    • (1998) J. Cell Biol. , vol.140 , pp. 659-674
    • Nakata, T.1    Terada, S.2    Hirokawa, N.3
  • 116
    • 84910119019 scopus 로고    scopus 로고
    • The role of the clathrin adaptor AP-1: polarized sorting and beyond
    • Nakatsu, F., Hase, K., Ohno, H., The role of the clathrin adaptor AP-1: polarized sorting and beyond. Membranes (Basel) 4:4 (2014), 747–763.
    • (2014) Membranes (Basel) , vol.4 , Issue.4 , pp. 747-763
    • Nakatsu, F.1    Hase, K.2    Ohno, H.3
  • 117
    • 0036851186 scopus 로고    scopus 로고
    • Brefeldin A, deciphering an enigmatic inhibitor of secretion
    • Nebenführ, A., Ritzenthaler, C., Robinson, D.G., Brefeldin A, deciphering an enigmatic inhibitor of secretion. Plant Physiol. 130:3 (2002), 1102–1108.
    • (2002) Plant Physiol. , vol.130 , Issue.3 , pp. 1102-1108
    • Nebenführ, A.1    Ritzenthaler, C.2    Robinson, D.G.3
  • 120
    • 58749087878 scopus 로고    scopus 로고
    • Co-clustering of Golgi complex and other cytoplasmic organelles to crescentic region of half-moon nuclei during apoptosis
    • Nozawa, K., Fritzler, M.J., Takasaki, Y., Wood, M.R., Chan, E.K., Co-clustering of Golgi complex and other cytoplasmic organelles to crescentic region of half-moon nuclei during apoptosis. Cell Biol. Int. 33:2 (2009), 148–157.
    • (2009) Cell Biol. Int. , vol.33 , Issue.2 , pp. 148-157
    • Nozawa, K.1    Fritzler, M.J.2    Takasaki, Y.3    Wood, M.R.4    Chan, E.K.5
  • 121
    • 0027499531 scopus 로고
    • ß-COP localizes mainly to the cis-Golgi side in exocrine pancreas
    • Oprins, A., Duden, R., Kreis, T.E., Geuze, H.J., Slot, J.W., ß-COP localizes mainly to the cis-Golgi side in exocrine pancreas. J. Cell Biol. 121 (1993), 49–59.
    • (1993) J. Cell Biol. , vol.121 , pp. 49-59
    • Oprins, A.1    Duden, R.2    Kreis, T.E.3    Geuze, H.J.4    Slot, J.W.5
  • 123
    • 0023052287 scopus 로고
    • A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack
    • Orci, L., Glick, B.S., Rothman, J.E., A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack. Cell 46 (1986), 171–184.
    • (1986) Cell , vol.46 , pp. 171-184
    • Orci, L.1    Glick, B.S.2    Rothman, J.E.3
  • 124
    • 0032478142 scopus 로고    scopus 로고
    • Vesicles on strings, morphological evidence for processive transport within the Golgi stack
    • Orci, L., Perrelet, A., Rothman, J.E., Vesicles on strings, morphological evidence for processive transport within the Golgi stack. Proc. Natl. Acad. Sci. U. S. A. 95:5 (1998), 2279–2283.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.5 , pp. 2279-2283
    • Orci, L.1    Perrelet, A.2    Rothman, J.E.3
  • 125
    • 0017695355 scopus 로고
    • The corpus luteum of the guinea pig: fine structure at the time of maximum progesterone secretion and during regression
    • Paavola, L.G., The corpus luteum of the guinea pig: fine structure at the time of maximum progesterone secretion and during regression. Am. J. Anat. 150:4 (1978), 565–603.
    • (1978) Am. J. Anat. , vol.150 , Issue.4 , pp. 565-603
    • Paavola, L.G.1
  • 126
    • 0018146049 scopus 로고
    • The corpus luteum of the guinea pig. II. Cytochemical studies on the Golgi complex, GERL, and lysosomes in luteal cells during maximal progesterone secretion
    • Paavola, L.G., The corpus luteum of the guinea pig. II. Cytochemical studies on the Golgi complex, GERL, and lysosomes in luteal cells during maximal progesterone secretion. J. Cell Biol. 79:1 (1978), 45–58.
