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Volumn 4, Issue OCT, 2013, Pages

Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells

Author keywords

Fluorescence microscopy; Fluorescent protein; Forster resonance energy transfer; Quantitative imaging

Indexed keywords


EID: 84888610856     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2013.00413     Document Type: Review
Times cited : (99)

References (130)
  • 1
    • 0032115893 scopus 로고    scopus 로고
    • Response ofthe in vivo chlorophyll fluorescence spectrum to environmental factors and laser excitation wavelength
    • doi: 10.1088/09639659/7/4/016
    • Agati, G.(1998). Response ofthe in vivo chlorophyll fluorescence spectrum to environmental factors and laser excitation wavelength. Pure Appl. Opt. 7, 797-807. doi: 10.1088/09639659/7/4/016
    • (1998) Pure Appl. Opt , vol.7 , pp. 797-807
    • Agati, G.1
  • 2
    • 33845751079 scopus 로고    scopus 로고
    • Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: Structural characterization and applications in fluorescence imaging
    • doi: 10.1042/BJ20060874
    • Ai, H. W., Henderson, J. N., Remington, S. J., and Campbell, R. E. (2006). Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging. Biochem. J. 400, 531-540. doi: 10.1042/BJ20060874
    • (2006) Biochem. J , vol.400 , pp. 531-540
    • Ai, H.W.1    Henderson, J.N.2    Remington, S.J.3    Campbell, R.E.4
  • 3
    • 77952745940 scopus 로고    scopus 로고
    • Forster distances for fluorescent resonance energy transfer between mCherry and other visible fluorescent proteins
    • doi: 10.1016/j.ab.2010.03.026
    • Akrap, N., Seidel, T., and Barisas, G. (2010). Forster distances for fluorescent resonance energy transfer between mCherry and other visible fluorescent proteins. Anal. Biochem. 402, 105-106. doi: 10.1016/j.ab.2010.03.026
    • (2010) Anal. Biochem , vol.402 , pp. 105-106
    • Akrap, N.1    Seidel, T.2    Barisas, G.3
  • 4
    • 0033554379 scopus 로고    scopus 로고
    • The origin of lignin fluorescence
    • doi: 10.1016/S0022-2860(98)00913-2
    • Albinsson, B., Li, S. M., Lundquist, K., and Stomberg, R. (1999). The origin of lignin fluorescence. J. Mol. Struc. 508, 19-27. doi: 10.1016/S0022-2860(98)00913-2
    • (1999) J. Mol. Struc , vol.508 , pp. 19-27
    • Albinsson, B.1    Li, S.M.2    Lundquist, K.3    Stomberg, R.4
  • 5
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • doi: 10.1073/pnas. 97.22.11984
    • Baird, G. S., Zacharias, D. A., and Tsien, R. Y. (2000). Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. U.S.A. 97, 11984-11989. doi: 10.1073/pnas. 97.22.11984
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 6
    • 55549087588 scopus 로고    scopus 로고
    • Combination of novel green fluorescent protein mutant TSapphire and DsRed variant mOrange to set up a versatile in planta FRET-FLIM Assay
    • doi: 10.1104/pp.l08.117358
    • Bayle, V., Nussaume, L., and Bhat, R. A. (2008). Combination of novel green fluorescent protein mutant TSapphire and DsRed variant mOrange to set up a versatile in planta FRET-FLIM Assay. Plant Physiol. 148, 51-60. doi: 10.1104/pp.l08.117358
    • (2008) Plant Physiol , vol.148 , pp. 51-60
    • Bayle, V.1    Nussaume, L.2    Bhat, R.A.3
  • 7
    • 33745183370 scopus 로고    scopus 로고
    • A phos phatidylinositol-3-kinase-dependent signal transition regulates ARF1 and ARF6 during FCy receptor-mediatedphagocy tosis
    • doi: 10.1371/journal.pbio.0040162
    • Beemiller, P., Hoppe, A. D., and Swanson, J. A. (2006). A phos phatidylinositol-3-kinase-dependent signal transition regulates ARF1 and ARF6 during FCy receptor-mediatedphagocy tosis. PLoS Biol. 4:e162. doi: 10.1371/journal.pbio.0040162
    • (2006) PLoS Biol , vol.4
    • Beemiller, P.1    Hoppe, A.D.2    Swanson, J.A.3
  • 8
    • 59249105808 scopus 로고    scopus 로고
    • FRET and FLIM applications in plants
    • doi: 10.1016/ S0075-7535(08)00010-7
    • Bhat, R. A. (2009). FRET and FLIM applications in plants. Lab. Tech. Biochem. Mol. Biol. 33, 413-446. doi: 10.1016/ S0075-7535(08)00010-7
    • (2009) Lab. Tech. Biochem. Mol. Biol , vol.33 , pp. 413-446
    • Bhat, R.A.1
  • 9
    • 33748456465 scopus 로고    scopus 로고
    • The visible touch: In planta visualization of protein-proteininteractions by fluorophore-based methods
    • doi: 10.1186/1746-4811-2-12
    • Bhat, R. A., Lahaye, T., and Panstruga, R. (2006). The visible touch: in planta visualization of protein-proteininteractions by fluorophore-based methods. Plant Methods 2:12. doi: 10.1186/1746-4811-2-12
    • (2006) Plant Methods , vol.2 , pp. 12
    • Bhat, R.A.1    Lahaye, T.2    Panstruga, R.3
  • 10
    • 78650245901 scopus 로고    scopus 로고
    • Dark proteins disturb multichromophore coupling in tetratmeric fluorescent proteins
    • doi: 10.1002/jbio.201000075
    • Blum, C., Mexiner, A. J., and Subramaniam, V. (2011). Dark proteins disturb multichromophore coupling in tetratmeric fluorescent proteins. J. Biophotonics 4, 114-121. doi: 10.1002/jbio.201000075
    • (2011) J. Biophotonics , vol.4 , pp. 114-121
    • Blum, C.1    Mexiner, A.J.2    Subramaniam, V.3
  • 12
    • 79955419621 scopus 로고    scopus 로고
    • Dynamic imaging of glucose flux impedance using FRET-sensors in wild-type Arabidopsis plants
    • doi: 10.1093/jxb/erq444
    • Chaudhuri, B., Hormann, F., and Frommer, W. B. (2011). Dynamic imaging of glucose flux impedance using FRET-sensors in wild-type Arabidopsis plants. J. Exp. Bot. 62, 2411-2417. doi: 10.1093/jxb/erq444
    • (2011) J. Exp. Bot , vol.62 , pp. 2411-2417
    • Chaudhuri, B.1    Hormann, F.2    Frommer, W.B.3
  • 13
    • 34548272472 scopus 로고    scopus 로고
    • Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions
    • doi: 10.1111/j.1365-2818.2007.01838.x
    • Chen, Y. E., Mauldin, J. P., Day, R. N., and Periasamy, A. (2007). Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions. J. Microsc. 228, 139-152. doi: 10.1111/j.1365-2818.2007.01838.x
    • (2007) J. Microsc , vol.228 , pp. 139-152
    • Chen, Y.E.1    Mauldin, J.P.2    Day, R.N.3    Periasamy, A.4
  • 14
    • 33748459957 scopus 로고    scopus 로고
    • Measurement of FRET efficiency and ratio of donor to acceptor concentration in living cells
    • doi: 10.1529/bio-physj.106.088773
    • Chen, H., Puhl, H. L., Koushik, S. V., Vogel, S. S., and Ikeda, S. R. (2006). Measurement of FRET efficiency and ratio of donor to acceptor concentration in living cells. Biophys. J. 91, L39-L41. doi: 10.1529/bio-physj.106.088773
    • (2006) Biophys. J , vol.91
    • Chen, H.1    Puhl, H.L.2    Koushik, S.V.3    Vogel, S.S.4    Ikeda, S.R.5
  • 15
    • 0000056380 scopus 로고
    • Resonance energy transfer
    • ed J. R. Lakowicz (New York, NY: Plenum Press
    • Cheung, H. C. (1991). "Resonance energy transfer," in Topics in Fluorescence Spectroscopy, Vol. 2, ed J. R. Lakowicz (New York, NY: Plenum Press), 128-176
    • (1991) Topics In Fluorescence Spectroscopy , vol.2 , pp. 128-176
    • Cheung, H.C.1
  • 16
    • 68049137311 scopus 로고    scopus 로고
    • A novel far-red bimolecular fluorescence complementation system that allows for efficient visualization of protein interactions under physiological conditions
    • doi: 10.1016/j.bios.2009.06.008
