메뉴 건너뛰기




Volumn 19, Issue 7, 2005, Pages 1675-1686

Imaging molecular interactions in living cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR;

EID: 22444447736     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2005-0028     Document Type: Short Survey
Times cited : (76)

References (102)
  • 1
    • 0035102090 scopus 로고    scopus 로고
    • The color of mice: In the light of GFP-variant reporters
    • Hadjantonakis AK, Nagy A 2001 The color of mice: in the light of GFP-variant reporters. Histochem Cell Biol 115:49-58
    • (2001) Histochem Cell Biol , vol.115 , pp. 49-58
    • Hadjantonakis, A.K.1    Nagy, A.2
  • 2
    • 3142736368 scopus 로고    scopus 로고
    • Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer
    • Karasawa S, Araki T, Nagai T, Mizuno H, Miyawaki A 2004 Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer. Biochem J 381:307-312
    • (2004) Biochem J , vol.381 , pp. 307-312
    • Karasawa, S.1    Araki, T.2    Nagai, T.3    Mizuno, H.4    Miyawaki, A.5
  • 3
    • 0036793311 scopus 로고    scopus 로고
    • Family of the green fluorescent protein: Journey to the end of the rainbow
    • Matz MV, Lukyanov KA, Lukyanov SA 2002 Family of the green fluorescent protein: journey to the end of the rainbow. Bioessays 24:953-959
    • (2002) Bioessays , vol.24 , pp. 953-959
    • Matz, M.V.1    Lukyanov, K.A.2    Lukyanov, S.A.3
  • 5
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner NC, Campbell RE, Steinbach PA, Giepmans BN, Palmer AE, Tsien RY 2004 Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 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
  • 9
    • 0037426977 scopus 로고    scopus 로고
    • In vivo time-lapse imaging of synaptic takeover associated with naturally occurring synapse elimination
    • Walsh MK, Lichtman JW 2003 In vivo time-lapse imaging of synaptic takeover associated with naturally occurring synapse elimination. Neuron 37:67-73
    • (2003) Neuron , vol.37 , pp. 67-73
    • Walsh, M.K.1    Lichtman, J.W.2
  • 11
    • 0036143190 scopus 로고    scopus 로고
    • Imaging into the future: Visualizing gene expression and protein interactions with fluorescent proteins
    • van Roessel P, Brand AH 2002 Imaging into the future: visualizing gene expression and protein interactions with fluorescent proteins. Nat Cell Biol 4:E15-E20
    • (2002) Nat Cell Biol , vol.4
    • Van Roessel, P.1    Brand, A.H.2
  • 13
    • 0036266863 scopus 로고    scopus 로고
    • To 5D and beyond: Quantitative fluorescence microscopy in the post-genomic era
    • Andrews PD, Harper IS, Swedlow JR 2002 To 5D and beyond: quantitative fluorescence microscopy in the post-genomic era. Traffic 3:29-36
    • (2002) Traffic , vol.3 , pp. 29-36
    • Andrews, P.D.1    Harper, I.S.2    Swedlow, J.R.3
  • 14
    • 0036823318 scopus 로고    scopus 로고
    • Live cell imaging using wide-field microscopy and deconvolution
    • Swedlow JR, Platani M 2002 Live cell imaging using wide-field microscopy and deconvolution. Cell Struct Funct 27:335-342
    • (2002) Cell Struct Funct , vol.27 , pp. 335-342
    • Swedlow, J.R.1    Platani, M.2
  • 15
    • 0042839654 scopus 로고    scopus 로고
    • 4D imaging to assay complex dynamics in live specimens
    • Gerlich D, Ellenberg J 2003 4D imaging to assay complex dynamics in live specimens. Nat Cell Biol:S14-S19
    • (2003) Nat Cell Biol
    • Gerlich, D.1    Ellenberg, J.2
  • 16
    • 1442306482 scopus 로고    scopus 로고
    • Quantitative fluorescence microscopy and image deconvolution
    • Swedlow JR 2003 Quantitative fluorescence microscopy and image deconvolution. Methods Cell Biol 72:349-367
    • (2003) Methods Cell Biol , vol.72 , pp. 349-367
    • Swedlow, J.R.1
  • 17
    • 0037133239 scopus 로고    scopus 로고
