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Volumn 14, Issue 7, 2014, Pages 11691-11713

Engineering genetically encoded FRET sensors

Author keywords

Directed evolution; Fluorescent proteins; FRET; Multiparameter imaging; Protein engineering; Sensors

Indexed keywords

ENERGY TRANSFER; FLUORESCENCE; PROTEINS;

EID: 84903703514     PISSN: 14248220     EISSN: None     Source Type: Journal    
DOI: 10.3390/s140711691     Document Type: Review
Times cited : (75)

References (112)
  • 1
    • 77949900419 scopus 로고    scopus 로고
    • Fluorescent imaging of transition metal homeostasis using genetically encoded sensors
    • Vinkenborg, J.L.; Koay, M.S.; Merkx, M. Fluorescent imaging of transition metal homeostasis using genetically encoded sensors. Curr. Opin. Chem. Biol. 2010, 14, 231-237.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 231-237
    • Vinkenborg, J.L.1    Koay, M.S.2    Merkx, M.3
  • 2
    • 24344499212 scopus 로고    scopus 로고
    • Genetically encoded FRET sensors for visualizing metabolites with subcellular resolution in living cells
    • Looger, L.L.; Lalonde, S.; Frommer, W.B. Genetically encoded FRET sensors for visualizing metabolites with subcellular resolution in living cells. Plant Physiol. 2005, 138, 555-557.
    • (2005) Plant Physiol. , vol.138 , pp. 555-557
    • Looger, L.L.1    Lalonde, S.2    Frommer, W.B.3
  • 3
    • 84899572376 scopus 로고    scopus 로고
    • Fluorescent sensors for measuring metal ions in living systems
    • Carter, K.P.; Young, A.M.; Palmer, A.E. Fluorescent sensors for measuring metal ions in living systems. Chem. Rev. 2014, 114, 4564-4601.
    • (2014) Chem. Rev. , vol.114 , pp. 4564-4601
    • Carter, K.P.1    Young, A.M.2    Palmer, A.E.3
  • 4
    • 84897136274 scopus 로고    scopus 로고
    • Engineering and characterizing monomeric fluorescent proteins for live-cell imaging applications
    • Ai, H.W.; Baird, M.A.; Shen, Y.; Davidson, M.W.; Campbell, R.E. Engineering and characterizing monomeric fluorescent proteins for live-cell imaging applications. Nat. Protoc. 2014, 9, 910-928.
    • (2014) Nat. Protoc. , vol.9 , pp. 910-928
    • Ai, H.W.1    Baird, M.A.2    Shen, Y.3    Davidson, M.W.4    Campbell, R.E.5
  • 6
    • 84867746272 scopus 로고    scopus 로고
    • Red fluorescent proteins: Chromophore formation and cellular applications
    • Miyawaki, A.; Shcherbakova, D.M.; Verkhusha, V.V. Red fluorescent proteins: chromophore formation and cellular applications. Curr. Opin. Struct. Biol. 2012, 22, 679-688.
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 679-688
    • Miyawaki, A.1    Shcherbakova, D.M.2    Verkhusha, V.V.3
  • 7
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock, G.; De Angelis, D.A.; Rothman, J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 1998, 394, 192-195.
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 8
    • 0035502932 scopus 로고    scopus 로고
    • Shedding light on disulfide bond formation: Engineering a redox switch in green fluorescent protein
    • Ostergaard, H.; Henriksen, A.; Hansen, F.G.; Winther, J.R. Shedding light on disulfide bond formation: Engineering a redox switch in green fluorescent protein. EMBO J. 2001, 20, 5853-5862.
    • (2001) EMBO J. , vol.20 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 9
    • 0033613235 scopus 로고    scopus 로고
    • Circular permutation and receptor insertion within green fluorescent proteins
    • Baird, G.S.; Zacharias, D.A.; Tsien, R.Y. Circular permutation and receptor insertion within green fluorescent proteins. Proc. Natl. Acad. Sci. USA 1999, 96, 11241-11246.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 10
    • 0035129282 scopus 로고    scopus 로고
    • 2+ probe composed of a single green fluorescent protein
    • 2+ probe composed of a single green fluorescent protein. Nat. Biotechnol. 2001, 19, 137-141.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 137-141
    • Nakai, J.1    Ohkura, M.2    Imoto, K.3
  • 11
    • 44849120336 scopus 로고    scopus 로고
    • Genetically encoded calcium sensors
    • Mank, M.; Griesbeck, O. Genetically encoded calcium sensors. Chem. Rev. 2008, 108, 1550-1564.