    • (1978) J. Cell Biol. , vol.79 , Issue.1 , pp. 45-58
    • Paavola, L.G.1
  • 127
    • 0018084818 scopus 로고
    • The corpus luteum of the guinea pig. III. Cytochemical studies on the Golgi complex and GERL during normal postpartum regression of luteal cells, emphasizing the origin of lysosomes and autophagic vacuoles
    • Paavola, L.G., The corpus luteum of the guinea pig. III. Cytochemical studies on the Golgi complex and GERL during normal postpartum regression of luteal cells, emphasizing the origin of lysosomes and autophagic vacuoles. J. Cell Biol. 79:1 (1978), 59–73.
    • (1978) J. Cell Biol. , vol.79 , Issue.1 , pp. 59-73
    • Paavola, L.G.1
  • 128
    • 84988324922 scopus 로고    scopus 로고
    • COPI selectively drives maturation of the early Golgi
    • Papanikou, E., Day, K.J., Austin, J., Glick, B.S., COPI selectively drives maturation of the early Golgi. Elife, 2015, 10.7554/eLife.13232.
    • (2015) Elife
    • Papanikou, E.1    Day, K.J.2    Austin, J.3    Glick, B.S.4
  • 129
    • 0027217617 scopus 로고
    • Early and late transformations occurring at organelles of the Golgi area under the influence of brefeldin A, an ultrastructural and lectin cytochemical study
    • Pavelka, M., Ellinger, A., Early and late transformations occurring at organelles of the Golgi area under the influence of brefeldin A, an ultrastructural and lectin cytochemical study. J. Histochem. Cytochem. 41:7 (1993), 1031–1042.
    • (1993) J. Histochem. Cytochem. , vol.41 , Issue.7 , pp. 1031-1042
    • Pavelka, M.1    Ellinger, A.2
  • 130
    • 0006496113 scopus 로고
    • Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles
    • Pearse, B.M., Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles. Proc. Natl. Acad. Sci. U. S. A. 73:4 (1976), 1255–1259.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , Issue.4 , pp. 1255-1259
    • Pearse, B.M.1
  • 131
    • 84877300116 scopus 로고    scopus 로고
    • A non-enzymatic function of Golgi glycosyltransferases: mediation of Golgi fragmentation by interaction with non-muscle myosin IIA
    • Petrosyan, A., Cheng, P.W., A non-enzymatic function of Golgi glycosyltransferases: mediation of Golgi fragmentation by interaction with non-muscle myosin IIA. Glycobiology 23:6 (2013), 690–708.
    • (2013) Glycobiology , vol.23 , Issue.6 , pp. 690-708
    • Petrosyan, A.1    Cheng, P.W.2
  • 132
    • 84919372694 scopus 로고    scopus 로고
    • Restoration of compact Golgi morphology in advanced prostate cancer enhances susceptibility to galectin-1-induced apoptosis by modifying mucin O-glycan synthesis
    • Petrosyan, A., Holzapfel, M.S., Muirhead, D.E., Cheng, P.W., Restoration of compact Golgi morphology in advanced prostate cancer enhances susceptibility to galectin-1-induced apoptosis by modifying mucin O-glycan synthesis. Mol. Cancer Res. 12:12 (2014), 1704–1716.
    • (2014) Mol. Cancer Res. , vol.12 , Issue.12 , pp. 1704-1716
    • Petrosyan, A.1    Holzapfel, M.S.2    Muirhead, D.E.3    Cheng, P.W.4
  • 133
    • 84999514935 scopus 로고    scopus 로고
    • Onco-Golgi: is fragmentation a gate to cancer progression?
    • (pii)
    • Petrosyan, A., Onco-Golgi: is fragmentation a gate to cancer progression?. Biochem. Mol. Biol. J., 1(1), 2015, 16 (pii).
    • (2015) Biochem. Mol. Biol. J. , vol.1 , Issue.1 , pp. 16
    • Petrosyan, A.1
  • 134
    • 84999514935 scopus 로고    scopus 로고
    • Apoptosis induces golgi vesiculation and fragmentation. onco-Golgi, is fragmentation a gate to cancer progression?
