메뉴 건너뛰기




Volumn 2, Issue 6, 2001, Pages 444-456

Studying protein dynamics in living cells

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; PHOTOPROTEIN; PROTEIN;

EID: 0035374872     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35073068     Document Type: Review
Times cited : (1020)

References (130)
  • 1
    • 0032867477 scopus 로고    scopus 로고
    • Fluorescent proteins from nonbioluminescent Anthozoa species
    • erratum 17, 1227 (1999)
    • Matz, M. V. et al. Fluorescent proteins from nonbioluminescent Anthozoa species. Nature Biotechnol. 17, 969-973 (1999); erratum 17, 1227 (1999).
    • (1999) Nature Biotechnol. , vol.17 , pp. 969-973
    • Matz, M.V.1
  • 2
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. The green fluorescent protein. Annu. Pev. Biochem. 67, 509-544 (1998).
    • (1998) Annu. Pev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 3
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • Heim, R., Prasher, D. C. & Tsien, R. Y. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc. Natl Acad. Sci. USA 91, 12501-12504 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 4
    • 0031000601 scopus 로고    scopus 로고
    • Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
    • Swaminathan, R., Hoang, C. P. & Verkman, A. S. Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys. J. 72, 1900-1907 (1997). Characterizes the photobleaching properties of GFP in solution and in vivo in the cytoplasm.
    • (1997) Biophys. J. , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 5
    • 0003840881 scopus 로고    scopus 로고
    • (eds Sullivan, K. & Kay. S.) Academic, San Diego
    • Lippincott-Schwartz, J. et al. in Green Fluorescent Proteins (eds Sullivan, K. & Kay. S.) 261-291 (Academic, San Diego, 1999).
    • (1999) Green Fluorescent Proteins , pp. 261-291
    • Lippincott-Schwartz, J.1
  • 6
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G. & Phillips, G. N. J. The molecular structure of green fluorescent protein. Nature Biotechnol. 14, 1246-1251 (1996).
    • (1996) Nature Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips, G.N.J.3
  • 7
    • 0032621293 scopus 로고    scopus 로고
    • Biophysics of the green fluorescent protein
    • Prendergast, F. G. Biophysics of the green fluorescent protein. Methods Cell Biol. 58, 1-18 (1999).
    • (1999) Methods Cell Biol. , vol.58 , pp. 1-18
    • Prendergast, F.G.1
  • 8
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., Koppel, D. E., Schlessinger, J., Elson, E. & Webb, W. W. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16, 1055-1069 (1976).
    • (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
  • 9
    • 0033082623 scopus 로고    scopus 로고
    • Photobleaching GFP reveals protein dynamics inside living cells
    • White, J. & Stelzer, E. Photobleaching GFP reveals protein dynamics inside living cells. Trends Cell Biol. 9, 61-65 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 61-65
    • White, J.1    Stelzer, E.2
  • 10
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: Applications to membrane dynamics
    • Saxton, M. J. & Jacobsen, K. Single-particle tracking: applications to membrane dynamics. Annu. Rev. Biophys. Biomol. Struct. 26, 373-399 (1997).
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobsen, K.2
  • 11
    • 0001864939 scopus 로고
    • eds Edidin, M., Szollosi, J. & Iron. L. CRC Press, Boca Raton, Florida
    • Edidin, M. in Mobility and Proximity in Biological Membranes (eds Edidin, M., Szollosi, J. & Iron. L.) 109-135 (CRC Press, Boca Raton, Florida, 1994).
    • (1994) Mobility and Proximity in Biological Membranes , pp. 109-135
    • Edidin, M.1
  • 12
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
    • Feder, T. J., Brust-Mascher, I., Slattery, J. P., Baird, B. & Webb, W. W. Constrained diffusion or immobile fraction on cell surfaces: a new interpretation. Biophys. J. 70, 2767-2773 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 2767-2773
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 13
    • 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. et al. 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). Shows the connectivity of the endoplasmic reticulum (ER) and nuclear envelope in vivo and provides a visual example of how a protein can be mobile in one domain of the cell and immobile in another domain.
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1
  • 15
    • 0029784190 scopus 로고    scopus 로고
    • Diffusional mobility of Golgi proteins in membranes of living cells
    • Cole, N. B. et al. Diffusional mobility of Golgi proteins in membranes of living cells. Science 273, 797-801 (1996). First paper to use FRAP to measure the diffusion rate of a GFP chimaera in a cellular organelle, the Golgi. In addition, this paper introduces the FLIP method of photobleaching.
    • (1996) Science , vol.273 , pp. 797-801
    • Cole, N.B.1
  • 16
    • 0030782188 scopus 로고    scopus 로고
    • Golgi tubule traffic and the effects of brefeldin A visualized in living cells
    • Sciaky, N. et al. Golgi tubule traffic and the effects of brefeldin A visualized in living cells. J. Cell Biol. 139, 1137-1155 (1997).
    • (1997) J. Cell Biol. , vol.139 , pp. 1137-1155
    • Sciaky, N.1
  • 17
    • 0000037251 scopus 로고    scopus 로고
    • Rapid diffusion of green fluorescent protein in the mitochondrial matrix
    • Partikian, A., Olveczky, B., Swaminathan, R., Li, Y. & Verkman, A. S. Rapid diffusion of green fluorescent protein in the mitochondrial matrix. J. Cell Biol. 140, 821-829 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 821-829
    • Partikian, A.1    Olveczky, B.2    Swaminathan, R.3    Li, Y.4    Verkman, A.S.5
  • 18
    • 0031968609 scopus 로고    scopus 로고
    • Monte Carlo analysis of obstructed diffusion in three dimensions: Application to molecular diffusion in organelles
    • Olveczky, B. P. & Verkman, A. S. Monte Carlo analysis of obstructed diffusion in three dimensions: application to molecular diffusion in organelles. Biophys. J. 74, 2722-2730 (1998).
