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Volumn 1, Issue 10, 2009, Pages 565-573

FRET and mechanobiology

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; EQUIPMENT DESIGN; FLUORESCENCE MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; INSTRUMENTATION; MECHANOTRANSDUCTION; METHODOLOGY; PHYSIOLOGY; REVIEW;

EID: 70849116975     PISSN: 17579694     EISSN: 17579708     Source Type: Journal    
DOI: 10.1039/b913093b     Document Type: Review
Times cited : (33)

References (101)
  • 1
    • 42949146948 scopus 로고    scopus 로고
    • Fluorescent protein FRET pairs for ratiometric imaging of dual biosensors
    • H. W. Ai K. L. Hazelwood M. W. Davidson R. E. Campbell Fluorescent protein FRET pairs for ratiometric imaging of dual biosensors Nat. Methods 2008 5 401 403
    • (2008) Nat. Methods , vol.5 , pp. 401-403
    • Ai, H.W.1    Hazelwood, K.L.2    Davidson, M.W.3    Campbell, R.E.4
  • 2
    • 33845751079 scopus 로고    scopus 로고
    • Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: Structural characterization and applications in fluorescence imaging
    • H. W. Ai J. N. Henderson S. J. Remington R. E. Campbell Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging Biochem. J. 2006 400 531 540
    • (2006) Biochem. J. , vol.400 , pp. 531-540
    • Ai, H.W.1    Henderson, J.N.2    Remington, S.J.3    Campbell, R.E.4
  • 3
    • 34249007166 scopus 로고    scopus 로고
    • Exploration of new chromophore structures leads to the identification of improved blue fluorescent proteins
    • H. W. Ai N. C. Shaner Z. Cheng R. Y. Tsien R. E. Campbell Exploration of new chromophore structures leads to the identification of improved blue fluorescent proteins Biochemistry 2007 46 5904 5910
    • (2007) Biochemistry , vol.46 , pp. 5904-5910
    • Ai, H.W.1    Shaner, N.C.2    Cheng, Z.3    Tsien, R.Y.4    Campbell, R.E.5
  • 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 J. Zhang Signal propagation from membrane messengers to nuclear effectors revealed by reporters of phosphoinositide dynamics and Akt activity Proc. Natl. Acad. Sci. U. S. A. 2005 102 15081 15086
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15081-15086
    • Ananthanarayanan, B.1    Ni, Q.2    Zhang, J.3
  • 5
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • G. S. Baird D. A. Zacharias R. Y. Tsien Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral Proc. Natl. Acad. Sci. U. S. A. 2000 97 11984 11989
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 7
    • 33750366860 scopus 로고    scopus 로고
    • G protein-coupled receptors sense fluid shear stress in endothelial cells
    • M. Chachisvilis Y. L. Zhang J. A. Frangos G protein-coupled receptors sense fluid shear stress in endothelial cells Proc. Natl. Acad. Sci. U. S. A. 2006 103 15463 15468
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15463-15468
    • Chachisvilis, M.1    Zhang, Y.L.2    Frangos, J.A.3
  • 8
  • 9
    • 1842563953 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer, in
    • X. F. Wang and B. Herman, John Wiley & Sons, Inc., New York, pp. 179-252
    • R. M. Clegg, Fluorescence resonance energy transfer, in Fluorescence Imaging Spectroscopy and Microscopy, ed., X. F. Wang, and, B. Herman, John Wiley & Sons, Inc., New York, 1996, pp. 179-252
    • (1996) Fluorescence Imaging Spectroscopy and Microscopy, Ed.
    • Clegg, R.M.1
  • 10
    • 72149125927 scopus 로고    scopus 로고
    • Nuts and bolts of excitation energy migration and energy transfer, in
    • G. C. Papageorgiou and Govindjee, Springer, New York, pp. 83-105
    • R. M. Clegg, Nuts and bolts of excitation energy migration and energy transfer, in Chlorophyll a Fluorescence: A Signature of Photosynthesis, ed., G. C. Papageorgiou, and, Govindjee, Springer, New York, 2005, pp. 83-105
    • (2005) Chlorophyll A Fluorescence: A Signature of Photosynthesis, Ed.
