메뉴 건너뛰기




Volumn 16, Issue 1 SPEC. ISS., 2005, Pages 19-27

Imaging protein molecules using FRET and FLIM microscopy

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY TRANSFER; FLUORESCENCE; MOLECULAR BIOLOGY; RESONANCE; THROUGHPUT;

EID: 13844297577     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2004.12.002     Document Type: Review
Times cited : (623)

References (65)
  • 1
    • 0037418906 scopus 로고    scopus 로고
    • Light microscopy techniques for live cell imaging
    • D.J. Stephens, and V.J. Allan Light microscopy techniques for live cell imaging Science 300 2003 82 86
    • (2003) Science , vol.300 , pp. 82-86
    • Stephens, D.J.1    Allan, V.J.2
  • 5
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • A. Miyawaki Visualization of the spatial and temporal dynamics of intracellular signaling Dev Cell 4 2003 295 305
    • (2003) Dev Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 6
    • 12244312784 scopus 로고    scopus 로고
    • Characterization of one- and two-photon excitation fluorescence resonance energy transfer microscopy
    • M. Elangovan, H. Wallrabe, Y. Chen, R.N. Day, M. Barroso, and A. Periasamy Characterization of one- and two-photon excitation fluorescence resonance energy transfer microscopy Methods 29 2003 58 73 Microscopy-based FRET imaging requires data analysis software to remove contamination from the FRET image. This paper describes a step-by-step algorithm to remove the SBT contamination in the FRET image collected using wide-field, confocal, and two-photon FRET microscopy systems.
    • (2003) Methods , vol.29 , pp. 58-73
    • Elangovan, M.1    Wallrabe, H.2    Chen, Y.3    Day, R.N.4    Barroso, M.5    Periasamy, A.6
  • 7
    • 0347756761 scopus 로고    scopus 로고
    • Protein localization in living cells and tissues using FRET and FLIM
    • Y. Chen, J.D. Mills, and A. Periasamy Protein localization in living cells and tissues using FRET and FLIM Differentiation 71 2003 528 541
    • (2003) Differentiation , vol.71 , pp. 528-541
    • Chen, Y.1    Mills, J.D.2    Periasamy, A.3
  • 8
    • 0037974186 scopus 로고    scopus 로고
    • Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes
    • H. Wallrabe, M. Elangovan, A. Burchard, A. Periasamy, and M. Barroso Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes Biophys J 85 2003 559 571 This paper describes the usage of confocal FRET microscopy for quantitative analysis of receptor clustering in the apical endocytic compartments in MDCK cells. Mathematical modelling was used to differentiate between clustered and random distributions of fluorophore-bound molecules on the basis of the dependence of FRET intensity on donor and acceptor concentrations.
    • (2003) Biophys J , vol.85 , pp. 559-571
    • Wallrabe, H.1    Elangovan, M.2    Burchard, A.3    Periasamy, A.4    Barroso, M.5
  • 9
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • R.B. Sekar, and A. Periasamy Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations J Cell Biol 160 2003 629 633
    • (2003) J Cell Biol , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 11
    • 0036164650 scopus 로고    scopus 로고
    • Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell
    • M. Elangovan, R.N. Day, and A. Periasamy Nanosecond fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy to localize the protein interactions in a single living cell J Microsc 205 2002 3 14
    • (2002) J Microsc , vol.205 , pp. 3-14
    • Elangovan, M.1    Day, R.N.2    Periasamy, A.3
  • 12
    • 0346307455 scopus 로고    scopus 로고
    • Characterization of two-photon excitation fluorescence lifetime imaging microscopy for protein localization
    • Y. Chen, and A. Periasamy Characterization of two-photon excitation fluorescence lifetime imaging microscopy for protein localization Microsc Res Tech 63 2004 72 80
    • (2004) Microsc Res Tech , vol.63 , pp. 72-80
    • Chen, Y.1    Periasamy, A.2
  • 13
    • 1842715882 scopus 로고    scopus 로고
    • Imaging molecular interactions by multiphoton FLIM
