메뉴 건너뛰기




Volumn 6, Issue 9, 2011, Pages 1324-1340

Investigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopy

Author keywords

[No Author keywords available]

Indexed keywords

CCAAT ENHANCER BINDING PROTEIN ALPHA;

EID: 80052399465     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2011.364     Document Type: Article
Times cited : (207)

References (80)
  • 2
    • 80052421739 scopus 로고    scopus 로고
    • Fluorescence lifetime-resolved imaging: What, why, how-a prologue
    • eds. Periasamy, A. & Clegg, R.M. CRC Press
    • Clegg, R.M. Fluorescence lifetime-resolved imaging: what, why, how-a prologue. In FLIM Microscopy in Biology and Medicine (eds. Periasamy, A. & Clegg, R.M.) 3-34 (CRC Press, 2009).
    • (2009) FLIM Microscopy in Biology and Medicine , pp. 3-34
    • Clegg, R.M.1
  • 4
    • 27344446580 scopus 로고
    • Microscope phase fuorometer for determining the fuorescence lifetimes of fuorochromes
    • Venetta, B.D. Microscope phase fuorometer for determining the fuorescence lifetimes of fuorochromes. Rev. Sci. Instrum. 30, 450-457 (1959).
    • (1959) Rev. Sci. Instrum. , vol.30 , pp. 450-457
    • Venetta, B.D.1
  • 5
    • 80052410766 scopus 로고    scopus 로고
    • FLIM applications in the biomedical sciences
    • eds. Periasamy, A. & Clegg, R.M. CRC Press
    • Periasamy, A. & Clegg, R.M. FLIM applications in the biomedical sciences. In FLIM Microscopy in Biology and Medicine (eds. Periasamy, A. & Clegg, R.M.) 385-400 (CRC Press, 2009).
    • (2009) FLIM Microscopy in Biology and Medicine , pp. 385-400
    • Periasamy, A.1    Clegg, R.M.2
  • 8
    • 21644450243 scopus 로고    scopus 로고
    • Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotropy
    • DOI 10.1074/jbc.M502475200
    • Vishwasrao, H.D., Heikal, A.A., Kasischke, K.A. & Webb, W.W. Conformational dependence of intracellular NADH on metabolic state revealed by associated fuorescence anisotropy. J. Biol. Chem. 280, 25119-25126 (2005). (Pubitemid 40934604)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25119-25126
    • Vishwasrao, H.D.1    Heikal, A.A.2    Kasischke, K.A.3    Webb, W.W.4
  • 9
    • 60849102190 scopus 로고    scopus 로고
    • Differentiation of apoptosis from necrosis by dynamic changes of reduced nicotinamide adenine dinucleotide fuorescence lifetime in live cells
    • Wang, H.W. et al. Differentiation of apoptosis from necrosis by dynamic changes of reduced nicotinamide adenine dinucleotide fuorescence lifetime in live cells. J. Biomed. Opt. 13, 054011 (2008).
    • (2008) J. Biomed. Opt. , vol.13 , pp. 054011
    • Wang, H.W.1
  • 11
    • 33847144568 scopus 로고    scopus 로고
    • Multiphoton fluorescence lifetime imaging of human hair
    • DOI 10.1002/jemt.20395
    • Ehlers, A., Riemann, I., Stark, M. & Konig, K. Multiphoton fuorescence lifetime imaging of human hair. Microsc. Res. Tech. 70, 154-161 (2007). (Pubitemid 46292250)
    • (2007) Microscopy Research and Technique , vol.70 , Issue.2 , pp. 154-161
    • Ehlers, A.1    Riemann, I.2    Stark, M.3    Konig, K.4
  • 12
    • 60849115874 scopus 로고    scopus 로고
    • Two-photon autofuorescence and second-harmonic imaging of adult stem cells
    • Uchugonova, A. & Konig, K. Two-photon autofuorescence and second-harmonic imaging of adult stem cells. J. Biomed. Opt. 13, 054068 (2008).
