메뉴 건너뛰기




Volumn 84, Issue 2 I, 2003, Pages 1317-1327

Real-time imaging of nuclear permeation by EGFP in single intact cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; GREEN FLUORESCENT PROTEIN;

EID: 0037306231     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74947-9     Document Type: Article
Times cited : (86)

References (50)
  • 1
    • 0034126815 scopus 로고    scopus 로고
    • The nuclear pore complex: Mediator of translocation between nucleus and cytoplasm
    • Allen, T. D., J. M. Cronshaw, S. Bagley, E. Kiseleva, and M. W. Goldberg. 2000. The nuclear pore complex: mediator of translocation between nucleus and cytoplasm. J. Cell Sci. 113:1651-1659.
    • (2000) J. Cell Sci. , vol.113 , pp. 1651-1659
    • Allen, T.D.1    Cronshaw, J.M.2    Bagley, S.3    Kiseleva, E.4    Goldberg, M.W.5
  • 2
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., D. E. Koppel, J. Schlessinger, E. Elson, and W. W. Webb. 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
    • 0025269856 scopus 로고
    • Facilitated nuclear transport of histone HI and other small nucleophilic proteins
    • Breeuwer, M., and D. S. Goldfarb. 1990. Facilitated nuclear transport of histone HI and other small nucleophilic proteins. Cell. 60:999-1008.
    • (1990) Cell , vol.60 , pp. 999-1008
    • Breeuwer, M.1    Goldfarb, D.S.2
  • 4
    • 0034077209 scopus 로고    scopus 로고
    • Nuclear pore function viewed with atomic force microscopy
    • Danker, T., and H. Oberleithner. 2000. Nuclear pore function viewed with atomic force microscopy. Pflugers Arch. 439:671-681.
    • (2000) Pflugers Arch. , vol.439 , pp. 671-681
    • Danker, T.1    Oberleithner, H.2
  • 6
    • 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
  • 7
    • 0032792341 scopus 로고    scopus 로고
    • 2+ signaling through modulation of sphingolipid metabolism
    • 2+ signaling through modulation of sphingolipid metabolism. FASEB J. 13:1291-1301.
    • (1999) FASEB J. , vol.13 , pp. 1291-1301
    • Fatatis, A.1    Miller, R.J.2
  • 8
    • 0025371353 scopus 로고
    • The permeability of the nuclear envelope in dividing and nondividing cell cultures
    • Feldherr, C. M., and D. Akin. 1990. The permeability of the nuclear envelope in dividing and nondividing cell cultures. J. Cell Biol. 111:1-8.
    • (1990) J. Cell Biol. , vol.111 , pp. 1-8
    • Feldherr, C.M.1    Akin, D.2
  • 9
    • 0021717131 scopus 로고
    • Movement of a karyophilic protein through the nuclear pores of oocytes
    • Feldherr, C. M., E. Kallenbach, and N. Schultz. 1984. Movement of a karyophilic protein through the nuclear pores of oocytes. J. Cell Biol. 99:2216-2222.
    • (1984) J. Cell Biol. , vol.99 , pp. 2216-2222
    • Feldherr, C.M.1    Kallenbach, E.2    Schultz, N.3
  • 10
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes and binding is modulated by mitotic phosphorylation
    • Foisner, R., and L. Gerace. 1993. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes and binding is modulated by mitotic phosphorylation. Cell. 73:1267-1279.
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 11
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace, L., and B. Burke. 1988. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4:335-374.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 12
    • 0028851245 scopus 로고
    • Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus
    • Greber, U. F., and L. Gerace. 1995. Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus. J. Cell Biol. 128:5-14.
    • (1995) J. Cell Biol. , vol.128 , pp. 5-14
    • Greber, U.F.1    Gerace, L.2
  • 14
    • 0029557842 scopus 로고
    • Protein import into the nucleus: An integrated view
    • Hicks, G. R., and N. V. Raikhel. 1995. Protein import into the nucleus: an integrated view. Annu. Rev. Cell Dev. Biol. 11:155-188.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 155-188
    • Hicks, G.R.1    Raikhel, N.V.2
  • 15
    • 0032974756 scopus 로고    scopus 로고
    • Permeability of single nuclear pores
    • Keminer, O., and R. Peters. 1999. Permeability of single nuclear pores. Biophys. J. 77:217-228.
