메뉴 건너뛰기




Volumn 237, Issue , 2004, Pages 205-277

Visualization of molecular activities inside living cells with fluorescent labels

Author keywords

Biosensors; Fluorescence; FRET; GFP; Microscopy; Protein protein interactions

Indexed keywords

ACTIN; CALMODULIN; CYAN FLUORESCENT PROTEIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP; CYTOPLASM PROTEIN; EPIDERMAL GROWTH FACTOR; GANGLIOSIDE GM1; GENE PRODUCT; GLUCOCORTICOID RECEPTOR; GREEN FLUORESCENT PROTEIN; GUANOSINE TRIPHOSPHATASE; LANTHANIDE; RAP PROTEIN; RHO FACTOR; RHODAMINE; YELLOW FLUORESCENT PROTEIN; ZINC FINGER PROTEIN;

EID: 4544237524     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(04)37005-1     Document Type: Article
Times cited : (62)

References (242)
  • 1
    • 0032518204 scopus 로고    scopus 로고
    • Green fluorescent protein as a scaffold for intracellular presentation of peptides
    • Abedi M.R., Caponigro G., Kamb A. Green fluorescent protein as a scaffold for intracellular presentation of peptides. Nucleic Acids Res. 26:1998;623-630
    • (1998) Nucleic Acids Res. , vol.26 , pp. 623-630
    • Abedi, M.R.1    Caponigro, G.2    Kamb, A.3
  • 2
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams S.R., Campbell R.E., Gross L.A., Martin B.R., Walkup G.K., Yao Y., Llopis J., Tsien R.Y. New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications. J. Am. Chem. Soc. 124:2002;6063-6076
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 5
    • 0242441610 scopus 로고    scopus 로고
    • Actin filament uncapping localizes to ruffling lamellae and rocketing vesicles
    • Allen P.G. Actin filament uncapping localizes to ruffling lamellae and rocketing vesicles. Nat. Cell Biol. 5:2003;972-979
    • (2003) Nat. Cell Biol. , vol.5 , pp. 972-979
    • Allen, P.G.1
  • 6
    • 0037126841 scopus 로고    scopus 로고
    • Protein affinity labeling mediated by genetically encoded peptide tags
    • Amini F., Kodadek T., Brown K.C. Protein affinity labeling mediated by genetically encoded peptide tags. Angew Chem. Int. Ed. Engl. 41:2002;356-359
    • (2002) Angew Chem. Int. Ed. Engl. , vol.41 , pp. 356-359
    • Amini, F.1    Kodadek, T.2    Brown, K.C.3
  • 7
    • 0036789916 scopus 로고    scopus 로고
    • An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein
    • Ando R., Hama H., Yamamoto-Hino M., Mizuno H., Miyawaki A. An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein. Proc. Natl. Acad. Sci. 99:2002;12651-12656
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 12651-12656
    • Ando, R.1    Hama, H.2    Yamamoto-Hino, M.3    Mizuno, H.4    Miyawaki, A.5
  • 8
    • 0347683437 scopus 로고    scopus 로고
    • Spatio-temporal regulation of Rac1 and Cdc42 activity during nerve growth factor-induced neurite outgrowth in PC12 cells
    • Aoki K., Nakamura T., Matsuda M. Spatio-temporal regulation of Rac1 and Cdc42 activity during nerve growth factor-induced neurite outgrowth in PC12 cells. J. Biol. Chem. 279:2004;713-719
    • (2004) J. Biol. Chem. , vol.279 , pp. 713-719
    • Aoki, K.1    Nakamura, T.2    Matsuda, M.3
  • 9
    • 0036221893 scopus 로고    scopus 로고
    • A genetically targetable fluorescent probe of channel gating with rapid kinetics
    • Ataka K., Pieribone V.A. A genetically targetable fluorescent probe of channel gating with rapid kinetics. Biophys. J. 82:2002;509-516
    • (2002) Biophys. J. , vol.82 , pp. 509-516
    • Ataka, K.1    Pieribone, V.A.2
  • 10
    • 0035941063 scopus 로고    scopus 로고
    • Antigen-independent selection of stable intracellular single-chain antibodies
    • Auf der Maur A., Escher D., Barberis A. Antigen-independent selection of stable intracellular single-chain antibodies. FEBS Lett. 508:2001;407-412
    • (2001) FEBS Lett. , vol.508 , pp. 407-412
    • Auf Der Maur, A.1    Escher, D.2    Barberis, A.3
  • 11
    • 0037397577 scopus 로고    scopus 로고
    • Optical nanosensors - Anenabling technology for intracellular measurements
    • Aylott J.W. Optical nanosensors - anenabling technology for intracellular measurements. Analyst. 128:2003;309-312
    • (2003) Analyst , vol.128 , pp. 309-312
    • Aylott, J.W.1
  • 12
    • 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. 96:1999;11241-11246
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 11241-11246
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 13
    • 0034710920 scopus 로고    scopus 로고
    • Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral
    • Baird G.S., Zacharias D.A., Tsien R.Y. Biochemistry, mutagenesis, and oligomerization of DsRed, a red fluorescent protein from coral. Proc. Natl. Acad. Sci. 97:2000;11984-11989
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 11984-11989
    • Baird, G.S.1    Zacharias, D.A.2    Tsien, R.Y.3
  • 16
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney C., Danuser G. FRET or no FRET: A quantitative comparison. Biophys. J. 84:2003;3992-4010
    • (2003) Biophys. J. , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 17
    • 0036138545 scopus 로고    scopus 로고
    • Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed)
    • Bevis B.J., Glick B.S. Rapidly maturing variants of the Discosoma red fluorescent protein (DsRed). Nat. Biotechnol. 20:2002;83-87
    • (2002) Nat. Biotechnol. , vol.20 , pp. 83-87
    • Bevis, B.J.1    Glick, B.S.2
  • 18
    • 0035871239 scopus 로고    scopus 로고
    • Seeing the wood through the trees: A review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence
    • Billinton N., Knight A.W. Seeing the wood through the trees: A review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence. Anal. Biochem. 291:2001;175-197
    • (2001) Anal. Biochem. , vol.291 , pp. 175-197
    • Billinton, N.1    Knight, A.W.2
  • 19
    • 10844257238 scopus 로고    scopus 로고
    • Getting proteins into cells
    • Bonetta L. Getting proteins into cells. The Scientist. 16:2002;38
    • (2002) The Scientist. , vol.16 , pp. 38
    • Bonetta, L.1
  • 20
    • 0035872320 scopus 로고    scopus 로고
    • Fluorescent nanosensors for intracellular chemical analysis: Decyl methacrylate liquid polymer matrix and ion-exchange-based potassium PEBBLE sensors with real-time application to viable rat C6 glioma cells
    • Brasuel M., Kopelman R., Miller T.J., Tjalkens R., Philbert M.A. Fluorescent nanosensors for intracellular chemical analysis: Decyl methacrylate liquid polymer matrix and ion-exchange-based potassium PEBBLE sensors with real-time application to viable rat C6 glioma cells. Anal. Chem. 73:2001;2221-2228
    • (2001) Anal. Chem. , vol.73 , pp. 2221-2228
    • Brasuel, M.1    Kopelman, R.2    Miller, T.J.3    Tjalkens, R.4    Philbert, M.A.5
  • 21
    • 0242351681 scopus 로고    scopus 로고
    • Liquid polymer nano-PEBBLEs for Cl-analysis and biological applications
    • Brasuel M.G., Miller T.J., Kopelman R., Philbert M.A. Liquid polymer nano-PEBBLEs for Cl-analysis and biological applications. Analyst. 128:2003;1262-1267
    • (2003) Analyst , vol.128 , pp. 1262-1267
    • Brasuel, M.G.1    Miller, T.J.2    Kopelman, R.3    Philbert, M.A.4
  • 22
    • 0242380805 scopus 로고    scopus 로고
    • Hetero-oligomeric tagging diminishes non-specific aggregation of target proteins fused with Anthozoa fluorescent proteins
    • Bulina M.E., Verkhusha V.V., Staroverov D.B., Chudakov D.M., Lukyanov K.A. Hetero-oligomeric tagging diminishes non-specific aggregation of target proteins fused with Anthozoa fluorescent proteins. Biochem. J. 371:2003;109-114
    • (2003) Biochem. J. , vol.371 , pp. 109-114
    • Bulina, M.E.1    Verkhusha, V.V.2    Staroverov, D.B.3    Chudakov, D.M.4    Lukyanov, K.A.5
  • 23
    • 0347364629 scopus 로고    scopus 로고
    • Gi protein activation in intact cells involves subunit rearrangement rather than dissociation
    • Bunemann M., Frank M., Lohse M.J. Gi protein activation in intact cells involves subunit rearrangement rather than dissociation. Proc. Natl. Acad. Sci. 100:2003;16077-16082
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 16077-16082
    • Bunemann, M.1    Frank, M.2    Lohse, M.J.3
  • 26
    • 0031019334 scopus 로고    scopus 로고
    • Confocal fluorescence microscopy using spectral and lifetime information to simultaneously record four fluorophores with high channel separation
    • Carlsson K., Liljeborg A. Confocal fluorescence microscopy using spectral and lifetime information to simultaneously record four fluorophores with high channel separation. J. Microsc. 185:1997;37-46
    • (1997) J. Microsc. , vol.185 , pp. 37-46
    • Carlsson, K.1    Liljeborg, A.2
  • 28
    • 0033621510 scopus 로고    scopus 로고