    • Clegg, R.M.1
  • 11
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • B. P. Cormack R. H. Valdivia S. Falkow FACS-optimized mutants of the green fluorescent protein (GFP) Gene 1996 173 33 38
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 12
    • 9344220483 scopus 로고    scopus 로고
    • Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments
    • L. M. DiPilato X. Cheng J. Zhang Fluorescent indicators of cAMP and Epac activation reveal differential dynamics of cAMP signaling within discrete subcellular compartments Proc. Natl. Acad. Sci. U. S. A. 2004 101 16513 16518
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16513-16518
    • Dipilato, L.M.1    Cheng, X.2    Zhang, J.3
  • 13
    • 0029061274 scopus 로고
    • Green-fluorescent protein mutants with altered fluorescence excitation spectra
    • T. Ehrig D. J. O'Kane F. G. Prendergast Green-fluorescent protein mutants with altered fluorescence excitation spectra FEBS Lett. 1995 367 163 166
    • (1995) FEBS Lett. , vol.367 , pp. 163-166
    • Ehrig, T.1    O'Kane, D.J.2    Prendergast, F.G.3
  • 14
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • A. J. Engler S. Sen H. L. Sweeney D. E. Discher Matrix elasticity directs stem cell lineage specification Cell 2006 126 677 689
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 15
    • 33750827052 scopus 로고    scopus 로고
    • Detection of constitutive homomeric associations of the integrins Mac-1 subunits by fluorescence resonance energy transfer in living cells
    • G. Fu C. Wang G. Y. Wang Y. Z. Chen C. He Z. Z. Xu Detection of constitutive homomeric associations of the integrins Mac-1 subunits by fluorescence resonance energy transfer in living cells Biochem. Biophys. Res. Commun. 2006 351 847 852
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 847-852
    • Fu, G.1    Wang, C.2    Wang, G.Y.3    Chen, Y.Z.4    He, C.5    Xu, Z.Z.6
  • 16
    • 33745193026 scopus 로고    scopus 로고
    • Detection of constitutive heterodimerization of the integrin Mac-1 subunits by fluorescence resonance energy transfer in living cells
    • G. Fu H. Y. Yang C. Wang F. Zhang Z. D. You et al. Detection of constitutive heterodimerization of the integrin Mac-1 subunits by fluorescence resonance energy transfer in living cells Biochem. Biophys. Res. Commun. 2006 346 986 991
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 986-991
    • Fu, G.1    Yang, H.Y.2    Wang, C.3    Zhang, F.4    You, Z.D.5
  • 17
    • 33646852421 scopus 로고    scopus 로고
    • Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes
    • A. Fujioka K. Terai R. E. Itoh K. Aoki T. Nakamura et al. Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes J. Biol. Chem. 2006 281 8917 8926
    • (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
  • 18
    • 16444368541 scopus 로고    scopus 로고
    • Distinct NF-kappaB regulation by shear stress through Ras-dependent IkappaBalpha oscillations: Real-time analysis of flow-mediated activation in live cells
    • A. Ganguli L. Persson I. R. Palmer I. Evans L. Yang et al. Distinct NF-kappaB regulation by shear stress through Ras-dependent IkappaBalpha oscillations: real-time analysis of flow-mediated activation in live cells Circ. Res. 2005 96 626 634
    • (2005) Circ. Res. , vol.96 , pp. 626-634
    • Ganguli, A.1    Persson, L.2    Palmer, I.R.3    Evans, I.4    Yang, L.5
  • 19
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • S. Gasman Y. Kalaidzidis M. Zerial RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase Nat. Cell Biol. 2003 5 195 204
    • (2003) Nat. Cell Biol. , vol.5 , pp. 195-204
    • Gasman, S.1    Kalaidzidis, Y.2    Zerial, M.3
  • 20
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • B. N. Giepmans S. R. Adams M. H. Ellisman R. Y. Tsien The fluorescent toolbox for assessing protein location and function Science 2006 312 217 224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 21
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • O. Griesbeck G. S. Baird R. E. Campbell D. A. Zacharias R. Y. Tsien Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications J. Biol. Chem. 2001 276 29188 29194
    • (2001) J. Biol. Chem. , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 22
    • 0028580734 scopus 로고