    • (1998) Biophys. J. , vol.74 , pp. 2722-2730
    • Olveczky, B.P.1    Verkman, A.S.2
  • 19
    • 0033807598 scopus 로고    scopus 로고
    • Diffusion in an inhomogeneous media: Theory and simulations applied to a whole cell photobleach recovery
    • Siggia, E. D., Lippincott-Schwartz, J. & Bekiranov, S. Diffusion in an inhomogeneous media: theory and simulations applied to a whole cell photobleach recovery. Biophys. J. 79, 1761-1770 (2000). Describes a simulation program that can be used to calculate diffusion rates from FRAP data obtained by a confocal microscope.
    • (2000) Biophys. J. , vol.79 , pp. 1761-1770
    • Siggia, E.D.1    Lippincott-Schwartz, J.2    Bekiranov, S.3
  • 20
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • Dayel, M. J., Horn, E. F. Y. & Verkman, A. S. Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys. J. 76, 2843-2851 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Horn, E.F.Y.2    Verkman, A.S.3
  • 21
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D. & Misteli, T. High mobility of proteins in the mammalian cell nucleus. Nature 404, 604-609 (2000). The relatively slow diffusion rates of several nuclear GFP chimaeras are due to the high density of binding sites for the chimaeras throughout the nucleus. A kinetic model of the protein dynamics is used to calculate the on/off rates of chimaera binding.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 22
    • 0028936853 scopus 로고
    • Analysis of simulated and experimental fluorescence recovery after photobleaching. Data for two diffusing components
    • Gordon, G. W., Chazotte, B., Wang, X. F. & Herman, B. Analysis of simulated and experimental fluorescence recovery after photobleaching. Data for two diffusing components. Biophys. J. 68, 766-778 (1995).
    • (1995) Biophys. J. , vol.68 , pp. 766-778
    • Gordon, G.W.1    Chazotte, B.2    Wang, X.F.3    Herman, B.4
  • 23
    • 0031861817 scopus 로고    scopus 로고
    • Analysis of fluorophore diffusion by continous distributions of diffusion coefficients: Application to photobleaching measurements of multicomponent and anomalous diffusion
    • Periasamy, N. & Verkman, A. S. Analysis of fluorophore diffusion by continous distributions of diffusion coefficients: application to photobleaching measurements of multicomponent and anomalous diffusion. Biophys. J. 75, 557-567 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 557-567
    • Periasamy, N.1    Verkman, A.S.2
  • 24
    • 0034631851 scopus 로고    scopus 로고
    • Reduced mobility of the alternate splicing factor (ASF) through the nucleoplasm and steady state speckle compartments
    • Kruhlak, M. J. et al. Reduced mobility of the alternate splicing factor (ASF) through the nucleoplasm and steady state speckle compartments. J. Cell Biol. 150, 41-51 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 41-51
    • Kruhlak, M.J.1
  • 25
    • 0033532342 scopus 로고    scopus 로고
    • Action of DMA repair endonuclease ERCC1/XPF in living cells
    • Houtsmuller, A. B. et al. Action of DMA repair endonuclease ERCC1/XPF in living cells. Science 284, 958-961 (2000).
    • (2000) Science , vol.284 , pp. 958-961
    • Houtsmuller, A.B.1
  • 26
    • 0016146318 scopus 로고
    • Lateral diffusion of rhodopsin in the photoreceptor membrane
    • Poo, M. M. & Cone, R. A. Lateral diffusion of rhodopsin in the photoreceptor membrane. Nature 247, 438-441 (1974).
    • (1974) Nature , vol.247 , pp. 438-441
    • Poo, M.M.1    Cone, R.A.2
  • 27
    • 0033180470 scopus 로고    scopus 로고
    • Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assemby and retention of these molecules in the endoplasmic reticulum
    • Marguet, D. et al. Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assemby and retention of these molecules in the endoplasmic reticulum. Immunity 11, 231-240 (1999). Characterizes the effect of the formation of large protein complexes of TAP and MHC class I in the ER membrane on the diffusion rate, and calculates the relative contributions of several diffusing species to a single apparent diffusion coefficient.
    • (1999) Immunity , vol.11 , pp. 231-240
    • Marguet, D.1
  • 28
    • 0033544712 scopus 로고    scopus 로고
    • Golgi membranes are absorbed into and reemerge from the ER during mitosis
    • Zaal, K. J. M. et al. Golgi membranes are absorbed into and reemerge from the ER during mitosis. Cell 99, 589-601 (1999). Uses FRAP to measure the mobilty of a Golgi membrane protein during interphase and metaphase to test whether the Golgi fragments or fuses with the endoplasmic reticulum during mitosis. In addition, selective photobleaching is used to calculate the relative rates of transport between the ER and Golgi in both directions.
    • (1999) Cell , vol.99 , pp. 589-601
    • Zaal, K.J.M.1
  • 29
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • Saxton, M. Anomalous diffusion due to obstacles: a Monte Carlo study. Biophys. J. 66, 394-401 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 394-401
    • Saxton, M.1
  • 30
    • 0030050141 scopus 로고    scopus 로고
    • Anomalous diffusion due to binding: A Monte Carlo study
    • Saxton, M. Anomalous diffusion due to binding: a Monte Carlo study. Biophys. J. 70, 1250-1262 (1996).
