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Volumn 94, Issue 8, 2008, Pages 3323-3339

Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR;

EID: 43149119497     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.123182     Document Type: Article
Times cited : (141)

References (29)
  • 1
    • 23944459610 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching: Application to nuclear proteins
    • Houtsmuller, A. B. 2005. Fluorescence recovery after photobleaching: application to nuclear proteins. Adv. Biochem. Eng. Biotechnol. 95:177-199.
    • (2005) Adv. Biochem. Eng. Biotechnol , vol.95 , pp. 177-199
    • Houtsmuller, A.B.1
  • 2
    • 33645969033 scopus 로고    scopus 로고
    • Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins
    • Beaudouin, J., F. Mora-Bermudez, T. Klee, N. Daigle, and J. Ellenberg. 2006. Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins. Biophys. J. 90:1878-1894.
    • (2006) Biophys. J , vol.90 , pp. 1878-1894
    • Beaudouin, J.1    Mora-Bermudez, F.2    Klee, T.3    Daigle, N.4    Ellenberg, J.5
  • 3
    • 34147151617 scopus 로고    scopus 로고
    • A reaction-diffusion model to study RNA motion by quantitative fluorescence recovery after photobleaching
    • Braga, J., J. G. McNally, and M. Carmo-Fonseca. 2007. A reaction-diffusion model to study RNA motion by quantitative fluorescence recovery after photobleaching. Biophys. J. 92:2694-2703.
    • (2007) Biophys. J , vol.92 , pp. 2694-2703
    • Braga, J.1    McNally, J.G.2    Carmo-Fonseca, M.3
  • 4
    • 12244293410 scopus 로고    scopus 로고
    • Using FRAP and mathematical modeling to determine the in vivo kinetics of nuclear proteins
    • Carrero, G., D. McDonald, E. Crawford, G. de Vries, and M. J. Hendzel. 2003. Using FRAP and mathematical modeling to determine the in vivo kinetics of nuclear proteins. Methods. 29:14-28.
    • (2003) Methods , vol.29 , pp. 14-28
    • Carrero, G.1    McDonald, D.2    Crawford, E.3    de Vries, G.4    Hendzel, M.J.5
  • 5
    • 7444240826 scopus 로고    scopus 로고
    • Characterizing fluorescence recovery curves for nuclear proteins undergoing binding events
    • Carrero, G., E. Crawford, M. J. Hendzel, and G. de Vries. 2004. Characterizing fluorescence recovery curves for nuclear proteins undergoing binding events. Bull. Math. Biol. 66:1515-1545.
    • (2004) Bull. Math. Biol , vol.66 , pp. 1515-1545
    • Carrero, G.1    Crawford, E.2    Hendzel, M.J.3    de Vries, G.4
  • 7
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • Phair, R. D., P. Scaffidi, C. Elbi, J. Vecerova, A. Dey, K. Ozato, D. T. Brown, G. Hager, M. Bustin, and T. Misteli. 2004. Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins. Mol. Cell. Biol. 24:6393-6402.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerova, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 8
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • Sprague, B. L., R. L. Pego, D. A. Stavreva, and J. G. McNally. 2004. Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys. J. 86:3473-3495.
    • (2004) Biophys. J , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 9
    • 12144290835 scopus 로고    scopus 로고
    • Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes
    • Stavreva, D. A., W. G. Muller, G. L. Hager, C. L. Smith, and J. G. McNally. 2004. Rapid glucocorticoid receptor exchange at a promoter is coupled to transcription and regulated by chaperones and proteasomes. Mol. Cell. Biol. 24:2682-2697.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 2682-2697
    • Stavreva, D.A.1    Muller, W.G.2    Hager, G.L.3    Smith, C.L.4    McNally, J.G.5
  • 10
    • 10044250938 scopus 로고    scopus 로고
    • Dynamic interactions of a transcription factor with DNA are accelerated by a chromatin remodeller
    • 5:1064-1070
    • Karpova, T. S., T. Y. Chen, B. L. Sprague, and J. G. McNally. 2004. Dynamic interactions of a transcription factor with DNA are accelerated by a chromatin remodeller. EMBO Rep. 5:1064-1070.
