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Volumn 76, Issue 5, 1999, Pages 2843-2851

Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

BREFELDIN A; DITHIOTHREITOL; GREEN FLUORESCENT PROTEIN;

EID: 0033059157     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77438-2     Document Type: Article
Times cited : (266)

References (45)
  • 2
    • 0031025764 scopus 로고    scopus 로고
    • Internal trafficking and surface mobility of a functionally intact β2-adrenergic receptor-green fluorescent protein conjugate
    • Barak, L. S., S. S. Ferguson, J. Zhang, C. Matenson, T. Meyer, and M. G. Caron. 1997. Internal trafficking and surface mobility of a functionally intact β2-adrenergic receptor-green fluorescent protein conjugate. Mol. Pharmacol. 51:177-184.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 177-184
    • Barak, L.S.1    Ferguson, S.S.2    Zhang, J.3    Matenson, C.4    Meyer, T.5    Caron, M.G.6
  • 3
    • 0027319987 scopus 로고
    • Cytoplasmic viscosity near the cell plasma membrane: Measurement by evanescent field frequency-domain microfluorimetry
    • Bicknese, S., N. Periasamy, S. B. Shohet, and A. S. Verkman. 1993. Cytoplasmic viscosity near the cell plasma membrane: measurement by evanescent field frequency-domain microfluorimetry. Biophys. J. 165: 1272-1282.
    • (1993) Biophys. J. , vol.165 , pp. 1272-1282
    • Bicknese, S.1    Periasamy, N.2    Shohet, S.B.3    Verkman, A.S.4
  • 6
    • 0030879870 scopus 로고    scopus 로고
    • The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane
    • Cox, J. S., R. E. Chapman, and P. Walter. 1997. The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol. Biol. Cell. 8:1805-1814.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1805-1814
    • Cox, J.S.1    Chapman, R.E.2    Walter, P.3
  • 9
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg, J., E. D. Siggia, J. E. Moreira, C. L. Smith, J. F. Presley, H. J. Worman, and J. Lippincott-Schwartz. 1997. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell. Biol. 138:1193-1206.
    • (1997) J. Cell. Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 10
    • 0028930178 scopus 로고
    • Cell volume measured in adherent cells by total internal reflection microfluorimetry: Application to permeability in cells transfected with water channel homologs
    • Farinas, J., V. Simenak, and A. S. Verkman. 1995. Cell volume measured in adherent cells by total internal reflection microfluorimetry: application to permeability in cells transfected with water channel homologs. Biophys. J. 68:1613-1620.
    • (1995) Biophys. J. , vol.68 , pp. 1613-1620
    • Farinas, J.1    Simenak, V.2    Verkman, A.S.3
  • 11
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
    • Feder, T. J., I. Brust-Mascher, J. P. Slattery, B. Baird, and W. W. Webb. 1996. Constrained diffusion or immobile fraction on cell surfaces: a new interpretation. Biophys. J. 70:2367-2373.
    • (1996) Biophys. J. , vol.70 , pp. 2367-2373
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 12
    • 0025976539 scopus 로고
    • Low viscosity in the aqueous domain of cytoplasm measured by picosecond polarization microscopy
    • Fushimi, K., and A. S. Verkman. 1991. Low viscosity in the aqueous domain of cytoplasm measured by picosecond polarization microscopy. J. Cell Biol. 112:719-725.
    • (1991) J. Cell Biol. , vol.112 , pp. 719-725
    • Fushimi, K.1    Verkman, A.S.2
  • 13
    • 0030600135 scopus 로고    scopus 로고
    • Green fluorescent protein: Applications to cell biology
    • Gerdes, H.-H., and C. Kaether. 1996. Green fluorescent protein: applications to cell biology. FEBS Lett. 389:44-47.
    • (1996) FEBS Lett. , vol.389 , pp. 44-47
    • Gerdes, H.-H.1    Kaether, C.2
  • 14
    • 0028091981 scopus 로고
    • Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells
    • Griffiths, G., M. Ericsson, J. Krijnse-Locker, T. Nilsson, B. Goud, H. D. Sàling, B. L. Tang, S. H. Wong, and W. Hong. 1994. Localization of the Lys, Asp, Glu, Leu tetrapeptide receptor to the Golgi complex and the intermediate compartment in mammalian cells. J. Cell Biol. 127: 1557-1574.