    • (2008) Chem. Rev. , vol.108 , pp. 1550-1564
    • Mank, M.1    Griesbeck, O.2
  • 14
    • 59349118696 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter of ATP: ADP ratio
    • Berg, J.; Hung, Y.P.; Yellen, G. A genetically encoded fluorescent reporter of ATP: ADP ratio. Nat. Methods 2009, 6, 161-166.
    • (2009) Nat. Methods , vol.6 , pp. 161-166
    • Berg, J.1    Hung, Y.P.2    Yellen, G.3
  • 15
    • 84888873103 scopus 로고    scopus 로고
    • Imaging energy status in live cells with a fluorescent biosensor of the intracellular ATP-to-ADP ratio
    • Tantama, M.; Martinez-Francois, J.R.; Mongeon, R.; Yellen, G. Imaging energy status in live cells with a fluorescent biosensor of the intracellular ATP-to-ADP ratio. Nat. Commun. 2013, 4, 2550.
    • (2013) Nat. Commun. , vol.4 , pp. 2550
    • Tantama, M.1    Martinez-Francois, J.R.2    Mongeon, R.3    Yellen, G.4
  • 17
    • 84866000005 scopus 로고    scopus 로고
    • Single action potentials and subthreshold electrical events imaged in neurons with a fluorescent protein voltage probe
    • Jin, L.; Han, Z.; Platisa, J.; Wooltorton, J.R.; Cohen, L.B.; Pieribone, V.A. Single action potentials and subthreshold electrical events imaged in neurons with a fluorescent protein voltage probe. Neuron 2012, 75, 779-785.
    • (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
  • 18
    • 84882838081 scopus 로고    scopus 로고
    • Genetically targeted optical electrophysiology in intact neural circuits
    • Cao, G.; Platisa, J.; Pieribone, V.A.; Raccuglia, D.; Kunst, M.; Nitabach, M.N. Genetically targeted optical electrophysiology in intact neural circuits. Cell 2013, 154, 904-913.
    • (2013) Cell , vol.154 , pp. 904-913
    • Cao, G.1    Platisa, J.2    Pieribone, V.A.3    Raccuglia, D.4    Kunst, M.5    Nitabach, M.N.6
  • 21
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • Hanson, G.T.; Aggeler, R.; Oglesbee, D.; Cannon, M.; Capaldi, R.A.; Tsien, R.Y.; Remington, S.J. Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J. Biol. Chem. 2004, 279, 13044-13053.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbee, D.3    Cannon, M.4    Capaldi, R.A.5    Tsien, R.Y.6    Remington, S.J.7
  • 24
    • 33644767158 scopus 로고    scopus 로고
    • Single-molecule FRET study of denaturant induced unfolding of RNase H
    • Kuzmenkina, E.V.; Heyes, C.D.; Nienhaus, G.U. Single-molecule FRET study of denaturant induced unfolding of RNase H. J. Mol. Biol. 2006, 357, 313-324.
    • (2006) J. Mol. Biol. , vol.357 , pp. 313-324
    • Kuzmenkina, E.V.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 25
    • 2542516405 scopus 로고    scopus 로고
    • The density and refractive index of adsorbing protein layers
    • Voros, J. The density and refractive index of adsorbing protein layers. Biophys. J. 2004, 87, 553-561.
    • (2004) Biophys. J. , vol.87 , pp. 553-561
    • Voros, J.1
  • 26
    • 0034633010 scopus 로고    scopus 로고
    • Forster distances between green fluorescent protein pairs
    • Patterson, G.H.; Piston, D.W.; Barisas, B.G. Forster distances between green fluorescent protein pairs. Anal. Biochem. 2000, 284, 438-440.
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 27
    • 77952745940 scopus 로고    scopus 로고
    • Förster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins
    • Akrap, N.; Seidel, T.; Barisas, B.G. Förster distances for fluorescence resonant energy transfer between mCherry and other visible fluorescent proteins. Anal. Biochem. 2010, 402, 105-106.
