메뉴 건너뛰기




Volumn 7, Issue OCT, 2013, Pages

Application of FRET probes in the analysis of neuronal plasticity

Author keywords

Fluorescence lifetime imaging microscopy; F rster resonance energy transfer; Optical probes; Synaptic plasticity

Indexed keywords

GREEN FLUORESCENT PROTEIN;

EID: 84887002013     PISSN: 16625110     EISSN: None     Source Type: Journal    
DOI: 10.3389/fncir.2013.00163     Document Type: Review
Times cited : (23)

References (204)
  • 1
    • 0026029895 scopus 로고
    • Fluorescence ratio imaging of cyclic AMP in single cells
    • doi: 10.1038/349694a0
    • Adams, S. R., Harootunian, A. T., Buechler, Y. J., Taylor, S. S., and Tsien, R. Y. (1991). Fluorescence ratio imaging of cyclic AMP in single cells. Nature 349, 694-697. doi: 10.1038/349694a0
    • (1991) Nature , vol.349 , pp. 694-697
    • Adams, S.R.1    Harootunian, A.T.2    Buechler, Y.J.3    Taylor, S.S.4    Tsien, R.Y.5
  • 2
    • 84866531774 scopus 로고    scopus 로고
    • Imaging neural circuit dynamics with a voltage-sensitive fluorescent protein
    • doi: 10.1152/jn.00452.2012
    • Akemann, W., Mutoh, H., Perron, A., Park, Y. K., Iwamoto, Y., and Knöpfel, T. (2012). Imaging neural circuit dynamics with a voltage-sensitive fluorescent protein. J. Neurophysiol. 108, 2323-2337. doi: 10.1152/jn.00452.2012
    • (2012) J. Neurophysiol. , vol.108 , pp. 2323-2337
    • Akemann, W.1    Mutoh, H.2    Perron, A.3    Park, Y.K.4    Iwamoto, Y.5    Knöpfel, T.6
  • 3
    • 84880785785 scopus 로고    scopus 로고
    • Two-photon voltage imaging using a genetically encoded voltage indicator
    • doi: 10.1038/srep02231
    • Akemann, W., Sasaki, M., Mutoh, H., Imamura, T., Honkura, N., and Knopfel, T. (2013). Two-photon voltage imaging using a genetically encoded voltage indicator. Sci. Rep. 3, 2231. doi: 10.1038/srep02231
    • (2013) Sci. Rep. , vol.3 , pp. 2231
    • Akemann, W.1    Sasaki, M.2    Mutoh, H.3    Imamura, T.4    Honkura, N.5    Knopfel, T.6
  • 4
    • 0347683437 scopus 로고    scopus 로고
    • Spatio-temporal regulation of Rac1 and Cdc42 activity during nerve growth factor-induced neurite outgrowth in PC12 cells
    • doi: 10.1074/jbc.M306382200
    • Aoki, K., Nakamura, T., and Matsuda, M. (2004). Spatio-temporal regulation of Rac1 and Cdc42 activity during nerve growth factor-induced neurite outgrowth in PC12 cells. J. Biol. Chem. 279, 713-719. doi: 10.1074/jbc.M306382200
    • (2004) J. Biol. Chem. , vol.279 , pp. 713-719
    • Aoki, K.1    Nakamura, T.2    Matsuda, M.3
  • 5
    • 73949117548 scopus 로고    scopus 로고
    • PIP3 controls synaptic function by maintaining AMPA receptor clustering at the postsynaptic membrane
    • doi: 10.1038/nn.2462
    • Arendt, K. L., Royo, M., Fernandez-Monreal, M., Knafo, S., Petrok, C. N., Martens, J. R., et al. (2010). PIP3 controls synaptic function by maintaining AMPA receptor clustering at the postsynaptic membrane. Nat. Neurosci. 13, 36-44. doi: 10.1038/nn.2462
    • (2010) Nat. Neurosci. , vol.13 , pp. 36-44
    • Arendt, K.L.1    Royo, M.2    Fernandez-Monreal, M.3    Knafo, S.4    Petrok, C.N.5    Martens, J.R.6
  • 6
    • 33746216307 scopus 로고    scopus 로고
    • A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells
    • doi: 10.1002/anie.200503185
    • Awais, M., Sato, M., Lee, X., and Umezawa, Y. (2006). A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells. Angew. Chem. Int. Ed. Engl. 45, 2707-2712. doi: 10.1002/anie.200503185
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 2707-2712
    • Awais, M.1    Sato, M.2    Lee, X.3    Umezawa, Y.4
  • 7
    • 1942454742 scopus 로고    scopus 로고
    • A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells
    • doi: 10.1021/ac030410g
    • Awais, M., Sato, M., Sasaki, K., and Umezawa, Y. (2004). A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells. Anal. Chem. 76, 2181-2186. doi: 10.1021/ac030410g
    • (2004) Anal. Chem. , vol.76 , pp. 2181-2186
    • Awais, M.1    Sato, M.2    Sasaki, K.3    Umezawa, Y.4
  • 8
    • 35348981760 scopus 로고    scopus 로고
    • Optical probes to identify the glucocorticoid receptor ligands in living cells
    • doi: 10.1016/j.steroids.2007.08.006
    • Awais, M., Sato, M., and Umezawa, Y. (2007a). Optical probes to identify the glucocorticoid receptor ligands in living cells. Steroids 72, 949-954. doi: 10.1016/j.steroids.2007.08.006
    • (2007) Steroids , vol.72 , pp. 949-954
    • Awais, M.1    Sato, M.2    Umezawa, Y.3
  • 9
    • 34250860872 scopus 로고    scopus 로고
    • Imaging of selective nuclear receptor modulator-induced conformational changes in the nuclear receptor to allow interaction with coactivator and corepressor proteins in living cells
    • doi: 10.1002/cbic.200700001
    • Awais, M., Sato, M., and Umezawa, Y. (2007b). Imaging of selective nuclear receptor modulator-induced conformational changes in the nuclear receptor to allow interaction with coactivator and corepressor proteins in living cells. Chembiochem 8, 737-743. doi: 10.1002/cbic.200700001
    • (2007) Chembiochem , vol.8 , pp. 737-743
    • Awais, M.1    Sato, M.2    Umezawa, Y.3
  • 10
    • 0035976770 scopus 로고    scopus 로고
    • Novel green fluorescent protein-based ratiometric indicators for monitoring pH in defined intracellular microdomains
    • doi: 10.1006/bbrc.2001.6004
    • Awaji, T., Hirasawa, A., Shirakawa, H., Tsujimoto, G., and Miyazaki, S. (2001). Novel green fluorescent protein-based ratiometric indicators for monitoring pH in defined intracellular microdomains. Biochem. Biophys. Res. Commun. 289, 457-462. doi: 10.1006/bbrc.2001.6004
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 457-462
    • Awaji, T.1    Hirasawa, A.2    Shirakawa, H.3    Tsujimoto, G.4    Miyazaki, S.5
  • 11
    • 44149098577 scopus 로고    scopus 로고
    • Imaging synaptic inhibition in transgenic mice expressing the chloride indicator, Clomeleon
    • doi: 10.1007/s11068-008-9019-6
    • Berglund, K., Schleich, W., Krieger, P., Loo, L. S., Wang, D., Cant, N. B., et al. (2006). Imaging synaptic inhibition in transgenic mice expressing the chloride indicator, Clomeleon. Brain Cell Biol. 35, 207-228. doi: 10.1007/s11068-008-9019-6
    • (2006) Brain Cell Biol. , vol.35 , pp. 207-228
    • Berglund, K.1    Schleich, W.2    Krieger, P.3    Loo, L.S.4    Wang, D.5    Cant, N.B.6
  • 12
    • 84863462907 scopus 로고    scopus 로고
    • Structural plasticity of dendritic spines
    • doi: 10.1016/j.conb.2011.09.002
    • Bosch, M., and Hayashi, Y. (2012). Structural plasticity of dendritic spines. Curr. Opin. Neurobiol. 22, 383-388. doi: 10.1016/j.conb.2011.09.002
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 383-388
    • Bosch, M.1    Hayashi, Y.2
  • 13
    • 14844285356 scopus 로고    scopus 로고
    • Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cdelta in the intact cell
    • doi: 10.1074/jbc.M413896200
    • Braun, D. C., Garfield, S. H., and Blumberg, P. M. (2005). Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cdelta in the intact cell. J. Biol. Chem. 280, 8164-8171. doi: 10.1074/jbc.M413896200
    • (2005) J. Biol. Chem. , vol.280 , pp. 8164-8171
    • Braun, D.C.1    Garfield, S.H.2    Blumberg, P.M.3
  • 14
    • 37549060016 scopus 로고    scopus 로고
    • Spatial and temporal regulation of focal adhesion kinase activity in living cells
    • doi: 10.1128/MCB.01324-07
    • Cai, X., Lietha, D., Ceccarelli, D. F., Karginov, A. V., Rajfur, Z., Jacobson, K., et al. (2008). Spatial and temporal regulation of focal adhesion kinase activity in living cells. Mol. Cell. Biol. 28, 201-214. doi: 10.1128/MCB.01324-07
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 201-214
    • Cai, X.1    Lietha, D.2    Ceccarelli, D.F.3    Karginov, A.V.4    Rajfur, Z.5    Jacobson, K.6
  • 15
    • 34247391898 scopus 로고    scopus 로고
    • Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo
    • doi: 10.1371/journal.pbio.0050095
    • Calleja, V., Alcor, D., Laguerre, M., Park, J., Vojnovic, B., Hemmings, B. A., et al. (2007). Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo. PLoS Biol. 5:e95. doi: 10.1371/journal.pbio.0050095
    • (2007) PLoS Biol. , vol.5
    • Calleja, V.1    Alcor, D.2    Laguerre, M.3    Park, J.4    Vojnovic, B.5    Hemmings, B.A.6
  • 16
    • 33845200606 scopus 로고    scopus 로고
    • A cellular FRET-based sensor for beta-O-GlcNAc, a dynamic carbohydrate modification involved in signaling
    • doi: 10.1021/ja065835+
    • Carrillo, L. D., Krishnamoorthy, L., and Mahal, L. K. (2006). A cellular FRET-based sensor for beta-O-GlcNAc, a dynamic carbohydrate modification involved in signaling. J. Am. Chem. Soc. 128, 14768-14769. doi: 10.1021/ja065835+
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14768-14769
    • Carrillo, L.D.1    Krishnamoorthy, L.2    Mahal, L.K.3
  • 17
    • 0035282334 scopus 로고    scopus 로고
    • Mammalian MAP kinase signalling cascades
    • doi: 10.1038/35065000
    • Chang, L., and Karin, M. (2001). Mammalian MAP kinase signalling cascades. Nature 410, 37-40. doi: 10.1038/35065000
    • (2001) Nature , vol.410 , pp. 37-40
    • Chang, L.1    Karin, M.2
  • 18
    • 84880511705 scopus 로고    scopus 로고
    • Behaviour-dependent recruitment of long-range projection neurons in somatosensory cortex
    • doi: 10.1038/nature12236
    • Chen, J. L., Carta, S., Soldado-Magraner, J., Schneider, B. L., and Helmchen, F. (2013). Behaviour-dependent recruitment of long-range projection neurons in somatosensory cortex. Nature 499, 336-340. doi: 10.1038/nature12236
    • (2013) Nature , vol.499 , pp. 336-340
    • Chen, J.L.1    Carta, S.2    Soldado-Magraner, J.3    Schneider, B.L.4    Helmchen, F.5
  • 19
    • 23844516687 scopus 로고    scopus 로고
    • Mass of the postsynaptic density and enumeration of three key molecules
    • doi: 10.1073/pnas.0505359102
    • Chen, X., Vinade, L., Leapman, R. D., Petersen, J. D., Nakagawa, T., Phillips, T. M., et al. (2005). Mass of the postsynaptic density and enumeration of three key molecules. Proc. Natl. Acad. Sci. U.S.A. 102, 11551-11556. doi: 10.1073/pnas.0505359102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 11551-11556
    • Chen, X.1    Vinade, L.2    Leapman, R.D.3    Petersen, J.D.4    Nakagawa, T.5    Phillips, T.M.6
  • 20
    • 0037017397 scopus 로고    scopus 로고
    • A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows
    • doi: 10.1083/jcb.200110161
    • Chew, T. L., Wolf, W. A., Gallagher, P. J., Matsumura, F., and Chisholm, R. L. (2002). A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows. J. Cell Biol. 156 543-553. doi: 10.1083/jcb.200110161
    • (2002) J. Cell Biol. , vol.156 , pp. 543-553
    • Chew, T.L.1    Wolf, W.A.2    Gallagher, P.J.3    Matsumura, F.4    Chisholm, R.L.5
  • 21
    • 36549075574 scopus 로고    scopus 로고
    • Synaptic plasticity: Multiple forms, functions, and mechanisms
    • doi: 10.1038/sj.npp.1301559
    • Citri, A., and Malenka, R. C. (2008). Synaptic plasticity: multiple forms, functions, and mechanisms. Neuropsychopharmacology 33, 18-41. doi: 10.1038/sj.npp.1301559
    • (2008) Neuropsychopharmacology , vol.33 , pp. 18-41
    • Citri, A.1    Malenka, R.C.2
  • 23
    • 37249015845 scopus 로고    scopus 로고
    • Intramolecular fluorescence resonance energy transfer between fused autofluorescent proteins reveals rearrangements of the N-and C-terminal segments of the plasma membrane Ca2+ pump involved in the activation
    • doi: 10.1074/jbc.M703377200
    • Corradi, G. R., and Adamo, H. P. (2007). Intramolecular fluorescence resonance energy transfer between fused autofluorescent proteins reveals rearrangements of the N-and C-terminal segments of the plasma membrane Ca2+ pump involved in the activation. J. Biol. Chem. 282, 35440-35448. doi: 10.1074/jbc.M703377200
    • (2007) J. Biol. Chem. , vol.282 , pp. 35440-35448
    • Corradi, G.R.1    Adamo, H.P.2
  • 24
    • 0037203821 scopus 로고    scopus 로고
    • Mechanism for the learning deficits in a mouse model of neurofibromatosis type 1
    • doi: 10.1038/nature711
    • Costa, R. M., Federov, N. B., Kogan, J. H., Murphy, G. G., Stern, J., Ohno, M., et al. (2002). Mechanism for the learning deficits in a mouse model of neurofibromatosis type 1. Nature 415, 526-530. doi: 10.1038/nature711
    • (2002) Nature , vol.415 , pp. 526-530
    • Costa, R.M.1    Federov, N.B.2    Kogan, J.H.3    Murphy, G.G.4    Stern, J.5    Ohno, M.6
  • 25
    • 0034660615 scopus 로고    scopus 로고
    • The MAPK/ERK cascade targets both Elk-1 and cAMP response element-binding protein to control long-term potentiation-dependent gene expression in the dentate gyrus in vivo
    • Davis, S., Vanhoutte, P., Pages, C., Caboche, J., and Laroche, S. (2000). The MAPK/ERK cascade targets both Elk-1 and cAMP response element-binding protein to control long-term potentiation-dependent gene expression in the dentate gyrus in vivo. J. Neurosci. 20, 4563-4572.