    • In vivo enzymatic protein biotinylation
    • Chapman-Smith A., Cronan J.E. Jr. In vivo enzymatic protein biotinylation. Biomol. Eng. 16:1999a;119-125
    • (1999) Biomol. Eng. , vol.16 , pp. 119-125
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 29
    • 0033199782 scopus 로고    scopus 로고
    • The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity
    • Chapman-Smith A., Cronan J.E. Jr. The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity. Trends Biochem. Sci. 24:1999b;359-363
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 359-363
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 30
    • 0029842109 scopus 로고    scopus 로고
    • Structure of the FKBP 12-rapamycin complex interacting with the binding domain of human FRAP
    • Choi J., Chen J., Schreiber S.L., Clardy J. Structure of the FKBP 12-rapamycin complex interacting with the binding domain of human FRAP. Science. 273:1996;239-242
    • (1996) Science , vol.273 , pp. 239-242
    • Choi, J.1    Chen, J.2    Schreiber, S.L.3    Clardy, J.4
  • 31
    • 1342309032 scopus 로고    scopus 로고
    • Gene delivery using physical methods: An overview
    • Chou T.H., Biswas S., Lu S. Gene delivery using physical methods: An overview. Methods Mol. Biol. 245:2004;147-166
    • (2004) Methods Mol. Biol. , vol.245 , pp. 147-166
    • Chou, T.H.1    Biswas, S.2    Lu, S.3
  • 33
    • 0347129672 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors
    • Clapp A.R., Medintz I.L., Mauro J.M., Fisher B.R., Bawendi M.G., Mattoussi H. Fluorescence resonance energy transfer between quantum dot donors and dye-labeled protein acceptors. J. Am. Chem. Soc. 126:2004;301-310
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 301-310
    • Clapp, A.R.1    Medintz, I.L.2    Mauro, J.M.3    Fisher, B.R.4    Bawendi, M.G.5    Mattoussi, H.6
  • 34
    • 0033231311 scopus 로고    scopus 로고
    • Optical nanosensors for chemical analysis inside single living cells. 1. Fabrication, characterization, and methods for intracellular delivery of PEBBLE sensors
    • Clark H.A., Hoyer M., Philbert M.A., Kopelman R. Optical nanosensors for chemical analysis inside single living cells. 1. Fabrication, characterization, and methods for intracellular delivery of PEBBLE sensors. Anal. Chem. 71:1999a;4831-4836
    • (1999) Anal. Chem. , vol.71 , pp. 4831-4836
    • Clark, H.A.1    Hoyer, M.2    Philbert, M.A.3    Kopelman, R.4
  • 35
    • 0033230266 scopus 로고    scopus 로고
    • Optical nanosensors for chemical analysis inside single living cells. 2. Sensors for pH and calcium and the intracellular application of PEBBLE sensors
    • Clark H.A., Kopelman R., Tjalkens R., Philbert M.A. Optical nanosensors for chemical analysis inside single living cells. 2. Sensors for pH and calcium and the intracellular application of PEBBLE sensors. Anal. Chem. 71:1999b;4837-4843
    • (1999) Anal. Chem. , vol.71 , pp. 4837-4843
    • Clark, H.A.1    Kopelman, R.2    Tjalkens, R.3    Philbert, M.A.4
  • 36
  • 37
    • 0000287353 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer
    • X.F. Wang, & B. Herman. London: Wiley
    • Clegg R.M. Fluorescence resonance energy transfer. Wang X.F., Herman B. "Fluorescence imaging spectroscopy and microscopy" 1996;180-252 Wiley, London
    • (1996) "fluorescence Imaging Spectroscopy and Microscopy" , pp. 180-252
    • Clegg, R.M.1
  • 39
    • 0034039320 scopus 로고    scopus 로고
    • LINKER: A program to generate linker sequences for fusion proteins
    • Crasto C.J., Feng J.A. LINKER: A program to generate linker sequences for fusion proteins. Protein Eng. 13:2000;309-312
    • (2000) Protein Eng. , vol.13 , pp. 309-312
    • Crasto, C.J.1    Feng, J.A.2
  • 40
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins
    • Cronan J.E. Jr. Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins. J. Biol. Chem. 265:1990;10327-10333
    • (1990) J. Biol. Chem. , vol.265 , pp. 10327-10333
    • Cronan Jr., J.E.1
  • 41
    • 0028816609 scopus 로고
    • The gene encoding the biotin-apoprotein ligase of Saccharomyces cerevisiae
    • Cronan J.E. Jr., Wallace J.C. The gene encoding the biotin-apoprotein ligase of Saccharomyces cerevisiae. FEMS Microbiol. Lett. 130:1995;221-229
    • (1995) FEMS Microbiol. Lett. , vol.130 , pp. 221-229
    • Cronan Jr., J.E.1    Wallace, J.C.2
  • 42
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M., Levi S., Luccardini C., Rostaing P., Riveau B., Triller A. Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science. 302:2003;442-445
    • (2003) Science , vol.302 , pp. 442-445
    • Dahan, M.1    Levi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5    Triller, A.6
  • 44
    • 0142134227 scopus 로고    scopus 로고
    • Cell damage and reactive oxygen species production induced by fluorescence microscopy: Effect on mitosis and guidelines for non-invasive fluorescence microscopy
    • Dixit R., Cyr R. Cell damage and reactive oxygen species production induced by fluorescence microscopy: Effect on mitosis and guidelines for non-invasive fluorescence microscopy. Plant J. 36:2003;280-290
    • (2003) Plant J. , vol.36 , pp. 280-290
    • Dixit, R.1    Cyr, R.2
  • 45
    • 0032784511 scopus 로고    scopus 로고
    • Design of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution
    • Doi N., Yanagawa H. Design of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution. FEBS Lett. 453:1999;305-307
    • (1999) FEBS Lett. , vol.453 , pp. 305-307
    • Doi, N.1    Yanagawa, H.2
  • 47
    • 0036160561 scopus 로고    scopus 로고
    • Fluorescence localization after photobleaching (FLAP): A new method for studying protein dynamics in living cells
    • Dunn G.A., Dobbie I.M., Monypenny J., Holt M.R., Zicha D. Fluorescence localization after photobleaching (FLAP): A new method for studying protein dynamics in living cells. J. Microsc. 205:2002;109-112
    • (2002) J. Microsc. , vol.205 , pp. 109-112
    • Dunn, G.A.1    Dobbie, I.M.2    Monypenny, J.3    Holt, M.R.4    Zicha, D.5
  • 48
    • 0037377291 scopus 로고    scopus 로고
    • A method for functional evaluation of caspase activation pathways in intact lymphoid cells using electroporation-mediated protein delivery and flow cytometric analysis
    • Eksioglu-Demiralp E., Kitada S., Carson D., Garland J., Andreef M., Reed J.C. A method for functional evaluation of caspase activation pathways in intact lymphoid cells using electroporation-mediated protein delivery and flow cytometric analysis. J. Immunol. Methods. 275:2003;41-56
    • (2003) J. Immunol. Methods , vol.275 , pp. 41-56
    • Eksioglu-Demiralp, E.1    Kitada, S.2    Carson, D.3    Garland, J.4    Andreef, M.5    Reed, J.C.6
  • 49
    • 12244312784 scopus 로고    scopus 로고
    • Characterization of one- and two-photon excitation fluorescence resonance energy transfer microscopy
    • Elangovan M., Wallrabe H., Chen Y., Day R.N., Barroso M., Periasamy A. Characterization of one- and two-photon excitation fluorescence resonance energy transfer microscopy. Methods. 29:2003;58-73
    • (2003) Methods , vol.29 , pp. 58-73
    • Elangovan, M.1    Wallrabe, H.2    Chen, Y.3    Day, R.N.4    Barroso, M.5    Periasamy, A.6
  • 50
    • 0030568916 scopus 로고    scopus 로고
    • The lanhanides as luminescent probes in investigation of biochemical systems
    • Elbanowski M., Makowska B. The lanhanides as luminescent probes in investigation of biochemical systems. J. Photochem. Photobiol. A. 99:1996;85-92
    • (1996) J. Photochem. Photobiol. A. , vol.99 , pp. 85-92
    • Elbanowski, M.1    Makowska, B.2
  • 52
    • 0037442458 scopus 로고    scopus 로고
    • Cytotoxicity of pEGFP vector is due to residues encoded by multiple cloning site
    • Endemann G., Schechtman D., Mochly-Rosen D. Cytotoxicity of pEGFP vector is due to residues encoded by multiple cloning site. Anal. Biochem. 313:2003;345-347
    • (2003) Anal. Biochem. , vol.313 , pp. 345-347
    • Endemann, G.1    Schechtman, D.2    Mochly-Rosen, D.3
  • 53
    • 0037564929 scopus 로고    scopus 로고
    • DsRed as a potential FRET partner with CFP and GFP
    • Erickson M.G., Moon D.L., Yue D.T. DsRed as a potential FRET partner with CFP and GFP. Biophys. J. 85:2003;599-611
    • (2003) Biophys. J. , vol.85 , pp. 599-611
    • Erickson, M.G.1    Moon, D.L.2    Yue, D.T.3
  • 54
    • 28044457973 scopus 로고    scopus 로고
    • Fluorescence Lifetime Imaging Microscopy (FLIM) (Unit 14.3)
    • New York: Wiley
    • Esposito A., Wouters F.S. Fluorescence Lifetime Imaging Microscopy (FLIM) (Unit 14.3). Current Protocols in Cell Biology,. 2004;Wiley, New York