    • Chu, J., Zhang, Z., Zheng, Y., Yang, J., Qin, L., Lu, J., et al. (2009). A novel far-red bimolecular fluorescence complementation system that allows for efficient visualization of protein interactions under physiological conditions. Biosens. Bioelectron. 25, 234-239. doi: 10.1016/j.bios.2009.06.008
    • (2009) Biosens. Bioelectron , vol.25 , pp. 234-239
    • Chu, J.1    Zhang, Z.2    Zheng, Y.3    Yang, J.4    Qin, L.5    Lu, J.6
  • 17
    • 13744261071 scopus 로고    scopus 로고
    • Dual-channel photobleaching FRET-microscopy for improved resolution of protein association states in living cells
    • doi: 10.1007/s00249-004-0427-y
    • Clayton, A. H., Klonis, N., Cody, S. H., and Nice, E. C. (2005). Dual-channel photobleaching FRET-microscopy for improved resolution of protein association states in living cells. Eur. Biophys. J. 34, 82-90. doi: 10.1007/s00249-004-0427-y
    • (2005) Eur. Biophys. J , vol.34 , pp. 82-90
    • Clayton, A.H.1    Klonis, N.2    Cody, S.H.3    Nice, E.C.4
  • 18
    • 59249101019 scopus 로고    scopus 로고
    • Forster resonance energy transfer-FRET what it is, why do it, and how it's done
    • doi:10.1016/ S0075-7535(08)00001-6
    • Clegg, R. M. (2009). Forster resonance energy transfer-FRET what it is, why do it, and how it's done. Lab. Tech. Biochem. Mol. Biol. 33, 1-58 doi:10.1016/ S0075-7535(08)00001-6
    • (2009) Lab. Tech. Biochem. Mol. Biol , vol.33 , pp. 1-58
    • Clegg, R.M.1
  • 19
    • 79960355585 scopus 로고    scopus 로고
    • Forster resonance energy transfer demonstrates a flavonoid metabolon in living plant cells that displays competitive interactions between enzymes
    • doi: 10.1016/j.febslet.2011.05.066
    • Crosby, K. C., Petraczewska-Bogiel, A, Gadella, T. W. J., and Winkel, S. (2011). Forster resonance energy transfer demonstrates a flavonoid metabolon in living plant cells that displays competitive interactions between enzymes. FEBS Lett. 585, 2193-2198. doi: 10.1016/j.febslet.2011.05.066
    • (2011) FEBS Lett , vol.585 , pp. 2193-2198
    • Crosby, K.C.1    Petraczewska-Bogiel, A.2    Gadella, T.W.J.3    Winkel, S.4
  • 20
    • 0028832822 scopus 로고
    • Understanding, improving and using green fluorescent proteins
    • doi: 10.1016/S0968-0004(00)89099-4
    • Cubitt, A. B., Heim, R., Adams, S. R., Boyd, A. E., Gross, L. A., and Tsien, R. Y. (1995). Understanding, improving and using green fluorescent proteins. Trends Biochem. Sci. 20, 448-455. doi: 10.1016/S0968-0004(00)89099-4
    • (1995) Trends Biochem. Sci , vol.20 , pp. 448-455
    • Cubitt, A.B.1    Heim, R.2    Adams, S.R.3    Boyd, A.E.4    Gross, L.A.5    Tsien, R.Y.6
  • 21
    • 9644279587 scopus 로고    scopus 로고
    • In vivo HIV-1 Rev multimerization in the nucleolus and cytoplasm identified byfluorescence resonance energy transfer
    • doi: 10.1074/jbc. M407713200
    • Daelemans, D., Costes, S. V., Cho, E. H., Erwin-Cohen, R. A., Locket, S., and Pavlakis, G. N. (2004). In vivo HIV-1 Rev multimerization in the nucleolus and cytoplasm identified byfluorescence resonance energy transfer. J. Biol. Chem. 279, 50167-50175. doi: 10.1074/jbc. M407713200
    • (2004) J. Biol. Chem , vol.279 , pp. 50167-50175
    • Daelemans, D.1    Costes, S.V.2    Cho, E.H.3    Erwin-Cohen, R.A.4    Locket, S.5    Pavlakis, G.N.6
  • 22
    • 46749088343 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer of GFP and YFP by spectral imaging and quantitative acceptor bleaching
    • doi: 10.1111/j.1365-2818.2008.02020.x
    • Dinant, C., van Royen, M. E., Vermeulen, W., and Houtsmuller, A. B. (2008). Fluorescence resonance energy transfer of GFP and YFP by spectral imaging and quantitative acceptor bleaching. J. Microsc. 231, 97-104. doi: 10.1111/j.1365-2818.2008.02020.x
    • (2008) J. Microsc , vol.231 , pp. 97-104
    • Dinant, C.1    van Royen, M.E.2    Vermeulen, W.3    Houtsmuller, A.B.4
  • 23
    • 0142134227 scopus 로고    scopus 로고
    • Cell damage and reactive oxygen species production induced by fluorescence microscopy: Effect on mitosis and guidelines for non-invasive fluorescence microscopy
    • doi: 10.1046/j.1365-313X.2003.01868.x
    • Dixit, R., and Cyr, R. (2003). Cell damage and reactive oxygen species production induced by fluorescence microscopy: effect on mitosis and guidelines for non-invasive fluorescence microscopy. Plant J. 36, 280-290. doi: 10.1046/j.1365-313X.2003.01868.x
    • (2003) Plant J , vol.36 , pp. 280-290
    • Dixit, R.1    Cyr, R.2
  • 24
    • 33846418732 scopus 로고    scopus 로고
    • Deconvolution of fluorescence spectra: Contribution to the structural analysis of complex molecules
    • doi: 10.1016/j.colsurfb.2006.10.015
    • Djikanovic, D., Kalauzi, A., Jeremic, M., Micic, M., and Radotic, K. (2007). Deconvolution of fluorescence spectra: contribution to the structural analysis of complex molecules. Colloids Surf. B Biointerfaces 54, 188-192. doi: 10.1016/j.colsurfb.2006.10.015
    • (2007) Colloids Surf. B Biointerfaces , vol.54 , pp. 188-192
    • Djikanovic, D.1    Kalauzi, A.2    Jeremic, M.3    Micic, M.4    Radotic, K.5
  • 25
    • 37149052489 scopus 로고    scopus 로고
    • Imaging FRET standards by steady-state fluorescence and lifetime methods
    • doi: 10.1002/jemt.20509
    • Domingo, B., Sabariegos, R., Picazo, F., and Llopis, J. (2007). Imaging FRET standards by steady-state fluorescence and lifetime methods. Microsc. Res. Tech. 70, 1010-1021. doi: 10.1002/jemt.20509
    • (2007) Microsc. Res. Tech , vol.70 , pp. 1010-1021
    • Domingo, B.1    Sabariegos, R.2    Picazo, F.3    Llopis, J.4
  • 26
    • 33751274789 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy (FLIM) to quantify protein-protein interactions inside cells
    • doi: 10.1042/BST0340679
    • Duncan, R. R. (2006). Fluorescence lifetime imaging microscopy (FLIM) to quantify protein-protein interactions inside cells. Biochem. Soc. Transactiv. 34, 679-682. doi: 10.1042/BST0340679
    • (2006) Biochem. Soc. Transactiv , vol.34 , pp. 679-682
    • Duncan, R.R.1
  • 27
    • 0010296062 scopus 로고
    • Ultrastructure of acri-dine alkaloid idioblasts in roots and cell cultures of Ruta graveolens
    • doi: 10.1139/b86-149
    • Eilert, U., Wolters, B., and Constabel, F. (1986). Ultrastructure of acri-dine alkaloid idioblasts in roots and cell cultures of Ruta graveolens. Can. J. Bot. 64, 1089-1096. doi: 10.1139/b86-149
    • (1986) Can. J. Bot , vol.64 , pp. 1089-1096
    • Eilert, U.1    Wolters, B.2    Constabel, F.3
  • 28
    • 0037564929 scopus 로고    scopus 로고
    • DsRed as a potential FRET partner with CFP and YFP
    • doi: 10.1016/S0006-3495(03)74504-4
    • Erickson, M. G., Moon, D. L., and Yue, D. T. (2003). DsRed as a potential FRET partner with CFP and YFP. Biophys. J. 85, 599-611. doi: 10.1016/S0006-3495(03)74504-4
    • (2003) Biophys. J , vol.85 , pp. 599-611
    • Erickson, M.G.1    Moon, D.L.2    Yue, D.T.3
  • 29
    • 38049115791 scopus 로고    scopus 로고
    • Split mCherry as a new red bimolecular fluorescence complementation system for visualising protein-protein interactions in living cells
    • doi: 10.1016/j.bbrc. 2007.12.101
    • Fan, J. Y., Cui, Z. Q., Wei, H. P., Zhang, Z. P., Zhou, Y. F., Wang, Y. P., et al. (2007). Split mCherry as a new red bimolecular fluorescence complementation system for visualising protein-protein interactions in living cells. Biochem. Biophys. Res. Commun. 367, 47-53. doi: 10.1016/j.bbrc. 2007.12.101
