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Volumn 89, Issue , 2008, Pages 169-221

Chapter 7 Total Internal Reflection Fluorescence Microscopy

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; CELL; FLUORESCENCE MICROSCOPY; FLUORESCENCE POLARIZATION; FLUORESCENCE RECOVERY AFTER PHOTOBLEACHING; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; METHODOLOGY; MOUSE; REVIEW; ULTRASTRUCTURE;

EID: 57949112733     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0091-679X(08)00607-9     Document Type: Review
Times cited : (155)

References (184)
  • 1
    • 0026753813 scopus 로고
    • Evanescent interference patterns for fluorescence microscopy
    • Abney J.R., Scalettar B.A., and Thompson N.L. Evanescent interference patterns for fluorescence microscopy. Biophys. J. 61 (1992) 542-552
    • (1992) Biophys. J. , vol.61 , pp. 542-552
    • Abney, J.R.1    Scalettar, B.A.2    Thompson, N.L.3
  • 2
    • 33646806089 scopus 로고    scopus 로고
    • The small GTPase R-Ras regulates organization of actin and drives membrane protusions through the activity of PLC epsilon
    • Ada-Nguema A.S., Xenias H., Sheetz M.P., and Keely P.J. The small GTPase R-Ras regulates organization of actin and drives membrane protusions through the activity of PLC epsilon. J. Cell Sci. 119 (2006) 1307-1319
    • (2006) J. Cell Sci. , vol.119 , pp. 1307-1319
    • Ada-Nguema, A.S.1    Xenias, H.2    Sheetz, M.P.3    Keely, P.J.4
  • 3
    • 7944222012 scopus 로고    scopus 로고
    • Signal analysis of total internal reflection fluorescent speckle microscopy (TIR-FSM) and wide-field epi-fluorescence FSM of the actin cytoskeleton and focal adhesions in living cells
    • Adams M.C., Matov A., Yarar D., Gupton S.L., Danuser G., and Waterman-Storer C.M. Signal analysis of total internal reflection fluorescent speckle microscopy (TIR-FSM) and wide-field epi-fluorescence FSM of the actin cytoskeleton and focal adhesions in living cells. J. Microsc. 216 (2004) 138-152
    • (2004) J. Microsc. , vol.216 , pp. 138-152
    • Adams, M.C.1    Matov, A.2    Yarar, D.3    Gupton, S.L.4    Danuser, G.5    Waterman-Storer, C.M.6
  • 4
    • 33745743006 scopus 로고    scopus 로고
    • Motion matters: Secretory granule motion adjacent to the plasma membrane and exocytosis
    • Allersma M.W., Bittner M.A., Axelrod D., and Holz R.W. Motion matters: Secretory granule motion adjacent to the plasma membrane and exocytosis. Mol. Biol. Cell 17 (2006) 2424-2438
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2424-2438
    • Allersma, M.W.1    Bittner, M.A.2    Axelrod, D.3    Holz, R.W.4
  • 5
    • 4644248316 scopus 로고    scopus 로고
    • Visualization of regulated exocytosis with a granule-membrane probe using total internal reflection microscopy
    • Allersma M.W., Wang L., Axelrod D., and Holz R.W. Visualization of regulated exocytosis with a granule-membrane probe using total internal reflection microscopy. Mol. Biol. Cell 15 (2004) 4658-4668
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4658-4668
    • Allersma, M.W.1    Wang, L.2    Axelrod, D.3    Holz, R.W.4
  • 6
    • 0002707751 scopus 로고
    • The movement of fibrocytes
    • Ambrose E.J. The movement of fibrocytes. Exp. Cell Res. 8 Suppl. 1 (1961) 54-73
    • (1961) Exp. Cell Res. , vol.8 , Issue.SUPPL. 1 , pp. 54-73
    • Ambrose, E.J.1
  • 7
    • 0018389150 scopus 로고
    • Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization
    • Axelrod D. Carbocyanine dye orientation in red cell membrane studied by microscopic fluorescence polarization. Biophys. J. 26 (1979) 557-574
    • (1979) Biophys. J. , vol.26 , pp. 557-574
    • Axelrod, D.1
  • 8
    • 0019494948 scopus 로고
    • Cell surface contacts illuminated by total internal reflection fluorescence
    • Axelrod D. Cell surface contacts illuminated by total internal reflection fluorescence. J. Cell Biol. 89 (1981) 141-145
    • (1981) J. Cell Biol. , vol.89 , pp. 141-145
    • Axelrod, D.1