    • (1999) Biophys. J. , vol.77 , pp. 217-228
    • Keminer, O.1    Peters, R.2
  • 16
    • 0345517151 scopus 로고    scopus 로고
    • Nuclear protein transport pathways
    • Kohler, M., H. Haller, and E. Hartmann. 1999. Nuclear protein transport pathways. Exp. Nephrol. 7:290-294.
    • (1999) Exp. Nephrol. , vol.7 , pp. 290-294
    • Kohler, M.1    Haller, H.2    Hartmann, E.3
  • 18
    • 0029782625 scopus 로고    scopus 로고
    • Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia
    • Kuznetsov, G., K. T. Bush, P. L. Zhang, and S. K. Nigam. 1996. Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia. Proc. Natl. Acad. Sci. USA. 93:8584-8589.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8584-8589
    • Kuznetsov, G.1    Bush, K.T.2    Zhang, P.L.3    Nigam, S.K.4
  • 19
    • 0030857803 scopus 로고    scopus 로고
    • Stress, apoptosis, and mitosis induce phosphorylation of human keratin 8 at Ser-73 in tissues and cultured cells
    • Liao, J., N. O. Ku, and M. B. Omary. 1997. Stress, apoptosis, and mitosis induce phosphorylation of human keratin 8 at Ser-73 in tissues and cultured cells. J. Biol. Chem. 272:17565-17573.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17565-17573
    • Liao, J.1    Ku, N.O.2    Omary, M.B.3
  • 20
    • 0031989121 scopus 로고    scopus 로고
    • Graded ATP depletion can cause necrosis or apoptosis of cultured mouse proximal tubular cells
    • Lieberthal, W., S. A. Menza, and J. S. Levine. 1998. Graded ATP depletion can cause necrosis or apoptosis of cultured mouse proximal tubular cells. Am. J. Physiol. 274:F315-F327.
    • (1998) Am. J. Physiol. , vol.274
    • Lieberthal, W.1    Menza, S.A.2    Levine, J.S.3
  • 21
  • 22
    • 0034161430 scopus 로고    scopus 로고
    • Mechanisms of calcium decay kinetics in hippocampal spines: Role of spine calcium pumps and calcium diffusion through the spine neck in biochemical compartmentalization
    • Majewska, A., E. Brown, J. Ross, and R. Yuste. 2000. Mechanisms of calcium decay kinetics in hippocampal spines: role of spine calcium pumps and calcium diffusion through the spine neck in biochemical compartmentalization. J. Neurosci. 20:1722-1734.
    • (2000) J. Neurosci. , vol.20 , pp. 1722-1734
    • Majewska, A.1    Brown, E.2    Ross, J.3    Yuste, R.4
  • 24
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, 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
    • Ormo, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 25
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson, G. H., S. M. Knobel, W. D. Sharif, S. R. Kain, and D. W. Piston. 1997. Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 73:2782-2790.
    • (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
  • 28
    • 0033039738 scopus 로고    scopus 로고
    • Rho controls actin cytoskeletal assembly in renal epithelial cells during ATP depletion and recovery
    • Raman, N., and S. J. Atkinson. 1999. Rho controls actin cytoskeletal assembly in renal epithelial cells during ATP depletion and recovery. Am. J. Physiol. 276:C1312-C1324.
    • (1999) Am. J. Physiol. , vol.276
    • Raman, N.1    Atkinson, S.J.2
  • 29
    • 0020541188 scopus 로고
    • Ribonucleotide reductase - A radical enzyme
    • Reichard, P., and A. Ehrenberg. 1983. Ribonucleotide reductase - a radical enzyme. Science. 221:514-519.
    • (1983) Science , vol.221 , pp. 514-519
    • Reichard, P.1    Ehrenberg, A.2
  • 30
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck, K., and D. Gorlich. 2001. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20:1320-1330.
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 31
    • 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) J. Biol. Chem. , vol.272 , pp. 13270-13274
    • Romoser, V.A.1    Hinkle, P.M.2    Persechini, A.3
  • 32
    • 0004199763 scopus 로고
    • Cambridge University Press, Cambridge, UK
    • Rost, F. W. D. 1992. Fluorescence Microscopy. Cambridge University Press, Cambridge, UK.
    • (1992) Fluorescence Microscopy
    • Rost, F.W.D.1
  • 33
    • 0023221955 scopus 로고
    • Fluorescence redistribution after photobleaching as a tool for dissecting the control elements of nucleocytoplasmic transport
    • Schindler, M., and L. W. Jiang. 1987. Fluorescence redistribution after photobleaching as a tool for dissecting the control elements of nucleocytoplasmic transport. Methods Enzymol. 141:447-459.