    • (2004) EMBO Rep
    • Karpova, T.S.1    Chen, T.Y.2    Sprague, B.L.3    McNally, J.G.4
  • 11
    • 33746813983 scopus 로고    scopus 로고
    • How can biochemical reactions within cells differ from those in test tubes?
    • Minton, A. P. 2006. How can biochemical reactions within cells differ from those in test tubes? J. Cell Sci. 119:2863-2869.
    • (2006) J. Cell Sci , vol.119 , pp. 2863-2869
    • Minton, A.P.1
  • 12
    • 33646062855 scopus 로고    scopus 로고
    • An intact sequence-specific DNA-binding domain is required for human cytomegalovirus-mediated sequestration of p53 and may promote in vivo binding to the viral genome during infection
    • Rosenke, K., M. A. Samuel, E. T. McDowell, M. A. Toerne, and E. A. Fortunato. 2006. An intact sequence-specific DNA-binding domain is required for human cytomegalovirus-mediated sequestration of p53 and may promote in vivo binding to the viral genome during infection. Virology. 348:19-34.
    • (2006) Virology , vol.348 , pp. 19-34
    • Rosenke, K.1    Samuel, M.A.2    McDowell, E.T.3    Toerne, M.A.4    Fortunato, E.A.5
  • 14
    • 20044378479 scopus 로고    scopus 로고
    • A two-photon FRAP analysis of the cytoskeleton dynamics in the microvilli of intestinal cells
    • Waharte, F., C. M. Brown, S. Coscoy, E. Coudrier, and F. Amblard. 2005. A two-photon FRAP analysis of the cytoskeleton dynamics in the microvilli of intestinal cells. Biophys. J. 88:1467-1478.
    • (2005) Biophys. J , vol.88 , pp. 1467-1478
    • Waharte, F.1    Brown, C.M.2    Coscoy, S.3    Coudrier, E.4    Amblard, F.5
  • 15
    • 1642575954 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching (FRAP) methods for visualizing protein dynamics in living mammalian cell nuclei
    • Stavreva, D. A., and J. G. McNally. 2004. Fluorescence recovery after photobleaching (FRAP) methods for visualizing protein dynamics in living mammalian cell nuclei. Methods Enzymol. 375:443-455.
    • (2004) Methods Enzymol , vol.375 , pp. 443-455
    • Stavreva, D.A.1    McNally, J.G.2
  • 16
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • Sprague, B. L., and J. G. McNally. 2005. FRAP analysis of binding: proper and fitting. Trends Cell Biol. 15:84-91.
    • (2005) Trends Cell Biol , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 17
    • 33746805521 scopus 로고    scopus 로고
    • Analysis of binding at a single spatially localized cluster of binding sites by fluorescence recovery after photobleaching
    • Sprague, B. L., F. Muller, R. L. Pego, P. M. Bungay, D. A. Stavreva, and J. G. McNally. 2006. Analysis of binding at a single spatially localized cluster of binding sites by fluorescence recovery after photobleaching. Biophys. J. 91:1169-1191.
    • (2006) Biophys. J , vol.91 , pp. 1169-1191
    • Sprague, B.L.1    Muller, F.2    Pego, R.L.3    Bungay, P.M.4    Stavreva, D.A.5    McNally, J.G.6
  • 18
    • 4644243088 scopus 로고    scopus 로고
    • Intracellular macromolecular mobility measured by fluorescence recovery after photobleaching with confocal laser scanning microscopes
    • Braga, J., J. M. Desterro, and M. Carmo-Fonseca. 2004. Intracellular macromolecular mobility measured by fluorescence recovery after photobleaching with confocal laser scanning microscopes. Mol. Biol. Cell. 15:4749-4760.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4749-4760
    • Braga, J.1    Desterro, J.M.2    Carmo-Fonseca, M.3
  • 19
    • 0141530988 scopus 로고    scopus 로고
    • Three-dimensional fluorescence recovery after photobleaching with the confocal scanning laser microscope
    • Braeckmans, K., L. Peeters, N. N. Sanders, S. C. De Smedt, and J. Demeester. 2003. Three-dimensional fluorescence recovery after photobleaching with the confocal scanning laser microscope. Biophys. J. 85:2240-2252.