    • Wavelength mutations and posttranslational autoxidation of green fluorescent protein
    • R. Heim D. C. Prasher R. Y. Tsien Wavelength mutations and posttranslational autoxidation of green fluorescent protein Proc. Natl. Acad. Sci. U. S. A. 1994 91 12501 12504
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 12501-12504
    • Heim, R.1    Prasher, D.C.2    Tsien, R.Y.3
  • 23
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • R. Heim R. Y. Tsien Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer Curr. Biol. 1996 6 178 182
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 24
    • 27744476758 scopus 로고    scopus 로고
    • Fluorescence approaches for monitoring interactions of Rho GTPases with nucleotides, regulators, and effectors
    • L. Hemsath M. R. Ahmadian Fluorescence approaches for monitoring interactions of Rho GTPases with nucleotides, regulators, and effectors Methods 2005 37 173 182
    • (2005) Methods , vol.37 , pp. 173-182
    • Hemsath, L.1    Ahmadian, M.R.2
  • 25
    • 37249008219 scopus 로고    scopus 로고
    • Design and optimization of genetically encoded fluorescent biosensors: GTPase biosensors
    • L. Hodgson O. Pertz K. M. Hahn Design and optimization of genetically encoded fluorescent biosensors: GTPase biosensors Methods Cell Biol. 2008 85 63 81
    • (2008) Methods Cell Biol. , vol.85 , pp. 63-81
    • Hodgson, L.1    Pertz, O.2    Hahn, K.M.3
  • 26
    • 0142084723 scopus 로고    scopus 로고
    • Intracellular stress tomography reveals stress focusing and structural anisotropy in cytoskeleton of living cells
    • S. Hu J. Chen B. Fabry Y. Numaguchi A. Gouldstone et al. Intracellular stress tomography reveals stress focusing and structural anisotropy in cytoskeleton of living cells Am. J. Physiol.: Cell Physiol. 2003 285 C1082 C1090
    • (2003) Am. J. Physiol.: Cell Physiol. , vol.285
    • Hu, S.1    Chen, J.2    Fabry, B.3    Numaguchi, Y.4    Gouldstone, A.5
  • 27
    • 0028777967 scopus 로고
    • Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein
    • S. Inouye F. I. Tsuji Aequorea green fluorescent protein. Expression of the gene and fluorescence characteristics of the recombinant protein FEBS Lett. 1994 341 277 280
    • (1994) FEBS Lett. , vol.341 , pp. 277-280
    • Inouye, S.1    Tsuji, F.I.2
  • 28
    • 0036724188 scopus 로고    scopus 로고
    • Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • R. E. Itoh K. Kurokawa Y. Ohba H. Yoshizaki N. Mochizuki M. Matsuda Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells Mol. Cell. Biol. 2002 22 6582 6591
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 29
    • 0035937571 scopus 로고    scopus 로고
    • Receptor-mediated activation of heterotrimeric G-proteins in living cells
    • C. Janetopoulos T. Jin P. Devreotes Receptor-mediated activation of heterotrimeric G-proteins in living cells Science 2001 291 2408 2411
    • (2001) Science , vol.291 , pp. 2408-2411
    • Janetopoulos, C.1    Jin, T.2    Devreotes, P.3
  • 30
    • 0026611047 scopus 로고
    • Association of p60c-src with endosomal membranes in mammalian fibroblasts
    • K. B. Kaplan J. R. Swedlow H. E. Varmus D. O. Morgan Association of p60c-src with endosomal membranes in mammalian fibroblasts J. Cell Biol. 1992 118 321 333
    • (1992) J. Cell Biol. , vol.118 , pp. 321-333
    • Kaplan, K.B.1    Swedlow, J.R.2    Varmus, H.E.3    Morgan, D.O.4
  • 31
    • 0141483388 scopus 로고    scopus 로고
    • A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling
    • S. Karasawa T. Araki M. Yamamoto-Hino A. Miyawaki A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling J. Biol. Chem. 2003 278 34167 34171
    • (2003) J. Biol. Chem. , vol.278 , pp. 34167-34171
    • Karasawa, S.1    Araki, T.2    Yamamoto-Hino, M.3    Miyawaki, A.4
  • 33
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • M. Kim C. V. Carman T. A. Springer Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins Science 2003 301 1720 1725
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 34
    • 58149214692 scopus 로고    scopus 로고
    • Substrate rigidity regulates Ca2+ oscillation via RhoA pathway in stem cells
    • T. J. Kim J. Seong M. Ouyang J. Sun S. Lu et al. Substrate rigidity regulates Ca2+ oscillation via RhoA pathway in stem cells J. Cell. Physiol. 2009 218 285 293
