메뉴 건너뛰기




Volumn 3, Issue 2, 2009, Pages 107-113

Determination of supramolecular structure and spatial distribution of protein complexes in living cells

Author keywords

[No Author keywords available]

Indexed keywords

ACCEPTOR MOLECULES; DETERMINATION OF PROTEINS; EMISSION WAVELENGTH; EXCITATION WAVELENGTH; MOLECULAR COMPLEXES; PROTEIN COMPLEXES; RESONANT ENERGY TRANSFER; SUPRAMOLECULAR STRUCTURE;

EID: 59349092419     PISSN: 17494885     EISSN: 17494893     Source Type: Journal    
DOI: 10.1038/nphoton.2008.291     Document Type: Article
Times cited : (94)

References (49)
  • 1
    • 48449100036 scopus 로고    scopus 로고
    • Detection of heteromerization of more than two proteins by sequential BRET-FRET
    • Carriba, P. et al. Detection of heteromerization of more than two proteins by sequential BRET-FRET. Nature Methods 5, 727-733 (2008).
    • (2008) Nature Methods , vol.5 , pp. 727-733
    • Carriba, P.1
  • 2
    • 38549167408 scopus 로고    scopus 로고
    • Subcellular imaging of dynamic protein interactions by bioluminescence resonance energy transfer
    • Coulon, V. et al. Subcellular imaging of dynamic protein interactions by bioluminescence resonance energy transfer. Biophys. J. 94, 1001-1009 (2008).
    • (2008) Biophys. J , vol.94 , pp. 1001-1009
    • Coulon, V.1
  • 3
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to GPCR oligomerization
    • Maurel, D. et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization. Nature Methods 5, 561-567 (2008).
    • (2008) Nature Methods , vol.5 , pp. 561-567
    • Maurel, D.1
  • 4
    • 38349191944 scopus 로고    scopus 로고
    • Visualization of AP-1 NF-kB ternary complexes in living cells by using a BiFC-based FRET
    • Shyu, Y. J., Suarez, C. D. & Hu, C. D. Visualization of AP-1 NF-kB ternary complexes in living cells by using a BiFC-based FRET. Proc. Natl Acad. Sci. USA 105, 151-156 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 151-156
    • Shyu, Y.J.1    Suarez, C.D.2    Hu, C.D.3
  • 5
    • 48849083814 scopus 로고    scopus 로고
    • Enhanced FRET contrast in lifetime imaging
    • Spriet, C. et al. Enhanced FRET contrast in lifetime imaging. Cytometry A 73, 745-753 (2008).
    • (2008) Cytometry A , vol.73 , pp. 745-753
    • Spriet, C.1
  • 6
    • 34548272472 scopus 로고    scopus 로고
    • Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions
    • 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).
    • (2007) J. Microsc , vol.228 , pp. 139-152
    • Chen, Y.1    Mauldin, J.P.2    Day, R.N.3    Periasamy, A.4
  • 7
    • 34547147089 scopus 로고    scopus 로고
    • Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues
    • Xu, X. et al. Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues. Proc. Natl Acad. Sci. USA 104, 10264-10269 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 10264-10269
    • Xu, X.1
  • 8
    • 33745344683 scopus 로고    scopus 로고
    • Monitoring dynamic protein interactions with photoquenching FRET
    • Demarco, I. A., Periasamy, A., Booker, C. F. & Day, R. N. Monitoring dynamic protein interactions with photoquenching FRET. Nature Methods 3, 519-524 (2006).
    • (2006) Nature Methods , vol.3 , pp. 519-524
    • Demarco, I.A.1    Periasamy, A.2    Booker, C.F.3    Day, R.N.4
  • 9
    • 33144473025 scopus 로고    scopus 로고
    • FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
    • Meyer, B. H. et al. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl Acad. Sci. USA 103, 2138-2143 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2138-2143
    • Meyer, B.H.1
  • 10
    • 33646343978 scopus 로고    scopus 로고
    • Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)
    • Pfleger, K. D. & Eidne, K. A. Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nature Methods 3, 165-174 (2006).
    • (2006) Nature Methods , vol.3 , pp. 165-174
    • Pfleger, K.D.1    Eidne, K.A.2
  • 11
    • 12744280975 scopus 로고    scopus 로고
    • Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer
    • Raicu, V., Jansma, D. B., Miller, R. J. & Friesen, J. D. Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer. Biochem. J. 385, 265-277 (2005).
    • (2005) Biochem. J , vol.385 , pp. 265-277
    • Raicu, V.1    Jansma, D.B.2    Miller, R.J.3    Friesen, J.D.4