    • (1996) Biophys. J. , vol.70 , pp. 1250-1262
    • Saxton, M.1
  • 31
    • 0032563564 scopus 로고    scopus 로고
    • Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent-protein
    • Adams, C. L., Chen, Y., Smith, S. J. & Nelson, W. J. Mechanisms of epithelial cell-cell adhesion and cell compaction revealed by high-resolution tracking of E-cadherin-green fluorescent-protein. J. Cell Biol. 142, 1105-1119 (1998).
    • (1998) J. Cell Biol. , vol.142 , pp. 1105-1119
    • Adams, C.L.1    Chen, Y.2    Smith, S.J.3    Nelson, W.J.4
  • 32
    • 0033782030 scopus 로고    scopus 로고
    • Dynamics and retention of misfolded proteins in native ER membranes
    • Nehls, S. et al. Dynamics and retention of misfolded proteins in native ER membranes. Nature Cell Biol. 2, 288-295 (2000). The diffusion rates and mobility of misfolded aggregated ER membrane proteins are compared to correctly folded proteins and are found to be similar. Only conditions that globally perturb folding in the ER were found to have an effect on protein mobility.
    • (2000) Nature Cell Biol. , vol.2 , pp. 288-295
    • Nehls, S.1
  • 33
    • 0030780576 scopus 로고    scopus 로고
    • Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores
    • Subramanian, K. & Meyer, T. Calcium-induced restructuring of nuclear envelope and endoplasmic reticulum calcium stores. Cell 89, 963-971 (1997).
    • (1997) Cell , vol.89 , pp. 963-971
    • Subramanian, K.1    Meyer, T.2
  • 34
    • 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., Jaffe, L. A., Hunnicutt, G. R. & Hammer, J. A. R. 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).
    • (1996) Dev. Biol. , vol.179 , pp. 320-328
    • Terasaki, M.1    Jaffe, L.A.2    Hunnicutt, G.R.3    Hammer, J.A.R.4
  • 35
    • 0038620661 scopus 로고    scopus 로고
    • Exchange of protein molecules through connections between higher plastids
    • Kohler, R. H., Cao, J., Zipfel, W. R., Webb, W. W. & Hanson, M. R. Exchange of protein molecules through connections between higher plastids. Science 276, 2039-2042 (1997).
    • (1997) Science , vol.276 , pp. 2039-2042
    • Kohler, R.H.1    Cao, J.2    Zipfel, W.R.3    Webb, W.W.4    Hanson, M.R.5
  • 36
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of Golgi-resident glycosyttransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie, B. et al. Recycling of Golgi-resident glycosyttransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J. Cell Biol. 143, 1505-1521 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1505-1521
    • Storrie, B.1
  • 38
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate form COPII in close proximity to ER exit sites
    • Stephens, D. J., Lin-Marq, N., Pagano, A., Pepperkok, R. & Paccaud, J. P. COPI-coated ER-to-Golgi transport complexes segregate form COPII in close proximity to ER exit sites. J. Cell Sci. 113, 2177-2185 (2000).
    • (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
  • 39
    • 0031802483 scopus 로고    scopus 로고
    • The distribution and translocation of the G protein ADP-ribosylation factor 1 in live cells is determined by its GTPase activity
    • Vasudevan, C. et al. The distribution and translocation of the G protein ADP-ribosylation factor 1 in live cells is determined by its GTPase activity. J. Cell Sci. 111, 1277-1285 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 1277-1285
    • Vasudevan, C.1
  • 40
    • 0032498538 scopus 로고    scopus 로고
    • Fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators of diacylglycerd signaling in living cells
    • Oancea, E., Teruel, M. N., Quest, A. F. & Meyer, T. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators of diacylglycerd signaling in living cells. J. Cell Biol. 140, 485-498 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 485-498
    • Oancea, E.1    Teruel, M.N.2    Quest, A.F.3    Green, M.T.4
  • 42
    • 0030955328 scopus 로고    scopus 로고
    • ER-to-Golgi transport visualized in living cells
    • Presley, J. F. et al. ER-to-Golgi transport visualized in living cells. Nature 389, 81-65 (1997).
    • (1997) Nature , vol.389 , pp. 81-165
    • Presley, J.F.1
  • 43
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg, K. et al. Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143, 1485-1503 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 1485-1503
    • Hirschberg, K.1
  • 44
    • 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, 659-674 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 659-674
    • Nakata, T.1    Terada, S.2    Hirokawa, N.3
  • 45
    • 0028295796 scopus 로고
    • Resonance energy transfer: Methods and applications
    • Wu, P. & Brand, L. Resonance energy transfer: methods and applications. Anal. Biochem. 218, 1-13 (1994).
    • (1994) Anal. Biochem. , vol.218 , pp. 1-13
    • Wu, P.1    Brand, L.2
  • 46
    • 0028924992 scopus 로고
    • Fluorescence resonance energy transfer
    • Clegg, R. M. Fluorescence resonance energy transfer. Curr. Opin. Biotechnol. 6, 103-110 (1995).
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 103-110
    • Clegg, R.M.1
  • 47
    • 0034633010 scopus 로고    scopus 로고
    • Förster distances between green fluorescent protein pairs
    • Patterson, G. H., Piston, D. W. & Barisas, B. G. Förster distances between green fluorescent protein pairs. Anal. Biochem. 284, 438-440 (2000).
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 48
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok, B. A. & Heim, R. Using GFP in FRET-based applications. Trends Cell Biol. 9, 57-60 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 49
    • 0032622353 scopus 로고    scopus 로고
    • Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy
    • Penasamy, A. & Day, R. N. Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy. Methods Cell Biol. 58, 293-314 (1999).
    • (1999) Methods Cell Biol. , vol.58 , pp. 293-314
    • Penasamy, A.1    Day, R.N.2
  • 50
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R. & Tsien, R. Y. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6, 178-182 (1996).
