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Volumn 89, Issue , 2008, Pages 541-568

Chapter 21 Quantitative Fluorescence Lifetime Imaging in Cells as a Tool to Design Computational Models of Ran-Regulated Reaction Networks

Author keywords

[No Author keywords available]

Indexed keywords

KARYOPHERIN BETA; RAN PROTEIN;

EID: 57949089859     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(08)00621-3     Document Type: Review
Times cited : (3)

References (68)
  • 1
    • 33745075591 scopus 로고    scopus 로고
    • Tools for kinetic modeling of biochemical networks
    • Alves R., Antunes F., and Salvador A. Tools for kinetic modeling of biochemical networks. Nat. Biotechnol. 24 (2006) 667-672
    • (2006) Nat. Biotechnol. , vol.24 , pp. 667-672
    • Alves, R.1    Antunes, F.2    Salvador, A.3
  • 2
    • 27744475701 scopus 로고    scopus 로고
    • Anomalous diffusion of proteins due to molecular crowding
    • Banks D., and Fradin C. Anomalous diffusion of proteins due to molecular crowding. Biophys. J. 89 (2005) 2960-2971
    • (2005) Biophys. J. , vol.89 , pp. 2960-2971
    • Banks, D.1    Fradin, C.2
  • 5
    • 0035900714 scopus 로고    scopus 로고
    • Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks
    • Beresford P., Zhang D., Oh D., Fan Z., Greer E., Russo M., Jaju M., and Lieberman J. Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks. J. Biol. Chem. 276 (2001) 43285-43293
    • (2001) J. Biol. Chem. , vol.276 , pp. 43285-43293
    • Beresford, P.1    Zhang, D.2    Oh, D.3    Fan, Z.4    Greer, E.5    Russo, M.6    Jaju, M.7    Lieberman, J.8
  • 6
    • 25444510346 scopus 로고    scopus 로고
    • Metabolic mapping of MCF10A human breast cells via multiphoton fluorescence lifetime imaging of the coenzyme NADH
    • Bird D.K., Yan L., Vrotsos K.M., Eliceiri K.W., Vaughan E.M., Keely P.J., White J.G., and Ramanujam N. Metabolic mapping of MCF10A human breast cells via multiphoton fluorescence lifetime imaging of the coenzyme NADH. Cancer Res. 65 (2005) 8766-8773
    • (2005) Cancer Res. , vol.65 , pp. 8766-8773
    • Bird, D.K.1    Yan, L.2    Vrotsos, K.M.3    Eliceiri, K.W.4    Vaughan, E.M.5    Keely, P.J.6    White, J.G.7    Ramanujam, N.8
  • 7
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante C., Marko J., Siggia E., and Smith S. Entropic elasticity of lambda-phage DNA. Science 265 (1994) 1599-1600
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.2    Siggia, E.3    Smith, S.4
  • 8
    • 23944436962 scopus 로고    scopus 로고
    • Spatial coordination of spindle assembly by chromosome-mediated signaling gradients
    • Caudron M., Bunt G., Bastiaens P., and Karsenti E. Spatial coordination of spindle assembly by chromosome-mediated signaling gradients. Science 309 (2005) 1373-1376
    • (2005) Science , vol.309 , pp. 1373-1376
    • Caudron, M.1    Bunt, G.2    Bastiaens, P.3    Karsenti, E.4
  • 9
    • 33750933474 scopus 로고    scopus 로고
    • Spectrally resolved time-correlated single photon counting: A novel approach for characterization of endogenous fluorescence in isolated cardiac myocytes
    • Chorvat Jr. D., and Chorvatova A. Spectrally resolved time-correlated single photon counting: A novel approach for characterization of endogenous fluorescence in isolated cardiac myocytes. Eur. Biophys. J. 36 (2006) 73-83
    • (2006) Eur. Biophys. J. , vol.36 , pp. 73-83
    • Chorvat Jr., D.1    Chorvatova, A.2
  • 10
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani G., Petosa C., Weis K., and Muller C.W. Structure of importin-beta bound to the IBB domain of importin-alpha. Nature 399 (1999) 221-229
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 12
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk W., Strickler J.H., and Webb W.W. Two-photon laser scanning fluorescence microscopy. Science 248 (1990) 73-76
