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Volumn 126, Issue 22, 2013, Pages 5091-5100

Imaging ER-to-golgi transport: Towards a systems view

Author keywords

Early secretory pathway; Endoplasmic reticulum; Golgi; Microscopy; Transport carriers

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 84888105959     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.121061     Document Type: Note
Times cited : (16)

References (130)
  • 1
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog, C. and Hauri, H. P. (2006). The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119, 2173-2183.
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 2
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E. and Webb, W. W. (1976). Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16, 1055-1069.
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 3
    • 31744436399 scopus 로고    scopus 로고
    • Fluorescence cross-correlation spectroscopy in living cells
    • Bacia, K., Kim, S. A. and Schwille, P. (2006). Fluorescence cross-correlation spectroscopy in living cells. Nat. Methods 3, 83-89.
    • (2006) Nat. Methods , vol.3 , pp. 83-89
    • Bacia, K.1    Kim, S.A.2    Schwille, P.3
  • 4
    • 84874484606 scopus 로고    scopus 로고
    • Correlative live-cell and superresolution microscopy reveals cargo transport dynamics at microtubule intersections
    • USA
    • Bálint, S., Verdeny Vilanova, I., Sandoval Ávarez, A. and Lakadamyali, M. (2013). Correlative live-cell and superresolution microscopy reveals cargo transport dynamics at microtubule intersections. Proc. Natl. Acad. Sci. USA 110, 3375-3380.
    • (2013) Proc. Natl. Acad. Sci. , vol.110 , pp. 3375-3380
    • Bálint, S.1    Verdeny Vilanova, I.2    Sandoval Álvarez, A.3    Lakadamyali, M.4
  • 7
    • 14044272872 scopus 로고    scopus 로고
    • Live imaging of bidirectional traffic from the ERGIC
    • Ben-Tekaya, H., Miura, K., Pepperkok, R. and Hauri, H. P. (2005). Live imaging of bidirectional traffic from the ERGIC. J. Cell Sci. 118, 357-367.
    • (2005) J. Cell Sci. , vol.118 , pp. 357-367
    • Ben-Tekaya, H.1    Miura, K.2    Pepperkok, R.3    Hauri, H.P.4
  • 10
    • 0036799651 scopus 로고    scopus 로고
    • De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
    • Bevis, B. J., Hammond, A. T., Reinke, C. A. and Glick, B. S. (2002). De novo formation of transitional ER sites and Golgi structures in Pichia pastoris. Nat. Cell Biol. 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
  • 13
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • Brandizzi, F. and Barlowe, C. (2013). Organization of the ER-Golgi interface for membrane traffic control. Nat. Rev. Mol. Cell Biol. 14, 382-392.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 14
    • 57949085420 scopus 로고    scopus 로고
    • Chapter 1: In vivo applications of fluorescence correlation spectroscopy
    • Chen, H., Farkas, E. R. and Webb, W. W. (2008). Chapter 1: In vivo applications of fluorescence correlation spectroscopy. Methods Cell Biol. 89, 3-35.
    • (2008) Methods Cell Biol. , vol.89 , pp. 3-35
    • Chen, H.1    Farkas, E.R.2    Webb, W.W.3
  • 15
    • 84873666238 scopus 로고    scopus 로고
    • Simple super-resolution live-cell imaging based on diffusion-assisted Förster resonance energy transfer
    • Cho, S., Jang, J., Song, C., Lee, H., Ganesan, P., Yoon, T. Y., Kim, M. W., Choi, M. C., Ihee, H., Do Heo, W. et al. (2013). Simple super-resolution live-cell imaging based on diffusion-assisted Förster resonance energy transfer. Sci. Rep. 3, 1208.
    • (2013) Sci. Rep. , vol.3 , pp. 1208
    • Cho, S.1    Jang, J.2    Song, C.3    Lee, H.4    Ganesan, P.5    Yoon, T.Y.6    Kim, M.W.7    Choi, M.C.8    Ihee, H.9    Do Heo, W.10
  • 18
    • 84355166675 scopus 로고    scopus 로고
    • Imaging proteins inside cells with fluorescent tags
    • Crivat, G. and Taraska, J. W. (2012). Imaging proteins inside cells with fluorescent tags. Trends Biotechnol. 30, 8-16.