    • Measuring tubulin content in Toxoplasma gondii: A comparison of laser-scanning confocal and wide-field fluorescence microscopy
    • Swedlow JR, Hu K, Andrews PD, Roos DS, Murray JM 2002 Measuring tubulin content in Toxoplasma gondii: a comparison of laser-scanning confocal and wide-field fluorescence microscopy. Proc Natl Acad Sci USA 99:2014-2019
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2014-2019
    • Swedlow, J.R.1    Hu, K.2    Andrews, P.D.3    Roos, D.S.4    Murray, J.M.5
  • 18
    • 0035167454 scopus 로고    scopus 로고
    • A working-person's guide to deconvolution in light microscopy
    • Wallace W, Schaefer LH, Swedlow JR 2001 A working-person's guide to deconvolution in light microscopy. Biotechniques 31:1076-1082
    • (2001) Biotechniques , vol.31 , pp. 1076-1082
    • Wallace, W.1    Schaefer, L.H.2    Swedlow, J.R.3
  • 19
    • 85047684372 scopus 로고    scopus 로고
    • Navigating steroid hormone receptors through the nuclear compartment
    • DeFranco DB 2002 Navigating steroid hormone receptors through the nuclear compartment. Mol Endocrinol 16:1449-1455
    • (2002) Mol Endocrinol , vol.16 , pp. 1449-1455
    • DeFranco, D.B.1
  • 23
    • 13844299381 scopus 로고    scopus 로고
    • Corepressor subnuclear organization is regulated by estrogen receptor via a mechanism that requires the DNA-binding domain
    • Voss TC, Demarco IA, Booker CF, Day RN 2005 Corepressor subnuclear organization is regulated by estrogen receptor via a mechanism that requires the DNA-binding domain. Mol Cell Endocrinol 231:33-47
    • (2005) Mol Cell Endocrinol , vol.231 , pp. 33-47
    • Voss, T.C.1    Demarco, I.A.2    Booker, C.F.3    Day, R.N.4
  • 24
    • 0035371920 scopus 로고    scopus 로고
    • Visualizing chromosome dynamics with GFP
    • Belmont AS 2001 Visualizing chromosome dynamics with GFP. Trends Cell Biol 11:250-257
    • (2001) Trends Cell Biol , vol.11 , pp. 250-257
    • Belmont, A.S.1
  • 25
    • 0037165965 scopus 로고    scopus 로고
    • Visualizing chromatin dynamics in interphase nuclei
    • Gasser SM 2002 Visualizing chromatin dynamics in interphase nuclei. Science 296:1412-1416
    • (2002) Science , vol.296 , pp. 1412-1416
    • Gasser, S.M.1
  • 26
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally JG, Müller WG, Walker D, Wolford R, Hager GL 2000 The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 287:1262-1265
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Müller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 27
    • 0030461543 scopus 로고    scopus 로고
    • In vivo localization of DNA sequences and visualization of large-scale chromatin organization using lac operator/repressor recognition
    • Robinett CC, Straight A, Li G, Willhelm C, Sudlow G, Murray A, Belmont AS 1996 In vivo localization of DNA sequences and visualization of large-scale chromatin organization using lac operator/repressor recognition. J Cell Biol 135:1685-1700
    • (1996) J Cell Biol , vol.135 , pp. 1685-1700
    • Robinett, C.C.1    Straight, A.2    Li, G.3    Willhelm, C.4    Sudlow, G.5    Murray, A.6    Belmont, A.S.7
  • 29
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz J, Patterson GH 2003 Development and use of fluorescent protein markers in living cells. Science 300:87-91
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 30
    • 0036532111 scopus 로고    scopus 로고
    • Protein dynamics in the nuclear compartment
    • Hager GL, Elbi C, Becker M 2002 Protein dynamics in the nuclear compartment. Curr Opin Genet Dev 12:137-141
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 137-141
    • Hager, G.L.1    Elbi, C.2    Becker, M.3
  • 33
    • 1942502820 scopus 로고    scopus 로고
    • Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling
    • Nagaich AK, Walker DA, Wolford R, Hager GL 2004 Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling. Mol Cell 14:163-174