    • (2009) J. Cell. Physiol. , vol.218 , pp. 285-293
    • Kim, T.J.1    Seong, J.2    Ouyang, M.3    Sun, J.4    Lu, S.5
  • 36
    • 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 A. C. Newton Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter J. Biol. Chem. 2004 280 5581 5587
    • (2004) 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
  • 37
    • 1942508987 scopus 로고    scopus 로고
    • Imaging sites of N-wasp activity in lamellipodia and invadopodia of carcinoma cells
    • M. Lorenz H. Yamaguchi Y. Wang R. H. Singer J. Condeelis Imaging sites of N-wasp activity in lamellipodia and invadopodia of carcinoma cells Curr. Biol. 2004 14 697 703
    • (2004) Curr. Biol. , vol.14 , pp. 697-703
    • Lorenz, M.1    Yamaguchi, H.2    Wang, Y.3    Singer, R.H.4    Condeelis, J.5
  • 38
    • 0034801529 scopus 로고    scopus 로고
    • Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosis in living HeLa cells
    • K. Q. Luo V. C. Yu Y. Pu D. C. Chang Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during UV-induced apoptosis in living HeLa cells Biochem. Biophys. Res. Commun. 2001 283 1054 1060
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 1054-1060
    • Luo, K.Q.1    Yu, V.C.2    Pu, Y.3    Chang, D.C.4
  • 39
    • 0033150406 scopus 로고    scopus 로고
    • Novel mutant green fluorescent protein protease substrates reveal the activation of specific caspases during apoptosis
    • N. P. Mahajan D. C. Harrison-Shostak J. Michaux B. Herman Novel mutant green fluorescent protein protease substrates reveal the activation of specific caspases during apoptosis Chem. Biol. 1999 6 401 409
    • (1999) Chem. Biol. , vol.6 , pp. 401-409
    • Mahajan, N.P.1    Harrison-Shostak, D.C.2    Michaux, J.3    Herman, B.4
  • 40
    • 0031865351 scopus 로고    scopus 로고
    • Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer
    • N. P. Mahajan K. Linder G. Berry G. W. Gordon R. Heim B. Herman Bcl-2 and Bax interactions in mitochondria probed with green fluorescent protein and fluorescence resonance energy transfer Nat. Biotechnol. 1998 16 547 552
    • (1998) Nat. Biotechnol. , vol.16 , pp. 547-552
    • Mahajan, N.P.1    Linder, K.2    Berry, G.3    Gordon, G.W.4    Heim, R.5    Herman, B.6
  • 42
    • 33845690052 scopus 로고    scopus 로고
    • Blue fluorescent proteins with enhanced brightness and photostability from a structurally targeted library
    • M. A. Mena T. P. Treynor S. L. Mayo P. S. Daugherty Blue fluorescent proteins with enhanced brightness and photostability from a structurally targeted library Nat. Biotechnol. 2006 24 1569 1571
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1569-1571
    • Mena, M.A.1    Treynor, T.P.2    Mayo, S.L.3    Daugherty, P.S.4
  • 43
  • 44
    • 19944431688 scopus 로고    scopus 로고
    • Effects of flow patterns on the localization and expression of VE-cadherin at vascular endothelial cell junctions: In vivo and in vitro investigations
    • H. Miao Y. L. Hu Y. T. Shiu S. Yuan Y. Zhao et al. Effects of flow patterns on the localization and expression of VE-cadherin at vascular endothelial cell junctions: in vivo and in vitro investigations J. Vasc. Res. 2005 42 77 89
    • (2005) J. Vasc. Res. , vol.42 , pp. 77-89
    • Miao, H.1    Hu, Y.L.2    Shiu, Y.T.3    Yuan, S.4    Zhao, Y.5
  • 45
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein
    • R. D. Mitra C. M. Silva D. C. Youvan Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein Gene 1996 173 13 17
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 47
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • A. Miyawaki J. Llopis R. Heim J. M. McCaffery J. A. Adams et al. Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin Nature 1997 388 882 887
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5
  • 48
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • A. Miyawaki R. Y. Tsien Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein Methods Enzymol. 2000 327 472 500
    • (2000) Methods Enzymol. , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 49
    • 0035963331 scopus 로고    scopus 로고
    • Spatio-temporal images of growth-factor-induced activation of Ras and Rap1
