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Volumn , Issue , 2005, Pages 146-164

Photobleaching FRET Microscopy

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EID: 85108715760     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-019517720-6.50017-1     Document Type: Chapter
Times cited : (2)

References (70)
  • 1
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts and other lipid domains
    • Anderson R.G.W., Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts and other lipid domains. Science 2002, 296:1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.W.1    Jacobson, K.2
  • 2
    • 0030566759 scopus 로고    scopus 로고
    • A photobleaching energy transfer analysis of CD8/MHC-I and LFA-1/ICAM-1 interactions in CTL-target cell conjugates
    • Bacso Z., Bene L., Bodnar A., Matko J., Damjanovich S. A photobleaching energy transfer analysis of CD8/MHC-I and LFA-1/ICAM-1 interactions in CTL-target cell conjugates. Immunol. Lett. 1996, 54:151-156.
    • (1996) Immunol. Lett. , vol.54 , pp. 151-156
    • Bacso, Z.1    Bene, L.2    Bodnar, A.3    Matko, J.4    Damjanovich, S.5
  • 3
    • 0029764358 scopus 로고    scopus 로고
    • Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: fluorescent-labeled protein kinase C beta I
    • Bastiaens P.I., Jovin T.M. Microspectroscopic imaging tracks the intracellular processing of a signal transduction protein: fluorescent-labeled protein kinase C beta I. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:8407-8412.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8407-8412
    • Bastiaens, P.I.1    Jovin, T.M.2
  • 4
    • 0001385205 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy
    • Academic Press, New York, J.E. Celis (Ed.)
    • Bastiaens P.I.H., Jovin T.M. Fluorescence resonance energy transfer microscopy. Cell Biology: A Laboratory Handbook 1998, 136-146. Academic Press, New York. J.E. Celis (Ed.).
    • (1998) Cell Biology: A Laboratory Handbook , pp. 136-146
    • Bastiaens, P.I.H.1    Jovin, T.M.2
  • 5
    • 0029741379 scopus 로고    scopus 로고
    • Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin
    • Bastiaens P.I., Majoul I.V., Verveer P.J., Soling H.D., Jovin T.M. Imaging the intracellular trafficking and state of the AB5 quaternary structure of cholera toxin. EMBO J. 1996, 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
  • 7
    • 0021956248 scopus 로고
    • Digital imaging fluorescence microscopy: spatial heterogeneity of photobleaching rate constants in individual cells
    • Benson D.M., Bryan J., Plant A.L., Gotto A.M., Smith L.C. Digital imaging fluorescence microscopy: spatial heterogeneity of photobleaching rate constants in individual cells. J. Cell. Biol. 1985, 100:1309-1323.
    • (1985) J. Cell. Biol. , vol.100 , pp. 1309-1323
    • Benson, D.M.1    Bryan, J.2    Plant, A.L.3    Gotto, A.M.4    Smith, L.C.5
  • 8
    • 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. 2003, 84:3992-4010.
    • (2003) Biophys. J. , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 9
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., London E. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 1998, 14:111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 10
    • 1842563953 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET)
    • John Wiley, New York, B. Herman (Ed.)
    • Clegg R.M. Fluorescence resonance energy transfer (FRET). Fluorescence Imaging Spectroscopy and Microscopy 1996, 179-252. John Wiley, New York. B. Herman (Ed.).
    • (1996) Fluorescence Imaging Spectroscopy and Microscopy , pp. 179-252
    • Clegg, R.M.1
  • 12
    • 0034802539 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus
    • Day R.N., Periasamy A., Schaufele F. Fluorescence resonance energy transfer microscopy of localized protein interactions in the living cell nucleus. Methods 2001, 25:4-18.
    • (2001) Methods , vol.25 , pp. 4-18
    • Day, R.N.1    Periasamy, A.2    Schaufele, F.3
  • 13
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: from model membranes to cells
    • Edidin M. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 2003, 32:257-283.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 14
    • 0035959942 scopus 로고    scopus 로고
    • Preassociation of calmodulin with voltage-gated Ca(2+) channels revealed by FRET in single living cells
    • Erickson M.G., Alseikhan B.A., Peterson B.Z., Yue D.T. Preassociation of calmodulin with voltage-gated Ca(2+) channels revealed by FRET in single living cells. Neuron 2001, 31:973-985.
    • (2001) Neuron , vol.31 , pp. 973-985
    • Erickson, M.G.1    Alseikhan, B.A.2    Peterson, B.Z.3    Yue, D.T.4
  • 15
    • 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. 2003, 85:599-611.