    • (pii)
    • Petrosyan, A., Apoptosis induces golgi vesiculation and fragmentation. onco-Golgi, is fragmentation a gate to cancer progression?. Biochem. Mol. Biol. J., 1(1), 2015, 16 (pii).
    • (2015) Biochem. Mol. Biol. J. , vol.1 , Issue.1 , pp. 16
    • Petrosyan, A.1
  • 135
    • 0842330701 scopus 로고    scopus 로고
    • Structural aspects of Golgi function
    • Polishchuk, R.S., Mironov, A.A., Structural aspects of Golgi function. Cell. Mol. Life Sci. 61:2 (2004), 146–158.
    • (2004) Cell. Mol. Life Sci. , vol.61 , Issue.2 , pp. 146-158
    • Polishchuk, R.S.1    Mironov, A.A.2
  • 136
    • 0033000412 scopus 로고    scopus 로고
    • Coalescence of Golgi fragments in microtubule-deprived living cells
    • Polishchuk, R.S., Polishchuk, E.V., Mironov, A.A., Coalescence of Golgi fragments in microtubule-deprived living cells. Eur. J. Cell Biol. 78 (1999), 170–185.
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 170-185
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Mironov, A.A.3
  • 137
    • 13344266172 scopus 로고
    • Cell fine structure and biosynthesis of intercellular molecules
    • Porter, K.R., Cell fine structure and biosynthesis of intercellular molecules. Biophys. J 4:Suppl (1964), 167–201.
    • (1964) Biophys. J. , vol.4 , pp. 167-201
    • Porter, K.R.1
  • 138
    • 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, E.G., Warren, G., Nilsson, T., Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides. J. Cell Sci. 108:Pt. 4 (1995), 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
  • 139
    • 0022519352 scopus 로고
    • Tridimensional structure of the Golgi apparatus in type A ganglion cells of the rat
    • Rambourg, A., Clermont, Y., Tridimensional structure of the Golgi apparatus in type A ganglion cells of the rat. Am. J. Anat. 176:4 (1986), 393–409.
    • (1986) Am. J. Anat. , vol.176 , Issue.4 , pp. 393-409
    • Rambourg, A.1    Clermont, Y.2
  • 140
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy, structure of the Golgi apparatus
    • Rambourg, A., Clermont, Y., Three-dimensional electron microscopy, structure of the Golgi apparatus. Eur. J. Cell Biol. 51:2 (1990), 189–200.
    • (1990) Eur. J. Cell Biol. , vol.51 , Issue.2 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 141
    • 0002471181 scopus 로고    scopus 로고
    • Three-dimensional structure of the Golgi apparatus in mammalian cells
    • Roth J E.G. Berger Birkhauser Basel
    • Rambourg, A., Clermont, Y., Three-dimensional structure of the Golgi apparatus in mammalian cells. Roth J, Berger, E.G., (eds.) The Golgi Apparatus, 1997, Birkhauser, Basel, 37–61.
    • (1997) The Golgi Apparatus , pp. 37-61
    • Rambourg, A.1    Clermont, Y.2
  • 142
    • 0016230363 scopus 로고
    • Three-dimensional structure of the osmium-impregnated Golgi apparatus as seen in the high voltage electron microscope
    • Rambourg, A., Clermont, Y., Marraud, A., Three-dimensional structure of the osmium-impregnated Golgi apparatus as seen in the high voltage electron microscope. Am. J. Anat. 140:1 (1974), 27–45.
    • (1974) Am. J. Anat. , vol.140 , Issue.1 , pp. 27-45
    • Rambourg, A.1    Clermont, Y.2    Marraud, A.3
  • 143
    • 0018409518 scopus 로고
    • Three-dimensional architecture of the Golgi apparatus in Sertoli cells of the rat
    • Rambourg, A., Clermont, Y., Hermo, L., Three-dimensional architecture of the Golgi apparatus in Sertoli cells of the rat. Am. J. Anat. 154 (1979), 455–476.
    • (1979) Am. J. Anat. , vol.154 , pp. 455-476
    • Rambourg, A.1    Clermont, Y.2    Hermo, L.3
  • 144
    • 0027461494 scopus 로고
    • Modulation of the Golgi apparatus in stimulated and nonstimulated prolactin cells of female rats
    • Rambourg, A., Clermont, Y., Chrétien, M., Olivier, L., Modulation of the Golgi apparatus in stimulated and nonstimulated prolactin cells of female rats. Anat. Rec. 235:3 (1993), 353–362.