    • (2007) Biochem. Biophys. Res. Commun , vol.367 , pp. 47-53
    • Fan, J.Y.1    Cui, Z.Q.2    Wei, H.P.3    Zhang, Z.P.4    Zhou, Y.F.5    Wang, Y.P.6
  • 30
    • 34250965243 scopus 로고
    • Energiewanderung und Fluoreszenz
    • doi: 10.1007/BF00585226
    • Forster, T. (1946). Energiewanderung und Fluoreszenz. Naturwiss 33, 166-175. doi: 10.1007/BF00585226
    • (1946) Naturwiss , vol.33 , pp. 166-175
    • Forster, T.1
  • 31
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • doi: 10.1002/andp.19484370105
    • Forster, T. (1948). Intermolecular energy migration and fluorescence. Ann. Phys. 2, 55-75. doi: 10.1002/andp.19484370105
    • (1948) Ann. Phys , vol.2 , pp. 55-75
    • Forster, T.1
  • 32
    • 84868305301 scopus 로고    scopus 로고
    • The single T65S mutation generates brighter cyan fluorescent proteins with increased photostability and pH insensitivity
    • doi: 10.1371/jour-nal.pone.0049149
    • Fredj, A., Pasquier, H., Demachy, I., Jonasson, G., Levy, B., Derrien, V., et al. (2012). The single T65S mutation generates brighter cyan fluorescent proteins with increased photostability and pH insensitivity. PLoS ONE 7:e49149. doi: 10.1371/jour-nal.pone.0049149
    • (2012) PLoS ONE , vol.7
    • Fredj, A.1    Pasquier, H.2    Demachy, I.3    Jonasson, G.4    Levy, B.5    Derrien, V.6
  • 33
    • 0032986625 scopus 로고    scopus 로고
    • GFP-based FRET microscopy in living plant cells
    • doi: 10.1016/ S1360-1385(99)01426-0
    • Gadella, T. W. J., van der Krogt, G. N., Bisseling, T. (1999). GFP-based FRET microscopy in living plant cells. Trends Plant Sci. 4, 287-291. doi: 10.1016/ S1360-1385(99)01426-0
    • (1999) Trends Plant Sci , vol.4 , pp. 287-291
    • Gadella, T.W.J.1    van der Krogt, G.N.2    Bisseling, T.3
  • 34
    • 15744403602 scopus 로고    scopus 로고
    • Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells
    • doi: 10.1038/nmeth720
    • Galperin, E., Verkhusha, V. V., and Sorkin, A. (2004). Three-chromophore FRET microscopy to analyze multiprotein interactions in living cells. Nat. Methods 1, 209-217. doi: 10.1038/nmeth720
    • (2004) Nat. Methods , vol.1 , pp. 209-217
    • Galperin, E.1    Verkhusha, V.V.2    Sorkin, A.3
  • 35
    • 38049061740 scopus 로고    scopus 로고
    • Light resonance energy transfer-based methods in the study of G protein-coupled receptor oligomerization
    • doi: 10.1002/bies.20682
    • Gandia, J., Lluis, C., Ferre, S., Franco, R., and Ciruela, F. (2008). Light resonance energy transfer-based methods in the study of G protein-coupled receptor oligomerization. Bioessays 30, 82-89. doi: 10.1002/bies.20682
    • (2008) Bioessays , vol.30 , pp. 82-89
    • Gandia, J.1    Lluis, C.2    Ferre, S.3    Franco, R.4    Ciruela, F.5
  • 36
    • 27644490273 scopus 로고    scopus 로고
    • Betaxanthines as pigments responsible for visible fluorescence in flowers
    • doi: 10.1007/s00425-005-0004-3
    • Gandia-Herrero, F., Escribano, J., and Garcia-Carmona, F. (2005). Betaxanthines as pigments responsible for visible fluorescence in flowers. Planta 222, 586-593. doi: 10.1007/s00425-005-0004-3
    • (2005) Planta , vol.222 , pp. 586-593
    • Gandia-Herrero, F.1    Escribano, J.2    Garcia-Carmona, F.3
  • 37
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based resonance energy accepting chromoprotein (REACh) for Forster resonance energytransfer with GFP
    • doi: 10.1073/pnas.0509922103
    • Ganesan, S., Ameer-beg, S. M., Ng, T. T., Vojnovic, B., and Wouters, S. (2006). A dark yellow fluorescent protein (YFP)-based resonance energy accepting chromoprotein (REACh) for Forster resonance energytransfer with GFP. Proc. Natl. Acad. Sci. U.S.A. 103, 4089-4094. doi: 10.1073/pnas.0509922103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, S.5
  • 39
    • 4243491227 scopus 로고
    • Carotenoid fluorescence
    • doi: 10.1016/0009-2614(89)87342-7
    • Gillbro, T., and Cogdell, R. J. (1989). Carotenoid fluorescence. Chem. Phys. Lett. 158, 312-316. doi: 10.1016/0009-2614(89)87342-7
    • (1989) Chem. Phys. Lett , vol.158 , pp. 312-316
    • Gillbro, T.1    Cogdell, R.J.2
  • 40
    • 77449139582 scopus 로고    scopus 로고
    • Bright cyan fluorescent protein variants ideinti-fied by fluorescence lifetime screening
    • doi: 10.1038/nmeth.1415
    • Goedhart, J., van Weeren, L., Hink, M. A., Vischer, N. O., Jalink, K., and Gadella, T. W. J. (2010). Bright cyan fluorescent protein variants ideinti-fied by fluorescence lifetime screening. Nat. Methods 7, 137-139. doi: 10.1038/nmeth.1415
    • (2010) Nat. Methods , vol.7 , pp. 137-139
    • Goedhart, J.1    van Weeren, L.2    Hink, M.A.3    Vischer, N.O.4    Jalink, K.5    Gadella, T.W.J.6
  • 41
    • 41549153281 scopus 로고    scopus 로고
    • Sensitive detection of p65 homodimers using red-shifted and fluorescent protein-based FRET-couples
    • doi: 10.1371/journal.pone.0001011
    • Goedhart, J., Vermeer, J. E. M., Adjobo-Hermans, M. J. W., van Weeren, L., and Gadella, T. W. J. (2010). Sensitive detection of p65 homodimers using red-shifted and fluorescent protein-based FRET-couples. PLoS ONE 10:e1011. doi: 10.1371/journal.pone.0001011
    • (2010) PLoS ONE , vol.10
    • Goedhart, J.1    Vermeer, J.E.M.2    Adjobo-Hermans, M.J.W.3    van Weeren, L.4    Gadella, T.W.J.5
  • 42
    • 84859173050 scopus 로고    scopus 로고
    • Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%
    • doi: 10.1038/ncomms1738
    • Goedhart, J., von Stetten, D., Noirclerc-Savoye, M., Lelimousin, M., Joosen, L., Hink, M. A., et al. (2012). Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%. Nat. Commun. 3,751. doi: 10.1038/ncomms1738
    • (2012) Nat. Commun , vol.3 , pp. 751
    • Goedhart, J.1    von Stetten, D.2    Noirclerc-Savoye, M.3    Lelimousin, M.4    Joosen, L.5    Hink, M.A.6
  • 43
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energytransfer measurements using fluorescence microscopy
    • doi: 10.1016/S0006-3495(98)77976-7
    • Gordon, G. W., Berry, G., Liang, X. H., Levine, B., and Herman, B. (1998). Quantitative fluorescence resonance energytransfer measurements using fluorescence microscopy. Biophys. J. 74, 2702-2713. doi: 10.1016/S0006-3495(98)77976-7
    • (1998) Biophys. J , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 44
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and application
    • doi: 10.1074/jbc.M102815200
    • Griesbeck, O., Baird, G. S., Campbell, R. E., Zacharias, D. A., and Tsien, R. Y. (2001). Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and application. J. Bio. Chem. 276, 29188-29194. doi: 10.1074/jbc.M102815200
    • (2001) J. Bio. Chem , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 45
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modeling
    • doi: 10.1002/elps.1150181505
    • Guex, N., and Peitsch, M. C. (1997). SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723. doi: 10.1002/elps.1150181505
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 46
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly
    • doi: 10.1073/pnas.94.6.2122
    • Haseloff, J., Siemering, K. R., Prasher, D. C., and Hodge, S. (1997). Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc. Natl. Acad. Sci. U.S.A. 94, 2122-2127. doi: 10.1073/pnas.94.6.2122