    • (2008) J. Biomed. Opt. , vol.13 , pp. 054068
    • Uchugonova, A.1    Konig, K.2
  • 13
    • 15244341378 scopus 로고    scopus 로고
    • Familial Alzheimer's disease presenilin 1 mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein
    • DOI 10.1523/JNEUROSCI.0364-05.2005
    • Berezovska, O. et al. Familial Alzheimer's disease presenilin 1 mutations cause alterations in the conformation of presenilin and interactions with amyloid precursor protein. J. Neurosci. 25, 3009-3017 (2005). (Pubitemid 40389259)
    • (2005) Journal of Neuroscience , vol.25 , Issue.11 , pp. 3009-3017
    • Berezovska, O.1    Lleo, A.2    Herl, L.D.3    Frosch, M.P.4    Stern, E.A.5    Bacskai, B.J.6    Hyman, B.T.7
  • 14
    • 33846190169 scopus 로고    scopus 로고
    • Application of novel low-intensity nonscanning fuorescence lifetime imaging microscopy for monitoring excited state dynamics in individual chloroplasts and living cells of photosynthetic organisms
    • Eckert, H., Petráek, Z. & Kemnitz, K. Application of novel low-intensity nonscanning fuorescence lifetime imaging microscopy for monitoring excited state dynamics in individual chloroplasts and living cells of photosynthetic organisms. Proc. SPIE 6372, 637207 (2006).
    • (2006) Proc. SPIE , vol.6372 , pp. 637207
    • Eckert, H.1    Petráek, Z.2    Kemnitz, K.3
  • 15
    • 76149092166 scopus 로고    scopus 로고
    • Wide-feld photon counting fuorescence lifetime imaging microscopy: Application to photosynthesizing systems
    • Petrasek, Z., Eckert, H.J. & Kemnitz, K. Wide-feld photon counting fuorescence lifetime imaging microscopy: application to photosynthesizing systems. Photosynth Res. 102, 157-168 (2009).
    • (2009) Photosynth Res. , vol.102 , pp. 157-168
    • Petrasek, Z.1    Eckert, H.J.2    Kemnitz, K.3
  • 16
    • 0033533709 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
    • DOI 10.1016/S0960-9822(99)80484-9
    • Wouters, F.S. & Bastiaens, P.I. Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells. Curr. Biol. 9, 1127-1130 (1999). (Pubitemid 29504485)
    • (1999) Current Biology , vol.9 , Issue.19 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.H.2
  • 17
    • 0347756761 scopus 로고    scopus 로고
    • Protein localization in living cells and tissues using FRET and FLIM
    • DOI 10.1111/j.1432-0436.2003.07109007.x
    • Chen, Y., Mills, J.D. & Periasamy, A. Protein localization in living cells and tissues using FRET and FLIM. Differentiation 71, 528-541 (2003). (Pubitemid 38091095)
    • (2003) Differentiation , vol.71 , Issue.9-10 , pp. 528-541
    • Chen, Y.1    Mills, J.D.2    Periasamy, A.3
  • 18
    • 0141509840 scopus 로고    scopus 로고
    • Quantitative imaging of protein-protein interactions by multiphoton fuorescence lifetime imaging microscopy using a streak camera
    • Krishnan, R.V., Masuda, A., Centonze, V.E. & Herman, B. Quantitative imaging of protein-protein interactions by multiphoton fuorescence lifetime imaging microscopy using a streak camera. J. Biomed. Opt. 8, 362-367 (2003).
    • (2003) J. Biomed. Opt. , vol.8 , pp. 362-367
    • Krishnan, R.V.1    Masuda, A.2    Centonze, V.E.3    Herman, B.4
  • 19
    • 0742270983 scopus 로고    scopus 로고
    • + channel subunits measured with a confocal microscope and a streak camera
    • DOI 10.1038/nbt935
    • + channel subunits measured with a confocal microscope and a streak camera. Nat. Biotechnol. 22, 220-224 (2004). (Pubitemid 38160539)
    • (2004) Nature Biotechnology , vol.22 , Issue.2 , pp. 220-224
    • Biskup, C.1    Zimmer, T.2    Benndorf, K.3
  • 20
    • 0346307455 scopus 로고    scopus 로고
    • Characterization of two-photon excitation fuorescence lifetime imaging microscopy for protein localization
    • DOI 10.1002/jemt.10430
    • Chen, Y. & Periasamy, A. Characterization of two-photon excitation fuorescence lifetime imaging microscopy for protein localization. Microsc. Res. Tech. 63, 72-80 (2004). (Pubitemid 37541973)
    • (2004) Microscopy Research and Technique , vol.63 , Issue.1 , pp. 72-80
    • Chen, Y.1    Periasamy, A.2
  • 22
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • DOI 10.1016/j.copbio.2004.12.002, PII S0958166904001673
    • Wallrabe, H. & Periasamy, A. Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16, 19-27 (2005). (Pubitemid 40249755)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.1 SPEC. ISS. , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 24
    • 33845935811 scopus 로고    scopus 로고
    • Spectrally resolved frequency domain analysis of multi-fluorophore systems undergoing energy transfer
    • DOI 10.1366/000370206779321544
    • Forde, T.S. & Hanley, Q.S. Spectrally resolved frequency domain analysis of multi-fuorophore systems undergoing energy transfer. Appl. Spectrosc. 60, 1442-1452 (2006). (Pubitemid 46034513)
    • (2006) Applied Spectroscopy , vol.60 , Issue.12 , pp. 1442-1452
    • Forde, T.S.1    Hanley, Q.S.2
  • 27
    • 79951963011 scopus 로고    scopus 로고
    • FRET microscopy in 2010: The legacy of Theodor Forster on the 100th anniversary of his birth
    • Sun, Y., Wallrabe, H., Seo, S.A. & Periasamy, A. FRET microscopy in 2010: The legacy of Theodor Forster on the 100th anniversary of his birth. Chemphyschem 12, 462-474 (2011).
