메뉴 건너뛰기




Volumn 21, Issue 2, 2014, Pages 186-197

Genetically encoded fluorescent biosensors for live-cell visualization of protein phosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; ANIMALS, GENETICALLY MODIFIED; BIOSENSING TECHNIQUES; FLUORESCENCE RESONANCE ENERGY TRANSFER; LUMINESCENT PROTEINS; MYOCYTES, CARDIAC; NEURONS; PEPTIDES; PHOSPHORYLATION; PROTEIN KINASES; RECOMBINANT FUSION PROTEINS;

EID: 84894491451     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2013.12.012     Document Type: Review
Times cited : (79)

References (126)
  • 2
    • 33746907024 scopus 로고    scopus 로고
    • Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters
    • M.D. Allen, and J. Zhang Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters Biochem. Biophys. Res. Commun. 348 2006 716 721
    • (2006) Biochem. Biophys. Res. Commun. , vol.348 , pp. 716-721
    • Allen, M.D.1    Zhang, J.2
  • 3
    • 84873324067 scopus 로고    scopus 로고
    • Adiponectin receptors form homomers and heteromers exhibiting distinct ligand binding and intracellular signaling properties
    • F. Almabouada, A. Diaz-Ruiz, Y. Rabanal-Ruiz, J.R. Peinado, R. Vazquez-Martinez, and M.M. Malagon Adiponectin receptors form homomers and heteromers exhibiting distinct ligand binding and intracellular signaling properties J. Biol. Chem. 288 2013 3112 3125
    • (2013) J. Biol. Chem. , vol.288 , pp. 3112-3125
    • Almabouada, F.1    Diaz-Ruiz, A.2    Rabanal-Ruiz, Y.3    Peinado, J.R.4    Vazquez-Martinez, R.5    Malagon, M.M.6
  • 4
    • 27244445187 scopus 로고    scopus 로고
    • Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity
    • B. Ananthanarayanan, Q. Ni, and J. Zhang Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity Proc. Natl. Acad. Sci. USA 102 2005 15081 15086
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15081-15086
    • Ananthanarayanan, B.1    Ni, Q.2    Zhang, J.3
  • 5
    • 37549002125 scopus 로고    scopus 로고
    • Live-cell molecular analysis of Akt activation reveals roles for activation loop phosphorylation
    • B. Ananthanarayanan, M. Fosbrink, M. Rahdar, and J. Zhang Live-cell molecular analysis of Akt activation reveals roles for activation loop phosphorylation J. Biol. Chem. 282 2007 36634 36641
    • (2007) J. Biol. Chem. , vol.282 , pp. 36634-36641
    • Ananthanarayanan, B.1    Fosbrink, M.2    Rahdar, M.3    Zhang, J.4
  • 6
    • 77955799768 scopus 로고    scopus 로고
    • Protein-protein interactions monitored in cells from transgenic mice using bioluminescence resonance energy transfer
    • M. Audet, M. Lagacé, D.W. Silversides, and M. Bouvier Protein-protein interactions monitored in cells from transgenic mice using bioluminescence resonance energy transfer FASEB J. 24 2010 2829 2838
    • (2010) FASEB J. , vol.24 , pp. 2829-2838
    • Audet, M.1    Lagacé, M.2    Silversides, D.W.3    Bouvier, M.4
  • 12
    • 77951653553 scopus 로고    scopus 로고
    • Type 4 phosphodiesterase plays different integrating roles in different cellular domains in pyramidal cortical neurons
    • L.R. Castro, N. Gervasi, E. Guiot, L. Cavellini, V.O. Nikolaev, D. Paupardin-Tritsch, and P. Vincent Type 4 phosphodiesterase plays different integrating roles in different cellular domains in pyramidal cortical neurons J. Neurosci. 30 2010 6143 6151
    • (2010) J. Neurosci. , vol.30 , pp. 6143-6151
    • Castro, L.R.1    Gervasi, N.2    Guiot, E.3    Cavellini, L.4    Nikolaev, V.O.5    Paupardin-Tritsch, D.6    Vincent, P.7
  • 14
    • 79955821040 scopus 로고    scopus 로고
    • AKAP150-mediated TRPV1 sensitization is disrupted by calcium/calmodulin
    • S. Chaudhury, M. Bal, S. Belugin, M.S. Shapiro, and N.A. Jeske AKAP150-mediated TRPV1 sensitization is disrupted by calcium/calmodulin Mol. Pain 7 2011 34
    • (2011) Mol. Pain , vol.7 , pp. 34
    • Chaudhury, S.1    Bal, M.2    Belugin, S.3    Shapiro, M.S.4    Jeske, N.A.5
  • 15
    • 84863482577 scopus 로고    scopus 로고
    • Signaling in dendritic spines and spine microdomains
    • Y. Chen, and B.L. Sabatini Signaling in dendritic spines and spine microdomains Curr. Opin. Neurobiol. 22 2012 389 396
    • (2012) Curr. Opin. Neurobiol. , vol.22 , pp. 389-396
    • Chen, Y.1    Sabatini, B.L.2
  • 17
    • 84859867549 scopus 로고    scopus 로고
    • Fluorescent proteins for FRET microscopy: Monitoring protein interactions in living cells
    • R.N. Day, and M.W. Davidson Fluorescent proteins for FRET microscopy: monitoring protein interactions in living cells Bioessays 34 2012 341 350
    • (2012) Bioessays , vol.34 , pp. 341-350
    • Day, R.N.1    Davidson, M.W.2
  • 18
    • 77956255305 scopus 로고    scopus 로고