    • (2004) Mol Cell , vol.14 , pp. 163-174
    • Nagaich, A.K.1    Walker, D.A.2    Wolford, R.3    Hager, G.L.4
  • 34
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R, Penot G, Hubner MR, Reid G, Brand H, Kos M, Gannon F 2003 Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115:751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 35
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling
    • Reid G, Hubner MR, Metivier R, Brand H, Denger S, Manu D, Beaudouin J, Ellenberg J, Gannon F 2003 Cyclic, proteasome-mediated turnover of unliganded and liganded ERα on responsive promoters is an integral feature of estrogen signaling. Mol Cell 11:695-707
    • (2003) Mol Cell , vol.11 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 36
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y, Hu X, DiRenzo J, Lazar MA, Brown M 2000 Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 103:843-852
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1    Hu, X.2    DiRenzo, J.3    Lazar, M.A.4    Brown, M.5
  • 37
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod D, Koppel DE, Schlessinger J, Elson E, Webb WW 1976 Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys J 16:1055-1069
    • (1976) Biophys J , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 38
    • 0035654399 scopus 로고    scopus 로고
    • Kinetic modelling approaches to in vivo imaging
    • Phair RD, Misteli T 2001 Kinetic modelling approaches to in vivo imaging. Nat Rev Mol Cell Biol 2:898-907
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 898-907
    • Phair, R.D.1    Misteli, T.2
  • 39
    • 4444279082 scopus 로고    scopus 로고
    • Challenges and artifacts in quantitative photobleaching experiments
    • Weiss M 2004 Challenges and artifacts in quantitative photobleaching experiments. Traffic 5:662-671
    • (2004) Traffic , vol.5 , pp. 662-671
    • Weiss, M.1
  • 40
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli T 2001 Protein dynamics: implications for nuclear architecture and gene expression. Science 291:843-847
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1
  • 41
    • 0037372002 scopus 로고    scopus 로고
    • Molecular determinants of glucocorticoid receptor mobility in living cells: The importance of ligand affinity
    • Schaaf MJ, Cidlowski JA 2003 Molecular determinants of glucocorticoid receptor mobility in living cells: the importance of ligand affinity. Mol Cell Biol 23:1922-1934
    • (2003) Mol Cell Biol , vol.23 , pp. 1922-1934
    • Schaaf, M.J.1    Cidlowski, J.A.2
  • 42
    • 0037809279 scopus 로고    scopus 로고
    • Dynamic shuttling and intranuclear mobility of nuclear hormone receptors
    • Maruvada P, Baumann CT, Hager GL, Yen PM 2003 Dynamic shuttling and intranuclear mobility of nuclear hormone receptors. J Biol Chem 278:12425-12432
    • (2003) J Biol Chem , vol.278 , pp. 12425-12432
    • Maruvada, P.1    Baumann, C.T.2    Hager, G.L.3    Yen, P.M.4
  • 51
    • 0029742203 scopus 로고    scopus 로고
    • Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement
    • Yokoe H, Meyer T 1996 Spatial dynamics of GFP-tagged proteins investigated by local fluorescence enhancement. Nat Biotechnol 14:1252-1256
    • (1996) Nat Biotechnol , vol.14 , pp. 1252-1256
    • Yokoe, H.1    Meyer, T.2
  • 52
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson GH, Lippincott-Schwartz J 2002 A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297:1873-1877
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 53
    • 0037450726 scopus 로고    scopus 로고
    • Steady-state dynamics of Cajal body components in the Xenopus germinal vesicle
    • Handwerger KE, Murphy C, Gall JG 2003 Steady-state dynamics of Cajal body components in the Xenopus germinal vesicle. J Cell Biol 160:495-504