    • N. Mochizuki S. Yamashita K. Kurokawa Y. Ohba T. Nagai et al. Spatio-temporal images of growth-factor-induced activation of Ras and Rap1 Nature 2001 411 1065 1068
    • (2001) Nature , vol.411 , pp. 1065-1068
    • Mochizuki, N.1    Yamashita, S.2    Kurokawa, K.3    Ohba, Y.4    Nagai, T.5
  • 50
    • 44349189707 scopus 로고    scopus 로고
    • Rapid signal transduction in living cells is a unique feature of mechanotransduction
    • S. Na O. Collin F. Chowdhury B. Tay M. Ouyang et al. Rapid signal transduction in living cells is a unique feature of mechanotransduction Proc. Natl. Acad. Sci. U. S. A. 2008 105 6626 6631
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6626-6631
    • Na, S.1    Collin, O.2    Chowdhury, F.3    Tay, B.4    Ouyang, M.5
  • 51
    • 55749086825 scopus 로고    scopus 로고
    • Application of fluorescence resonance energy transfer and magnetic twisting cytometry to quantify mechanochemical signaling activities in a living cell
    • S. Na N. Wang Application of fluorescence resonance energy transfer and magnetic twisting cytometry to quantify mechanochemical signaling activities in a living cell Sci. Signal 2008 1 pl1
    • (2008) Sci. Signal , vol.1 , pp. 1
    • Na, S.1    Wang, N.2
  • 52
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • T. Nagai K. Ibata E. S. Park M. Kubota K. Mikoshiba A. Miyawaki 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
  • 54
    • 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 A. Miyawaki Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins Proc. Natl. Acad. Sci. U. S. A. 2004 101 10554 10559
    • (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
  • 55
    • 0035129282 scopus 로고    scopus 로고
    • A high signal-to-noise Ca(2+) probe composed of a single green fluorescent protein
    • J. Nakai M. Ohkura K. Imoto A high signal-to-noise Ca(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
  • 57
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • A. W. Nguyen P. S. Daugherty 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
  • 58
    • 0033578742 scopus 로고    scopus 로고
    • Transient and steady-state effects of shear stress on endothelial cell adherens junctions
    • S. Noria D. B. Cowan A. I. Gotlieb B. L. Langille Transient and steady-state effects of shear stress on endothelial cell adherens junctions Circ. Res. 1999 85 504 514
    • (1999) Circ. Res. , vol.85 , pp. 504-514
    • Noria, S.1    Cowan, D.B.2    Gotlieb, A.I.3    Langille, B.L.4
  • 61
    • 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 Y. Wang Determination of hierarchical relationship of Src and Rac at subcellular locations with FRET biosensors Proc. Natl. Acad. Sci. U. S. A. 2008 105 14353 14358
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14353-14358
    • Ouyang, M.1    Sun, J.2    Chien, S.3    Wang, Y.4
  • 64
    • 2342436482 scopus 로고    scopus 로고
    • Designing biosensors for Rho family proteins - Deciphering the dynamics of Rho family GTPase activation in living cells
    • O. Pertz K. M. Hahn Designing biosensors for Rho family proteins - deciphering the dynamics of Rho family GTPase activation in living cells J. Cell Sci. 2004 117 1313 1318
    • (2004) J. Cell Sci. , vol.117 , pp. 1313-1318
    • Pertz, O.1    Hahn, K.M.2
  • 65
    • 33646197411 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of RhoA activity in migrating cells
    • O. Pertz L. Hodgson R. L. Klemke K. M. Hahn Spatiotemporal dynamics of RhoA activity in migrating cells Nature 2006 440 1069 1072
    • (2006) Nature , vol.440 , pp. 1069-1072
    • Pertz, O.1    Hodgson, L.2    Klemke, R.L.3    Hahn, K.M.4
  • 66
    • 42449154333 scopus 로고    scopus 로고
    • Simultaneous recording of multiple cellular events by FRET
    • A. Piljic C. Schultz 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
  • 67
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • D. W. Piston G. J. Kremers Fluorescent protein FRET: the good, the bad and the ugly Trends Biochem. Sci. 2007 32 407 414
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremers, G.J.2
  • 70
    • 0031011418 scopus 로고    scopus 로고
    • Detection in living cells of Ca2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators
