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Volumn 140, Issue 4, 1998, Pages 821-829

Rapid diffusion of green fluorescent protein in the mitochondrial matrix

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 0000037251     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.140.4.821     Document Type: Article
Times cited : (203)

References (49)
  • 1
    • 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
  • 2
    • 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
  • 5
    • 0025099503 scopus 로고
    • Mapping of fluorescence anisotropy in living cells by ratio imaging: Application to cytoplasmic viscosity
    • Dix, J.A., and A.S. Verkman. 1990. Mapping of fluorescence anisotropy in living cells by ratio imaging: application to cytoplasmic viscosity. Biophys. J. 57:231-240.
    • (1990) Biophys. J. , vol.57 , pp. 231-240
    • Dix, J.A.1    Verkman, A.S.2
  • 6
    • 0029844822 scopus 로고    scopus 로고
    • Evidence for electrostatic channeling in a fusion protein of malate dehydrogenase and citrate synthase
    • Elcock, A.H., and J.A. Macammon. 1996. Evidence for electrostatic channeling in a fusion protein of malate dehydrogenase and citrate synthase. Biochemistry. 35-12652-12658.
    • (1996) Biochemistry , vol.35 , pp. 12652-12658
    • Elcock, A.H.1    Macammon, J.A.2
  • 7
    • 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. 70:2767-2773.
    • (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
  • 8
    • 0025720835 scopus 로고
    • Self-diffusion and probe diffusion in dilute and semidilute aqueous solutions of dextran
    • Furakawa, R., J.L. Arauz-Lara, and B.R. Ware. 1991. Self-diffusion and probe diffusion in dilute and semidilute aqueous solutions of dextran. Macromolecules. 24:599-605.
    • (1991) Macromolecules , vol.24 , pp. 599-605
    • Furakawa, R.1    Arauz-Lara, J.L.2    Ware, B.R.3
  • 9
    • 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
  • 10
    • 0030600135 scopus 로고    scopus 로고
    • Green fluorescent protein applications in living cells
    • Gerdes, H.H., and C. Kaether, 1996. Green fluorescent protein applications in living cells. FEBS Lett. 389:44-47.
    • (1996) FEBS Lett. , vol.389 , pp. 44-47
    • Gerdes, H.H.1    Kaether, C.2
  • 12
    • 0014347959 scopus 로고
    • Chemical and physical fixation of isolated mitochondria in low energy and high energy states
    • Hackenbrock, C.R. 1968. Chemical and physical fixation of isolated mitochondria in low energy and high energy states. Proc. Natl. Acad. Sci. USA. 61:598-605.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.61 , pp. 598-605
    • Hackenbrock, C.R.1
  • 13
    • 0022790702 scopus 로고
    • The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport
    • Hackenbrock, C.R., B. Chazotte, and S.S. Gupte. 1986. The random collision model and a critical assessment of diffusion and collision in mitochondrial electron transport. J. Bioenerg. Biomembr. 18:331-368.
    • (1986) J. Bioenerg. Biomembr. , vol.18 , pp. 331-368
    • Hackenbrock, C.R.1    Chazotte, B.2    Gupte, S.S.3
  • 14
    • 0024539763 scopus 로고
    • The regulation of the matrix volume of mammalian mitochondria in vivo and in vitro and its role in the control of mitochondrial metabolism
    • Halestrap, A.P. 1989. The regulation of the matrix volume of mammalian mitochondria in vivo and in vitro and its role in the control of mitochondrial metabolism. Biochim. Biophys. Acta. 973:355-382.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 355-382
    • Halestrap, A.P.1
  • 15
    • 0027293090 scopus 로고
    • Macromolecular diffusion in crowded solutions
    • Han, J., and J. Herzfeld. 1993. Macromolecular diffusion in crowded solutions. Biophys. J. 65:1155-1243.