    • (1993) Anat. Rec. , vol.235 , Issue.3 , pp. 353-362
    • Rambourg, A.1    Clermont, Y.2    Chrétien, M.3    Olivier, L.4
  • 145
    • 0027379811 scopus 로고
    • Modulation of the Golgi apparatus in Sacharomyces cerevisiae sec7 mutants as seen by three-dimensional electron microscopy
    • Rambourg, A., Clermont, Y., Kepes, F., Modulation of the Golgi apparatus in Sacharomyces cerevisiae sec7 mutants as seen by three-dimensional electron microscopy. Anat. Rec. 237 (1993), 441–452.
    • (1993) Anat. Rec. , vol.237 , pp. 441-452
    • Rambourg, A.1    Clermont, Y.2    Kepes, F.3
  • 146
    • 84920195417 scopus 로고    scopus 로고
    • Morphodynamics of the yeast Golgi apparatus
    • A.A. Mironov M. Pavelka Springer-Verlag Wien (Chapter 3.11.)
    • Rambourg, A., Daraspe, J., Kepes, F., Verbavatz, J.-M., Morphodynamics of the yeast Golgi apparatus. Mironov, A.A., Pavelka, M., (eds.) Golgi Apparatus, 2008, Springer-Verlag, Wien, 630–646 (Chapter 3.11.).
    • (2008) Golgi Apparatus , pp. 630-646
    • Rambourg, A.1    Daraspe, J.2    Kepes, F.3    Verbavatz, J.-M.4
  • 148
    • 84933041423 scopus 로고    scopus 로고
    • Vesicles versus tubes, Is endoplasmic reticulum-Golgi transport in plants fundamentally different from other eukaryotes?
    • Robinson, D.G., Brandizzi, F., Hawes, C., Nakano, A., Vesicles versus tubes, Is endoplasmic reticulum-Golgi transport in plants fundamentally different from other eukaryotes?. Plant Physiol. 168:2 (2015), 393–406.
    • (2015) Plant Physiol. , vol.168 , Issue.2 , pp. 393-406
    • Robinson, D.G.1    Brandizzi, F.2    Hawes, C.3    Nakano, A.4
  • 149
    • 0034839401 scopus 로고    scopus 로고
    • Deconstructing golgi inheritance
    • Rossanese, O.W., Glick, B.S., Deconstructing golgi inheritance. Traffic 2:9 (2001), 589–596.
    • (2001) Traffic , vol.2 , Issue.9 , pp. 589-596
    • Rossanese, O.W.1    Glick, B.S.2
  • 150
    • 0019307049 scopus 로고
    • Transport of the membrane glycoprotein of vesicular stomatitis virus to the cell surface in two stages by clathrin-coated vesicles
    • Rothman, J.E., Bursztyn-Pettegrew, H., Fine, R.E., Transport of the membrane glycoprotein of vesicular stomatitis virus to the cell surface in two stages by clathrin-coated vesicles. J. Cell Biol. 86:1 (1980), 162–171.
    • (1980) J. Cell Biol. , vol.86 , Issue.1 , pp. 162-171
    • Rothman, J.E.1    Bursztyn-Pettegrew, H.2    Fine, R.E.3
  • 152
    • 0017737407 scopus 로고
    • Electron microscopic studies of the assembly, intracellular transport, and secretion of chylomicrons by rat intestine
    • Sabesin, S.M., Frase, S., Electron microscopic studies of the assembly, intracellular transport, and secretion of chylomicrons by rat intestine. J. Lipid Res. 18 (1977), 496–511.
    • (1977) J. Lipid Res. , vol.18 , pp. 496-511
    • Sabesin, S.M.1    Frase, S.2
  • 153
    • 77950974131 scopus 로고    scopus 로고
    • Signaling from the Golgi: mechanisms and models for Golgi phosphoprotein 3-mediated oncogenesis
    • Scott, K.L., Chin, L., Signaling from the Golgi: mechanisms and models for Golgi phosphoprotein 3-mediated oncogenesis. Clin. Cancer Res. 16:8 (2010), 2229–2234.