    • (2012) Trends Biotechnol. , vol.30 , pp. 8-16
    • Crivat, G.1    Taraska, J.W.2
  • 19
    • 78049487235 scopus 로고    scopus 로고
    • A whole genome RNAi screen of Drosophila S2 cell spreading performed using automated computational image analysis
    • D'Ambrosio, M. V. and Vale, R. D. (2010). A whole genome RNAi screen of Drosophila S2 cell spreading performed using automated computational image analysis. J. Cell Biol. 191, 471-478.
    • (2010) J. Cell Biol. , vol.191 , pp. 471-478
    • D'Ambrosio, M.V.1    Vale, R.D.2
  • 20
    • 77953642000 scopus 로고    scopus 로고
    • Protein sorting receptors in the early secretory pathway
    • Dancourt, J. and Barlowe, C. (2010). Protein sorting receptors in the early secretory pathway. Annu. Rev. Biochem. 79, 777-802.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 777-802
    • Dancourt, J.1    Barlowe, C.2
  • 21
    • 84863584294 scopus 로고    scopus 로고
    • Widely accessible method for superresolution fluorescence imaging of living systems
    • USA
    • Dedecker, P., Mo, G. C., Dertinger, T. and Zhang, J. (2012). Widely accessible method for superresolution fluorescence imaging of living systems. Proc. Natl. Acad. Sci. USA 109, 10909-10914.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 10909-10914
    • Dedecker, P.1    Mo, G.C.2    Dertinger, T.3    Zhang, J.4
  • 22
    • 84879895738 scopus 로고    scopus 로고
    • STED microscopy of living cells-new frontiers in membrane and neurobiology
    • Eggeling, C., Willig, K. I. and Barrantes, F. J. (2013). STED microscopy of living cells-new frontiers in membrane and neurobiology. J. Neurochem. 126, 203-212.
    • (2013) J. Neurochem. , vol.126 , pp. 203-212
    • Eggeling, C.1    Willig, K.I.2    Barrantes, F.J.3
  • 24
    • 0017103825 scopus 로고
    • Cell surface distribution of lectin receptors determined by resonance energy transfer
    • Fernandez, S. M. and Berlin, R. D. (1976). Cell surface distribution of lectin receptors determined by resonance energy transfer. Nature 264, 411-415.
    • (1976) Nature , vol.264 , pp. 411-415
    • Fernandez, S.M.1    Berlin, R.D.2
  • 25
    • 84859475063 scopus 로고    scopus 로고
    • Time-lapse two-color 3D imaging of live cells with doubled resolution using structured illumination
    • USA
    • Fiolka, R., Shao, L., Rego, E. H., Davidson, M. W. and Gustafsson, M. G. (2012). Time-lapse two-color 3D imaging of live cells with doubled resolution using structured illumination. Proc. Natl. Acad. Sci. USA 109, 5311-5315.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 5311-5315
    • Fiolka, R.1    Shao, L.2    Rego, E.H.3    Davidson, M.W.4    Gustafsson, M.G.5
  • 27
    • 84894244456 scopus 로고    scopus 로고
    • Energy migration and fluorescence
    • Förster, T. (2012). Energy migration and fluorescence. 1946. J. Biomed. Opt. 17, 011002.
    • (2012) 1946. J. Biomed. Opt. , vol.17 , pp. 011002
    • Förster, T.1
  • 29
    • 0009355284 scopus 로고
    • Transport of vesicular stomatitis virus glycoprotein in a cell-free extract
    • USA
    • Fries, E. and Rothman, J. E. (1980). Transport of vesicular stomatitis virus glycoprotein in a cell-free extract. Proc. Natl. Acad. Sci. USA 77, 3870-3874.
    • (1980) Proc. Natl. Acad. Sci. , vol.77 , pp. 3870-3874
    • Fries, E.1    Rothman, J.E.2
  • 31
    • 84864439768 scopus 로고    scopus 로고
    • Targeted gene knockout by direct delivery of zinc-finger nuclease proteins
    • Gaj, T., Guo, J., Kato, Y., Sirk, S. J. and Barbas, C. F., 3rd (2012). Targeted gene knockout by direct delivery of zinc-finger nuclease proteins. Nat. Methods 9, 805-807.
    • (2012) Nat. Methods , vol.9 , pp. 805-807
    • Gaj, T.1    Guo, J.2    Kato, Y.3    Sirk, S.J.4    Barbas, C.F.5
  • 33
    • 84870860504 scopus 로고    scopus 로고
    • Noninvasive imaging beyond the diffraction limit of 3D dynamics in thickly fluorescent specimens
    • Gao, L., Shao, L., Higgins, C. D., Poulton, J. S., Peifer, M., Davidson, M. W., Wu, X., Goldstein, B. and Betzig, E. (2012). Noninvasive imaging beyond the diffraction limit of 3D dynamics in thickly fluorescent specimens. Cell 151, 1370-1385.