    • Equilibrium between adenylyl cyclase and phosphodiesterase patterns adrenergic agonist dose-dependent spatiotemporal cAMP/protein kinase A activities in cardiomyocytes
    • V. De Arcangelis, S. Liu, D. Zhang, D. Soto, and Y.K. Xiang Equilibrium between adenylyl cyclase and phosphodiesterase patterns adrenergic agonist dose-dependent spatiotemporal cAMP/protein kinase A activities in cardiomyocytes Mol. Pharmacol. 78 2010 340 349
    • (2010) Mol. Pharmacol. , vol.78 , pp. 340-349
    • De Arcangelis, V.1    Liu, S.2    Zhang, D.3    Soto, D.4    Xiang, Y.K.5
  • 19
    • 84875441344 scopus 로고    scopus 로고
    • Dance of the SNAREs: Assembly and rearrangements detected with FRET at neuronal synapses
    • V. Degtyar, I.M. Hafez, C. Bray, and R.S. Zucker Dance of the SNAREs: assembly and rearrangements detected with FRET at neuronal synapses J. Neurosci. 33 2013 5507 5523
    • (2013) J. Neurosci. , vol.33 , pp. 5507-5523
    • Degtyar, V.1    Hafez, I.M.2    Bray, C.3    Zucker, R.S.4
  • 20
    • 84861443604 scopus 로고    scopus 로고
    • ExiFRET: Flexible tool for understanding FRET in complex geometries
    • E. Deplazes, D. Jayatilaka, and B. Corry ExiFRET: flexible tool for understanding FRET in complex geometries J. Biomed. Opt. 17 2012 011005
    • (2012) J. Biomed. Opt. , vol.17 , pp. 011005
    • Deplazes, E.1    Jayatilaka, D.2    Corry, B.3
  • 21
    • 78650157273 scopus 로고    scopus 로고
    • Visualization of PKA activity in plasma membrane microdomains
    • C. Depry, M.D. Allen, and J. Zhang Visualization of PKA activity in plasma membrane microdomains Mol. Biosyst. 7 2011 52 58
    • (2011) Mol. Biosyst. , vol.7 , pp. 52-58
    • Depry, C.1    Allen, M.D.2    Zhang, J.3
  • 22
    • 84878298397 scopus 로고    scopus 로고
    • Multiplexed visualization of dynamic signaling networks using genetically encoded fluorescent protein-based biosensors
    • C. Depry, S. Mehta, and J. Zhang Multiplexed visualization of dynamic signaling networks using genetically encoded fluorescent protein-based biosensors Pflugers Arch. 465 2013 373 381
    • (2013) Pflugers Arch. , vol.465 , pp. 373-381
    • Depry, C.1    Mehta, S.2    Zhang, J.3
  • 23
    • 77951985322 scopus 로고    scopus 로고
    • AKAP79 interacts with multiple adenylyl cyclase (AC) isoforms and scaffolds AC5 and -6 to α-amino-3-hydroxyl-5-methyl-4-isoxazole-propionate (AMPA) receptors
    • R. Efendiev, B.K. Samelson, B.T. Nguyen, P.V. Phatarpekar, F. Baameur, J.D. Scott, and C.W. Dessauer AKAP79 interacts with multiple adenylyl cyclase (AC) isoforms and scaffolds AC5 and -6 to α-amino-3-hydroxyl-5-methyl-4- isoxazole-propionate (AMPA) receptors J. Biol. Chem. 285 2010 14450 14458
    • (2010) J. Biol. Chem. , vol.285 , pp. 14450-14458
    • Efendiev, R.1    Samelson, B.K.2    Nguyen, B.T.3    Phatarpekar, P.V.4    Baameur, F.5    Scott, J.D.6    Dessauer, C.W.7
  • 24
    • 84873689852 scopus 로고    scopus 로고
    • Scaffolding by A-kinase anchoring protein enhances functional coupling between adenylyl cyclase and TRPV1 channel
    • R. Efendiev, A. Bavencoffe, H. Hu, M.X. Zhu, and C.W. Dessauer Scaffolding by A-kinase anchoring protein enhances functional coupling between adenylyl cyclase and TRPV1 channel J. Biol. Chem. 288 2013 3929 3937
    • (2013) J. Biol. Chem. , vol.288 , pp. 3929-3937
    • Efendiev, R.1    Bavencoffe, A.2    Hu, H.3    Zhu, M.X.4    Dessauer, C.W.5
  • 25
    • 84855598857 scopus 로고    scopus 로고
    • G-PKDrep-live, a genetically encoded FRET reporter to measure PKD activity at the trans-Golgi-network
    • S.A. Eisler, Y.F. Fuchs, K. Pfizenmaier, and A. Hausser G-PKDrep-live, a genetically encoded FRET reporter to measure PKD activity at the trans-Golgi-network Biotechnol. J. 7 2012 148 154
    • (2012) Biotechnol. J. , vol.7 , pp. 148-154
    • Eisler, S.A.1    Fuchs, Y.F.2    Pfizenmaier, K.3    Hausser, A.4
  • 26
    • 80052962709 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based sensor Camui provides new insight into mechanisms of calcium/calmodulin-dependent protein kinase II activation in intact cardiomyocytes
    • J.R. Erickson, R. Patel, A. Ferguson, J. Bossuyt, and D.M. Bers Fluorescence resonance energy transfer-based sensor Camui provides new insight into mechanisms of calcium/calmodulin-dependent protein kinase II activation in intact cardiomyocytes Circ. Res. 109 2011 729 738
    • (2011) Circ. Res. , vol.109 , pp. 729-738
    • Erickson, J.R.1    Patel, R.2    Ferguson, A.3    Bossuyt, J.4    Bers, D.M.5
  • 27
    • 77950434011 scopus 로고    scopus 로고
    • Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor
    • M. Fosbrink, N.N. Aye-Han, R. Cheong, A. Levchenko, and J. Zhang Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor Proc. Natl. Acad. Sci. USA 107 2010 5459 5464