    • (2010) Clin. Cancer Res. , vol.16 , Issue.8 , pp. 2229-2234
    • Scott, K.L.1    Chin, L.2
  • 155
    • 23444432501 scopus 로고
    • A three-dimensional reconstruction study of the rough ER-Golgi interface in serial thin sections of the pancreatic acinar cell of the rat
    • Sesso, A., de Faria, F.P., Iwamura, E.S., Corrêa, H., A three-dimensional reconstruction study of the rough ER-Golgi interface in serial thin sections of the pancreatic acinar cell of the rat. J. Cell Sci. 107 (1994), 517–528.
    • (1994) J. Cell Sci. , vol.107 , pp. 517-528
    • Sesso, A.1    de Faria, F.P.2    Iwamura, E.S.3    Corrêa, H.4
  • 157
    • 41849150103 scopus 로고    scopus 로고
    • Protein trafficking inside Toxoplasma gondii
    • Sheiner, L., Soldati-Favre, D., Protein trafficking inside Toxoplasma gondii. Traffic 9:5 (2008), 636–646.
    • (2008) Traffic , vol.9 , Issue.5 , pp. 636-646
    • Sheiner, L.1    Soldati-Favre, D.2
  • 158
    • 70449860010 scopus 로고    scopus 로고
    • Structure and function of the Golgi organelle in parasitic protists
    • A.A. Mironov M. Pavelka Springer-Verlag Wien (Chapter 4.14.)
    • Sokolova, Y.Y., Mironov, A.A., Structure and function of the Golgi organelle in parasitic protists. Mironov, A.A., Pavelka, M., (eds.) The Golgi Apparatus. State of the Art 110 Years After Camillo Golgi's Discovery, 2008, Springer-Verlag, Wien, 647–674 (Chapter 4.14.).
    • (2008) The Golgi Apparatus. State of the Art 110 Years After Camillo Golgi's Discovery , pp. 647-674
    • Sokolova, Y.Y.1    Mironov, A.A.2
  • 159
    • 0031460148 scopus 로고    scopus 로고
    • 1997: The mechanism of Golgi segregation during mitosis is cell type-specific
    • Stanley, H., Botas, J., Malhotra, V., 1997: The mechanism of Golgi segregation during mitosis is cell type-specific. Proc. Natl. Acad. Sci. U. S. A. 94 (1997), 14467–14470.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14467-14470
    • Stanley, H.1    Botas, J.2    Malhotra, V.3
  • 160
    • 0037175399 scopus 로고    scopus 로고
    • Neural cell adhesion molecule promotes accumulation of TGN organelles at sites of neuron-to-neuron contacts
    • Sytnyk, V., Leshchyns'ka, I., Delling, M., Dityateva, G., Dityatev, A., Schachner, M., Neural cell adhesion molecule promotes accumulation of TGN organelles at sites of neuron-to-neuron contacts. J. Cell Biol. 159:4 (2002), 649–661.
    • (2002) J. Cell Biol. , vol.159 , Issue.4 , pp. 649-661
    • Sytnyk, V.1    Leshchyns'ka, I.2    Delling, M.3    Dityateva, G.4    Dityatev, A.5    Schachner, M.6
  • 161
    • 0842323787 scopus 로고    scopus 로고
    • Trans-Golgi network delivery of synaptic proteins in synaptogenesis
    • Sytnyk, V., Leshchyns'ka, I., Dityatev, A., Schachner, M., Trans-Golgi network delivery of synaptic proteins in synaptogenesis. J. Cell Sci. 117:Pt. 3 (2004), 381–388.
    • (2004) J. Cell Sci. , vol.117 , pp. 381-388
    • Sytnyk, V.1    Leshchyns'ka, I.2    Dityatev, A.3    Schachner, M.4
  • 162
    • 0022587346 scopus 로고
    • Three-dimensional architecture of the Golgi complex observed by high resolution scanning electron microscopy
    • Tanaka, K., Mitsushima, A., Fukudome, H., Kashima, Y., Three-dimensional architecture of the Golgi complex observed by high resolution scanning electron microscopy. J. Submicrosc. Cytol. 18:1 (1986), 1–9.