    • (2012) Cell , vol.151 , pp. 1370-1385
    • Gao, L.1    Shao, L.2    Higgins, C.D.3    Poulton, J.S.4    Peifer, M.5    Davidson, M.W.6    Wu, X.7    Goldstein, B.8    Betzig, E.9
  • 34
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans, B. N., Adams, S. R., Ellisman, M. H. and Tsien, R. Y. (2006). The fluorescent toolbox for assessing protein location and function. Science 312, 217-224.
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 36
    • 0031559885 scopus 로고    scopus 로고
    • A cisternal maturation mechanism can explain the asymmetry of the Golgi stack
    • Glick, B. S., Elston, T. and Oster, G. (1997). A cisternal maturation mechanism can explain the asymmetry of the Golgi stack. FEBS Lett. 414, 177-181.
    • (1997) FEBS Lett. , vol.414 , pp. 177-181
    • Glick, B.S.1    Elston, T.2    Oster, G.3
  • 39
    • 0034028826 scopus 로고    scopus 로고
    • Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy
    • Gustafsson, M. G. (2000). Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy. J. Microsc. 198, 82-87.
    • (2000) J. Microsc. , vol.198 , pp. 82-87
    • Gustafsson, M.G.1
  • 40
    • 42949147434 scopus 로고    scopus 로고
    • Super-resolution light microscopy goes live
    • Gustafsson, M. G. (2008). Super-resolution light microscopy goes live. Nat. Methods 5, 385-387.
    • (2008) Nat. Methods , vol.5 , pp. 385-387
    • Gustafsson, M.G.1
  • 41
    • 84881147545 scopus 로고    scopus 로고
    • Gene knockout and knockin by zinc-finger nucleases: current status and perspectives
    • Hauschild-Quintern, J., Petersen, B., Cost, G. J. and Niemann, H. (2013). Gene knockout and knockin by zinc-finger nucleases: current status and perspectives. Cell. Mol. Life Sci. 70, 2969-2983.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 2969-2983
    • Hauschild-Quintern, J.1    Petersen, B.2    Cost, G.J.3    Niemann, H.4
  • 42
    • 55049135085 scopus 로고    scopus 로고
    • Stimulated emission depletion (STED) nanoscopy of a fluorescent protein-labeled organelle inside a living cell
    • Hein, B., Willig, K. I. and Hell, S. W. (2008). Stimulated emission depletion (STED) nanoscopy of a fluorescent protein-labeled organelle inside a living cell. Proc. Natl. Acad. Sci. USA 105, 14271-14276.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14271-14276
    • Hein, B.1    Willig, K.I.2    Hell, S.W.3
  • 43
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy
    • Hell, S. W. and Wichmann, J. (1994). Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 19, 780-782.
    • (1994) Opt. Lett. , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 44
    • 9444272907 scopus 로고    scopus 로고
    • mRNA localization and ER-based protein sorting mechanisms dictate the use of transitional endoplasmic reticulum-golgi units involved in gurken transport in Drosophila oocytes
    • Herpers, B. and Rabouille, C. (2004). mRNA localization and ER-based protein sorting mechanisms dictate the use of transitional endoplasmic reticulum-golgi units involved in gurken transport in Drosophila oocytes. Mol. Biol. Cell 15, 5306-5317.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5306-5317
    • Herpers, B.1    Rabouille, C.2
  • 45
    • 33748751347 scopus 로고    scopus 로고
    • Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: real-time visualization with confocal fluorescence resonance energy transfer
    • Herrick-Davis, K., Weaver, B. A., Grinde, E. and Mazurkiewicz, J. E. (2006). Serotonin 5-HT2C receptor homodimer biogenesis in the endoplasmic reticulum: real-time visualization with confocal fluorescence resonance energy transfer. J. Biol. Chem. 281, 27109-27116.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27109-27116
    • Herrick-Davis, K.1    Weaver, B.A.2    Grinde, E.3    Mazurkiewicz, J.E.4
  • 46
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess, S. T., Girirajan, T. P. and Mason, M. D. (2006). Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophys. J. 91, 4258-4272.