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 52
    • 0033533709 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
    • Wouters, F. S. & Bastiaens, P. I. Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells. Curr. Biol. 9, 1127-1130 (1999). Describes a clever assay to evaluate the phosphorylation state of a protein using FRET.
    • (1999) Curr. Biol. , vol.9 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 53
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy; spatial resolution of biochemical processes in the cell
    • Bastiaens, P. I. & Squire, A. Fluorescence lifetime imaging microscopy; spatial resolution of biochemical processes in the cell. Trends Cell Biol. 9, 48-52 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-52
    • Bastiaens, P.I.1    Squire, A.2
  • 54
    • 0033605542 scopus 로고    scopus 로고
    • Imaging protein kinase Cα activation in cells
    • Ng, T. et al. Imaging protein kinase Cα activation in cells. Science 283, 2085-2089 (1999).
    • (1999) Science , vol.283 , pp. 2085-2089
    • Ng, T.1
  • 55
    • 0033565261 scopus 로고    scopus 로고
    • PKCα regulates β1 intergrin-dependent cell motility through association and control of integrin traffic
    • Ng, T. et al. PKCα regulates β1 intergrin-dependent cell motility through association and control of integrin traffic. EMBO J. 18, 3909-3923 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3909-3923
    • Ng, T.1
  • 56
    • 0033606891 scopus 로고    scopus 로고
    • 2+ concentration changes at the secretory vesicle surface with a recombinant targeted cameleon
    • 2+ concentration changes at the secretory vesicle surface with a recombinant targeted cameleon. Curr. Biol. 9, 915-918 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 915-918
    • Emmanouilidou, E.1
  • 57
    • 0031011418 scopus 로고    scopus 로고
    • 2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. a new class of fluorescent indicators
    • 2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators. J. Biol. Chem. 272, 13270-13274 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 13270-13274
    • Romoser, V.A.1    Hinkle, P.M.2    Persechini, A.3
  • 58
    • 0030610646 scopus 로고    scopus 로고
    • 2+ based on green fluorescent proteins and calmodulin
    • 2+ based on green fluorescent proteins and calmodulin. Nature 388, 882-887 (1997).
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1
  • 59
    • 0033622319 scopus 로고    scopus 로고
    • A genetically encoded, fluorescent indicator for cyclic AMP in living cells
    • Zaccolo, M. et al. A genetically encoded, fluorescent indicator for cyclic AMP in living cells. Nature Cell Biol. 2, 25-29 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 25-29
    • Zaccolo, M.1
  • 60
    • 0035956940 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator
    • Honda, A. et al. Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator. Proc. Natl Acad. Sci. USA 98, 2437-2442 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2437-2442
    • Honda, A.1
  • 61
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein
    • Mitra, R. D., Silva, C. M. & Youvan, D. C. Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene 173, 13-17 (1996).
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 62
    • 0033150406 scopus 로고    scopus 로고
    • Novel mutant green fluorescent protein protease substrates reveal the activation of specific caspases during apoptosis
    • Mahajan, N. P., Harrison-Shostak, D. C., Michaux, J. & Herman, B. Novel mutant green fluorescent protein protease substrates reveal the activation of specific caspases during apoptosis. Chem. Biol. 6, 401-409 (1999).
    • (1999) Chem. Biol. , vol.6 , pp. 401-409
    • Mahajan, N.P.1    Harrison-Shostak, D.C.2    Michaux, J.3    Herman, B.4
  • 63
    • 0033045712 scopus 로고    scopus 로고
    • Imaging fluorescence resonance energy transfer between two green fluorescent proteins in living yeast
    • Sagot, I., Bonneu, M., Balguerie, A. & Aigle, M. Imaging fluorescence resonance energy transfer between two green fluorescent proteins in living yeast. FEBS Lett. 447, 53-57 (1999).
    • (1999) FEBS Lett. , vol.447 , pp. 53-57
    • Sagot, I.1    Bonneu, M.2    Balguerie, A.3    Aigle, M.4
  • 64
    • 0034094370 scopus 로고    scopus 로고
    • Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer
    • Vanderklish, P. W. et al. Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proc. Natl Acad. Sci. USA 97, 2253-2258 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 2253-2258
    • Vanderklish, P.W.1
  • 65
    • 0032522223 scopus 로고    scopus 로고
    • Detection of programmed cell death using fluorescence energy transfer
    • Xu, X. et al. Detection of programmed cell death using fluorescence energy transfer. Nucleic Acids Res. 26, 2034-2035 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2034-2035
    • Xu, X.1
  • 66
    • 0032472195 scopus 로고    scopus 로고
    • Quantitation of transcription and clonal selection of single living cells with β-lactamase as reporter
    • Zlokarnik, G. et al. Quantitation of transcription and clonal selection of single living cells with β-lactamase as reporter. Science 279, 84-88 (1998).
    • (1998) Science , vol.279 , pp. 84-88
    • Zlokarnik, G.1
  • 67
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D. W. & Johnson, C. H. A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl Acad. Sci. USA 96, 151-156 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 68
    • 0034733584 scopus 로고    scopus 로고
    • Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    • Siegel, R. M. et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations. Science 288, 2354-2357 (2000).
    • (2000) Science , vol.288 , pp. 2354-2357
    • Siegel, R.M.1
  • 69
    • 0034733682 scopus 로고    scopus 로고
    • A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling
    • Chan, F. K.-M. et al. A domain in TNF receptors that mediates ligand-independent receptor assembly and signaling. Science 288, 2351-2354 (2000).