    • (2010) Anal. Biochem. , vol.402 , pp. 105-106
    • Akrap, N.1    Seidel, T.2    Barisas, B.G.3
  • 28
    • 84889043177 scopus 로고    scopus 로고
    • Method for accurate determination of dissociation constants of optical ratiometric systems: Chemical probes, genetically encoded sensors, and interacting molecules
    • Pomorski, A.; Kochanczyk, T.; Miloch, A.; Krezel, A. Method for accurate determination of dissociation constants of optical ratiometric systems: Chemical probes, genetically encoded sensors, and interacting molecules. Anal. Chem. 2013, 85, 11479-11486.
    • (2013) Anal. Chem. , vol.85 , pp. 11479-11486
    • Pomorski, A.1    Kochanczyk, T.2    Miloch, A.3    Krezel, A.4
  • 29
    • 68049093089 scopus 로고    scopus 로고
    • Fluorescent-protein-based biosensors: Modulation of energy transfer as a design principle
    • Campbell, R.E. Fluorescent-protein-based biosensors: Modulation of energy transfer as a design principle. Anal. Chem. 2009, 81, 5972-5979.
    • (2009) Anal. Chem. , vol.81 , pp. 5972-5979
    • Campbell, R.E.1
  • 30
    • 33645233077 scopus 로고    scopus 로고
    • A dark yellow fluorescent protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for Forster resonance energy transfer with GFP
    • Ganesan, S.; Ameer-Beg, S.M.; Ng, T.T.; Vojnovic, B.; Wouters, F.S. A dark yellow fluorescent protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. USA 2006, 103, 4089-4094.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4089-4094
    • Ganesan, S.1    Ameer-Beg, S.M.2    Ng, T.T.3    Vojnovic, B.4    Wouters, F.S.5
  • 31
    • 57049179582 scopus 로고    scopus 로고
    • Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP
    • Murakoshi, H.; Lee, S.J.; Yasuda, R. Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP. Brain Cell Biol. 2008, 36, 31-42.
    • (2008) Brain Cell Biol. , vol.36 , pp. 31-42
    • Murakoshi, H.1    Lee, S.J.2    Yasuda, R.3
  • 32
    • 84864023955 scopus 로고    scopus 로고
    • Ultramarine, a chromoprotein acceptor for Forster resonance energy transfer
    • doi:10.1371/journal.pone.0041028
    • Pettikiriarachchi, A.; Gong, L.; Perugini, M.A.; Devenish, R.J.; Prescott, M. Ultramarine, a chromoprotein acceptor for Forster resonance energy transfer. PLoS One 2012, doi:10.1371/journal.pone.0041028.
    • (2012) PLoS One
    • Pettikiriarachchi, A.1    Gong, L.2    Perugini, M.A.3    Devenish, R.J.4    Prescott, M.5
  • 35
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B.A.; Adams, S.R.; Tsien, R.Y. Specific covalent labeling of recombinant protein molecules inside live cells. Science 1998, 281, 269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 36
    • 0037399074 scopus 로고    scopus 로고
    • Directed evolution of O6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo
    • Juillerat, A.; Gronemeyer, T.; Keppler, A.; Gendreizig, S.; Pick, H.; Vogel, H.; Johnsson, K. Directed evolution of O6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo. Chem. Biol. 2003, 10, 313-317.
    • (2003) Chem. Biol. , vol.10 , pp. 313-317
    • Juillerat, A.1    Gronemeyer, T.2    Keppler, A.3    Gendreizig, S.4    Pick, H.5    Vogel, H.6    Johnsson, K.7
  • 37
    • 70149112322 scopus 로고    scopus 로고
    • Semisynthetic fluorescent sensor proteins based on self-labeling protein tags
    • Brun, M.A.; Tan, K.T.; Nakata, E.; Hinner, M.J.; Johnsson, K. Semisynthetic fluorescent sensor proteins based on self-labeling protein tags. J. Am. Chem. Soc. 2009, 131, 5873-5884.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5873-5884
    • Brun, M.A.1    Tan, K.T.2    Nakata, E.3    Hinner, M.J.4    Johnsson, K.5
  • 41
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A.W.; Daugherty, P.S. Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 2005, 23, 355-360.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 42
    • 49249125063 scopus 로고    scopus 로고
    • Contribution of fluorophores to protein kinase C FRET probe performance
    • Jost, C.A.; Reither, G.; Hoffmann, C.; Schultz, C. Contribution of fluorophores to protein kinase C FRET probe performance. ChemBioChem 2008, 9, 1379-1384.