    • M. Peter, and S.M. Ameer-Beg Imaging molecular interactions by multiphoton FLIM Biol Cell 96 2004 231 236
    • (2004) Biol Cell , vol.96 , pp. 231-236
    • Peter, M.1    Ameer-Beg, S.M.2
  • 14
    • 0141644224 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer determinations using multiphoton fluorescence lifetime imaging microscopy to characterize amyloid-beta plaques
    • B.J. Bacskai, J. Skoch, G.A. Hickey, R. Allen, and B.T. Hyman Fluorescence resonance energy transfer determinations using multiphoton fluorescence lifetime imaging microscopy to characterize amyloid-beta plaques J Biomed Opt 8 2003 368 375
    • (2003) J Biomed Opt , vol.8 , pp. 368-375
    • Bacskai, B.J.1    Skoch, J.2    Hickey, G.A.3    Allen, R.4    Hyman, B.T.5
  • 15
    • 0141509840 scopus 로고    scopus 로고
    • Quantitative imaging of protein-protein interactions by multiphoton fluorescence lifetime imaging microscopy using a streak camera
    • R.V. Krishnan, A. Masuda, V.E. Centonze, and B. Herman Quantitative imaging of protein-protein interactions by multiphoton fluorescence lifetime imaging microscopy using a streak camera J Biomed Opt 8 2003 362 367
    • (2003) J Biomed Opt , vol.8 , pp. 362-367
    • Krishnan, R.V.1    Masuda, A.2    Centonze, V.E.3    Herman, B.4
  • 17
    • 0037340121 scopus 로고    scopus 로고
    • Imaging the localized protein interactions between Pit-1 and the CCAAT/enhancer binding protein α in the living pituitary cell nucleus
    • R.N. Day, T.C. Voss, J.F. Enwright III, C.F. Booker, A. Periasamy, and F. Schaufele Imaging the localized protein interactions between Pit-1 and the CCAAT/enhancer binding protein α in the living pituitary cell nucleus Mol Endocrinol 17 2003 333 345
    • (2003) Mol Endocrinol , vol.17 , pp. 333-345
    • Day, R.N.1    Voss, T.C.2    Enwright III, J.F.3    Booker, C.F.4    Periasamy, A.5    Schaufele, F.6
  • 20
    • 0037280108 scopus 로고    scopus 로고
    • Fluorescence lifetime-resolved imaging: Measuring lifetimes in an image
    • R.M. Clegg, O. Holub, and C. Gohlke Fluorescence lifetime-resolved imaging: measuring lifetimes in an image Methods Enzymol 360 2003 509 542
    • (2003) Methods Enzymol , vol.360 , pp. 509-542
    • Clegg, R.M.1    Holub, O.2    Gohlke, C.3
  • 21
    • 0036016786 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging in scanning microscopes: Acquisition speed, photon economy and lifetime resolution
    • H.C. Gerritsen, M.A. Asselbergs, A.V. Agronskaia, and W.G. Van Sark Fluorescence lifetime imaging in scanning microscopes: acquisition speed, photon economy and lifetime resolution J Microsc 206 2002 218 224
    • (2002) J Microsc , vol.206 , pp. 218-224
    • Gerritsen, H.C.1    Asselbergs, M.A.2    Agronskaia, A.V.3    Van Sark, W.G.4
  • 22
    • 0141644218 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging for the two-photon microscope: Time-domain and frequency-domain methods
    • E. Gratton, S. Breusegem, J. Sutin, Q. Ruan, and N. Barry Fluorescence lifetime imaging for the two-photon microscope: time-domain and frequency-domain methods J Biomed Opt 8 2003 381 390
    • (2003) J Biomed Opt , vol.8 , pp. 381-390
    • Gratton, E.1    Breusegem, S.2    Sutin, J.3    Ruan, Q.4    Barry, N.5
  • 24
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • L. Stryer Fluorescence energy transfer as a spectroscopic ruler Annu Rev Biochem 47 1978 819 846
    • (1978) Annu Rev Biochem , vol.47 , pp. 819-846
    • Stryer, L.1
  • 26
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • C. Berney, and G. Danuser FRET or no FRET: a quantitative comparison Biophys J 84 2003 3992 4010 This paper compares different FRET data analysis algorithms from the literature to remove the contamination in the FRET image.
    • (2003) Biophys J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 27
    • 70349374751 scopus 로고    scopus 로고
    • FRET data analysis: The algorithm
    • Edited by A Periasamy and RN Day. New York: Oxford University Press. Chapter 7: in press.