    • (2003) J Cell Biol , vol.160 , pp. 495-504
    • Handwerger, K.E.1    Murphy, C.2    Gall, J.G.3
  • 54
    • 1842687498 scopus 로고    scopus 로고
    • Dynamics of coilin in Cajal bodies of the Xenopus germinal vesicle
    • Deryusheva S, Gall JG 2004 Dynamics of coilin in Cajal bodies of the Xenopus germinal vesicle. Proc Natl Acad Sci USA 101:4810-4814
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4810-4814
    • Deryusheva, S.1    Gall, J.G.2
  • 55
    • 3242697223 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: A new tool for quantification of molecular interactions
    • Berland KM 2004 Fluorescence correlation spectroscopy: a new tool for quantification of molecular interactions. Methods Mol Biol 261:383-398
    • (2004) Methods Mol Biol , vol.261 , pp. 383-398
    • Berland, K.M.1
  • 56
    • 0037282643 scopus 로고    scopus 로고
    • A dynamic view of cellular processes by in vivo fluorescence auto- and cross-correlation spectroscopy
    • Bacia K, Schwille P 2003 A dynamic view of cellular processes by in vivo fluorescence auto- and cross-correlation spectroscopy. Methods 29:74-85
    • (2003) Methods , vol.29 , pp. 74-85
    • Bacia, K.1    Schwille, P.2
  • 57
    • 0036789423 scopus 로고    scopus 로고
    • Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy
    • Hess ST, Webb WW 2002 Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy. Biophys J 83:2300-2317
    • (2002) Biophys J , vol.83 , pp. 2300-2317
    • Hess, S.T.1    Webb, W.W.2
  • 59
    • 0033770633 scopus 로고    scopus 로고
    • Two-photon image correlation spectroscopy and image cross-correlation spectroscopy
    • Wiseman PW, Squier JA, Ellisman MH, Wilson KR 2000 Two-photon image correlation spectroscopy and image cross-correlation spectroscopy. J Microsc 200:14-25
    • (2000) J Microsc , vol.200 , pp. 14-25
    • Wiseman, P.W.1    Squier, J.A.2    Ellisman, M.H.3    Wilson, K.R.4
  • 60
    • 0346734134 scopus 로고    scopus 로고
    • Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy
    • Chen Y, Wei L-N, Müller JD 2003 Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy. Proc Natl Acad Sci USA 100:15492-15497
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15492-15497
    • Chen, Y.1    Wei, L.-N.2    Müller, J.D.3
  • 61
    • 0347319178 scopus 로고    scopus 로고
    • Triple-color coincidence analysis: One step further in following higher order molecular complex formation
    • Heinze KG, Jahnz M, Schwille P 2004 Triple-color coincidence analysis: one step further in following higher order molecular complex formation. Biophys J 86:506-516
    • (2004) Biophys J , vol.86 , pp. 506-516
    • Heinze, K.G.1    Jahnz, M.2    Schwille, P.3
  • 62
    • 0347286638 scopus 로고    scopus 로고
    • Imaging analysis of subcellular correlation of androgen receptor and estrogen receptor α in single living cells using green fluorescent protein color variants
    • Ochiai I, Matsuda K, Nishi M, Ozawa H, Kawata M 2004 Imaging analysis of subcellular correlation of androgen receptor and estrogen receptor α in single living cells using green fluorescent protein color variants. Mol Endocrinol 18:26-42
    • (2004) Mol Endocrinol , vol.18 , pp. 26-42
    • Ochiai, I.1    Matsuda, K.2    Nishi, M.3    Ozawa, H.4    Kawata, M.5
  • 63
    • 0034534579 scopus 로고    scopus 로고
    • Temporally distinct and ligand-specific recruitment of nuclear receptor interacting peptides and co-factors to subnuclear domains containing the estrogen receptor
    • Schaufele F, Chang C-Y, Liu W, Baxter JD, Wan Y, Nordeen S, Day RN, McDonnell DP 2000 Temporally distinct and ligand-specific recruitment of nuclear receptor interacting peptides and co-factors to subnuclear domains containing the estrogen receptor. Mol Endocrinol 14:2024-2039
    • (2000) Mol Endocrinol , vol.14 , pp. 2024-2039