    • (2008) ChemBioChem , vol.9 , pp. 1379-1384
    • Jost, C.A.1    Reither, G.2    Hoffmann, C.3    Schultz, C.4
  • 43
    • 48449091054 scopus 로고    scopus 로고
    • Improving membrane voltage measurements using FRET with new fluorescent proteins
    • Tsutsui, H.; Karasawa, S.; Okamura, Y.; Miyawaki, A. Improving membrane voltage measurements using FRET with new fluorescent proteins. Nat. Methods 2008, 5, 683-685.
    • (2008) Nat. Methods , vol.5 , pp. 683-685
    • Tsutsui, H.1    Karasawa, S.2    Okamura, Y.3    Miyawaki, A.4
  • 44
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer, M.A.; Hellinga, H.W. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr. Opin. Struct. Biol. 2004, 14, 495-504.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 45
    • 24344451972 scopus 로고    scopus 로고
    • Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering
    • Deuschle, K.; Okumoto, S.; Fehr, M.; Looger, L.L.; Kozhukh, L.; Frommer, W.B. Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering. Protein Sci. 2005, 14, 2304-2314.
    • (2005) Protein Sci. , vol.14 , pp. 2304-2314
    • Deuschle, K.1    Okumoto, S.2    Fehr, M.3    Looger, L.L.4    Kozhukh, L.5    Frommer, W.B.6
  • 46
    • 0038819942 scopus 로고    scopus 로고
    • In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors
    • Fehr, M.; Lalonde, S.; Lager, I.; Wolff, M.W.; Frommer, W.B. In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors. J. Biol. Chem. 2003, 278, 19127-19133.
    • (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
  • 47
    • 40949111343 scopus 로고    scopus 로고
    • GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor
    • Takanaga, H.; Chaudhuri, B.; Frommer, W.B. GLUT1 and GLUT9 as major contributors to glucose influx in HepG2 cells identified by a high sensitivity intramolecular FRET glucose sensor. Biochim. Biophys. Acta 2008, 1778, 1091-1099.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1091-1099
    • Takanaga, H.1    Chaudhuri, B.2    Frommer, W.B.3
  • 48
    • 47949123143 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer sensors for quantitative monitoring of pentose and disaccharide accumulation in bacteria
    • Kaper, T.; Lager, I.; Looger, L.L.; Chermak, D.; Frommer, W.B. Fluorescence resonance energy transfer sensors for quantitative monitoring of pentose and disaccharide accumulation in bacteria. Biotechnol. Biofuels 2008, 1, 11.
    • (2008) Biotechnol. Biofuels , vol.1 , pp. 11
    • Kaper, T.1    Lager, I.2    Looger, L.L.3    Chermak, D.4    Frommer, W.B.5
  • 49
    • 0037162304 scopus 로고    scopus 로고
    • Visualization of maltose uptake in living yeast cells by fluorescent nanosensors
    • Fehr, M.; Frommer, W.B.; Lalonde, S. Visualization of maltose uptake in living yeast cells by fluorescent nanosensors. Proc. Natl. Acad. Sci. USA 2002, 99, 9846-9851.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9846-9851
    • Fehr, M.1    Frommer, W.B.2    Lalonde, S.3
  • 50
    • 73149090616 scopus 로고    scopus 로고
    • Circular permutation of ligand-binding module improves dynamic range of genetically encoded FRET-based nanosensor
    • Okada, S.; Ota, K.; Ito, T. Circular permutation of ligand-binding module improves dynamic range of genetically encoded FRET-based nanosensor. Protein Sci. 2009, 18, 2518-2527.
    • (2009) Protein Sci. , vol.18 , pp. 2518-2527
    • Okada, S.1    Ota, K.2    Ito, T.3
  • 51
    • 34249781722 scopus 로고    scopus 로고
    • Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures
    • Borrok, M.J.; Kiessling, L.L.; Forest, K.T. Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures. Protein Sci. 2007, 16, 1032-1041.