  • 9
    • 0034745197 scopus 로고    scopus 로고
    • Selective imaging of surface fluorescence with very high aperture microscope objectives
    • Axelrod D. Selective imaging of surface fluorescence with very high aperture microscope objectives. J. Biomed. Opt. 6 (2001) 6-13
    • (2001) J. Biomed. Opt. , vol.6 , pp. 6-13
    • Axelrod, D.1
  • 10
    • 0037284103 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • Biophotonics, Part B
    • Axelrod D. Total internal reflection fluorescence microscopy in cell biology. Biophotonics, Part B. Methods Enzymol. 361 (2003) 1-33
    • (2003) Methods Enzymol. , vol.361 , pp. 1-33
    • Axelrod, D.1
  • 13
    • 33244494673 scopus 로고    scopus 로고
    • Experimental verification of near-wall hindered diffusion for the Brownian motion of nanoparticles using evanescent wave microscopy
    • Banerjee A., and Kihm K.D. Experimental verification of near-wall hindered diffusion for the Brownian motion of nanoparticles using evanescent wave microscopy. Phys. E Rev. 72 (2005) 042101
    • (2005) Phys. E Rev. , vol.72 , pp. 042101
    • Banerjee, A.1    Kihm, K.D.2
  • 15
    • 23044469426 scopus 로고    scopus 로고
    • Expansion of calcium microdomains regulates fast exocytosis at a ribbon synapse
    • Beaumont V., Llobet A., and Lagnado L. Expansion of calcium microdomains regulates fast exocytosis at a ribbon synapse. Proc. Natl. Acad. Sci. USA 102 (2005) 10700-10705
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 10700-10705
    • Beaumont, V.1    Llobet, A.2    Lagnado, L.3
  • 16
    • 0033824598 scopus 로고    scopus 로고
    • Measuring colloidal forces using evanescent wave scattering
    • Bike S.G. Measuring colloidal forces using evanescent wave scattering. Curr. Opin. Colloid Interface Sci. 5 (2000) 144-150
    • (2000) Curr. Opin. Colloid Interface Sci. , vol.5 , pp. 144-150
    • Bike, S.G.1
  • 17
    • 23244442263 scopus 로고    scopus 로고
    • Three-dimensional characterization of tethered microspheres by total internal reflection fluorescence microscopy
    • Blumberg S., Gajraj A., Pennington M.W., and Meiners J.C. Three-dimensional characterization of tethered microspheres by total internal reflection fluorescence microscopy. Biophys. J. 89 (2005) 1272-1281
    • (2005) Biophys. J. , vol.89 , pp. 1272-1281
    • Blumberg, S.1    Gajraj, A.2    Pennington, M.W.3    Meiners, J.C.4
  • 18
    • 3042785832 scopus 로고    scopus 로고
    • Real-time pH microscopy down to the molecular level by combined scanning electrochemical microscopy/single-molecule fluorescence spectroscopy
    • Boldt F.M., Heinze J., Diez M., Petersen J., and Borsch M. Real-time pH microscopy down to the molecular level by combined scanning electrochemical microscopy/single-molecule fluorescence spectroscopy. Anal. Chem. 76 (2004) 3473-3481
    • (2004) Anal. Chem. , vol.76 , pp. 3473-3481
    • Boldt, F.M.1    Heinze, J.2    Diez, M.3    Petersen, J.4    Borsch, M.5
  • 19
    • 30344437281 scopus 로고    scopus 로고
    • Measuring rotations of a few cross-bridges in skeletal muscle
    • Borejdo J., Talent J., and Akopova I. Measuring rotations of a few cross-bridges in skeletal muscle. Exp. Biol. Med. 231 (2006) 23-38
    • (2006) Exp. Biol. Med. , vol.231 , pp. 23-38
    • Borejdo, J.1    Talent, J.2    Akopova, I.3
  • 20
    • 33644982036 scopus 로고    scopus 로고
    • Rotations of a few cross bridges in muscle by confocal total internal reflection microscopy
    • Borejdo J., Talent J., Akopova I., and Burghardt T.P. Rotations of a few cross bridges in muscle by confocal total internal reflection microscopy. Biochim. Biophys. Acta Mol. Cell Res. 1763 (2006) 137-140
    • (2006) Biochim. Biophys. Acta Mol. Cell Res. , vol.1763 , pp. 137-140
    • Borejdo, J.1    Talent, J.2    Akopova, I.3    Burghardt, T.P.4
  • 21
    • 34247231421 scopus 로고    scopus 로고
    • Two forms of single-vesicle astrocyte exocytosis imaged with total internal reflection fluorescence microscopy