    • (2011) Chemphyschem , vol.12 , pp. 462-474
    • Sun, Y.1    Wallrabe, H.2    Seo, S.A.3    Periasamy, A.4
  • 28
    • 0002413436 scopus 로고
    • Delocalized excitation and excitation transfer
    • ed. Sinanoglu, O. Academic Press
    • Förster, T. Delocalized excitation and excitation transfer. In In Modern Quantum Chemistry (ed. Sinanoglu, O.) 93-137 (Academic Press, 1965).
    • (1965) Modern Quantum Chemistry , pp. 93-137
    • Förster, T.1
  • 29
    • 1842563953 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer
    • eds. Wang, X.F. & Herman, B. John Wiley & Sons
    • Clegg, R.M. Fluorescence resonance energy transfer. In Fluorescence Imaging Spectroscopy and Microscopy (eds. Wang, X.F. & Herman, B.) 179-251 (John Wiley & Sons, 1996).
    • (1996) Fluorescence Imaging Spectroscopy and Microscopy , pp. 179-251
    • Clegg, R.M.1
  • 31
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • DOI 10.1083/jcb.200210140
    • Sekar, R.B. & Periasamy, A. Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 160, 629-633 (2003). (Pubitemid 36298259)
    • (2003) Journal of Cell Biology , vol.160 , Issue.5 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 33
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • DOI 10.1016/j.tibs.2007.08.003, PII S0968000407001910
    • Piston, D.W. & Kremers, G.J. Fluorescent protein FRET: the good, the bad and the ugly. Trends Biochem. Sci. 32, 407-414 (2007). (Pubitemid 47369164)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.9 , pp. 407-414
    • Piston, D.W.1    Kremers, G.-J.2
  • 35
    • 0036047349 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging (FLIM) of green fuorescent fusion proteins in living cells
    • Periasamy, A., Elangovan, M., Elliott, E. & Brautigan, D.L. Fluorescence lifetime imaging (FLIM) of green fuorescent fusion proteins in living cells. Methods Mol. Biol. 183, 89-100 (2002)
    • (2002) Methods Mol. Biol. , vol.183 , pp. 89-100
    • Periasamy, A.1    Elangovan, M.2    Elliott, E.3    Brautigan, D.L.4
  • 37
    • 0037974186 scopus 로고    scopus 로고
    • Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes
    • Wallrabe, H., Elangovan, M., Burchard, A., Periasamy, A. & Barroso, M. Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes. Biophys. J. 85, 559-571 (2003). (Pubitemid 36753658)
    • (2003) Biophysical Journal , vol.85 , Issue.1 , pp. 559-571
    • Wallrabe, H.1    Elangovan, M.2    Burchard, A.3    Periasamy, A.4    Barroso, M.5
  • 38
    • 33745344683 scopus 로고    scopus 로고
    • Monitoring dynamic protein interactions with photoquenching FRET
    • DOI 10.1038/nmeth889, PII N889
    • Demarco, I.A., Periasamy, A., Booker, C.F. & Day, R.N. Monitoring dynamic protein interactions with photoquenching FRET. Nat. Methods 3, 519-524 (2006). (Pubitemid 43941769)
    • (2006) Nature Methods , vol.3 , Issue.7 , pp. 519-524
    • Demarco, I.A.1    Periasamy, A.2    Booker, C.F.3    Day, R.N.4
  • 39
    • 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., Mauldin, J.P., Day, R.N. & Periasamy, A. Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions. J. Microsc. 228, 139-152 (2007). (Pubitemid 350013224)
    • (2007) Journal of Microscopy , vol.228 , Issue.2 , pp. 139-152
    • Chen, Y.1    Mauldin, J.P.2    Day, R.N.3    Periasamy, A.4
  • 40
    • 51649094852 scopus 로고    scopus 로고
    • Rab4 and Rab11 coordinately regulate the recycling of angiotensin II type i receptor as demonstrated by fuorescence resonance energy transfer microscopy
    • Li, H., Li, H.F., Felder, R.A., Periasamy, A. & Jose, P.A. Rab4 and Rab11 coordinately regulate the recycling of angiotensin II type I receptor as demonstrated by fuorescence resonance energy transfer microscopy. J. Biomed. Opt. 13, 031206 (2008).