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5459-5464
    • Fosbrink, M.1    Aye-Han, N.N.2    Cheong, R.3    Levchenko, A.4    Zhang, J.5
  • 28
    • 65249175108 scopus 로고    scopus 로고
    • A Golgi PKD activity reporter reveals a crucial role of PKD in nocodazole-induced Golgi dispersal
    • Y.F. Fuchs, S.A. Eisler, G. Link, O. Schlicker, G. Bunt, K. Pfizenmaier, and A. Hausser A Golgi PKD activity reporter reveals a crucial role of PKD in nocodazole-induced Golgi dispersal Traffic 10 2009 858 867
    • (2009) Traffic , vol.10 , pp. 858-867
    • Fuchs, Y.F.1    Eisler, S.A.2    Link, G.3    Schlicker, O.4    Bunt, G.5    Pfizenmaier, K.6    Hausser, A.7
  • 30
    • 57349145336 scopus 로고    scopus 로고
    • Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains
    • X. Gao, and J. Zhang Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains Mol. Biol. Cell 19 2008 4366 4373
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4366-4373
    • Gao, X.1    Zhang, J.2
  • 31
    • 80052275615 scopus 로고    scopus 로고
    • PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains
    • X. Gao, P.R. Lowry, X. Zhou, C. Depry, Z. Wei, G.W. Wong, and J. Zhang PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains PNAS 108 2011 14509 14514
    • (2011) PNAS , vol.108 , pp. 14509-14514
    • Gao, X.1    Lowry, P.R.2    Zhou, X.3    Depry, C.4    Wei, Z.5    Wong, G.W.6    Zhang, J.7
  • 33
    • 77951177406 scopus 로고    scopus 로고
    • Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis
    • O. Gavet, and J. Pines Activation of cyclin B1-Cdk1 synchronizes events in the nucleus and the cytoplasm at mitosis J. Cell Biol. 189 2010 247 259
    • (2010) J. Cell Biol. , vol.189 , pp. 247-259
    • Gavet, O.1    Pines, J.2
  • 34
    • 1642532373 scopus 로고    scopus 로고
    • Quantitative measurements of Ca(2+)/calmodulin binding and activation of myosin light chain kinase in cells
    • R. Geguchadze, G. Zhi, K.S. Lau, E. Isotani, A. Persechini, K.E. Kamm, and J.T. Stull Quantitative measurements of Ca(2+)/calmodulin binding and activation of myosin light chain kinase in cells FEBS Lett. 557 2004 121 124
    • (2004) FEBS Lett. , vol.557 , pp. 121-124
    • Geguchadze, R.1    Zhi, G.2    Lau, K.S.3    Isotani, E.4    Persechini, A.5    Kamm, K.E.6    Stull, J.T.7
  • 36
    • 76849113585 scopus 로고    scopus 로고
    • PKA dynamics in a Drosophila learning center: Coincidence detection by rutabaga adenylyl cyclase and spatial regulation by dunce phosphodiesterase
    • N. Gervasi, P. Tchénio, and T. Preat PKA dynamics in a Drosophila learning center: coincidence detection by rutabaga adenylyl cyclase and spatial regulation by dunce phosphodiesterase Neuron 65 2010 516 529
    • (2010) Neuron , vol.65 , pp. 516-529
    • Gervasi, N.1    Tchénio, P.2    Preat, T.3
  • 37
    • 84874924189 scopus 로고    scopus 로고
    • GDNF and endothelin 3 regulate migration of enteric neural crest-derived cells via protein kinase A and Rac1
    • A. Goto, K. Sumiyama, Y. Kamioka, E. Nakasyo, K. Ito, M. Iwasaki, H. Enomoto, and M. Matsuda GDNF and endothelin 3 regulate migration of enteric neural crest-derived cells via protein kinase A and Rac1 J. Neurosci. 33 2013 4901 4912
    • (2013) J. Neurosci. , vol.33 , pp. 4901-4912
    • Goto, A.1    Sumiyama, K.2    Kamioka, Y.3    Nakasyo, E.4    Ito, K.5    Iwasaki, M.6    Enomoto, H.7    Matsuda, M.8
  • 38
    • 77949482986 scopus 로고    scopus 로고
    • A FRET-based microplate assay for human protein kinase CK2, a target in neoplastic disease
    • A. Gratz, C. Götz, and J. Jose A FRET-based microplate assay for human protein kinase CK2, a target in neoplastic disease J. Enzyme Inhib. Med. Chem. 25 2010 234 239
    • (2010) J. Enzyme Inhib. Med. Chem. , vol.25 , pp. 234-239
    • Gratz, A.1    Götz, C.2    Jose, J.3
  • 39
    • 74149088545 scopus 로고    scopus 로고
    • β-adrenergic receptor signaling in the heart: Role of CaMKII
    • M. Grimm, and J.H. Brown β-adrenergic receptor signaling in the heart: role of CaMKII J. Mol. Cell. Cardiol. 48 2010 322 330
    • (2010) J. Mol. Cell. Cardiol. , vol.48 , pp. 322-330
    • Grimm, M.1    Brown, J.H.2
  • 40
    • 33845359060 scopus 로고    scopus 로고
    • FRET and colocalization analyzer - A method to validate measurements of sensitized emission FRET acquired by confocal microscopy and available as an ImageJ plug-in
    • M. Hachet-Haas, N. Converset, O. Marchal, H. Matthes, S. Gioria, J.L. Galzi, and S. Lecat FRET and colocalization analyzer - a method to validate measurements of sensitized emission FRET acquired by confocal microscopy and available as an ImageJ plug-in Microsc. Res. Tech. 69 2006 941 956
    • (2006) Microsc. Res. Tech. , vol.69 , pp. 941-956
