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Volumn 8226, Issue , 2012, Pages

Dynamic nuclear protein interactions investigated using fluorescence lifetime and fluorescence fluctuation spectroscopy

Author keywords

fluorescence fluctuation spectroscopy (FFS); fluorescence lifetime imaging microscopy (FLIM); fluorescence resonance energy transfer (FRET) microscopy; fluorescent proteins (FPs); protein interactions

Indexed keywords

FLUORESCENCE FLUCTUATION SPECTROSCOPY; FLUORESCENCE LIFETIME IMAGING MICROSCOPY (FLIM); FLUORESCENCE RESONANCE ENERGY TRANSFER (FRET) MICROSCOPY; FLUORESCENT PROTEINS (FPS); PROTEIN INTERACTIONS;

EID: 84859611354     PISSN: 16057422     EISSN: None     Source Type: Conference Proceeding    
DOI: 10.1117/12.912883     Document Type: Conference Paper
Times cited : (3)

References (37)
  • 1
    • 70349515538 scopus 로고    scopus 로고
    • The fluorescent protein palette: Tools for cellular imaging
    • R. N. Day, and M. W. Davidson, "The fluorescent protein palette: tools for cellular imaging," Chem Soc Rev, 38(10), 2887-921 (2009).
    • (2009) Chem Soc Rev , vol.38 , Issue.10 , pp. 2887-2921
    • Day, R.N.1    Davidson, M.W.2
  • 2
    • 0036902813 scopus 로고    scopus 로고
    • Creating new fluorescent probes for cell biology
    • J. Zhang, R. E. Campbell, A. Y. Ting et al., "Creating new fluorescent probes for cell biology," Nat Rev Mol Cell Biol, 3(12), 906-18 (2002).
    • (2002) Nat Rev Mol Cell Biol , vol.3 , Issue.12 , pp. 906-918
    • Zhang, J.1    Campbell, R.E.2    Ting, A.Y.3
  • 3
    • 79959474049 scopus 로고    scopus 로고
    • Indicators based on fluorescence resonance energy transfer
    • ed. R Yuste, A Konnerth, Cold Spring Harbor, NY: CSHL Press
    • Tsien R.Y., "Indicators based on fluorescence resonance energy transfer." [Imaging in Neuroscience and Development] ed. R Yuste, A Konnerth, pp. 549-56. Cold Spring Harbor, NY: CSHL Press (2005).
    • (2005) Imaging in Neuroscience and Development , pp. 549-556
    • Tsien, R.Y.1
  • 4
    • 33749054066 scopus 로고    scopus 로고
    • Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy
    • R. Yasuda, "Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy," Curr Opin Neurobiol, 16(5), 551-61 (2006).
    • (2006) Curr Opin Neurobiol , vol.16 , Issue.5 , pp. 551-561
    • Yasuda, R.1
  • 5
    • 79959458043 scopus 로고    scopus 로고
    • Development of probes for cellular functions using fluorescent proteins and fluorescence resonance energy transfer
    • A. Miyawaki, "Development of probes for cellular functions using fluorescent proteins and fluorescence resonance energy transfer," Annu Rev Biochem, 80, 357-73 (2011).
    • (2011) Annu Rev Biochem , vol.80 , pp. 357-373
    • Miyawaki, A.1
  • 6
    • 33745344683 scopus 로고    scopus 로고
    • Monitoring dynamic protein interactions with photoquenching FRET
    • I. A. Demarco, A. Periasamy, C. F. Booker et al., "Monitoring dynamic protein interactions with photoquenching FRET," Nat Methods, 3(7), 519-24 (2006).
    • (2006) Nat Methods , vol.3 , Issue.7 , pp. 519-524
    • Demarco, I.A.1    Periasamy, A.2    Booker, C.F.3
  • 7
    • 21644462493 scopus 로고    scopus 로고
    • Molecular stop signs: Regulation of cell-cycle arrest by C/EBP transcription factors
    • P. F. Johnson, "Molecular stop signs: regulation of cell-cycle arrest by C/EBP transcription factors," J Cell Sci, 118(Pt 12), 2545-55 (2005).