    • Chen Y, Elangovan M, Periasamy A: FRET data analysis: the algorithm. In Molecular Imaging: FRET Microscopy and Spectroscopy. Edited by A Periasamy and RN Day. New York: Oxford University Press. Chapter 7: in press. This book chapter describes an advanced level step-by-step algorithm for FRET data analysis including SBT and the back bleedthrough contamination correction in the FRET image. The detector spectral sensitivity correction for the donor and acceptor channels and their quantum yields are also included to estimate the efficiency and the distance. Moreover, this book has 16 chapters in total covering various FRET microscopy and spectroscopy basics and methodology of preparation of FRET assays for intensity-based FRET and lifetime FRET imaging techniques with interesting biological applications.
    • Molecular Imaging: FRET Microscopy and Spectroscopy
    • Chen, Y.1    Elangovan, M.2    Periasamy, A.3
  • 28
    • 13844304470 scopus 로고    scopus 로고
    • Photobleaching FRET microscopy
    • Edited by A Periasamy and R Day. New York: Oxford University Press. Chapter 8: in press.
    • Kenworthy AK: Photobleaching FRET microscopy. In Molecular Imaging: FRET Microscopy and Spectroscopy. Edited by A Periasamy and R Day. New York: Oxford University Press. Chapter 8: in press.
    • Molecular Imaging: FRET Microscopy and Spectroscopy
    • Kenworthy, A.K.1
  • 29
    • 0347064158 scopus 로고    scopus 로고
    • Assembly of α4β2 nicotinic acetylcholine receptors assessed with functional fluorescently labeled subunits: Effects of localization, trafficking, and nicotine-induced upregulation in clonal mammalian cells and in cultured midbrain neurons
    • R. Nashmi, M.E. Dickinson, S. McKinney, M. Jareb, C. Labarca, S.E. Fraser, and H.A. Lester Assembly of α4β2 nicotinic acetylcholine receptors assessed with functional fluorescently labeled subunits: effects of localization, trafficking, and nicotine-induced upregulation in clonal mammalian cells and in cultured midbrain neurons J Neurosci 23 2003 11554 11567
    • (2003) J Neurosci , vol.23 , pp. 11554-11567
    • Nashmi, R.1    Dickinson, M.E.2    McKinney, S.3    Jareb, M.4    Labarca, C.5    Fraser, S.E.6    Lester, H.A.7
  • 30
    • 13844279010 scopus 로고    scopus 로고
    • Time-correlated single photon counting (TCSPC) FLIM-FRET microscopy for protein localization
    • Edited by A Periasamy and RN Day. New York: Oxford University Press. Chapter 13: in press.
    • Chen Y, Periasamy A: Time-correlated single photon counting (TCSPC) FLIM-FRET microscopy for protein localization. In Molecular Imaging: FRET Microscopy and Spectroscopy. Edited by A Periasamy and RN Day. New York: Oxford University Press. Chapter 13: in press.
    • Molecular Imaging: FRET Microscopy and Spectroscopy
    • Chen, Y.1    Periasamy, A.2
  • 31
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • S. Hohng, C. Joo, and T. Ha Single-molecule three-color FRET Biophys J 87 2004 1328 1337 FRET has been demonstrated for two fluorophore models and this paper describes an estimation of more than one distance between donor and acceptor molecule using three spectrally distinct fluorophores for FRET.