    • Hachet-Haas, M.1    Converset, N.2    Marchal, O.3    Matthes, H.4    Gioria, S.5    Galzi, J.L.6    Lecat, S.7
  • 43
    • 77954380512 scopus 로고    scopus 로고
    • T-cell receptor microclusters critical for T-cell activation are formed independently of lipid raft clustering
    • A. Hashimoto-Tane, T. Yokosuka, C. Ishihara, M. Sakuma, W. Kobayashi, and T. Saito T-cell receptor microclusters critical for T-cell activation are formed independently of lipid raft clustering Mol. Cell. Biol. 30 2010 3421 3429
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3421-3429
    • Hashimoto-Tane, A.1    Yokosuka, T.2    Ishihara, C.3    Sakuma, M.4    Kobayashi, W.5    Saito, T.6
  • 44
    • 79954563435 scopus 로고    scopus 로고
    • Luminescent kinase activity biosensors based on a versatile bimolecular switch
    • K.J. Herbst, M.D. Allen, and J. Zhang Luminescent kinase activity biosensors based on a versatile bimolecular switch J. Am. Chem. Soc. 133 2011 5676 5679
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5676-5679
    • Herbst, K.J.1    Allen, M.D.2    Zhang, J.3
  • 45
    • 41949134810 scopus 로고    scopus 로고
    • Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters
    • S.A. Hires, Y. Zhu, and R.Y. Tsien Optical measurement of synaptic glutamate spillover and reuptake by linker optimized glutamate-sensitive fluorescent reporters Proc. Natl. Acad. Sci. USA 105 2008 4411 4416
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4411-4416
    • Hires, S.A.1    Zhu, Y.2    Tsien, R.Y.3
  • 46
    • 81055138866 scopus 로고    scopus 로고
    • A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors
    • A. Ibraheem, H. Yap, Y. Ding, and R.E. Campbell A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors BMC Biotechnol. 11 2011 105
    • (2011) BMC Biotechnol. , vol.11 , pp. 105
    • Ibraheem, A.1    Yap, H.2    Ding, Y.3    Campbell, R.E.4
  • 48
    • 34547824221 scopus 로고    scopus 로고
    • Monitoring ATM kinase activity in living cells
    • S.A. Johnson, Z. You, and T. Hunter Monitoring ATM kinase activity in living cells DNA Repair (Amst.) 6 2007 1277 1284
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1277-1284
    • Johnson, S.A.1    You, Z.2    Hunter, T.3
  • 49
    • 78650635555 scopus 로고    scopus 로고
    • Protein kinase C δ-specific activity reporter reveals agonist-evoked nuclear activity controlled by Src family of kinases
    • T. Kajimoto, S. Sawamura, Y. Tohyama, Y. Mori, and A.C. Newton Protein kinase C δ-specific activity reporter reveals agonist-evoked nuclear activity controlled by Src family of kinases J. Biol. Chem. 285 2010 41896 41910
    • (2010) J. Biol. Chem. , vol.285 , pp. 41896-41910
    • Kajimoto, T.1    Sawamura, S.2    Tohyama, Y.3    Mori, Y.4    Newton, A.C.5
  • 51
    • 6044247522 scopus 로고    scopus 로고
    • Single color fluorescent indicators of protein phosphorylation for multicolor imaging of intracellular signal flow dynamics
    • Y. Kawai, M. Sato, and Y. Umezawa Single color fluorescent indicators of protein phosphorylation for multicolor imaging of intracellular signal flow dynamics Anal. Chem. 76 2004 6144 6149
    • (2004) Anal. Chem. , vol.76 , pp. 6144-6149
    • Kawai, Y.1    Sato, M.2    Umezawa, Y.3
  • 53
    • 14044266297 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter
    • M.T. Kunkel, Q. Ni, R.Y. Tsien, J. Zhang, and A.C. Newton Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter J. Biol. Chem. 280 2005 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
  • 55
    • 79957961826 scopus 로고    scopus 로고
    • Glutamate induces de novo growth of functional spines in developing cortex
    • H.B. Kwon, and B.L. Sabatini Glutamate induces de novo growth of functional spines in developing cortex Nature 474 2011 100 104
    • (2011) Nature , vol.474 , pp. 100-104
    • Kwon, H.B.1    Sabatini, B.L.2
  • 56
    • 62649108345 scopus 로고    scopus 로고
    • Activation of CaMKII in single dendritic spines during long-term potentiation
    • S.J. Lee, Y. Escobedo-Lozoya, E.M. Szatmari, and R. Yasuda Activation of CaMKII in single dendritic spines during long-term potentiation Nature 458 2009 299 304
    • (2009) Nature , vol.458 , pp. 299-304
    • Lee, S.J.1    Escobedo-Lozoya, Y.2    Szatmari, E.M.3    Yasuda, R.4
  • 57
    • 84888373123 scopus 로고    scopus 로고
    • Role of AKAP79/150 protein in β1-adrenergic receptor trafficking and signaling in mammalian cells
    • X. Li, M.M. Nooh, and S.W. Bahouth Role of AKAP79/150 protein in β1-adrenergic receptor trafficking and signaling in mammalian cells J. Biol. Chem. 288 2013 33797 33812
    • (2013) J. Biol. Chem. , vol.288 , pp. 33797-33812
    • Li, X.1    Nooh, M.M.2    Bahouth, S.W.3
  • 58