    • (1994) J. Cell Biol. , vol.127 , pp. 1557-1574
    • Griffiths, G.1    Ericsson, M.2    Krijnse-Locker, J.3    Nilsson, T.4    Goud, B.5    Sàling, H.D.6    Tang, B.L.7    Wong, S.H.8    Hong, W.9
  • 15
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and A. Helenius. 1995. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7:525-539.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 525-539
    • Hammond, C.1    Helenius, A.2
  • 16
    • 0026659680 scopus 로고
    • The endoplasmic reticulum as a protein-folding compartment
    • Helenius, A., T. Marquardt, and I. Braakman. 1992. The endoplasmic reticulum as a protein-folding compartment. Trends Cell Biol. 2:227-231.
    • (1992) Trends Cell Biol. , vol.2 , pp. 227-231
    • Helenius, A.1    Marquardt, T.2    Braakman, I.3
  • 17
    • 0027529545 scopus 로고
    • Determinants of the translational diffusion of a small solute in cytoplasm
    • Kao, H. P., J. R. Abney, and A. S. Verkman. 1993. Determinants of the translational diffusion of a small solute in cytoplasm. J. Cell Biol. 120:175-184.
    • (1993) J. Cell Biol. , vol.120 , pp. 175-184
    • Kao, H.P.1    Abney, J.R.2    Verkman, A.S.3
  • 18
    • 0029919980 scopus 로고    scopus 로고
    • Construction and performance of a FRAP instrument with microsecond time resolution
    • Kao, H. P., and A. S. Verkman. 1996. Construction and performance of a FRAP instrument with microsecond time resolution. Biophys. Chem. 59:203-210.
    • (1996) Biophys. Chem. , vol.59 , pp. 203-210
    • Kao, H.P.1    Verkman, A.S.2
  • 19
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R. D., J. G. Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 20
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen, M., J. Farinas, Y. Li, and A. S. Verkman. 1998. Green fluorescent protein as a noninvasive intracellular pH indicator. Biophys. J. 74: 1591-1600.
    • (1998) Biophys. J. , vol.74 , pp. 1591-1600
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 21
    • 0023334387 scopus 로고
    • Visualization of the intact endoplasmic reticulum by immunofluorescence with antibodies to the major ER glycoprotein, endoplasmin
    • Koch, G. L. E., D. R. J. Macer, and M. J. Smith. 1987. Visualization of the intact endoplasmic reticulum by immunofluorescence with antibodies to the major ER glycoprotein, endoplasmin. J. Cell. Sci. 87:535-542.
    • (1987) J. Cell. Sci. , vol.87 , pp. 535-542
    • Koch, G.L.E.1    Macer, D.R.J.2    Smith, M.J.3
  • 22
    • 0023693945 scopus 로고
    • Dynamic behavior of endoplasmic reticulum in living cells
    • Lee, C., and L. B. Chen. 1988. Dynamic behavior of endoplasmic reticulum in living cells. Cell 54:37-46.
    • (1988) Cell , vol.54 , pp. 37-46
    • Lee, C.1    Chen, L.B.2
  • 23
    • 0023375957 scopus 로고
    • Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 fibroblasts
    • Luby-Phelps, K., P. E. Castle, D. L. Taylor, and F. Lanni. 1987. Hindered diffusion of inert tracer particles in the cytoplasm of mouse 3T3 fibroblasts. Proc. Natl. Acad. Sci. USA. 84:4910-4913.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4910-4913
    • Luby-Phelps, K.1    Castle, P.E.2    Taylor, D.L.3    Lanni, F.4
  • 24
    • 0027244531 scopus 로고
    • A novel fluorescence ratiometric method confirms the low solvent viscosity of the cytoplasm
    • Luby-Phelps, K., S. Mujundar, R. Mujundar, L. Ernst, W. Galbraith, and A. Waggoner. 1993. A novel fluorescence ratiometric method confirms the low solvent viscosity of the cytoplasm. Biophys. J. 65:236-242.
    • (1993) Biophys. J. , vol.65 , pp. 236-242
    • Luby-Phelps, K.1    Mujundar, S.2    Mujundar, R.3    Ernst, L.4    Galbraith, W.5    Waggoner, A.6
  • 25
    • 0028077034 scopus 로고
    • The cellular response to unfolded proteins: Intercompartmental signaling
    • McMillan, D. R., M. J. Gething, and J. Sambrook. 1994. The cellular response to unfolded proteins: intercompartmental signaling. Curr. Opin. Biotechnol. 5:540-545.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 540-545
    • McMillan, D.R.1    Gething, M.J.2    Sambrook, J.3
  • 26
    • 0031968609 scopus 로고    scopus 로고
    • Monte Carlo analysis of obstructed diffusion in three dimensions: Application to molecular diffusion in organelles
    • Ölveczky, B. P., and A. S. Verkman. 1998. Monte Carlo analysis of obstructed diffusion in three dimensions: application to molecular diffusion in organelles. Biophys. J. 74:2722-2730.