    • (2000) J. Neurosci. , vol.20 , pp. 4563-4572
    • Davis, S.1    Vanhoutte, P.2    Pages, C.3    Caboche, J.4    Laroche, S.5
  • 26
    • 0032498172 scopus 로고    scopus 로고
    • Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations
    • doi: 10.1126/science.279.5348.227
    • De Koninck, P., and Schulman, H. (1998). Sensitivity of CaM kinase II to the frequency of Ca2+ oscillations. Science 279, 227-230. doi: 10.1126/science.279.5348.227
    • (1998) Science , vol.279 , pp. 227-230
    • De Koninck, P.1    Schulman, H.2
  • 27
    • 77951782126 scopus 로고    scopus 로고
    • Chloride channels: Often enigmatic, rarely predictable
    • doi: 10.1146/annurev-physiol-021909-135811
    • Duran, C., Thompson, C. H., Xiao, Q., and Hartzell, H. C. (2010). Chloride channels: often enigmatic, rarely predictable. Annu. Rev. Physiol. 72, 95-121. doi: 10.1146/annurev-physiol-021909-135811
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 95-121
    • Duran, C.1    Thompson, C.H.2    Xiao, Q.3    Hartzell, H.C.4
  • 28
    • 27544454650 scopus 로고    scopus 로고
    • Method for detection of specific nucleic acids by recombinant protein with fluorescent resonance energy transfer
    • doi: 10.1021/ac048491j
    • Endoh, T., Funabashi, H., Mie, M., and Kobatake, E. (2005). Method for detection of specific nucleic acids by recombinant protein with fluorescent resonance energy transfer. Anal. Chem. 77, 4308-4314. doi: 10.1021/ac048491j
    • (2005) Anal. Chem. , vol.77 , pp. 4308-4314
    • Endoh, T.1    Funabashi, H.2    Mie, M.3    Kobatake, E.4
  • 29
    • 0037162304 scopus 로고    scopus 로고
    • Visualization of maltose uptake in living yeast cells by fluorescent nanosensors
    • doi: 10.1073/pnas.142089199
    • Fehr, M., Frommer, W. B., and Lalonde, S. (2002). Visualization of maltose uptake in living yeast cells by fluorescent nanosensors. Proc. Natl. Acad. Sci. U.S.A. 99, 9846-9851. doi: 10.1073/pnas.142089199
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9846-9851
    • Fehr, M.1    Frommer, W.B.2    Lalonde, S.3
  • 30
    • 0038819942 scopus 로고    scopus 로고
    • In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors
    • doi: 10.1074/jbc.M301333200
    • Fehr, M., Lalonde, S., Lager, I., Wolff, M. W., and Frommer, W. B. (2003). In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors. J. Biol. Chem. 278, 19127-19133. doi: 10.1074/jbc.M301333200
    • (2003) J. Biol. Chem. , vol.278 , pp. 19127-19133
    • Fehr, M.1    Lalonde, S.2    Lager, I.3    Wolff, M.W.4    Frommer, W.B.5
  • 31
    • 34250965243 scopus 로고
    • Energiewanderung und Fluoreszenz
    • doi: 10.1007/BF00585226
    • Förster, T. (1946). Energiewanderung und Fluoreszenz. Naturbreakwissenschaften 33, 166-175. doi: 10.1007/BF00585226
    • (1946) Naturbreakwissenschaften , vol.33 , pp. 166-175
    • Förster, T.1
  • 32
    • 77950434011 scopus 로고    scopus 로고
    • Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor
    • doi: 10.1073/pnas.0909671107
    • Fosbrink, M., Aye-Han, N. N., Cheong, R., Levchenko, A., and Zhang, J. (2010). Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor. Proc. Natl. Acad. Sci. U.S.A. 107, 5459-5464. doi: 10.1073/pnas.0909671107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5459-5464
    • Fosbrink, M.1    Aye-Han, N.N.2    Cheong, R.3    Levchenko, A.4    Zhang, J.5
  • 33
    • 77954484935 scopus 로고    scopus 로고
    • Single-molecule discrimination of discrete perisynaptic and distributed sites of actin filament assembly within dendritic spines
    • doi: 10.1016/j.neuron.2010.05.026
    • Frost, N. A., Shroff, H., Kong, H., Betzig, E., and Blanpied, T. A. (2010). Single-molecule discrimination of discrete perisynaptic and distributed sites of actin filament assembly within dendritic spines. Neuron 67, 86-99. doi: 10.1016/j.neuron.2010.05.026
    • (2010) Neuron , vol.67 , pp. 86-99
    • Frost, N.A.1    Shroff, H.2    Kong, H.3    Betzig, E.4    Blanpied, T.A.5
  • 34
    • 84876952581 scopus 로고    scopus 로고
    • Nonlinear decoding and asymmetric representation of neuronal input information by CaMKIIα and calcineurin
    • doi: 10.1016/j.celrep.2013.03.033
    • Fujii, H., Inoue, M., Okuno, H., Sano, Y., Takemoto-Kimura, S., Kitamura, K., et al. (2013). Nonlinear decoding and asymmetric representation of neuronal input information by CaMKIIα and calcineurin. Cell Rep. 3, 978-987. doi: 10.1016/j.celrep.2013.03.033
    • (2013) Cell Rep. , vol.3 , pp. 978-987
    • Fujii, H.1    Inoue, M.2    Okuno, H.3    Sano, Y.4    Takemoto-Kimura, S.5    Kitamura, K.6
  • 35
    • 33646852421 scopus 로고    scopus 로고
    • Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes
    • doi: 10.1074/jbc.M509344200
    • Fujioka, A., Terai, K., Itoh, R. E., Aoki, K., Nakamura, T., Kuroda, S., et al. (2006). Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes. J. Biol. Chem. 281, 8917-8926. doi: 10.1074/jbc.M509344200
    • (2006) J. Biol. Chem. , vol.281 , pp. 8917-8926
    • Fujioka, A.1    Terai, K.2    Itoh, R.E.3    Aoki, K.4    Nakamura, T.5    Kuroda, S.6
  • 36
    • 45749115811 scopus 로고    scopus 로고
    • Midzone activation of aurora B in anaphase produces an intracellular phosphorylation gradient
    • doi: 10.1038/nature06923
    • Fuller, B. G., Lampson, M. A., Foley, E. A., Rosasco-Nitcher, S., Le, K. V., Tobelmann, P., et al. (2008). Midzone activation of aurora B in anaphase produces an intracellular phosphorylation gradient. Nature 453, 1132-1136. doi: 10.1038/nature06923
    • (2008) Nature , vol.453 , pp. 1132-1136
    • Fuller, B.G.1    Lampson, M.A.2    Foley, E.A.3    Rosasco-Nitcher, S.4    Le, K.V.5    Tobelmann, P.6
  • 37
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Förster resonance energy transfer with GFP
    • doi: 10.1073/pnas.0509922103
    • Ganesan, S., Ameer-Beg, S. M., Ng, T. T., Vojnovic, B., and Wouters, F. S. (2006). A dark yellow fluorescent protein (YFP)-based resonance energy-accepting chromoprotein (REACh) for Förster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. U.S.A. 103, 4089-4094. doi: 10.1073/pnas.0509922103
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 38
    • 13844294048 scopus 로고    scopus 로고
    • Enhanced Ras activity promotes spine formation in synRas mice neocortex
    • doi: 10.1097/00001756-200502080-00016
    • Gartner, U., Alpar, A., Behrbohm, J., Heumann, R., and Arendt, T. (2005). Enhanced Ras activity promotes spine formation in synRas mice neocortex. Neuroreport 16, 149-152. doi: 10.1097/00001756-200502080-00016
    • (2005) Neuroreport , vol.16 , pp. 149-152
    • Gartner, U.1    Alpar, A.2    Behrbohm, J.3    Heumann, R.4    Arendt, T.5
  • 39
    • 77951184302 scopus 로고    scopus 로고
    • Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis
    • doi: 10.1016/j.devcel.2010.02.013
    • Gavet, O., and Pines, J. (2010). Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis. Dev. Cell 18, 533-543. doi: 10.1016/j.devcel.2010.02.013
    • (2010) Dev. Cell , vol.18 , pp. 533-543
    • Gavet, O.1    Pines, J.2
  • 40
    • 0035885153 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase regulates early phosphorylation and delayed expression of Ca2+/calmodulin-dependent protein kinase II in long-term potentiation
    • Giovannini, M. G., Blitzer, R. D., Wong, T., Asoma, K., Tsokas, P., Morrison, J. H., et al. (2001). Mitogen-activated protein kinase regulates early phosphorylation and delayed expression of Ca2+/calmodulin-dependent protein kinase II in long-term potentiation. J. Neurosci. 21, 7053-7062.
    • (2001) J. Neurosci. , vol.21 , pp. 7053-7062
    • Giovannini, M.G.1    Blitzer, R.D.2    Wong, T.3    Asoma, K.4    Tsokas, P.5    Morrison, J.H.6
  • 41
    • 84859173050 scopus 로고    scopus 로고
    • Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%
    • doi: 10.1038/ncomms1738
    • Goedhart, J., von Stetten, D., Noirclerc-Savoye, M., Lelimousin, M., Joosen, L., Hink, M. A., et al. (2012). Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%. Nat. Commun. 3, 751. doi: 10.1038/ncomms1738
    • (2012) Nat. Commun. , vol.3 , pp. 751
    • Goedhart, J.1    von Stetten, D.2    Noirclerc-Savoye, M.3    Lelimousin, M.4    Joosen, L.5    Hink, M.A.6
  • 42
    • 0038008186 scopus 로고    scopus 로고
    • Protein kinase C and ERK involvement in dendritic spine plasticity in cultured rodent hippocampal neurons
    • doi: 10.1046/j.1460-9568.2003.02694.x
    • Goldin, M., and Segal, M. (2003). Protein kinase C and ERK involvement in dendritic spine plasticity in cultured rodent hippocampal neurons. Eur. J. Neurosci. 17, 2529-2539. doi: 10.1046/j.1460-9568.2003.02694.x
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 2529-2539
    • Goldin, M.1    Segal, M.2
  • 43
    • 0029118480 scopus 로고
    • Voltage sensing by fluorescence resonance energy transfer in single cells
    • doi: 10.1016/S0006-3495(95)80029-9
    • Gonzalez, J. E., and Tsien, R. Y. (1995). Voltage sensing by fluorescence resonance energy transfer in single cells. Biophys. J. 69, 1272-1280. doi: 10.1016/S0006-3495(95)80029-9
    • (1995) Biophys. J. , vol.69 , pp. 1272-1280
    • Gonzalez, J.E.1    Tsien, R.Y.2
  • 44
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • doi: 10.1126/science.1067566
    • Haj, F. G., Verveer, P. J., Squire, A., Neel, B. G., and Bastiaens, P. I. (2002). Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295, 1708-1711. doi: 10.1126/science.1067566
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.5
  • 45
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • doi: 10.1126/science.279.5350.558
    • Han, J., Luby-Phelps, K., Das, B., Shu, X., Xia, Y., Mosteller, R. D., et al. (1998). Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 279, 558-560. doi: 10.1126/science.279.5350.558
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5    Mosteller, R.D.6
  • 46
    • 51649110721 scopus 로고    scopus 로고
    • Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1
    • doi: 10.1083/jcb.200803110
    • Hao, Y., and Macara, I. G. (2008). Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1. J. Cell Biol. 182, 827-836. doi: 10.1083/jcb.200803110
    • (2008) J. Cell Biol. , vol.182 , pp. 827-836
    • Hao, Y.1    Macara, I.G.2
  • 47
    • 4544232721 scopus 로고    scopus 로고
    • Imaging endoplasmic reticulum calcium with a fluorescent biosensor in transgenic mice
    • doi: 10.1152/ajpcell.00151.2004
    • Hara, M., Bindokas, V., Lopez, J. P., Kaihara, K., Landa, L. R. Jr., Harbeck, M., et al. (2004). Imaging endoplasmic reticulum calcium with a fluorescent biosensor in transgenic mice. Am. J. Physiol. Cell Physiol. 287, C932-C938. doi: 10.1152/ajpcell.00151.2004
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287
    • Hara, M.1    Bindokas, V.2    Lopez, J.P.3    Kaihara, K.4    Landa Jr., L.R.5    Harbeck, M.6
  • 49
    • 46849102728 scopus 로고    scopus 로고
    • The spread of Ras activity triggered by activation of a single dendritic spine
    • doi: 10.1126/science.1159675
    • Harvey, C. D., Yasuda, R., Zhong, H., and Svoboda, K. (2008b). The spread of Ras activity triggered by activation of a single dendritic spine. Science 321, 136-140. doi: 10.1126/science.1159675
    • (2008) Science , vol.321 , pp. 136-140
    • Harvey, C.D.1    Yasuda, R.2    Zhong, H.3    Svoboda, K.4
  • 50
    • 77955870489 scopus 로고    scopus 로고
    • Motoneurons dedicated to either forward or backward locomotion in the nematode Caenorhabditis elegans
    • doi: 10.1523/JNEUROSCI.2244-10.2010
    • Haspel, G., O'Donovan, M. J., and Hart, A. C. (2010). Motoneurons dedicated to either forward or backward locomotion in the nematode Caenorhabditis elegans. J. Neurosci. 30, 11151-11156. doi: 10.1523/JNEUROSCI.2244-10.2010
    • (2010) J. Neurosci. , vol.30 , pp. 11151-11156
    • Haspel, G.1    O'Donovan, M.J.2    Hart, A.C.3
  • 51
    • 20444376592 scopus 로고    scopus 로고
    • Dendritic spine geometry: Functional implication and regulation
    • doi: 10.1016/j.neuron.2005.05.006
    • Hayashi, Y., and Majewska, A. K. (2005). Dendritic spine geometry: functional implication and regulation. Neuron 46, 529-532. doi: 10.1016/j.neuron.2005.05.006
    • (2005) Neuron , vol.46 , pp. 529-532
    • Hayashi, Y.1    Majewska, A.K.2
  • 52
    • 1842790629 scopus 로고    scopus 로고
    • Genetically encoded indicators of cellular calcium dynamics based on troponin C and green fluorescent protein