    • 84857356081 scopus 로고    scopus 로고
    • Mechanisms of CaMKII action in long-term potentiation
    • J. Lisman, R. Yasuda, and S. Raghavachari Mechanisms of CaMKII action in long-term potentiation Nat. Rev. Neurosci. 13 2012 169 182
    • (2012) Nat. Rev. Neurosci. , vol.13 , pp. 169-182
    • Lisman, J.1    Yasuda, R.2    Raghavachari, S.3
  • 59
    • 27744564512 scopus 로고    scopus 로고
    • Improvement of a FRET-based indicator for cAMP by linker design and stabilization of donor-acceptor interaction
    • V. Lissandron, A. Terrin, M. Collini, L. D'alfonso, G. Chirico, S. Pantano, and M. Zaccolo Improvement of a FRET-based indicator for cAMP by linker design and stabilization of donor-acceptor interaction J. Mol. Biol. 354 2005 546 555
    • (2005) J. Mol. Biol. , vol.354 , pp. 546-555
    • Lissandron, V.1    Terrin, A.2    Collini, M.3    D'Alfonso, L.4    Chirico, G.5    Pantano, S.6    Zaccolo, M.7
  • 60
    • 78651369353 scopus 로고    scopus 로고
    • FRET-based direct detection of dynamic protein kinase A activity on the sarcoplasmic reticulum in cardiomyocytes
    • S. Liu, J. Zhang, and Y.K. Xiang FRET-based direct detection of dynamic protein kinase A activity on the sarcoplasmic reticulum in cardiomyocytes Biochem. Biophys. Res. Commun. 404 2011 581 586
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 581-586
    • Liu, S.1    Zhang, J.2    Xiang, Y.K.3
  • 61
    • 84858203893 scopus 로고    scopus 로고
    • Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling
    • M.J. Lohse, S. Nuber, and C. Hoffmann Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling Pharmacol. Rev. 64 2012 299 336
    • (2012) Pharmacol. Rev. , vol.64 , pp. 299-336
    • Lohse, M.J.1    Nuber, S.2    Hoffmann, C.3
  • 64
    • 79959451416 scopus 로고    scopus 로고
    • Reporting from the field: Genetically encoded fluorescent reporters uncover signaling dynamics in living biological systems
    • S. Mehta, and J. Zhang Reporting from the field: genetically encoded fluorescent reporters uncover signaling dynamics in living biological systems Annu. Rev. Biochem. 80 2011 375 401
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 375-401
    • Mehta, S.1    Zhang, J.2
  • 65
    • 84862695182 scopus 로고    scopus 로고
    • Conformational analysis of a genetically encoded FRET biosensor by SAXS
    • H.D. Mertens, A. Piljić, C. Schultz, and D.I. Svergun Conformational analysis of a genetically encoded FRET biosensor by SAXS Biophys. J. 102 2012 2866 2875
    • (2012) Biophys. J. , vol.102 , pp. 2866-2875
    • Mertens, H.D.1    Piljić, A.2    Schultz, C.3    Svergun, D.I.4
  • 66
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • A. Miyawaki Visualization of the spatial and temporal dynamics of intracellular signaling Dev. Cell 4 2003 295 305
    • (2003) Dev. Cell , vol.4 , pp. 295-305
    • Miyawaki, A.1
  • 69
    • 3242706582 scopus 로고    scopus 로고
    • Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins
    • T. Nagai, S. Yamada, T. Tominaga, M. Ichikawa, and A. Miyawaki Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins Proc. Natl. Acad. Sci. USA 101 2004 10554 10559
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10554-10559
    • Nagai, T.1    Yamada, S.2    Tominaga, T.3    Ichikawa, M.4    Miyawaki, A.5
  • 70
    • 0035129282 scopus 로고    scopus 로고
    • A high signal-to-noise Ca(2+) probe composed of a single green fluorescent protein
    • J. Nakai, M. Ohkura, and K. Imoto A high signal-to-noise Ca(2+) probe composed of a single green fluorescent protein Nat. Biotechnol. 19 2001 137 141
    • (2001) Nat. Biotechnol. , vol.19 , pp. 137-141
    • Nakai, J.1    Ohkura, M.2    Imoto, K.3
  • 71
    • 0034859534 scopus 로고    scopus 로고
    • FRET-based detection of different conformations of MK2
    • A. Neininger, H. Thielemann, and M. Gaestel FRET-based detection of different conformations of MK2 EMBO Rep. 2 2001 703 708
    • (2001) EMBO Rep. , vol.2 , pp. 703-708
    • Neininger, A.1    Thielemann, H.2    Gaestel, M.3
  • 72
    • 43949103755 scopus 로고    scopus 로고
    • Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor
    • R.H. Newman, and J. Zhang Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor Mol. Biosyst. 4 2008 496 501
    • (2008) Mol. Biosyst. , vol.4 , pp. 496-501
    • Newman, R.H.1    Zhang, J.2
  • 75
    • 84872294746 scopus 로고    scopus 로고
    • An improved Ras sensor for highly sensitive and quantitative FRET-FLIM imaging
    • A.F. Oliveira, and R. Yasuda An improved Ras sensor for highly sensitive and quantitative FRET-FLIM imaging PLoS ONE 8 2013 e52874
    • (2013) PLoS ONE , vol.8 , pp. 52874
    • Oliveira, A.F.1    Yasuda, R.2
  • 77
    • 53149108997 scopus 로고    scopus 로고