    • (2008) J. Biomed. Opt. , vol.13 , pp. 031206
    • Li, H.1    Li, H.F.2    Felder, R.A.3    Periasamy, A.4    Jose, P.A.5
  • 41
    • 51649120352 scopus 로고    scopus 로고
    • Characterization of an improved donor fuorescent protein for Forster resonance energy transfer microscopy
    • Day, R.N., Booker, C.F. & Periasamy, A. Characterization of an improved donor fuorescent protein for Forster resonance energy transfer microscopy. J. Biomed. Opt. 13, 031203 (2008).
    • (2008) J. Biomed. Opt. , vol.13 , pp. 031203
    • Day, R.N.1    Booker, C.F.2    Periasamy, A.3
  • 42
    • 57949104871 scopus 로고    scopus 로고
    • Chapter 22: Quantitation of protein-protein interactions: Confocal FRET microscopy
    • Periasamy, A., Wallrabe, H., Chen, Y. & Barroso, M. Chapter 22: Quantitation of protein-protein interactions: confocal FRET microscopy. Methods Cell Biol. 89, 569-598 (2008).
    • (2008) Methods Cell Biol. , vol.89 , pp. 569-598
    • Periasamy, A.1    Wallrabe, H.2    Chen, Y.3    Barroso, M.4
  • 43
    • 74049125375 scopus 로고    scopus 로고
    • Characterization of an orange acceptor fuorescent protein for sensitized spectral fuorescence resonance energy transfer microscopy using a white-light laser
    • Sun, Y. et al. Characterization of an orange acceptor fuorescent protein for sensitized spectral fuorescence resonance energy transfer microscopy using a white-light laser. J. Biomed. Opt. 14, 054009 (2009).
    • (2009) J. Biomed. Opt. , vol.14 , pp. 054009
    • Sun, Y.1
  • 44
    • 79951999288 scopus 로고    scopus 로고
    • Actin cytoskeleton-dependent Rab GTPase-regulated angiotensin type i receptor lysosomal degradation studied by fuorescence lifetime imaging microscopy
    • Li, H. et al. Actin cytoskeleton-dependent Rab GTPase-regulated angiotensin type I receptor lysosomal degradation studied by fuorescence lifetime imaging microscopy. J. Biomed. Opt. 15, 056003 (2010).
    • (2010) J. Biomed. Opt. , vol.15 , pp. 056003
    • Li, H.1
  • 45
    • 0034802539 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus
    • DOI 10.1006/meth.2001.1211
    • Day, R.N., Periasamy, A. & Schaufele, F. Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus. Methods 25, 4-18 (2001). (Pubitemid 32905284)
    • (2001) Methods , vol.25 , Issue.1 , pp. 4-18
    • Day, R.N.1    Periasamy, A.2    Schaufele, F.3
  • 46
    • 0141644218 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging for the two-photon microscope: Time-domain and frequency-domain methods
    • Gratton, E., Breusegem, S., Sutin, J., Ruan, Q. & Barry, N. Fluorescence lifetime imaging for the two-photon microscope: time-domain and frequency-domain methods. J. Biomed. Opt. 8, 381-390 (2003).