    • (2003) Biophys. J , vol.85 , pp. 2240-2252
    • Braeckmans, K.1    Peeters, L.2    Sanders, N.N.3    De Smedt, S.C.4    Demeester, J.5
  • 20
    • 33751316311 scopus 로고    scopus 로고
    • Anomalous photobleaching in fluorescence recovery after photobleaching measurements due to excitation saturation-a case study for fluorescein
    • Braeckmans, K., B. G. Stubbe, K. Remaut, J. Demeester, and S. C. De Smedt. 2006. Anomalous photobleaching in fluorescence recovery after photobleaching measurements due to excitation saturation-a case study for fluorescein. J. Biomed. Opt. 11:044013.
    • (2006) J. Biomed. Opt , vol.11 , pp. 044013
    • Braeckmans, K.1    Stubbe, B.G.2    Remaut, K.3    Demeester, J.4    De Smedt, S.C.5
  • 21
    • 37549050539 scopus 로고    scopus 로고
    • Role of three-dimensional bleach distribution in confocal and two-photon fluorescence recovery after photobleaching experiments
    • Mazza, D., F. Cella, G. Vicidomini, S. Krol, and A. Diaspro. 2007. Role of three-dimensional bleach distribution in confocal and two-photon fluorescence recovery after photobleaching experiments. Appl. Opt. 46:7401-7411.
    • (2007) Appl. Opt , vol.46 , pp. 7401-7411
    • Mazza, D.1    Cella, F.2    Vicidomini, G.3    Krol, S.4    Diaspro, A.5
  • 22
    • 34447263750 scopus 로고    scopus 로고
    • Probing the nanoscale viscoelasticity of intracellular fluids in living cells
    • Guigas, G., C. Kalla, and M. Weiss. 2007. Probing the nanoscale viscoelasticity of intracellular fluids in living cells. Biophys. J. 93:316-323.
    • (2007) Biophys. J , vol.93 , pp. 316-323
    • Guigas, G.1    Kalla, C.2    Weiss, M.3
  • 23
    • 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
  • 24
    • 33845437204 scopus 로고    scopus 로고
    • Intranuclear binding kinetics and mobility of single native U1 snRNP particles in living cells
    • Grünwald, D., B. Spottke, V. Buschmann, and U. Kubitscheck. 2006. Intranuclear binding kinetics and mobility of single native U1 snRNP particles in living cells. Mol. Biol. Cell. 17:5017-5027.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5017-5027
    • Grünwald, D.1    Spottke, B.2    Buschmann, V.3    Kubitscheck, U.4
  • 25
    • 15944375439 scopus 로고    scopus 로고
    • GR and HMGB1 interact only within chromatin and influence each other's residence time
    • Agresti, A., P. Scaffidi, A. Riva, V. R. Caiolfa, and M. E. Bianchi. 2005. GR and HMGB1 interact only within chromatin and influence each other's residence time. Mol. Cell. 18:109-121.
    • (2005) Mol. Cell , vol.18 , pp. 109-121
    • Agresti, A.1    Scaffidi, P.2    Riva, A.3    Caiolfa, V.R.4    Bianchi, M.E.5
  • 26
    • 0036656143 scopus 로고    scopus 로고
    • How to get from A to B: Strategies for analysing protein motion on DNA
    • Halford, S. E., and M. D. Szczelkun. 2002. How to get from A to B: strategies for analysing protein motion on DNA. Eur. Biophys. J. 31:257-267.
    • (2002) Eur. Biophys. J , vol.31 , pp. 257-267
    • Halford, S.E.1    Szczelkun, M.D.2
  • 27
    • 4444279082 scopus 로고    scopus 로고
    • Challenges and artifacts in quantitative photobleaching experiments
    • Weiss, M. 2004. Challenges and artifacts in quantitative photobleaching experiments. Traffic. 5:662-671.
    • (2004) Traffic , vol.5 , pp. 662-671
    • Weiss, M.1
  • 28
    • 18244362575 scopus 로고    scopus 로고
    • Reversible photobleaching of enhanced green fluorescent proteins
    • Sinnecker, D., P. Voigt, N. Hellwig, and M. Schaefer. 2005. Reversible photobleaching of enhanced green fluorescent proteins. Biochemistry. 44:7085-7094.
    • (2005) Biochemistry , vol.44 , pp. 7085-7094
    • Sinnecker, D.1    Voigt, P.2    Hellwig, N.3    Schaefer, M.4


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