    • (2005) J Cell Sci , vol.118 , Issue.PART 12 , pp. 2545-2555
    • Johnson, P.F.1
  • 11
    • 0033533709 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
    • F. S. Wouters, and P. I. Bastiaens, "Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells," Curr Biol, 9(19), 1127-30 (1999).
    • (1999) Curr Biol , vol.9 , Issue.19 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 12
    • 77958163349 scopus 로고    scopus 로고
    • Three-color spectral FRET microscopy localizes three interacting proteins in living cells
    • Y. Sun, H. Wallrabe, C. F. Booker et al., "Three-color spectral FRET microscopy localizes three interacting proteins in living cells," Biophys J, 99(4), 1274-83 (2010).
    • (2010) Biophys J , vol.99 , Issue.4 , pp. 1274-1283
    • Sun, Y.1    Wallrabe, H.2    Booker, C.F.3
  • 13
    • 80052399465 scopus 로고    scopus 로고
    • Investigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopy
    • Y. Sun, R. N. Day, and A. Periasamy, "Investigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopy," Nat Protoc, 6(9), 1324-40 (2011).
    • (2011) Nat Protoc , vol.6 , Issue.9 , pp. 1324-1340
    • Sun, Y.1    Day, R.N.2    Periasamy, A.3
  • 14
    • 0036789423 scopus 로고    scopus 로고
    • Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy
    • S. T. Hess, and W. W. Webb, "Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy," Biophys J, 83(4), 2300-17 (2002).
    • (2002) Biophys J , vol.83 , Issue.4 , pp. 2300-2317
    • Hess, S.T.1    Webb, W.W.2
  • 15
    • 27744475701 scopus 로고    scopus 로고
    • Anomalous diffusion of proteins due to molecular crowding
    • D. S. Banks, and C. Fradin, "Anomalous diffusion of proteins due to molecular crowding," Biophys J, 89(5), 2960-71 (2005).
    • (2005) Biophys J , vol.89 , Issue.5 , pp. 2960-2971
    • Banks, D.S.1    Fradin, C.2
  • 16
    • 0344603641 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy
    • Y. Chen, J. D. Muller, P. T. So et al., "The photon counting histogram in fluorescence fluctuation spectroscopy," Biophys J, 77(1), 553-67 (1999).
    • (1999) Biophys J , vol.77 , Issue.1 , pp. 553-567
    • Chen, Y.1    Muller, J.D.2    So, P.T.3
  • 17
    • 80053345593 scopus 로고    scopus 로고
    • Native ligands change integrin sequestering but not oligomerization in raft-mimicking lipid mixtures
    • A. P. Siegel, A. Kimble-Hill, S. Garg et al., "Native ligands change integrin sequestering but not oligomerization in raft-mimicking lipid mixtures," Biophys J, 101(7), 1642-50 (2011).
    • (2011) Biophys J , vol.101 , Issue.7 , pp. 1642-1650
    • Siegel, A.P.1    Kimble-Hill, A.2    Garg, S.3
  • 18
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • T. Nagai, K. Ibata, E. S. Park et al., "A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications," Nat Biotechnol, 20(1), 87-90 (2002).
    • (2002) Nat Biotechnol , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3
  • 19
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • M. A. Rizzo, G. H. Springer, B. Granada et al., "An improved cyan fluorescent protein variant useful for FRET," Nat Biotechnol, 22(4), 445-9 (2004).
    • (2004) Nat Biotechnol , vol.22 , Issue.4 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3
  • 20
    • 79953186589 scopus 로고    scopus 로고
    • An improved cerulean fluorescent protein with enhanced brightness and reduced reversible photoswitching