    • (2004) Current Protocols in Cell Biology
    • Esposito, A.1    Wouters, F.S.2
  • 55
    • 0033583073 scopus 로고    scopus 로고
    • Receptor-mediated targeting of fluorescent probes in living cells
    • Farinas J., Verkman A.S. Receptor-mediated targeting of fluorescent probes in living cells. J. Biol. Chem. 274:1999;7603-7606
    • (1999) J. Biol. Chem. , vol.274 , pp. 7603-7606
    • Farinas, J.1    Verkman, A.S.2
  • 56
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • Förster T. Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann. Phys. 2:1948;55-75
    • (1948) Ann. Phys. , vol.2 , pp. 55-75
    • Förster, T.1
  • 57
    • 0002413436 scopus 로고
    • Delocalized Excitation and Excitation Transfer
    • O. Sinanoglu. New York: Academic Press
    • Förster T. Delocalized Excitation and Excitation Transfer. Sinanoglu O. "Modern Quantum Chemistry - Istanbul Lectures, Part III" 1965;93-137 Academic Press, New York
    • (1965) "modern Quantum Chemistry - Istanbul Lectures, Part III" , pp. 93-137
    • Förster, T.1
  • 61
    • 0346752072 scopus 로고    scopus 로고
    • Visualization of Rab5 activity in living cells by FRET microscopy and influence of plasma-membrane-targeted Rab5 on clathrin-dependent endocytosis
    • Galperin E., Sorkin A. Visualization of Rab5 activity in living cells by FRET microscopy and influence of plasma-membrane-targeted Rab5 on clathrin-dependent endocytosis. J. Cell Sci. 116:2003;4799-4810
    • (2003) J. Cell Sci. , vol.116 , pp. 4799-4810
    • Galperin, E.1    Sorkin, A.2
  • 62
    • 0038172566 scopus 로고    scopus 로고
    • Three modes of synaptic vesicular recycling revealed by single-vesicle imaging
    • Gandhi S.P., Stevens C.F. Three modes of synaptic vesicular recycling revealed by single-vesicle imaging. Nature. 423:2003;607-613
    • (2003) Nature , vol.423 , pp. 607-613
    • Gandhi, S.P.1    Stevens, C.F.2
  • 63
    • 1842836463 scopus 로고    scopus 로고
    • Quantum-dot nanocrystals for ultrasensitive biological labeling and multicolor optical encoding
    • Gao X., Chan W.C., Nie S. Quantum-dot nanocrystals for ultrasensitive biological labeling and multicolor optical encoding. J. Biomed. Opt. 7:2002;532-537
    • (2002) J. Biomed. Opt. , vol.7 , pp. 532-537
    • Gao, X.1    Chan, W.C.2    Nie, S.3
  • 64
    • 0035807983 scopus 로고    scopus 로고
    • The nature of fluorescence emission in the red fluorescent protein DsRed, revealed by single-molecule detection
    • Garcia-Parajo M.F., Koopman M., van Dijk E.M., Subramaniam V., van Hulst N.F. The nature of fluorescence emission in the red fluorescent protein DsRed, revealed by single-molecule detection. Proc. Natl. Acad. Sci. 98:2001;14392-14397
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 14392-14397
    • Garcia-Parajo, M.F.1    Koopman, M.2    Van Dijk, E.M.3    Subramaniam, V.4    Van Hulst, N.F.5
  • 67
    • 0036434301 scopus 로고    scopus 로고
    • An approach for reducing unwanted oligomerisation of DsRed fusion proteins
    • Gavin P., Devenish R.J., Prescott M. An approach for reducing unwanted oligomerisation of DsRed fusion proteins. Biochem. Biophys. Res. Commun. 298:2002;707-713
    • (2002) Biochem. Biophys. Res. Commun. , vol.298 , pp. 707-713
    • Gavin, P.1    Devenish, R.J.2    Prescott, M.3
  • 68
    • 0037590604 scopus 로고    scopus 로고
    • Overview of the Alliance for Cellular Signaling
    • Gilman A.G., Simon M.I., Bourne H.R., Harris B.A., Long R. the participating investigators and scientists of the Alliance for Cellular Signaling. Overview of the Alliance for Cellular Signaling. Nature. 420:2002;703-706
    • (2002) Nature , vol.420 , pp. 703-706
    • Gilman, A.G.1    Simon, M.I.2    Bourne, H.R.3    Harris, B.A.4    Long, R.5
  • 69
    • 0037178132 scopus 로고    scopus 로고
    • Diheteroarylethenes as thermally stable photoswitchable acceptors in photochromic fluorescence resonance energy transfer (pcFRET)
    • Giordano L., Jovin T.M., Irie M., Jares-Erijman E.A. Diheteroarylethenes as thermally stable photoswitchable acceptors in photochromic fluorescence resonance energy transfer (pcFRET). J. Am. Chem. Soc. 124:2002;7481-7489
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 7481-7489
    • Giordano, L.1    Jovin, T.M.2    Irie, M.3    Jares-Erijman, E.A.4
  • 70
    • 0037774580 scopus 로고    scopus 로고
    • Protein semi-synthesis in living cells
    • Giriat I., Muir T.W. Protein semi-synthesis in living cells. J. Am. Chem. Soc. 125:2003;7180-7181
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7180-7181
    • Giriat, I.1    Muir, T.W.2
  • 72
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon G.W., Berry G., Liang X.H., Levine B., Herman B. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74:1998;2702-2713
    • (1998) Biophys. J. , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 73
    • 0035884384 scopus 로고    scopus 로고
    • A method to measure the interaction of RacCdc42 with their binding partners using fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Graham D.L., Lowe P.N., Chalk P.A. A method to measure the interaction of RacCdc42 with their binding partners using fluorescence resonance energy transfer between mutants of green fluorescent protein. Anal. Biochem. 296:2001;208-217
    • (2001) Anal. Biochem. , vol.296 , pp. 208-217
    • Graham, D.L.1    Lowe, P.N.2    Chalk, P.A.3
  • 74
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • Griesbeck O., Baird G.S., Campbell R.E., Zacharias D.A., Tsien R.Y. Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications. J. Biol. Chem. 276:2001;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
  • 75
    • 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. 281:1998;269-272
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 77
    • 0036929862 scopus 로고    scopus 로고
    • Tuning FlaSh: Redesign of the dynamics, voltage range, and color of the genetically encoded optical sensor of membrane potential
    • Guerrero G., Siegel M.S., Roska B., Loots E., Isacoff E.Y. Tuning FlaSh: Redesign of the dynamics, voltage range, and color of the genetically encoded optical sensor of membrane potential. Biophys. J. 83:2002;3607-3618
    • (2002) Biophys. J. , vol.83 , pp. 3607-3618
    • Guerrero, G.1    Siegel, M.S.2    Roska, B.3    Loots, E.4    Isacoff, E.Y.5
  • 79
    • 0034941396 scopus 로고    scopus 로고
    • Quantum-dot-tagged microbeads for multiplexed optical coding of biomolecules
    • Han M., Gao X., Su J.Z., Nie S. Quantum-dot-tagged microbeads for multiplexed optical coding of biomolecules. Nat. Biotechnol. 19:2001;631-635
    • (2001) Nat. Biotechnol. , vol.19 , pp. 631-635
    • Han, M.1    Gao, X.2    Su, J.Z.3    Nie, S.4
  • 80
  • 82
    • 0035122528 scopus 로고    scopus 로고
    • Imaging FRET between spectrally similar GFP molecules in single cells
    • Harpur A.G., Wouters F.S., Bastiaens P.I. Imaging FRET between spectrally similar GFP molecules in single cells. Nat. Biotechnol. 19:2001;167-169
    • (2001) Nat. Biotechnol. , vol.19 , pp. 167-169
    • Harpur, A.G.1    Wouters, F.S.2    Bastiaens, P.I.3
  • 83
    • 0041810129 scopus 로고    scopus 로고
    • Triple FRET: A tool for studying long-range molecular interactions
    • Haustein E., Jahnz M., Schwille P. Triple FRET: A tool for studying long-range molecular interactions. Chemphyschem. 4:2003;745-748
    • (2003) Chemphyschem , vol.4 , pp. 745-748
    • Haustein, E.1    Jahnz, M.2    Schwille, P.3
  • 84
    • 0034710922 scopus 로고    scopus 로고
    • Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: Coral red (dsRed) and yellow (Citrine)
    • Heikal A.A., Hess S.T., Baird G.S., Tsien R.Y., Webb W.W. Molecular spectroscopy and dynamics of intrinsically fluorescent proteins: Coral red (dsRed) and yellow (Citrine). Proc. Natl. Acad. Sci. 97:2000;11996-12001
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 11996-12001
    • Heikal, A.A.1    Hess, S.T.2    Baird, G.S.3    Tsien, R.Y.4    Webb, W.W.5
  • 85
    • 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. 279:2004;14280-14286
    • (2004) J. Biol. Chem , vol.279 , pp. 14280-14286
    • Heim, N.1    Griesbeck, O.2
  • 86
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim R., Tsien R.Y. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6:1996;178-182
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 88
    • 0036669824 scopus 로고    scopus 로고
    • Measuring protein conformational changes by FRETLRET
    • Heyduk T. Measuring protein conformational changes by FRETLRET. Curr. Opin. Biotechnol. 13:2002;292-296
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 292-296