    • doi: 10.1074/jbc.M312751200
    • Heim, N., and Griesbeck, O. (2004). Genetically encoded indicators of cellular calcium dynamics based on troponin C and green fluorescent protein. J. Biol. Chem. 279, 14280-14286. doi: 10.1074/jbc.M312751200
    • (2004) J. Biol. Chem. , vol.279 , pp. 14280-14286
    • Heim, N.1    Griesbeck, O.2
  • 53
    • 34249306702 scopus 로고    scopus 로고
    • Epidermal growth factor directs sex-specific steroid signaling through Src activation
    • doi: 10.1074/jbc.M610444200
    • Hitosugi, T., Sasaki, K., Sato, M., Suzuki, Y., and Umezawa, Y. (2007). Epidermal growth factor directs sex-specific steroid signaling through Src activation. J. Biol. Chem. 282, 10697-10706. doi: 10.1074/jbc.M610444200
    • (2007) J. Biol. Chem. , vol.282 , pp. 10697-10706
    • Hitosugi, T.1    Sasaki, K.2    Sato, M.3    Suzuki, Y.4    Umezawa, Y.5
  • 54
    • 69249100460 scopus 로고    scopus 로고
    • Experience-dependent structural synaptic plasticity in the mammalian brain
    • doi: 10.1038/nrn2699
    • Holtmaat, A., and Svoboda, K. (2009). Experience-dependent structural synaptic plasticity in the mammalian brain. Nat. Rev. Neurosci. 10, 647-658. doi: 10.1038/nrn2699
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 647-658
    • Holtmaat, A.1    Svoboda, K.2
  • 55
    • 38649140136 scopus 로고    scopus 로고
    • Ca2+ influx through P2X receptors induces actin cytoskeleton reorganization by the formation of cofilin rods in neurites
    • doi: 10.1016/j.mcn.2007.10.001
    • Homma, K., Niino, Y., Hotta, K., and Oka, K. (2008). Ca2+ influx through P2X receptors induces actin cytoskeleton reorganization by the formation of cofilin rods in neurites. Mol. Cell. Neurosci. 37, 261-270. doi: 10.1016/j.mcn.2007.10.001
    • (2008) Mol. Cell. Neurosci. , vol.37 , pp. 261-270
    • Homma, K.1    Niino, Y.2    Hotta, K.3    Oka, K.4
  • 56
    • 0035956940 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of guanosine 3', 5'-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator
    • doi: 10.1073/pnas.051631298
    • Honda, A., Adams, S. R., Sawyer, C. L., Lev-Ram, V., Tsien, R. Y., and Dostmann, W. R. (2001). Spatiotemporal dynamics of guanosine 3', 5'-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator. Proc. Natl. Acad. Sci. U.S.A. 98, 2437-2442. doi: 10.1073/pnas.051631298
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2437-2442
    • Honda, A.1    Adams, S.R.2    Sawyer, C.L.3    Lev-Ram, V.4    Tsien, R.Y.5    Dostmann, W.R.6
  • 57
    • 40249097516 scopus 로고    scopus 로고
    • The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines
    • doi: 10.1016/j.neuron.2008.01.013
    • Honkura, N., Matsuzaki, M., Noguchi, J., Ellis-Davies, G. C., and Kasai, H. (2008). The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57, 719-729. doi: 10.1016/j.neuron.2008.01.013
    • (2008) Neuron , vol.57 , pp. 719-729
    • Honkura, N.1    Matsuzaki, M.2    Noguchi, J.3    Ellis-Davies, G.C.4    Kasai, H.5
  • 58
    • 77956340960 scopus 로고    scopus 로고
    • Spontaneous network activity visualized by ultrasensitive Ca(2+) indicators, yellow cameleon-nano
    • doi: 10.1038/nmeth.1488
    • Horikawa, K., Yamada, Y., Matsuda, T., Kobayashi, K., Hashimoto, M., Matsu-ura, T., et al. (2010). Spontaneous network activity visualized by ultrasensitive Ca(2+) indicators, yellow cameleon-nano. Nat. Methods 7, 729-732. doi: 10.1038/nmeth.1488
    • (2010) Nat. Methods , vol.7 , pp. 729-732
    • Horikawa, K.1    Yamada, Y.2    Matsuda, T.3    Kobayashi, K.4    Hashimoto, M.5    Matsu-ura, T.6
  • 59
    • 70349449239 scopus 로고    scopus 로고
    • Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators
    • doi: 10.1073/pnas.0904764106
    • Imamura, H., Nhat, K. P., Togawa, H., Saito, K., Iino, R., Kato-Yamada, Y., et al. (2009). Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators. Proc. Natl. Acad. Sci. U.S.A. 106, 15651-15656. doi: 10.1073/pnas.0904764106
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 15651-15656
    • Imamura, H.1    Nhat, K.P.2    Togawa, H.3    Saito, K.4    Iino, R.5    Kato-Yamada, Y.6
  • 60
    • 72149098399 scopus 로고    scopus 로고
    • An activity-induced microRNA controls dendritic spine formation by regulating Rac1-PAK signaling
    • doi: 10.1016/j.mcn.2009.10.005
    • Impey, S., Davare, M., Lesiak, A., Fortin, D., Ando, H., Varlamova, O., et al. (2010). An activity-induced microRNA controls dendritic spine formation by regulating Rac1-PAK signaling. Mol. Cell. Neurosci. 43, 146-156. doi: 10.1016/j.mcn.2009.10.005
    • (2010) Mol. Cell. Neurosci. , vol.43 , pp. 146-156
    • Impey, S.1    Davare, M.2    Lesiak, A.3    Fortin, D.4    Ando, H.5    Varlamova, O.6
  • 61
    • 0032191933 scopus 로고    scopus 로고
    • Cross talk between ERK and PKA is required for Ca2+ stimulation of CREB-dependent transcription and ERK nuclear translocation
    • doi: 10.1016/S0896-6273(00)80602-9
    • Impey, S., Obrietan, K., Wong, S. T., Poser, S., Yano, S., Wayman, G., et al. (1998a). Cross talk between ERK and PKA is required for Ca2+ stimulation of CREB-dependent transcription and ERK nuclear translocation. Neuron 21, 869-883. doi: 10.1016/S0896-6273(00)80602-9
    • (1998) Neuron , vol.21 , pp. 869-883
    • Impey, S.1    Obrietan, K.2    Wong, S.T.3    Poser, S.4    Yano, S.5    Wayman, G.6
  • 62
    • 0032195577 scopus 로고    scopus 로고
    • Stimulation of cAMP response element (CRE)-mediated transcription during contextual learning
    • Impey, S., Smith, D. M., Obrietan, K., Donahue, R., Wade, C., and Storm, D. R. (1998b). Stimulation of cAMP response element (CRE)-mediated transcription during contextual learning. Nat. Neurosci. 1, 595-601.
    • (1998) Nat. Neurosci. , vol.1 , pp. 595-601
    • Impey, S.1    Smith, D.M.2    Obrietan, K.3    Donahue, R.4    Wade, C.5    Storm, D.R.6
  • 63
    • 0037421209 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase activates Rac by entering in a complex with Eps8, Abi1, and Sos-1
    • doi: 10.1083/jcb.200206079
    • Innocenti, M., Frittoli, E., Ponzanelli, I., Falck, J. R., Brachmann, S. M., Di Fiore, P. P., et al. (2003). Phosphoinositide 3-kinase activates Rac by entering in a complex with Eps8, Abi1, and Sos-1. J. Cell Biol. 160, 17-23. doi: 10.1083/jcb.200206079
    • (2003) J. Cell Biol. , vol.160 , pp. 17-23
    • Innocenti, M.1    Frittoli, E.2    Ponzanelli, I.3    Falck, J.R.4    Brachmann, S.M.5    Di Fiore, P.P.6
  • 64
    • 0036828940 scopus 로고    scopus 로고
    • EphB receptors regulate dendritic spine development via intersectin, Cdc42 and N-WASP
    • doi: 10.1038/nn964
    • Irie, F., and Yamaguchi, Y. (2002). EphB receptors regulate dendritic spine development via intersectin, Cdc42 and N-WASP. Nat. Neurosci. 5, 1117-1118. doi: 10.1038/nn964
    • (2002) Nat. Neurosci. , vol.5 , pp. 1117-1118
    • Irie, F.1    Yamaguchi, Y.2
  • 65
    • 30544449810 scopus 로고    scopus 로고
    • Control of dendritic arborization by the phosphoinositide-3′-kinase-Akt-mammalian target of rapamycin pathway
    • doi: 10.1523/JNEUROSCI.2270-05.2005
    • Jaworski, J., Spangler, S., Seeburg, D. P., Hoogenraad, C. C., and Sheng, M. (2005). Control of dendritic arborization by the phosphoinositide-3′-kinase-Akt-mammalian target of rapamycin pathway. J. Neurosci. 25, 11300-11312. doi: 10.1523/JNEUROSCI.2270-05.2005
    • (2005) J. Neurosci. , vol.25 , pp. 11300-11312
    • Jaworski, J.1    Spangler, S.2    Seeburg, D.P.3    Hoogenraad, C.C.4    Sheng, M.5
  • 66
    • 84866000005 scopus 로고    scopus 로고
    • Single action potentials and subthreshold electrical events imaged in neurons with a fluorescent protein voltage probe
    • doi: 10.1016/j.neuron.2012.06.040
    • Jin, L., Han, Z., Platisa, J., Wooltorton, J. R., Cohen, L. B., and Pieribone, V. A. (2012). Single action potentials and subthreshold electrical events imaged in neurons with a fluorescent protein voltage probe. Neuron 75, 779-785. doi: 10.1016/j.neuron.2012.06.040
    • (2012) Neuron , vol.75 , pp. 779-785
    • Jin, L.1    Han, Z.2    Platisa, J.3    Wooltorton, J.R.4    Cohen, L.B.5    Pieribone, V.A.6
  • 67
    • 34547824221 scopus 로고    scopus 로고
    • Monitoring ATM kinase activity in living cells
    • doi: 10.1016/j.dnarep.2007.02.025
    • Johnson, S. A., You, Z., and Hunter, T. (2007). Monitoring ATM kinase activity in living cells. DNA Repair (Amst.) 6, 1277-1284. doi: 10.1016/j.dnarep.2007.02.025
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1277-1284
    • Johnson, S.A.1    You, Z.2    Hunter, T.3
  • 68
    • 79957619035 scopus 로고    scopus 로고
    • High throughput ratio imaging to profile caspase activity: Potential application in multiparameter high content apoptosis analysis and drug screening
    • doi: 10.1371/journal.pone.0020114
    • Joseph, J., Seervi, M., Sobhan, P. K., and Retnabai, S. T. (2011). High throughput ratio imaging to profile caspase activity: potential application in multiparameter high content apoptosis analysis and drug screening. PLoS ONE 6:e20114. doi: 10.1371/journal.pone.0020114
    • (2011) PLoS ONE , vol.6
    • Joseph, J.1    Seervi, M.2    Sobhan, P.K.3    Retnabai, S.T.4
  • 69
    • 84862304850 scopus 로고    scopus 로고
    • Live imaging of protein kinase activities in transgenic mice expressing FRET biosensors
    • doi: 10.1247/csf.11045
    • Kamioka, Y., Sumiyama, K., Mizuno, R., Sakai, Y., Hirata, E., Kiyokawa, E., et al. (2012). Live imaging of protein kinase activities in transgenic mice expressing FRET biosensors. Cell Struct. Funct. 37, 65-73. doi: 10.1247/csf.11045
    • (2012) Cell Struct. Funct. , vol.37 , pp. 65-73
    • Kamioka, Y.1    Sumiyama, K.2    Mizuno, R.3    Sakai, Y.4    Hirata, E.5    Kiyokawa, E.6
  • 70
    • 33747858041 scopus 로고    scopus 로고
    • GTP hydrolysis by the Rho family GTPase TC10 promotes exocytic vesicle fusion
    • doi: 10.1016/j.devcel.2006.07.008
    • Kawase, K., Nakamura, T., Takaya, A., Aoki, K., Namikawa, K., Kiyama, H., et al. (2006). GTP hydrolysis by the Rho family GTPase TC10 promotes exocytic vesicle fusion. Dev. Cell 11, 411-421. doi: 10.1016/j.devcel.2006.07.008
    • (2006) Dev. Cell , vol.11 , pp. 411-421
    • Kawase, K.1    Nakamura, T.2    Takaya, A.3    Aoki, K.4    Namikawa, K.5    Kiyama, H.6
  • 71
    • 0038823489 scopus 로고
    • Biochemical and immunochemical evidence that the "major postsynaptic density protein" is a subunit of a calmodulin-dependent protein kinase
    • doi: 10.1073/pnas.80.23.7357
    • Kennedy, M. B., Bennett, M. K., and Erondu, N. E. (1983). Biochemical and immunochemical evidence that the "major postsynaptic density protein" is a subunit of a calmodulin-dependent protein kinase. Proc. Natl. Acad. Sci. U.S.A. 80, 7357-7361. doi: 10.1073/pnas.80.23.7357
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 7357-7361
    • Kennedy, M.B.1    Bennett, M.K.2    Erondu, N.E.3
  • 72
    • 77956568206 scopus 로고    scopus 로고
    • Nerve growth factor induces axonal filopodia through localized microdomains of phosphoinositide 3-kinase activity that drive the formation of cytoskeletal precursors to filopodia
    • doi: 10.1523/JNEUROSCI.1740-10.2010
    • Ketschek, A., and Gallo, G. (2010). Nerve growth factor induces axonal filopodia through localized microdomains of phosphoinositide 3-kinase activity that drive the formation of cytoskeletal precursors to filopodia. J. Neurosci. 30, 12185-12197. doi: 10.1523/JNEUROSCI.1740-10.2010
    • (2010) J. Neurosci. , vol.30 , pp. 12185-12197
    • Ketschek, A.1    Gallo, G.2
  • 73
    • 43449136758 scopus 로고    scopus 로고
    • Imaging of Rab5 activity identifies essential regulators for phagosome maturation
    • doi: 10.1038/nature06857
    • Kitano, M., Nakaya, M., Nakamura, T., Nagata, S., and Matsuda, M. (2008). Imaging of Rab5 activity identifies essential regulators for phagosome maturation. Nature 453, 241-245. doi: 10.1038/nature06857
    • (2008) Nature , vol.453 , pp. 241-245
    • Kitano, M.1    Nakaya, M.2    Nakamura, T.3    Nagata, S.4    Matsuda, M.5
  • 74
    • 79951981589 scopus 로고    scopus 로고
    • Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of forster resonance energy transfer (FRET): Implications for signaling and pharmacology
    • doi: 10.1146/annurev-pharmtox-010510-100234