    • (1986) J. Submicrosc. Cytol. , vol.18 , Issue.1 , pp. 1-9
    • Tanaka, K.1    Mitsushima, A.2    Fukudome, H.3    Kashima, Y.4
  • 163
    • 84923288088 scopus 로고    scopus 로고
    • Glycans and cancer: role of N-glycans in cancer biomarker progression and metastasis, and therapeutics
    • Taniguchi, N., Kizuka, Y., Glycans and cancer: role of N-glycans in cancer biomarker progression and metastasis, and therapeutics. Adv. Cancer Res. 126 (2015), 11–51.
    • (2015) Adv. Cancer Res. , vol.126 , pp. 11-51
    • Taniguchi, N.1    Kizuka, Y.2
  • 164
    • 0030822623 scopus 로고    scopus 로고
    • Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities
    • Taylor, R.S., Jones, S.M., Dahl, R.H., Nordeen, M.H., Howell, K.E., Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities. Mol. Biol. Cell. 8 (1997), 1911–1931.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1911-1931
    • Taylor, R.S.1    Jones, S.M.2    Dahl, R.H.3    Nordeen, M.H.4    Howell, K.E.5
  • 165
    • 0025818111 scopus 로고
    • Glucose-6-phosphatase activity of endoplasmic reticulum and Golgi apparatus in spermatocytes and spermatids of the rat, an electron microscopic cytochemical study
    • Thorne-Tjomsland, G., Clermont, Y., Tang, X.M., Glucose-6-phosphatase activity of endoplasmic reticulum and Golgi apparatus in spermatocytes and spermatids of the rat, an electron microscopic cytochemical study. Biol. Cell. 71 (1991), 33–41.
    • (1991) Biol. Cell. , vol.71 , pp. 33-41
    • Thorne-Tjomsland, G.1    Clermont, Y.2    Tang, X.M.3
  • 166
    • 0031916434 scopus 로고    scopus 로고
    • 3D topography of noncompact zone Golgi tubules in rat spermatids: a computer-assisted serial section reconstruction study
    • Thorne-Tjomsland, G., Dumontier, M., Jamieson, J.C., 3D topography of noncompact zone Golgi tubules in rat spermatids: a computer-assisted serial section reconstruction study. Anat. Rec. 250:4 (1998), 381–396.
    • (1998) Anat. Rec. , vol.250 , Issue.4 , pp. 381-396
    • Thorne-Tjomsland, G.1    Dumontier, M.2    Jamieson, J.C.3
  • 167
    • 84940585104 scopus 로고    scopus 로고
    • Brefeldin A exerts differential effects on anaplastic lymphoma kinase positive anaplastic large cell lymphoma and classical Hodgkin lymphoma cell lines
    • Toda, T., Watanabe, M., Kawato, J., Kadin, M.E., Higashihara, M., Kunisada, T., Umezawa, K., Horie, R., Brefeldin A exerts differential effects on anaplastic lymphoma kinase positive anaplastic large cell lymphoma and classical Hodgkin lymphoma cell lines. Br. J. Haematol. 170:6 (2015), 837–846.
    • (2015) Br. J. Haematol. , vol.170 , Issue.6 , pp. 837-846
    • Toda, T.1    Watanabe, M.2    Kawato, J.3    Kadin, M.E.4    Higashihara, M.5    Kunisada, T.6    Umezawa, K.7    Horie, R.8
  • 169
    • 0025735232 scopus 로고
    • Effects of Brefeldin A on the Golgi complex, endoplasmic reticulum and viral envelope glycoproteins in murine erythroleukemia cells
    • Ulmer, J.B., Palade, G.E., Effects of Brefeldin A on the Golgi complex, endoplasmic reticulum and viral envelope glycoproteins in murine erythroleukemia cells. Eur. J. Cell Biol. 54:1 (1991), 38–54.
    • (1991) Eur. J. Cell Biol. , vol.54 , Issue.1 , pp. 38-54
    • Ulmer, J.B.1    Palade, G.E.2
  • 170
    • 84989160070 scopus 로고    scopus 로고
    • Interplay between inflammation and cellular stress triggered by flaviviridae viruses
    • Valadão, A.L., Aguiar, R.S., de Arruda, L.B., Interplay between inflammation and cellular stress triggered by flaviviridae viruses. Front. Microbiol., 7, 2016, 1233.