    • (2003) Biophys. J. , vol.85 , pp. 599-611
    • Erickson, M.G.1    Moon, D.L.2    Yue, D.T.3
  • 16
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella T.W., Jovin T.M. Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 1995, 129:1543-1558.
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella, T.W.1    Jovin, T.M.2
  • 17
    • 12644270211 scopus 로고    scopus 로고
    • Fast algorithms for the analysis of single and double exponetial decay curved with a background term. Application to time-resolved imaging microscopy
    • Gadella T.W.J.J., Jovin T.M. Fast algorithms for the analysis of single and double exponetial decay curved with a background term. Application to time-resolved imaging microscopy. Bioimaging 1997, 5:5-39.
    • (1997) Bioimaging , vol.5 , pp. 5-39
    • Gadella, T.W.J.J.1    Jovin, T.M.2
  • 18
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localzied activation of the T-cell receptor
    • Glebov O.O., Nichols B.J. Lipid raft proteins have a random distribution during localzied activation of the T-cell receptor. Nat. Cell Biol. 2004, 6:238-243.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 19
    • 0029987587 scopus 로고    scopus 로고
    • Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor
    • Ha T., Enderle T., Ogletree D.F., Chemla D.S., Selvin P.R., Weiss S. Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor. Proc. Natl. Acad. Sci. U.S.A. 1996, 93:6264-6268.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6264-6268
    • Ha, T.1    Enderle, T.2    Ogletree, D.F.3    Chemla, D.S.4    Selvin, P.R.5    Weiss, S.6
  • 20
    • 0027398446 scopus 로고
    • Correctly sorted molecules of a GPI-anchored protein are clustered and immobile when they arrive at the apical surface of MDCK cells
    • Hannan L.A., Lisanti M.P., Rodriguez-Boulan E., Edidin M. Correctly sorted molecules of a GPI-anchored protein are clustered and immobile when they arrive at the apical surface of MDCK cells. J. Cell Biol. 1993, 120:353-358.
    • (1993) J. Cell Biol. , vol.120 , pp. 353-358
    • Hannan, L.A.1    Lisanti, M.P.2    Rodriguez-Boulan, E.3    Edidin, M.4
  • 21
    • 1842588906 scopus 로고    scopus 로고
    • Lipids as targeting signals: lipid rafts and intracellular trafficking
    • Helms J.B., Zurzolo C. Lipids as targeting signals: lipid rafts and intracellular trafficking. Traffic 2004, 5:247-254.
    • (2004) Traffic , vol.5 , pp. 247-254
    • Helms, J.B.1    Zurzolo, C.2
  • 22
    • 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. 2002, 83:3652-3664.
    • (2002) Biophys. J. , vol.83 , pp. 3652-3664
    • Hoppe, A.1    Christensen, K.2    Swanson, J.A.3
  • 25
    • 0002090886 scopus 로고
    • FRET microscopy: digital imaging of fluorescence resonance energy transfer. Application in cell biology
    • Academic Press, Orlando, E. Kohen, J.S. Ploem, J.G. Hirschberg (Eds.)
    • Jovin T.M., Arndt-Jovin D.J. FRET microscopy: digital imaging of fluorescence resonance energy transfer. Application in cell biology. Cell Structure and Function by Microspectrofluorimetry 1989, 99-117. Academic Press, Orlando. E. Kohen, J.S. Ploem, J.G. Hirschberg (Eds.).
    • (1989) Cell Structure and Function by Microspectrofluorimetry , pp. 99-117
    • Jovin, T.M.1    Arndt-Jovin, D.J.2
  • 27
    • 0030026814 scopus 로고    scopus 로고
    • Proximity relationships between the type I receptor for Fcε. (FcεRI) and the mast cell function-associated antigen (MAFA) studied by donor photobleaching fluorescence resonance energy transfer microscopy
    • Jurgens L., Arndt-Jovin D., Pecht I., Jovin T.M. Proximity relationships between the type I receptor for Fcε. (FcεRI) and the mast cell function-associated antigen (MAFA) studied by donor photobleaching fluorescence resonance energy transfer microscopy. Eur. J. Immunol. 1996, 26:84-91.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 84-91
    • Jurgens, L.1    Arndt-Jovin, D.2    Pecht, I.3    Jovin, T.M.4
  • 28
    • 0037238461 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser
    • Karpova T.S., Baumann C.T., He L., Wu X., Grammer A., Lipsky P., Hager G.L., McNally J.G. Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser. J. Microsc. 2003, 209:56-70.