    • Kiyokawa, E., Aoki, K., Nakamura, T., and Matsuda, M. (2011). Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of forster resonance energy transfer (FRET): implications for signaling and pharmacology. Annu. Rev. Pharmacol. Toxicol. 51, 337-358. doi: 10.1146/annurev-pharmtox-010510-100234
    • (2011) Annu. Rev. Pharmacol. Toxicol. , vol.51 , pp. 337-358
    • Kiyokawa, E.1    Aoki, K.2    Nakamura, T.3    Matsuda, M.4
  • 75
    • 79958860033 scopus 로고    scopus 로고
    • Development of a high-dynamic range, GFP-based FRET probe sensitive to oxidative microenvironments
    • doi: 10.1258/ebm.2011.011009
    • Kolossov, V. L., Spring, B. Q., Clegg, R. M., Henry, J. J., Sokolowski, A., Kenis, P. J., et al. (2011). Development of a high-dynamic range, GFP-based FRET probe sensitive to oxidative microenvironments. Exp. Biol. Med. (Maywood) 236, 681-691. doi: 10.1258/ebm.2011.011009
    • (2011) Exp. Biol. Med. (Maywood) , vol.236 , pp. 681-691
    • Kolossov, V.L.1    Spring, B.Q.2    Clegg, R.M.3    Henry, J.J.4    Sokolowski, A.5    Kenis, P.J.6
  • 76
    • 82655181489 scopus 로고    scopus 로고
    • Development of an optimized backbone of FRET biosensors for kinases and GTPases
    • doi: 10.1091/mbc.E11-01-0072
    • Komatsu, N., Aoki, K., Yamada, M., Yukinaga, H., Fujita, Y., Kamioka, Y., et al. (2011). Development of an optimized backbone of FRET biosensors for kinases and GTPases. Mol. Biol. Cell 22, 4647-4656. doi: 10.1091/mbc.E11-01-0072
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4647-4656
    • Komatsu, N.1    Aoki, K.2    Yamada, M.3    Yukinaga, H.4    Fujita, Y.5    Kamioka, Y.6
  • 77
    • 0033724998 scopus 로고    scopus 로고
    • A genetically encoded ratiometric indicator for chloride: Capturing chloride transients in cultured hippocampal neurons
    • doi: 10.1016/S0896-6273(00)00056-8
    • Kuner, T., and Augustine, G. J. (2000). A genetically encoded ratiometric indicator for chloride: capturing chloride transients in cultured hippocampal neurons. Neuron 27, 447-459. doi: 10.1016/S0896-6273(00)00056-8
    • (2000) Neuron , vol.27 , pp. 447-459
    • Kuner, T.1    Augustine, G.J.2
  • 78
    • 14044266297 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter
    • doi: 10.1074/jbc.M411534200
    • Kunkel, M. T., Ni, Q., Tsien, R. Y., Zhang, J., and Newton, A. C. (2005). Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter. J. Biol. Chem. 280, 5581-5587. doi: 10.1074/jbc.M411534200
    • (2005) J. Biol. Chem. , vol.280 , pp. 5581-5587
    • Kunkel, M.T.1    Ni, Q.2    Tsien, R.Y.3    Zhang, J.4    Newton, A.C.5
  • 79
    • 34250338923 scopus 로고    scopus 로고
    • Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter
    • doi: 10.1074/jbc.M608086200
    • Kunkel, M. T., Toker, A., Tsien, R. Y., and Newton, A. C. (2007). Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter. J. Biol. Chem. 282, 6733-6742. doi: 10.1074/jbc.M608086200
    • (2007) J. Biol. Chem. , vol.282 , pp. 6733-6742
    • Kunkel, M.T.1    Toker, A.2    Tsien, R.Y.3    Newton, A.C.4
  • 80
    • 0035903217 scopus 로고    scopus 로고
    • A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo
    • doi: 10.1074/jbc.M104341200
    • Kurokawa, K., Mochizuki, N., Ohba, Y., Mizuno, H., Miyawaki, A., and Matsuda, M. (2001). A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. J. Biol. Chem. 276, 31305-31310. doi: 10.1074/jbc.M104341200
    • (2001) J. Biol. Chem. , vol.276 , pp. 31305-31310
    • Kurokawa, K.1    Mochizuki, N.2    Ohba, Y.3    Mizuno, H.4    Miyawaki, A.5    Matsuda, M.6
  • 81
    • 40949113123 scopus 로고    scopus 로고
    • Genetically encoded probe for fluorescence lifetime imaging of CaMKII activity
    • doi: 10.1016/j.bbrc.2008.02.070
    • Kwok, S., Lee, C., Sanchez, S. A., Hazlett, T. L., Gratton, E., and Hayashi, Y. (2008). Genetically encoded probe for fluorescence lifetime imaging of CaMKII activity. Biochem. Biophys. Res. Commun. 369, 519-525. doi: 10.1016/j.bbrc.2008.02.070
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 519-525
    • Kwok, S.1    Lee, C.2    Sanchez, S.A.3    Hazlett, T.L.4    Gratton, E.5    Hayashi, Y.6
  • 82
    • 0141571333 scopus 로고    scopus 로고
    • Development of a fluorescent nanosensor for ribose
    • doi: 10.1016/S0014-5793(03)00976-1
    • Lager, I., Fehr, M., Frommer, W. B., and Lalonde, S. (2003). Development of a fluorescent nanosensor for ribose. FEBS Lett. 553, 85-89. doi: 10.1016/S0014-5793(03)00976-1
    • (2003) FEBS Lett. , vol.553 , pp. 85-89
    • Lager, I.1    Fehr, M.2    Frommer, W.B.3    Lalonde, S.4
  • 83
    • 84867084476 scopus 로고    scopus 로고
    • Improving FRET dynamic range with bright green and red fluorescent proteins
    • doi: 10.1038/nmeth.2171
    • Lam, A. J., St-Pierre, F., Gong, Y., Marshall, J. D., Cranfill, P. J., Baird, M. A., et al. (2012). Improving FRET dynamic range with bright green and red fluorescent proteins. Nat. Methods 9, 1005-1012. doi: 10.1038/nmeth.2171
    • (2012) Nat. Methods , vol.9 , pp. 1005-1012
    • Lam, A.J.1    St-Pierre, F.2    Gong, Y.3    Marshall, J.D.4    Cranfill, P.J.5    Baird, M.A.6
  • 84
    • 26944451290 scopus 로고    scopus 로고
    • CaMK-II oligomerization potential determined using CFP/YFP FRET
    • doi: 10.1016/j.bbamcr.2005.08.005
    • Lantsman, K., and Tombes, R. M. (2005). CaMK-II oligomerization potential determined using CFP/YFP FRET. Biochim. Biophys. Acta 1746, 45-54. doi: 10.1016/j.bbamcr.2005.08.005
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 45-54
    • Lantsman, K.1    Tombes, R.M.2
  • 85
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • doi: 10.1038/nature07842
    • Lee, S. J., Escobedo-Lozoya, Y., Szatmari, E. M., and Yasuda, R. (2009). Activation of CaMKII in single dendritic spines during long-term potentiation. Nature 458, 299-304. doi: 10.1038/nature07842
    • (2009) Nature , vol.458 , pp. 299-304
    • Lee, S.J.1    Escobedo-Lozoya, Y.2    Szatmari, E.M.3    Yasuda, R.4
  • 86
    • 34047104569 scopus 로고    scopus 로고
    • FRET evidence that an isoform of caspase-7 binds but does not cleave its substrate
    • doi: 10.1109/IEMBS.2006.260832
    • Li, I. T., Chiang, J. J., and Truong, K. (2006). FRET evidence that an isoform of caspase-7 binds but does not cleave its substrate. Conf. Proc. IEEE Eng. Med. Biol. Soc. 1, 531-534. doi: 10.1109/IEMBS.2006.260832
    • (2006) Conf. Proc. IEEE Eng. Med. Biol. Soc. , vol.1 , pp. 531-534
    • Li, I.T.1    Chiang, J.J.2    Truong, K.3
  • 87
    • 2442570040 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of histone methylation in living cells
    • doi: 10.1021/ja038854h
    • Lin, C. W., Jao, C. Y., and Ting, A. Y. (2004). Genetically encoded fluorescent reporters of histone methylation in living cells. J. Am. Chem. Soc. 126, 5982-5983. doi: 10.1021/ja038854h
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5982-5983
    • Lin, C.W.1    Jao, C.Y.2    Ting, A.Y.3
  • 88
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • doi: 10.1038/nrn753
    • Lisman, J., Schulman, H., and Cline, H. (2002). The molecular basis of CaMKII function in synaptic and behavioural memory. Nat. Rev. Neurosci. 3, 175-190. doi: 10.1038/nrn753
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 89
    • 1942508987 scopus 로고    scopus 로고
    • Imaging sites of N-wasp activity in lamellipodia and invadopodia of carcinoma cells
    • doi: 10.1016/j.cub.2004.04.008
    • Lorenz, M., Yamaguchi, H., Wang, Y., Singer, R. H., and Condeelis, J. (2004). Imaging sites of N-wasp activity in lamellipodia and invadopodia of carcinoma cells. Curr. Biol. 14, 697-703. doi: 10.1016/j.cub.2004.04.008
    • (2004) Curr. Biol. , vol.14 , pp. 697-703
    • Lorenz, M.1    Yamaguchi, H.2    Wang, Y.3    Singer, R.H.4    Condeelis, J.5
  • 90
    • 51349144633 scopus 로고    scopus 로고
    • Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
    • doi: 10.1038/nature07185
    • Macurek, L., Lindqvist, A., Lim, D., Lampson, M. A., Klompmaker, R., Freire, R., et al. (2008). Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery. Nature 455, 119-123. doi: 10.1038/nature07185
    • (2008) Nature , vol.455 , pp. 119-123
    • McUrek, L.1    Lindqvist, A.2    Lim, D.3    Lampson, M.A.4    Klompmaker, R.5    Freire, R.6
  • 91
    • 0037762556 scopus 로고    scopus 로고
    • Activation of PI3-kinase is required for AMPA receptor insertion during LTP of mEPSCs in cultured hippocampal neurons
    • doi: 10.1016/S0896-6273(03)00228-9
    • Man, H. Y., Wang, Q., Lu, W. Y., Ju, W., Ahmadian, G., Liu, L., et al. (2003). Activation of PI3-kinase is required for AMPA receptor insertion during LTP of mEPSCs in cultured hippocampal neurons. Neuron 38, 611-624. doi: 10.1016/S0896-6273(03)00228-9
    • (2003) Neuron , vol.38 , pp. 611-624
    • Man, H.Y.1    Wang, Q.2    Lu, W.Y.3    Ju, W.4    Ahmadian, G.5    Liu, L.6
  • 92
    • 33747380269 scopus 로고    scopus 로고
    • Cytosolic inositol 1 4, 5-trisphosphate dynamics during intracellular calcium oscillations in living cells
    • doi: 10.1083/jcb.200512141
    • Matsu-ura, T., Michikawa, T., Inoue, T., Miyawaki, A., Yoshida, M., and Mikoshiba, K. (2006). Cytosolic inositol 1 4, 5-trisphosphate dynamics during intracellular calcium oscillations in living cells. J. Cell Biol. 173, 755-765. doi: 10.1083/jcb.200512141
    • (2006) J. Cell Biol. , vol.173 , pp. 755-765
    • Matsu-ura, T.1    Michikawa, T.2    Inoue, T.3    Miyawaki, A.4    Yoshida, M.5    Mikoshiba, K.6
  • 93
    • 3042554012 scopus 로고    scopus 로고
    • Structural basis of long-term potentiation in single dendritic spines
    • doi: 10.1038/nature02617
    • Matsuzaki, M., Honkura, N., Ellis-Davies, G. C., and Kasai, H. (2004). Structural basis of long-term potentiation in single dendritic spines. Nature 429, 761-766. doi: 10.1038/nature02617
    • (2004) Nature , vol.429 , pp. 761-766
    • Matsuzaki, M.1    Honkura, N.2    Ellis-Davies, G.C.3    Kasai, H.4
  • 94
    • 13844250636 scopus 로고    scopus 로고
    • Growth of dendritic spines: A continuing story
    • doi: 10.1016/j.conb.2005.01.015
    • Matus, A. (2005). Growth of dendritic spines: a continuing story. Curr. Opin. Neurobiol. 15, 67-72. doi: 10.1016/j.conb.2005.01.015
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 67-72
    • Matus, A.1
  • 95
    • 44349176807 scopus 로고    scopus 로고
    • A fluorescence energy transfer-based mechanical stress sensor for specific proteins in situ
    • doi: 10.1111/j.1742-4658.2008.06461.x
    • Meng, F., Suchyna, T. M., and Sachs, F. (2008). A fluorescence energy transfer-based mechanical stress sensor for specific proteins in situ. FEBS J. 275, 3072-3087. doi: 10.1111/j.1742-4658.2008.06461.x
    • (2008) FEBS J. , vol.275 , pp. 3072-3087
    • Meng, F.1    Suchyna, T.M.2    Sachs, F.3
  • 96
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein
    • doi: 10.1016/0378-1119(95)00768-7
    • Mitra, R. D., Silva, C. M., and Youvan, D. C. (1996). Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene 173, 13-17. doi: 10.1016/0378-1119(95)00768-7
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 97
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • doi: 10.1016/S1534-5807(03)00060-1
    • Miyawaki, A. (2003). Visualization of the spatial and temporal dynamics of intracellular signaling. Dev. Cell 4, 295-305. doi: 10.1016/S1534-5807(03)00060-1
    • (2003) Dev. Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 98
    • 26944499780 scopus 로고    scopus 로고
    • Innovations in the imaging of brain functions using fluorescent proteins
    • doi: 10.1016/j.neuron.2005.10.003
    • Miyawaki, A. (2005). Innovations in the imaging of brain functions using fluorescent proteins. Neuron 48, 189-199. doi: 10.1016/j.neuron.2005.10.003
    • (2005) Neuron , vol.48 , pp. 189-199
    • Miyawaki, A.1
  • 99
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • doi: 10.1038/42264
    • Miyawaki, A., Llopis, J., Heim, R., McCaffery, J. M., Adams, J. A., Ikura, M., et al. (1997). Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature 388, 882-887. doi: 10.1038/42264
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6
  • 100
    • 84883217028 scopus 로고    scopus 로고
    • Transgenic zebrafish for ratiometric imaging of cytosolic and mitochondrial Ca response in teleost embryo
    • doi: 10.1016/j.ceca.2013.06.007