  • 12
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe, H. & Periasamy, A. Imaging protein molecules using FRET and FLIM microscopy. Curr. Opin. Biotechnol. 16, 19-27 (2005).
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 13
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • An, S. J. & Almers, W. Tracking SNARE complex formation in live endocrine cells. Science 306, 1042-1046 (2004).
    • (2004) Science , vol.306 , pp. 1042-1046
    • An, S.J.1    Almers, W.2
  • 14
    • 0346307455 scopus 로고    scopus 로고
    • Characterization of two-photon excitation fluorescence lifetime imaging microscopy for protein localization
    • Chen, Y. & Periasamy, A. Characterization of two-photon excitation fluorescence lifetime imaging microscopy for protein localization. Microscopy Res. Tech. 63, 72-80 (2004).
    • (2004) Microscopy Res. Tech , vol.63 , pp. 72-80
    • Chen, Y.1    Periasamy, A.2
  • 15
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz, J. & Patterson, G. H. Development and use of fluorescent protein markers in living cells. Science 300, 87-91 (2003).
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 18
    • 0033823060 scopus 로고    scopus 로고
    • The renaissance of fluorescence resonance energy transfer
    • Selvin, P. R. The renaissance of fluorescence resonance energy transfer. Nat. Struct. Biol. 7, 730-734 (2000).
    • (2000) Nat. Struct. Biol , vol.7 , pp. 730-734
    • Selvin, P.R.1
  • 20
    • 40149099722 scopus 로고    scopus 로고
    • Efficiency of resonance energy transfer in homo-oligomeric complexes of proteins
    • Raicu, V. Efficiency of resonance energy transfer in homo-oligomeric complexes of proteins. J. Biol. Phys. 33, 109-127 (2007).
    • (2007) J. Biol. Phys , vol.33 , pp. 109-127
    • Raicu, V.1
  • 21
    • 0029057619 scopus 로고
    • Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy
    • Song, L., Hennink, E. J., Young, I. T. & Tanke, H. J. Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy. Biophys. J. 68, 2588-2600 (1995).
    • (1995) Biophys. J , vol.68 , pp. 2588-2600
    • Song, L.1    Hennink, E.J.2    Young, I.T.3    Tanke, H.J.4
  • 22
    • 0027500214 scopus 로고
    • Distribution of type I Fc-receptors on the surface of mast cells probed by fluorescence resonance energy transfer
    • Kubitscheck, U., Schweitzer-Stenner, R., Arndt-Jovin, D. J., Jovin, T. M. & Pecht, I. Distribution of type I Fc-receptors on the surface of mast cells probed by fluorescence resonance energy transfer. Biophys. J. 64, 110-120 (1993).
    • (1993) Biophys. J , vol.64 , pp. 110-120
    • Kubitscheck, U.1    Schweitzer-Stenner, R.2    Arndt-Jovin, D.J.3    Jovin, T.M.4    Pecht, I.5
  • 23
    • 38549181839 scopus 로고    scopus 로고
    • Analysis of FRET signals in the presence of free donors and acceptors
    • Wlodarczyk, J. et al. Analysis of FRET signals in the presence of free donors and acceptors. Biophys. J. 94, 986-1000 (2008).
    • (2008) Biophys. J , vol.94 , pp. 986-1000
    • Wlodarczyk, J.1
  • 24
    • 4344564695 scopus 로고    scopus 로고
    • Applying spectral fingerprinting to the analysis of FRET images
    • Neher, R. A. & Neher, E. Applying spectral fingerprinting to the analysis of FRET images. Microsc. Res. Tech. 64, 185-195 (2004).
    • (2004) Microsc. Res. Tech , vol.64 , pp. 185-195
    • Neher, R.A.1    Neher, E.2
  • 25
    • 0037032454 scopus 로고    scopus 로고
    • Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2-YFP FRET pair
    • Zimmermann, T., Rietdorf, J., Girod, A., Georget, V. & Pepperkok, R. Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2-YFP FRET pair. FEBS Lett. 531, 245-249 (2002).
    • (2002) FEBS Lett , vol.531 , pp. 245-249
    • Zimmermann, T.1    Rietdorf, J.2    Girod, A.3    Georget, V.4    Pepperkok, R.5
  • 26
    • 33846028172 scopus 로고    scopus 로고
    • Three-color alternating-laser excitation of single molecules: Monitoring multiple interactions and distances
    • Lee, N. K. et al. Three-color alternating-laser excitation of single molecules: monitoring multiple interactions and distances. Biophys. J. 92, 303-312 (2007).
    • (2007) Biophys. J , vol.92 , pp. 303-312
    • Lee, N.K.1
  • 27
    • 23244451444 scopus 로고    scopus 로고