    • (2003) J. Microsc. , vol.209 , pp. 56-70
    • Karpova, T.S.1    Baumann, C.T.2    He, L.3    Wu, X.4    Grammer, A.5    Lipsky, P.6    Hager, G.L.7    McNally, J.G.8
  • 29
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy A.K. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 2001, 24:289-296.
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 30
    • 0036710588 scopus 로고    scopus 로고
    • Peering inside lipid rafts and caveolae
    • Kenworthy A.K. Peering inside lipid rafts and caveolae. Trends Biochem. Sci. 2002, 27:435-438.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 435-438
    • Kenworthy, A.K.1
  • 31
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100using imaging fluorescence resonance energy transfer
    • Kenworthy A.K., Edidin M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100using imaging fluorescence resonance energy transfer. J. Cell Biol. 1998, 142:69-84.
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 32
    • 0032605667 scopus 로고    scopus 로고
    • Imaging fluorescence resonance energy transfer as a probe of membrane organization and molecular associations of GPI-anchored proteins
    • Humana Press, Totowa, NJ, M.H. Gelb (Ed.)
    • Kenworthy A.K., Edidin M. Imaging fluorescence resonance energy transfer as a probe of membrane organization and molecular associations of GPI-anchored proteins. Protein Lipidation Protocols 1999, 37-49. Humana Press, Totowa, NJ. M.H. Gelb (Ed.).
    • (1999) Protein Lipidation Protocols , pp. 37-49
    • Kenworthy, A.K.1    Edidin, M.2
  • 33
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy A.K., Petranova N., Edidin M. High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell 2000, 11:1645-1655.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 34
    • 0035503797 scopus 로고    scopus 로고
    • Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: role of the intracellular adapter protein Fe65
    • Kinoshita A., Whelan C.M., Smith C.J., Mikhailenko I., Rebeck G.W., Strickland D.K., Hyman B.T. Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: role of the intracellular adapter protein Fe65. J. Neurosci. 2001, 21:8354-8361.
    • (2001) J. Neurosci. , vol.21 , pp. 8354-8361
    • Kinoshita, A.1    Whelan, C.M.2    Smith, C.J.3    Mikhailenko, I.4    Rebeck, G.W.5    Strickland, D.K.6    Hyman, B.T.7
  • 35
    • 0035203097 scopus 로고    scopus 로고
    • Role of lipid rafts in Shiga toxin 1 interaction with the apical surface of Caco-2 cells
    • Kovbasnjuk O., Edidin M., Donowitz M. Role of lipid rafts in Shiga toxin 1 interaction with the apical surface of Caco-2 cells. J. Cell Sci. 2001, 114:4025-4031.
    • (2001) J. Cell Sci. , vol.114 , pp. 4025-4031
    • Kovbasnjuk, O.1    Edidin, M.2    Donowitz, M.3
  • 36
    • 0027500214 scopus 로고
    • Distribution of type I Fcε-receptors on the surface of mast cells probed by fluorescence resonance energy transfer
    • Kubitscheck U., Schweitzer-Stenner R., Arndt-Jovin D.J., Jovin T.M., Pecht I. Distribution of type I Fcε-receptors on the surface of mast cells probed by fluorescence resonance energy transfer. Biophys. J. 1993, 64:110-120.
    • (1993) Biophys. J. , vol.64 , pp. 110-120
    • Kubitscheck, U.1    Schweitzer-Stenner, R.2    Arndt-Jovin, D.J.3    Jovin, T.M.4    Pecht, I.5
  • 37
    • 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 J., Cho C.Y., Kurokawa R., Mullen T.M., Rose D.W., Rosenfeld M.G., Tsien R.Y., Glass C.K. 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. U.S.A. 2000, 97:4363-4368.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 4363-4368
    • Llopis, J.1    Westin, S.2    Ricote, M.3    Wang, J.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
  • 39
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • Maxfield F.R. Plasma membrane microdomains. Curr. Opin. Cell Biol. 2002, 14:483-487.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 40
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor S., Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 2004, 5:231-240.
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 41
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki A., Tsien R.Y. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol. 2000, 327:472-500.
    • (2000) Methods Enzymol. , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 42
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive?. Cell 2003, 115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 43
    • 0344447088 scopus 로고    scopus 로고
    • Intensity-based energy transfer measurements in digital imaging microscopy
    • Nagy P., Vamosi G., Bodnar A., Lockett S.J., Szollosi J. Intensity-based energy transfer measurements in digital imaging microscopy. Eur. Biophys. J. 1998, 27:377-389.