    • Mizuno, H., Sassa, T., Higashijima, S. I., Okamoto, H., and Miyawaki, A. (2013). Transgenic zebrafish for ratiometric imaging of cytosolic and mitochondrial Ca response in teleost embryo. Cell Calcium 54, 236-245. doi: 10.1016/j.ceca.2013.06.007
    • (2013) Cell Calcium , vol.54 , pp. 236-245
    • Mizuno, H.1    Sassa, T.2    Higashijima, S.I.3    Okamoto, H.4    Miyawaki, A.5
  • 101
    • 0035963331 scopus 로고    scopus 로고
    • Spatio-temporal images of growth-factor-induced activation of Ras and Rap1
    • doi: 10.1038/35082594
    • Mochizuki, N., Yamashita, S., Kurokawa, K., Ohba, Y., Nagai, T., Miyawaki, A., et al. (2001). Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature 411, 1065-1068. doi: 10.1038/35082594
    • (2001) Nature , vol.411 , pp. 1065-1068
    • Mochizuki, N.1    Yamashita, S.2    Kurokawa, K.3    Ohba, Y.4    Nagai, T.5    Miyawaki, A.6
  • 102
    • 84855491548 scopus 로고    scopus 로고
    • Experience-dependent regulation of CaMKII activity within single visual cortex synapses in vivo
    • doi: 10.1073/pnas.1108261109
    • Mower, A. F., Kwok, S., Yu, H., Majewska, A. K., Okamoto, K., Hayashi, Y., et al. (2011). Experience-dependent regulation of CaMKII activity within single visual cortex synapses in vivo. Proc. Natl. Acad. Sci. U.S.A. 108, 21241-21246. doi: 10.1073/pnas.1108261109
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 21241-21246
    • Mower, A.F.1    Kwok, S.2    Yu, H.3    Majewska, A.K.4    Okamoto, K.5    Hayashi, Y.6
  • 103
    • 57049179582 scopus 로고    scopus 로고
    • Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP
    • doi: 10.1007/s11068-008-9024-9
    • Murakoshi, H., Lee, S. J., and Yasuda, R. (2008). Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP. Brain Cell Biol. 36, 31-42. doi: 10.1007/s11068-008-9024-9
    • (2008) Brain Cell Biol. , vol.36 , pp. 31-42
    • Murakoshi, H.1    Lee, S.J.2    Yasuda, R.3
  • 104
    • 79953748494 scopus 로고    scopus 로고
    • Local, persistent activation of Rho GTPases during plasticity of single dendritic spines
    • doi: 10.1038/nature09823
    • Murakoshi, H., Wang, H., and Yasuda, R. (2011). Local, persistent activation of Rho GTPases during plasticity of single dendritic spines. Nature 472, 100-104. doi: 10.1038/nature09823
    • (2011) Nature , vol.472 , pp. 100-104
    • Murakoshi, H.1    Wang, H.2    Yasuda, R.3
  • 105
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • doi: 10.1038/nature03650
    • Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K., and Okamura, Y. (2005). Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435, 1239-1243. doi: 10.1038/nature03650
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 106
    • 0035853040 scopus 로고    scopus 로고
    • Circularly permuted green fluorescent proteins engineered to sense Ca2+
    • doi: 10.1073/pnas.051636098
    • Nagai, T., Sawano, A., Park, E. S., and Miyawaki, A. (2001). Circularly permuted green fluorescent proteins engineered to sense Ca2+. Proc. Natl. Acad. Sci. U.S.A. 98, 3197-3202. doi: 10.1073/pnas.051636098
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 3197-3202
    • Nagai, T.1    Sawano, A.2    Park, E.S.3    Miyawaki, A.4
  • 107
    • 3242706582 scopus 로고    scopus 로고
    • Expanded dynamic range of fluorescent indicators for Ca2+ by circularly permuted yellow fluorescent proteins
    • doi: 10.1073/pnas.0400417101
    • Nagai, T., Yamada, S., Tominaga, T., Ichikawa, M., and Miyawaki, A. (2004). Expanded dynamic range of fluorescent indicators for Ca2+ by circularly permuted yellow fluorescent proteins. Proc. Natl. Acad. Sci. U.S.A. 101, 10554-10559. doi: 10.1073/pnas.0400417101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10554-10559
    • Nagai, T.1    Yamada, S.2    Tominaga, T.3    Ichikawa, M.4    Miyawaki, A.5
  • 108
    • 0034019496 scopus 로고    scopus 로고
    • A fluorescent indicator for visualizing cAMP-induced phosphorylation in vivo
    • doi: 10.1038/73767
    • Nagai, Y., Miyazaki, M., Aoki, R., Zama, T., Inouye, S., Hirose, K., et al. (2000). A fluorescent indicator for visualizing cAMP-induced phosphorylation in vivo. Nat. Biotechnol. 18, 313-316. doi: 10.1038/73767
    • (2000) Nat. Biotechnol. , vol.18 , pp. 313-316
    • Nagai, Y.1    Miyazaki, M.2    Aoki, R.3    Zama, T.4    Inouye, S.5    Hirose, K.6
  • 109
    • 0035129282 scopus 로고    scopus 로고
    • A high signal-to-noise Ca2+ probe composed of a single green fluorescent protein
    • doi: 10.1038/84397
    • Nakai, J., Ohkura, M., and Imoto, K. (2001). A high signal-to-noise Ca2+ probe composed of a single green fluorescent protein. Nat. Biotechnol. 19, 137-141. doi: 10.1038/84397
    • (2001) Nat. Biotechnol. , vol.19 , pp. 137-141
    • Nakai, J.1    Ohkura, M.2    Imoto, K.3
  • 110
    • 48049085479 scopus 로고    scopus 로고
    • Cell-based fluorescent indicator to visualize brain-derived neurotrophic factor secreted from living neurons
    • doi: 10.1021/cb800052v
    • Nakajima, T., Sato, M., Akaza, N., and Umezawa, Y. (2008). Cell-based fluorescent indicator to visualize brain-derived neurotrophic factor secreted from living neurons. ACS Chem. Biol. 3, 352-358. doi: 10.1021/cb800052v
    • (2008) ACS Chem. Biol. , vol.3 , pp. 352-358
    • Nakajima, T.1    Sato, M.2    Akaza, N.3    Umezawa, Y.4
  • 111
    • 84874639191 scopus 로고    scopus 로고
    • Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor
    • doi: 10.1371/journal.pone.0058175
    • Nakanishi, Y., Iida, S., Ueoka-Nakanishi, H., Niimi, T., Tomioka, R., and Maeshima, M. (2013). Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. PLoS ONE 8:e58175. doi: 10.1371/journal.pone.0058175
    • (2013) PLoS ONE , vol.8
    • Nakanishi, Y.1    Iida, S.2    Ueoka-Nakanishi, H.3    Niimi, T.4    Tomioka, R.5    Maeshima, M.6
  • 112
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama, A. Y., Harms, M. B., and Luo, L. (2000). Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J. Neurosci. 20, 5329-5338.
    • (2000) J. Neurosci. , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.3
  • 113
    • 79955894911 scopus 로고    scopus 로고
    • Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells
    • doi: 10.1021/cr100002u
    • Newman, R. H., Fosbrink, M. D., and Zhang, J. (2011). Genetically encodable fluorescent biosensors for tracking signaling dynamics in living cells. Chem. Rev. 111, 3614-3666. doi: 10.1021/cr100002u
    • (2011) Chem. Rev. , vol.111 , pp. 3614-3666
    • Newman, R.H.1    Fosbrink, M.D.2    Zhang, J.3
  • 114
    • 43949103755 scopus 로고    scopus 로고
    • Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor
    • doi: 10.1039/b720034j
    • Newman, R. H., and Zhang, J. (2008). Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor. Mol. Biosyst. 4, 496-501. doi: 10.1039/b720034j
    • (2008) Mol. Biosyst. , vol.4 , pp. 496-501
    • Newman, R.H.1    Zhang, J.2
  • 115
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • doi: 10.1038/nbt1066
    • Nguyen, A. W., and Daugherty, P. S. (2005). Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23, 355-360. doi: 10.1038/nbt1066
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 116
    • 82055196689 scopus 로고    scopus 로고
    • Dynamic visualization of cellular signaling
    • doi: 10.1007/10_2008_48
    • Ni, Q., and Zhang, J. (2010). Dynamic visualization of cellular signaling. Adv. Biochem. Eng. Biotechnol. 119, 79-97. doi: 10.1007/10_2008_48
    • (2010) Adv. Biochem. Eng. Biotechnol. , vol.119 , pp. 79-97
    • Ni, Q.1    Zhang, J.2
  • 117
    • 77958064707 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) analysis demonstrates dimer/oligomer formation of the human breast cancer resistance protein (BCRP/ABCG2) in intact cells
    • Ni, Z., Mark, M. E., Cai, X., and Mao, Q. (2010). Fluorescence resonance energy transfer (FRET) analysis demonstrates dimer/oligomer formation of the human breast cancer resistance protein (BCRP/ABCG2) in intact cells. Int. J. Biochem. Mol. Biol. 1, 1-11.
    • (2010) Int. J. Biochem. Mol. Biol. , vol.1 , pp. 1-11
    • Ni, Z.1    Mark, M.E.2    Cai, X.3    Mao, Q.4
  • 118
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • doi: 10.1074/jbc.C400302200
    • Nikolaev, V. O., Bunemann, M., Hein, L., Hannawacker, A., and Lohse, M. J. (2004). Novel single chain cAMP sensors for receptor-induced signal propagation. J. Biol. Chem. 279, 37215-37218. doi: 10.1074/jbc.C400302200
    • (2004) J. Biol. Chem. , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1    Bunemann, M.2    Hein, L.3    Hannawacker, A.4    Lohse, M.J.5
  • 119
    • 31344471740 scopus 로고    scopus 로고
    • Fluorescent sensors for rapid monitoring of intracellular cGMP
    • doi: 10.1038/nmeth816
    • Nikolaev, V. O., Gambaryan, S., and Lohse, M. J. (2006). Fluorescent sensors for rapid monitoring of intracellular cGMP. Nat. Methods 3, 23-25. doi: 10.1038/nmeth816
    • (2006) Nat. Methods , vol.3 , pp. 23-25
    • Nikolaev, V.O.1    Gambaryan, S.2    Lohse, M.J.3
  • 120
    • 2542510885 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor and mineralocorticoid receptor interactions in living cells with GFP-based fluorescence resonance energy transfer
    • doi: 10.1523/JNEUROSCI.5495-03.2004
    • Nishi, M., Tanaka, M., Matsuda, K., Sunaguchi, M., and Kawata, M. (2004). Visualization of glucocorticoid receptor and mineralocorticoid receptor interactions in living cells with GFP-based fluorescence resonance energy transfer. J. Neurosci. 24, 4918-4927. doi: 10.1523/JNEUROSCI.5495-03.2004
    • (2004) J. Neurosci. , vol.24 , pp. 4918-4927
    • Nishi, M.1    Tanaka, M.2    Matsuda, K.3    Sunaguchi, M.4    Kawata, M.5
  • 121
    • 57349126275 scopus 로고    scopus 로고
    • Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells
    • doi: 10.1091/mbc.E08-03-0315
    • Nishioka, T., Aoki, K., Hikake, K., Yoshizaki, H., Kiyokawa, E., and Matsuda, M. (2008). Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells. Mol. Biol. Cell 19, 4213-4223. doi: 10.1091/mbc.E08-03-0315
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4213-4223
    • Nishioka, T.1    Aoki, K.2    Hikake, K.3    Yoshizaki, H.4    Kiyokawa, E.5    Matsuda, M.6
  • 122
    • 78149273391 scopus 로고    scopus 로고
    • Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Foster resonance energy transfer (FRET) biosensor
    • doi: 10.1074/jbc.M110.153007
    • Nishioka, T., Frohman, M. A., Matsuda, M., and Kiyokawa, E. (2010). Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Foster resonance energy transfer (FRET) biosensor. J. Biol. Chem. 285, 35979-35987. doi: 10.1074/jbc.M110.153007
    • (2010) J. Biol. Chem. , vol.285 , pp. 35979-35987
    • Nishioka, T.1    Frohman, M.A.2    Matsuda, M.3    Kiyokawa, E.4
  • 123
    • 34250885891 scopus 로고    scopus 로고
    • An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins
    • doi: 10.1110/ps.072845607
    • Ohashi, T., Galiacy, S. D., Briscoe, G., and Erickson, H. P. (2007). An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins. Protein Sci. 16, 1429-1438. doi: 10.1110/ps.072845607
    • (2007) Protein Sci. , vol.16 , pp. 1429-1438
    • Ohashi, T.1    Galiacy, S.D.2    Briscoe, G.3    Erickson, H.P.4
  • 124
    • 84871162013 scopus 로고    scopus 로고
    • Genetically encoded green fluorescent Ca2+ indicators with improved detectability for neuronal Ca2+ signals
    • doi: 10.1371/journal.pone.0051286
    • Ohkura, M., Sasaki, T., Sadakari, J., Gengyo-Ando, K., Kagawa-Nagamura, Y., Kobayashi, C., et al. (2012). Genetically encoded green fluorescent Ca2+ indicators with improved detectability for neuronal Ca2+ signals. PLoS ONE 7:e51286. doi: 10.1371/journal.pone.0051286
    • (2012) PLoS ONE , vol.7
    • Ohkura, M.1    Sasaki, T.2    Sadakari, J.3    Gengyo-Ando, K.4    Kagawa-Nagamura, Y.5    Kobayashi, C.6
  • 125
    • 2342552557 scopus 로고    scopus 로고
    • PtdIns(3 4, 5)P3 binding is necessary for WAVE2-induced formation of lamellipodia
    • doi: 10.1038/ncb1125
    • Oikawa, T., Yamaguchi, H., Itoh, T., Kato, M., Ijuin, T., Yamazaki, D., et al. (2004). PtdIns(3 4, 5)P3 binding is necessary for WAVE2-induced formation of lamellipodia. Nat. Cell Biol. 6, 420-426. doi: 10.1038/ncb1125
    • (2004) Nat. Cell Biol. , vol.6 , pp. 420-426
    • Oikawa, T.1    Yamaguchi, H.2    Itoh, T.3    Kato, M.4    Ijuin, T.5    Yamazaki, D.6
  • 126
    • 74049108643 scopus 로고    scopus 로고
    • The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: A potential molecular identity of a synaptic tag?