    • Rapid analysis of Forster resonance energy transfer by two-color global fluorescence correlation spectroscopy: Trypsin proteinase reaction
    • Eggeling, C., Kask, P., Winkler, D. & Jager, S. Rapid analysis of Forster resonance energy transfer by two-color global fluorescence correlation spectroscopy: trypsin proteinase reaction. Biophys. J. 89, 605-618 (2005).
    • (2005) Biophys. J , vol.89 , pp. 605-618
    • Eggeling, C.1    Kask, P.2    Winkler, D.3    Jager, S.4
  • 28
    • 0034724192 scopus 로고    scopus 로고
    • Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET)
    • Angers, S. et al. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl Acad. Sci. USA 97, 3684-3689 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3684-3689
    • Angers, S.1
  • 29
    • 0033524455 scopus 로고    scopus 로고
    • A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins
    • Xu, Y., Piston, D. W. & Johnson, C. H. A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl Acad. Sci. USA 96, 151-156 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 151-156
    • Xu, Y.1    Piston, D.W.2    Johnson, C.H.3
  • 30
    • 34547619629 scopus 로고    scopus 로고
    • Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging
    • Hoshino, H., Nakajima, Y. & Ohmiya, Y. Luciferase-YFP fusion tag with enhanced emission for single-cell luminescence imaging. Nature Methods 4, 637-639 (2007).
    • (2007) Nature Methods , vol.4 , pp. 637-639
    • Hoshino, H.1    Nakajima, Y.2    Ohmiya, Y.3
  • 31
    • 84876604582 scopus 로고    scopus 로고
    • US patent application 11/904,860 2007
    • Raicu, V. & Fung, R. US patent application 11/904,860 (2007).
    • Raicu, V.1    Fung, R.2
  • 32
    • 0242353872 scopus 로고    scopus 로고
    • Nonlinear magic: Multiphoton microscopy in the biosciences
    • Zipfel, W. R, Williams, R. M. & Webb, W. W. Nonlinear magic: multiphoton microscopy in the biosciences. Nature Biotechnol 21, 1369-1377 (2003).
    • (2003) Nature Biotechnol , vol.21 , pp. 1369-1377
    • Zipfel, W.R.1    Williams, R.M.2    Webb, W.W.3
  • 33
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk, W., Strickler, J. H. & Webb, W. W. Two-photon laser scanning fluorescence microscopy. Science 248, 73-76 (1990).
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 34
    • 35548978682 scopus 로고    scopus 로고
    • A line-scanning semi-confocal multi-photon fluorescence microscope with a simultaneous broadband spectral acquisition and its application to the study of the thylakoid membrane of a cyanobacterium Anabaena PCC7120
    • Kumazaki, S. et al A line-scanning semi-confocal multi-photon fluorescence microscope with a simultaneous broadband spectral acquisition and its application to the study of the thylakoid membrane of a cyanobacterium Anabaena PCC7120. J. Microsc. 228, 240-254 (2007).
    • (2007) J. Microsc , vol.228 , pp. 240-254
    • Kumazaki, S.1
  • 35
    • 84876597499 scopus 로고    scopus 로고
    • Raicu, V., Fung, R., Melnichuk, M., Chaturvedi, A. & Gillman, D. in Proc. SPIE (eds Periasamy, A. & So, P. T. C.) 6442 M6441-6442 M6445 (SPIE, 2007).
    • Raicu, V., Fung, R., Melnichuk, M., Chaturvedi, A. & Gillman, D. in Proc. SPIE (eds Periasamy, A. & So, P. T. C.) 6442 M6441-6442 M6445 (SPIE, 2007).
  • 36
    • 0000791517 scopus 로고    scopus 로고
    • Femtosecond pulse shaping using spatial light modulators
    • Weiner, A. M. Femtosecond pulse shaping using spatial light modulators. Rev. Sci. Instrum. 71, 1929-1960 (2000).
    • (2000) Rev. Sci. Instrum , vol.71 , pp. 1929-1960
    • Weiner, A.M.1
  • 37
    • 42149192556 scopus 로고    scopus 로고
    • eds Periasamy, A. & So, P. T. C, SPIE
    • Raicu, V. et al. in Proc. SPIE (eds Periasamy, A. & So, P. T. C.) 686018 (SPIE, 2008).
    • (2008) Proc. SPIE , pp. 686018
    • Raicu, V.1
  • 38
  • 39
    • 29144466481 scopus 로고    scopus 로고
    • Oligomerization of G-protein-coupled receptors: Lessons from the yeast Saccharomyces cerevisiae
    • Overton, M. C., Chinault, S. L. & Blumer, K. J. Oligomerization of G-protein-coupled receptors: Lessons from the yeast Saccharomyces cerevisiae. Eukaryotic Cell 4, 1963-1970 (2005).
    • (2005) Eukaryotic Cell , vol.4 , pp. 1963-1970