    • (2004) Biophys J , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 32
  • 33
    • 0141530039 scopus 로고    scopus 로고
    • Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy
    • D.R. Larson, Y.M. Ma, V.M. Vogt, and W.W. Webb Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy J Cell Biol 162 2003 1233 1244
    • (2003) J Cell Biol , vol.162 , pp. 1233-1244
    • Larson, D.R.1    Ma, Y.M.2    Vogt, V.M.3    Webb, W.W.4
  • 34
    • 0346220020 scopus 로고    scopus 로고
    • Simultaneous DNA binding and bending by EcoRV endonuclease observed by real-time fluorescence
    • D.A. Hiller, J.M. Fogg, A.M. Martin, J.M. Beechem, N.O. Reich, and J.J. Perona Simultaneous DNA binding and bending by EcoRV endonuclease observed by real-time fluorescence Biochemistry 42 2003 14375 14385
    • (2003) Biochemistry , vol.42 , pp. 14375-14385
    • Hiller, D.A.1    Fogg, J.M.2    Martin, A.M.3    Beechem, J.M.4    Reich, N.O.5    Perona, J.J.6
  • 36
    • 0038664388 scopus 로고    scopus 로고
    • Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy
    • I. Riven, E. Kalmanzon, L. Segev, and E. Reuveny Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy Neuron 38 2003 225 235
    • (2003) Neuron , vol.38 , pp. 225-235
    • Riven, I.1    Kalmanzon, E.2    Segev, L.3    Reuveny, E.4
  • 39
    • 3242735110 scopus 로고    scopus 로고
    • Microscopic analysis of fluorescence resonance energy transfer (FRET)
    • B. Herman, R.V. Krishnan, and V.E. Centonze Microscopic analysis of fluorescence resonance energy transfer (FRET) Methods Mol Biol 261 2004 351 370
    • (2004) Methods Mol Biol , vol.261 , pp. 351-370
    • Herman, B.1    Krishnan, R.V.2    Centonze, V.E.3
  • 41
    • 0035430344 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein
    • F.K. Chan, R.M. Siegel, D. Zacharias, R. Swofford, K.L. Holmes, R.Y. Tsien, and M.J. Lenardo Fluorescence resonance energy transfer analysis of cell surface receptor interactions and signaling using spectral variants of the green fluorescent protein Cytometry 44 2001 361 368
    • (2001) Cytometry , vol.44 , pp. 361-368
    • Chan, F.K.1    Siegel, R.M.2    Zacharias, D.3    Swofford, R.4    Holmes, K.L.5    Tsien, R.Y.6    Lenardo, M.J.7
  • 42
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • J. Lippincott-Schwartz, and G.H. Patterson Development and use of fluorescent protein markers in living cells Science 300 2003 87 91
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 43
    • 0041837561 scopus 로고    scopus 로고
    • Lighting up cells: Labelling proteins with fluorophores
    • A. Miyawaki, A. Sawano, and T. Kogure Lighting up cells: labelling proteins with fluorophores Nat Cell Biol Suppl 2003 S1 S7
    • (2003) Nat Cell Biol
    • Miyawaki, A.1    Sawano, A.2    Kogure, T.3
  • 44
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • M.A. Rizzo, G.H. Springer, B. Granada, and D.W. Piston An improved cyan fluorescent protein variant useful for FRET Nat Biotechnol 22 2004 445 449
    • (2004) Nat Biotechnol , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 47
    • 1942445036 scopus 로고    scopus 로고
    • Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton
    • E. Butkevich, S. Hulsmann, D. Wenzel, T. Shirao, R. Duden, and I. Majoul Drebrin is a novel connexin-43 binding partner that links gap junctions to the submembrane cytoskeleton Curr Biol 14 2004 650 658
    • (2004) Curr Biol , vol.14 , pp. 650-658
    • Butkevich, E.1    Hulsmann, S.2    Wenzel, D.3    Shirao, T.4    Duden, R.5    Majoul, I.6
  • 48
    • 0037421222 scopus 로고    scopus 로고
    • Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy
    • S.F. Oliveria, L.L. Gomez, and M.L. Dell'Acqua Imaging kinase-AKAP79-phosphatase scaffold complexes at the plasma membrane in living cells using FRET microscopy J Cell Biol 160 2003 101 112
    • (2003) J Cell Biol , vol.160 , pp. 101-112
    • Oliveria, S.F.1    Gomez, L.L.2    Dell'Acqua, M.L.3
  • 49
    • 2542601493 scopus 로고    scopus 로고
    • A three-fluorophore FRET assay for high-throughput screening of small-molecule inhibitors of ribosome assembly
    • D. Klostermeier, P. Sears, C.H. Wong, D.P. Millar, and J.R. Williamson A three-fluorophore FRET assay for high-throughput screening of small-molecule inhibitors of ribosome assembly Nucleic Acids Res 32 2004 2707 2715
    • (2004) Nucleic Acids Res , vol.32 , pp. 2707-2715