    • doi: 10.1152/physiol.00029.2009
    • Okamoto, K., Bosch, M., and Hayashi, Y. (2009). The roles of CaMKII and F-actin in the structural plasticity of dendritic spines: a potential molecular identity of a synaptic tag? Physiology (Bethesda) 24, 357-366. doi: 10.1152/physiol.00029.2009
    • (2009) Physiology (Bethesda) , vol.24 , pp. 357-366
    • Okamoto, K.1    Bosch, M.2    Hayashi, Y.3
  • 127
    • 34548773976 scopus 로고    scopus 로고
    • Visualization of F-actin and G-actin equilibrium using fluorescence resonance energy transfer (FRET) in cultured cells and neurons in slices
    • doi: 10.1038/nprot.2006.122
    • Okamoto, K., and Hayashi, Y. (2006). Visualization of F-actin and G-actin equilibrium using fluorescence resonance energy transfer (FRET) in cultured cells and neurons in slices. Nat. Protoc. 1, 911-919. doi: 10.1038/nprot.2006.122
    • (2006) Nat. Protoc. , vol.1 , pp. 911-919
    • Okamoto, K.1    Hayashi, Y.2
  • 128
    • 7044267351 scopus 로고    scopus 로고
    • Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity
    • doi: 10.1038/nn1311
    • Okamoto, K., Nagai, T., Miyawaki, A., and Hayashi, Y. (2004). Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nat. Neurosci. 7, 1104-1112. doi: 10.1038/nn1311
    • (2004) Nat. Neurosci. , vol.7 , pp. 1104-1112
    • Okamoto, K.1    Nagai, T.2    Miyawaki, A.3    Hayashi, Y.4
  • 129
    • 34547523623 scopus 로고    scopus 로고
    • The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure
    • doi: 10.1073/pnas.0701656104
    • Okamoto, K., Narayanan, R., Lee, S. H., Murata, K., and Hayashi, Y. (2007). The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure. Proc. Natl. Acad. Sci. U.S.A. 104, 6418-6423. doi: 10.1073/pnas.0701656104
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 6418-6423
    • Okamoto, K.1    Narayanan, R.2    Lee, S.H.3    Murata, K.4    Hayashi, Y.5
  • 130
    • 20844449080 scopus 로고    scopus 로고
    • Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors
    • doi: 10.1073/pnas.0503274102
    • Okumoto, S., Looger, L. L., Micheva, K. D., Reimer, R. J., Smith, S. J., and Frommer, W. B. (2005). Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors. Proc. Natl. Acad. Sci. U.S.A. 102, 8740-8745. doi: 10.1073/pnas.0503274102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8740-8745
    • Okumoto, S.1    Looger, L.L.2    Micheva, K.D.3    Reimer, R.J.4    Smith, S.J.5    Frommer, W.B.6
  • 131
    • 0037069360 scopus 로고    scopus 로고
    • Confirmation by FRET in individual living cells of the absence of significant amyloid beta-mediated caspase 8 activation
    • doi: 10.1073/pnas.232177599
    • Onuki, R., Nagasaki, A., Kawasaki, H., Baba, T., Uyeda, T. Q., and Taira, K. (2002). Confirmation by FRET in individual living cells of the absence of significant amyloid beta-mediated caspase 8 activation. Proc. Natl. Acad. Sci. U.S.A. 99, 14716-14721. doi: 10.1073/pnas.232177599
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14716-14721
    • Onuki, R.1    Nagasaki, A.2    Kawasaki, H.3    Baba, T.4    Uyeda, T.Q.5    Taira, K.6
  • 132
    • 47749090496 scopus 로고    scopus 로고
    • Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging
    • doi: 10.1074/jbc.M709872200
    • Ouyang, M., Lu, S., Li, X. Y., Xu, J., Seong, J., Giepmans, B. N., et al. (2008). Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging. J. Biol. Chem. 283, 17740-17748. doi: 10.1074/jbc.M709872200
    • (2008) J. Biol. Chem. , vol.283 , pp. 17740-17748
    • Ouyang, M.1    Lu, S.2    Li, X.Y.3    Xu, J.4    Seong, J.5    Giepmans, B.N.6
  • 133
    • 66149139873 scopus 로고    scopus 로고
    • Dynamic conformational changes in the FERM domain of FAK are involved in focal-adhesion behavior during cell spreading and motility
    • doi: 10.1242/jcs.028738
    • Papusheva, E., Mello de Queiroz, F., Dalous, J., Han, Y., Esposito, A., Jares-Erijmanxa, E. A., et al. (2009). Dynamic conformational changes in the FERM domain of FAK are involved in focal-adhesion behavior during cell spreading and motility. J. Cell. Sci. 122, 656-666. doi: 10.1242/jcs.028738
    • (2009) J. Cell. Sci. , vol.122 , pp. 656-666
    • Papusheva, E.1    Mello de Queiroz, F.2    Dalous, J.3    Han, Y.4    Esposito, A.5    Jares-Erijmanxa, E.A.6
  • 134
    • 69949177832 scopus 로고    scopus 로고
    • Dissecting activation of the PAK1 kinase at protrusions in living cells
    • doi: 10.1074/jbc.M109.015271
    • Parrini, M. C., Camonis, J., Matsuda, M., and de Gunzburg, J. (2009). Dissecting activation of the PAK1 kinase at protrusions in living cells. J. Biol. Chem. 284, 24133-24143. doi: 10.1074/jbc.M109.015271
    • (2009) J. Biol. Chem. , vol.284 , pp. 24133-24143
    • Parrini, M.C.1    Camonis, J.2    Matsuda, M.3    de Gunzburg, J.4
  • 135
    • 0034773788 scopus 로고    scopus 로고
    • Some forms of cAMP-mediated long-lasting potentiation are associated with release of BDNF and nuclear translocation of phospho-MAP kinase
    • doi: 10.1016/S0896-6273(01)00443-3
    • Patterson, S. L., Pittenger, C., Morozov, A., Martin, K. C., Scanlin, H., Drake, C., et al. (2001). Some forms of cAMP-mediated long-lasting potentiation are associated with release of BDNF and nuclear translocation of phospho-MAP kinase. Neuron 32, 123-140. doi: 10.1016/S0896-6273(01)00443-3
    • (2001) Neuron , vol.32 , pp. 123-140
    • Patterson, S.L.1    Pittenger, C.2    Morozov, A.3    Martin, K.C.4    Scanlin, H.5    Drake, C.6
  • 136
    • 79960490475 scopus 로고    scopus 로고
    • Rapid development of genetically encoded FRET reporters
    • doi: 10.1021/cb100402n
    • Piljic, A., de Diego, I., Wilmanns, M., and Schultz, C. (2011). Rapid development of genetically encoded FRET reporters. ACS Chem. Biol. 6, 685-691. doi: 10.1021/cb100402n
    • (2011) ACS Chem. Biol. , vol.6 , pp. 685-691
    • Piljic, A.1    de Diego, I.2    Wilmanns, M.3    Schultz, C.4
  • 137
    • 45249124996 scopus 로고    scopus 로고
    • A novel ZAP-70 dependent FRET based biosensor reveals kinase activity at both the immunological synapse and the antisynapse
    • doi: 10.1371/journal.pone.0001521
    • Randriamampita, C., Mouchacca, P., Malissen, B., Marguet, D., Trautmann, A., and Lellouch, A. C. (2008). A novel ZAP-70 dependent FRET based biosensor reveals kinase activity at both the immunological synapse and the antisynapse. PLoS ONE 3:e1521. doi: 10.1371/journal.pone.0001521
    • (2008) PLoS ONE , vol.3
    • Randriamampita, C.1    Mouchacca, P.2    Malissen, B.3    Marguet, D.4    Trautmann, A.5    Lellouch, A.C.6
  • 138
    • 33745659186 scopus 로고    scopus 로고
    • Optimization of pairings and detection conditions for measurement of FRET between cyan and yellow fluorescent proteins
    • doi: 10.1017/S1431927606060235
    • Rizzo, M. A., Springer, G., Segawa, K., Zipfel, W. R., and Piston, D. W. (2006). Optimization of pairings and detection conditions for measurement of FRET between cyan and yellow fluorescent proteins. Microsc. Microanal. 12, 238-254. doi: 10.1017/S1431927606060235
    • (2006) Microsc. Microanal. , vol.12 , pp. 238-254
    • Rizzo, M.A.1    Springer, G.2    Segawa, K.3    Zipfel, W.R.4    Piston, D.W.5
  • 139
    • 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., and Piston, D. W. (2004). An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449. doi: 10.1038/nbt945
    • (2004) Nat. Biotechnol. , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 140
    • 0033152333 scopus 로고    scopus 로고
    • The mitogen-activated protein kinase cascade couples PKA and PKC to cAMP response element binding protein phosphorylation in area CA1 of hippocampus
    • Roberson, E. D., English, J. D., Adams, J. P., Selcher, J. C., Kondratick, C., and Sweatt, J. D. (1999). The mitogen-activated protein kinase cascade couples PKA and PKC to cAMP response element binding protein phosphorylation in area CA1 of hippocampus. J. Neurosci. 19, 4337-4348.
    • (1999) J. Neurosci. , vol.19 , pp. 4337-4348
    • Roberson, E.D.1    English, J.D.2    Adams, J.P.3    Selcher, J.C.4    Kondratick, C.5    Sweatt, J.D.6
  • 141
    • 0034912282 scopus 로고    scopus 로고
    • Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein
    • doi: 10.1046/j.0953-816x.2001.01617.x
    • Sakai, R., Repunte-Canonigo, V., Raj, C. D., and Knöpfel, T. (2001). Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein. Eur. J. Neurosci. 13, 2314-2318. doi: 10.1046/j.0953-816x.2001.01617.x
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 2314-2318
    • Sakai, R.1    Repunte-Canonigo, V.2    Raj, C.D.3    Knöpfel, T.4
  • 142
    • 0033365730 scopus 로고    scopus 로고
    • Can molecules explain long-term potentiation?
    • doi: 10.1038/10154
    • Sanes, J. R., and Lichtman, J. W. (1999). Can molecules explain long-term potentiation? Nat. Neurosci. 2, 597-604. doi: 10.1038/10154
    • (1999) Nat. Neurosci. , vol.2 , pp. 597-604
    • Sanes, J.R.1    Lichtman, J.W.2
  • 143
    • 84865330853 scopus 로고    scopus 로고
    • The Ca2+ and Rho GTPase signaling pathways underlying activity-dependent actin remodeling at dendritic spines
    • doi: 10.1002/cm.21037
    • Saneyoshi, T., and Hayashi, Y. (2012). The Ca2+ and Rho GTPase signaling pathways underlying activity-dependent actin remodeling at dendritic spines. Cytoskeleton (Hoboken) 69, 545-554. doi: 10.1002/cm.21037
    • (2012) Cytoskeleton (Hoboken) , vol.69 , pp. 545-554
    • Saneyoshi, T.1    Hayashi, Y.2
  • 144
    • 70349494059 scopus 로고    scopus 로고
    • Real-time imaging of histone H4 hyperacetylation in living cells
    • doi: 10.1073/pnas.0902150106
    • Sasaki, K., Ito, T., Nishino, N., Khochbin, S., and Yoshida, M. (2009). Real-time imaging of histone H4 hyperacetylation in living cells. Proc. Natl. Acad. Sci. U.S.A. 106, 16257-16262. doi: 10.1073/pnas.0902150106
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16257-16262
    • Sasaki, K.1    Ito, T.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5
  • 145
    • 0042733215 scopus 로고    scopus 로고
    • Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells
    • doi: 10.1074/jbc.M212167200
    • Sasaki, K., Sato, M., and Umezawa, Y. (2003). Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells. J. Biol. Chem. 278, 30945-30951. doi: 10.1074/jbc.M212167200
    • (2003) J. Biol. Chem. , vol.278 , pp. 30945-30951
    • Sasaki, K.1    Sato, M.2    Umezawa, Y.3
  • 146
    • 0034671963 scopus 로고    scopus 로고
    • Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Ialpha and green fluorescent proteins
    • doi: 10.1021/ac0006167
    • Sato, M., Hida, N., Ozawa, T., and Umezawa, Y. (2000). Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Ialpha and green fluorescent proteins. Anal. Chem. 72, 5918-5924. doi: 10.1021/ac0006167
    • (2000) Anal. Chem. , vol.72 , pp. 5918-5924
    • Sato, M.1    Hida, N.2    Ozawa, T.3    Umezawa, Y.4
  • 147
    • 33947361161 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells
    • doi: 10.1021/ac062171d
    • Sato, M., Kawai, Y., and Umezawa, Y. (2007). Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells. Anal. Chem. 79, 2570-2575. doi: 10.1021/ac062171d
    • (2007) Anal. Chem. , vol.79 , pp. 2570-2575
    • Sato, M.1    Kawai, Y.2    Umezawa, Y.3
  • 148
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • doi: 10.1038/nbt0302-287
    • Sato, M., Ozawa, T., Inukai, K., Asano, T., and Umezawa, Y. (2002). Fluorescent indicators for imaging protein phosphorylation in single living cells. Nat. Biotechnol. 20, 287-294. doi: 10.1038/nbt0302-287
    • (2002) Nat. Biotechnol. , vol.20 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 149
    • 23044505605 scopus 로고    scopus 로고
    • Locating inositol 1 4, 5-trisphosphate in the nucleus and neuronal dendrites with genetically encoded fluorescent indicators
    • doi: 10.1021/ac040195j
    • Sato, M., Ueda, Y., Shibuya, M., and Umezawa, Y. (2005a). Locating inositol 1 4, 5-trisphosphate in the nucleus and neuronal dendrites with genetically encoded fluorescent indicators. Anal. Chem. 77, 4751-4758. doi: 10.1021/ac040195j
    • (2005) Anal. Chem. , vol.77 , pp. 4751-4758
    • Sato, M.1    Ueda, Y.2    Shibuya, M.3    Umezawa, Y.4
  • 150
    • 26844450450 scopus 로고    scopus 로고
    • Imaging the nanomolar range of nitric oxide with an amplifier-coupled fluorescent indicator in living cells
    • doi: 10.1073/pnas.0505136102
    • Sato, M., Hida, N., and Umezawa, Y. (2005b). Imaging the nanomolar range of nitric oxide with an amplifier-coupled fluorescent indicator in living cells. Proc. Natl. Acad. Sci. U.S.A. 102, 14515-14520. doi: 10.1073/pnas.0505136102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14515-14520
    • Sato, M.1    Hida, N.2    Umezawa, Y.3
  • 151
    • 0242441598 scopus 로고    scopus 로고
    • Production of PtdInsP3 at endomembranes is triggered by receptor endocytosis
    • doi: 10.1038/ncb1054
    • Sato, M., Ueda, Y., Takagi, T., and Umezawa, Y. (2003). Production of PtdInsP3 at endomembranes is triggered by receptor endocytosis. Nat. Cell Biol. 5, 1016-1022. doi: 10.1038/ncb1054
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1016-1022
    • Sato, M.1    Ueda, Y.2    Takagi, T.3    Umezawa, Y.4
  • 152
    • 33748998746 scopus 로고    scopus 로고
    • Imaging diacylglycerol dynamics at organelle membranes
    • doi: 10.1038/nmeth930
    • Sato, M., Ueda, Y., and Umezawa, Y. (2006a). Imaging diacylglycerol dynamics at organelle membranes. Nat. Methods 3, 797-799. doi: 10.1038/nmeth930
    • (2006) Nat. Methods , vol.3 , pp. 797-799
    • Sato, M.1    Ueda, Y.2    Umezawa, Y.3
  • 153
    • 33845527724 scopus 로고    scopus 로고
    • Cell-based indicator to visualize picomolar dynamics of nitric oxide release from living cells
    • doi: 10.1021/ac061791b
    • Sato, M., Nakajima, T., Goto, M., and Umezawa, Y. (2006b). Cell-based indicator to visualize picomolar dynamics of nitric oxide release from living cells. Anal. Chem. 78, 8175-8182. doi: 10.1021/ac061791b