    • Overton, M.C.1    Chinault, S.L.2    Blumer, K.J.3
  • 40
    • 3042541532 scopus 로고    scopus 로고
    • Multi-dimensional time-correlated single photon counting (TCSPC) fluorescence lifetime imaging microscopy (FLIM) to detect FRET in cells
    • Duncan, R. R., Bergmann, A., Cousin, M. A., Apps, D. K. & Shipston, M. J. Multi-dimensional time-correlated single photon counting (TCSPC) fluorescence lifetime imaging microscopy (FLIM) to detect FRET in cells. J. Microsc. 215, 1-12 (2004).
    • (2004) J. Microsc , vol.215 , pp. 1-12
    • Duncan, R.R.1    Bergmann, A.2    Cousin, M.A.3    Apps, D.K.4    Shipston, M.J.5
  • 41
    • 33751215258 scopus 로고    scopus 로고
    • A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer
    • James, J. R, Oliveira, M. I., Carmo, A. M., Iaboni, A. & Davis, S. J. A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer. Nature Methods 3, 1001-1006 (2006).
    • (2006) Nature Methods , vol.3 , pp. 1001-1006
    • James, J.R.1    Oliveira, M.I.2    Carmo, A.M.3    Iaboni, A.4    Davis, S.J.5
  • 42
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositolanchored protein at the apical surface of MDCK cells examined at a resolution of 〈 100 Åusing imaging fluorescence resonance energy transfer
    • Kenworthy, A. K. & Edidin, M. Distribution of a glycosylphosphatidylinositolanchored protein at the apical surface of MDCK cells examined at a resolution of 〈 100 Åusing imaging fluorescence resonance energy transfer. J. Cell Biol. 142, 69-84 (1998).
    • (1998) J. Cell Biol , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 43
    • 0018650688 scopus 로고
    • An analytic solution to the Forster Energy Transfer problem in two dimensions
    • Wolber, P. K. & Hudson, B. S. An analytic solution to the Forster Energy Transfer problem in two dimensions. Biophys. J. 28, 197-210 (1979).
    • (1979) Biophys. J , vol.28 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 44
    • 33646500642 scopus 로고    scopus 로고
    • Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: Regulation of receptor down-regulation by heterodimerization
    • Goin, J. C. & Nathanson, N. M. Quantitative analysis of muscarinic acetylcholine receptor homo- and heterodimerization in live cells: regulation of receptor down-regulation by heterodimerization. J. Biol. Chem. 281, 5416-5425 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 5416-5425
    • Goin, J.C.1    Nathanson, N.M.2
  • 45
    • 0037160105 scopus 로고    scopus 로고
    • Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer
    • Mercier, J. F., Salahpour, A., Angers, S., Breit, A. & Bouvier, M. Quantitative assessment of beta 1- and beta 2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 44925-44931 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 44925-44931
    • Mercier, J.F.1    Salahpour, A.2    Angers, S.3    Breit, A.4    Bouvier, M.5
  • 46
    • 0001366883 scopus 로고    scopus 로고
    • High-speed, two-photon scanning microscope
    • Kim, K. H., Buehler, C. & So, P. T. C. High-speed, two-photon scanning microscope. Appl. Opt. 38, 6004-6009 (1999).
    • (1999) Appl. Opt , vol.38 , pp. 6004-6009
    • Kim, K.H.1    Buehler, C.2    So, P.T.C.3
  • 47
    • 0036144866 scopus 로고    scopus 로고
    • Linker-mediated recombinational subcloning of large DNA fragments using yeast
    • Raymond, C. K., Sims, E. H. & Olson, M. V. Linker-mediated recombinational subcloning of large DNA fragments using yeast. Genome Res. 12, 190-197 (2002).
    • (2002) Genome Res , vol.12 , pp. 190-197
    • Raymond, C.K.1    Sims, E.H.2    Olson, M.V.3
  • 48
    • 0026637326 scopus 로고
    • Pheromone response in yeast
    • Kurjan, J. Pheromone response in yeast. Annu. Rev. Biochem. 61, 1097-1129 (1992).
    • (1992) Annu. Rev. Biochem , vol.61 , pp. 1097-1129
    • Kurjan, J.1
  • 49
    • 0033555524 scopus 로고    scopus 로고
    • A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G protein-coupled receptor
    • Stefan, C. J. & Blumer, K. J. A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G protein-coupled receptor. J. Biol. Chem. 274, 1835-1841 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 1835-1841
    • Stefan, C.J.1    Blumer, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.