    • (2000) Science , vol.288 , pp. 2351-2354
    • Chan, F.K.-M.1
  • 70
    • 0034644538 scopus 로고    scopus 로고
    • Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction
    • Teruel, M. N. & Meyer, T. Translocation and reversible localization of signaling proteins: a dynamic future for signal transduction. Cell 103, 181-184 (2000).
    • (2000) Cell , vol.103 , pp. 181-184
    • Teruel, M.N.1    Meyer, T.2
  • 71
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K. & Ikonen, E. Functional rafts in cell membranes. Nature 387, 569-572 (1997).
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 73
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R. & Mayor, S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394, 798-801 (1998). Uses a variation of FRET, homotransfer, to infer the structure of lipid rafts on the cell surface.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 74
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer
    • Kenworthy, A. K. & Edidin, M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Å using imaging fluorescence resonance energy transfer. J. Cell Biol. 142, 69-84 (1998). Uses acceptor photobleaching FRET to assess the organization of lipid rafts at the cell surface. Contains a detailed discussion of the theory for interpreting FRET from donors and acceptors constrained to membranes.
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 75
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy, A. K., Petranova, N. & Edidin, M. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell 11, 1645-1655 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 77
    • 0030671161 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Diagnostics for sparse molecules
    • Maiti, S., Haupts, V. & Webb, W. W. Fluorescence correlation spectroscopy: diagnostics for sparse molecules. Proc. Natl Acad. Sci. USA 94, 11753-11757 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11753-11757
    • Maiti, S.1    Haupts, V.2    Webb, W.W.3
  • 78
    • 0028229903 scopus 로고
    • Sorting single molecules: Application to diagnostics and evolutionary biotechnology
    • Eigen, M. & Rigler, R. Sorting single molecules: application to diagnostics and evolutionary biotechnology. Proc. Natl Acad. Sci. USA 91, 5740-5747 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 79
    • 0034057428 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Molecular recognition at the single molecule level
    • Van Craenenbroeck, E. & Engelborghs, Y. Fluorescence correlation spectroscopy: molecular recognition at the single molecule level. J. Mol. Recog. 13, 93-100 (2000).
    • (2000) J. Mol. Recog. , vol.13 , pp. 93-100
    • Van Craenenbroeck, E.1    Engelborghs, Y.2
  • 80
    • 0034009901 scopus 로고    scopus 로고
    • An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells
    • Cluzel, P., Surette, M. & Leibler, S. An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells. Science 287, 1652-1655 (2000).
    • (2000) Science , vol.287 , pp. 1652-1655
    • Cluzel, P.1    Surette, M.2    Leibler, S.3
  • 81
    • 0034641711 scopus 로고    scopus 로고
    • Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis
    • Heinze, K. G., Koltermann, A. & Schwille, P. Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis. Proc. Natl Acad. Sci. USA 97, 10377-10382 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10377-10382
    • Heinze, K.G.1    Koltermann, A.2    Schwille, P.3
  • 83
    • 0029742203 scopus 로고    scopus 로고
    • Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement
    • Yokoe, H. & Meyer, T. Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement. Nature Biotechnol. 14, 1252-1256 (1996).
    • (1996) Nature Biotechnol. , vol.14 , pp. 1252-1256
    • Yokoe, H.1    Meyer, T.2
  • 85
    • 0030832226 scopus 로고    scopus 로고
    • On/off blinking and switching behaviour of single molecules of green fluorescent protein
    • Dickson, R. M., Cubitt, A. B., Tsien, R. Y. & Moerner, W. E. On/off blinking and switching behaviour of single molecules of green fluorescent protein. Nature 388, 355-358 (1997).
    • (1997) Nature , vol.388 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 86
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R. & Tsien, R. Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272 (1998).
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 87
    • 0033583073 scopus 로고    scopus 로고
    • Receptor-mediated targeting of fluorescent probes in living cells
    • Farinas, J. & Verkman, A. S. Receptor-mediated targeting of fluorescent probes in living cells. J. Biol. Chem. 274, 7603-7606 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7603-7606
    • Farinas, J.1    Verkman, A.S.2
  • 88
    • 0033850088 scopus 로고    scopus 로고
    • Actin dynamics at the living cell submembrane imaged by total internal reflection fluorescence photobleaching
    • Sund, S. E. & Axelrod, D. Actin dynamics at the living cell submembrane imaged by total internal reflection fluorescence photobleaching. Biophys. J. 79, 1655-1669 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1655-1669
    • Sund, S.E.1    Axelrod, D.2
  • 89
    • 0034599547 scopus 로고    scopus 로고
    • Observing fusion of constitutive membrane traffic in real time by evanescent wave microscopy
    • Toomre, D. K., Steyer, J. A., Almers, W. & Simons, K. Observing fusion of constitutive membrane traffic in real time by evanescent wave microscopy. J. Cell Biol. 149, 33-40 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 33-40
    • Toomre, D.K.1    Steyer, J.A.2    Almers, W.3    Simons, K.4
  • 90
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection fluorescence microscopy
    • Schmoranzer, J., Goulian, M., Axelrod, D. & Simon, S. M. Imaging constitutive exocytosis with total internal reflection fluorescence microscopy. J. Cell Biol. 149, 23-32 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 23-32
    • Schmoranzer, J.1    Goulian, M.2    Axelrod, D.3    Simon, S.M.4
  • 91
    • 0344172555 scopus 로고    scopus 로고
    • Measurement of molecular diffusion in solution by multiphoton fluorescence photobleaching recovery
    • Brown, E. B., Wu, E. S., Zipfel, W. & Webb, W. W. Measurement of molecular diffusion in solution by multiphoton fluorescence photobleaching recovery. Biophys. J. 77, 2837-2849 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 2837-2849
    • Brown, E.B.1    Wu, E.S.2    Zipfel, W.3    Webb, W.W.4
  • 92
    • 0347741641 scopus 로고    scopus 로고
    • Analysis of membrane protein cluster densities and sizes in situ by image correlation spectroscopy
    • discussion 331-343 (1998)
    • Petersen, N. O. et al. Analysis of membrane protein cluster densities and sizes in situ by image correlation spectroscopy. Faraday Discuss. 289-305; discussion 331-343 (1998).