    • MRNA display selection of a high-affinity, modification-specific phospho-IκBα-binding fibronectin
    • C.A. Olson, H.I. Liao, R. Sun, and R.W. Roberts mRNA display selection of a high-affinity, modification-specific phospho-IκBα-binding fibronectin ACS Chem. Biol. 3 2008 480 485
    • (2008) ACS Chem. Biol. , vol.3 , pp. 480-485
    • Olson, C.A.1    Liao, H.I.2    Sun, R.3    Roberts, R.W.4
  • 78
    • 55749093427 scopus 로고    scopus 로고
    • Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors
    • M. Ouyang, J. Sun, S. Chien, and Y. Wang Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors Proc. Natl. Acad. Sci. USA 105 2008 14353 14358
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14353-14358
    • Ouyang, M.1    Sun, J.2    Chien, S.3    Wang, Y.4
  • 79
    • 84859848908 scopus 로고    scopus 로고
    • FRET microscopy in the living cell: Different approaches, strengths and weaknesses
    • S. Padilla-Parra, and M. Tramier FRET microscopy in the living cell: different approaches, strengths and weaknesses Bioessays 34 2012 369 376
    • (2012) Bioessays , vol.34 , pp. 369-376
    • Padilla-Parra, S.1    Tramier, M.2
  • 81
    • 79951671135 scopus 로고    scopus 로고
    • Design and application of genetically encoded biosensors
    • A.E. Palmer, Y. Qin, J.G. Park, and J.E. McCombs Design and application of genetically encoded biosensors Trends Biotechnol. 29 2011 144 152
    • (2011) Trends Biotechnol. , vol.29 , pp. 144-152
    • Palmer, A.E.1    Qin, Y.2    Park, J.G.3    McCombs, J.E.4
  • 82
    • 69949177832 scopus 로고    scopus 로고
    • Dissecting activation of the PAK1 kinase at protrusions in living cells
    • M.C. Parrini, J. Camonis, M. Matsuda, and J. de Gunzburg Dissecting activation of the PAK1 kinase at protrusions in living cells J. Biol. Chem. 284 2009 24133 24143
    • (2009) J. Biol. Chem. , vol.284 , pp. 24133-24143
    • Parrini, M.C.1    Camonis, J.2    Matsuda, M.3    De Gunzburg, J.4
  • 83
    • 57949104871 scopus 로고    scopus 로고
    • Chapter 22: Quantitation of protein-protein interactions: Confocal FRET microscopy
    • A. Periasamy, H. Wallrabe, Y. Chen, and M. Barroso Chapter 22: Quantitation of protein-protein interactions: confocal FRET microscopy Methods Cell Biol. 89 2008 569 598
    • (2008) Methods Cell Biol. , vol.89 , pp. 569-598
    • Periasamy, A.1    Wallrabe, H.2    Chen, Y.3    Barroso, M.4
  • 85
    • 37249032741 scopus 로고    scopus 로고
    • FRET by fluorescence polarization microscopy
    • D.W. Piston, and M.A. Rizzo FRET by fluorescence polarization microscopy Methods Cell Biol. 85 2008 415 430
    • (2008) Methods Cell Biol. , vol.85 , pp. 415-430
    • Piston, D.W.1    Rizzo, M.A.2
  • 87
    • 48049095596 scopus 로고    scopus 로고
    • Combining protein complementation assays with resonance energy transfer to detect multipartner protein complexes in living cells
    • R.V. Rebois, M. Robitaille, D. Pétrin, P. Zylbergold, P. Trieu, and T.E. Hébert Combining protein complementation assays with resonance energy transfer to detect multipartner protein complexes in living cells Methods 45 2008 214 218
    • (2008) Methods , vol.45 , pp. 214-218
    • Rebois, R.V.1    Robitaille, M.2    Pétrin, D.3    Zylbergold, P.4    Trieu, P.5    Hébert, T.E.6
  • 88
    • 24344456096 scopus 로고    scopus 로고
    • Chemical approaches for investigating phosphorylation in signal transduction networks
    • D.M. Rothman, M.D. Shults, and B. Imperiali Chemical approaches for investigating phosphorylation in signal transduction networks Trends Cell Biol. 15 2005 502 510
    • (2005) Trends Cell Biol. , vol.15 , pp. 502-510
    • Rothman, D.M.1    Shults, M.D.2    Imperiali, B.3
  • 89
    • 79956131603 scopus 로고    scopus 로고
    • AKAP signaling complexes in regulation of excitatory synaptic plasticity
    • J.L. Sanderson, and M.L. Dell'Acqua AKAP signaling complexes in regulation of excitatory synaptic plasticity Neuroscientist 17 2011 321 336
    • (2011) Neuroscientist , vol.17 , pp. 321-336
    • Sanderson, J.L.1    Dell'Acqua, M.L.2
  • 90
    • 0042733215 scopus 로고    scopus 로고
    • Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells
    • K. Sasaki, M. Sato, and Y. Umezawa Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells J. Biol. Chem. 278 2003 30945 30951
    • (2003) J. Biol. Chem. , vol.278 , pp. 30945-30951
    • Sasaki, K.1    Sato, M.2    Umezawa, Y.3
  • 91
    • 1542375241 scopus 로고    scopus 로고
    • Imaging protein phosphorylation by fluorescence in single living cells
    • M. Sato, and Y. Umezawa Imaging protein phosphorylation by fluorescence in single living cells Methods 32 2004 451 455
    • (2004) Methods , vol.32 , pp. 451-455
    • Sato, M.1    Umezawa, Y.2
  • 92