    • Bowser D.N., and Khakh B.S. Two forms of single-vesicle astrocyte exocytosis imaged with total internal reflection fluorescence microscopy. Proc. Natl. Acad. Sci. USA 104 (2007) 4212-4217
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4212-4217
    • Bowser, D.N.1    Khakh, B.S.2
  • 22
    • 0019350624 scopus 로고
    • Total internal reflection/fluorescence photobleaching recovery study of serum albumin adsorption dynamics
    • Burghardt T.P., and Axelrod D. Total internal reflection/fluorescence photobleaching recovery study of serum albumin adsorption dynamics. Biophys. J. 33 (1981) 455-468
    • (1981) Biophys. J. , vol.33 , pp. 455-468
    • Burghardt, T.P.1    Axelrod, D.2
  • 23
    • 33744822157 scopus 로고    scopus 로고
    • In situ fluorescent protein imaging with metal film-enhanced total internal reflection microscopy
    • Burghardt T.P., Charlesworth J.E., Halstead M.F., Tarara J.E., and Ajtai K. In situ fluorescent protein imaging with metal film-enhanced total internal reflection microscopy. Biophys. J. 90 (2006) 4662-4671
    • (2006) Biophys. J. , vol.90 , pp. 4662-4671
    • Burghardt, T.P.1    Charlesworth, J.E.2    Halstead, M.F.3    Tarara, J.E.4    Ajtai, K.5
  • 24
    • 0021668349 scopus 로고
    • Effect of planar dielectric interfaces on fluorescence emission and detection
    • Evanescent excitation with high-aperture collection
    • Burghardt T.P., and Thompson N.L. Effect of planar dielectric interfaces on fluorescence emission and detection. Evanescent excitation with high-aperture collection. Biophys. J. 46 (1984) 729-737
    • (1984) Biophys. J. , vol.46 , pp. 729-737
    • Burghardt, T.P.1    Thompson, N.L.2
  • 26
    • 15944375154 scopus 로고    scopus 로고
    • G-protein threshold behavior in the human neutrophil oxidant response: Measurement of G-proteins available for signaling in responding and non-responding subpopulations
    • Chang P.S., Axelrod D., Omann G.M., and Linderman J.J. G-protein threshold behavior in the human neutrophil oxidant response: Measurement of G-proteins available for signaling in responding and non-responding subpopulations. Cell. Signal. 17 (2005) 605-614
    • (2005) Cell. Signal. , vol.17 , pp. 605-614
    • Chang, P.S.1    Axelrod, D.2    Omann, G.M.3    Linderman, J.J.4
  • 27
    • 1442331597 scopus 로고    scopus 로고
    • Scanning total internal reflection fluorescence microscopy under one-photon and two-photon excitation: Image formation
    • Chon J.W.M., and Gu M. Scanning total internal reflection fluorescence microscopy under one-photon and two-photon excitation: Image formation. Appl. Optics 43 (2004) 1063-1071
    • (2004) Appl. Optics , vol.43 , pp. 1063-1071
    • Chon, J.W.M.1    Gu, M.2
  • 28
    • 31444449011 scopus 로고    scopus 로고
    • Dynamic study of the transition from hyaluronan- to integrin-mediated adhesion in chondrocytes
    • Cohen M., Kam Z., Addadi L., and Geiger B. Dynamic study of the transition from hyaluronan- to integrin-mediated adhesion in chondrocytes. EMBO J. 25 (2006) 302-311
    • (2006) EMBO J. , vol.25 , pp. 302-311
    • Cohen, M.1    Kam, Z.2    Addadi, L.3    Geiger, B.4
  • 29
    • 0002889077 scopus 로고    scopus 로고
    • Lateral resolution enhancement with standing evanescent waves
    • Cragg G.E., and So P.T.C. Lateral resolution enhancement with standing evanescent waves. Opt. Lett. 25 (2000) 46-48
    • (2000) Opt. Lett. , vol.25 , pp. 46-48
    • Cragg, G.E.1    So, P.T.C.2
  • 30
    • 0037377774 scopus 로고    scopus 로고
    • Reorientational dynamics of enzymes adsorbed on quartz: A temperature-dependent time-resolved TIRF anisotropy study
    • Czeslik C., Royer C., Hazlett T., and Mantulin W. Reorientational dynamics of enzymes adsorbed on quartz: A temperature-dependent time-resolved TIRF anisotropy study. Biophys. J. 84 (2003) 2533-2541
    • (2003) Biophys. J. , vol.84 , pp. 2533-2541