    • Klostermeier, D.1    Sears, P.2    Wong, C.H.3    Millar, D.P.4    Williamson, J.R.5
  • 51
    • 0347364629 scopus 로고    scopus 로고
    • Gi protein activation in intact cells involves subunit rearrangement rather than dissociation
    • M. Bunemann, M. Frank, and M.J. Lohse Gi protein activation in intact cells involves subunit rearrangement rather than dissociation Proc Natl Acad Sci USA 100 2003 16077 16082
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 16077-16082
    • Bunemann, M.1    Frank, M.2    Lohse, M.J.3
  • 55
    • 2442681401 scopus 로고    scopus 로고
    • A high-throughput method for development of FRET-based indicators for proteolysis
    • T. Nagai, and A. Miyawaki A high-throughput method for development of FRET-based indicators for proteolysis Biochem Biophys Res Commun 319 2004 72 77
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 72-77
    • Nagai, T.1    Miyawaki, A.2
  • 58
    • 13844284976 scopus 로고    scopus 로고
    • Association of a model transmembrane peptide containing Gly in a heptad sequence motif
    • J.D. Lear, A. Stouffer, H. Gratkowski, V. Nanda, and W.F. DeGrado Association of a model transmembrane peptide containing Gly in a heptad sequence motif Biophys J 87 2004 3421 3429
    • (2004) Biophys J , vol.87 , pp. 3421-3429
    • Lear, J.D.1    Stouffer, A.2    Gratkowski, H.3    Nanda, V.4    Degrado, W.F.5
  • 60
    • 0141867742 scopus 로고    scopus 로고
    • One- and two-photon fluorescence resonance energy transfer microscopy to establish a clustered distribution of receptor-ligand complexes in endocytic membranes
    • H. Wallrabe, M. Stanley, A. Periasamy, and M. Barroso One- and two-photon fluorescence resonance energy transfer microscopy to establish a clustered distribution of receptor-ligand complexes in endocytic membranes J Biomed Opt 8 2003 339 346
    • (2003) J Biomed Opt , vol.8 , pp. 339-346
    • Wallrabe, H.1    Stanley, M.2    Periasamy, A.3    Barroso, M.4
  • 61
    • 3042730955 scopus 로고    scopus 로고
    • Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfer
    • B. Mueller, C.B. Karim, I.V. Negrashov, H. Kutchai, and D.D. Thomas Direct detection of phospholamban and sarcoplasmic reticulum Ca-ATPase interaction in membranes using fluorescence resonance energy transfer Biochemistry 43 2004 8754 8765
    • (2004) Biochemistry , vol.43 , pp. 8754-8765
    • Mueller, B.1    Karim, C.B.2    Negrashov, I.V.3    Kutchai, H.4    Thomas, D.D.5
  • 62
    • 4043050974 scopus 로고    scopus 로고
    • LTA 252G allele containing haplotype block is associated with high serum C-reactive protein levels
    • G. Suzuki, S. Izumi, M. Hakoda, and N. Takahashi LTA 252G allele containing haplotype block is associated with high serum C-reactive protein levels Atherosclerosis 176 2004 91 94
    • (2004) Atherosclerosis , vol.176 , pp. 91-94
    • Suzuki, G.1    Izumi, S.2    Hakoda, M.3    Takahashi, N.4
  • 63
    • 1842583796 scopus 로고    scopus 로고
    • Calcium activation of the Ca-ATPase enhances conformational heterogeneity between nucleotide binding and phosphorylation domains
    • B. Chen, T.C. Squier, and D.J. Bigelow Calcium activation of the Ca-ATPase enhances conformational heterogeneity between nucleotide binding and phosphorylation domains Biochemistry 43 2004 4366 4374
    • (2004) Biochemistry , vol.43 , pp. 4366-4374
    • Chen, B.1    Squier, T.C.2    Bigelow, D.J.3
  • 64
    • 1942519322 scopus 로고    scopus 로고
    • Conformation of prion protein repeat peptides probed by FRET measurements and molecular dynamics simulations
    • M. Gustiananda, J.R. Liggins, P.L. Cummins, and J.E. Gready Conformation of prion protein repeat peptides probed by FRET measurements and molecular dynamics simulations Biophys J 86 2004 2467 2483
    • (2004) Biophys J , vol.86 , pp. 2467-2483
    • Gustiananda, M.1    Liggins, J.R.2    Cummins, P.L.3    Gready, J.E.4
  • 65
    • 9644279587 scopus 로고    scopus 로고
    • In vivo HIV-1 Rev multimerization in the nucleolus and cytoplasm by fluorescence resonance energy transfer
    • D. Daelemans, S.V. Costes, E.H. Cho, R.A. Erwin-Cohen, S. Lockett, and G.N. Pavlakis In vivo HIV-1 Rev multimerization in the nucleolus and cytoplasm by fluorescence resonance energy transfer J Biol Chem 279 2004 50167 50175
    • (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    Lockett, S.5    Pavlakis, G.N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.