    • (1998) Eur. Biophys. J. , vol.27 , pp. 377-389
    • Nagy, P.1    Vamosi, G.2    Bodnar, A.3    Lockett, S.J.4    Szollosi, J.5
  • 44
    • 0037446837 scopus 로고    scopus 로고
    • GM1-containing lipid rafts are depleted within clathrin-coated pits
    • Nichols B.J. GM1-containing lipid rafts are depleted within clathrin-coated pits. Curr. Biol. 2003, 13:686-690.
    • (2003) Curr. Biol. , vol.13 , pp. 686-690
    • Nichols, B.J.1
  • 45
    • 0035338444 scopus 로고    scopus 로고
    • Clustering of peptide-loaded MHC class I molecules for endoplasmic reticulum export imaged by fluorescence resonance energy transfer
    • Pentcheva T., Edidin M. Clustering of peptide-loaded MHC class I molecules for endoplasmic reticulum export imaged by fluorescence resonance energy transfer. J. Immunol. 2001, 166:6625-6632.
    • (2001) J. Immunol. , vol.166 , pp. 6625-6632
    • Pentcheva, T.1    Edidin, M.2
  • 46
    • 0037083359 scopus 로고    scopus 로고
    • Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites
    • Pentcheva T., Spiliotis E.T., Edidin M. Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites. J. Immunol. 2002, 168:1538-1541.
    • (2002) J. Immunol. , vol.168 , pp. 1538-1541
    • Pentcheva, T.1    Spiliotis, E.T.2    Edidin, M.3
  • 47
    • 0037732635 scopus 로고    scopus 로고
    • Regulation of beta cell glucokinase by S-nitrosylation and association with nitric oxide synthase
    • Rizzo M.A., Piston D.W. Regulation of beta cell glucokinase by S-nitrosylation and association with nitric oxide synthase. J. Cell Biol. 2003, 161:243-248.
    • (2003) J. Cell Biol. , vol.161 , pp. 243-248
    • Rizzo, M.A.1    Piston, D.W.2
  • 49
    • 0037763890 scopus 로고    scopus 로고
    • Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment
    • Rocheleau J.V., Edidin M., Piston D.W. Intrasequence GFP in class I MHC molecules, a rigid probe for fluorescence anisotropy measurements of the membrane environment. Biophys. J. 2003, 84:4078-4086.
    • (2003) Biophys. J. , vol.84 , pp. 4078-4086
    • Rocheleau, J.V.1    Edidin, M.2    Piston, D.W.3
  • 50
    • 0034677745 scopus 로고    scopus 로고
    • Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers
    • Rocheville M., Lange D.C., Kumar U., Sasi R., Patel R.C., Patel Y.C. Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers. J. Biol. Chem. 2000, 275:7862-7869.
    • (2000) J. Biol. Chem. , vol.275 , pp. 7862-7869
    • Rocheville, M.1    Lange, D.C.2    Kumar, U.3    Sasi, R.4    Patel, R.C.5    Patel, Y.C.6
  • 53
    • 0036733578 scopus 로고    scopus 로고
    • Cholesterol, lipid rafts, and disease
    • Simons K., Ehehalt R. Cholesterol, lipid rafts, and disease. J. Clin. Invest. 2002, 110:597-603.
    • (2002) J. Clin. Invest. , vol.110 , pp. 597-603
    • Simons, K.1    Ehehalt, R.2
  • 54
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 56
    • 1842561598 scopus 로고    scopus 로고
    • The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells
    • Snapp E.L., Reinhart G.A., Bogert B.A., Lippincott-Schwartz J., Hegde R.S. The organization of engaged and quiescent translocons in the endoplasmic reticulum of mammalian cells. J. Cell Biol. 2004, 164:997-1007.
    • (2004) J. Cell Biol. , vol.164 , pp. 997-1007
    • Snapp, E.L.1    Reinhart, G.A.2    Bogert, B.A.3    Lippincott-Schwartz, J.4    Hegde, R.S.5
  • 57
    • 0029057619 scopus 로고
    • Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy
    • Song L., Hennink E.J., Young I.T., Tanke H.J. Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy. Biophys. J. 1995, 68:2588-2600.
    • (1995) Biophys. J. , vol.68 , pp. 2588-2600
    • Song, L.1    Hennink, E.J.2    Young, I.T.3    Tanke, H.J.4
  • 58
    • 0030029881 scopus 로고    scopus 로고
    • Influence of the triplet excited state on the photobleaching kinetics on fluorescein in microscopy
    • Song L., Varma C.A., Verhoeven J.W., Tanke H.J. Influence of the triplet excited state on the photobleaching kinetics on fluorescein in microscopy. Biophys. J. 1996, 70:2959.