    • (2006) Biophys. J. , vol.91 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.2    Mason, M.D.3
  • 48
    • 70450223889 scopus 로고    scopus 로고
    • Mechanisms of COPI vesicle formation
    • Hsu, V. W. and Yang, J. S. (2009). Mechanisms of COPI vesicle formation. FEBS Lett. 583, 3758-3763.
    • (2009) FEBS Lett. , vol.583 , pp. 3758-3763
    • Hsu, V.W.1    Yang, J.S.2
  • 49
    • 38949216802 scopus 로고    scopus 로고
    • Three-dimensional superresolution imaging by stochastic optical reconstructionmicroscopy
    • Huang, B., Wang, W., Bates, M. and Zhuang, X. (2008). Three-dimensional superresolution imaging by stochastic optical reconstructionmicroscopy. Science 319, 810-813.
    • (2008) Science , vol.319 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 50
    • 39149086740 scopus 로고    scopus 로고
    • Assembly, organization, and function of the COPII coat
    • Hughes, H. and Stephens, D. J. (2008). Assembly, organization, and function of the COPII coat. Histochem. Cell Biol. 129, 129-151.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 129-151
    • Hughes, H.1    Stephens, D.J.2
  • 52
    • 0014118370 scopus 로고
    • Intracellular transport of secretory proteins in the pancreatic exocrine cell.I. Role of the peripheral elements of the Golgi complex.
    • Jamieson, J. D. and Palade, G. E. (1967). Intracellular transport of secretory proteins in the pancreatic exocrine cell. I. Role of the peripheral elements of the Golgi complex. J. Cell Biol. 34, 577-596.
    • (1967) J. Cell Biol. , vol.34 , pp. 577-596
    • Jamieson, J.D.1    Palade, G.E.2
  • 53
    • 0014384434 scopus 로고
    • Intracellular transport of secretory proteins in the pancreatic exocrine cell. 3. Dissociation of intracellular transport from protein synthesis.
    • Jamieson, J. D. and Palade, G. E. (1968). Intracellular transport of secretory proteins in the pancreatic exocrine cell. 3. Dissociation of intracellular transport from protein synthesis. J. Cell Biol. 39, 580-588.
    • (1968) J. Cell Biol. , vol.39 , pp. 580-588
    • Jamieson, J.D.1    Palade, G.E.2
  • 54
    • 79957823841 scopus 로고    scopus 로고
    • Fast, three-dimensional superresolution imaging of live cells
    • Jones, S. A., Shim, S. H., He, J. and Zhuang, X. (2011). Fast, three-dimensional superresolution imaging of live cells. Nat. Methods 8, 499-505.
    • (2011) Nat. Methods , vol.8 , pp. 499-505
    • Jones, S.A.1    Shim, S.H.2    He, J.3    Zhuang, X.4
  • 55
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen, M., Sun, Y. and Drubin, D. G. (2003). A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115, 475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 56
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin-and actin-mediated endocytosis machinery
    • Kaksonen, M., Toret, C. P. and Drubin, D. G. (2005). A modular design for the clathrin-and actin-mediated endocytosis machinery. Cell 123, 305-320.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 57
    • 79952034405 scopus 로고    scopus 로고
    • Identification of ER proteins involved in the functional organisation of the early secretory pathway in Drosophila cells by a targeted RNAi screen
    • Kondylis, V., Tang, Y., Fuchs, F., Boutros, M. and Rabouille, C. (2011). Identification of ER proteins involved in the functional organisation of the early secretory pathway in Drosophila cells by a targeted RNAi screen. PLoS ONE 6, e17173.
    • (2011) PLoS ONE , vol.6
    • Kondylis, V.1    Tang, Y.2    Fuchs, F.3    Boutros, M.4    Rabouille, C.5
  • 58
    • 84864592255 scopus 로고    scopus 로고
    • Plasma membrane reshaping during endocytosis is revealed by time-resolved electron tomography
    • Kukulski, W., Schorb, M., Kaksonen, M. and Briggs, J. A. (2012). Plasma membrane reshaping during endocytosis is revealed by time-resolved electron tomography. Cell 150, 508-520.
    • (2012) Cell , vol.150 , pp. 508-520
    • Kukulski, W.1    Schorb, M.2    Kaksonen, M.3    Briggs, J.A.4
  • 60
    • 84864982866 scopus 로고    scopus 로고
    • Advances in high-resolution imaging-techniques for three-dimensional imaging of cellular structures
    • Lidke, D. S. and Lidke, K. A. (2012). Advances in high-resolution imaging-techniques for three-dimensional imaging of cellular structures. J. Cell Sci. 125, 2571-2580.