    • Schaufele, F.1    Chang, C.-Y.2    Liu, W.3    Baxter, J.D.4    Wan, Y.5    Nordeen, S.6    Day, R.N.7    McDonnell, D.P.8
  • 64
    • 0037385141 scopus 로고    scopus 로고
    • Isoform-selective interactions between estrogen receptors and steroid receptor coactivators promoted by estradiol and ErbB-2 signaling in living cells
    • Bai Y, Giguere V 2003 Isoform-selective interactions between estrogen receptors and steroid receptor coactivators promoted by estradiol and ErbB-2 signaling in living cells. Mol Endocrinol 17:589-599
    • (2003) Mol Endocrinol , vol.17 , pp. 589-599
    • Bai, Y.1    Giguere, V.2
  • 65
    • 0034636104 scopus 로고    scopus 로고
    • Ligand-dependent interactions of coactivators steroid receptor coactivator-1 and peroxisome proliferator-activated receptor binding protein with nuclear hormone receptors can be imaged in live cells and are required for transcription
    • Llopis J, Westin S, Ricote M, Wang Z, Cho CY, Kurokawa R, Mullen TM, Rose DW, Rosenfeld MG, Tsien RY, Glass CK 2000 Ligand-dependent interactions of coactivators steroid receptor coactivator-1 and peroxisome proliferator- activated receptor binding protein with nuclear hormone receptors can be imaged in live cells and are required for transcription. Proc Natl Acad Sci USA 97:4363-4368
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4363-4368
    • Llopis, J.1    Westin, S.2    Ricote, M.3    Wang, Z.4    Cho, C.Y.5    Kurokawa, R.6    Mullen, T.M.7    Rose, D.W.8    Rosenfeld, M.G.9    Tsien, R.Y.10    Glass, C.K.11
  • 67
    • 0035834009 scopus 로고    scopus 로고
    • Nuclear relocation of a transactivator subunit precedes target gene activation
    • Francastel C, Magis W, Groudine M 2001 Nuclear relocation of a transactivator subunit precedes target gene activation. Proc Natl Acad Sci USA 98:12120-12125
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12120-12125
    • Francastel, C.1    Magis, W.2    Groudine, M.3
  • 68
    • 0038022718 scopus 로고    scopus 로고
    • Targeting genes and transcription factors to segregated nuclear compartments
    • Isogai Y, Tjian R 2003 Targeting genes and transcription factors to segregated nuclear compartments. Curr Opin Cell Biol 15:1-8
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 1-8
    • Isogai, Y.1    Tjian, R.2
  • 70
    • 2342639627 scopus 로고    scopus 로고
    • Measuring the size of biological nanostructures with spatially modulated illumination microscopy
    • Martin S, Failla AV, Spori U, Cremer C, Pombo A 2004 Measuring the size of biological nanostructures with spatially modulated illumination microscopy. Mol Biol Cell 15:2449-2455
    • (2004) Mol Biol Cell , vol.15 , pp. 2449-2455
    • Martin, S.1    Failla, A.V.2    Spori, U.3    Cremer, C.4    Pombo, A.5
  • 72
    • 0032622353 scopus 로고    scopus 로고
    • Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy
    • Periasamy A, Day RN 1999 Visualizing protein interactions in living cells using digitized GFP imaging and FRET microscopy. Methods Cell Biol 58:293-314
    • (1999) Methods Cell Biol , vol.58 , pp. 293-314
    • Periasamy, A.1    Day, R.N.2
  • 73
    • 0033083490 scopus 로고    scopus 로고
    • Using GFP in FRET-based applications
    • Pollok BA, Heim R 1999 Using GFP in FRET-based applications. Trends Cell Biol 9:57-60
    • (1999) Trends Cell Biol , vol.9 , pp. 57-60
    • Pollok, B.A.1    Heim, R.2
  • 74
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • Truong K, Ikura M 2001 The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo. Curr Opin Struct Biol 11:573-578
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 75
    • 12244312784 scopus 로고    scopus 로고
    • Characterization of one- and two-photon excitation fluorescence resonance energy transfer microscopy