    • (2003) J. Biomed. Opt. , vol.8 , pp. 381-390
    • Gratton, E.1    Breusegem, S.2    Sutin, J.3    Ruan, Q.4    Barry, N.5
  • 47
    • 40649092856 scopus 로고    scopus 로고
    • A novel fluorescence lifetime imaging system that optimizes photon efficiency
    • DOI 10.1002/jemt.20540
    • Colyer, R.A., Lee, C. & Gratton, E. A novel fuorescence lifetime imaging system that optimizes photon effciency. Microsc. Res. Tech. 71, 201-213 (2008). (Pubitemid 351374447)
    • (2008) Microscopy Research and Technique , vol.71 , Issue.3 , pp. 201-213
    • Colyer, R.A.1    Lee, C.2    Gratton, E.3
  • 48
    • 0036164650 scopus 로고    scopus 로고
    • Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell
    • DOI 10.1046/j.0022-2720.2001.00984.x
    • Elangovan, M., Day, R.N. & Periasamy, A. Nanosecond fuorescence resonance energy transfer-fuorescence lifetime imaging microscopy to localize the protein interactions in a single living cell. J. Microsc. 205, 3-14 (2002). (Pubitemid 34131778)
    • (2002) Journal of Microscopy , vol.205 , Issue.1 , pp. 3-14
    • Elangovan, M.1    Day, R.N.2    Periasamy, A.3
  • 49
    • 51649093566 scopus 로고    scopus 로고
    • Rapid frequency-domain FLIM spinning disk confocal microscope: Lifetime resolution, image improvement and wavelet analysis
    • Buranachai, C., Kamiyama, D., Chiba, A., Williams, B.D. & Clegg, R.M. Rapid frequency-domain FLIM spinning disk confocal microscope: lifetime resolution, image improvement and wavelet analysis. J. Fluoresc. 18, 929-942 (2008).
    • (2008) J. Fluoresc. , vol.18 , pp. 929-942
    • Buranachai, C.1    Kamiyama, D.2    Chiba, A.3    Williams, B.D.4    Clegg, R.M.5
  • 50
    • 0036016786 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging in scanning microscopes: Acquisition speed, photon economy and lifetime resolution
    • DOI 10.1046/j.1365-2818.2002.01031.x
    • Gerritsen, H.C., Asselbergs, M.A., Agronskaia, A.V. & Van Sark, W.G. Fluorescence lifetime imaging in scanning microscopes: acquisition speed, photon economy and lifetime resolution. J. Microsc. 206, 218-224 (2002). (Pubitemid 34639419)
    • (2002) Journal of Microscopy , vol.206 , Issue.3 , pp. 218-224
    • Gerritsen, H.C.1    Asselbergs, M.A.H.2    Agronskaia, A.V.3    Van Sark, W.G.J.H.M.4
  • 51
    • 36849041206 scopus 로고    scopus 로고
    • High speed optically sectioned fuorescence lifetime imaging permits study of live cell signaling events
    • Grant, D.M. et al. High speed optically sectioned fuorescence lifetime imaging permits study of live cell signaling events. Opt. Express 15, 15656-15673 (2007).
    • (2007) Opt. Express , vol.15 , pp. 15656-15673
    • Grant, D.M.1
  • 52
    • 65349089020 scopus 로고    scopus 로고
    • Fluorescence lifetime optical projection tomography
    • McGinty, J. et al. Fluorescence lifetime optical projection tomography. J. Biophotonics 1, 390-394 (2008).
    • (2008) J. Biophotonics , vol.1 , pp. 390-394
    • McGinty, J.1
  • 55
    • 80052420326 scopus 로고    scopus 로고
    • Error analysis of the rapid lifetime determination method for double-exponential decays and new windowing schemes
    • Sharman, K.K., Periasamy, A., Asworth, H. & Demas, J.N. Error analysis of the rapid lifetime determination method for double-exponential decays and new windowing schemes. Anal. Chem. 71947-71952.