    • (2016) Front. Microbiol. , vol.7 , pp. 1233
    • Valadão, A.L.1    Aguiar, R.S.2    de Arruda, L.B.3
  • 171
    • 85023203388 scopus 로고    scopus 로고
    • Mechanisms and regulation of the mitotic inheritance of the golgi complex
    • Valente, C., Colanzi, A., Mechanisms and regulation of the mitotic inheritance of the golgi complex. Front. Cell Dev. Biol., 3, 2015, 79.
    • (2015) Front. Cell Dev. Biol. , vol.3 , pp. 79
    • Valente, C.1    Colanzi, A.2
  • 173
    • 51249118719 scopus 로고    scopus 로고
    • Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex interface
    • Vivero-Salmerón, G., Ballesta, J., Martínez-Menárguez, J.A., Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex interface. Histochem. Cell Biol. 130:4 (2008), 709–717.
    • (2008) Histochem. Cell Biol. , vol.130 , Issue.4 , pp. 709-717
    • Vivero-Salmerón, G.1    Ballesta, J.2    Martínez-Menárguez, J.A.3
  • 174
    • 84887249616 scopus 로고    scopus 로고
    • 3-D analysis of dictyosomes and multivesicular bodies in the green alga Micrasterias denticulata by FIB/SEM tomography
    • Wanner, G., Schäfer, T., Lütz-Meindl, U., 3-D analysis of dictyosomes and multivesicular bodies in the green alga Micrasterias denticulata by FIB/SEM tomography. J. Struct. Biol. 184:2 (2013), 203–211.
    • (2013) J. Struct. Biol. , vol.184 , Issue.2 , pp. 203-211
    • Wanner, G.1    Schäfer, T.2    Lütz-Meindl, U.3
  • 175
    • 0000534956 scopus 로고
    • New cytoplasmic components in arterial endothelia
    • Weibel, E.R., Palade, G.E., New cytoplasmic components in arterial endothelia. J. Cell Biol. 23 (1964), 101–112.
    • (1964) J. Cell Biol. , vol.23 , pp. 101-112
    • Weibel, E.R.1    Palade, G.E.2
  • 177
    • 84988430449 scopus 로고    scopus 로고
    • Suppression of breast cancer metastasis through the inactivation of ADP-ribosylation factor 1
    • Xie, X., Tang, S.C., Cai, Y., Pi, W., Deng, L., Wu, G., Chavanieu, A., Teng, Y., Suppression of breast cancer metastasis through the inactivation of ADP-ribosylation factor 1. Oncotarget, 10(August), 2016.
    • (2016) Oncotarget , vol.10 , Issue.August
    • Xie, X.1    Tang, S.C.2    Cai, Y.3    Pi, W.4    Deng, L.5    Wu, G.6    Chavanieu, A.7    Teng, Y.8
  • 178
    • 0027154603 scopus 로고
    • Effect of monensin on plant Golgi, re-examination of the monensin-induced changes in cisternal architecture and functional activities of the Golgi apparatus of sycamore suspension-cultured cells
    • Zhang, G.F., Driouich, A., Staehelin, L.A., Effect of monensin on plant Golgi, re-examination of the monensin-induced changes in cisternal architecture and functional activities of the Golgi apparatus of sycamore suspension-cultured cells. J. Cell Sci. 104 (1993), 819–831.
    • (1993) J. Cell Sci. , vol.104 , pp. 819-831
    • Zhang, G.F.1    Driouich, A.2    Staehelin, L.A.3
  • 179
    • 0031662791 scopus 로고    scopus 로고
    • The Golgi apparatus and the centrosome are localized to the sites of newly emerging axons in cerebellar granule neurons in vitro
    • Zmuda, J.F., Rivas, R.J., The Golgi apparatus and the centrosome are localized to the sites of newly emerging axons in cerebellar granule neurons in vitro. Cell Motil. Cytoskeleton 41:1 (1998), 18–38.
    • (1998) Cell Motil. Cytoskeleton , vol.41 , Issue.1 , pp. 18-38
    • Zmuda, J.F.1    Rivas, R.J.2


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