    • (2007) Protein Sci. , vol.16 , pp. 1032-1041
    • Borrok, M.J.1    Kiessling, L.L.2    Forest, K.T.3
  • 53
    • 33745051531 scopus 로고    scopus 로고
    • Zinc binding to a regulatory zinc-sensing domain monitored in vivo by using FRET
    • Qiao, W.; Mooney, M.; Bird, A.J.; Winge, D.R.; Eide, D.J. Zinc binding to a regulatory zinc-sensing domain monitored in vivo by using FRET. Proc. Natl. Acad. Sci. USA 2006, 103, 8674-8679.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8674-8679
    • Qiao, W.1    Mooney, M.2    Bird, A.J.3    Winge, D.R.4    Eide, D.J.5
  • 54
    • 23344433223 scopus 로고    scopus 로고
    • Engineering a signal transduction mechanism for protein-based biosensors
    • Kohn, J.E.; Plaxco, K.W. Engineering a signal transduction mechanism for protein-based biosensors. Proc. Natl. Acad. Sci. USA 2005, 102, 10841-10845.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10841-10845
    • Kohn, J.E.1    Plaxco, K.W.2
  • 57
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T.; Ibata, K.; Park, E.S.; Kubota, M.; Mikoshiba, K.; Miyawaki, A. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 2002, 20, 87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 58
    • 1842790629 scopus 로고    scopus 로고
    • Genetically encoded indicators of cellular calcium dynamics based on troponin C and green fluorescent protein
    • Heim, N.; Griesbeck, O. Genetically encoded indicators of cellular calcium dynamics based on troponin C and green fluorescent protein. J. Biol. Chem. 2004, 279, 14280-14286.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14280-14286
    • Heim, N.1    Griesbeck, O.2
  • 59
    • 33646145526 scopus 로고    scopus 로고
    • A FRET-based calcium biosensor with fast signal kinetics and high fluorescence change
    • Mank, M.; Reiff, D.F.; Heim, N.; Friedrich, M.W.; Borst, A.; Griesbeck, O. A FRET-based calcium biosensor with fast signal kinetics and high fluorescence change. Biophys. J. 2006, 90, 1790-1796.
    • (2006) Biophys. J. , vol.90 , pp. 1790-1796
    • Mank, M.1    Reiff, D.F.2    Heim, N.3    Friedrich, M.W.4    Borst, A.5    Griesbeck, O.6
  • 62
    • 77449142667 scopus 로고    scopus 로고
    • Reversible dimerization of Aequorea victoria fluorescent proteins increases the dynamic range of FRET-based indicators
    • Kotera, I.; Iwasaki, T.; Imamura, H.; Noji, H.; Nagai, T. Reversible dimerization of Aequorea victoria fluorescent proteins increases the dynamic range of FRET-based indicators. ACS Chem. Biol. 2010, 5, 215-222.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 215-222
    • Kotera, I.1    Iwasaki, T.2    Imamura, H.3    Noji, H.4    Nagai, T.5
  • 66
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • Nikolaev, V.O.; Bunemann, M.; Hein, L.; Hannawacker, A.; Lohse, M.J. Novel single chain cAMP sensors for receptor-induced signal propagation. J. Biol. Chem. 2004, 279, 37215-37218.
    • (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
  • 67
    • 44849141908 scopus 로고    scopus 로고
    • A comparison of donor-acceptor pairs for genetically encoded FRET sensors: Application to the Epac cAMP sensor as an example
    • doi:10.1371/journal.pone.0001916
    • Van der Krogt, G.N.; Ogink, J.; Ponsioen, B.; Jalink, K. A comparison of donor-acceptor pairs for genetically encoded FRET sensors: Application to the Epac cAMP sensor as an example. PLoS One 2008, doi:10.1371/journal.pone.0001916.
    • (2008) PLoS One
    • Van der Krogt, G.N.1    Ogink, J.2    Ponsioen, B.3    Jalink, K.4
  • 69
    • 79955716877 scopus 로고    scopus 로고
    • A mTurquoise-based cAMP sensor for both FLIM and ratiometric read-out has improved dynamic range
    • doi:10.1371/journal.pone.0019170
    • Klarenbeek, J.B.; Goedhart, J.; Hink, M.A.; Gadella, T.W.; Jalink, K. A mTurquoise-based cAMP sensor for both FLIM and ratiometric read-out has improved dynamic range. PLoS One 2011, doi:10.1371/journal.pone.0019170.