    • 33947361161 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells
    • M. Sato, Y. Kawai, and Y. Umezawa Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells Anal. Chem. 79 2007 2570 2575
    • (2007) Anal. Chem. , vol.79 , pp. 2570-2575
    • Sato, M.1    Kawai, Y.2    Umezawa, Y.3
  • 94
    • 75749145003 scopus 로고    scopus 로고
    • Local and long-range reciprocal regulation of cAMP and cGMP in axon/dendrite formation
    • M. Shelly, B.K. Lim, L. Cancedda, S.C. Heilshorn, H. Gao, and M.M. Poo Local and long-range reciprocal regulation of cAMP and cGMP in axon/dendrite formation Science 327 2010 547 552
    • (2010) Science , vol.327 , pp. 547-552
    • Shelly, M.1    Lim, B.K.2    Cancedda, L.3    Heilshorn, S.C.4    Gao, H.5    Poo, M.M.6
  • 97
    • 84866774623 scopus 로고    scopus 로고
    • Protein interaction affinity determination by quantitative FRET technology
    • Y. Song, V.G. Rodgers, J.S. Schultz, and J. Liao Protein interaction affinity determination by quantitative FRET technology Biotechnol. Bioeng. 109 2012 2875 2883
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 2875-2883
    • Song, Y.1    Rodgers, V.G.2    Schultz, J.S.3    Liao, J.4
  • 98
    • 84883054185 scopus 로고    scopus 로고
    • Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells
    • Y. Sun, C. Rombola, V. Jyothikumar, and A. Periasamy Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells Cytometry A 83 2013 780 793
    • (2013) Cytometry A , vol.83 , pp. 780-793
    • Sun, Y.1    Rombola, C.2    Jyothikumar, V.3    Periasamy, A.4
  • 100
    • 84857076245 scopus 로고    scopus 로고
    • Optogenetic reporters: Fluorescent protein-based genetically encoded indicators of signaling and metabolism in the brain
    • M. Tantama, Y.P. Hung, and G. Yellen Optogenetic reporters: fluorescent protein-based genetically encoded indicators of signaling and metabolism in the brain Prog. Brain Res. 196 2012 235 263
    • (2012) Prog. Brain Res. , vol.196 , pp. 235-263
    • Tantama, M.1    Hung, Y.P.2    Yellen, G.3
  • 101
    • 16844385887 scopus 로고    scopus 로고
    • Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase
    • K. Terai, and M. Matsuda Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase EMBO Rep. 6 2005 251 255
    • (2005) EMBO Rep. , vol.6 , pp. 251-255
    • Terai, K.1    Matsuda, M.2
  • 102
    • 33747615527 scopus 로고    scopus 로고
    • The amino-terminal B-Raf-specific region mediates calcium-dependent homo- and hetero-dimerization of Raf
    • K. Terai, and M. Matsuda The amino-terminal B-Raf-specific region mediates calcium-dependent homo- and hetero-dimerization of Raf EMBO J. 25 2006 3556 3564
    • (2006) EMBO J. , vol.25 , pp. 3556-3564
    • Terai, K.1    Matsuda, M.2
  • 103
    • 82355171931 scopus 로고    scopus 로고
    • Microtubule affinity regulating kinase activity in living neurons was examined by a genetically encoded fluorescence resonance energy transfer/fluorescence lifetime imaging-based biosensor: Inhibitors with therapeutic potential
    • T. Timm, J.P. von Kries, X. Li, H. Zempel, E. Mandelkow, and E.M. Mandelkow Microtubule affinity regulating kinase activity in living neurons was examined by a genetically encoded fluorescence resonance energy transfer/fluorescence lifetime imaging-based biosensor: inhibitors with therapeutic potential J. Biol. Chem. 286 2011 41711 41722
    • (2011) J. Biol. Chem. , vol.286 , pp. 41711-41722
    • Timm, T.1    Von Kries, J.P.2    Li, X.3    Zempel, H.4    Mandelkow, E.5    Mandelkow, E.M.6
  • 104
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • A.Y. Ting, K.H. Kain, R.L. Klemke, and R.Y. Tsien Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells Proc. Natl. Acad. Sci. USA 98 2001 15003 15008
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 105
    • 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
    • T. Tomida, M. Takekawa, P. O'Grady, and H. Saito 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 2009 6117 6127
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6117-6127
    • Tomida, T.1    Takekawa, M.2    O'Grady, P.3    Saito, H.4
  • 107
    • 79953732149 scopus 로고    scopus 로고
    • A fluorescent reporter of AMPK activity and cellular energy stress
    • P. Tsou, B. Zheng, C.H. Hsu, A.T. Sasaki, and L.C. Cantley A fluorescent reporter of AMPK activity and cellular energy stress Cell Metab. 13 2011 476 486
    • (2011) Cell Metab. , vol.13 , pp. 476-486
    • Tsou, P.1    Zheng, B.2    Hsu, C.H.3    Sasaki, A.T.4    Cantley, L.C.5
  • 109
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • J.D. Violin, J. Zhang, R.Y. Tsien, and A.C. Newton A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C J. Cell Biol. 161 2003 899 909