    • (2012) J. Cell Sci. , vol.125 , pp. 2571-2580
    • Lidke, D.S.1    Lidke, K.A.2
  • 61
    • 33748962857 scopus 로고    scopus 로고
    • Insights into COPI coat assembly and function in living cells
    • Lippincott-Schwartz, J. and Liu, W. (2006). Insights into COPI coat assembly and function in living cells. Trends Cell Biol. 16, e1-e4.
    • (2006) Trends Cell Biol. , vol.16
    • Lippincott-Schwartz, J.1    Liu, W.2
  • 62
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz, J. and Patterson, G. H. (2003). Development and use of fluorescent protein markers in living cells. Science 300, 87-91.
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 63
    • 0042338695 scopus 로고    scopus 로고
    • Photobleaching and photoactivation: following protein dynamics in living cells
    • Lippincott-Schwartz, J., Altan-Bonnet, N. and Patterson, G. H. (2003). Photobleaching and photoactivation: following protein dynamics in living cells. Nat. Cell Biol. Suppl, S7-S14.
    • (2003) Nat. Cell Biol. , Issue.SUPPL.
    • Lippincott-Schwartz, J.1    Altan-Bonnet, N.2    Patterson, G.H.3
  • 65
    • 0035407522 scopus 로고    scopus 로고
    • KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET
    • Majoul, I., Straub, M., Hell, S. W., Duden, R. and Söling, H. D. (2001). KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET. Dev. Cell 1, 139-153.
    • (2001) Dev. Cell , vol.1 , pp. 139-153
    • Majoul, I.1    Straub, M.2    Hell, S.W.3    Duden, R.4    Söling, H.D.5
  • 66
    • 1842681953 scopus 로고    scopus 로고
    • Direct continuities between cisternae at different levelsof theGolgi complex inglucose-stimulated mouse islet beta cells
    • USA
    • Marsh, B. J., Volkmann, N., McIntosh, J. R. and Howell, K. E. (2004). Direct continuities between cisternae at different levelsof theGolgi complex inglucose-stimulated mouse islet beta cells. Proc. Natl. Acad. Sci. USA 101, 5565-5570.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 5565-5570
    • Marsh, B.J.1    Volkmann, N.2    McIntosh, J.R.3    Howell, K.E.4
  • 69
    • 84876541392 scopus 로고    scopus 로고
    • Direct proteomic quantification of the secretome of activated immune cells
    • Meissner, F., Scheltema, R. A., Mollenkopf, H. J. and Mann, M. (2013). Direct proteomic quantification of the secretome of activated immune cells. Science 340, 475-478.
    • (2013) Science , vol.340 , pp. 475-478
    • Meissner, F.1    Scheltema, R.A.2    Mollenkopf, H.J.3    Mann, M.4
  • 70
    • 79953726298 scopus 로고    scopus 로고
    • Photoactivatable and cell-membrane-permeable phosphatidylinositol 3,4,5-trisphosphate
    • Mentel, M., Laketa, V., Subramanian, D., Gillandt, H. and Schultz, C. (2011). Photoactivatable and cell-membrane-permeable phosphatidylinositol 3,4,5-trisphosphate. Angew. Chem. Int. Ed. Engl. 50, 3811-3814.
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 3811-3814
    • Mentel, M.1    Laketa, V.2    Subramanian, D.3    Gillandt, H.4    Schultz, C.5
  • 71
    • 0034255726 scopus 로고    scopus 로고
    • Visualizing membrane traffic in vivo by combined video fluorescence and 3D electron microscopy
    • Mironov, A. A., Polishchuk, R. S. and Luini, A. (2000). Visualizing membrane traffic in vivo by combined video fluorescence and 3D electron microscopy. Trends Cell Biol. 10, 349-353.
    • (2000) Trends Cell Biol. , vol.10 , pp. 349-353
    • Mironov, A.A.1    Polishchuk, R.S.2    Luini, A.3
  • 73
    • 0842309131 scopus 로고    scopus 로고
    • ER-to-Golgi transport and cytoskeletal interactions in animal cells
    • Murshid, A. and Presley, J. F. (2004). ER-to-Golgi transport and cytoskeletal interactions in animal cells. Cell. Mol. Life Sci. 61, 133-145.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 133-145
    • Murshid, A.1    Presley, J.F.2
  • 76
    • 13444267652 scopus 로고    scopus 로고
    • Protein localization studies in the age of 'Omics'
    • O'Rourke, N. A., Meyer, T. and Chandy, G. (2005). Protein localization studies in the age of 'Omics'. Curr. Opin. Chem. Biol. 9, 82-87.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 82-87
    • O'Rourke, N.A.1    Meyer, T.2    Chandy, G.3
  • 77
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade, G. (1975). Intracellular aspects of the process of protein synthesis. Science 189, 867.