    • M. L. Markwardt, G. J. Kremers, C. A. Kraft et al., "An improved cerulean fluorescent protein with enhanced brightness and reduced reversible photoswitching," PLoS One, 6(3), e17896 (2011).
    • (2011) PLoS One , vol.6 , Issue.3
    • Markwardt, M.L.1    Kremers, G.J.2    Kraft, C.A.3
  • 21
    • 77449139582 scopus 로고    scopus 로고
    • Bright cyan fluorescent protein variants identified by fluorescence lifetime screening
    • J. Goedhart, L. van Weeren, M. A. Hink et al., "Bright cyan fluorescent protein variants identified by fluorescence lifetime screening," Nat Methods, 7(2), 137-9 (2010).
    • (2010) Nat Methods , vol.7 , Issue.2 , pp. 137-139
    • Goedhart, J.1    Van Weeren, L.2    Hink, M.A.3
  • 22
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of bright monomeric orange and red fluorescent proteins
    • N. C. Shaner, M. Z. Lin, M. R. McKeown et al., "Improving the photostability of bright monomeric orange and red fluorescent proteins," Nat Methods, 5(6), 545-51 (2008).
    • (2008) Nat Methods , vol.5 , Issue.6 , pp. 545-551
    • Shaner, N.C.1    Lin, M.Z.2    McKeown, M.R.3
  • 23
    • 10744228652 scopus 로고    scopus 로고
    • Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin
    • A. Thiru, D. Nietlispach, H. R. Mott et al., "Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin," EMBO J, 23(3), 489-99 (2004).
    • (2004) EMBO J , vol.23 , Issue.3 , pp. 489-499
    • Thiru, A.1    Nietlispach, D.2    Mott, H.R.3
  • 24
    • 0024046156 scopus 로고
    • Isolation of a recombinant copy of the gene encoding C/EBP
    • W. H. Landschulz, P. F. Johnson, E. Y. Adashi et al., "Isolation of a recombinant copy of the gene encoding C/EBP," Genes Dev, 2(7), 786-800 (1988).
    • (1988) Genes Dev , vol.2 , Issue.7 , pp. 786-800
    • Landschulz, W.H.1    Johnson, P.F.2    Adashi, E.Y.3
  • 25
    • 0027168640 scopus 로고
    • GHF-1-promoter-targeted immortalization of a somatotropic progenitor cell results in dwarfism in transgenic mice
    • D. Lew, H. Brady, K. Klausing et al., "GHF-1-promoter-targeted immortalization of a somatotropic progenitor cell results in dwarfism in transgenic mice," Genes Dev, 7(4), 683-93 (1993).
    • (1993) Genes Dev , vol.7 , Issue.4 , pp. 683-693
    • Lew, D.1    Brady, H.2    Klausing, K.3
  • 26
    • 40649092856 scopus 로고    scopus 로고
    • A novel fluorescence lifetime imaging system that optimizes photon efficiency
    • R. A. Colyer, C. Lee, and E. Gratton, "A novel fluorescence lifetime imaging system that optimizes photon efficiency," Microsc Res Tech, 71(3), 201-13 (2008).
    • (2008) Microsc Res Tech , vol.71 , Issue.3 , pp. 201-213
    • Colyer, R.A.1    Lee, C.2    Gratton, E.3
  • 27
    • 29144446288 scopus 로고    scopus 로고
    • Polar plot representation for frequency-domain analysis of fluorescence lifetimes
    • G. I. Redford, and R. M. Clegg, "Polar plot representation for frequency-domain analysis of fluorescence lifetimes," J Fluoresc, 15(5), 805-15 (2005).
    • (2005) J Fluoresc , vol.15 , Issue.5 , pp. 805-815
    • Redford, G.I.1    Clegg, R.M.2
  • 28
    • 33845755946 scopus 로고    scopus 로고
    • Heterochromatin revisited
    • S. I. Grewal, and S. Jia, "Heterochromatin revisited," Nat Rev Genet, 8(1), 35-46 (2007).
    • (2007) Nat Rev Genet , vol.8 , Issue.1 , pp. 35-46
    • Grewal, S.I.1    Jia, S.2
  • 29
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • A. J. Bannister, P. Zegerman, J. F. Partridge et al., "Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain," Nature, 410(6824), 120-4 (2001).