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 13
    • 0030993430 scopus 로고    scopus 로고
    • Photon upmanship: Why multiphoton imaging is more than a gimmick
    • Denk W., and Svoboda K. Photon upmanship: Why multiphoton imaging is more than a gimmick. Neuron 18 (1997) 351-357
    • (1997) Neuron , vol.18 , pp. 351-357
    • Denk, W.1    Svoboda, K.2
  • 15
    • 33750728028 scopus 로고    scopus 로고
    • Quantitative understanding of the energy transfer between fluorescent proteins connected via flexible peptide linkers
    • Evers T.H., van Dongen E.M., Faesen A.C., Meijer E.W., and Merkx M. Quantitative understanding of the energy transfer between fluorescent proteins connected via flexible peptide linkers. Biochemistry 45 (2006) 13183-13192
    • (2006) Biochemistry , vol.45 , pp. 13183-13192
    • Evers, T.H.1    van Dongen, E.M.2    Faesen, A.C.3    Meijer, E.W.4    Merkx, M.5
  • 16
    • 34250965243 scopus 로고
    • Energiewanderung und Fluoreszenz
    • Förster T. Energiewanderung und Fluoreszenz. Naturwissenschaften 6 (1946) 166-175
    • (1946) Naturwissenschaften , vol.6 , pp. 166-175
    • Förster, T.1
  • 17
    • 84981779372 scopus 로고
    • Zwischenmoleculare Energiewanderung und Fluoreszenz (Inter-molecular energy migration and fluorescence)
    • Förster T. Zwischenmoleculare Energiewanderung und Fluoreszenz (Inter-molecular energy migration and fluorescence). Annalen der Physik 2 (1948) 55-75
    • (1948) Annalen der Physik , vol.2 , pp. 55-75
    • Förster, T.1
  • 18
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP
    • Ganesan S., Ameer-Beg S.M., Ng T.T., Vojnovic B., and Wouters F.S. A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. USA 103 (2006) 4089-4094
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 19
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans B.N., Adams S.R., Ellisman M.H., and Tsien R.Y. The fluorescent toolbox for assessing protein location and function. Science 312 (2006) 217-224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 20
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon G.W., Berry G., Liang X.H., Levine B., and Herman B. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74 (1998) 2702-2713
    • (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
  • 21
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • Gorlich D., Seewald M.J., and Ribbeck K. Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J. 22 (2003) 1088-1100
    • (2003) EMBO J. , vol.22 , pp. 1088-1100
    • Gorlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 22
    • 4644233153 scopus 로고    scopus 로고
    • The mechanism of spindle assembly: Functions of Ran and its target TPX2
    • Gruss O.J., and Vernos I. The mechanism of spindle assembly: Functions of Ran and its target TPX2. J. Cell Biol. 166 (2004) 949-955
    • (2004) J. Cell Biol. , vol.166 , pp. 949-955
    • Gruss, O.J.1    Vernos, I.2
  • 23
    • 0036802885 scopus 로고    scopus 로고
    • New developments in multiphoton microscopy
    • Helmchen F., and Denk W. New developments in multiphoton microscopy. Curr. Opin. Neurobiol. 12 (2002) 593-601
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 593-601
    • Helmchen, F.1    Denk, W.2
  • 24
    • 0036306726 scopus 로고    scopus 로고
    • The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly
    • Hetzer M., Gruss O.J., and Mattaj I.W. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nat. Cell Biol. 4 (2002) E177-E184
    • (2002) Nat. Cell Biol. , vol.4
    • Hetzer, M.1    Gruss, O.J.2    Mattaj, I.W.3
  • 25
    • 33947500247 scopus 로고    scopus 로고
    • Chemical tools for biomolecular imaging