    • Czeslik, C.1    Royer, C.2    Hazlett, T.3    Mantulin, W.4
  • 31
    • 2142763928 scopus 로고    scopus 로고
    • Imaging the activity and localization of single voltage-gated Ca2+ channels by total internal reflection fluorescence microscopy
    • Demuro A., and Parker I. Imaging the activity and localization of single voltage-gated Ca2+ channels by total internal reflection fluorescence microscopy. Biophys. J. 86 (2004) 3250-3259
    • (2004) Biophys. J. , vol.86 , pp. 3250-3259
    • Demuro, A.1    Parker, I.2
  • 32
    • 0032517711 scopus 로고    scopus 로고
    • Simultaneous imaging of individual molecules aligned both parallel and perpendicular to the optic axis
    • Dickson R.M., Norris D.J., and Moerner W.E. Simultaneous imaging of individual molecules aligned both parallel and perpendicular to the optic axis. Phys. Rev. Lett. 81 (1998) 5322-5325
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 5322-5325
    • Dickson, R.M.1    Norris, D.J.2    Moerner, W.E.3
  • 33
    • 0030575902 scopus 로고    scopus 로고
    • Three-dimensional imaging of single molecules solvated in pores of poly(acrylamide) gels
    • Dickson R.M., Norris D.J., Tzeng Y.-L., and Moerner W.E. Three-dimensional imaging of single molecules solvated in pores of poly(acrylamide) gels. Science 274 (1996) 966-969
    • (1996) Science , vol.274 , pp. 966-969
    • Dickson, R.M.1    Norris, D.J.2    Tzeng, Y.-L.3    Moerner, W.E.4
  • 35
    • 23244466867 scopus 로고    scopus 로고
    • Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy
    • Forkey J.N., Quinlan M.E., and Goldman Y.E. Measurement of single macromolecule orientation by total internal reflection fluorescence polarization microscopy. Biophys. J. 89 (2005) 1261-1271
    • (2005) Biophys. J. , vol.89 , pp. 1261-1271
    • Forkey, J.N.1    Quinlan, M.E.2    Goldman, Y.E.3
  • 36
    • 15944425187 scopus 로고
    • Dynamics of nonspecific adsorption of insulin to erythrocyte membrane
    • Fulbright R.M., and Axelrod D. Dynamics of nonspecific adsorption of insulin to erythrocyte membrane. J. Fluoresc. 3 (1993) 1-16
    • (1993) J. Fluoresc. , vol.3 , pp. 1-16
    • Fulbright, R.M.1    Axelrod, D.2
  • 37
    • 20444452736 scopus 로고    scopus 로고
    • Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection
    • Gavutis M., Lata S., Lamken P., Muller P., and Piehler J. Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection. Biophys. J. 88 (2005) 4289-4302
    • (2005) Biophys. J. , vol.88 , pp. 4289-4302
    • Gavutis, M.1    Lata, S.2    Lamken, P.3    Muller, P.4    Piehler, J.5
  • 38
    • 0028015627 scopus 로고
    • Annexin IV reduces the rate of lateral lipid diffusion and changes the fluid phase structure of the lipid bilayer when it binds to negatively charged membranes in the presence of calcium
    • Gilmanshin R., Creutz C.E., and Tamm L.K. Annexin IV reduces the rate of lateral lipid diffusion and changes the fluid phase structure of the lipid bilayer when it binds to negatively charged membranes in the presence of calcium. Biochemistry 33 (1994) 8225-8832
    • (1994) Biochemistry , vol.33 , pp. 8225-8832
    • Gilmanshin, R.1    Creutz, C.E.2    Tamm, L.K.3
  • 39
    • 17044447869 scopus 로고
    • General electromagnetic theory of internal reflection fluorescence: The quantitative basis for mapping cell-substratum topography
    • Gingell D., Heavens O.S., and Mellor J.S. General electromagnetic theory of internal reflection fluorescence: The quantitative basis for mapping cell-substratum topography. J. Cell Sci. 87 (1987) 677-693
    • (1987) J. Cell Sci. , vol.87 , pp. 677-693
    • Gingell, D.1    Heavens, O.S.2    Mellor, J.S.3
  • 40
    • 33749489511 scopus 로고    scopus 로고
    • Insulin signalling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane
    • Gonzalez E., and McGraw T.E. Insulin signalling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane. Mol. Biol. Cell 17 (2006) 4484-4493
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4484-4493