    • Elangovan M, Wallrabe H, Chen Y, Day RN, Barroso M, Periasamy A 2003 Characterization of one- and two-photon excitation fluorescence resonance energy transfer microscopy. Methods 29:58-73
    • (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
  • 76
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon GW, Berry G, Liang XH, Levine B, Herman B 1998 Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74:2702-2713
    • (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
  • 77
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Xia Z, Liu Y 2001 Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys J 81:2395-2402
    • (2001) Biophys J , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 78
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney C, Danuser G 2003 FRET or no FRET: a quantitative comparison. Biophys J 84:3992-4010
    • (2003) Biophys J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 79
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy AK 2001 Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24:289-296
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 80
    • 0002557253 scopus 로고    scopus 로고
    • Calibration of fluorescence resonance energy transfer in microscopy using genetically engineered GFP derivatives on nickel chelating beads
    • Youvan DC, Silva CM, Bylina EJ, Coleman WJ, Dilworth MR, YangMM1997 Calibration of fluorescence resonance energy transfer in microscopy using genetically engineered GFP derivatives on nickel chelating beads. Biotechnology et alia, www.et-al.com 3:1-18
    • (1997) Biotechnology et Alia , vol.3 , pp. 1-18
    • Youvan, D.C.1    Silva, C.M.2    Bylina, E.J.3    Coleman, W.J.4    Dilworth, M.R.5    Yang, M.M.6
  • 81
    • 0029764358 scopus 로고    scopus 로고
    • Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: Fluorescent-labeled protein kinase C β I
    • Bastiaens PI, Jovin TM 1996 Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: fluorescent-labeled protein kinase C β I. Proc Natl Acad Sci USA 93:8407-8412
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8407-8412
    • Bastiaens, P.I.1    Jovin, T.M.2
  • 82
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens PI, Majoul IV, Verveer PJ, Soling HD, Jovin TM 1996 Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J 15:4246-4253
    • (1996) EMBO J , vol.15 , pp. 4246-4253
    • Bastiaens, P.I.1    Majoul, I.V.2    Verveer, P.J.3    Soling, H.D.4    Jovin, T.M.5
  • 83
    • 0034802539 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus
    • Day RN, Periasamy A, Schaufele F 2001 Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus. Methods 25:4-18
    • (2001) Methods , vol.25 , pp. 4-18
    • Day, R.N.1    Periasamy, A.2    Schaufele, F.3
  • 84
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki A, Tsien RY 2000 Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol 327:472-500
    • (2000) Methods Enzymol , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 85
    • 2142762991 scopus 로고    scopus 로고
    • Probing plasma membrane microdomains in cowpea protoplasts using lipidated GFP-fusion proteins and multimode FRET microscopy
    • Vermeer JE, van Munster EB, Vischer NO, Gadella TWJ 2004 Probing plasma membrane microdomains in cowpea protoplasts using lipidated GFP-fusion proteins and multimode FRET microscopy. J Microsc 214:190-200
    • (2004) J Microsc , vol.214 , pp. 190-200
    • Vermeer, J.E.1    Van Munster, E.B.2    Vischer, N.O.3    Gadella, T.W.J.4
  • 86
    • 0037280108 scopus 로고    scopus 로고
    • Fluorescence lifetime-resolved imaging: Measuring lifetimes in an image
    • Clegg RM, Holub O, Gohlke C 2003 Fluorescence lifetime-resolved imaging: measuring lifetimes in an image. Methods Enzymol 360:509-542
    • (2003) Methods Enzymol , vol.360 , pp. 509-542
    • Clegg, R.M.1    Holub, O.2    Gohlke, C.3