    • (1997) Proc. Natl. Acad. Sci. U.S.A , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodge, S.4
  • 47
    • 0041810129 scopus 로고    scopus 로고
    • Triple FRET: A tool for studying long-range molecular interactions
    • doi: 10.1002/cphc.200200634
    • Haustein, E., Jahnz, M., Schwille, P. (2003). Triple FRET: A tool for studying long-range molecular interactions. Chem. Phys. Chem. 4, 745-748. doi: 10.1002/cphc.200200634
    • (2003) Chem. Phys. Chem , vol.4 , pp. 745-748
    • Haustein, E.1    Jahnz, M.2    Schwille, P.3
  • 48
    • 11244334124 scopus 로고    scopus 로고
    • TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-(kappa)B activation
    • doi: 10.1074/jbc.M407284200
    • He, L., Grammer, A. C., Wu, X., and Lipsky, P. E. (2004). TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-(kappa)B activation. J. Biol. Chem. 279, 55855-55865. doi: 10.1074/jbc.M407284200
    • (2004) J. Biol. Chem , vol.279 , pp. 55855-55865
    • He, L.1    Grammer, A.C.2    Wu, X.3    Lipsky, P.E.4
  • 49
    • 28644442719 scopus 로고    scopus 로고
    • Determination of tumor necrosis factor receptor-associated factor trimerization in living cells by CFP->YFP->mRFP FRET detected by flow cytometry
    • doi: 10.1093/nar/gni057
    • He, L., Wu, X., Simone, J., Hewgill, D., and Lipsky, P. E. (2005). Determination of tumor necrosis factor receptor-associated factor trimerization in living cells by CFP->YFP->mRFP FRET detected by flow cytometry. Nucleic Acid Res. 33, e61. doi: 10.1093/nar/gni057
    • (2005) Nucleic Acid Res , vol.e61 , pp. 33
    • He, L.1    Wu, X.2    Simone, J.3    Hewgill, D.4    Lipsky, P.E.5
  • 50
    • 0034710922 scopus 로고    scopus 로고
    • Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: Coral red (dsRed) and yellow (Citrine)
    • doi: 10.1073/pnas. 97.22.11996
    • Heikal, A. A., Hess, S. T., Baird, G.S., Tsien, R. Y., and Webb, W. W. (2000). Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: coral red (dsRed) and yellow (Citrine). Proc. Natl. Acad. Sci. U.S.A. 97, 11996-12001. doi: 10.1073/pnas. 97.22.11996
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 11996-12001
    • Heikal, A.A.1    Hess, S.T.2    Baird, G.S.3    Tsien, R.Y.4    Webb, W.W.5
  • 51
    • 84874627951 scopus 로고    scopus 로고
    • Signal transfer in the plant plasma membrane: Phospholipase A2 is regulated via an inhibitory Ga protein and a cyclophylin
    • doi: 10.1042/BJ20120793
    • Heinze, M., Herre, M., Massalski, C, Hermann, I., Conrad, U., and Roos, W. (2013). Signal transfer in the plant plasma membrane: phospholipase A2 is regulated via an inhibitory Ga protein and a cyclophylin. Biochem. J. 450, 497-509. doi: 10.1042/BJ20120793
    • (2013) Biochem. J , vol.450 , pp. 497-509
    • Heinze, M.1    Herre, M.2    Massalski, C.3    Hermann, I.4    Conrad, U.5    Roos, W.6
  • 52
    • 0036909519 scopus 로고    scopus 로고
    • Imaging proteinprotein interactions in living plant cells
    • doi: 10.1023/A:1021282619035
    • Hink, M. A., Bisseling, T., and Visser, A. J. (2002). Imaging proteinprotein interactions in living plant cells. Plant Mol. Biol. 50, 871-883. doi: 10.1023/A:1021282619035
    • (2002) Plant Mol. Biol , vol.50 , pp. 871-883
    • Hink, M.A.1    Bisseling, T.2    Visser, A.J.3
  • 53
    • 0036924067 scopus 로고    scopus 로고
    • Fluorescence Resonance Energy Transferbased stoichiometry in living cells
    • doi: 10.1016/S0006-3495(02)75365-4
    • Hoppe, A. D., Christensen, K., and Swanson, J. A. (2002). Fluorescence Resonance Energy Transferbased stoichiometry in living cells. Biophys. J. 83, 3652-3664. doi: 10.1016/S0006-3495(02)75365-4
    • (2002) Biophys. J , vol.83 , pp. 3652-3664
    • Hoppe, A.D.1    Christensen, K.2    Swanson, J.A.3
  • 55
    • 33746435428 scopus 로고    scopus 로고
    • An improved mRFP1 adds red to bimolecular fluorescence complementation
    • doi: 10.1038/nmeth901
    • Jach, G., Pesch, M., Richter, K., Frins, S., Uhrig, J. F. (2006). An improved mRFP1 adds red to bimolecular fluorescence complementation. Nat. Methods 3, 597-600. doi: 10.1038/nmeth901
    • (2006) Nat. Methods , vol.3 , pp. 597-600
    • Jach, G.1    Pesch, M.2    Richter, K.3    Frins, S.4    Uhrig, J.F.5
  • 56
    • 59249109205 scopus 로고    scopus 로고
    • Filter FRET: Quantitative imaging of sensitized emission
    • ed T. W. J. Gadella (Oxford: Elsevier
    • Jalink, K., and van Rheenen, J. (2009). "Filter FRET: quantitative imaging of sensitized emission, in Laboratory Techniques in Biochemistry and Molecular Biology, Vol. 33, ed T. W. J. Gadella (Oxford: Elsevier), 289-350
    • (2009) Laboratory Techniques In Biochemistry and Molecular Biology , vol.33 , pp. 289-350
    • Jalink, K.1    van Rheenen, J.2
  • 57
    • 0242385405 scopus 로고    scopus 로고
    • FRET imaging
    • doi: 10.1038/nbt896
    • Jares-Erijman, E. A., and Jovin, T. M. (2003). FRET imaging. Nat. Biotechnol. 21, 1387-1395. doi: 10.1038/nbt896
    • (2003) Nat. Biotechnol , vol.21 , pp. 1387-1395
    • Jares-Erijman, E.A.1    Jovin, T.M.2
  • 58
    • 0037238461 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photo-bleaching using confocal microscopy and a single laser
    • doi: 10.1046/j.1365-2818.2003. 01100.x
    • Karpova, T. S., Baumann, C. T., He, L., Wu, X., Grammer, A., Lipsky, P., et al. (2003). Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photo-bleaching using confocal microscopy and a single laser. J. Microsc. 209, 56-70. doi: 10.1046/j.1365-2818.2003. 01100.x
    • (2003) J. Microsc , vol.209 , pp. 56-70
    • Karpova, T.S.1    Baumann, C.T.2    He, L.3    Wu, X.4    Grammer, A.5    Lipsky, P.6
  • 59
    • 84885098884 scopus 로고    scopus 로고
    • The membrane-tethered transcription factor ANAC089 serves as redoxdependent suppressor of stromal ascorbate peroxidase gene expression
    • doi: 10.3389/fpls.2012.00247
    • Klein, P., Seidel, T., Stocker, B., Dietz, K. J. (2012). The membrane-tethered transcription factor ANAC089 serves as redoxdependent suppressor of stromal ascorbate peroxidase gene expression. Front. Plant Sci. 3:247. doi: 10.3389/fpls.2012.00247
    • (2012) Front. Plant Sci , vol.3 , pp. 247
    • Klein, P.1    Seidel, T.2    Stocker, B.3    Dietz, K.J.4
  • 61
    • 10144263345 scopus 로고    scopus 로고
    • Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex
    • doi: 10.1186/1471-2121-5-29
    • Kluge, C., Seidel, T., Bolte, S., Sharma, S. S., Hanitzsch, M., Satiat-Jeunemaitre, B., et al. (2004). Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex. BMC Cell Biol. 5:29. doi: 10.1186/1471-2121-5-29
    • (2004) BMC Cell Biol , vol.5 , pp. 29
    • Kluge, C.1    Seidel, T.2    Bolte, S.3    Sharma, S.S.4    Hanitzsch, M.5    Satiat-Jeunemaitre, B.6
  • 62
    • 71049156731 scopus 로고    scopus 로고
    • Anomalous surplus energy transfer observed with multiple FRET-acceptors
    • doi: 10.1371/jour-nal.pone.0008031
    • Koushik, S. V., Blank, P. S., and Vogel, S. S. (2009). Anomalous surplus energy transfer observed with multiple FRET-acceptors. PLoS ONE 4:e8031. doi: 10.1371/jour-nal.pone.0008031
    • (2009) PLoS ONE , vol.4
    • Koushik, S.V.1    Blank, P.S.2    Vogel, S.S.3
  • 63
    • 33845443776 scopus 로고    scopus 로고
    • Cerulean, Venus and VenusY67C FRET reference standards