    • Gonzalez, E.1    McGraw, T.E.2
  • 41
    • 30344473311 scopus 로고    scopus 로고
    • Organized arrays of individual DIVA molecules tethered to supported lipid bilayers
    • Graneli A., Yeykal C.C., Prasad T.K., and Greene E.C. Organized arrays of individual DIVA molecules tethered to supported lipid bilayers. Langmuir 22 (2006) 292-299
    • (2006) Langmuir , vol.22 , pp. 292-299
    • Graneli, A.1    Yeykal, C.C.2    Prasad, T.K.3    Greene, E.C.4
  • 42
    • 0033682973 scopus 로고    scopus 로고
    • Doubling the lateral resolution of wide-field fluorescence microscopy using structured illumination
    • Three-Dimensional and Multidimensional Microscopy: Image Acquisition Processing VII. Jose-Angel Conchello J.-A., Cogswell C.J., and Wilson T. (Eds)
    • Gustafsson M.G.L., Agard D.A., and Sedat J.W. Doubling the lateral resolution of wide-field fluorescence microscopy using structured illumination. In: Jose-Angel Conchello J.-A., Cogswell C.J., and Wilson T. (Eds). Three-Dimensional and Multidimensional Microscopy: Image Acquisition Processing VII. Proc SPIE 3919 (2000) 141-150
    • (2000) Proc SPIE , vol.3919 , pp. 141-150
    • Gustafsson, M.G.L.1    Agard, D.A.2    Sedat, J.W.3
  • 43
    • 24944539530 scopus 로고    scopus 로고
    • Nonlinear structured-illumination microscopy: Wide-field fluorescence imaging with theoretically unlimited resolution
    • Gustafsson M.G.L. Nonlinear structured-illumination microscopy: Wide-field fluorescence imaging with theoretically unlimited resolution. Proc. Natl. Acad. Sci. USA 102 (2005) 13081-13086
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13081-13086
    • Gustafsson, M.G.L.1
  • 46
    • 0033460188 scopus 로고    scopus 로고
    • Neuropeptide release by efficient recruitment of diffusing cytoplasmic secretory vesicles
    • Han W., Ng Y.-K., Axelrod D., and Levitan E.S. Neuropeptide release by efficient recruitment of diffusing cytoplasmic secretory vesicles. Proc. Natl. Acad. Sci. USA 96 (1999) 14577-14582
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14577-14582
    • Han, W.1    Ng, Y.-K.2    Axelrod, D.3    Levitan, E.S.4
  • 48
    • 0001535273 scopus 로고
    • Multiple internal reflection fluorescence spectroscopy
    • Harrick N.J., and Loeb G.I. Multiple internal reflection fluorescence spectroscopy. Anal. Chem. 45 (1973) 687-691
    • (1973) Anal. Chem. , vol.45 , pp. 687-691
    • Harrick, N.J.1    Loeb, G.I.2
  • 49
    • 0038360766 scopus 로고    scopus 로고
    • Lateral diffusion dynamics for single molecules of fluorescent cyanine dye at the free and surfactant-modifted dodecane-water interface
    • Hashimoto F., Tsukahara S., and Watarai H. Lateral diffusion dynamics for single molecules of fluorescent cyanine dye at the free and surfactant-modifted dodecane-water interface. Langmuir 19 (2003) 4197-4204
    • (2003) Langmuir , vol.19 , pp. 4197-4204
    • Hashimoto, F.1    Tsukahara, S.2    Watarai, H.3
  • 50
    • 11244324710 scopus 로고    scopus 로고
    • High count rates with total internal reflection fluorescence correlation spectroscopy
    • Hassler K., Anhut T., Rigler R., Gosch M., and Lasser T. High count rates with total internal reflection fluorescence correlation spectroscopy. Biophys. J. 88 (2005) L1-L3
    • (2005) Biophys. J. , vol.88
    • Hassler, K.1    Anhut, T.2    Rigler, R.3    Gosch, M.4    Lasser, T.5
  • 51
    • 25144466193 scopus 로고    scopus 로고
    • Total internal reflection fluorescence correlation spectroscopy (TIR-FCS) with low background and high count-rate per molecule
    • Hassler K., Leutenegger M., Rigler P., Rao R., Rigler R., Gosch M., and Lasser T. Total internal reflection fluorescence correlation spectroscopy (TIR-FCS) with low background and high count-rate per molecule. Opt. Express 13 (2005) 7415-7423
    • (2005) Opt. Express , vol.13 , pp. 7415-7423
    • Hassler, K.1    Leutenegger, M.2    Rigler, P.3    Rao, R.4    Rigler, R.5    Gosch, M.6    Lasser, T.7