    • Heyduk, T.1
  • 89
    • 0036823319 scopus 로고    scopus 로고
    • Multispectral imaging fluorescence microscopy for living cells
    • Hiraoka Y., Shimi T., Haraguchi T. Multispectral imaging fluorescence microscopy for living cells. Cell Struct. Funct. 27:2002;367-374
    • (2002) Cell Struct. Funct. , vol.27 , pp. 367-374
    • Hiraoka, Y.1    Shimi, T.2    Haraguchi, T.3
  • 90
    • 0035956940 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator
    • Honda A., Adams S.R., Sawyer C.L., Lev-Ram V., Tsien R.Y., Dostmann W.R. Spatiotemporal dynamics of guanosine 3′,5′-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator. Proc. Natl. Acad. Sci. 98:2001;2437-2442
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 2437-2442
    • Honda, A.1    Adams, S.R.2    Sawyer, C.L.3    Lev-Ram, V.4    Tsien, R.Y.5    Dostmann, W.R.6
  • 91
    • 0036924067 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based stoichiometry in living cells
    • Hoppe A., Christensen K., Swanson J.A. Fluorescence resonance energy transfer-based stoichiometry in living cells. Biophys. J. 83:2002;3652-3664
    • (2002) Biophys. J. , vol.83 , pp. 3652-3664
    • Hoppe, A.1    Christensen, K.2    Swanson, J.A.3
  • 92
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu C.D., Chinenov Y., Kerppola T.K. Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell. 9:2002;789-798
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 93
    • 0037995710 scopus 로고    scopus 로고
    • Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis
    • Hu C.D., Kerppola T.K. Simultaneous visualization of multiple protein interactions in living cells using multicolor fluorescence complementation analysis. Nat. Biotechnol. 21:2003;539-545
    • (2003) Nat. Biotechnol. , vol.21 , pp. 539-545
    • Hu, C.D.1    Kerppola, T.K.2
  • 94
    • 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
    • Itoh R.E., Kurokawa K., Ohba Y., Yoshizaki H., Mochizuki N., Matsuda M. 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. 22:2002;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
  • 95
    • 0035844128 scopus 로고    scopus 로고
    • Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus
    • Iwai H., Lingel A., Pluckthun A. Cyclic green fluorescent protein produced in vivo using an artificially split PI-PfuI intein from Pyrococcus furiosus. J. Biol. Chem. 276:2001;16548-16554
    • (2001) J. Biol. Chem. , vol.276 , pp. 16548-16554
    • Iwai, H.1    Lingel, A.2    Pluckthun, A.3
  • 96
    • 0348087040 scopus 로고    scopus 로고
    • Long-term multiple color imaging of live cells using quantum dot bioconjugates
    • Jaiswal J.K., Mattoussi H., Mauro J.M., Simon S.M. Long-term multiple color imaging of live cells using quantum dot bioconjugates. Nat. Biotechnol. 21:2003;47-51
    • (2003) Nat. Biotechnol. , vol.21 , pp. 47-51
    • Jaiswal, J.K.1    Mattoussi, H.2    Mauro, J.M.3    Simon, S.M.4
  • 97
    • 0142246587 scopus 로고    scopus 로고
    • Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen
    • Jakobs S., Schauss A.C., Hell S.W. Photoconversion of matrix targeted GFP enables analysis of continuity and intermixing of the mitochondrial lumen. FEBS Lett. 554:2003;194-200
    • (2003) FEBS Lett. , vol.554 , pp. 194-200
    • Jakobs, S.1    Schauss, A.C.2    Hell, S.W.3
  • 99
    • 0034052719 scopus 로고    scopus 로고
    • Mechanism and cellular applications of a green fluorescent protein-based halide sensor
    • Jayaraman S., Haggie P., Wachter R.M., Remington S.J., Verkman A.S. Mechanism and cellular applications of a green fluorescent protein-based halide sensor. J. Biol. Chem. 275:2000;6047-6050
    • (2000) J. Biol. Chem. , vol.275 , pp. 6047-6050
    • Jayaraman, S.1    Haggie, P.2    Wachter, R.M.3    Remington, S.J.4    Verkman, A.S.5
  • 100
    • 0035969973 scopus 로고    scopus 로고
    • Enhanced fluorescence resonance energy transfer between spectral variants of green fluorescent protein through zinc-site engineering
    • Jensen K.K., Martini L., Schwartz T.W. Enhanced fluorescence resonance energy transfer between spectral variants of green fluorescent protein through zinc-site engineering. Biochemistry. 40:2001;938-945
    • (2001) Biochemistry , vol.40 , pp. 938-945
    • Jensen, K.K.1    Martini, L.2    Schwartz, T.W.3
  • 101
    • 0033777736 scopus 로고    scopus 로고
    • Development and application of a GFP-FRET intracellular caspase assay for drug screening
    • Jones J., Heim R., Hare E., Stack J., Pollok B.A. Development and application of a GFP-FRET intracellular caspase assay for drug screening. J. Biomol. Screen. 5:2000;307-318
    • (2000) J. Biomol. Screen , vol.5 , pp. 307-318
    • Jones, J.1    Heim, R.2    Hare, E.3    Stack, J.4    Pollok, B.A.5
  • 102
    • 0034644509 scopus 로고    scopus 로고
    • Signaling networks: The origins of cellular multitasking
    • Jordan J.D., Landau E.M., Iyengar R. Signaling networks: The origins of cellular multitasking. Cell. 103:2000;193-200
    • (2000) Cell , vol.103 , pp. 193-200
    • Jordan, J.D.1    Landau, E.M.2    Iyengar, R.3
  • 103
    • 0002090886 scopus 로고
    • FRET microscopy: Digital imaging of fluorescence resonance energy transfer. Application in cell biology
    • E. Kohen, J.S. Ploem, & J.G. Hirschberg. Orlando, FL: Academic Press
    • Jovin T.M., Arndt-Jovin D.J. FRET microscopy: Digital imaging of fluorescence resonance energy transfer. Application in cell biology. Kohen E., Ploem J.S., Hirschberg J.G. "Cell Structure and Function by Microspectrofluorometry" 1989;99-117 Academic Press, Orlando, FL
    • (1989) "cell Structure and Function by Microspectrofluorometry" , pp. 99-117
    • Jovin, T.M.1    Arndt-Jovin, D.J.2
  • 105
    • 0037399074 scopus 로고    scopus 로고
    • Directed evolution of O(6)-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 O(6)-Alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo. Chem. Biol. 10:2003;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
  • 106
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • Kalab P., Weis K., Heald R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science. 295:2002;2452-2456
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 108
    • 0141483388 scopus 로고    scopus 로고
    • A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling
    • Karasawa S., Araki T., Yamamoto-Hino M., Miyawaki A. A green-emitting fluorescent protein from Galaxeidae coral and its monomeric version for use in fluorescent labeling. Biol. Chem. 278:2003;34167-34171
    • (2003) Biol. Chem. , vol.278 , pp. 34167-34171
    • Karasawa, S.1    Araki, T.2    Yamamoto-Hino, M.3    Miyawaki, A.4
  • 109
    • 0033590779 scopus 로고    scopus 로고
    • Sequential multistep energy transfer: Enhancement of efficiency of long-range fluorescence resonance energy transfer
    • Kawahara S., Uchimaru T., Murata S. Sequential multistep energy transfer: Enhancement of efficiency of long-range fluorescence resonance energy transfer. Chem. Commun. 6:1999a;563-564
    • (1999) Chem. Commun. , vol.6 , pp. 563-564
    • Kawahara, S.1    Uchimaru, T.2    Murata, S.3
  • 110
    • 0033287416 scopus 로고    scopus 로고
    • Efficiency enhancement of long-range energy transfer by sequential multistep FRET using fluorescence labeled DNA
    • Kawahara S., Uchimaru T., Murata S. Efficiency enhancement of long-range energy transfer by sequential multistep FRET using fluorescence labeled DNA. Nucleic Acids Symp. Ser. 42:1999b;241-242
    • (1999) Nucleic Acids Symp. Ser. , vol.42 , pp. 241-242
    • Kawahara, S.1    Uchimaru, T.2    Murata, S.3
  • 111
    • 0035543198 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag
    • Keefe A.D., Wilson D.S., Seelig B., Szostak J.W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag. Protein Expr. Purif. 23:2001;440-446
    • (2001) Protein Expr. Purif. , vol.23 , pp. 440-446
    • Keefe, A.D.1    Wilson, D.S.2    Seelig, B.3    Szostak, J.W.4
  • 113
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., Springer T.A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science. 301:2003;1720-1725
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 114
    • 0031885535 scopus 로고    scopus 로고
    • Green fluorescent protein as a noninvasive intracellular pH indicator
    • Kneen M., Farinas J., Li Y., Verkman A.S. Green fluorescent protein as a noninvasive intracellular pH indicator. Biophys. J. 74:1998;1591-1599
    • (1998) Biophys. J. , vol.74 , pp. 1591-1599
    • Kneen, M.1    Farinas, J.2    Li, Y.3    Verkman, A.S.4
  • 115
    • 0036752203 scopus 로고    scopus 로고