    • (2001) Nature , vol.410 , Issue.6824 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3
  • 30
    • 1842733449 scopus 로고    scopus 로고
    • HP1 and the dynamics of heterochromatin maintenance
    • C. Maison, and G. Almouzni, "HP1 and the dynamics of heterochromatin maintenance," Nat Rev Mol Cell Biol, 5(4), 296-304 (2004).
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.4 , pp. 296-304
    • Maison, C.1    Almouzni, G.2
  • 31
    • 79952704960 scopus 로고    scopus 로고
    • The changing faces of HP1: From heterochromatin formation and gene silencing to euchromatic gene expression: HP1 acts as a positive regulator of transcription
    • S. H. Kwon, and J. L. Workman, "The changing faces of HP1: From heterochromatin formation and gene silencing to euchromatic gene expression: HP1 acts as a positive regulator of transcription," Bioessays, 33(4), 280-9 (2011).
    • (2011) Bioessays , vol.33 , Issue.4 , pp. 280-289
    • Kwon, S.H.1    Workman, J.L.2
  • 32
    • 0033200389 scopus 로고    scopus 로고
    • Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation
    • Q. Q. Tang, and M. D. Lane, "Activation and centromeric localization of CCAAT/enhancer-binding proteins during the mitotic clonal expansion of adipocyte differentiation," Genes Dev, 13(17), 2231-41 (1999).
    • (1999) Genes Dev , vol.13 , Issue.17 , pp. 2231-2241
    • Tang, Q.Q.1    Lane, M.D.2
  • 33
    • 0034802539 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus
    • R. N. Day, A. Periasamy, and F. Schaufele, "Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus," Methods, 25(1), 4-18 (2001).
    • (2001) Methods , vol.25 , Issue.1 , pp. 4-18
    • Day, R.N.1    Periasamy, A.2    Schaufele, F.3
  • 34
    • 10744228652 scopus 로고    scopus 로고
    • Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin
    • A. Thiru, D. Nietlispach, H. R. Mott et al., "Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin," EMBO J, 23(3), 489-99 (2004).
    • (2004) EMBO J , vol.23 , Issue.3 , pp. 489-499
    • Thiru, A.1    Nietlispach, D.2    Mott, H.R.3
  • 35
    • 0034599522 scopus 로고    scopus 로고
    • The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer
    • S. V. Brasher, B. O. Smith, R. H. Fogh et al., "The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer," EMBO J, 19(7), 1587-97 (2000).
    • (2000) EMBO J , vol.19 , Issue.7 , pp. 1587-1597
    • Brasher, S.V.1    Smith, B.O.2    Fogh, R.H.3
  • 36
    • 79955068697 scopus 로고    scopus 로고
    • The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners
    • D. L. Mendez, D. Kim, M. Chruszcz et al., "The HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners," Chembiochem, 12(7), 1084-96 (2011).
    • (2011) Chembiochem , vol.12 , Issue.7 , pp. 1084-1096
    • Mendez, D.L.1    Kim, D.2    Chruszcz, M.3
  • 37
    • 68949108727 scopus 로고    scopus 로고
    • Direct measurement of association and dissociation rates of DNA binding in live cells by fluorescence correlation spectroscopy
    • A. Michelman-Ribeiro, D. Mazza, T. Rosales et al., "Direct measurement of association and dissociation rates of DNA binding in live cells by fluorescence correlation spectroscopy," Biophys J, 97(1), 337-46 (2009).
    • (2009) Biophys J , vol.97 , Issue.1 , pp. 337-346
    • Michelman-Ribeiro, A.1    Mazza, D.2    Rosales, T.3


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