  • 52
    • 19944394564 scopus 로고    scopus 로고
    • Motion of single DNA molecules at a liquid-solid interface as revealed by variable-angle evanescent-field microscopy
    • He Y., Li H.W., and Yeung E.S. Motion of single DNA molecules at a liquid-solid interface as revealed by variable-angle evanescent-field microscopy. J. Phys. Chem. B 109 (2005) 8820-8832
    • (2005) J. Phys. Chem. B , vol.109 , pp. 8820-8832
    • He, Y.1    Li, H.W.2    Yeung, E.S.3
  • 53
    • 84975574862 scopus 로고
    • Fluorescence emission at dielectric and metal-film interfaces
    • Hellen E.H., and Axelrod D. Fluorescence emission at dielectric and metal-film interfaces. J. Opt. Soc. Am. B 4 (1987) 337-350
    • (1987) J. Opt. Soc. Am. B , vol.4 , pp. 337-350
    • Hellen, E.H.1    Axelrod, D.2
  • 54
    • 0001295176 scopus 로고
    • Kinetics of epidermal growth factor/receptor binding on cells measured by total internal reflection/fluorescence recovery after photobleaching
    • Hellen E.H., and Axelrod D. Kinetics of epidermal growth factor/receptor binding on cells measured by total internal reflection/fluorescence recovery after photobleaching. J. Fluoresc. 1 (1991) 113-128
    • (1991) J. Fluoresc. , vol.1 , pp. 113-128
    • Hellen, E.H.1    Axelrod, D.2
  • 55
    • 0011201341 scopus 로고
    • Total internal reflection fluorescence: Theory and applications at biosurfaces
    • Loew L. (Ed), CRC Press, Boca Raton
    • Hellen E.H., Fulbright R.M., and Axelrod D. Total internal reflection fluorescence: Theory and applications at biosurfaces. In: Loew L. (Ed). Spectroscopic Membrane Probes (1988), CRC Press, Boca Raton 47-79
    • (1988) Spectroscopic Membrane Probes , pp. 47-79
    • Hellen, E.H.1    Fulbright, R.M.2    Axelrod, D.3
  • 56
    • 0028043265 scopus 로고
    • Reconstitution of membrane fusion sites. A total internal reflection fluorescence microscopy study of influenza hemagglutinin-mediated membrane fusion
    • Hinterdorfer P., Baber G., and Tamm L.K. Reconstitution of membrane fusion sites. A total internal reflection fluorescence microscopy study of influenza hemagglutinin-mediated membrane fusion. J. Biol. Chem. 269 (1994) 20360-20368
    • (1994) J. Biol. Chem. , vol.269 , pp. 20360-20368
    • Hinterdorfer, P.1    Baber, G.2    Tamm, L.K.3
  • 57
    • 0001452103 scopus 로고
    • Total reflection fluorescence (TRF)
    • Hirschfeld T. Total reflection fluorescence (TRF). Can. Spectrosc. 10 (1965) 128
    • (1965) Can. Spectrosc. , vol.10 , pp. 128
    • Hirschfeld, T.1
  • 58
    • 39049184569 scopus 로고    scopus 로고
    • Analysis of the late steps of exocytosis: Biochemical and total internal reflection fluorescence microscopy (TIRFM) studies
    • Holz R.W. Analysis of the late steps of exocytosis: Biochemical and total internal reflection fluorescence microscopy (TIRFM) studies. Cell. Mol. Neurobiol. 26 (2006) 439-447
    • (2006) Cell. Mol. Neurobiol. , vol.26 , pp. 439-447
    • Holz, R.W.1
  • 59
    • 20444372302 scopus 로고    scopus 로고
    • Simultaneous multicolor detection system of the single-molecular microbial antigen with total internal reflection fluorescence microscopy
    • Hoshino A., Fujioka K., Manabe N., Yamaya S., Goto Y., Yasuhara M., and Yamamoto K. Simultaneous multicolor detection system of the single-molecular microbial antigen with total internal reflection fluorescence microscopy. Microbiol. Immunol. 49 (2005) 461-470
    • (2005) Microbiol. Immunol. , vol.49 , pp. 461-470
    • Hoshino, A.1    Fujioka, K.2    Manabe, N.3    Yamaya, S.4    Goto, Y.5    Yasuhara, M.6    Yamamoto, K.7
  • 60
    • 0027448957 scopus 로고
    • Theory for 2-photon excitation in pattern photobleaching with evanescent illumination
    • Huang Z.P., and Thompson N.L. Theory for 2-photon excitation in pattern photobleaching with evanescent illumination. Biophys. Chem. 47 (1993) 241-249
    • (1993) Biophys. Chem. , vol.47 , pp. 241-249