    • Improved version of the red fluorescent protein (drFP583DsRedRFP)
    • 592, 594, 596-598, passim
    • Knop M., Barr F., Riedel C.G., Heckel T., Reichel C. Improved version of the red fluorescent protein (drFP583DsRedRFP). Biotechniques. 33:2002;. 592, 594, 596-598, passim
    • (2002) Biotechniques , vol.33
    • Knop, M.1    Barr, F.2    Riedel, C.G.3    Heckel, T.4    Reichel, C.5
  • 116
    • 0037125999 scopus 로고    scopus 로고
    • A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins
    • Kohl T., Heinze K.G., Kuhlemann R., Koltermann A., Schwille P. A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins. Proc. Natl. Acad. Sci. 99:2002;12161-12166
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 12161-12166
    • Kohl, T.1    Heinze, K.G.2    Kuhlemann, R.3    Koltermann, A.4    Schwille, P.5
  • 118
    • 1542373753 scopus 로고    scopus 로고
    • Co-activation of Rac1 and Cdc42 at lamellipodia and membrane ruffles induced by epidermal growth factor
    • Kurokawa K., Itoh R.E., Yoshizaki H., Ohba Y., Nakamura T., Matsuda M. Co-activation of Rac1 and Cdc42 at lamellipodia and membrane ruffles induced by epidermal growth factor. Mol. Biol. Cell. 15:2003;1003-1010
    • (2003) Mol. Biol. Cell. , vol.15 , pp. 1003-1010
    • Kurokawa, K.1    Itoh, R.E.2    Yoshizaki, H.3    Ohba, Y.4    Nakamura, T.5    Matsuda, M.6
  • 119
    • 0035903217 scopus 로고    scopus 로고
    • A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo
    • Kurokawa K., Mochizuki N., Ohba Y., Mizuno H., Miyawakr A., Matsuda M. A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. J. Biol. Chem. 276:2001;31305-31310
    • (2001) J. Biol. Chem. , vol.276 , pp. 31305-31310
    • Kurokawa, K.1    Mochizuki, N.2    Ohba, Y.3    Mizuno, H.4    Miyawakr, A.5    Matsuda, M.6
  • 121
    • 0347597739 scopus 로고    scopus 로고
    • The nano-tag, a streptavidin-binding peptide for the purification and detection of recombinant proteins
    • Lamla T., Erdmann V.A. The nano-tag, a streptavidin-binding peptide for the purification and detection of recombinant proteins. Protein Expr. Purif. 33:2004;39-47
    • (2004) Protein Expr. Purif. , vol.33 , pp. 39-47
    • Lamla, T.1    Erdmann, V.A.2
  • 125
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz J., Patterson G.H. Development and use of fluorescent protein markers in living cells. Science. 300:2003;87-91
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 128
    • 0037176245 scopus 로고    scopus 로고
    • FRET study of a trifluorophore-labeled DNAzyme
    • Liu J., Lu Y. FRET study of a trifluorophore-labeled DNAzyme. J. Am. Chem. Soc. 124:2002;15208-15216
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15208-15216
    • Liu, J.1    Lu, Y.2
  • 129
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis J., McCaffery J.M., Miyawaki A., Farquhar M.G., Tsien R.Y. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. 95:1998;6803-6808
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 130
    • 0035577918 scopus 로고    scopus 로고
    • Development of a time-resolved fluorescence resonance energy transfer assay (cell TR-FRET) for protein detection on intact cells
    • Lundin K., Blomberg K., Nordstrom T., Lindqvist C. Development of a time-resolved fluorescence resonance energy transfer assay (cell TR-FRET) for protein detection on intact cells. Anal. Biochem. 299:2001;92-97
    • (2001) Anal. Biochem. , vol.299 , pp. 92-97
    • Lundin, K.1    Blomberg, K.2    Nordstrom, T.3    Lindqvist, C.4
  • 131
    • 0034930509 scopus 로고    scopus 로고
    • Multiphoton-evoked color change of DsRed as an optical highlighter for cellular and subcellular labeling
    • Marchant J.S., Stutzmann G.E., Leissring M.A., LaFerla F.M., Parker I. Multiphoton-evoked color change of DsRed as an optical highlighter for cellular and subcellular labeling. Nat. Biotechnol. 19:2001;645-649
    • (2001) Nat. Biotechnol. , vol.19 , pp. 645-649
    • Marchant, J.S.1    Stutzmann, G.E.2    Leissring, M.A.3    Laferla, F.M.4    Parker, I.5
  • 132
    • 0033776271 scopus 로고    scopus 로고
    • Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis
    • Matsuyama S., Llopis J., Deveraux Q.L., Tsien R.Y., Reed J.C. Changes in intramitochondrial and cytosolic pH: Early events that modulate caspase activation during apoptosis. Nat. Cell Biol. 2:2000;318-325
    • (2000) Nat. Cell Biol. , vol.2 , pp. 318-325
    • Matsuyama, S.1    Llopis, J.2    Deveraux, Q.L.3    Tsien, R.Y.4    Reed, J.C.5
  • 134
    • 0036793311 scopus 로고    scopus 로고
    • Family of the green fluorescent protein: Journey to the end of the rainbow
    • Matz M.V., Lukyanov K.A., Lukyanov S.A. Family of the green fluorescent protein: Journey to the end of the rainbow. Bioessays. 24:2002;953-959
    • (2002) Bioessays , vol.24 , pp. 953-959
    • Matz, M.V.1    Lukyanov, K.A.2    Lukyanov, S.A.3
  • 135
    • 0035984645 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy for the detection and study of single molecules in biology
    • Medina M.A., Schwille P. Fluorescence correlation spectroscopy for the detection and study of single molecules in biology. Bioessays. 24:2002;758-764
    • (2002) Bioessays , vol.24 , pp. 758-764
    • Medina, M.A.1    Schwille, P.2
  • 137
    • 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. 394:1998;192-195
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 138
    • 0029898330 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein
    • Mitra R.D., Silva C.M., Youvan D.C. Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene. 173:1996;13-17
    • (1996) Gene , vol.173 , pp. 13-17
    • Mitra, R.D.1    Silva, C.M.2    Youvan, D.C.3
  • 139
    • 0037343944 scopus 로고    scopus 로고
    • Visualization of the spatial and temporal dynamics of intracellular signaling
    • Miyawaki A. 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
  • 140
    • 0033514515 scopus 로고    scopus 로고
    • Dynamic and quantitative Ca2+ measurements using improved cameleons
    • Miyawaki A., Griesbeck O., Heim R., Tsien R.Y. Dynamic and quantitative Ca2+ measurements using improved cameleons. Proc. Natl. Acad. Sci. 96:1999;2135-2140
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 2135-2140
    • Miyawaki, A.1    Griesbeck, O.2    Heim, R.3    Tsien, R.Y.4
  • 142
    • 0242361312 scopus 로고    scopus 로고
    • Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein
    • Mizuno H., Mal T.K., Tong K.I., Ando R., Furuta T., Ikura M., Miyawaki A. Photo-induced peptide cleavage in the green-to-red conversion of a fluorescent protein. Mol. Cell. 12:2003;1051-1058
    • (2003) Mol. Cell , vol.12 , pp. 1051-1058
    • Mizuno, H.1    Mal, T.K.2    Tong, K.I.3    Ando, R.4    Furuta, T.5    Ikura, M.6    Miyawaki, A.7
  • 143
    • 0035957110 scopus 로고    scopus 로고
    • Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer
    • Mizuno H., Sawano A., Eli P., Hama H., Miyawaki A. Red fluorescent protein from Discosoma as a fusion tag and a partner for fluorescence resonance energy transfer. Biochemistry. 40:2001;2502-2510
    • (2001) Biochemistry , vol.40 , pp. 2502-2510
    • Mizuno, H.1    Sawano, A.2    Eli, P.3    Hama, H.4    Miyawaki, A.5
  • 145
    • 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. 20:2002;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
  • 146
    • 0035853040 scopus 로고    scopus 로고
    • Circularly permuted green fluorescent proteins engineered to sense Ca2+
    • Nagai T., Sawano A., Park E.S., Miyawaki A. Circularly permuted green fluorescent proteins engineered to sense Ca2+. Proc. Natl. Acad. Sci. 98:2001;3197-3202
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 3197-3202
    • Nagai, T.1    Sawano, A.2    Park, E.S.3    Miyawaki, A.4
  • 147
    • 0035129282 scopus 로고    scopus 로고
    • A high signal-to-noise Ca(2+) probe composed of a single green fluorescent protein
    • Nakai J., Ohkura M., Imoto K. 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
  • 148
    • 0035387683 scopus 로고    scopus 로고
    • Imaging of conformational changes of proteins with a new environment-sensitive fluorescent probe designed for site-specific labeling of recombinant proteins in live cells
    • Nakanishi J., Nakajima T., Sato M., Ozawa T., Tohda K., Umezawa Y. Imaging of conformational changes of proteins with a new environment-sensitive fluorescent probe designed for site-specific labeling of recombinant proteins in live cells. Anal. Chem. 73:2001;2920-2928
    • (2001) Anal. Chem. , vol.73 , pp. 2920-2928
    • Nakanishi, J.1    Nakajima, T.2    Sato, M.3    Ozawa, T.4    Tohda, K.5    Umezawa, Y.6