    • Anal. Chem. , pp. 71947-71952
    • Sharman, K.K.1    Periasamy, A.2    Asworth, H.3    Demas, J.N.4
  • 56
    • 17144409955 scopus 로고    scopus 로고
    • AB-plot assisted determination of fluorophore mixtures in a fluorescence lifetime microscope using spectra or quenchers
    • DOI 10.1111/j.1365-2818.2005.01463.x
    • Hanley, Q.S. & Clayton, A.H. AB-plot assisted determination of fuorophore mixtures in a fuorescence lifetime microscope using spectra or quenchers. J. Microsc. 218, 62-67 (2005). (Pubitemid 40524169)
    • (2005) Journal of Microscopy , vol.218 , Issue.1 , pp. 62-67
    • Hanley, Q.S.1    Clayton, A.H.A.2
  • 57
    • 29144446288 scopus 로고    scopus 로고
    • Polar plot representation for frequency-domain analysis of fluorescence lifetimes
    • DOI 10.1007/s10895-005-2990-8
    • Redford, G.I. & Clegg, R.M. Polar plot representation for frequency-domain analysis of fuorescence lifetimes. J. Fluoresc. 15, 805-815 (2005). (Pubitemid 41795606)
    • (2005) Journal of Fluorescence , vol.15 , Issue.5 , pp. 805-815
    • Redford, G.I.1    Clegg, R.M.2
  • 58
    • 38349018672 scopus 로고    scopus 로고
    • The phasor approach to fuorescence lifetime imaging analysis
    • Digman, M.A., Caiolfa, V.R., Zamai, M. & Gratton, E. The phasor approach to fuorescence lifetime imaging analysis. Biophys. J. 94, L14-6 (2008).
    • (2008) Biophys. J. , vol.94
    • Digman, M.A.1    Caiolfa, V.R.2    Zamai, M.3    Gratton, E.4
  • 59
    • 0034029599 scopus 로고    scopus 로고
    • Global analysis of fluorescence lifetime imaging microscopy data
    • Verveer, P.J., Squire, A. & Bastiaens, P.I. Global analysis of fuorescence lifetime imaging microscopy data. Biophys. J. 78, 2127-2137 (2000). (Pubitemid 30183606)
    • (2000) Biophysical Journal , vol.78 , Issue.4 , pp. 2127-2137
    • Verveer, P.J.1    Squire, A.2    Bastiaens, P.I.H.3
  • 60
    • 16444386411 scopus 로고    scopus 로고
    • A fast global ftting algorithm for fuorescence lifetime imaging microscopy based on image segmentation
    • Pelet, S., Previte, M.J., Laiho, L.H. & So, P.T. A fast global ftting algorithm for fuorescence lifetime imaging microscopy based on image segmentation. Biophys. J. 87, 2807-2817 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 2807-2817
    • Pelet, S.1    Previte, M.J.2    Laiho, L.H.3    So, P.T.4
  • 63
    • 0035577918 scopus 로고    scopus 로고
    • Development of a time-resolved fluorescence resonance energy transfer assay (Cell TR-FRET) for protein detection on intact cells
    • DOI 10.1006/abio.2001.5370
    • Lundin, K., Blomberg, K., Nordstrom, T. & Lindqvist, C. Development of a time-resolved fuorescence resonance energy transfer assay (cell TR-FRET) for protein detection on intact cells. Anal. Biochem. 299, 92-97 (2001). (Pubitemid 33124132)
    • (2001) Analytical Biochemistry , vol.299 , Issue.1 , pp. 92-97
    • Lundin, K.1    Blomberg, K.2    Nordstrom, T.3    Lindqvist, C.4
  • 64
    • 3242722132 scopus 로고    scopus 로고
    • A time-resolved fluorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors
    • DOI 10.1016/j.ab.2004.04.011, PII S000326970400329X
    • Zhou, V. et al. A time-resolved fuorescence resonance energy transfer-based HTS assay and a surface plasmon resonance-based binding assay for heat shock protein 90 inhibitors. Anal. Biochem. 331, 349-357 (2004). (Pubitemid 38953086)
    • (2004) Analytical Biochemistry , vol.331 , Issue.2 , pp. 349-357
    • Zhou, V.1    Han, S.2    Brinker, A.3    Klock, H.4    Caldwell, J.5    Gu, X.-J.6
  • 65
    • 70349963770 scopus 로고    scopus 로고
    • Development of high-throughput TR-FRET and AlphaScreen assays for identifcation of potent inhibitors of PDK1
    • Xu, Z. et al. Development of high-throughput TR-FRET and AlphaScreen assays for identifcation of potent inhibitors of PDK1. J. Biomol. Screen. 14, 1257-1262 (2009).