    • (1993) Biophys. J. , vol.65 , pp. 1155-1243
    • Han, J.1    Herzfeld, J.2
  • 16
    • 0027426259 scopus 로고
    • Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex
    • Kamijo, T., T. Aoyama, J. Miyazaki and T. Hashimoto. 1993. Molecular cloning of the cDNAs for the subunits of rat mitochondrial fatty acid β-oxidation multienzyme complex. J. Biol. Chem. 268:26452-26460.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26452-26460
    • Kamijo, T.1    Aoyama, T.2    Miyazaki, J.3    Hashimoto, T.4
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0028053707 scopus 로고
    • Metabolic studies on saccharomyces cervisiae containing fused citrate synthase malate dehydrogenase
    • Lindbladh, C., R.D. Brodeur, G. Lilius, and L. Bulow. 1994. Metabolic studies on saccharomyces cervisiae containing fused citrate synthase malate dehydrogenase. Biochemistry. 94:11684-11691.
    • (1994) Biochemistry , vol.94 , pp. 11684-11691
    • Lindbladh, C.1    Brodeur, R.D.2    Lilius, G.3    Bulow, L.4
  • 20
    • 0026783791 scopus 로고
    • Long tail kinetics in biophysics?
    • Nagle, J.F. 1992. Long tail kinetics in biophysics? Biophys. J. 63:366-370.
    • (1992) Biophys. J. , vol.63 , pp. 366-370
    • Nagle, J.F.1
  • 21
    • 0031968609 scopus 로고    scopus 로고
    • Monte-Carlo analysis of obstructed diffusion in 3 dimensions: Application to molecular diffusion in organelles
    • In press
    • Ölveczky, B.P., and A.S. Verkman. 1998. Monte-Carlo analysis of obstructed diffusion in 3 dimensions: application to molecular diffusion in organelles. Biophys. J. In press.
    • (1998) Biophys. J.
    • Ölveczky, B.P.1    Verkman, A.S.2
  • 22
  • 23
    • 0025895417 scopus 로고
    • Physiological significance of metabolic channeling
    • Ovadi, J. 1991. Physiological significance of metabolic channeling. J. Theor. Biol. 152:1-22.
    • (1991) J. Theor. Biol. , vol.152 , pp. 1-22
    • Ovadi, J.1
  • 25
    • 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
  • 26
    • 0000241205 scopus 로고
    • Dynamics of polymers in concentrated solutions: The universal scaling equation derived
    • Phillies, G.D.J. 1987. Dynamics of polymers in concentrated solutions: the universal scaling equation derived. Macromolecules. 20:558-564.
    • (1987) Macromolecules , vol.20 , pp. 558-564
    • Phillies, G.D.J.1
  • 27
    • 0024680212 scopus 로고
    • The hydrodynamic scaling method for polymer self-diffusion
    • Phillies, G.D.J. 1989. The hydrodynamic scaling method for polymer self-diffusion. J. Phys. Chem. 93:5029-5039.
    • (1989) J. Phys. Chem. , vol.93 , pp. 5029-5039
    • Phillies, G.D.J.1
  • 28
    • 0022233869 scopus 로고
    • Organizations of Krebs tricarboxylic acid cycle enzymes in mitochondria
    • Robinson, J.B., and P.A. Srere. 1985. Organizations of Krebs tricarboxylic acid cycle enzymes in mitochondria. J. Biol. Chem. 260:10800-10805.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10800-10805
    • Robinson, J.B.1    Srere, P.A.2
  • 30
    • 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
  • 31
    • 0027163092 scopus 로고
    • Lateral diffusion in an archielago. Dependence on tracer size
    • Saxton, M.J. 1993. Lateral diffusion in an archielago. Dependence on tracer size. Biophys. J. 64:1053-1062.
    • (1993) Biophys. J. , vol.64 , pp. 1053-1062
    • Saxton, M.J.1
  • 32
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • Saxton, M.J. 1994. Anomalous diffusion due to obstacles: a Monte Carlo study. Biophys. J. 66:394-401.