    • doi: 10.1529/bio-physj.106.096206
    • Koushik, S. V., Chen, H., Thaler, C., Puhl, H. L., and Vogel, S. S. (2006). Cerulean, Venus and VenusY67C FRET reference standards. Biophys. J. 91, L99-L101. doi: 10.1529/bio-physj.106.096206
    • (2006) Biophys. J , vol.91
    • Koushik, S.V.1    Chen, H.2    Thaler, C.3    Puhl, H.L.4    Vogel, S.S.5
  • 65
    • 59249103725 scopus 로고    scopus 로고
    • Visible fluorescent proteins for FRET
    • doi: 10.1016/S0075-7535(08)00005-3
    • Kremers, G. J., and Goedhart, J. (2009). Visible fluorescent proteins for FRET. Lab. Tech. Biochem. Mol. Biol. 33, 171-224. doi: 10.1016/S0075-7535(08)00005-3
    • (2009) Lab. Tech. Biochem. Mol. Biol , vol.33 , pp. 171-224
    • Kremers, G.J.1    Goedhart, J.2
  • 66
    • 33744779420 scopus 로고    scopus 로고
    • Cyan and yellow fluorescent proteins with improved brightness, protein folding, and FRET Forster radius
    • doi: 10.1021/ bi0516273
    • Kremers, G. J., Goedhart, J., van Munster, E. B., and Gadella, T. W. J. (2006). Cyan and yellow fluorescent proteins with improved brightness, protein folding, and FRET Forster radius. Biochem. 45, 6570-6580. doi: 10.1021/ bi0516273
    • (2006) Biochem , vol.45 , pp. 6570-6580
    • Kremers, G.J.1    Goedhart, J.2    van Munster, E.B.3    Gadella, T.W.J.4
  • 67
    • 77949520163 scopus 로고    scopus 로고
    • Combined bimolecular fluorescence complementation and Forster resonance energy transfer reveals ternary SNARE complex formation in living plant cells
    • doi: 10.1104/pp. 109.151142
    • Kwaaitaal, M., Keinath, N. F., Pajonk, S., Biskup, C., and Panstruga, R. (2010). Combined bimolecular fluorescence complementation and Forster resonance energy transfer reveals ternary SNARE complex formation in living plant cells. Plant Physiol. 152, 1135-1147. doi: 10.1104/pp. 109.151142
    • (2010) Plant Physiol , vol.152 , pp. 1135-1147
    • Kwaaitaal, M.1    Keinath, N.F.2    Pajonk, S.3    Biskup, C.4    Panstruga, R.5
  • 68
  • 69
    • 84867084476 scopus 로고    scopus 로고
    • Improving FRET dynamic range with bright green and red fluorescent protein
    • doi: 10.1038/nmeth.2171
    • Lam, A., St-Pierre, F., Gong, Y., Marshall, J. D., Cranfill, P. J., Baird, M. A., et al. (2012). Improving FRET dynamic range with bright green and red fluorescent protein. Nat. Methods 9, 1005-1012. doi: 10.1038/nmeth.2171
    • (2012) Nat. Methods , vol.9 , pp. 1005-1012
    • Lam, A.1    St-Pierre, F.2    Gong, Y.3    Marshall, J.D.4    Cranfill, P.J.5    Baird, M.A.6
  • 70
    • 0142184429 scopus 로고    scopus 로고
    • Imaging molecular interactions in cells bydynamic and static fluorescence anisotropy (rFLIM and emFRET)
    • doi: 10.1042/BST0311020
    • Lidke, D. S., Nagy, P., Barisas, B. G., Heintzmann, R., Post, J. N., Lidke, K. A., et al. (2003). Imaging molecular interactions in cells bydynamic and static fluorescence anisotropy (rFLIM and emFRET). Biochem. Soc. Trans. 31, 1020-1027. doi: 10.1042/BST0311020
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 1020-1027
    • Lidke, D.S.1    Nagy, P.2    Barisas, B.G.3    Heintzmann, R.4    Post, J.N.5    Lidke, K.A.6
  • 71
    • 79954511828 scopus 로고    scopus 로고
    • Some secrets of fluorescent proteins: Distinct bleaching in various mounting fluids and photoactivation of cyan fluorescent proteins at yfp-excitation
    • doi: 10.1371/journal.pone.0018586
    • Malkani, N., and Schmid, J. A. (2011). Some secrets of fluorescent proteins: distinct bleaching in various mounting fluids and photoactivation of cyan fluorescent proteins at yfp-excitation. PLoS ONE 6:e18586. doi: 10.1371/journal.pone.0018586
    • (2011) PLoS ONE , vol.6
    • Malkani, N.1    Schmid, J.A.2
  • 72
    • 79953186589 scopus 로고    scopus 로고
    • An improved cerulean fluorescent protein with enhanced brightness and reduced reversible photoswitching
    • doi: 10.1371/journal.pone.0017896
    • Markwardt, M. L., Kremers, G. J., Kraft, C. A., Ray, K., Cranfill, P. J., Wilson, K. A., et al. (2011). An improved cerulean fluorescent protein with enhanced brightness and reduced reversible photoswitching. PLoS ONE 6:e17896. doi: 10.1371/journal.pone.0017896
    • (2011) PLoS ONE , vol.6
    • Markwardt, M.L.1    Kremers, G.J.2    Kraft, C.A.3    Ray, K.4    Cranfill, P.J.5    Wilson, K.A.6
  • 75
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • doi: 10.1016/S0076-6879(00)27297-2
    • Miyawaki, A., and Tsien, R. Y. (2000). Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol. 327, 427-500. doi: 10.1016/S0076-6879(00)27297-2
    • (2000) Methods Enzymol , vol.327 , pp. 427-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 77
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • doi: 10.1021/bi002263b
    • Mizuno, H., Sawano, A., Eli, P., Hama, H., and Miyawaki, A. (2001). Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry. 40, 2502-2510. doi: 10.1021/bi002263b
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5
  • 78
    • 57049179582 scopus 로고    scopus 로고
    • Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP
    • doi: 10.1007/s11068-008-9024-9
    • Murakoshi, H., Lee, S. J., and Yasuda, R. (2008).Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP. Brain Cell Biol. 36, 31-42. doi: 10.1007/s11068-008-9024-9
    • (2008) Brain Cell Biol , vol.36 , pp. 31-42
    • Murakoshi, H.1    Lee, S.J.2    Yasuda, R.3
  • 79
    • 71249124044 scopus 로고    scopus 로고
    • Multiple redox and nonredox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast
    • doi: 10.1093/mp/ssp089
    • Muthuramalingam, M., Seidel, T., Laxa, M., Nunes de Miranda, S. M., Gartner, F., Stroher, E., et al. (2009).Multiple redox and nonredox interactions define 2-Cys peroxiredoxin as a regulatory hub in the chloroplast. Mol. Plant 2, 1288. doi: 10.1093/mp/ssp089
    • (2009) Mol. Plant , pp. 2
    • Muthuramalingam, M.1    Seidel, T.2    Laxa, M.3    Nunes de Miranda, S.M.4    Gartner, F.5    Stroher, E.6
  • 80
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • doi: 10.1038/nbt0102-87
    • Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K., and Miyawaki A, (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90. doi: 10.1038/nbt0102-87
    • (2002) Nat. Biotechnol , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 82
    • 84872110559 scopus 로고    scopus 로고
    • Quantitative imaging with fluorescent biosensors
    • doi: 10.1146/annurev-arplant-042110-103745
    • Okumoto, S., Jones, A., and Frommer, W. B. (2012). Quantitative imaging with fluorescent biosensors. Annu. Rev. Plant Biol. 63, 663-706. doi: 10.1146/annurev-arplant-042110-103745
    • (2012) Annu. Rev. Plant Biol , vol.63 , pp. 663-706
    • Okumoto, S.1    Jones, A.2    Frommer, W.B.3
  • 83
    • 28544434112 scopus 로고    scopus 로고
    • Characterization of vacuolar transport of the endogenous alkaloid berberine in
    • doi: 10.1104/pp. 105.064352
    • Otani, M., Shitan, N., Sakai, K., Martinoia, E., Sato, F., and Yazaki, K. (2005). Characterization of vacuolar transport of the endogenous alkaloid berberine in Coptis japonica. Plant Physiol. 138, 1939-1946. doi: 10.1104/pp. 105.064352
    • (2005) Coptis Japonica. Plant Physiol , vol.138 , pp. 1939-1946
    • Otani, M.1    Shitan, N.2    Sakai, K.3    Martinoia, E.4    Sato, F.5    Yazaki, K.6