    • (2011) PLoS One
    • Klarenbeek, J.B.1    Goedhart, J.2    Hink, M.A.3    Gadella, T.W.4    Jalink, K.5
  • 70
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • Zhang, J.; Ma, Y.; Taylor, S.S.; Tsien, R.Y. Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl. Acad. Sci. USA 2001, 98, 14997-15002.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14997-15002
    • Zhang, J.1    Ma, Y.2    Taylor, S.S.3    Tsien, R.Y.4
  • 71
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • Sato, M.; Ozawa, T.; Inukai, K.; Asano, T.; Umezawa, Y. Fluorescent indicators for imaging protein phosphorylation in single living cells. Nat. Biotechnol. 2002, 20, 287-294.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 76
    • 1942454742 scopus 로고    scopus 로고
    • A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells
    • Awais, M.; Sato, M.; Sasaki, K.; Umezawa, Y. A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells. Anal. Chem. 2004, 76, 2181-2186.
    • (2004) Anal. Chem. , vol.76 , pp. 2181-2186
    • Awais, M.1    Sato, M.2    Sasaki, K.3    Umezawa, Y.4
  • 77
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • Aranda, A.; Pascual, A. Nuclear hormone receptors and gene expression. Physiol. Rev. 2001, 81, 1269-1304.
    • (2001) Physiol. Rev. , vol.81 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 78
    • 33746216307 scopus 로고    scopus 로고
    • A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells
    • Awais, M.; Sato, M.; Lee, X.; Umezawa, Y. A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells. Angew. Chem. Int. Ed. Engl. 2006, 45, 2707-2712.
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 2707-2712
    • Awais, M.1    Sato, M.2    Lee, X.3    Umezawa, Y.4
  • 79
    • 35348981760 scopus 로고    scopus 로고
    • Optical probes to identify the glucocorticoid receptor ligands in living cells
    • Awais, M.; Sato, M.; Umezawa, Y. Optical probes to identify the glucocorticoid receptor ligands in living cells. Steroids 2007, 72, 949-954.
    • (2007) Steroids , vol.72 , pp. 949-954
    • Awais, M.1    Sato, M.2    Umezawa, Y.3
  • 80
    • 84884623859 scopus 로고    scopus 로고
    • Rational design of FRET sensor proteins based on mutually exclusive domain interactions
    • Merkx, M.; Golynskiy, M.V.; Lindenburg, L.H.; Vinkenborg, J.L. Rational design of FRET sensor proteins based on mutually exclusive domain interactions. Biochem. Soc. Trans. 2013, 41, 1201-1205.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1201-1205
    • Merkx, M.1    Golynskiy, M.V.2    Lindenburg, L.H.3    Vinkenborg, J.L.4
  • 81
    • 34547600697 scopus 로고    scopus 로고
    • Enhanced sensitivity of FRET-based protease sensors by redesign of the GFP dimerization interface
    • Vinkenborg, J.L.; Evers, T.H.; Reulen, S.W.; Meijer, E.W.; Merkx, M. Enhanced sensitivity of FRET-based protease sensors by redesign of the GFP dimerization interface. ChemBioChem 2007, 8, 1119-1121.
    • (2007) ChemBioChem , vol.8 , pp. 1119-1121
    • Vinkenborg, J.L.1    Evers, T.H.2    Reulen, S.W.3    Meijer, E.W.4    Merkx, M.5
  • 82
    • 34250885891 scopus 로고    scopus 로고
    • An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins
    • Ohashi, T.; Galiacy, S.D.; Briscoe, G.; Erickson, H.P. An experimental study of GFP-based FRET, with application to intrinsically unstructured proteins. Protein Sci. 2007, 16, 1429-1438.