    • Johnsson N., and Johnsson K. Chemical tools for biomolecular imaging. ACS Chem. Biol. 2 (2007) 31-38
    • (2007) ACS Chem. Biol. , vol.2 , pp. 31-38
    • Johnsson, N.1    Johnsson, K.2
  • 26
    • 19744365121 scopus 로고    scopus 로고
    • The photophysics of green fluorescent protein: Influence of the key amino acids at positions 65, 203, and 222
    • Jung G., Wiehler J., and Zumbusch A. The photophysics of green fluorescent protein: Influence of the key amino acids at positions 65, 203, and 222. Biophys. J. 88 (2005) 1932-1947
    • (2005) Biophys. J. , vol.88 , pp. 1932-1947
    • Jung, G.1    Wiehler, J.2    Zumbusch, A.3
  • 27
    • 33750324246 scopus 로고    scopus 로고
    • FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids
    • Kajihara D., Abe R., Iijima I., Komiyama C., Sisido M., and Hohsaka T. FRET analysis of protein conformational change through position-specific incorporation of fluorescent amino acids. Nat. Methods 3 (2006) 923-929
    • (2006) Nat. Methods , vol.3 , pp. 923-929
    • Kajihara, D.1    Abe, R.2    Iijima, I.3    Komiyama, C.4    Sisido, M.5    Hohsaka, T.6
  • 28
    • 46249113438 scopus 로고    scopus 로고
    • The RanGTP gradient - A GPS for the mitotic spindle
    • Kalab P., and Heald R. The RanGTP gradient - A GPS for the mitotic spindle. J. Cell Sci. 121 (2008) 1577-1586
    • (2008) J. Cell Sci. , vol.121 , pp. 1577-1586
    • Kalab, P.1    Heald, R.2
  • 29
    • 33645452992 scopus 로고    scopus 로고
    • Analysis of a RanGTP-regulated gradient in mitotic somatic cells
    • Kalab P., Pralle A., Isacoff E.Y., Heald R., and Weis K. Analysis of a RanGTP-regulated gradient in mitotic somatic cells. Nature 440 (2006) 697-701
    • (2006) Nature , vol.440 , pp. 697-701
    • Kalab, P.1    Pralle, A.2    Isacoff, E.Y.3    Heald, R.4    Weis, K.5
  • 30
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • Kalab P., Weis K., and Heald R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science 295 (2002) 2452-2456
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 31
    • 0037079054 scopus 로고    scopus 로고
    • Computational systems biology
    • Kitano H. Computational systems biology. Nature 420 (2002) 206-210
    • (2002) Nature , vol.420 , pp. 206-210
    • Kitano, H.1
  • 32
    • 33747566427 scopus 로고
    • How many photons are necessary for fluorescence-lifetime measurements
    • Kollner M., and Wolfrum J. How many photons are necessary for fluorescence-lifetime measurements. Chem. Phys. Lett. 200 (1992) 199-204
    • (1992) Chem. Phys. Lett. , vol.200 , pp. 199-204
    • Kollner, M.1    Wolfrum, J.2
  • 35
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein
    • Mitra R.D., Silva C.M., and Youvan D.C. Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene 173 (1996) 13-17
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 37
    • 27144515959 scopus 로고    scopus 로고
    • Cell and tissue autofluorescence research and diagnostic applications
    • Monici M. Cell and tissue autofluorescence research and diagnostic applications. Biotechnol. Annu. Rev. 11 (2005) 227-256
    • (2005) Biotechnol. Annu. Rev. , vol.11 , pp. 227-256
    • Monici, M.1
  • 38
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen A.W., and Daugherty P.S. Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23 (2005) 355-360
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 39
    • 1642322097 scopus 로고    scopus 로고
    • Stathmin-tubulin interaction gradients in motile and mitotic cells
    • Niethammer P., Bastiaens P., and Karsenti E. Stathmin-tubulin interaction gradients in motile and mitotic cells. Science 303 (2004) 1862-1866
    • (2004) Science , vol.303 , pp. 1862-1866
    • Niethammer, P.1    Bastiaens, P.2    Karsenti, E.3
  • 40
    • 34250885891 scopus 로고    scopus 로고