    • V. A. Romoser P. M. Hinkle A. Persechini Detection in living cells of Ca2+-dependent changes in the fluorescence emission of an indicator composed of two green fluorescent protein variants linked by a calmodulin-binding sequence. A new class of fluorescent indicators J. Biol. Chem. 1997 272 13270 13274
    • (1997) J. Biol. Chem. , vol.272 , pp. 13270-13274
    • Romoser, V.A.1    Hinkle, P.M.2    Persechini, A.3
  • 71
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • M. Sato T. Ozawa K. Inukai T. Asano Y. Umezawa 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
  • 72
    • 0037446762 scopus 로고    scopus 로고
    • Rational design of genetically encoded fluorescence resonance energy transfer-based sensors of cellular Cdc42 signaling
    • A. Seth T. Otomo H. L. Yin M. K. Rosen Rational design of genetically encoded fluorescence resonance energy transfer-based sensors of cellular Cdc42 signaling Biochemistry 2003 42 3997 4008
    • (2003) Biochemistry , vol.42 , pp. 3997-4008
    • Seth, A.1    Otomo, T.2    Yin, H.L.3    Rosen, M.K.4
  • 73
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • N. C. Shaner R. E. Campbell P. A. Steinbach B. N. Giepmans A. E. Palmer R. Y. Tsien 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
  • 74
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of bright monomeric orange and red fluorescent proteins
    • N. C. Shaner M. Z. Lin M. R. McKeown P. A. Steinbach K. L. Hazelwood et al. Improving the photostability of bright monomeric orange and red fluorescent proteins Nat. Methods 2008 5 545 551
    • (2008) Nat. Methods , vol.5 , pp. 545-551
    • Shaner, N.C.1    Lin, M.Z.2    McKeown, M.R.3    Steinbach, P.A.4    Hazelwood, K.L.5
  • 77
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • O. Shimomura F. H. Johnson Y. Saiga Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea J. Cell. Comp. Physiol. 1962 59 223 239
    • (1962) J. Cell. Comp. Physiol. , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 78
    • 65649113981 scopus 로고    scopus 로고
    • Mammalian expression of infrared fluorescent proteins engineered from a bacterial phytochrome
    • X. Shu A. Royant M. Z. Lin T. A. Aguilera V. Lev-Ram et al. 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
  • 79
    • 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 R. Y. Tsien Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells Proc. Natl. Acad. Sci. U. S. A. 2001 98 15003 15008
    • (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
  • 81
    • 0024488636 scopus 로고
    • Fluorescent probes of cell signaling
    • R. Y. Tsien Fluorescent probes of cell signaling Annu. Rev. Neurosci. 1989 12 227 253
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 227-253
    • Tsien, R.Y.1
  • 82
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • R. Y. Tsien The green fluorescent protein Annu. Rev. Biochem. 1998 67 509 544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 83
    • 14544286521 scopus 로고    scopus 로고
    • Building and breeding molecules to spy on cells and tumors
    • R. Y. Tsien Building and breeding molecules to spy on cells and tumors FEBS Lett. 2005 579 927 932
    • (2005) FEBS Lett. , vol.579 , pp. 927-932
    • Tsien, R.Y.1
  • 84
    • 0037121966 scopus 로고    scopus 로고
    • Activation of Rac1 by shear stress in endothelial cells mediates both cytoskeletal reorganization and effects on gene expression
    • E. Tzima M. A. Del Pozo W. B. Kiosses S. A. Mohamed S. Li et al. Activation of Rac1 by shear stress in endothelial cells mediates both cytoskeletal reorganization and effects on gene expression EMBO J. 2002 21 6791 6800
    • (2002) EMBO J. , vol.21 , pp. 6791-6800
    • Tzima, E.1    Del Pozo, M.A.2    Kiosses, W.B.3    Mohamed, S.A.4    Li, S.5
  • 85
    • 0042232206 scopus 로고    scopus 로고
    • Localized cdc42 activation detected using a novel assay mediates microtubule organizing center positioning in endothelial cells in response to fluid shear stress
    • E. Tzima W. B. Kiosses M. A. del Pozo M. A. Schwartz Localized cdc42 activation detected using a novel assay mediates microtubule organizing center positioning in endothelial cells in response to fluid shear stress J. Biol. Chem. 2003 278 31020 31023
    • (2003) J. Biol. Chem. , vol.278 , pp. 31020-31023