    • Faraday Discuss. , pp. 289-305
    • Petersen, N.O.1
  • 93
    • 0032110688 scopus 로고    scopus 로고
    • Cell biological applications of scanning near-field optical microscopy (SNOM)
    • Subramaniam, V., Kirsch, A. K. & Jovin. T. M. Cell biological applications of scanning near-field optical microscopy (SNOM). Cell. Mol. Biol. 44, 689-700 (1998).
    • (1998) Cell. Mol. Biol. , vol.44 , pp. 689-700
    • Subramaniam, V.1    Kirsch, A.K.2    Jovin, T.M.3
  • 94
    • 0034682512 scopus 로고    scopus 로고
    • Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission
    • Klar, T., Jakobs, S., Dyba, M., Egner, A. & Hell, S. Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission. Proc. Natl Acad. Sci. USA 97, 8206-8210 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8206-8210
    • Klar, T.1    Jakobs, S.2    Dyba, M.3    Egner, A.4    Hell, S.5
  • 95
    • 0032215689 scopus 로고    scopus 로고
    • 4Pi-confocal microscopy provides three-dimensional images of the microtubule network with 100- To 150-nm resolution
    • Nagorni, M. & Hell, S. W. 4Pi-confocal microscopy provides three-dimensional images of the microtubule network with 100-to 150-nm resolution. J. Struct. Biol. 123, 236-247 (1998).
    • (1998) J. Struct. Biol. , vol.123 , pp. 236-247
    • Nagorni, M.1    Hell, S.W.2
  • 96
    • 0030784698 scopus 로고    scopus 로고
    • Use of green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson, G. H., Knobel, S. M., Sharif, W. D., Kain, S. R. & Piston, D. W. Use of green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 73, 2782-2790 (1997).
    • (1997) Biophys. J. , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 97
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry. mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • Baird, G. S., Zacharias, D. A. & Tsien, R. Y. Biochemistry. mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl Acad. Sci. USA 97, 11984-11989 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 98
    • 0032489799 scopus 로고    scopus 로고
    • Pericentrin and γ-tubulin form a protein complex and are organized into a novel lattice at the centrosome
    • Dictenberg, J. B. et al. Pericentrin and γ-tubulin form a protein complex and are organized into a novel lattice at the centrosome. J. Cell Biol. 141, 163-174 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 163-174
    • Dictenberg, J.B.1
  • 99
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens, P. I., Majoul, I. V., Verveer, P. J., Soling, H. D. & Jovin, T. M. Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J. 15, 4246-4253 (1996).
    • (1996) EMBO J. , vol.15 , pp. 4246-4253
    • Bastiaens, P.I.1    Majoul, I.V.2    Verveer, P.J.3    Soling, H.D.4    Jovin, T.M.5
  • 100
    • 0028799667 scopus 로고
    • Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human tymphoblastoid cells
    • Damjanovich, S. et al. Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human tymphoblastoid cells. Proc. Natl Acad. Sci. USA 92, 1122-1126 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1122-1126
    • Damjanovich, S.1
  • 102
    • 0034019496 scopus 로고    scopus 로고
    • A fluorescent indicator for visualizing cAMP-induced phosphorylation in vivo
    • Nagai, Y. et al. A fluorescent indicator for visualizing cAMP-induced phosphorylation in vivo. Nature Biotechnol. 18, 313-316 (2000).
    • (2000) Nature Biotechnol. , vol.18 , pp. 313-316
    • Nagai, Y.1
  • 103
    • 0028925273 scopus 로고
    • Mapping of adherens junction components using microscopic resonance energy transfer imaging
    • Kam, Z., Volberg, T. & Geiger, B. Mapping of adherens junction components using microscopic resonance energy transfer imaging. J. Cell Sci. 108, 1051-1062 (1995). An elegant FRET microscopy study using immunofluorescence labelling to probe the distribution of proteins in adherens junctions.
    • (1995) J. Cell Sci. , vol.108 , pp. 1051-1062
    • Kam, Z.1    Volberg, T.2    Geiger, B.3
  • 104
    • 0035910511 scopus 로고    scopus 로고
    • Stable SNARE complex prior to evoked synaptic vesicle fusion revealed by fluorescence resonance energy transfer
    • Xia, Z., Zhou, Q., Lin, J. & Liu, Y. Stable SNARE complex prior to evoked synaptic vesicle fusion revealed by fluorescence resonance energy transfer. J. Biol. Chem. 276, 1766-1771 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 1766-1771
    • Xia, Z.1    Zhou, Q.2    Lin, J.3    Liu, Y.4
  • 105
    • 0032535138 scopus 로고    scopus 로고
    • FRET microscopy demonstrates molecular assocation of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes
    • Wouters, F. S., Bastiaens, P. I. H., Wirtz, K. W. A. & Jovin, T. M. FRET microscopy demonstrates molecular assocation of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes. EMBO J. 17, 7179-7189 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7179-7189
    • Wouters, F.S.1    Bastiaens, P.I.H.2    Wirtz, K.W.A.3    Jovin, T.M.4
  • 106
    • 0030566759 scopus 로고    scopus 로고
    • A photobleaching energy transfer analysis of CD8/MHC-I and LFA-1/ICAM-1 interactions in CTL-target cell conjugates
    • Bacsó, Z., Bene, L, Bodnár, A., Matkó, J. & Damjanovich, S. A photobleaching energy transfer analysis of CD8/MHC-I and LFA-1/ICAM-1 interactions in CTL-target cell conjugates. Immunol. Lett. 54, 151-156 (1996).