    • An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins
    • Ohashi T., Galiacy S.D., Briscoe G., and Erickson H.P. An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins. Protein Sci. 16 (2007) 1429-1438
    • (2007) Protein Sci. , vol.16 , pp. 1429-1438
    • Ohashi, T.1    Galiacy, S.D.2    Briscoe, G.3    Erickson, H.P.4
  • 42
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton L.F., and Paschal B.M. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6 (2005) 187-198
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 43
    • 21244478918 scopus 로고    scopus 로고
    • Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions
    • Peter M., Ameer-Beg S.M., Hughes M.K., Keppler M.D., Prag S., Marsh M., Vojnovic B., and Ng T. Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions. Biophys. J. 88 (2005) 1224-1237
    • (2005) Biophys. J. , vol.88 , pp. 1224-1237
    • Peter, M.1    Ameer-Beg, S.M.2    Hughes, M.K.3    Keppler, M.D.4    Prag, S.5    Marsh, M.6    Vojnovic, B.7    Ng, T.8
  • 44
    • 33747624926 scopus 로고    scopus 로고
    • High-throughput fluorescence microscopy for systems biology
    • Pepperkok R., and Ellenberg J. High-throughput fluorescence microscopy for systems biology. Nat. Rev. Mol. Cell Biol. 7 (2006) 690-696
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 690-696
    • Pepperkok, R.1    Ellenberg, J.2
  • 45
    • 38949147878 scopus 로고    scopus 로고
    • Precise measurement of diffusion coefficients using scanning fluorescence correlation spectroscopy
    • Petrasek Z., and Schwille P. Precise measurement of diffusion coefficients using scanning fluorescence correlation spectroscopy. Biophys. J. 94 (2007) 1437-1448
    • (2007) Biophys. J. , vol.94 , pp. 1437-1448
    • Petrasek, Z.1    Schwille, P.2
  • 46
    • 0037313033 scopus 로고    scopus 로고
    • Theoretical investigation of the signal-to-noise ratio in fluorescence lifetime imaging
    • Philip J., and Carlsson K. Theoretical investigation of the signal-to-noise ratio in fluorescence lifetime imaging. J. Opt. Soc. Am. A Opt. Image Sci. Vis. 20 (2003) 368-379
    • (2003) J. Opt. Soc. Am. A Opt. Image Sci. Vis. , vol.20 , pp. 368-379
    • Philip, J.1    Carlsson, K.2
  • 47
    • 34547448862 scopus 로고    scopus 로고
    • Fluorescent proteins: Maturation, photochemistry and photophysics
    • Remington S.J. Fluorescent proteins: Maturation, photochemistry and photophysics. Curr. Opin. Struct. Biol. 16 (2006) 714-721
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 714-721
    • Remington, S.J.1
  • 48
    • 16844374515 scopus 로고    scopus 로고
    • A systems analysis of importin-α-β mediated nuclear protein import
    • Riddick G., and Macara I.G. A systems analysis of importin-α-β mediated nuclear protein import. J. Cell Biol. 168 (2005) 1027-1038
    • (2005) J. Cell Biol. , vol.168 , pp. 1027-1038
    • Riddick, G.1    Macara, I.G.2
  • 49
  • 50
    • 33846026713 scopus 로고    scopus 로고
    • Multiple diffusion mechanisms due to nanostructuring in crowded environments
    • Sanabria H., Kubota Y., and Waxham M. Multiple diffusion mechanisms due to nanostructuring in crowded environments. Biophys. J. 92 (2007) 313-322
    • (2007) Biophys. J. , vol.92 , pp. 313-322
    • Sanabria, H.1    Kubota, Y.2    Waxham, M.3
  • 51
    • 33646893036 scopus 로고    scopus 로고
    • Concatenation of cyan and yellow fluorescent proteins for efficient resonance energy transfer
    • Shimozono S., Hosoi H., Mizuno H., Fukano T., Tahara T., and Miyawaki A. Concatenation of cyan and yellow fluorescent proteins for efficient resonance energy transfer. Biochemistry 45 (2006) 6267-6271
    • (2006) Biochemistry , vol.45 , pp. 6267-6271