    • Tzima, E.1    Kiosses, W.B.2    Del Pozo, M.A.3    Schwartz, M.A.4
  • 86
    • 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 A. C. Newton A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C J. Cell Biol. 2003 161 899 909
    • (2003) J. Cell Biol. , vol.161 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 87
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • V. Vogel M. Sheetz Local force and geometry sensing regulate cell functions Nat. Rev. Mol. Cell Biol. 2006 7 265 275
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 89
    • 58049211966 scopus 로고    scopus 로고
    • Mechanotransduction at a distance: Mechanically coupling the extracellular matrix with the nucleus
    • N. Wang J. D. Tytell D. E. Ingber Mechanotransduction at a distance: mechanically coupling the extracellular matrix with the nucleus Nat. Rev. Mol. Cell Biol. 2009 10 75 82
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 75-82
    • Wang, N.1    Tytell, J.D.2    Ingber, D.E.3
  • 91
    • 33947362038 scopus 로고    scopus 로고
    • Development of fluorescent biosensors for probing the function of motor proteins
    • M. R. Webb Development of fluorescent biosensors for probing the function of motor proteins Mol. BioSyst. 2007 3 249 256
    • (2007) Mol. BioSyst. , vol.3 , pp. 249-256
    • Webb, M.R.1
  • 92
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • F. Yang L. G. Moss G. N. Phillips Jr The molecular structure of green fluorescent protein Nat. Biotechnol. 1996 14 1246 1251
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr, G.N.3
  • 93
    • 0042672950 scopus 로고    scopus 로고
    • Activity of Rho-family GTPases during cell division as visualized with FRET-based probes
    • H. Yoshizaki Y. Ohba K. Kurokawa R. E. Itoh T. Nakamura et al. Activity of Rho-family GTPases during cell division as visualized with FRET-based probes J. Cell Biol. 2003 162 223 232
    • (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
  • 94
    • 0033622319 scopus 로고    scopus 로고
    • A genetically encoded, fluorescent indicator for cyclic AMP in living cells
    • M. Zaccolo F. De Giorgi C. Y. Cho L. Feng T. Knapp et al. A genetically encoded, fluorescent indicator for cyclic AMP in living cells Nat. Cell Biol. 2000 2 25 29
    • (2000) Nat. Cell Biol. , vol.2 , pp. 25-29
    • Zaccolo, M.1    De Giorgi, F.2    Cho, C.Y.3    Feng, L.4    Knapp, T.5
  • 95
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • M. Zaccolo T. Pozzan Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes Science 2002 295 1711 1715
    • (2002) Science , vol.295 , pp. 1711-1715
    • Zaccolo, M.1    Pozzan, T.2
  • 96
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • D. A. Zacharias J. D. Violin A. C. Newton R. Y. Tsien 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
  • 97
    • 26244434925 scopus 로고    scopus 로고
    • Polarized downregulation of the paxillin-p130CAS-Rac1 pathway induced by shear flow
    • R. Zaidel-Bar Z. Kam B. Geiger Polarized downregulation of the paxillin-p130CAS-Rac1 pathway induced by shear flow J. Cell Sci. 2005 118 3997 4007
    • (2005) J. Cell Sci. , vol.118 , pp. 3997-4007
    • Zaidel-Bar, R.1    Kam, Z.2    Geiger, B.3
  • 98
    • 3042511548 scopus 로고    scopus 로고
    • Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP
    • O. Zapata-Hommer O. Griesbeck Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP BMC Biotechnol. 2003 3 5
    • (2003) BMC Biotechnol. , vol.3 , pp. 5
    • Zapata-Hommer, O.1    Griesbeck, O.2
  • 100
    • 25644446102 scopus 로고    scopus 로고
    • Insulin disrupts beta-adrenergic signalling to protein kinase A in adipocytes
    • J. Zhang C. J. Hupfeld S. S. Taylor J. M. Olefsky R. Y. Tsien Insulin disrupts beta-adrenergic signalling to protein kinase A in adipocytes Nature 2005 437 569 573
    • (2005) Nature , vol.437 , pp. 569-573
    • Zhang, J.1    Hupfeld, C.J.2    Taylor, S.S.3    Olefsky, J.M.4    Tsien, R.Y.5
  • 101
    • 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 R. Y. Tsien Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering Proc. Natl. Acad. Sci. U. S. A. 2001 98 14997 15002
    • (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


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