    • (2009) J. Biomol. Screen. , vol.14 , pp. 1257-1262
    • Xu, Z.1
  • 68
    • 0029940327 scopus 로고    scopus 로고
    • Quantitative comparison of excited state properties and intensity-dependent photosensitization by rose bengal
    • DOI 10.1016/1011-1344(95)07248-9
    • Stiel, H., Teuchner, K., Paul, A., Leupold, D. & Kochevar, I.E. Quantitative comparison of excited state properties and intensity-dependent photo-sensitization by rose bengal. J. Photochem. Photobiol. B. 33, 245-254 (1996). (Pubitemid 26188946)
    • (1996) Journal of Photochemistry and Photobiology B: Biology , vol.33 , Issue.3 , pp. 245-254
    • Stiel, H.1    Teuchner, K.2    Paul, A.3    Leupold, D.4    Kochevar, I.E.5
  • 70
    • 79959546978 scopus 로고    scopus 로고
    • Recording the instrument response function of a multiphoton FLIM system
    • Becker, W. Recording the instrument response function of a multiphoton FLIM system. Application Notes (2007).
    • (2007) Application Notes
    • Becker, W.1
  • 71
    • 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. & Piston, D.W. An improved cyan fuorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449 (2004). (Pubitemid 38451376)
    • (2004) Nature Biotechnology , vol.22 , Issue.4 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 73
    • 25844499242 scopus 로고    scopus 로고
    • Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer
    • DOI 10.1529/biophysj.105.061853
    • Thaler, C., Koushik, S.V., Blank, P.S. & Vogel, S.S. Quantitative multiphoton spectral imaging and its use for measuring resonance energy transfer. Biophys. J. 89, 2736-2749 (2005). (Pubitemid 41401063)
    • (2005) Biophysical Journal , vol.89 , Issue.4 , pp. 2736-2749
    • Thaler, C.1    Koushik, S.V.2    Blank, P.S.3    Vogel, S.S.4
  • 74
    • 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. et al. A variant of yellow fuorescent protein with fast and effcient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90 (2002). (Pubitemid 34044921)
    • (2002) Nature Biotechnology , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 75
    • 0033200389 scopus 로고    scopus 로고
    • Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation
    • DOI 10.1101/gad.13.17.2231
    • Tang, Q.Q. & Lane, M.D. Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation. Genes Dev. 13, 2231-2241 (1999). (Pubitemid 29426728)
    • (1999) Genes and Development , vol.13 , Issue.17 , pp. 2231-2241
    • Tang, Q.-Q.1    Lane, M.D.2
  • 76
    • 0037317399 scopus 로고    scopus 로고
    • A PIT-1 homeodomain mutant blocks the intranuclear recruitment of the CCAAT/enhancer binding protein α required for prolactin gene transcription
    • DOI 10.1210/me.2001-0222
    • Enwright, J.F. III., Kawecki-Crook, M.A., Voss, T.C., Schaufele, F. & Day, R.N. A PIT-1 homeodomain mutant blocks the intranuclear recruitment of the CCAAT/enhancer binding protein alpha required for prolactin gene transcription. Mol. Endocrinol. 17, 209-222 (2003). (Pubitemid 36183145)
    • (2003) Molecular Endocrinology , vol.17 , Issue.2 , pp. 209-222
    • Enwright III, J.F.1    Kawecki-Crook, M.A.2    Voss, T.C.3    Schaufele, F.4    Day, R.N.5
  • 79
    • 80052415416 scopus 로고    scopus 로고
    • Time-correlated single photon counting (TCSPC) FLIM-FRET microscopy for protein localization
    • eds. Periasamy, A. & Day, R.N. Oxford University Press
    • Chen, Y. & Periasamy, A. Time-correlated single photon counting (TCSPC) FLIM-FRET microscopy for protein localization. In Molecular Imaging: FRET Microscopy and Spectroscopy (eds. Periasamy, A. & Day, R.N.) 239-259 (Oxford University Press, 2005).
    • (2005) Molecular Imaging: FRET Microscopy and Spectroscopy , pp. 239-259
    • Chen, Y.1    Periasamy, A.2
  • 80
    • 77956641670 scopus 로고    scopus 로고
    • Additional correction for energy transfer effciency calculation in flter-based Forster resonance energy transfer microscopy for more accurate results
    • Sun, Y. & Periasamy, A. Additional correction for energy transfer effciency calculation in flter-based Forster resonance energy transfer microscopy for more accurate results. J. Biomed. Opt. 15, 020513 (2010)
    • (2010) J. Biomed. Opt. , vol.15 , pp. 020513
    • Sun, Y.1    Periasamy, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.