    • (1998) Biophys. J. , vol.74 , pp. 2722-2730
    • Ölveczky, B.P.1    Verkman, A.S.2
  • 27
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormø, M., A. B. Cubitt, K. Kallio, L. A. Gross, R. Y. Tsien, and S. J. Remington. 1996. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 273:1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormø, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 28
    • 0000037251 scopus 로고    scopus 로고
    • Rapid diffusion of green fluorescent protein in the mitochondrial matrix
    • Partikian, A., B. Ölveczky, R. Swaminathan, Y. Li, and A. S. Verkman. 1998. Rapid diffusion of green fluorescent protein in the mitochondrial matrix. J. Cell Biol. 140:821-829.
    • (1998) J. Cell Biol. , vol.140 , pp. 821-829
    • Partikian, A.1    Ölveczky, B.2    Swaminathan, R.3    Li, Y.4    Verkman, A.S.5
  • 29
    • 0030093975 scopus 로고    scopus 로고
    • Reversible photobleaching of fluorescein conjugates in air-saturated viscous solutions: Molecular tryptophan as a triplet state quencher
    • Periasamy, N., S. Bicknese, and A. S. Verkman. 1996. Reversible photobleaching of fluorescein conjugates in air-saturated viscous solutions: molecular tryptophan as a triplet state quencher. Photochem. Photobiol. 63:265-271.
    • (1996) Photochem. Photobiol. , vol.63 , pp. 265-271
    • Periasamy, N.1    Bicknese, S.2    Verkman, A.S.3
  • 30
    • 0031861817 scopus 로고    scopus 로고
    • Analysis of fluorophore diffusion by continuous distributions of diffusion coefficients: Application to photobleaching measurements of simple and anomalous diffusion
    • Periasamy, N., and A. S. Verkman. 1998. Analysis of fluorophore diffusion by continuous distributions of diffusion coefficients: application to photobleaching measurements of simple and anomalous diffusion. Biophys. J. 75:557-567.
    • (1998) Biophys. J. , vol.75 , pp. 557-567
    • Periasamy, N.1    Verkman, A.S.2
  • 31
    • 0030955328 scopus 로고    scopus 로고
    • ER to Golgi transport visualized in living cells: Microtubule dependent translocation of tubulovesiclar intermediates
    • Presley, J. F., N. B. Cole., T. A. Schroer, K. Hirschberg, K. J. M. Zaal, and J. Lippincott-Schwartz. 1997. ER to Golgi transport visualized in living cells: microtubule dependent translocation of tubulovesiclar intermediates. Nature. 389:81-85.
    • (1997) Nature , vol.389 , pp. 81-85
    • Presley, J.F.1    Cole, N.B.2    Schroer, T.A.3    Hirschberg, K.4    Zaal, K.J.M.5    Lippincott-Schwartz, J.6
  • 32
    • 0029311281 scopus 로고
    • Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells
    • Rizzuto, R., M. Brini, P. Pizzo, M. Murgia, and T. Pozzan. 1995. Chimeric green fluorescent protein as a tool for visualizing subcellular organelles in living cells. Curr. Biol. 5:636-642.
    • (1995) Curr. Biol. , vol.5 , pp. 636-642
    • Rizzuto, R.1    Brini, M.2    Pizzo, P.3    Murgia, M.4    Pozzan, T.5
  • 34
    • 0030742748 scopus 로고    scopus 로고
    • Translational diffusion of macromolecule-size solutes in cytoplasm and nucleus
    • Seksek, O., J. Biwersi, and A. S. Verkman. 1997. Translational diffusion of macromolecule-size solutes in cytoplasm and nucleus. J. Cell. Biol. 138:131-142.
    • (1997) J. Cell. Biol. , vol.138 , pp. 131-142
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 36
    • 0029610381 scopus 로고
    • Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex
    • Stinchcombe, J. C., H. Nomoto, D. F. Cutler, and C. R. Hopkins. 1995. Anterograde and retrograde traffic between the rough endoplasmic reticulum and the Golgi complex. J. Cell Biol. 131:1387-1401.