    • (1975) Science , vol.189 , pp. 867
    • Palade, G.1
  • 79
    • 33747624926 scopus 로고    scopus 로고
    • High-throughput fluorescence microscopy for systems biology
    • Pepperkok, R. and Ellenberg, J. (2006). High-throughput fluorescence microscopy for systems biology. Nat. Rev. Mol. Cell Biol. 7, 690-696.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 690-696
    • Pepperkok, R.1    Ellenberg, J.2
  • 80
    • 84856251270 scopus 로고    scopus 로고
    • Growth and metabolic control of lipid signalling at the Golgi
    • Piao, H. and Mayinger, P. (2012). Growth and metabolic control of lipid signalling at the Golgi. Biochem. Soc. Trans. 40, 205-209.
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 205-209
    • Piao, H.1    Mayinger, P.2
  • 81
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: the good, the bad and the ugly
    • Piston, D. W. and Kremers, G. J. (2007). Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem. Sci. 32, 407-414.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremers, G.J.2
  • 86
    • 0027056183 scopus 로고
    • Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy
    • Preuss, D., Mulholland, J., Franzusoff, A., Segev, N. and Botstein, D. (1992). Characterization of the Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol. Biol. Cell 3, 789-803.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 789-803
    • Preuss, D.1    Mulholland, J.2    Franzusoff, A.3    Segev, N.4    Botstein, D.5
  • 88
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese, O. W., Soderholm, J., Bevis, B. J., Sears, I. B., O'Connor, J., Williamson, E. K. and Glick, B. S. (1999). Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 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
  • 89
    • 0030020733 scopus 로고    scopus 로고
    • The protein machinery of vesicle budding and fusion
    • Rothman, J. E. (1996). The protein machinery of vesicle budding and fusion. Protein Sci. 5, 185-194.
    • (1996) Protein Sci. , vol.5 , pp. 185-194
    • Rothman, J.E.1
  • 90
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust, M. J., Bates, M. and Zhuang, X. (2006). Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3, 793-795.
    • (2006) Nat. Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 93
    • 84856716170 scopus 로고    scopus 로고
    • Monitoring phospholipid dynamics during phagocytosis: application of genetically-encoded fluorescent probes
    • Sarantis, H. and Grinstein, S. (2012). Monitoring phospholipid dynamics during phagocytosis: application of genetically-encoded fluorescent probes. Methods Cell Biol. 108, 429-444.
    • (2012) Methods Cell Biol. , vol.108 , pp. 429-444
    • Sarantis, H.1    Grinstein, S.2
  • 94
    • 0347723909 scopus 로고    scopus 로고
    • Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting
    • Sato, K. and Nakano, A. (2004). Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J. Biol. Chem. 279, 1330-1335.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1330-1335
    • Sato, K.1    Nakano, A.2
  • 95
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales, S. J., Pepperkok, R. and Kreis, T. E. (1997). Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 90, 1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.J.1    Pepperkok, R.2    Kreis, T.E.3
  • 96
    • 77953796801 scopus 로고    scopus 로고
    • Challenges in studying phospholipid signaling
    • Schultz, C. (2010). Challenges in studying phospholipid signaling. Nat. Chem. Biol. 6, 473-475.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 473-475
    • Schultz, C.1
  • 98
    • 84870796692 scopus 로고    scopus 로고
    • Visualizing cell structure and function with point-localization superresolution imaging
    • Sengupta, P., Van Engelenburg, S. and Lippincott-Schwartz, J. (2012). Visualizing cell structure and function with point-localization superresolution imaging. Dev. Cell 23, 1092-1102.
    • (2012) Dev. Cell , vol.23 , pp. 1092-1102
    • Sengupta, P.1    Van Engelenburg, S.2    Lippincott-Schwartz, J.3
  • 99
    • 30944467113 scopus 로고    scopus 로고
    • A guide to choosing fluorescent proteins
    • Shaner, N. C., Steinbach, P. A. and Tsien, R. Y. (2005). A guide to choosing fluorescent proteins. Nat. Methods 2, 905-909.
