메뉴 건너뛰기




Volumn 97, Issue 5, 2009, Pages 1501-1511

A generalization of theory for two-dimensional fluorescence recovery after photobleaching applicable to confocal laser scanning microscopes

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL; GREEN FLUORESCENT PROTEIN;

EID: 70349589255     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.06.017     Document Type: Article
Times cited : (79)

References (27)
  • 1
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., D. Koppel, J. Schlessinger, E. Elson, and 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.2    Schlessinger, J.3    Elson, E.4    Webb, W.5
  • 3
    • 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
  • 4
    • 37249044282 scopus 로고    scopus 로고
    • Quantitative FRAP in analysis of molecular binding dynamics in vivo
    • McNally, J. G. 2008. Quantitative FRAP in analysis of molecular binding dynamics in vivo. Methods Cell Biol. 85:329-351.
    • (2008) Methods Cell Biol. , vol.85 , pp. 329-351
    • McNally, J.G.1
  • 6
    • 4444279082 scopus 로고    scopus 로고
    • Challenges and artifacts in quantitative photobleaching experiments
    • DOI 10.1111/j.1600-0854.2004.00215.x
    • Weiss, M. 2004. Challenges and artifacts in quantitative photobleaching experiments. Traffic. 5:662-671. (Pubitemid 39199130)
    • (2004) Traffic , vol.5 , Issue.9 , pp. 662-671
    • Weiss, M.1
  • 7
    • 4644243088 scopus 로고    scopus 로고
    • Intracellular macromolecular mobility measured by fluorescence recovery after photobleaching with confocal laser scanning microscopes
    • Braga, J., J. M. P. 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.P.2    Carmo-Fonseca, M.3
  • 8
    • 33645659240 scopus 로고    scopus 로고
    • Confocal fluorescence recovery after photobleaching of green fluorescent protein in solution
    • Pucadyil, T. J., and A. Chattopadhyay. 2006. Confocal fluorescence recovery after photobleaching of green fluorescent protein in solution. J. Fluoresc. 16:87-94.
    • (2006) J. Fluoresc. , vol.16 , pp. 87-94
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 9
    • 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
    • Mueller, F., P. Wach, and J. G. McNally. 2008. Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching. Biophys. J. 94:3323-3339.
    • (2008) Biophys. J. , vol.94 , pp. 3323-3339
    • Mueller, F.1    Wach, P.2    McNally, J.G.3
  • 10
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • Soumpasis, D. M. 1983. Theoretical analysis of fluorescence photobleaching recovery experiments. Biophys. J. 41:95-97.
    • (1983) Biophys. J. , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 12
    • 0027466791 scopus 로고
    • Fluorescence photobleaching recovery in the confocal scanning light microscope
    • Blonk, J., A. Don, H. V. Aalst, and J. J. Birmingham. 1993. Fluorescence photobleaching recovery in the confocal scanning light microscope. J. Microsc. 169:363-374. (Pubitemid 23119680)
    • (1993) Journal of Microscopy , vol.169 , Issue.3 , pp. 363-374
    • Blonk, J.C.G.1    Don, A.2    Van Aalst, H.3    Birmingham, J.J.4
  • 13
    • 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. D. Smedt, and J. Demeester. 2003. Three-dimensional fluorescence recovery after photobleaching with the confocal scanning laser microscope. Biophys. J. 85:2240-2252. (Pubitemid 37210775)
    • (2003) Biophysical Journal , vol.85 , Issue.4 , pp. 2240-2252
    • Braeckmans, K.1    Peeters, L.2    Sanders, N.N.3    De Smedt, S.C.4    Demeester, J.5
  • 14
    • 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
  • 15
    • 49249120958 scopus 로고    scopus 로고
    • Cellular dynamics of Ku: Characterization and purification of Ku-EGFP
    • Merkle, D., D. Zheng, T. Ohrt, K. Crell, and P. Schwille. 2008. Cellular dynamics of Ku: characterization and purification of Ku-EGFP. Chem. Bio. Chem. 9:1251-1259.
    • (2008) Chem. Bio. Chem. , vol.9 , pp. 1251-1259
    • Merkle, D.1    Zheng, D.2    Ohrt, T.3    Crell, K.4    Schwille, P.5
  • 16
    • 20444433204 scopus 로고    scopus 로고
    • Measuring protein-protein interactions inside living cells using single color fluorescence correlation spectroscopy. Application to human immunodeficiency virus type 1 integrase and LEDGF/p75