  • 149
    • 0742286846 scopus 로고    scopus 로고
    • Optimizing imaging parameters for the separation of multiple labels in a fluorescence image
    • Neher R., Neher E. Optimizing imaging parameters for the separation of multiple labels in a fluorescence image. J. Microsc. 213:2004;46-62
    • (2004) J. Microsc. , vol.213 , pp. 46-62
    • Neher, R.1    Neher, E.2
  • 151
    • 0347418285 scopus 로고    scopus 로고
    • Application of quantum dots as probes for correlative fluorescence, conventional, and energy-filtered transmission electron microscopy
    • Nisman R., Dellaire G., Ren Y., Li R., Bazett-Jones D.P. Application of quantum dots as probes for correlative fluorescence, conventional, and energy-filtered transmission electron microscopy. J. Histochem. Cytochem. 52:2004;13-18
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 13-18
    • Nisman, R.1    Dellaire, G.2    Ren, Y.3    Li, R.4    Bazett-Jones, D.P.5
  • 152
    • 0037419262 scopus 로고    scopus 로고
    • A powerful combinatorial screen to identify high-affinity Terbium(III)-binding peptides
    • Nitz M., Franz K.J., Maglathlin R.L., Imperiali B. A powerful combinatorial screen to identify high-affinity Terbium(III)-binding peptides. Chem. Bio. Chem. 4:2003;272-276
    • (2003) Chem. Bio. Chem. , vol.4 , pp. 272-276
    • Nitz, M.1    Franz, K.J.2    Maglathlin, R.L.3    Imperiali, B.4
  • 154
    • 0037112385 scopus 로고    scopus 로고
    • A homogeneous and noncompetitive immunoassay based on the enhanced fluorescence resonance energy transfer by leucine zipper interaction
    • Ohiro Y., Arai R., Ueda H., Nagamune T. A homogeneous and noncompetitive immunoassay based on the enhanced fluorescence resonance energy transfer by leucine zipper interaction. Anal. Chem. 74:2002;5786-5792
    • (2002) Anal. Chem. , vol.74 , pp. 5786-5792
    • Ohiro, Y.1    Arai, R.2    Ueda, H.3    Nagamune, T.4
  • 156
    • 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. 20:2001;5853-5862
    • (2001) EMBO J. , vol.20 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 157
    • 0042563228 scopus 로고    scopus 로고
    • Ratiometric optical PEBBLE nanosensors for real-time magnesium ion concentrations inside viable cells
    • Park E.J., Brasuel M., Behrend C., Philbert M.A., Kopelman R. Ratiometric optical PEBBLE nanosensors for real-time magnesium ion concentrations inside viable cells. Anal. Chem. 75:2003;3784-3791
    • (2003) Anal. Chem. , vol.75 , pp. 3784-3791
    • Park, E.J.1    Brasuel, M.2    Behrend, C.3    Philbert, M.A.4    Kopelman, R.5
  • 158
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson G.H., Lippincott-Schwartz J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science. 297:2002;1873-1877
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 159
    • 0033545695 scopus 로고    scopus 로고
    • Simultaneous detection of multiple fluorescent proteins in live cells by fluorescence lifetime imaging microscopy
    • Pepperkok R., Squire A., Geley S., Bastiaens P.I.H. Simultaneous detection of multiple fluorescent proteins in live cells by fluorescence lifetime imaging microscopy. Curr. Biol. 11:1999;269-272
    • (1999) Curr. Biol. , vol.11 , pp. 269-272
    • Pepperkok, R.1    Squire, A.2    Geley, S.3    Bastiaens, P.I.H.4
  • 163
    • 0034880727 scopus 로고    scopus 로고
    • Biochemically functionalized silica nanoparticles
    • Qhobosheane M., Santra S., Zhang P., Tan W. Biochemically functionalized silica nanoparticles. Analyst. 126:2001;1274-1278
    • (2001) Analyst , vol.126 , pp. 1274-1278
    • Qhobosheane, M.1    Santra, S.2    Zhang, P.3    Tan, W.4
  • 164
    • 0037025346 scopus 로고    scopus 로고
    • Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3
    • Rehm M., Dussmann H., Janicke R.U., Tavare J.M., Kogel D., Prehn J.H. Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3. J. Biol. Chem. 277:2002;24506-24514
    • (2002) J. Biol. Chem. , vol.277 , pp. 24506-24514
    • Rehm, M.1    Dussmann, H.2    Janicke, R.U.3    Tavare, J.M.4    Kogel, D.5    Prehn, J.H.6
  • 165
    • 0038664388 scopus 로고    scopus 로고
    • Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy
    • Riven I., Kalmanzon E., Segev L., Reuveny E. Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy. Neuron. 38:2003;225-235
    • (2003) Neuron , vol.38 , pp. 225-235
    • Riven, I.1    Kalmanzon, E.2    Segev, L.3    Reuveny, E.4
  • 167
    • 0037077713 scopus 로고    scopus 로고
    • Oligomerization of DsRed is required for the generation of a functional red fluorescent chromophore
    • Sacchetti A., Subramaniam V., Jovin T.M., Alberti S. Oligomerization of DsRed is required for the generation of a functional red fluorescent chromophore. FEBS Lett. 525:2002;13-19
    • (2002) FEBS Lett. , vol.525 , pp. 13-19
    • Sacchetti, A.1    Subramaniam, V.2    Jovin, T.M.3    Alberti, S.4
  • 168
    • 0034912282 scopus 로고    scopus 로고
    • Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein
    • Sakai R., Repunte-Canonigo V., Raj C.D., Knopfel T. Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein. Eur. J. Neurosci. 13:2001;2314-2318
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 2314-2318
    • Sakai, R.1    Repunte-Canonigo, V.2    Raj, C.D.3    Knopfel, T.4
  • 169
    • 0036823444 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy for single-molecule imaging in living cells
    • Sako Y., Uyemura T. Total internal reflection fluorescence microscopy for single-molecule imaging in living cells. Cell Struct. Funct. 27:2002;357-365
    • (2002) Cell Struct. Funct. , vol.27 , pp. 357-365
    • Sako, Y.1    Uyemura, T.2
  • 170
  • 171
    • 0025060796 scopus 로고
    • Expression of a cloned streptavidin gene in Escherichia coli
    • Sano T., Cantor C.R. Expression of a cloned streptavidin gene in Escherichia coli. Proc. Natl. Acad. Sci. 87:1990;142-146
    • (1990) Proc. Natl. Acad. Sci. , vol.87 , pp. 142-146
    • Sano, T.1    Cantor, C.R.2
  • 172
    • 0035886682 scopus 로고    scopus 로고
    • Conjugation of biomolecules with luminophore-doped silica nanoparticles for photostable biomarkers
    • Santra S., Zhang P., Wang K., Tapec R., Tan W. Conjugation of biomolecules with luminophore-doped silica nanoparticles for photostable biomarkers. Anal. Chem. 73:2001;4988-4993
    • (2001) Anal. Chem. , vol.73 , pp. 4988-4993
    • Santra, S.1    Zhang, P.2    Wang, K.3    Tapec, R.4    Tan, W.5
  • 173
    • 0034671963 scopus 로고    scopus 로고
    • Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Ialpha and green fluorescent proteins
    • Sato M., Hida N., Ozawa T., Umezawa Y. Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Ialpha and green fluorescent proteins. Anal. Chem. 72:2000;5918-5924
    • (2000) Anal. Chem. , vol.72 , pp. 5918-5924
    • Sato, M.1    Hida, N.2    Ozawa, T.3    Umezawa, Y.4
  • 174
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • Sato M., Dzawa T., Inukai K., Asano T., Umezawa Y. Fluorescent indicators for imaging protein phosphorylation in single living cells. Nat. Biotechnol. 20:2002;287-294
    • (2002) Nat. Biotechnol. , vol.20 , pp. 287-294
    • Sato, M.1    Dzawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 175
    • 0031241658 scopus 로고    scopus 로고
    • Photoactivation of green fluorescent protein
    • Sawin K.E., Nurse P. Photoactivation of green fluorescent protein. Curr. Biol. 7:1997;R606-R607
    • (1997) Curr. Biol. , vol.7
    • Sawin, K.E.1    Nurse, P.2
  • 176
    • 0032715660 scopus 로고    scopus 로고
    • Nonlinear fluorescence through intermolecular energy transfer and resolution increase in fluorescence microscopy
    • Schönle A., Hänninen P.E., Hell S.W. Nonlinear fluorescence through intermolecular energy transfer and resolution increase in fluorescence microscopy. Ann. Phys. 8:1999;115-144
    • (1999) Ann. Phys. , vol.8 , pp. 115-144
    • Schönle, A.1    Hänninen, P.E.2    Hell, S.W.3
  • 177
    • 0037446762 scopus 로고    scopus 로고
    • Rational design of genetically encoded fluorescence resonance energy transfer-based sensors of cellular Cdc42 signaling
    • Seth A., Otomo T., Yin H.L., Rosen M.K. Rational design of genetically encoded fluorescence resonance energy transfer-based sensors of cellular Cdc42 signaling. Biochemistry. 42:2003;3997-4008
    • (2003) Biochemistry , vol.42 , pp. 3997-4008
    • Seth, A.1    Otomo, T.2    Yin, H.L.3    Rosen, M.K.4
  • 179
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O., Johnson F.H., Saiga Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell Comp. Physiol. 59:1962;223-239
