메뉴 건너뛰기




Volumn 102, Issue 7, 2012, Pages 1656-1665

Minimizing the impact of photoswitching of fluorescent proteins on FRAP analysis

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; HISTONE; TATA BINDING PROTEIN;

EID: 84859378171     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.02.029     Document Type: Article
Times cited : (51)

References (21)
  • 1
    • 23944459610 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching: Application to nuclear proteins
    • A.B. Houtsmuller Fluorescence recovery after photobleaching: application to nuclear proteins Adv. Biochem. Eng. Biotechnol. 95 2005 177 199
    • (2005) Adv. Biochem. Eng. Biotechnol. , vol.95 , pp. 177-199
    • Houtsmuller, A.B.1
  • 2
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • B.L. Sprague, and J.G. McNally FRAP analysis of binding: proper and fitting Trends Cell Biol. 15 2005 84 91
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 3
    • 77954815037 scopus 로고    scopus 로고
    • FRAP and kinetic modeling in the analysis of nuclear protein dynamics: What do we really know?
    • F. Mueller, and D. Mazza J.G. McNally FRAP and kinetic modeling in the analysis of nuclear protein dynamics: what do we really know? Curr. Opin. Cell Biol. 22 2010 403 411
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 403-411
    • Mueller, F.1    Mazza, D.2    McNally, J.G.3
  • 4
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • E.A.J. Reits, and J.J. Neefjes From fixed to FRAP: measuring protein mobility and activity in living cells Nat. Cell Biol. 3 2001 E145 E147
    • (2001) Nat. Cell Biol. , vol.3
    • Reits, E.A.J.1    Neefjes, J.J.2
  • 5
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • M.J. Dayel, E.F.Y. Hom, and A.S. Verkman Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum Biophys. J. 76 1999 2843 2851
    • (1999) Biophys. J. , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Hom, E.F.Y.2    Verkman, A.S.3
  • 6
    • 0030832226 scopus 로고    scopus 로고
    • On/off blinking and switching behaviour of single molecules of green fluorescent protein
    • R.M. Dickson, and A.B. Cubitt W.E. Moerner On/off blinking and switching behaviour of single molecules of green fluorescent protein Nature 388 1997 355 358
    • (1997) Nature , vol.388 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Moerner, W.E.3
  • 7
    • 34249844859 scopus 로고    scopus 로고
    • Structural basis for reversible photobleaching of a green fluorescent protein homologue
    • J.N. Henderson, and H.W. Ai S.J. Remington Structural basis for reversible photobleaching of a green fluorescent protein homologue Proc. Natl. Acad. Sci. USA 104 2007 6672 6677
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6672-6677
    • Henderson, J.N.1    Ai, H.W.2    Remington, S.J.3
  • 8
    • 68349142975 scopus 로고    scopus 로고
    • Using conventional fluorescent markers for far-field fluorescence localization nanoscopy allows resolution in the 10-nm range
    • P. Lemmer, and M. Gunkel C. Cremer Using conventional fluorescent markers for far-field fluorescence localization nanoscopy allows resolution in the 10-nm range J. Microsc. 235 2009 163 171
    • (2009) J. Microsc. , vol.235 , pp. 163-171
    • Lemmer, P.1    Gunkel, M.2    Cremer, C.3
  • 9
    • 18244362575 scopus 로고    scopus 로고
    • Reversible photobleaching of enhanced green fluorescent proteins
    • D. Sinnecker, and P. Voigt M. Schaefer Reversible photobleaching of enhanced green fluorescent proteins Biochemistry 44 2005 7085 7094
    • (2005) Biochemistry , vol.44 , pp. 7085-7094
    • Sinnecker, D.1    Voigt, P.2    Schaefer, M.3
  • 10
    • 0034691034 scopus 로고    scopus 로고
    • Real-time light-driven dynamics of the fluorescence emission in single green fluorescent protein molecules
    • M.F. Garcia-Parajo, and G.M.J. Segers-Nolten N.F. van Hulst Real-time light-driven dynamics of the fluorescence emission in single green fluorescent protein molecules Proc. Natl. Acad. Sci. USA 97 2000 7237 7242