    • (1995) J. Cell Biol. , vol.131 , pp. 1387-1401
    • Stinchcombe, J.C.1    Nomoto, H.2    Cutler, D.F.3    Hopkins, C.R.4
  • 37
    • 0030780576 scopus 로고    scopus 로고
    • Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores
    • Subramanian, K., and T. Meyer. 1997. Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores. Cell. 89: 963-71.
    • (1997) Cell , vol.89 , pp. 963-971
    • Subramanian, K.1    Meyer, T.2
  • 38
    • 0029782661 scopus 로고    scopus 로고
    • Cytoplasmic viscosity near the cell plasma membrane: Translation of BCECF measured by total internal reflection-fluorescence photobleaching recovery
    • Swaminathan, R., S. Bicknese, N. Periasamy, and A. S. Verkman. 1996. Cytoplasmic viscosity near the cell plasma membrane: translation of BCECF measured by total internal reflection-fluorescence photobleaching recovery. Biophys. J. 71:1140-1151.
    • (1996) Biophys. J. , vol.71 , pp. 1140-1151
    • Swaminathan, R.1    Bicknese, S.2    Periasamy, N.3    Verkman, A.S.4
  • 39
    • 0031000601 scopus 로고    scopus 로고
    • Photochemical properties of green fluorescent protein GFP-S65T in solution and transfected CHO cells: Analysis of cytoplasmic viscosity by GFP translational and rotational diffusion
    • Swaminathan, R., C. P. Hoang, and A. S. Verkman. 1997. Photochemical properties of green fluorescent protein GFP-S65T in solution and transfected CHO cells: analysis of cytoplasmic viscosity by GFP translational and rotational diffusion. Biophys. J. 72:1900-1907.
    • (1997) Biophys. J. , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 40
    • 0032524048 scopus 로고    scopus 로고
    • Defective trafficking of AQP2 water channels in nephrogenic diabetes insipidus and correction by chemical chaperones
    • Tamarappoo, B. K., and A. S. Verkman. 1998. Defective trafficking of AQP2 water channels in nephrogenic diabetes insipidus and correction by chemical chaperones. J. Clin. Invest. 101:2257-2267.
    • (1998) J. Clin. Invest. , vol.101 , pp. 2257-2267
    • Tamarappoo, B.K.1    Verkman, A.S.2
  • 41
    • 0030296813 scopus 로고    scopus 로고
    • Structural change of the endoplasmic reticulum during fertilization: Evidence for loss of membrane continuity using the green fluorescent protein
    • Terasaki, M., L. A. Jaffe, G. R. Hunnicutt, and J. A. Hammer. 1996. Structural change of the endoplasmic reticulum during fertilization: evidence for loss of membrane continuity using the green fluorescent protein. Dev. Biol. 179:320-328.
    • (1996) Dev. Biol. , vol.179 , pp. 320-328
    • Terasaki, M.1    Jaffe, L.A.2    Hunnicutt, G.R.3    Hammer, J.A.4
  • 42
    • 0032938970 scopus 로고    scopus 로고
    • Green fluorescent protein as a probe to study intracellular solute diffusion
    • Verkman, A. S. 1999. Green fluorescent protein as a probe to study intracellular solute diffusion. Meth. Enzymol 302:250-265.
    • (1999) Meth. Enzymol , vol.302 , pp. 250-265
    • Verkman, A.S.1
  • 43
    • 0025805239 scopus 로고
    • Construction and evaluation of a frequency-domain epifluorescence microscope for lifetime and anisotropy decay measurements in subcellular domains
    • Verkman, A. S., M. Armijo, and K. Fushimi. 1991. Construction and evaluation of a frequency-domain epifluorescence microscope for lifetime and anisotropy decay measurements in subcellular domains. Biophys. Chem. 40:117-125.
    • (1991) Biophys. Chem. , vol.40 , pp. 117-125
    • Verkman, A.S.1    Armijo, M.2    Fushimi, K.3
  • 45
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., L. G. Moss, and G. N. Phillips. 1996. The molecular structure of green fluorescent protein. Nature Biotech. 14:1264-1251.
    • (1996) Nature Biotech. , vol.14 , pp. 1264-11251
    • Yang, F.1    Moss, L.G.2    Phillips, G.N.3


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