    • (1962) J. Cell Comp. Physiol. , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 181
    • 0030834492 scopus 로고    scopus 로고
    • A genetically encoded optical probe of membrane voltage
    • Siegel M.S., Isacoff E.Y. A genetically encoded optical probe of membrane voltage. Neuron. 19:1997;735-741
    • (1997) Neuron , vol.19 , pp. 735-741
    • Siegel, M.S.1    Isacoff, E.Y.2
  • 182
    • 0037093074 scopus 로고    scopus 로고
    • Labeling of antibodies by in situ modification of thiol groups generated from selenol-catalyzed reduction of native disulfide bonds
    • Singh R., Maloney E.K. Labeling of antibodies by in situ modification of thiol groups generated from selenol-catalyzed reduction of native disulfide bonds. Anal. Biochem. 304:2002;147-156
    • (2002) Anal. Biochem. , vol.304 , pp. 147-156
    • Singh, R.1    Maloney, E.K.2
  • 183
    • 0000010409 scopus 로고
    • Time-resolved fluorescence of lanthanide probes and applications in biotechnology
    • Soini E., Lövgren T. Time-resolved fluorescence of lanthanide probes and applications in biotechnology. CRC Crit. Rev. Am. Chem. 18:1987;105-154
    • (1987) CRC Crit. Rev. Am. Chem. , vol.18 , pp. 105-154
    • Soini, E.1    Lövgren, T.2
  • 184
    • 0035836703 scopus 로고    scopus 로고
    • The many ways to cross the plasma membrane
    • Stephens D.J., Pepperkok R. The many ways to cross the plasma membrane. Proc. Natl. Acad. Sci. 98:2001;4295-4298
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 4295-4298
    • Stephens, D.J.1    Pepperkok, R.2
  • 185
    • 0036141883 scopus 로고    scopus 로고
    • A fluorescent PEBBLE nanosensor for intracellular free zinc
    • Sumner J.P., Aylott J.W., Monson E., Kopelman R. A fluorescent PEBBLE nanosensor for intracellular free zinc. Analyst. 127:2002;11-16
    • (2002) Analyst , vol.127 , pp. 11-16
    • Sumner, J.P.1    Aylott, J.W.2    Monson, E.3    Kopelman, R.4
  • 186
    • 0037419268 scopus 로고    scopus 로고
    • A novel design method of ratiometric fluorescent probes based on fluorescence resonance energy transfer switching by spectral overlap integral
    • Takakusa H., Kikuchi K., Urano Y., Kojima H., Nagano T. A novel design method of ratiometric fluorescent probes based on fluorescence resonance energy transfer switching by spectral overlap integral. Chemistry. 9:2003;1479-1485
    • (2003) Chemistry , vol.9 , pp. 1479-1485
    • Takakusa, H.1    Kikuchi, K.2    Urano, Y.3    Kojima, H.4    Nagano, T.5
  • 187
    • 0037455553 scopus 로고    scopus 로고
    • Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects
    • Takemoto K., Nagai T., Miyawaki A., Miura M. Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects. J. Cell Biol. 160:2003;235-243
    • (2003) J. Cell Biol. , vol.160 , pp. 235-243
    • Takemoto, K.1    Nagai, T.2    Miyawaki, A.3    Miura, M.4
  • 188
    • 0842321977 scopus 로고    scopus 로고
    • Time-wavelength two-dimensional femtosecond fluorescence imaging
    • Takeuchi S., Tahara T. Time-wavelength two-dimensional femtosecond fluorescence imaging. Opt. Lett. 29:2004;313-315
    • (2004) Opt. Lett. , vol.29 , pp. 313-315
    • Takeuchi, S.1    Tahara, T.2
  • 189
    • 0041366860 scopus 로고    scopus 로고
    • Development of organic dye-doped silica nanoparticles for bioanalysis and biosensors
    • Tapec R., Zhao X.J., Tan W. Development of organic dye-doped silica nanoparticles for bioanalysis and biosensors. J. Nanosci. Nanotechnol. 2:2002;405-409
    • (2002) J. Nanosci. Nanotechnol. , vol.2 , pp. 405-409
    • Tapec, R.1    Zhao, X.J.2    Tan, W.3
  • 190
    • 0035135797 scopus 로고    scopus 로고
    • Quantitative analysis of fluorescent caspase substrate cleavage in intact cells and identification of novel inhibitors of apoptosis
    • Tawa P., Tam J., Cassady R., Nicholson D.W., Xanthoudakis S. Quantitative analysis of fluorescent caspase substrate cleavage in intact cells and identification of novel inhibitors of apoptosis. Cell Death Differ. 8:2001;30-37
    • (2001) Cell Death Differ , vol.8 , pp. 30-37
    • Tawa, P.1    Tam, J.2    Cassady, R.3    Nicholson, D.W.4    Xanthoudakis, S.5
  • 191
    • 0345873536 scopus 로고    scopus 로고
    • Delivery of bioactive, gel-isolated proteins into live cells
    • Taylor J.E., Fernandez-Patron C. Delivery of bioactive, gel-isolated proteins into live cells. Electrophoresis. 24:2003;1331-1337
    • (2003) Electrophoresis , vol.24 , pp. 1331-1337
    • Taylor, J.E.1    Fernandez-Patron, C.2
  • 193
    • 0037040893 scopus 로고    scopus 로고
    • Analysis of DsRed mutants. Space around the fluorophore accelerates fluorescence development
    • Terskikh A.V., Fradkov A.F., Zaraisky A.G., Kajava A.V., Angres B. Analysis of DsRed mutants. Space around the fluorophore accelerates fluorescence development. J. Biol. Chem. 277:2002;7633-7636
    • (2002) J. Biol. Chem. , vol.277 , pp. 7633-7636
    • Terskikh, A.V.1    Fradkov, A.F.2    Zaraisky, A.G.3    Kajava, A.V.4    Angres, B.5
  • 194
    • 0034644538 scopus 로고    scopus 로고
    • Translocation and reversible localization of signaling proteins: A dynamic future for signal transduction
    • Teruel M.N., Meyer T. Translocation and reversible localization of signaling proteins: a dynamic future for signal transduction. Cell. 103:2000;181-184
    • (2000) Cell , vol.103 , pp. 181-184
    • Teruel, M.N.1    Meyer, T.2
  • 195
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting A.Y., Kain K.H., Klemke R.L., Tsien R.Y. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl. Acad. Sci. 98:2001;15003-15008
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 196
    • 0037124666 scopus 로고    scopus 로고
    • New methods for proteomic research: Preparation of proteins with N-terminal cysteines for labeling and conjugation
    • Tolbert T.J., Wong C.-H. New methods for proteomic research: Preparation of proteins with N-terminal cysteines for labeling and conjugation. Angew Chem. Int. Ed. Engl. 41:2002;2171-2174
    • (2002) Angew Chem. Int. Ed. Engl. , vol.41 , pp. 2171-2174
    • Tolbert, T.J.1    Wong, C.-H.2
  • 197
    • 0037427330 scopus 로고    scopus 로고
    • Solvent-sensitive dyes to report protein conformational changes in living cells
    • Toutchkine A., Kraynov V., Hahn K. Solvent-sensitive dyes to report protein conformational changes in living cells. J. Am. Chem. Soc. 125:(14):2003;4132-4145
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.14 , pp. 4132-4145
    • Toutchkine, A.1    Kraynov, V.2    Hahn, K.3
  • 198
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien R.Y. The green fluorescent protein. Annu. Rev. Biochem. 67:1998;509-544
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 199
    • 0037121966 scopus 로고    scopus 로고
    • Activation of Rac1 by shear stress in endothelial cells mediates both cytoskeletal reorganization and effects on gene expression
    • Tzima E., Del Pozo M.A., Kiosses W.B., Mohamed S.A., Li S., Chien S., Schwartz M.A. Activation of Rac1 by shear stress in endothelial cells mediates both cytoskeletal reorganization and effects on gene expression. EMBO J. 21:2002;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    Chien, S.6    Schwartz, M.A.7
  • 200
    • 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
    • Tzima E., Kiosses W.B., del Pozo M.A., Schwartz M.A. 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. 278:2003;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
  • 202
    • 1542336956 scopus 로고    scopus 로고
    • The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins
    • Verkhusha V.V., Lukyanov K.A. The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins. Nat. Biotechnol. 22:2004;289-296
    • (2004) Nat. Biotechnol. , vol.22 , pp. 289-296
    • Verkhusha, V.V.1    Lukyanov, K.A.2
  • 203
    • 0035839465 scopus 로고    scopus 로고
    • An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation
    • Verkhusha V.V., Otsuna H., Awasaki T., Oda H., Tsukita S., Ito K. An enhanced mutant of red fluorescent protein DsRed for double labeling and developmental timer of neural fiber bundle formation. J. Biol. Chem. 276:2001;29621-29624
    • (2001) J. Biol. Chem. , vol.276 , pp. 29621-29624
    • Verkhusha, V.V.1    Otsuna, H.2    Awasaki, T.3    Oda, H.4    Tsukita, S.5    Ito, K.6
  • 204
    • 0034029599 scopus 로고    scopus 로고
    • Global analysis of fluorescence lifetime imaging microscopy data
    • Verveer P.J., Squire A., Bastiaens P.I. Global analysis of fluorescence lifetime imaging microscopy data. Biophys. J. 78:2000b;2127-2137
    • (2000) Biophys. J. , vol.78 , pp. 2127-2137