    • (1996) Immunol. Lett. , vol.54 , pp. 151-156
    • Bacsó, Z.1    Bene, L.2    Bodnár, A.3    Matkó, J.4    Damjanovich, S.5
  • 107
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella, T. W. Jr & Jovin, T. M. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 129, 1543-1558 (1995).
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella Jr., T.W.1    Jovin, T.M.2
  • 108
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako, Y., Minoghchi, S. & Yanagida, T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nature Cell Biol. 2, 168-172 (2000). Combines single-molecule fluorescence techniques, total internal reflection microscopy, and FRET to follow the dimerization of the EGFR upon EGF binding.
    • (2000) Nature Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 109
    • 0034724192 scopus 로고    scopus 로고
    • Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S. et al. Detection of β2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl Acad. Sci. USA 97, 3684-3689 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1
  • 110
    • 0037874731 scopus 로고    scopus 로고
    • Propeties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • Schütz, G. J., Kada, G., Pastushenko, V. P. & Schindler, H. Propeties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J. 19, 892-901 (2000).
    • (2000) EMBO J. , vol.19 , pp. 892-901
    • Schütz, G.J.1    Kada, G.2    Pastushenko, V.P.3    Schindler, H.4
  • 111
    • 0031865351 scopus 로고    scopus 로고
    • Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer
    • Mahajan, N. P. et al. Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer. Nature Biotechrol. 16, 547-552 (1998).
    • (1998) Nature Biotechrol. , vol.16 , pp. 547-552
    • Mahajan, N.P.1
  • 112
    • 0032704961 scopus 로고    scopus 로고
    • Cyclic AMP-dependent protein kinase binding to A-kinase anchoring proteins in living cells by fluorescence resonance energy transfer of green fluorescent protein fusion proteins
    • Ruehr, M. L., Zakhary, D. R., Damron, D. S. & Bond, M. Cyclic AMP-dependent protein kinase binding to A-kinase anchoring proteins in living cells by fluorescence resonance energy transfer of green fluorescent protein fusion proteins. J. Biol. Chem. 274, 33092-33096 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 33092-33096
    • Ruehr, M.L.1    Zakhary, D.R.2    Damron, D.S.3    Bond, M.4
  • 113
    • 0034650438 scopus 로고    scopus 로고
    • Ebola virus secretory glycoprotein (sGP) diminishes Fcγy RIIIB-to-CR3 proximity on neutrophils
    • Kindzelskii, A. L, Yang, Z., Nabel, G. J., Todd, R. F. R. & Petty, H. R. Ebola virus secretory glycoprotein (sGP) diminishes Fcγy RIIIB-to-CR3 proximity on neutrophils. J. Immunol. 164, 953-958 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 953-958
    • Kindzelskii, A.L.1    Yang, Z.2    Nabel, G.J.3    Todd, R.F.R.4    Petty, H.R.5
  • 114
    • 0033966543 scopus 로고    scopus 로고
    • Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex
    • Damelin, M. & Silver, P. A. Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Mol. Cell 5, 133-140 (2000). Novel interactions between nuclear transport factors and nucleoporins are revealed in a FRET-based protein-protein interaction screen in yeast.
    • (2000) Mol. Cell , vol.5 , pp. 133-140
    • Damelin, M.1    Silver, P.A.2
  • 115
    • 0032161918 scopus 로고    scopus 로고
    • Visualization of Pit-1 transcription factor interactions in the living cell nucleus by fluorescence resonance energy transfer microscopy
    • Day, R. N. Visualization of Pit-1 transcription factor interactions in the living cell nucleus by fluorescence resonance energy transfer microscopy. Mol. Endocrinol. 12, 1410-1419 (1998).
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1410-1419
    • Day, R.N.1
  • 116
    • 0034595687 scopus 로고    scopus 로고
    • Dynamics of NF-κB and IκBα studied with green fluorescent protein (GFP) fusion proteins. Investigation of GFP-p65 binding to DMA by fluorescence resonance energy transfer
    • Schmid, J. A. et al. Dynamics of NF-κB and IκBα studied with green fluorescent protein (GFP) fusion proteins. Investigation of GFP-p65 binding to DMA by fluorescence resonance energy transfer. J. Biol. Chem. 275, 17035-17042 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 17035-17042
    • Schmid, J.A.1
  • 117
    • 0034636104 scopus 로고    scopus 로고
    • Ugand-dependent interactions of coactivators steroid receptor coactivator-1 and peroxisome proliferator-activated receptor binding protein with nuclear hormone receptors can be imaged in live cells and are required for transcription
    • erratum 97, 9819 (2000)
    • Uopis, J. et al. Ugand-dependent interactions of coactivators steroid receptor coactivator-1 and peroxisome proliferator-activated receptor binding protein with nuclear hormone receptors can be imaged in live cells and are required for transcription. Proc. Natl Acad. Sci. USA 97, 4363-4368 (2000): erratum 97, 9819 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4363-4368
    • Uopis, J.1
  • 118
    • 0034731436 scopus 로고    scopus 로고
    • Dimerization with retinoid X receptors promotes nuclear localization and subnuclear targeting of vitamin D receptors
    • Prufer, K., Racz, A., Lin, G. C. & Barsony, J. Dimerization with retinoid X receptors promotes nuclear localization and subnuclear targeting of vitamin D receptors. J. Biol. Chem. 275, 41114-411123 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 41114-411123
    • Prufer, K.1    Racz, A.2    Lin, G.C.3    Barsony, J.4
  • 119
    • 0033621065 scopus 로고    scopus 로고
    • Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy
    • Brock, R., Vamosi, G., Vereb, G. & Jovin, T. M. Rapid characterization of green fluorescent protein fusion proteins on the molecular and cellular level by fluorescence correlation microscopy. Proc. Natl Acad. Sci. USA 96, 10123-10128 (1999). Provides a concise overview of how FCS and confocal microscopy can be linked to study the diffusional mobility of GFP-tagged proteins in cells.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10123-10128
    • Brock, R.1    Vamosi, G.2    Vereb, G.3    Jovin, T.M.4
  • 120
    • 0032111838 scopus 로고    scopus 로고
    • Fluorescence correlation microscopy (FCM)-fluorescence correlation spectroscopy (FCS) taken into the cell
    • Brock, R. & Jovin, T. M. Fluorescence correlation microscopy (FCM)-fluorescence correlation spectroscopy (FCS) taken into the cell. Cell Mol. Biol. 44, 847-856 (1998).