    • (2006) Anal. Chem. , vol.78 , pp. 8175-8182
    • Sato, M.1    Nakajima, T.2    Goto, M.3    Umezawa, Y.4
  • 154
    • 30944467113 scopus 로고    scopus 로고
    • A guide to choosing fluorescent proteins
    • doi: 10.1038/nmeth819
    • Shaner, N. C., Steinbach, P. A., and Tsien, R. Y. (2005). A guide to choosing fluorescent proteins. Nat. Methods 2, 905-909. doi: 10.1038/nmeth819
    • (2005) Nat. Methods , vol.2 , pp. 905-909
    • Shaner, N.C.1    Steinbach, P.A.2    Tsien, R.Y.3
  • 155
    • 84876294515 scopus 로고    scopus 로고
    • Visualization of an endogenous retinoic acid gradient across embryonic development
    • doi: 10.1038/nature12037
    • Shimozono, S., Iimura, T., Kitaguchi, T., Higashijima, S., and Miyawaki, A. (2013). Visualization of an endogenous retinoic acid gradient across embryonic development. Nature 496, 363-366. doi: 10.1038/nature12037
    • (2013) Nature , vol.496 , pp. 363-366
    • Shimozono, S.1    Iimura, T.2    Kitaguchi, T.3    Higashijima, S.4    Miyawaki, A.5
  • 156
    • 0037129193 scopus 로고    scopus 로고
    • SWAP-70 is a guanine-nucleotide-exchange factor that mediates signalling of membrane ruffling
    • doi: 10.1038/416759a
    • Shinohara, M., Terada, Y., Iwamatsu, A., Shinohara, A., Mochizuki, N., Higuchi, M., et al. (2002). SWAP-70 is a guanine-nucleotide-exchange factor that mediates signalling of membrane ruffling. Nature 416, 759-763. doi: 10.1038/416759a
    • (2002) Nature , vol.416 , pp. 759-763
    • Shinohara, M.1    Terada, Y.2    Iwamatsu, A.3    Shinohara, A.4    Mochizuki, N.5    Higuchi, M.6
  • 157
    • 2442614163 scopus 로고    scopus 로고
    • Trans-endocytosis via spinules in adult rat hippocampus
    • doi: 10.1523/JNEUROSCI.0287-04.2004
    • Spacek, J., and Harris, K. M. (2004). Trans-endocytosis via spinules in adult rat hippocampus. J. Neurosci. 24, 4233-4241. doi: 10.1523/JNEUROSCI.0287-04.2004
    • (2004) J. Neurosci. , vol.24 , pp. 4233-4241
    • Spacek, J.1    Harris, K.M.2
  • 158
    • 0036176244 scopus 로고    scopus 로고
    • Rapid turnover of actin in dendritic spines and its regulation by activity
    • doi: 10.1038/nn811
    • Star, E. N., Kwiatkowski, D. J., and Murthy, V. N. (2002). Rapid turnover of actin in dendritic spines and its regulation by activity. Nat. Neurosci. 5, 239-246. doi: 10.1038/nn811
    • (2002) Nat. Neurosci. , vol.5 , pp. 239-246
    • Star, E.N.1    Kwiatkowski, D.J.2    Murthy, V.N.3
  • 159
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • doi: 10.1146/annurev.bi.47.070178.004131
    • Stryer, L. (1978). Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819-846. doi: 10.1146/annurev.bi.47.070178.004131
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 160
    • 0032569898 scopus 로고    scopus 로고
    • Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps
    • doi: 10.1038/24640
    • Suzuki, Y., Yasunaga, T., Ohkura, R., Wakabayashi, T., and Sutoh, K. (1998). Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps. Nature 396, 380-383. doi: 10.1038/24640
    • (1998) Nature , vol.396 , pp. 380-383
    • Suzuki, Y.1    Yasunaga, T.2    Ohkura, R.3    Wakabayashi, T.4    Sutoh, K.5
  • 161
    • 16244382837 scopus 로고    scopus 로고
    • Visualization of synaptic Ca2+/calmodulin-dependent protein kinase II activity in living neurons
    • doi: 10.1523/JNEUROSCI.0085-05.2005
    • Takao, K., Okamoto, K., Nakagawa, T., Neve, R. L., Nagai, T., Miyawaki, A., et al. (2005). Visualization of synaptic Ca2+/calmodulin-dependent protein kinase II activity in living neurons. J. Neurosci. 25, 3107-3112. doi: 10.1523/JNEUROSCI.0085-05.2005
    • (2005) J. Neurosci. , vol.25 , pp. 3107-3112
    • Takao, K.1    Okamoto, K.2    Nakagawa, T.3    Neve, R.L.4    Nagai, T.5    Miyawaki, A.6
  • 162
    • 2542476025 scopus 로고    scopus 로고
    • RalA activation at nascent lamellipodia of epidermal growth factor-stimulated Cos7 cells and migrating Madin-Darby canine kidney cells
    • doi: 10.1091/mbc.E03-11-0857
    • Takaya, A., Ohba, Y., Kurokawa, K., and Matsuda, M. (2004). RalA activation at nascent lamellipodia of epidermal growth factor-stimulated Cos7 cells and migrating Madin-Darby canine kidney cells. Mol. Biol. Cell 15, 2549-2557. doi: 10.1091/mbc.E03-11-0857
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2549-2557
    • Takaya, A.1    Ohba, Y.2    Kurokawa, K.3    Matsuda, M.4
  • 163
    • 4644260485 scopus 로고    scopus 로고
    • Fluorescent biosensor for quantitative real-time measurements of inositol 1 4, 5-trisphosphate in single living cells
    • doi: 10.1074/jbc.C400312200
    • Tanimura, A., Nezu, A., Morita, T., Turner, R. J., and Tojyo, Y. (2004). Fluorescent biosensor for quantitative real-time measurements of inositol 1 4, 5-trisphosphate in single living cells. J. Biol. Chem. 279, 38095-38098. doi: 10.1074/jbc.C400312200
    • (2004) J. Biol. Chem. , vol.279 , pp. 38095-38098
    • Tanimura, A.1    Nezu, A.2    Morita, T.3    Turner, R.J.4    Tojyo, Y.5
  • 164
    • 0033807686 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology by the rho family of small GTPases: Antagonistic roles of Rac and Rho
    • doi: 10.1093/cercor/10.10.927
    • Tashiro, A., Minden, A., and Yuste, R. (2000). Regulation of dendritic spine morphology by the rho family of small GTPases: antagonistic roles of Rac and Rho. Cereb. Cortex 10, 927-938. doi: 10.1093/cercor/10.10.927
    • (2000) Cereb. Cortex , vol.10 , pp. 927-938
    • Tashiro, A.1    Minden, A.2    Yuste, R.3
  • 165
    • 16844385887 scopus 로고    scopus 로고
    • Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase
    • doi: 10.1038/sj.embor.7400349
    • Terai, K., and Matsuda, M. (2005). Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase. EMBO Rep. 6, 251-255. doi: 10.1038/sj.embor.7400349
    • (2005) EMBO Rep. , vol.6 , pp. 251-255
    • Terai, K.1    Matsuda, M.2
  • 166
    • 33747615527 scopus 로고    scopus 로고
    • The amino-terminal B-Raf-specific region mediates calcium-dependent homo-and hetero-dimerization of Raf
    • doi: 10.1038/sj.emboj.7601241
    • Terai, K., and Matsuda, M. (2006). The amino-terminal B-Raf-specific region mediates calcium-dependent homo-and hetero-dimerization of Raf. EMBO J. 25, 3556-3564. doi: 10.1038/sj.emboj.7601241
    • (2006) EMBO J. , vol.25 , pp. 3556-3564
    • Terai, K.1    Matsuda, M.2
  • 167
    • 0035447056 scopus 로고    scopus 로고
    • Crystal structure of the phosphatidylinositol 3, 4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): Molecular basis of lipid specificity
    • doi: 10.1042/0264-6021:3580287
    • Thomas, C. C., Dowler, S., Deak, M., Alessi, D. R., and van Aalten, D. M. (2001). Crystal structure of the phosphatidylinositol 3, 4-bisphosphate-binding pleckstrin homology (PH) domain of tandem PH-domain-containing protein 1 (TAPP1): molecular basis of lipid specificity. Biochem. J. 358, 287-294. doi: 10.1042/0264-6021:3580287
    • (2001) Biochem. J. , vol.358 , pp. 287-294
    • Thomas, C.C.1    Dowler, S.2    Deak, M.3    Alessi, D.R.4    van Aalten, D.M.5
  • 168
    • 84881661965 scopus 로고    scopus 로고
    • Transgenic Mice for cGMP Imaging
    • doi: 10.1161/CIRCRESAHA.113.301063
    • Thunemann, M., Wen, L., Hillenbrand, M., Vachaviolos, A., Feil, S., Ott, T., et al. (2013). Transgenic Mice for cGMP Imaging. Circ. Res. 113, 365-371. doi: 10.1161/CIRCRESAHA.113.301063
    • (2013) Circ. Res. , vol.113 , pp. 365-371
    • Thunemann, M.1    Wen, L.2    Hillenbrand, M.3    Vachaviolos, A.4    Feil, S.5    Ott, T.6
  • 169
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • doi: 10.1073/pnas.211564598
    • Ting, A. Y., Kain, K. H., Klemke, R. L., and Tsien, R. Y. (2001). Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl. Acad. Sci. U.S.A. 98, 15003-15008. doi: 10.1073/pnas.211564598
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 170
    • 71949090473 scopus 로고    scopus 로고
    • Stimulus-specific distinctions in spatial and temporal dynamics of stress-activated protein kinase kinase kinases revealed by a fluorescence resonance energy transfer biosensor
    • doi: 10.1128/MCB.00571-09
    • Tomida, T., Takekawa, M., O'Grady, P., and Saito, H. (2009). Stimulus-specific distinctions in spatial and temporal dynamics of stress-activated protein kinase kinase kinases revealed by a fluorescence resonance energy transfer biosensor. Mol. Cell. Biol. 29, 6117-6127. doi: 10.1128/MCB.00571-09
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6117-6127
    • Tomida, T.1    Takekawa, M.2    O'Grady, P.3    Saito, H.4
  • 171
    • 48449091054 scopus 로고    scopus 로고
    • Improving membrane voltage measurements using FRET with new fluorescent proteins
    • doi: 10.1038/nmeth.1235
    • Tsutsui, H., Karasawa, S., Okamura, Y., and Miyawaki, A. (2008). Improving membrane voltage measurements using FRET with new fluorescent proteins. Nat. Methods 5, 683-685. doi: 10.1038/nmeth.1235
    • (2008) Nat. Methods , vol.5 , pp. 683-685
    • Tsutsui, H.1    Karasawa, S.2    Okamura, Y.3    Miyawaki, A.4
  • 172
    • 78649650268 scopus 로고    scopus 로고
    • Real-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia
    • doi: 10.1158/1535-7163.MCT-10-0623
    • Tunceroglu, A., Matsuda, M., and Birge, R. B. (2010). Real-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia. Mol. Cancer Ther. 9, 3065-3073. doi: 10.1158/1535-7163.MCT-10-0623
    • (2010) Mol. Cancer Ther. , vol.9 , pp. 3065-3073
    • Tunceroglu, A.1    Matsuda, M.2    Birge, R.B.3
  • 173
    • 84880469585 scopus 로고    scopus 로고
    • PIP3 regulates spinule formation in dendritic spines during structural long-term potentiation
    • doi: 10.1523/JNEUROSCI.3122-12.2013
    • Ueda, Y., and Hayashi, Y. (2013). PIP3 regulates spinule formation in dendritic spines during structural long-term potentiation. J. Neurosci. 33, 11040-11047. doi: 10.1523/JNEUROSCI.3122-12.2013
    • (2013) J. Neurosci. , vol.33 , pp. 11040-11047
    • Ueda, Y.1    Hayashi, Y.2
  • 174
    • 70849116652 scopus 로고    scopus 로고
    • Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio
    • doi: 10.1371/journal.pone.0007893
    • Uemura, K., Lill, C. M., Li, X., Peters, J. A., Ivanov, A., Fan, Z., et al. (2009). Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio. PLoS ONE 4:e7893. doi: 10.1371/journal.pone.0007893
    • (2009) PLoS ONE , vol.4
    • Uemura, K.1    Lill, C.M.2    Li, X.3    Peters, J.A.4    Ivanov, A.5    Fan, Z.6
  • 175
    • 0034094370 scopus 로고    scopus 로고
    • Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer
    • doi: 10.1073/pnas.040565597
    • Vanderklish, P. W., Krushel, L. A., Holst, B. H., Gally, J. A., Crossin, K. L., and Edelman, G. M. (2000). Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. U.S.A. 97, 2253-2258. doi: 10.1073/pnas.040565597
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2253-2258
    • Vanderklish, P.W.1    Krushel, L.A.2    Holst, B.H.3    Gally, J.A.4    Crossin, K.L.5    Edelman, G.M.6
  • 177
    • 5444268133 scopus 로고    scopus 로고
    • SynGAP regulates spine formation
    • doi: 10.1523/JNEUROSCI.3213-04.2004
    • Vazquez, L. E., Chen, H. J., Sokolova, I., Knuesel, I., and Kennedy, M. B. (2004). SynGAP regulates spine formation. J. Neurosci. 24, 8862-8872. doi: 10.1523/JNEUROSCI.3213-04.2004
    • (2004) J. Neurosci. , vol.24 , pp. 8862-8872
    • Vazquez, L.E.1    Chen, H.J.2    Sokolova, I.3    Knuesel, I.4    Kennedy, M.B.5
  • 178
    • 0038729670 scopus 로고    scopus 로고
    • Measurement of the millisecond activation switch of G protein-coupled receptors in living cells
    • doi: 10.1038/nbt838
    • Vilardaga, J. P., Bunemann, M., Krasel, C., Castro, M., and Lohse, M. J. (2003). Measurement of the millisecond activation switch of G protein-coupled receptors in living cells. Nat. Biotechnol. 21, 807-812. doi: 10.1038/nbt838
    • (2003) Nat. Biotechnol. , vol.21 , pp. 807-812
    • Vilardaga, J.P.1    Bunemann, M.2    Krasel, C.3    Castro, M.4    Lohse, M.J.5
  • 179
    • 70349621400 scopus 로고    scopus 로고
    • Genetically encoded FRET sensors to monitor intracellular Zn2+ homeostasis
    • doi: 10.1038/nmeth.1368
    • Vinkenborg, J. L., Nicolson, T. J., Bellomo, E. A., Koay, M. S., Rutter, G. A., and Merkx, M. (2009). Genetically encoded FRET sensors to monitor intracellular Zn2+ homeostasis. Nat. Methods 6, 737-740. doi: 10.1038/nmeth.1368
    • (2009) Nat. Methods , vol.6 , pp. 737-740
    • Vinkenborg, J.L.1    Nicolson, T.J.2    Bellomo, E.A.3    Koay, M.S.4    Rutter, G.A.5    Merkx, M.6
  • 180
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • doi: 10.1083/jcb.200302125
    • Violin, J. D., Zhang, J., Tsien, R. Y., and Newton, A. C. (2003). A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J. Cell Biol. 161, 899-909. doi: 10.1083/jcb.200302125
    • (2003) J. Cell Biol. , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 181
    • 50849145148 scopus 로고    scopus 로고
    • Single-spike detection in vitro and in vivo with a genetic Ca2+ sensor
    • doi: 10.1038/nmeth.1242
    • Wallace, D. J., Meyer zum Alten Borgloh, S., Astori, S., Yang, Y., Bausen, M., Kugler, S., et al. (2008). Single-spike detection in vitro and in vivo with a genetic Ca2+ sensor. Nat. Methods 5, 797-804. doi: 10.1038/nmeth.1242
    • (2008) Nat. Methods , vol.5 , pp. 797-804
    • Wallace, D.J.1    Meyer zum Alten Borgloh, S.2    Astori, S.3    Yang, Y.4    Bausen, M.5    Kugler, S.6
  • 182
    • 0035425948 scopus 로고    scopus 로고
    • Arg3.1/Arc mRNA induction by Ca2+ and cAMP requires protein kinase A and mitogen-activated protein kinase/extracellular regulated kinase activation
    • Waltereit, R., Dammermann, B., Wulff, P., Scafidi, J., Staubli, U., Kauselmann, G., et al. (2001). Arg3.1/Arc mRNA induction by Ca2+ and cAMP requires protein kinase A and mitogen-activated protein kinase/extracellular regulated kinase activation. J. Neurosci. 21, 5484-5493.