    • (2007) Protein Sci. , vol.16 , pp. 1429-1438
    • Ohashi, T.1    Galiacy, S.D.2    Briscoe, G.3    Erickson, H.P.4
  • 83
    • 33947631807 scopus 로고    scopus 로고
    • Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range
    • Van Dongen, E.M.; Evers, T.H.; Dekkers, L.M.; Meijer, E.W.; Klomp, L.W.; Merkx, M. Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range. J. Am. Chem. Soc. 2007, 129, 3494-3495.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3494-3495
    • Van Dongen, E.M.1    Evers, T.H.2    Dekkers, L.M.3    Meijer, E.W.4    Klomp, L.W.5    Merkx, M.6
  • 85
  • 86
    • 78049318476 scopus 로고    scopus 로고
    • Antibody detection by using a FRET-based protein conformational switch
    • Golynskiy, M.V.; Rurup, W.F.; Merkx, M. Antibody detection by using a FRET-based protein conformational switch. ChemBioChem 2010, 11, 2264-2267.
    • (2010) ChemBioChem , vol.11 , pp. 2264-2267
    • Golynskiy, M.V.1    Rurup, W.F.2    Merkx, M.3
  • 87
    • 44349104094 scopus 로고    scopus 로고
    • Design of protein function leaps by directed domain interface evolution
    • Huang, J.; Koide, A.; Makabe, K.; Koide, S. Design of protein function leaps by directed domain interface evolution. Proc. Natl. Acad. Sci. USA 2008, 105, 6578-6583.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6578-6583
    • Huang, J.1    Koide, A.2    Makabe, K.3    Koide, S.4
  • 88
    • 77949808895 scopus 로고    scopus 로고
    • Rational conversion of affinity reagents into label-free sensors for Peptide motifs by designed allostery
    • Huang, J.; Koide, S. Rational conversion of affinity reagents into label-free sensors for Peptide motifs by designed allostery. ACS Chem. Biol. 2010, 5, 273-277.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 273-277
    • Huang, J.1    Koide, S.2
  • 90
    • 80054930783 scopus 로고    scopus 로고
    • Imaging the coordination of multiple signalling activities in living cells
    • Welch, C.M.; Elliott, H.; Danuser, G.; Hahn, K.M. Imaging the coordination of multiple signalling activities in living cells. Nat. Rev. Mol. Cell Biol. 2011, 12, 749-756.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 749-756
    • Welch, C.M.1    Elliott, H.2    Danuser, G.3    Hahn, K.M.4
  • 91
    • 84859868813 scopus 로고    scopus 로고
    • Parallel tracking of cAMP and PKA signaling dynamics in living cells with FRET-based fluorescent biosensors
    • Aye-Han, N.N.; Allen, M.D.; Ni, Q.; Zhang, J. Parallel tracking of cAMP and PKA signaling dynamics in living cells with FRET-based fluorescent biosensors. Mol. Biosyst. 2012, 8, 1435-1440.
    • (2012) Mol. Biosyst. , vol.8 , pp. 1435-1440
    • Aye-Han, N.N.1    Allen, M.D.2    Ni, Q.3    Zhang, J.4
  • 94
    • 77950273418 scopus 로고    scopus 로고
    • Simultaneous visualization of protumorigenic Src and MT1-MMP activities with fluorescence resonance energy transfer
    • Ouyang, M.; Huang, H.; Shaner, N.C.; Remacle, A.G.; Shiryaev, S.A.; Strongin, A.Y.; Tsien, R.Y.; Wang, Y. Simultaneous visualization of protumorigenic Src and MT1-MMP activities with fluorescence resonance energy transfer. Cancer Res. 2010, 70, 2204-2212.