    • (1998) Cell Mol. Biol. , vol.44 , pp. 847-856
    • Brock, R.1    Jovin, T.M.2
  • 121
    • 0031785044 scopus 로고    scopus 로고
    • Fluorescence correlation microscopy of cells in the presence of autofluorescence
    • Brock, R., Hink, M. A. & Jovin, T. M. Fluorescence correlation microscopy of cells in the presence of autofluorescence. Biophys. J. 75, 2547-2557 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 2547-2557
    • Brock, R.1    Hink, M.A.2    Jovin, T.M.3
  • 122
    • 0034640133 scopus 로고    scopus 로고
    • Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy
    • Wachsmuth, M., Waldeck, W. & Langowski, J. Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy. J. Mol. Biol. 298, 677-689 (2000).
    • (2000) J. Mol. Biol. , vol.298 , pp. 677-689
    • Wachsmuth, M.1    Waldeck, W.2    Langowski, J.3
  • 123
    • 0033167917 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes
    • Schwille, P., Korlach, J. & Webb, W. W. Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes. Cytometry 36, 176-182 (1999).
    • (1999) Cytometry , vol.36 , pp. 176-182
    • Schwille, P.1    Korlach, J.2    Webb, W.W.3
  • 124
    • 0032568529 scopus 로고    scopus 로고
    • Intranuclear diffusion and hybridization state of oligonucleotides measured by fluorescence correlation spectroscopy in living cells
    • Politz, J. C., Browne, E. S., Wolf, D. E. & Pederson, T. Intranuclear diffusion and hybridization state of oligonucleotides measured by fluorescence correlation spectroscopy in living cells. Proc. Natl Acad. Sci. USA 95, 6043-6048 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 6043-6048
    • Politz, J.C.1    Browne, E.S.2    Wolf, D.E.3    Pederson, T.4
  • 125
    • 0034472564 scopus 로고    scopus 로고
    • Active protein transport through plastid tubles: Velocity quantified by fluorescence correlation spectroscopy
    • Köhler, R. H., Schwille, P., Webb, W. W. & Hanson, M. R. Active protein transport through plastid tubles: velocity quantified by fluorescence correlation spectroscopy. J. Cell Sci. 113, 3921-3930 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 3921-3930
    • Köhler, R.H.1    Schwille, P.2    Webb, W.W.3    Hanson, M.R.4
  • 126
    • 0034730328 scopus 로고    scopus 로고
    • Oligomeric tubulin in large transporting complex is transported via kinesin in squid giant axons
    • Terada, S., Kinjo, M. & Hirokawa, N. Oligomeric tubulin in large transporting complex is transported via kinesin in squid giant axons. Cell 103, 141-155 (2000).
    • (2000) Cell , vol.103 , pp. 141-155
    • Terada, S.1    Kinjo, M.2    Hirokawa, N.3
  • 127
    • 13044253479 scopus 로고    scopus 로고
    • Specific binding of proinsulin C-peptide to human cell membranes
    • Rigler, R. et al. Specific binding of proinsulin C-peptide to human cell membranes. Proc. Natl Acad. Sci. USA 96, 13318-13323 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13318-13323
    • Rigler, R.1
  • 128
    • 0032989995 scopus 로고    scopus 로고
    • Fusion of the binding domain of Raf-1 kinase with green fluorescent protein for activated Ras detection by fluorescence correlation spectroscopy
    • Trier, U., Olah, Z., Kleuser, B. & Schafer-Korting, M. Fusion of the binding domain of Raf-1 kinase with green fluorescent protein for activated Ras detection by fluorescence correlation spectroscopy. Pharmazie 54, 263-268 (1999).
    • (1999) Pharmazie , vol.54 , pp. 263-268
    • Trier, U.1    Olah, Z.2    Kleuser, B.3    Schafer-Korting, M.4
  • 129
    • 0029558909 scopus 로고
    • Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy
    • Terry, B. R., Matthews, E. K. & Haseloff, J. Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy. Biochem. Biophys. Res. Commun. 217, 21-27 (1995).
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 21-27
    • Terry, B.R.1    Matthews, E.K.2    Haseloff, J.3
  • 130
    • 0032506222 scopus 로고    scopus 로고
    • Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy
    • Haupts, U., Maiti, S., Schwille, P. & Webb, W. W. Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc. Natl Acad. Sci. USA 95, 13573-13578 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13573-13578
    • Haupts, U.1    Maiti, S.2    Schwille, P.3    Webb, W.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.