    • (1987) Methods Enzymol. , vol.141 , pp. 447-459
    • Schindler, M.1    Jiang, L.W.2
  • 34
    • 0030742748 scopus 로고    scopus 로고
    • Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus
    • Seksek, O., J. Biwersi, and A. S. Verkman. 1997. Translational diffusion of macromolecule-sized 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
  • 37
    • 0033537992 scopus 로고    scopus 로고
    • Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy
    • Stoffler, D., K. N. Goldie, B. Feja, and U. Aebi. 1999. Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J. Mol. Biol. 287:741-752.
    • (1999) J. Mol. Biol. , vol.287 , pp. 741-752
    • Stoffler, D.1    Goldie, K.N.2    Feja, B.3    Aebi, U.4
  • 39
    • 0030023673 scopus 로고    scopus 로고
    • Direct measurement of coupling between dendritic spines and shafts
    • Svoboda, K., D. W. Tank, and W. Denk. 1996. Direct measurement of coupling between dendritic spines and shafts. Science. 272:716-719.
    • (1996) Science , vol.272 , pp. 716-719
    • Svoboda, K.1    Tank, D.W.2    Denk, W.3
  • 40
    • 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., C. P. Hoang, and A. S. Verkman. 1997. 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) Biophys. J. , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 41
    • 0023663113 scopus 로고
    • Nuclear reassembly excludes large macromolecules
    • Swanson, J. A., and P. L. McNeil. 1987. Nuclear reassembly excludes large macromolecules. Science. 238:548-550.
    • (1987) Science , vol.238 , pp. 548-550
    • Swanson, J.A.1    McNeil, P.L.2
  • 42
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. 1998. The green fluorescent protein. Annu. Rev. Biochem. 67:509-544.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 43
    • 0000568844 scopus 로고
    • Fluorophores for Confocal Microscopy
    • J. Pawley, editor. Plenum, New York
    • Tsien, R. Y., and A. Waggoner. 1995. Fluorophores for Confocal Microscopy. In Handbook of Biological Confocal Microscopy. J. Pawley, editor. Plenum, New York. 267-277.
    • (1995) Handbook of Biological Confocal Microscopy , pp. 267-277
    • Tsien, R.Y.1    Waggoner, A.2
  • 44
    • 0034640133 scopus 로고    scopus 로고
    • Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy
    • Wachsmuth, M., W. Waldeck, and J. Langowski. 2000. Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially-resolved fluorescence correlation spectroscopy. J. Mol. Biol. 298:677-689.
    • (2000) J. Mol. Biol. , vol.298 , pp. 677-689
    • Wachsmuth, M.1    Waldeck, W.2    Langowski, J.3
  • 45
    • 0033014673 scopus 로고    scopus 로고
    • Conformational changes of the in situ nuclear pore complex
    • Wang, H., and D. E. Clapham. 1999. Conformational changes of the in situ nuclear pore complex. Biophys. J. 77:241-247.
    • (1999) Biophys. J. , vol.77 , pp. 241-247
    • Wang, H.1    Clapham, D.E.2
  • 46
    • 0034717044 scopus 로고    scopus 로고
    • Gatekeepers of the nucleus
    • Wente, S. R. 2000. Gatekeepers of the nucleus. Science. 288:1374-1377.
    • (2000) Science , vol.288 , pp. 1374-1377
    • Wente, S.R.1
  • 47
    • 0033082623 scopus 로고    scopus 로고
    • Photobleaching GFP reveals protein dynamics inside live cells
    • White, J., and E. Stelzer. 1999. Photobleaching GFP reveals protein dynamics inside live cells. Trends Cell Biol. 9:61-65.
    • (1999) Trends Cell Biol. , vol.9 , pp. 61-65
    • White, J.1    Stelzer, E.2
  • 48
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., L. G. Moss, and G. N. Phillips, Jr. 1996. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14:1246-1251.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips G.N., Jr.3
  • 49
    • 0029742203 scopus 로고    scopus 로고
    • Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement
    • Yokoe, H., and T. Meyer. 1996. Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement. Nat. Biotechnol 14:1252-1256.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1252-1256
    • Yokoe, H.1    Meyer, T.2
  • 50
    • 0034717035 scopus 로고    scopus 로고
    • Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts
    • Zhang, C., and P. R. Clarke. 2000. Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts. Science. 288:1429-1432.
    • (2000) Science , vol.288 , pp. 1429-1432
    • Zhang, C.1    Clarke, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.