    • Maertens, G., J. Vercammen, Z. Debyser, and Y. Engelborghs. 2005. Measuring protein-protein interactions inside living cells using single color fluorescence correlation spectroscopy. Application to human immunodeficiency virus type 1 integrase and LEDGF/p75. FASEB J. 19:1039-1041.
    • (2005) FASEB J. , vol.19 , pp. 1039-1041
    • Maertens, G.1    Vercammen, J.2    Debyser, Z.3    Engelborghs, Y.4
  • 17
    • 22944460791 scopus 로고    scopus 로고
    • Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway
    • Goodwin, J. S., K. R. Drake, C. Rogers, L. Wright, J. Lippincott- Schwartz, et al. 2005. Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway. J. Cell Biol. 170:261-272.
    • (2005) J. Cell Biol. , vol.170 , pp. 261-272
    • Goodwin, J.S.1    Drake, K.R.2    Rogers, C.3    Wright, L.4    Lippincott-Schwartz, J.5
  • 18
    • 2442715340 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy investigation of a GFP mutantenhanced cyan fluorescent protein and its tubulin fusion in living cells with two-photon excitation
    • Wang, Z., J. V. Shah, Z. Chen, C.-H. Sun, and M. W. Berns. 2004. Fluorescence correlation spectroscopy investigation of a GFP mutantenhanced cyan fluorescent protein and its tubulin fusion in living cells with two-photon excitation. J. Biomed. Opt. 9:395-403.
    • (2004) J. Biomed. Opt. , vol.9 , pp. 395-403
    • Wang, Z.1    Shah, J.V.2    Chen, Z.3    Sun, C.-H.4    Berns, M.W.5
  • 19
    • 1642341110 scopus 로고    scopus 로고
    • Pleckstrin homology domain diffusion in Dictyostelium cytoplasm studied using fluorescence correlation spectroscopy
    • Ruchira, M., A. Hink, L. Bosgraaf, P. J. M. van Haastert, and A. J. W. G. Visser. 2004. Pleckstrin homology domain diffusion in Dictyostelium cytoplasm studied using fluorescence correlation spectroscopy. J. Biol. Chem. 279:10013-10019.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10013-10019
    • Ruchira, M.1    Hink, A.2    Bosgraaf, L.3    Van Haastert, P.J.M.4    Visser, A.J.W.G.5
  • 20
    • 0036220117 scopus 로고    scopus 로고
    • Molecular brightness characterization of EGFP in vivo by fluorescence fluctuation spectroscopy
    • Chen, Y., J. D. Müller, Q. Ruan, and E. Gratton. 2002. Molecular brightness characterization of EGFP in vivo by fluorescence fluctuation spectroscopy. Biophys. J. 82:133-144. (Pubitemid 34289788)
    • (2002) Biophysical Journal , vol.82 , Issue.1 , pp. 133-144
    • Chen, Y.1    Muller, J.D.2    Ruan, Q.3    Gratton, E.4
  • 21
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • Dayel, M. J., E. F. Hom, and A. S. Verkman. 1999. Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys. J. 76:2843-2851. (Pubitemid 29264645)
    • (1999) Biophysical Journal , vol.76 , Issue.5 , pp. 2843-2851
    • Dayel, M.J.1    Horn, E.F.Y.2    Verkman, A.S.3
  • 22
    • 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. (Pubitemid 27133128)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 24
    • 85024611673 scopus 로고
    • Viscosity of glycerol and its aqueous solutions
    • Segur, J. B., and H. E. Oberstar. 1951. Viscosity of glycerol and its aqueous solutions. Ind. Eng. Chem. 43:2117-2120.
    • (1951) Ind. Eng. Chem. , vol.43 , pp. 2117-2120
    • Segur, J.B.1    Oberstar, H.E.2
  • 25
    • 33748445547 scopus 로고    scopus 로고
    • EGFP-tagged core and linker histones diffuse via distinct mechanisms within living cells
    • DOI 10.1529/biophysj.105.079343
    • Bhattacharya, D., A. Mazumder, S. A. Miriam, and G. V. Shivashankar. 2006. EGFP-tagged core and linker histones diffuse via distinct mechanisms within living cells. Biophys. J. 91:2326-2336. (Pubitemid 44352415)
    • (2006) Biophysical Journal , vol.91 , Issue.6 , pp. 2326-2336
    • Bhattacharya, D.1    Mazumder, A.2    Miriam, S.A.3    Shivashankar, G.V.4
  • 26
    • 47749106407 scopus 로고    scopus 로고
    • A closed-form analytic expression for FRAP formula for the binding diffusion model
    • Kang, M., and A. K. Kenworthy. 2008. A closed-form analytic expression for FRAP formula for the binding diffusion model. Biophys. J. 95:L13-L15.
    • (2008) Biophys. J. , vol.95
    • Kang, M.1    Kenworthy, A.K.2
  • 27
    • 33645969033 scopus 로고    scopus 로고
    • Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins
    • Beaudouin, J., F. Mora-Bermúdez, 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-Bermúdez, F.2    Klee, T.3    Daigle, N.4    Ellenberg, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.