    • (2005) Nat. Methods , vol.2 , pp. 905-909
    • Shaner, N.C.1    Steinbach, P.A.2    Tsien, R.Y.3
  • 100
    • 45849119438 scopus 로고    scopus 로고
    • I5S: wide-field light microscopy with 100-nm-scale resolution in three dimensions
    • Shao, L., Isaac, B., Uzawa, S., Agard, D. A., Sedat, J. W. and Gustafsson, M. G. (2008). I5S: wide-field light microscopy with 100-nm-scale resolution in three dimensions. Biophys. J. 94, 4971-4983.
    • (2008) Biophys. J. , vol.94 , pp. 4971-4983
    • Shao, L.1    Isaac, B.2    Uzawa, S.3    Agard, D.A.4    Sedat, J.W.5    Gustafsson, M.G.6
  • 102
    • 0031781229 scopus 로고    scopus 로고
    • An ordered inheritance strategy for the Golgi apparatus: visualization of mitotic disassembly reveals a role for the mitotic spindle
    • Shima, D. T., Cabrera-Poch, N., Pepperkok, R. and Warren, G. (1998). An ordered inheritance strategy for the Golgi apparatus: visualization of mitotic disassembly reveals a role for the mitotic spindle. J. Cell Biol. 141, 955-966.
    • (1998) J. Cell Biol. , vol.141 , pp. 955-966
    • Shima, D.T.1    Cabrera-Poch, N.2    Pepperkok, R.3    Warren, G.4
  • 103
    • 0033615074 scopus 로고    scopus 로고
    • Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes
    • Shima, D. T., Scales, S. J., Kreis, T. E. and Pepperkok, R. (1999). Segregation of COPI-rich and anterograde-cargo-rich domains in endoplasmic-reticulum-to-Golgi transport complexes. Curr. Biol. 9, 821-824.
    • (1999) Curr. Biol. , vol.9 , pp. 821-824
    • Shima, D.T.1    Scales, S.J.2    Kreis, T.E.3    Pepperkok, R.4
  • 104
    • 42949083695 scopus 로고    scopus 로고
    • Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics
    • Shroff, H., Galbraith, C. G., Galbraith, J. A. and Betzig, E. (2008). Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat. Methods 5, 417-423.
    • (2008) Nat. Methods , vol.5 , pp. 417-423
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 106
    • 0034280113 scopus 로고    scopus 로고
    • Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing
    • Simpson, J. C., Wellenreuther, R., Poustka, A., Pepperkok, R. and Wiemann, S. (2000). Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. EMBO Rep. 1, 287-292.
    • (2000) EMBO Rep. , vol.1 , pp. 287-292
    • Simpson, J.C.1    Wellenreuther, R.2    Poustka, A.3    Pepperkok, R.4    Wiemann, S.5
  • 108
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: proper and fitting
    • Sprague, B. L. and McNally, J. G. (2005). FRAP analysis of binding: proper and fitting. Trends Cell Biol. 15, 84-91.
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 109
    • 34447549180 scopus 로고    scopus 로고
    • Differential requirements for ts-O45-G and procollagen biosynthetic transport
    • Starkuviene, V. and Pepperkok, R. (2007). Differential requirements for ts-O45-G and procollagen biosynthetic transport. Traffic 8, 1035-1051.
    • (2007) Traffic , vol.8 , pp. 1035-1051
    • Starkuviene, V.1    Pepperkok, R.2
  • 110
    • 6344222240 scopus 로고    scopus 로고
    • High-content screening microscopy identifies novel proteins with a putative role in secretory membrane traffic
    • Starkuviene, V., Liebel, U., Simpson, J. C., Erfle, H., Poustka, A., Wiemann, S. and Pepperkok, R. (2004). High-content screening microscopy identifies novel proteins with a putative role in secretory membrane traffic. Genome Res. 14 10A, 1948-1956.
    • (2004) Genome Res. , vol.1410 A , pp. 1948-1956
    • Starkuviene, V.1    Liebel, U.2    Simpson, J.C.3    Erfle, H.4    Poustka, A.5    Wiemann, S.6    Pepperkok, R.7
  • 112
    • 0037296519 scopus 로고    scopus 로고
    • De novo formation, fusion and fission of mammalian COPIIcoated endoplasmic reticulum exit sites
    • Stephens, D. J. (2003). De novo formation, fusion and fission of mammalian COPIIcoated endoplasmic reticulum exit sites. EMBO Rep. 4, 210-217.