    • Shimozono, S.1    Hosoi, H.2    Mizuno, H.3    Fukano, T.4    Tahara, T.5    Miyawaki, A.6
  • 54
    • 34250214344 scopus 로고    scopus 로고
    • In vivo multiphoton fluorescence lifetime imaging of protein-bound and free nicotinamide adenine dinucleotide in normal and precancerous epithelia
    • 024014
    • Skala M.C., Riching K.M., Bird D.K., Gendron-Fitzpatrick A., Eickhoff J., Eliceiri K.W., Keely P.J., and Ramanujam N. In vivo multiphoton fluorescence lifetime imaging of protein-bound and free nicotinamide adenine dinucleotide in normal and precancerous epithelia. J. Biomed. Opt. 12 (2007) 024014
    • (2007) J. Biomed. Opt. , vol.12
    • Skala, M.C.1    Riching, K.M.2    Bird, D.K.3    Gendron-Fitzpatrick, A.4    Eickhoff, J.5    Eliceiri, K.W.6    Keely, P.J.7    Ramanujam, N.8
  • 57
    • 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
    • Tramier M., Zahid M., Mevel J.C., Masse M.J., and Coppey-Moisan M. 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 (2006) 933-939
    • (2006) Microsc. Res. Tech. , vol.69 , pp. 933-939
    • Tramier, M.1    Zahid, M.2    Mevel, J.C.3    Masse, M.J.4    Coppey-Moisan, M.5
  • 58
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67 (1998) 509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 59
    • 23044431625 scopus 로고    scopus 로고
    • Breeding molecules to spy on cells
    • Tsien R.Y. Breeding molecules to spy on cells. Harvey Lect. 99 (2003) 77-93
    • (2003) Harvey Lect. , vol.99 , pp. 77-93
    • Tsien, R.Y.1
  • 60
    • 34247126936 scopus 로고    scopus 로고
    • Breeding and building molecules to spy on cells and tumors
    • Tsien R.Y. Breeding and building molecules to spy on cells and tumors. Keio J. Med. 55 (2006) 127-140
    • (2006) Keio J. Med. , vol.55 , pp. 127-140
    • Tsien, R.Y.1
  • 63
    • 0036164351 scopus 로고    scopus 로고
    • Solute and macromolecule diffusion in cellular aqueous compartments
    • Verkman A. Solute and macromolecule diffusion in cellular aqueous compartments. Trends Biochem. Sci. 27 (2002) 27-33
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 27-33
    • Verkman, A.1
  • 64
    • 34347251261 scopus 로고    scopus 로고
    • Evolving proteins in mammalian cells using somatic hypermutation
    • Wang L., and Tsien R.Y. Evolving proteins in mammalian cells using somatic hypermutation. Nat. Protoc. 1 (2006) 1346-1350
    • (2006) Nat. Protoc. , vol.1 , pp. 1346-1350
    • Wang, L.1    Tsien, R.Y.2
  • 65
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis K. Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle. Cell 112 (2003) 441-451
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 66
    • 33749054066 scopus 로고    scopus 로고
    • Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy
    • Yasuda R. Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy. Curr. Opin. Neurobiol. 16 (2006) 551-561
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 551-561
    • Yasuda, R.1
  • 67
    • 31544462618 scopus 로고    scopus 로고
    • Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging
    • Yasuda R., Harvey C.D., Zhong H., Sobczyk A., van Aelst L., and Svoboda K. Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging. Nat. Neurosci. 9 (2006) 283-291
    • (2006) Nat. Neurosci. , vol.9 , pp. 283-291
    • Yasuda, R.1    Harvey, C.D.2    Zhong, H.3    Sobczyk, A.4    van Aelst, L.5    Svoboda, K.6
  • 68
    • 33644623648 scopus 로고    scopus 로고
    • Molecular biology and mutation of green fluorescent protein
    • Zacharias D.A., and Tsien R.Y. Molecular biology and mutation of green fluorescent protein. Methods Biochem. Anal. 47 (2006) 83-120
    • (2006) Methods Biochem. Anal. , vol.47 , pp. 83-120
    • Zacharias, D.A.1    Tsien, R.Y.2


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