    • (1994) Biophys. J. , vol.66 , pp. 394-401
    • Saxton, M.J.1
  • 33
    • 0025883717 scopus 로고
    • Dynamics, structure, and function are coupled in the mitochondrial matrix
    • Scalettar, B.A., J.R. Abney, and C.R. Hackenbrock. 1991. Dynamics, structure, and function are coupled in the mitochondrial matrix. Proc. Natl. Acad. Sci. USA. 88:8057-8061.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8057-8061
    • Scalettar, B.A.1    Abney, J.R.2    Hackenbrock, C.R.3
  • 34
    • 84957866267 scopus 로고
    • Intracellular distribution of enzymes III. The oxidation of octanoic acid by rat liver fractions
    • Schneider, W.C. 1948. Intracellular distribution of enzymes III. The oxidation of octanoic acid by rat liver fractions. J. Biol. Chem. 176:259-266.
    • (1948) J. Biol. Chem. , vol.176 , pp. 259-266
    • Schneider, W.C.1
  • 35
    • 0028929733 scopus 로고
    • Direct measurement of trans-Golgi pH in living cells and regulation by second messengers
    • Seksek, O., J. Biwersi, and A.S. Verkman, 1995. Direct measurement of trans-Golgi pH in living cells and regulation by second messengers. J. Biol Chem. 270:4967-4970.
    • (1995) J. Biol Chem. , vol.270 , pp. 4967-4970
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 36
    • 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
  • 37
    • 0018074081 scopus 로고
    • The effect of viscosity on the apparent decomposition rate of enzyme-ligand complexes
    • Somogyi, B., F. Karasz, L. Tron, and P.R. Couchman. 1987. The effect of viscosity on the apparent decomposition rate of enzyme-ligand complexes. J. Theor. Biol. 74:209-216.
    • (1987) J. Theor. Biol. , vol.74 , pp. 209-216
    • Somogyi, B.1    Karasz, F.2    Tron, L.3    Couchman, P.R.4
  • 38
    • 0018854310 scopus 로고
    • The infrastructure of the mitochondrial matrix
    • Srere, P.A. 1980. The infrastructure of the mitochondrial matrix. Trends Biochem. Sci. 5:120-121.
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 120-121
    • Srere, P.A.1
  • 39
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P.A. 1987. Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56:89-124.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 40
    • 0025359442 scopus 로고
    • Enzyme-enzyme interactions and their metabolic role. A minireview
    • Srere, P.A., and J. Ovadi. 1990. Enzyme-enzyme interactions and their metabolic role. A minireview. FEBS Lett. 268:360-367.
    • (1990) FEBS Lett. , vol.268 , pp. 360-367
    • Srere, P.A.1    Ovadi, J.2
  • 41
    • 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
  • 42
    • 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
  • 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
  • 44
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • Von Hippel, P.H., and O.G. Berg. 1989. Facilitated target location in biological systems. J. Biol. Chem. 264:675-678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 45
    • 0024995218 scopus 로고
    • A "swell" way to regulate metabolism
    • Watford, M. 1990. A "swell" way to regulate metabolism. Trends Biochem. Sci. 15:329-330.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 329-330
    • Watford, M.1
  • 46
    • 0017411635 scopus 로고
    • On the role of organized multienzyme systems in cellular metabolism: A general synthesis
    • Welch, G.R. 1977. On the role of organized multienzyme systems in cellular metabolism: a general synthesis. Prog. Biophys. Mol. Biol. 32:103-191.
    • (1977) Prog. Biophys. Mol. Biol. , vol.32 , pp. 103-191
    • Welch, G.R.1
  • 47
    • 0028304634 scopus 로고
    • Metabolic channeling versus free diffusion: Transition-time analysis
    • Welch, G.R., and J.S. Easterby. 1994. Metabolic channeling versus free diffusion: transition-time analysis. Trends Biochem. Sci. 19:193-197.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 193-197
    • Welch, G.R.1    Easterby, J.S.2
  • 48
    • 0026436963 scopus 로고
    • Enzyme organization and the direction of metabolic flow: Physicochemical considerations
    • Westerhoff, H.V., and G.R. Welch. 1992. Enzyme organization and the direction of metabolic flow: physicochemical considerations. Curr. Top. Cell. Regul. 33:361-390.
    • (1992) Curr. Top. Cell. Regul. , vol.33 , pp. 361-390
    • Westerhoff, H.V.1    Welch, G.R.2
  • 49
    • 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 Jr., G.N.3


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