    • Verveer, P.J.1    Squire, A.2    Bastiaens, P.I.3
  • 205
    • 0034711405 scopus 로고    scopus 로고
    • Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane
    • Verveer P.J., Wouters F.S., Reynolds A.R., Bastiaens P.I. Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane. Science. 290:2000a;1567-1570
    • (2000) Science , vol.290 , pp. 1567-1570
    • Verveer, P.J.1    Wouters, F.S.2    Reynolds, A.R.3    Bastiaens, P.I.4
  • 206
    • 0034731391 scopus 로고    scopus 로고
    • Denaturation and partial renaturation of a tightly tetramerized DsRed protein under mildly acidic conditions
    • Vrzheshch P.V., Akovbian N.A., Varfolomeyey S.D., Verkhusha V.V. Denaturation and partial renaturation of a tightly tetramerized DsRed protein under mildly acidic conditions. FEBS Lett. 487:2000;203-208
    • (2000) FEBS Lett. , vol.487 , pp. 203-208
    • Vrzheshch, P.V.1    Akovbian, N.A.2    Varfolomeyey, S.D.3    Verkhusha, V.V.4
  • 207
    • 0033539088 scopus 로고    scopus 로고
    • Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate
    • Wachter R.M., Remington S.J. Sensitivity of the yellow variant of green fluorescent protein to halides and nitrate. Curr. Biol. 9:1999;R628-R629
    • (1999) Curr. Biol. , vol.9
    • Wachter, R.M.1    Remington, S.J.2
  • 209
    • 0038048992 scopus 로고    scopus 로고
    • Modulation of cellular function by TAT mediated transduction of full length proteins
    • Wadia J.S., Dowdy S.F. Modulation of cellular function by TAT mediated transduction of full length proteins. Curr. Protein Pept. Sci. 4:2003;97-104
    • (2003) Curr. Protein Pept. Sci. , vol.4 , pp. 97-104
    • Wadia, J.S.1    Dowdy, S.F.2
  • 211
    • 0033674629 scopus 로고    scopus 로고
    • The structural basis for red fluorescence in the tetrameric GFP homolog DsRed
    • Wall M.A., Socolich M., Ranganathan R. The structural basis for red fluorescence in the tetrameric GFP homolog DsRed. Nat. Struct. Biol. 7:2000;1133-1138
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1133-1138
    • Wall, M.A.1    Socolich, M.2    Ranganathan, R.3
  • 212
    • 0001444110 scopus 로고
    • A two-dimensional fluorescence lifetime imaging system using a gated image intensifier
    • Wang X.F., Uchida T., Coleman D.M., Minami S. A two-dimensional fluorescence lifetime imaging system using a gated image intensifier. Appl. Spectrosc. 45:1991;360-366
    • (1991) Appl. Spectrosc. , vol.45 , pp. 360-366
    • Wang, X.F.1    Uchida, T.2    Coleman, D.M.3    Minami, S.4
  • 214
    • 0037314241 scopus 로고    scopus 로고
    • Lighting up cells with quantum dots
    • 302-303
    • Watson A., Wu X., Bruchez M. Lighting up cells with quantum dots. Biotechniques. 34:2003;296-300. 302-303
    • (2003) Biotechniques , vol.34 , pp. 296-300
    • Watson, A.1    Wu, X.2    Bruchez, M.3
  • 216
    • 0642366760 scopus 로고    scopus 로고
    • Engineered nanomaterials for biophotonics applications: Improving sensing, imaging, and therapeutics
    • West J.L., Halas N.J. Engineered nanomaterials for biophotonics applications: Improving sensing, imaging, and therapeutics. Annu. Rev. Biomed. Eng. 5:2003;285-292
    • (2003) Annu. Rev. Biomed. Eng. , vol.5 , pp. 285-292
    • West, J.L.1    Halas, N.J.2
  • 217
    • 0033533709 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
    • Wouters F.S., Bastiaens P.I. Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells. Curr. Biol. 9:1999;1127-1130
    • (1999) Curr. Biol. , vol.9 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 218
    • 0032535138 scopus 로고    scopus 로고
    • FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes
    • Wouters F.S., Bastiaens P.I., Wirtz K.W., Jovin T.M. FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes. EMBO J. 17:1998;7179-7189
    • (1998) EMBO J. , vol.17 , pp. 7179-7189
    • Wouters, F.S.1    Bastiaens, P.I.2    Wirtz, K.W.3    Jovin, T.M.4
  • 223
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia Z., Liu Y. Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81:2001;2395-2402
    • (2001) Biophys. J. , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 224
    • 0036854369 scopus 로고    scopus 로고
    • Fluorescent nano-PEBBLE sensors designed for intracellular glucose imaging
    • Xu H., Aylott J.W., Kopelman R. Fluorescent nano-PEBBLE sensors designed for intracellular glucose imaging. Analyst. 127:2002;1471-1477
    • (2002) Analyst , vol.127 , pp. 1471-1477
    • Xu, H.1    Aylott, J.W.2    Kopelman, R.3
  • 225
    • 0035448944 scopus 로고    scopus 로고
    • A real-time ratiometric method for the determination of molecular oxygen inside living cells using sol-gel-based spherical optical nanosensors with applications to rat C6 glioma
    • Xu H., Aylott J.W., Kopelman R., Miller T.J., Philbert M.A. A real-time ratiometric method for the determination of molecular oxygen inside living cells using sol-gel-based spherical optical nanosensors with applications to rat C6 glioma. Anal. Chem. 73:2001;4124-4133
    • (2001) Anal. Chem. , vol.73 , pp. 4124-4133
    • Xu, H.1    Aylott, J.W.2    Kopelman, R.3    Miller, T.J.4    Philbert, M.A.5
  • 229
    • 0029742203 scopus 로고    scopus 로고
    • Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement
    • Yokoe H., Meyer T. Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement. Nat. Biotechnol. 14:1996;1252-1252
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1252-1252
    • Yokoe, H.1    Meyer, T.2
  • 231
    • 0034581555 scopus 로고    scopus 로고
    • Synapto-pHluorins: Chimeras between pH-sensitive mutants of green fluorescent protein and synaptic vesicle membrane proteins as reporters of neurotransmitter release
    • Yuste R., Miller R.B., Holthoff K., Zhang S., Miesenbock G. Synapto-pHluorins: Chimeras between pH-sensitive mutants of green fluorescent protein and synaptic vesicle membrane proteins as reporters of neurotransmitter release. Methods Enzymol. 327:2000;522-546
    • (2000) Methods Enzymol. , vol.327 , pp. 522-546
    • Yuste, R.1    Miller, R.B.2    Holthoff, K.3    Zhang, S.4    Miesenbock, G.5
  • 233
    • 0036500494 scopus 로고    scopus 로고
    • Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes
    • Zaccolo M., Pozzan T. 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
  • 234
    • 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. 296:2002;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
  • 235
    • 3042511548 scopus 로고    scopus 로고
    • Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP
    • Zapata-Hommer O., Griesbeck O. Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP. BMC Biotechnol. 3:2003;5
    • (2003) BMC Biotechnol. , vol.3 , pp. 5
    • Zapata-Hommer, O.1    Griesbeck, O.2
  • 237
    • 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. 98:2001;14997-15002
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 14997-15002
    • Zhang, J.1    Ma, Y.2    Taylor, S.S.3    Tsien, R.Y.4
  • 238
    • 0347511729 scopus 로고    scopus 로고
    • Intracellular cargo delivery using tat peptide and derivatives
    • Zhao M., Weissleder R. Intracellular cargo delivery using tat peptide and derivatives. Med. Res. Rev. 24:2004;1-12
    • (2004) Med. Res. Rev. , vol.24 , pp. 1-12
    • Zhao, M.1    Weissleder, R.2
  • 239
    • 0037028016 scopus 로고    scopus 로고
    • Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit
    • Zheng J., Trudeau M.C., Zagotta W.N. Rod cyclic nucleotide-gated channels have a stoichiometry of three CNGA1 subunits and one CNGB1 subunit. Neuron. 36:2002;891-896
    • (2002) Neuron , vol.36 , pp. 891-896
    • Zheng, J.1    Trudeau, M.C.2    Zagotta, W.N.3
  • 240
    • 0042336988 scopus 로고    scopus 로고
    • Disruption of an intersubunit interaction underlies Ca2+-calmodulin modulation of cyclic nucleotide-gated channels
    • Zheng J., Varnum M.D., Zagotta W.N. Disruption of an intersubunit interaction underlies Ca2+-calmodulin modulation of cyclic nucleotide-gated channels. J. Neurosci. 23:2003;8167-8175
    • (2003) J. Neurosci. , vol.23 , pp. 8167-8175
    • Zheng, J.1    Varnum, M.D.2    Zagotta, W.N.3
  • 242
    • 0037032454 scopus 로고    scopus 로고
    • Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2-YFP FRET pair
    • Zimmermann T., Rietdorf J., Girod A., Georget V., Pepperkok R. Spectral imaging and linear un-mixing enables improved FRET efficiency with a novel GFP2-YFP FRET pair. FEBS Lett. 531:2002;245-249
    • (2002) FEBS Lett. , vol.531 , pp. 245-249
    • Zimmermann, T.1    Rietdorf, J.2    Girod, A.3    Georget, V.4    Pepperkok, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.