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7237-7242
    • Garcia-Parajo, M.F.1    Segers-Nolten, G.M.J.2    Van Hulst, N.F.3
  • 11
    • 70349337796 scopus 로고    scopus 로고
    • The photochemistry of fluorescent proteins: Implications for their biological applications
    • H.E. Seward, and C.R. Bagshaw The photochemistry of fluorescent proteins: implications for their biological applications Chem. Soc. Rev. 38 2009 2842 2851
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2842-2851
    • Seward, H.E.1    Bagshaw, C.R.2
  • 12
    • 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
    • R.D. Phair, and P. Scaffidi T. Misteli Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins Mol. Cell. Biol. 24 2004 6393 6402
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Misteli, T.3
  • 13
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • B.L. Sprague, and R.L. Pego J.G. McNally Analysis of binding reactions by fluorescence recovery after photobleaching Biophys. J. 86 2004 3473 3495
    • (2004) Biophys. J. , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    McNally, J.G.3
  • 14
    • 43149119497 scopus 로고    scopus 로고
    • Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching
    • F. Mueller, P. Wach, and J.G. McNally Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching Biophys. J. 94 2008 3323 3339
    • (2008) Biophys. J. , vol.94 , pp. 3323-3339
    • Mueller, F.1    Wach, P.2    McNally, J.G.3
  • 15
    • 77955343194 scopus 로고    scopus 로고
    • Chromatin interaction of TATA-binding protein is dynamically regulated in human cells
    • P. de Graaf, and F. Mousson H.T. Timmers Chromatin interaction of TATA-binding protein is dynamically regulated in human cells J. Cell Sci. 123 2010 2663 2671
    • (2010) J. Cell Sci. , vol.123 , pp. 2663-2671
    • De Graaf, P.1    Mousson, F.2    Timmers, H.T.3
  • 16
    • 37549050539 scopus 로고    scopus 로고
    • Role of three-dimensional bleach distribution in confocal and two-photon fluorescence recovery after photobleaching experiments
    • D. Mazza, and F. Cella A. Diaspro Role of three-dimensional bleach distribution in confocal and two-photon fluorescence recovery after photobleaching experiments Appl. Opt. 46 2007 7401 7411
    • (2007) Appl. Opt. , vol.46 , pp. 7401-7411
    • Mazza, D.1    Cella, F.2    Diaspro, A.3
  • 17
    • 0033080794 scopus 로고    scopus 로고
    • Chromatin disruption and modification
    • A.P. Wolffe, and J.J. Hayes Chromatin disruption and modification Nucleic Acids Res. 27 1999 711 720
    • (1999) Nucleic Acids Res. , vol.27 , pp. 711-720
    • Wolffe, A.P.1    Hayes, J.J.2
  • 18
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • J.L. Workman, and R.E. Kingston Alteration of nucleosome structure as a mechanism of transcriptional regulation Annu. Rev. Biochem. 67 1998 545 579
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 19
    • 33645969033 scopus 로고    scopus 로고
    • Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins
    • J.L. Beaudouin, and F. Mora-Bermúdez J. Ellenberg Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins Biophys. J. 90 2006 1878 1894
    • (2006) Biophys. J. , vol.90 , pp. 1878-1894
    • Beaudouin, J.L.1    Mora-Bermúdez, F.2    Ellenberg, J.3
  • 20
    • 0036151490 scopus 로고    scopus 로고
    • TBP dynamics in living human cells: Constitutive association of TBP with mitotic chromosomes
    • D. Chen, and C.S. Hinkley S. Huang TBP dynamics in living human cells: constitutive association of TBP with mitotic chromosomes Mol. Biol. Cell 13 2002 276 284
    • (2002) Mol. Biol. Cell , vol.13 , pp. 276-284
    • Chen, D.1    Hinkley, C.S.2    Huang, S.3
  • 21
    • 78650861408 scopus 로고    scopus 로고
    • Live-cell dSTORM with SNAP-tag fusion proteins
    • T. Klein, and A. Löschberger M. Sauer Live-cell dSTORM with SNAP-tag fusion proteins Nat. Methods 8 2011 7 9
    • (2011) Nat. Methods , vol.8 , pp. 7-9
    • Klein, T.1    Löschberger, A.2    Sauer, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.