  • 84
    • 55549111893 scopus 로고    scopus 로고
    • Quantitative FRET-analysis by fast acquisitions time domain FLIM at high spatial resolution in living cells
    • doi: 10.1529/biophysj.108.131276
    • Padilla-Parra, S., Auduge, N., Coppey-Moisan, M., and Tramier, M. (2008). Quantitative FRET-analysis by fast acquisitions time domain FLIM at high spatial resolution in living cells. Biophys. J. 95, 2976-2988. doi: 10.1529/biophysj.108.131276
    • (2008) Biophys. J , vol.95 , pp. 2976-2988
    • Padilla-Parra, S.1    Auduge, N.2    Coppey-Moisan, M.3    Tramier, M.4
  • 85
    • 70449135167 scopus 로고    scopus 로고
    • Quantitative comparison of different fluorescent protein couples for fast FRET-FLIM acquisition
    • doi: 10.1016/j.bpj.2009.07.044
    • Padilla-Parra, S., Auduge, N., Lalucque, H, Mevel, J. C., Coppey-Moisan, M., and Tramier, M. (2009). Quantitative comparison of different fluorescent protein couples for fast FRET-FLIM acquisition. Biophys. J. 97, 2368-2376. doi: 10.1016/j.bpj.2009.07.044
    • (2009) Biophys. J , vol.97 , pp. 2368-2376
    • Padilla-Parra, S.1    Auduge, N.2    Lalucque, H.3    Mevel, J.C.4    Coppey-Moisan, M.5    Tramier, M.6
  • 86
    • 0034633010 scopus 로고    scopus 로고
    • Forster distances between green fluorescent protein pairs
    • doi: 10.1006/abio.2000.4708
    • Patterson, G. H., Piston, D. W., and Barisas, B. G. (2000). Forster distances between green fluorescent protein pairs. Anal. Biochem. 284, 438-440. doi: 10.1006/abio.2000.4708
    • (2000) Anal. Biochem , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 88
    • 0037436408 scopus 로고    scopus 로고
    • FRET-based in vivo screening for protein folding and increased protein stability
    • doi: 10.1016/S0022-2836(03)00077-9
    • Philipps, B., Hennecke, J., and Glockshuber, R. (2003). FRET-based in vivo screening for protein folding and increased protein stability. J. Mol. Biol. 327, 239-249. doi: 10.1016/S0022-2836(03)00077-9
    • (2003) J. Mol. Biol , vol.327 , pp. 239-249
    • Philipps, B.1    Hennecke, J.2    Glockshuber, R.3
  • 89
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • doi: 10.1016/j.tibs.2007.08.003
    • Piston, D. W., and Kremer, G. J. (2007). Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem. Sci. 32, 407-414. doi: 10.1016/j.tibs.2007.08.003
    • (2007) Trends Biochem. Sci , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremer, G.J.2
  • 90
    • 84858753232 scopus 로고    scopus 로고
    • Autofluorescence of atmospheric bioaerosols-fluorescent biomolecules and potential interferences
    • doi: 10.5194/amtd-4-5857-2011
    • Pohlker, C., Huffman, J. A., and Poschl, U. (2011). Autofluorescence of atmospheric bioaerosols-fluorescent biomolecules and potential interferences. Atmos. Meas. Tech. 4, 5857-5933. doi: 10.5194/amtd-4-5857-2011
    • (2011) Atmos. Meas. Tech , vol.4 , pp. 5857-5933
    • Pohlker, C.1    Huffman, J.A.2    Poschl, U.3
  • 91
    • 79953660304 scopus 로고    scopus 로고
    • Flow cytometric and fluorometric methods of quantifying and characterizing apoptotic cell death
    • ed M. A. Davis (Totowa, NJ: Humana Press, 11-36
    • Poot, M., Pierce, R. H., and Kavanagh, T. J. (2002). "Flow cytometric and fluorometric methods of quantifying and characterizing apoptotic cell death", in Apoptosis methods in Pharmakology and Toxikology, ed M. A. Davis (Totowa, NJ: Humana Press), 11-36
    • (2002) Apoptosis Methods In Pharmakology and Toxikology
    • Poot, M.1    Pierce, R.H.2    Kavanagh, T.J.3
  • 92
    • 70349238824 scopus 로고    scopus 로고
    • Enhanced yellow fluorescent protein photoconversion to a cyan fluorescent protein-like species is sensitive to thermal and diffusion conditions
    • doi: 10.1117/1.3103338
    • Raarup, M. K., Fjorback, A. W., Jensen, S.M. R., Müller, H. K., Kjærgaard, M. M., Poulsen, H., et al. (2009). Enhanced yellow fluorescent protein photoconversion to a cyan fluorescent protein-like species is sensitive to thermal and diffusion conditions. J. Biomed. Opt. 14, 034039. doi: 10.1117/1.3103338
    • (2009) J. Biomed. Opt , vol.14 , pp. 034039
    • Raarup, M.K.1    Fjorback, A.W.2    Jensen, S.M.R.3    Müller, H.K.4    Kjærgaard, M.M.5    Poulsen, H.6
  • 93
    • 12744280975 scopus 로고    scopus 로고
    • Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer
    • doi: 10.1042/ BJ20040226
    • Raicu, V., Jansma, D. B., Miller, R. J. D., and Friesen, J. D. (2005). Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer. Biochem. J. 385, 265-277. doi: 10.1042/ BJ20040226
    • (2005) Biochem. J , vol.385 , pp. 265-277
    • Raicu, V.1    Jansma, D.B.2    Miller, R.J.D.3    Friesen, J.D.4
  • 94
    • 33745659186 scopus 로고    scopus 로고
    • Optimization of pairings and detection conditions for measurement of FRET between cyan and yellow fluorescent proteins
    • doi: 10.1017/S143192760 6060235
    • Rizzo, M. A., Springer, G., Segawa, K., Zipfel, W. R., and Piston, D. W. (2006). Optimization of pairings and detection conditions for measurement of FRET between cyan and yellow fluorescent proteins. Microsc. Microanal. 12, 238-254. doi: 10.1017/S143192760 6060235
    • (2006) Microsc. Microanal , vol.12 , pp. 238-254
    • Rizzo, M.A.1    Springer, G.2    Segawa, K.3    Zipfel, W.R.4    Piston, D.W.5
  • 95
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • doi: 10.1038/nbt945
    • Rizzo, M. A., Springer, G. H., Granada, B, and Piston, D. W. (2004). An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449. doi: 10.1038/nbt945
    • (2004) Nat. Biotechnol , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 96
    • 84890215709 scopus 로고    scopus 로고
    • Vital autofluorescence: Application to the study of plant living cells
    • doi: 10.1155/2012/124672
    • Roshchina, V. V. (2012). Vital autofluorescence: application to the study of plant living cells. Int. J. Spectrosc. 2012, 1-14. doi: 10.1155/2012/124672
    • (2012) Int. J. Spectrosc , vol.2012 , pp. 1-14
    • Roshchina, V.V.1
  • 97
    • 0032773819 scopus 로고    scopus 로고
    • Changes in pollen autofluorescence induced by ozone
    • doi: 10.1023/A:1002120904588
    • Roshchina, V. V., and Karnaukhov, V. N. (1999). Changes in pollen autofluorescence induced by ozone. Biol. Plant. 42, 273-278. doi: 10.1023/A:1002120904588
    • (1999) Biol. Plant , vol.42 , pp. 273-278
    • Roshchina, V.V.1    Karnaukhov, V.N.2
  • 98
    • 0035830829 scopus 로고    scopus 로고
    • Oligomerization of the human serotonin transporter and of the rat GABA transporter 1 visualized byfluorescence resonance energy transfer microscopy in living cells
    • doi: 10.1074/jbc.M007357200
    • Schmid, J. A., Scholze, P., Kudlacek, O., Freissmuth, M., Singer, E. A., and Sitte, H. H. (2001). Oligomerization of the human serotonin transporter and of the rat GABA transporter 1 visualized byfluorescence resonance energy transfer microscopy in living cells. J. Biol. Chem. 276, 3805-3810. doi: 10.1074/jbc.M007357200
    • (2001) J. Biol. Chem , vol.276 , pp. 3805-3810
    • Schmid, J.A.1    Scholze, P.2    Kudlacek, O.3    Freissmuth, M.4    Singer, E.A.5    Sitte, H.H.6
  • 100
    • 57849154989 scopus 로고    scopus 로고
    • Fluorescent proteins for singlemolecule fluorescence applications
    • doi: 10.1002/jbio.200710024