    • Huang, Z.P.1    Thompson, N.L.2
  • 61
    • 4544249886 scopus 로고    scopus 로고
    • Single-molecule measurement in living cells
    • Ichinose J., and Sako Y. Single-molecule measurement in living cells. Trends Anal. Chem. 23 (2004) 587-594
    • (2004) Trends Anal. Chem. , vol.23 , pp. 587-594
    • Ichinose, J.1    Sako, Y.2
  • 63
    • 4444346762 scopus 로고    scopus 로고
    • Time-resolved total internal reflection fluorescence study on hybridization of complementary single-stranded DNAs at a water/oil interface
    • Ishizaka S., Ueda Y., and Kitamura N. Time-resolved total internal reflection fluorescence study on hybridization of complementary single-stranded DNAs at a water/oil interface. Anal. Chem. 76 (2004) 5075-5079
    • (2004) Anal. Chem. , vol.76 , pp. 5075-5079
    • Ishizaka, S.1    Ueda, Y.2    Kitamura, N.3
  • 64
    • 19344375822 scopus 로고    scopus 로고
    • Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis
    • Jaiswal J.K., Chakrabarti S., Andrews N.W., and Simon S.M. Synaptotagmin VII restricts fusion pore expansion during lysosomal exocytosis. PLOS Biol. 2 (2004) 1224-1232
    • (2004) PLOS Biol. , vol.2 , pp. 1224-1232
    • Jaiswal, J.K.1    Chakrabarti, S.2    Andrews, N.W.3    Simon, S.M.4
  • 65
    • 33846370222 scopus 로고    scopus 로고
    • Imaging single events at the cell membrane
    • Jaiswal J.K., and Simon S.M. Imaging single events at the cell membrane. Nat. Chem. Biol. 3 (2007) 92-98
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 92-98
    • Jaiswal, J.K.1    Simon, S.M.2
  • 66
  • 67
    • 0035795404 scopus 로고    scopus 로고
    • Restriction of secretory granule motion near the plasma membrane of chromaffin cells
    • Johns L.M., Levitan E.S., Shelden E.A., Holz R.W., and Axelrod D. Restriction of secretory granule motion near the plasma membrane of chromaffin cells. J. Cell Biol. 153 (2001) 177-190
    • (2001) J. Cell Biol. , vol.153 , pp. 177-190
    • Johns, L.M.1    Levitan, E.S.2    Shelden, E.A.3    Holz, R.W.4    Axelrod, D.5
  • 68
    • 33644965053 scopus 로고    scopus 로고
    • Investigation of cell adhesion to structured surfaces using total internal reflection fluorescence and confocal laser scanning microscopy
    • Joos U., Biskup T., Ernst O., Westphal I., Gherasim C., Schmidt R., Edinger K., Pilarczyk G., and Duschl C. Investigation of cell adhesion to structured surfaces using total internal reflection fluorescence and confocal laser scanning microscopy. Eur. J. Cell Biol. 85 (2006) 225-228
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 225-228
    • Joos, U.1    Biskup, T.2    Ernst, O.3    Westphal, I.4    Gherasim, C.5    Schmidt, R.6    Edinger, K.7    Pilarczyk, G.8    Duschl, C.9
  • 69
    • 0025096789 scopus 로고
    • Binding of proteins to specific target sites in membranes measured by total internal reflection fluorescence microscopy
    • Kalb E., Engel J., and Tamm L.K. Binding of proteins to specific target sites in membranes measured by total internal reflection fluorescence microscopy. Biochemistry 29 (1990) 1607-1613
    • (1990) Biochemistry , vol.29 , pp. 1607-1613
    • Kalb, E.1    Engel, J.2    Tamm, L.K.3
  • 70
    • 33749445649 scopus 로고    scopus 로고
    • Spatially and temporally synchronized atomic force and total internal reflection fluorescence microscopy for imaging and manipulating cells and biomolecules
    • Kellermayer M.S.Z., Karsai A., Kengyel A., Nagy A., Bianco P., Huber T., Kulcsar A., Niedetzky C., Proksch R., and Grama L. Spatially and temporally synchronized atomic force and total internal reflection fluorescence microscopy for imaging and manipulating cells and biomolecules. Biophys. J. 91 (2006) 2665-2677
    • (2006) Biophys. J. , vol.91 , pp. 2665-2677
    • Kellermayer, M.S.Z.1    Karsai, A.2    Kengyel, A.3    Nagy, A.4    Bianco, P.5    Huber, T.6    Kulcsar, A.7    Niedetzky, C.8    Proksch, R.9    Grama, L.10
  • 71
    • 10844236465 scopus 로고    scopus 로고