  • 88
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens PI, Squire A 1999 Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol 9:48-52
    • (1999) Trends Cell Biol , vol.9 , pp. 48-52
    • Bastiaens, P.I.1    Squire, A.2
  • 90
    • 0033533709 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells
    • Wouters FS, Bastiaens PI 1999 Fluorescence lifetime imaging of receptor tyrosine kinase activity in cells. Current Biol 9:1127-1130
    • (1999) Current Biol , vol.9 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 91
    • 0035577921 scopus 로고    scopus 로고
    • Multiphoton spectroscopy and excited state dynamics of enhanced green fluorescent protein (EGFP): Acid-base specificity
    • Heikal AA, Hess ST, Webb WW 2001 Multiphoton spectroscopy and excited state dynamics of enhanced green fluorescent protein (EGFP): acid-base specificity. Chem Phys 274:37-55
    • (2001) Chem Phys , vol.274 , pp. 37-55
    • Heikal, A.A.1    Hess, S.T.2    Webb, W.W.3
  • 92
    • 0000839617 scopus 로고    scopus 로고
    • Photochromicity and fluorescence lifetimes of green fluorescent protein
    • Striker G, Subramaniam V, Seidel CAM, Volkmer A 1999 Photochromicity and fluorescence lifetimes of green fluorescent protein. J Phys Chem B 103:8612-8617
    • (1999) J Phys Chem B , vol.103 , pp. 8612-8617
    • Striker, G.1    Subramaniam, V.2    Seidel, C.A.M.3    Volkmer, A.4
  • 95
    • 1242269786 scopus 로고    scopus 로고
    • Picosecond time-resolved microspectrofluorometry in live cells exemplified by complex fluorescence dynamics of popular probes ethidium and cyan fluorescent protein
    • Tramier M, Kemnitz K, Durieux C, Coppey-Moisan M 2004 Picosecond time-resolved microspectrofluorometry in live cells exemplified by complex fluorescence dynamics of popular probes ethidium and cyan fluorescent protein. J Microsc 213:110-118
    • (2004) J Microsc , vol.213 , pp. 110-118
    • Tramier, M.1    Kemnitz, K.2    Durieux, C.3    Coppey-Moisan, M.4
  • 96
    • 0742321791 scopus 로고    scopus 로고
    • Graphical representation and multicomponent analysis of single-frequency fluorescence lifetime imaging microscopy data
    • Clayton AH, Hanley QS, Verveer PJ 2004 Graphical representation and multicomponent analysis of single-frequency fluorescence lifetime imaging microscopy data. J Microsc 213:1-5
    • (2004) J Microsc , vol.213 , pp. 1-5
    • Clayton, A.H.1    Hanley, Q.S.2    Verveer, P.J.3
  • 97
    • 0346307455 scopus 로고    scopus 로고
    • Characterization of two-photon excitation fluorescence lifetime imaging microscopy for protein localization
    • Chen Y, Periasamy A 2004 Characterization of two-photon excitation fluorescence lifetime imaging microscopy for protein localization. Microsc Res Tech 63:72-80
    • (2004) Microsc Res Tech , vol.63 , pp. 72-80
    • Chen, Y.1    Periasamy, A.2
  • 99
    • 0037855765 scopus 로고    scopus 로고
    • Conformation of CCAAT/enhancer binding protein α dimers varies with intranuclear location in living cells
    • Schaufele F, Wang X, Liu X, Day RN 2003 Conformation of CCAAT/enhancer binding protein α dimers varies with intranuclear location in living cells. J Biol Chem 278:10578-10587
    • (2003) J Biol Chem , vol.278 , pp. 10578-10587
    • Schaufele, F.1    Wang, X.2    Liu, X.3    Day, R.N.4
  • 101
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY 2002 Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 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
  • 102
    • 0036710588 scopus 로고    scopus 로고
    • Peering inside lipid rafts and caveolae
    • Kenworthy A 2002 Peering inside lipid rafts and caveolae. Trends Biochem Sci 27:435-437
    • (2002) Trends Biochem Sci , vol.27 , pp. 435-437
    • Kenworthy, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.