    • (2003) EMBO Rep. , vol.4 , pp. 210-217
    • Stephens, D.J.1
  • 113
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
    • Stephens, D. J., Lin-Marq, N., Pagano, A., Pepperkok, R. and Paccaud, J. P. (2000). COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites. J. Cell Sci. 113, 2177-2185.
    • (2000) J. Cell Sci. , vol.113 , pp. 2177-2185
    • Stephens, D.J.1    Lin-Marq, N.2    Pagano, A.3    Pepperkok, R.4    Paccaud, J.P.5
  • 114
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie, B., White, J., Röttger, S., Stelzer, E. H., Suganuma, T. and Nilsson, T. (1998). Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143, 1505-1521.
    • (1998) J. Cell Biol. , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Röttger, S.3    Stelzer, E.H.4    Suganuma, T.5    Nilsson, T.6
  • 116
    • 80054729346 scopus 로고    scopus 로고
    • COPII and COPI traffic at the ER-Golgi interface
    • Szul, T. and Sztul, E. (2011). COPII and COPI traffic at the ER-Golgi interface. Physiology (Bethesda) 26, 348-364.
    • (2011) Physiology (Bethesda) , vol.26 , pp. 348-364
    • Szul, T.1    Sztul, E.2
  • 120
    • 84877798531 scopus 로고    scopus 로고
    • Feedback regulation of microscopes by image processing
    • Tsukada, Y. and Hashimoto, K. (2013). Feedback regulation of microscopes by image processing. Dev. Growth Differ. 55, 550-562.
    • (2013) Dev. Growth Differ. , vol.55 , pp. 550-562
    • Tsukada, Y.1    Hashimoto, K.2
  • 121
    • 84920166946 scopus 로고    scopus 로고
    • ER-to-Golgi transport
    • In The Golgi Apparatus (ed. A. Mironov and M. Pavelka). Vienna: Springer.
    • Verissimo, F. and Pepperkok, R. (2008). ER-to-Golgi transport. In The Golgi Apparatus (ed. A. Mironov and M. Pavelka), pp. 333-341. Vienna: Springer.
    • (2008) , pp. 333-341
    • Verissimo, F.1    Pepperkok, R.2
  • 124
    • 42049108013 scopus 로고    scopus 로고
    • Video-rate far-field optical nanoscopy dissects synaptic vesicle movement
    • Westphal, V., Rizzoli, S. O., Lauterbach, M. A., Kamin, D., Jahn, R. and Hell, S. W. (2008). Video-rate far-field optical nanoscopy dissects synaptic vesicle movement. Science 320, 246-249.
    • (2008) Science , vol.320 , pp. 246-249
    • Westphal, V.1    Rizzoli, S.O.2    Lauterbach, M.A.3    Kamin, D.4    Jahn, R.5    Hell, S.W.6
  • 126
    • 84856479181 scopus 로고    scopus 로고
    • Dual-objective STORM reveals threedimensional filament organization in the actin cytoskeleton
    • Xu, K., Babcock, H. P. and Zhuang, X. (2012). Dual-objective STORM reveals threedimensional filament organization in the actin cytoskeleton. Nat. Methods 9, 185-188.
    • (2012) Nat. Methods , vol.9 , pp. 185-188
    • Xu, K.1    Babcock, H.P.2    Zhuang, X.3
  • 127
    • 79953289031 scopus 로고    scopus 로고
    • Confined activation and subdiffractive localization enables whole-cell PALM with genetically expressed probes
    • York, A. G., Ghitani, A., Vaziri, A., Davidson, M. W. and Shroff, H. (2011). Confined activation and subdiffractive localization enables whole-cell PALM with genetically expressed probes. Nat. Methods 8, 327-333.
    • (2011) Nat. Methods , vol.8 , pp. 327-333
    • York, A.G.1    Ghitani, A.2    Vaziri, A.3    Davidson, M.W.4    Shroff, H.5
  • 129
    • 84868547684 scopus 로고    scopus 로고
    • Quantitative intensitybased FRET approaches-a comparative snapshot
    • Zeug, A., Woehler, A., Neher, E. and Ponimaskin, E. G. (2012). Quantitative intensitybased FRET approaches-a comparative snapshot. Biophys. J. 103, 1821-1827.
    • (2012) Biophys. J. , vol.103 , pp. 1821-1827
    • Zeug, A.1    Woehler, A.2    Neher, E.3    Ponimaskin, E.G.4


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