    • (2003) J. Cell Biol. , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 110
    • 54349105689 scopus 로고    scopus 로고
    • Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta
    • R. Waadt, L.K. Schmidt, M. Lohse, K. Hashimoto, R. Bock, and J. Kudla Multicolor bimolecular fluorescence complementation reveals simultaneous formation of alternative CBL/CIPK complexes in planta Plant J. 56 2008 505 516
    • (2008) Plant J. , vol.56 , pp. 505-516
    • Waadt, R.1    Schmidt, L.K.2    Lohse, M.3    Hashimoto, K.4    Bock, R.5    Kudla, J.6
  • 112
    • 0022351039 scopus 로고
    • Calcium gradients in single smooth muscle cells revealed by the digital imaging microscope using Fura-2
    • D.A. Williams, K.E. Fogarty, R.Y. Tsien, and F.S. Fay Calcium gradients in single smooth muscle cells revealed by the digital imaging microscope using Fura-2 Nature 318 1985 558 561
    • (1985) Nature , vol.318 , pp. 558-561
    • Williams, D.A.1    Fogarty, K.E.2    Tsien, R.Y.3    Fay, F.S.4
  • 114
    • 77958466186 scopus 로고    scopus 로고
    • Signal/noise analysis of FRET-based sensors
    • A. Woehler, J. Wlodarczyk, and E. Neher Signal/noise analysis of FRET-based sensors Biophys. J. 99 2010 2344 2354
    • (2010) Biophys. J. , vol.99 , pp. 2344-2354
    • Woehler, A.1    Wlodarczyk, J.2    Neher, E.3
  • 115
    • 84859525656 scopus 로고    scopus 로고
    • Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-β revealed by a novel fluorescence resonance energy transfer assay
    • H.Y. Wu, E. Hudry, T. Hashimoto, K. Uemura, Z.Y. Fan, O. Berezovska, C.L. Grosskreutz, B.J. Bacskai, and B.T. Hyman Distinct dendritic spine and nuclear phases of calcineurin activation after exposure to amyloid-β revealed by a novel fluorescence resonance energy transfer assay J. Neurosci. 32 2012 5298 5309
    • (2012) J. Neurosci. , vol.32 , pp. 5298-5309
    • Wu, H.Y.1    Hudry, E.2    Hashimoto, T.3    Uemura, K.4    Fan, Z.Y.5    Berezovska, O.6    Grosskreutz, C.L.7    Bacskai, B.J.8    Hyman, B.T.9
  • 116
    • 84868306607 scopus 로고    scopus 로고
    • Isozyme-specific interaction of protein kinase Cδ with mitochondria dissected using live cell fluorescence imaging
    • A.X. Wu-Zhang, A.N. Murphy, M. Bachman, and A.C. Newton Isozyme-specific interaction of protein kinase Cδ with mitochondria dissected using live cell fluorescence imaging J. Biol. Chem. 287 2012 37891 37906
    • (2012) J. Biol. Chem. , vol.287 , pp. 37891-37906
    • Wu-Zhang, A.X.1    Murphy, A.N.2    Bachman, M.3    Newton, A.C.4
  • 118
    • 84855506461 scopus 로고    scopus 로고
    • Live imaging of apoptosis in a novel transgenic mouse highlights its role in neural tube closure
    • Y. Yamaguchi, N. Shinotsuka, K. Nonomura, K. Takemoto, K. Kuida, H. Yosida, and M. Miura Live imaging of apoptosis in a novel transgenic mouse highlights its role in neural tube closure J. Cell Biol. 195 2011 1047 1060
    • (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    Miura, M.7
  • 119
    • 84867596381 scopus 로고    scopus 로고
    • Studying signal transduction in single dendritic spines
    • R. Yasuda Studying signal transduction in single dendritic spines Cold Spring Harb. Perspect. Biol. 4 2012 a005611
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. 005611
    • Yasuda, R.1
  • 120
    • 33846044650 scopus 로고    scopus 로고
    • Akt-PDK1 complex mediates epidermal growth factor-induced membrane protrusion through Ral activation
    • H. Yoshizaki, N. Mochizuki, Y. Gotoh, and M. Matsuda Akt-PDK1 complex mediates epidermal growth factor-induced membrane protrusion through Ral activation Mol. Biol. Cell 18 2007 119 128
    • (2007) Mol. Biol. Cell , vol.18 , pp. 119-128
    • Yoshizaki, H.1    Mochizuki, N.2    Gotoh, Y.3    Matsuda, M.4
  • 121
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • M. Zaccolo, and T. Pozzan Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes Science 295 2002 1711 1715
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 123
    • 75749086416 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation
    • S. Zadran, H. Jourdi, K. Rostamiani, Q. Qin, X. Bi, and M. Baudry Brain-derived neurotrophic factor and epidermal growth factor activate neuronal m-calpain via mitogen-activated protein kinase-dependent phosphorylation J. Neurosci. 30 2010 1086 1095
    • (2010) J. Neurosci. , vol.30 , pp. 1086-1095
    • Zadran, S.1    Jourdi, H.2    Rostamiani, K.3    Qin, Q.4    Bi, X.5    Baudry, M.6
  • 124
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • J. Zhang, Y. Ma, S.S. Taylor, and R.Y. Tsien Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering Proc. Natl. Acad. Sci. USA 98 2001 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.