    • Seefeldt, B., Kasper, R., Seidel, T., Tinnefeld, P., Dietz, K. J., Heilemann, M., et al. (2008). Fluorescent proteins for singlemolecule fluorescence applications. J. Biophotonics 1, 74-82. doi: 10.1002/jbio.200710024
    • (2008) J. Biophotonics , vol.1 , pp. 74-82
    • Seefeldt, B.1    Kasper, R.2    Seidel, T.3    Tinnefeld, P.4    Dietz, K.J.5    Heilemann, M.6
  • 101
    • 23644461946 scopus 로고    scopus 로고
    • Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements
    • doi: 10.1016/j.febslet.2005.06.077
    • Seidel, T., Golldack, D., and Dietz, K. J. (2005). Mapping of C-termini of V-ATPase subunits by in vivo-FRET measurements. FEBS Lett. 579, 4374-4382. doi: 10.1016/j.febslet.2005.06.077
    • (2005) FEBS Lett , vol.579 , pp. 4374-4382
    • Seidel, T.1    Golldack, D.2    Dietz, K.J.3
  • 103
    • 77956894756 scopus 로고    scopus 로고
    • In vivo analysis of the 2-Cys peroxiredoxin oligomeric state by twostep FRET
    • doi: 10.1016/j.jbiotec.2010.06.016
    • Seidel, T., Seefeldt, B., Sauer, M., and Dietz, K. J. (2010). In vivo analysis of the 2-Cys peroxiredoxin oligomeric state by twostep FRET. J. Biotechnol. 149, 272-279. doi: 10.1016/j.jbiotec.2010.06.016
    • (2010) J. Biotechnol , vol.149 , pp. 272-279
    • Seidel, T.1    Seefeldt, B.2    Sauer, M.3    Dietz, K.J.4
  • 104
    • 84875967395 scopus 로고    scopus 로고
    • Halide and proton binding kinetics of yellow fluorescent protein variants
    • doi: 10.1021/bi3016839
    • Seward, H. E., Basran, J., Denton, R., Pfuhl, M., Muskett, F. W., and Bagshaw, C. R. (2013). Halide and proton binding kinetics of yellow fluorescent protein variants. Biochemistry 52, 2482-2491. doi: 10.1021/bi3016839
    • (2013) Biochemistry , vol.52 , pp. 2482-2491
    • Seward, H.E.1    Basran, J.2    Denton, R.3    Pfuhl, M.4    Muskett, F.W.5    Bagshaw, C.R.6
  • 105
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • doi: 10.1038/nbt1037
    • Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N., Palmer, A. E., and Tsien, R. Y. (2004). Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22, 1567-1572. doi: 10.1038/nbt1037
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 106
    • 77956641670 scopus 로고    scopus 로고
    • Additional correction for energy transfer efficiency calculation in filter-based resonance energy transfer microscopy for more accurate results
    • doi: 10.1117/1.3407655
    • Sun, Y., and Periasamy, A. (2010). Additional correction for energy transfer efficiency calculation in filter-based resonance energy transfer microscopy for more accurate results. J. Biomed. Opt. 15, 020513. doi: 10.1117/1.3407655
    • (2010) J. Biomed. Opt , vol.15 , pp. 020513
    • Sun, Y.1    Periasamy, A.2
  • 107
    • 77958163349 scopus 로고    scopus 로고
    • Three-color spe-tral FRET microscopy localizes three interacting proteins in living cells
    • doi: 10.1016/j.bpj. 2010.06.004
    • Sun, Y., Wallrabe, H., Booker, C. F., Day, R. N., and Periasamy A, (2010). Three-color spe-tral FRET microscopy localizes three interacting proteins in living cells. Biophys. J. 99, 1283. doi: 10.1016/j.bpj. 2010.06.004
    • (2010) Biophys. J , vol.99 , pp. 1283
    • Sun, Y.1    Wallrabe, H.2    Booker, C.F.3    Day, R.N.4    Periasamy, A.5
  • 108
    • 26444493680 scopus 로고    scopus 로고
    • Computer program for analysing donor photobleaching FRET image series
    • doi: 10.1002/cyto.a.20175
    • Szentesi, G., Vereb, G., Horvath, G., Bodnar, A., Fabian, A., Matkó, J., et al. (2005). Computer program for analysing donor photobleaching FRET image series. Cytometry A 67A, 119-128. doi: 10.1002/cyto.a.20175
    • (2005) Cytometry A , vol.67 A , pp. 119-128
    • Szentesi, G.1    Vereb, G.2    Horvath, G.3    Bodnar, A.4    Fabian, A.5    Matkó, J.6
  • 109
    • 67349176187 scopus 로고    scopus 로고
    • An ultramarine fluorescent protein with increased photostability and pH insensitivity
    • doi: 10.1038/nmeth.1317
    • Tomosugi, W., Matsuda, T., Tani, T., Nemoto, T., Kotera, I., Saito, K., et al. (2009). An ultramarine fluorescent protein with increased photostability and pH insensitivity. Nat. Methods 6, 351-353. doi: 10.1038/nmeth.1317
    • (2009) Nat. Methods , vol.6 , pp. 351-353
    • Tomosugi, W.1    Matsuda, T.2    Tani, T.3    Nemoto, T.4    Kotera, I.5    Saito, K.6
  • 110
    • 33750708280 scopus 로고    scopus 로고
    • Sensitivity of CFP/YFP and GFP/mCherry pairs to donor photobleaching on FRET determination by fluorescence lifetime imaging microscopy in living cells
    • doi: 10.1002/ jemt.20370
    • Tramier, M., Zahid, M., Mevel, J., Masse, M. J., and Coppey-Moisan, M. (2006). Sensitivity of CFP/YFP and GFP/mCherry pairs to donor photobleaching on FRET determination by fluorescence lifetime imaging microscopy in living cells. Microsc. Res. Tech. 69, 933-939. doi: 10.1002/ jemt.20370
    • (2006) Microsc. Res. Tech , vol.69 , pp. 933-939
    • Tramier, M.1    Zahid, M.2    Mevel, J.3    Masse, M.J.4    Coppey-Moisan, M.5
  • 111
    • 28544448884 scopus 로고    scopus 로고
    • Photoconversion of YFP into a CFP-like species during acceptor photobleaching FRET experiments
    • doi: 10.1038/nmeth1105-801
    • Valentin, G., Verheggen, C., Piolot, T., Neel, H., Coppey-Moisan, M., and Bertrand, E. (2005). Photoconversion of YFP into a CFP-like species during acceptor photobleaching FRET experiments. Nat. Methods 2, 801. doi: 10.1038/nmeth1105-801
    • (2005) Nat. Methods , vol.2 , pp. 801
    • Valentin, G.1    Verheggen, C.2    Piolot, T.3    Neel, H.4    Coppey-Moisan, M.5    Bertrand, E.6
  • 112
    • 20444383852 scopus 로고    scopus 로고
    • Fluorescence resonance Energy transfer (FRET) measurement by gradual acceptor photobleaching
    • doi: 10.1111/j.1365-2818.2005.01483.x
    • van Munster, E. B., Kremers, G. J., Adjobo-Hermans, M. J. W., and Gadella, T. W. J. (2005). Fluorescence resonance Energy transfer (FRET) measurement by gradual acceptor photobleaching. J. Microsc. 218, 253-262. doi: 10.1111/j.1365-2818.2005.01483.x
    • (2005) J. Microsc , vol.218 , pp. 253-262
    • van Munster, E.B.1    Kremers, G.J.2    Adjobo-Hermans, M.J.W.3    Gadella, T.W.J.4
  • 113
    • 1942487298 scopus 로고    scopus 로고
    • Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission
    • doi: 10.1016/ S0006-3495(04)74307-6
    • van Rheenen, J., Langeslag, M., and Jalink, K. (2004). Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission. Biophys. J. 86, 2517-2529. doi: 10.1016/ S0006-3495(04)74307-6
    • (2004) Biophys. J , vol.86 , pp. 2517-2529
    • van Rheenen, J.1    Langeslag, M.2    Jalink, K.3
  • 114
    • 84870064092 scopus 로고    scopus 로고
    • The Arabidopsis B-type response regulator 18 homodimer-izes and positively regulates cytokinin responses
    • doi: 10.1111/j.1365-313X. 2012.05101.x
    • Veerabagu, M., Elgass, K., Kirchler, T., Huppenberger, P., Harter, K., Chaban, C., et al. (2012). The Arabidopsis B-type response regulator 18 homodimer-izes and positively regulates cytokinin responses. Plant J. 72, 721-731. doi: 10.1111/j.1365-313X. 2012.05101.x
    • (2012) Plant J , vol.72 , pp. 721-731
    • Veerabagu, M.1    Elgass, K.2    Kirchler, T.3    Huppenberger, P.4    Harter, K.5    Chaban, C.6
  • 115
    • 2142762991 scopus 로고    scopus 로고