    • (1996) Biophys. J. , vol.70 , pp. 2959
    • Song, L.1    Varma, C.A.2    Verhoeven, J.W.3    Tanke, H.J.4
  • 59
    • 0035999994 scopus 로고    scopus 로고
    • Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules
    • Spiliotis E.T., Pentcheva T., Edidin M. Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules. Mol. Biol. Cell 2002, 13:1566-1581.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1566-1581
    • Spiliotis, E.T.1    Pentcheva, T.2    Edidin, M.3
  • 60
    • 0026577623 scopus 로고
    • Epitope mapping by photobleaching fluorescence resonance energy transfer measurements using a laser scanning microscope system
    • Szaba G., Pine P.S., Weaver J.L., Kasari M., Aszalos A. Epitope mapping by photobleaching fluorescence resonance energy transfer measurements using a laser scanning microscope system. Biophys. J. 1992, 61:661-670.
    • (1992) Biophys. J. , vol.61 , pp. 661-670
    • Szaba, G.1    Pine, P.S.2    Weaver, J.L.3    Kasari, M.4    Aszalos, A.5
  • 61
    • 85129585509 scopus 로고
    • Experimental methods to measure fluorescence resonance energy transfer processes
    • CRC Press, Boca Raton, L. Tron (Ed.)
    • Tron L. Experimental methods to measure fluorescence resonance energy transfer processes. Mobility and Proximity in Biological Membranes 1994, 1-47. CRC Press, Boca Raton. L. Tron (Ed.).
    • (1994) Mobility and Proximity in Biological Membranes , pp. 1-47
    • Tron, L.1
  • 62
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 1998, 394:798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 63
    • 0035082123 scopus 로고    scopus 로고
    • Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers
    • Vyas K.A., Patel H.V., Vyas A.A., Schnaar R.L. Segregation of gangliosides GM1 and GD3 on cell membranes, isolated membrane rafts, and defined supported lipid monolayers. Biol. Chem. 2001, 382:241-250.
    • (2001) Biol. Chem. , vol.382 , pp. 241-250
    • Vyas, K.A.1    Patel, H.V.2    Vyas, A.A.3    Schnaar, R.L.4
  • 64
    • 0037974186 scopus 로고    scopus 로고
    • Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes
    • Wallrabe H., Elangovan M., Burchard A., Periasamy A., Barroso M. Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes. Biophys. J. 2003, 85:559-571.
    • (2003) Biophys. J. , vol.85 , pp. 559-571
    • Wallrabe, H.1    Elangovan, M.2    Burchard, A.3    Periasamy, A.4    Barroso, M.5
  • 65
    • 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. 1999, 9:1127-1130.
    • (1999) Curr. Biol. , vol.9 , pp. 1127-1130
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 66
    • 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.H., Wirtz K.W.A., 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. 1998, 17:7179-7189.
    • (1998) EMBO J. , vol.17 , pp. 7179-7189
    • Wouters, F.S.1    Bastiaens, P.I.H.2    Wirtz, K.W.A.3    Jovin, T.M.4
  • 67
    • 0028023293 scopus 로고
    • Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics
    • Young R.M., Arnette J.K., Roess D.A., Barias B.G. Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics. Biophys. J. 1994, 67:881-888.
    • (1994) Biophys. J. , vol.67 , pp. 881-888
    • Young, R.M.1    Arnette, J.K.2    Roess, D.A.3    Barias, B.G.4
  • 68
    • 0034083428 scopus 로고    scopus 로고
    • Recent advances in technology for measuring and manipulating cell signals
    • Zacharias D.A., Baird G.S., Tsien R.Y. Recent advances in technology for measuring and manipulating cell signals. Curr. Opin. Neurol. 2000, 10:416-421.
    • (2000) Curr. Opin. Neurol. , vol.10 , pp. 416-421
    • Zacharias, D.A.1    Baird, G.S.2    Tsien, R.Y.3
  • 69
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D.A., Violin J.D., Newton A.C., Tsien R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 2002, 296:913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 70
    • 2942640371 scopus 로고    scopus 로고
    • Photobleaching-corrected FRET efficiency imaging of live cells
    • Zal T., Gascoigne N.R. Photobleaching-corrected FRET efficiency imaging of live cells. Biophys. J. 2004, 86:3923-3939.
    • (2004) Biophys. J. , vol.86 , pp. 3923-3939
    • Zal, T.1    Gascoigne, N.R.2


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