    • (2010) Cancer Res. , vol.70 , pp. 2204-2212
    • Ouyang, M.1    Huang, H.2    Shaner, N.C.3    Remacle, A.G.4    Shiryaev, S.A.5    Strongin, A.Y.6    Tsien, R.Y.7    Wang, Y.8
  • 95
    • 42449154333 scopus 로고    scopus 로고
    • Simultaneous recording of multiple cellular events by FRET
    • Piljic, A.; Schultz, C. Simultaneous recording of multiple cellular events by FRET. ACS Chem. Biol. 2008, 3, 156-160.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 156-160
    • Piljic, A.1    Schultz, C.2
  • 96
    • 84860852635 scopus 로고    scopus 로고
    • An orange fluorescent protein with a large Stokes shift for single-excitation multicolor FCCS and FRET imaging
    • Shcherbakova, D.M.; Hink, M.A.; Joosen, L.; Gadella, T.W.; Verkhusha, V.V. An orange fluorescent protein with a large Stokes shift for single-excitation multicolor FCCS and FRET imaging. J. Am. Chem. Soc. 2012, 134, 7913-7923.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 7913-7923
    • Shcherbakova, D.M.1    Hink, M.A.2    Joosen, L.3    Gadella, T.W.4    Verkhusha, V.V.5
  • 97
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A.; Violin, J.D.; Newton, A.C.; Tsien, R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 2002, 296, 913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 99
    • 41949134810 scopus 로고    scopus 로고
    • Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters
    • Hires, S.A.; Zhu, Y.; Tsien, R.Y. Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters. Proc. Natl. Acad. Sci. USA 2008, 105, 4411-4416.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4411-4416
    • Hires, S.A.1    Zhu, Y.2    Tsien, R.Y.3
  • 100
    • 79960490475 scopus 로고    scopus 로고
    • Rapid Development of Genetically Encoded FRET Reporters
    • Piljic, A.; de Diego, I.; Wilmanns, M.; Schultz, C. Rapid Development of Genetically Encoded FRET Reporters. ACS Chem. Biol. 2011, 6, 685-691.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 685-691
    • Piljic, A.1    de Diego, I.2    Wilmanns, M.3    Schultz, C.4
  • 101
    • 81055138866 scopus 로고    scopus 로고
    • A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors
    • Ibraheem, A.; Yap, H.; Ding, Y.; Campbell, R.E. A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors. BMC Biotechnol. 2011, 11, 105.
    • (2011) BMC Biotechnol. , vol.11 , pp. 105
    • Ibraheem, A.1    Yap, H.2    Ding, Y.3    Campbell, R.E.4
  • 102
    • 84891466923 scopus 로고    scopus 로고
    • Optimization of a genetically encoded biosensor for cyclin B1-cyclin dependent kinase 1
    • Belal, A.S.; Sell, B.R.; Hoi, H.; Davidson, M.W.; Campbell, R.E. Optimization of a genetically encoded biosensor for cyclin B1-cyclin dependent kinase 1. Mol. Biosyst. 2014, 10, 191-195.
    • (2014) Mol. Biosyst. , vol.10 , pp. 191-195
    • Belal, A.S.1    Sell, B.R.2    Hoi, H.3    Davidson, M.W.4    Campbell, R.E.5
  • 103
    • 14044266297 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter
    • Kunkel, M.T.; Ni, Q.; Tsien, R.Y.; Zhang, J.; Newton, A.C. Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter. J. Biol. Chem. 2005, 280, 5581-5587.
    • (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
  • 104
    • 84856574226 scopus 로고    scopus 로고
    • Colorful calcium sensors
    • Lindenburg, L.; Merkx, M. Colorful calcium sensors. ChemBioChem 2012, 13, 349-351.
    • (2012) ChemBioChem , vol.13 , pp. 349-351
    • Lindenburg, L.1    Merkx, M.2
  • 108
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N.C.; Campbell, R.E.; Steinbach, P.A.; Giepmans, B.N.; Palmer, A.E.; Tsien, R.Y. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 2004, 22, 1567-1572.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 110
    • 84881481582 scopus 로고    scopus 로고
    • Near-infrared fluorescent proteins for multicolor in vivo imaging
    • Shcherbakova, D.M.; Verkhusha, V.V. Near-infrared fluorescent proteins for multicolor in vivo imaging. Nat. Methods 2013, 10, 751-754.
    • (2013) Nat. Methods , vol.10 , pp. 751-754
    • Shcherbakova, D.M.1    Verkhusha, V.V.2
  • 112
    • 65649113981 scopus 로고    scopus 로고
    • Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome
    • Shu, X.; Royant, A.; Lin, M.Z.; Aguilera, T.A.; Lev-Ram, V.; Steinbach, P.A.; Tsien, R.Y. Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome. Science 2009, 324, 804-807.
    • (2009) Science , vol.324 , pp. 804-807
    • Shu, X.1    Royant, A.2    Lin, M.Z.3    Aguilera, T.A.4    Lev-Ram, V.5    Steinbach, P.A.6    Tsien, R.Y.7


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