    • Probing plasma membrane microdomains in cowpea protoplasts using lapidated GFP-fusion proteins and multimode FRET microscopy
    • doi: 10.1111/j.0022-2720.2004.01318.x
    • Vermeer, J. E. M., van Munster, E. B, Vischer, N. O., and Gadella, T. W. J. (2004). Probing plasma membrane microdomains in cowpea protoplasts using lapidated GFP-fusion proteins and multimode FRET microscopy. J. Microsc. 214, 190-200. doi: 10.1111/j.0022-2720.2004.01318.x
    • (2004) J. Microsc , vol.214 , pp. 190-200
    • Vermeer, J.E.M.1    van Munster, E.B.2    Vischer, N.O.3    Gadella, T.W.J.4
  • 116
    • 59249104843 scopus 로고    scopus 로고
    • Frequency domain FLIM theory, instrumentation, and data analysis
    • doi: 10.1016/S0075-7535(08)00002-8
    • Verveer, P. J., and Hanley, Q. S. (2009). Frequency domain FLIM theory, instrumentation, and data analysis. Lab. Tech. Biochem. Mol. Biol. 33, 59-94. doi: 10.1016/S0075-7535(08)00002-8
    • (2009) Lab. Tech. Biochem. Mol. Biol , vol.33 , pp. 59-94
    • Verveer, P.J.1    Hanley, Q.S.2
  • 117
    • 80052950611 scopus 로고    scopus 로고
    • Immunofluorescence microscopy for localization of Arabidopsis chloroplast proteins
    • doi: 10.1007/978-1-61779-234-2_3
    • Vitha, S., and Osteryoung, K. W. (2011). Immunofluorescence microscopy for localization of Arabidopsis chloroplast proteins. Methods Mol. Biol. 774, 33-58. doi: 10.1007/978-1-61779-234-2_3
    • (2011) Methods Mol. Biol , vol.774 , pp. 33-58
    • Vitha, S.1    Osteryoung, K.W.2
  • 118
    • 84869021496 scopus 로고    scopus 로고
    • The impact of heterogeneity and dark acceptor states on FRET: Implications for using fluorescent protein donors and acceptors
    • doi: 10.1371/jour-nal.pone.0049593
    • Vogel, S. S., Nguyen, T. A., van der Meer, B. W., and Blank, P. S. (2012). The impact of heterogeneity and dark acceptor states on FRET: implications for using fluorescent protein donors and acceptors. PLoS ONE 7:e49593. doi: 10.1371/jour-nal.pone.0049593
    • (2012) PLoS ONE , vol.7
    • Vogel, S.S.1    Nguyen, T.A.2    van der Meer, B.W.3    Blank, P.S.4
  • 119
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • doi: 10.1016/j.copbio.2004.12.002
    • Wallrabe, H., and Periasamy, A. (2005). Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16, 19-27. doi: 10.1016/j.copbio.2004.12.002
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 120
    • 79951832251 scopus 로고    scopus 로고
    • Alanine zipper-like coiled-coil domains are necessary for homotypic dimer-ization of plant GAGA-factors in the nucleus and nucleolus
    • doi: 10.1371/journal.pone.0016070
    • Wanke, D., Hohenstatt, M. L., Dynowski, M., Bloss, U., Hecker, A., Elgass, K., et al. (2011). Alanine zipper-like coiled-coil domains are necessary for homotypic dimer-ization of plant GAGA-factors in the nucleus and nucleolus. PLoS ONE 6:e16070. doi: 10.1371/journal.pone.0016070
    • (2011) PLoS ONE , vol.6
    • Wanke, D.1    Hohenstatt, M.L.2    Dynowski, M.3    Bloss, U.4    Hecker, A.5    Elgass, K.6
  • 121
    • 0038788011 scopus 로고    scopus 로고
    • Two-step FRET as a structural tool
    • doi: 10.1021/ja034564p
    • Watrob, H. M., Pan, C. P., and Barkley, M. D. (2003). Two-step FRET as a structural tool. J. Am. Chem. Soc. 125, 7336-7343. doi: 10.1021/ja034564p
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 7336-7343
    • Watrob, H.M.1    Pan, C.P.2    Barkley, M.D.3
  • 122
    • 84864985839 scopus 로고    scopus 로고
    • Mitochondrial cysteine synthase complex regulates O-Acetylserine biosynthesis in plants
    • doi: 10.1074/jbc. M112.372656
    • Wirtz, M., Beard, K. F. M., Lee, C. P., Boltz, A., Schwarzlander, M., Fuchs, C,et al. (2012). Mitochondrial cysteine synthase complex regulates O-Acetylserine biosynthesis in plants. J. Biol. Chem. 287, 27941-27947. doi: 10.1074/jbc. M112.372656
    • (2012) J. Biol. Chem , vol.287 , pp. 27941-27947
    • Wirtz, M.1    Beard, K.F.M.2    Lee, C.P.3    Boltz, A.4    Schwarzlander, M.5    Fuchs, C.6
  • 123
    • 84885041942 scopus 로고    scopus 로고
    • Kaede for detection of protein oligomerization
    • doi: 10.1093/ mp/sst039
    • Wolf, H., Barisas, B. G., Dietz, K. J., and Seidel, T. (2013a). Kaede for detection of protein oligomerization. Mol. Plant. 1453-1462. doi: 10.1093/ mp/sst039
    • (2013) Mol. Plant , pp. 1453-1462
    • Wolf, H.1    Barisas, B.G.2    Dietz, K.J.3    Seidel, T.4
  • 124
    • 84872228493 scopus 로고    scopus 로고
    • Elements of the transcriptional machinery are compatible among plants and mammals
    • doi: 10.1371/journal.pone.0053737
    • Wolf, A., Akrap, N., Marg, B., Galliardt, H, Heiligentag, M., Humpert, F., et al. (2013b). Elements of the transcriptional machinery are compatible among plants and mammals. PLoS ONE 8:e53737. doi: 10.1371/journal.pone.0053737
    • (2013) PLoS ONE , vol.8
    • Wolf, A.1    Akrap, N.2    Marg, B.3    Galliardt, H.4    Heiligentag, M.5    Humpert, F.6
  • 125
    • 0000822375 scopus 로고
    • The fluorescence of organic natural products
    • ed S. G. Schulman (New York, NY: John Wiley and Sons)
    • Wolfbeis, O. S. (1985). "The fluorescence of organic natural products, in Molecular Luminescence Spectroscopy: Methods and Applications, ed S. G. Schulman (New York, NY: John Wiley and Sons).
    • (1985) Molecular Luminescence Spectroscopy: Methods and Applications
    • Wolfbeis, O.S.1
  • 126
    • 66149096239 scopus 로고    scopus 로고
    • Fluorescence fluctuation spectroscopy of mCherry in living cells
    • doi: 10.1016/j.bpj. 2008.12.3902
    • Wu, B., Chen, Y., and Muller, J. D. (2009). Fluorescence fluctuation spectroscopy of mCherry in living cells. Biophys. J. 96, 2391-2404. doi: 10.1016/j.bpj. 2008.12.3902
    • (2009) Biophys. J , vol.96 , pp. 2391-2404
    • Wu, B.1    Chen, Y.2    Muller, J.D.3
  • 127
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • doi: 10.1016/S0006-3495(01)75886-9
    • Xia, Z., and Liu, Y. (2001). Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402. doi: 10.1016/S0006-3495(01)75886-9
    • (2001) Biophys. J , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 128
    • 0029780351 scopus 로고    scopus 로고
    • Structure of the green fluorescent protein
    • doi: 10.1038/nbt1096-1246
    • Yang, F., Moss, L. G., and Philipps, Jr. (1996). Structure of the green fluorescent protein. Nat. Biotechnol. 14, 1246-1251. doi: 10.1038/nbt1096-1246
    • (1996) Nat. Biotechnol , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Philipps, J.3
  • 129
    • 2942640371 scopus 로고    scopus 로고
    • Photobleaching-corrected FRET efficiency imaging of live cells
    • doi: 10.1529/biophysj.103.022087
    • Zal, T., and Gascoigne, N. R. J. (2004). Photobleaching-corrected FRET efficiency imaging of live cells. Biophys. J. 86, 3923-3939. doi: 10.1529/biophysj.103.022087
    • (2004) Biophys. J , vol.86 , pp. 3923-3939
    • Zal, T.1    Gascoigne, N.R.J.2
  • 130
    • 3042511548 scopus 로고    scopus 로고
    • Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP
    • doi: 10.1186/14726750-3-5
    • Zapata-Hommer, O., Griesbeck, O. (2003). Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP. BMC Biotechnol. 3:5. doi: 10.1186/14726750-3-5
    • (2003) BMC Biotechnol , vol.3 , pp. 5
    • Zapata-Hommer, O.1    Griesbeck, O.2


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