    • (2001) J. Neurosci. , vol.21 , pp. 5484-5493
    • Waltereit, R.1    Dammermann, B.2    Wulff, P.3    Scafidi, J.4    Staubli, U.5    Kauselmann, G.6
  • 183
    • 84870516449 scopus 로고    scopus 로고
    • Hybrid voltage sensor imaging of electrical activity from neurons in hippocampal slices from transgenic mice
    • doi: 10.1152/jn.00722.2012
    • Wang, D., McMahon, S., Zhang, Z., and Jackson, M. B. (2012). Hybrid voltage sensor imaging of electrical activity from neurons in hippocampal slices from transgenic mice. J. Neurophysiol. 108, 3147-3160. doi: 10.1152/jn.00722.2012
    • (2012) J. Neurophysiol. , vol.108 , pp. 3147-3160
    • Wang, D.1    McMahon, S.2    Zhang, Z.3    Jackson, M.B.4
  • 184
    • 17844388845 scopus 로고    scopus 로고
    • Visualizing the mechanical activation of Src
    • doi: 10.1038/nature03469
    • Wang, Y., Botvinick, E. L., Zhao, Y., Berns, M. W., Usami, S., Tsien, R. Y., et al. (2005). Visualizing the mechanical activation of Src. Nature 434, 1040-1045. doi: 10.1038/nature03469
    • (2005) Nature , vol.434 , pp. 1040-1045
    • Wang, Y.1    Botvinick, E.L.2    Zhao, Y.3    Berns, M.W.4    Usami, S.5    Tsien, R.Y.6
  • 185
    • 0742305684 scopus 로고    scopus 로고
    • Visualization of spatially and temporally regulated N-WASP activity during cytoskeletal reorganization in living cells
    • doi: 10.1073/pnas.0306258101
    • Ward, M. E., Wu, J. Y., and Rao, Y. (2004). Visualization of spatially and temporally regulated N-WASP activity during cytoskeletal reorganization in living cells. Proc. Natl. Acad. Sci. U.S.A. 101, 970-974. doi: 10.1073/pnas.0306258101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 970-974
    • Ward, M.E.1    Wu, J.Y.2    Rao, Y.3
  • 186
    • 0035140593 scopus 로고    scopus 로고
    • Spaced stimuli stabilize MAPK pathway activation and its effects on dendritic morphology
    • doi: 10.1038/83976
    • Wu, G. Y., Deisseroth, K., and Tsien, R. W. (2001). Spaced stimuli stabilize MAPK pathway activation and its effects on dendritic morphology. Nat. Neurosci. 4, 151-158. doi: 10.1038/83976
    • (2001) Nat. Neurosci. , vol.4 , pp. 151-158
    • Wu, G.Y.1    Deisseroth, K.2    Tsien, R.W.3
  • 187
    • 0032522223 scopus 로고    scopus 로고
    • Detection of programmed cell death using fluorescence energy transfer
    • doi: 10.1093/nar/26.8.2034
    • Xu, X., Gerard, A. L., Huang, B. C., Anderson, D. C., Payan, D. G., and Luo, Y. (1998). Detection of programmed cell death using fluorescence energy transfer. Nucleic Acids Res. 26, 2034-2035. doi: 10.1093/nar/26.8.2034
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2034-2035
    • Xu, X.1    Gerard, A.L.2    Huang, B.C.3    Anderson, D.C.4    Payan, D.G.5    Luo, Y.6
  • 188
    • 84862600723 scopus 로고    scopus 로고
    • Quantitative comparison of genetically encoded Ca indicators in cortical pyramidal cells and cerebellar Purkinje cells
    • doi: 10.3389/fncel.2011.00018
    • Yamada, Y., Michikawa, T., Hashimoto, M., Horikawa, K., Nagai, T., Miyawaki, A., et al. (2011). Quantitative comparison of genetically encoded Ca indicators in cortical pyramidal cells and cerebellar Purkinje cells. Front. Cell. Neurosci. 5:18. doi: 10.3389/fncel.2011.00018
    • (2011) Front. Cell. Neurosci. , vol.5 , pp. 18
    • Yamada, Y.1    Michikawa, T.2    Hashimoto, M.3    Horikawa, K.4    Nagai, T.5    Miyawaki, A.6
  • 189
    • 84855506461 scopus 로고    scopus 로고
    • Live imaging of apoptosis in a novel transgenic mouse highlights its role in neural tube closure
    • doi: 10.1083/jcb.201104057
    • Yamaguchi, Y., Shinotsuka, N., Nonomura, K., Takemoto, K., Kuida, K., Yosida, H., et al. (2011). Live imaging of apoptosis in a novel transgenic mouse highlights its role in neural tube closure. J. Cell Biol. 195, 1047-1060. doi: 10.1083/jcb.201104057
    • (2011) J. Cell Biol. , vol.195 , pp. 1047-1060
    • Yamaguchi, Y.1    Shinotsuka, N.2    Nonomura, K.3    Takemoto, K.4    Kuida, K.5    Yosida, H.6
  • 190
    • 33847080456 scopus 로고    scopus 로고
    • Detection of MMP activity in living cells by a genetically encoded surface-displayed FRET sensor
    • doi: 10.1016/j.bbamcr.2006.11.002
    • Yang, J., Zhang, Z., Lin, J., Lu, J., Liu, B. F., Zeng, S., et al. (2007). Detection of MMP activity in living cells by a genetically encoded surface-displayed FRET sensor. Biochim. Biophys. Acta 1773, 400-407. doi: 10.1016/j.bbamcr.2006.11.002
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 400-407
    • Yang, J.1    Zhang, Z.2    Lin, J.3    Lu, J.4    Liu, B.F.5    Zeng, S.6
  • 191
    • 77955301626 scopus 로고    scopus 로고
    • A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes
    • doi: 10.1128/MCB.00121-10
    • Yano, T., Oku, M., Akeyama, N., Itoyama, A., Yurimoto, H., Kuge, S., et al. (2010). A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes. Mol. Cell. Biol. 30 3758-3766. doi: 10.1128/MCB.00121-10
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3758-3766
    • Yano, T.1    Oku, M.2    Akeyama, N.3    Itoyama, A.4    Yurimoto, H.5    Kuge, S.6
  • 192
    • 33749054066 scopus 로고    scopus 로고
    • Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy
    • doi: 10.1016/j.conb.2006.08.012
    • Yasuda, R. (2006). Imaging spatiotemporal dynamics of neuronal signaling using fluorescence resonance energy transfer and fluorescence lifetime imaging microscopy. Curr. Opin. Neurobiol. 16, 551-561. doi: 10.1016/j.conb.2006.08.012
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 551-561
    • Yasuda, R.1
  • 193
    • 84867596381 scopus 로고    scopus 로고
    • Studying signal transduction in single dendritic spines
    • doi: 10.1101/cshperspect.a005611
    • Yasuda, R. (2012). Studying signal transduction in single dendritic spines. Cold Spring Harb. Perspect. Biol. 4, 005611. doi: 10.1101/cshperspect.a005611
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. 005611
    • Yasuda, R.1
  • 194
    • 31544462618 scopus 로고    scopus 로고
    • Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging
    • doi: 10.1038/nn1635
    • Yasuda, R., Harvey, C. D., Zhong, H., Sobczyk, A., van Aelst, L., and Svoboda, K. (2006). Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging. Nat. Neurosci. 9, 283-291. doi: 10.1038/nn1635
    • (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
  • 195
    • 0042672950 scopus 로고    scopus 로고
    • Activity of Rho-family GTPases during cell division as visualized with FRET-based probes
    • doi: 10.1083/jcb.200212049
    • Yoshizaki, H., Ohba, Y., Kurokawa, K., Itoh, R. E., Nakamura, T., Mochizuki, N., et al. (2003). Activity of Rho-family GTPases during cell division as visualized with FRET-based probes. J. Cell Biol. 162, 223-232. doi: 10.1083/jcb.200212049
    • (2003) J. Cell Biol. , vol.162 , pp. 223-232
    • Yoshizaki, H.1    Ohba, Y.2    Kurokawa, K.3    Itoh, R.E.4    Nakamura, T.5    Mochizuki, N.6
  • 196
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • doi: 10.1126/science.1069982
    • Zaccolo, M., and Pozzan, T. (2002). Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science 295, 1711-1715. doi: 10.1126/science.1069982
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 197
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • doi: 10.1126/science.1068539
    • Zacharias, D. A., Violin, J. D., Newton, A. C., and Tsien, R. Y. (2002). Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916. doi: 10.1126/science.1068539
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 198
    • 33748253738 scopus 로고    scopus 로고
    • Resonance energy transfer between green fluorescent protein variants: Complexities revealed with myosin fusion proteins
    • doi: 10.1021/bi060943u
    • Zeng, W., Seward, H. E., Malnasi-Csizmadia, A., Wakelin, S., Woolley, R. J., Cheema, G. S., et al. (2006). Resonance energy transfer between green fluorescent protein variants: complexities revealed with myosin fusion proteins. Biochemistry 45, 10482-10491. doi: 10.1021/bi060943u
    • (2006) Biochemistry , vol.45 , pp. 10482-10491
    • Zeng, W.1    Seward, H.E.2    Malnasi-Csizmadia, A.3    Wakelin, S.4    Woolley, R.J.5    Cheema, G.S.6
  • 199
    • 33644747349 scopus 로고    scopus 로고
    • The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis
    • doi: 10.1038/ncb1368
    • Zhang, H., and Macara, I. G. (2006). The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis. Nat. Cell Biol. 8, 227-237. doi: 10.1038/ncb1368
    • (2006) Nat. Cell Biol. , vol.8 , pp. 227-237
    • Zhang, H.1    Macara, I.G.2
  • 200
    • 0036902813 scopus 로고    scopus 로고
    • Creating new fluorescent probes for cell biology
    • doi: 10.1038/nrm976
    • Zhang, J., Campbell, R. E., Ting, A. Y., and Tsien, R. Y. (2002). Creating new fluorescent probes for cell biology. Nat. Rev. Mol. Cell Biol. 3, 906-918. doi: 10.1038/nrm976
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 906-918
    • Zhang, J.1    Campbell, R.E.2    Ting, A.Y.3    Tsien, R.Y.4
  • 201
    • 77956695748 scopus 로고    scopus 로고
    • In vivo assessment of artery smooth muscle [Ca2+]i and MLCK activation in FRET-based biosensor mice
    • doi: 10.1152/ajpheart.00359.2010
    • Zhang, J., Chen, L., Raina, H., Blaustein, M. P., and Wier, W. G. (2010). In vivo assessment of artery smooth muscle [Ca2+]i and MLCK activation in FRET-based biosensor mice. Am. J. Physiol. Heart Circ. Physiol. 299, H946-H956. doi: 10.1152/ajpheart.00359.2010
    • (2010) Am. J. Physiol. Heart Circ. Physiol. , vol.299
    • Zhang, J.1    Chen, L.2    Raina, H.3    Blaustein, M.P.4    Wier, W.G.5
  • 202
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • doi: 10.1073/pnas.211566798
    • Zhang, J., Ma, Y., Taylor, S. S., and Tsien, R. Y. (2001). Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl. Acad. Sci. U.S.A. 98, 14997-15002. doi: 10.1073/pnas.211566798
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14997-15002
    • Zhang, J.1    Ma, Y.2    Taylor, S.S.3    Tsien, R.Y.4
  • 203
    • 80053371503 scopus 로고    scopus 로고
    • An expanded palette of genetically encoded Ca2+ indicators
    • doi: 10.1126/science.1208592
    • Zhao, Y., Araki, S., Wu, J., Teramoto, T., Chang, Y. F., Nakano, M., et al. (2011). An expanded palette of genetically encoded Ca2+ indicators. Science 333, 1888-1891. doi: 10.1126/science.1208592
    • (2011) Science , vol.333 , pp. 1888-1891
    • Zhao, Y.1    Araki, S.2    Wu, J.3    Teramoto, T.4    Chang, Y.F.5    Nakano, M.6
  • 204
    • 0037162696 scopus 로고    scopus 로고
    • Ras and Rap control AMPA receptor trafficking during synaptic plasticity
    • doi: 10.1016/S0092-8674(02)00897-8
    • Zhu, J. J., Qin, Y., Zhao, M., Van Aelst, L., and Malinow, R. (2002). Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110, 443-455. doi: 10.1016/S0092-8674(02)00897-8
    • (2002) Cell , vol.110 , pp. 443-455
    • Zhu, J.J.1    Qin, Y.2    Zhao, M.3    Van Aelst, L.4    Malinow, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.