    • Near-wall hindered Brownian diffusion of nanoparticles examined by three-dimensional ratiometric total internal reflection fluorescence microscopy (3-D R-TIRFM)
    • Kihm K.D., Banerjee A., Choi C.K., and Takagi T. Near-wall hindered Brownian diffusion of nanoparticles examined by three-dimensional ratiometric total internal reflection fluorescence microscopy (3-D R-TIRFM). Exp. Fluids 37 (2004) 811-824
    • (2004) Exp. Fluids , vol.37 , pp. 811-824
    • Kihm, K.D.1    Banerjee, A.2    Choi, C.K.3    Takagi, T.4
  • 72
    • 34247173028 scopus 로고    scopus 로고
    • Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actibn-capping protein-implications for how capping protein binds the actin filament
    • Kim K., McCully M.E., Bhattacharya N., Butler B., Sept D., and Cooper J.A. Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actibn-capping protein-implications for how capping protein binds the actin filament. J. Biol. Chem. 282 (2007) 5871-5879
    • (2007) J. Biol. Chem. , vol.282 , pp. 5871-5879
    • Kim, K.1    McCully, M.E.2    Bhattacharya, N.3    Butler, B.4    Sept, D.5    Cooper, J.A.6
  • 73
    • 0034457539 scopus 로고    scopus 로고
    • Muscle, myosin and single molecules
    • Higgins S.J., and Banting G. (Eds), Portland Press, London
    • Knight A.E., and Molloy J.E. Muscle, myosin and single molecules. In: Higgins S.J., and Banting G. (Eds). Molecular Motors, Essays in Biochemistry Vol. 35 (2000), Portland Press, London 200
    • (2000) Molecular Motors, Essays in Biochemistry , vol.35 , pp. 200
    • Knight, A.E.1    Molloy, J.E.2
  • 74
    • 22544433123 scopus 로고    scopus 로고
    • An angstrom scale interaction between plasma membrane ATP-gated P2X(2) and alpha(4)beta(2) nicotinic channels measured with fluorescence resonance energy transfer and total internal reflection fluorescence microscopy
    • Khakh B.S., Fisher J.A., Nashmi R., Bowser D.N., and Lester H.A. An angstrom scale interaction between plasma membrane ATP-gated P2X(2) and alpha(4)beta(2) nicotinic channels measured with fluorescence resonance energy transfer and total internal reflection fluorescence microscopy. J. Neurosci. 25 (2005) 6911-6920
    • (2005) J. Neurosci. , vol.25 , pp. 6911-6920
    • Khakh, B.S.1    Fisher, J.A.2    Nashmi, R.3    Bowser, D.N.4    Lester, H.A.5
  • 75
    • 0343006847 scopus 로고    scopus 로고
    • Interactions of the chemotaxis signal protein CheY with bacterial flagellar motors visualized by evanescent wave microscopy
    • Khan S., Pierce D., and Vale R.D. Interactions of the chemotaxis signal protein CheY with bacterial flagellar motors visualized by evanescent wave microscopy. Curr. Biol. 10 (2000) 927-930
    • (2000) Curr. Biol. , vol.10 , pp. 927-930
    • Khan, S.1    Pierce, D.2    Vale, R.D.3
  • 76
    • 3342978083 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy-a powerful tool to study single quantum dots
    • Kobitski A.Y., Heyes C.D., and Nienhaus G.U. Total internal reflection fluorescence microscopy-a powerful tool to study single quantum dots. Appl. Surf. Sci. 234 (2004) 86-92
    • (2004) Appl. Surf. Sci. , vol.234 , pp. 86-92
    • Kobitski, A.Y.1    Heyes, C.D.2    Nienhaus, G.U.3
  • 77
    • 33750967073 scopus 로고    scopus 로고
    • Imaging clathrin dynamics in Drosophila melanogaster hemocytes reveals a role for actin in vesicle fusion
    • Kochubey O., Majumdar A., and Klingauf J. Imaging clathrin dynamics in Drosophila melanogaster hemocytes reveals a role for actin in vesicle fusion. Traffic 7 (2006) 1614-1627
    • (2006) Traffic , vol.7 , pp. 1614-1627
    • Kochubey, O.1    Majumdar, A.2    Klingauf, J.3
  • 78
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar D.R., Harris E.S., Mahaffy R., Higgs H.N., and Pollard T.D. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124 (2006) 423-435
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 79
    • 33644897629 scopus 로고    scopus 로고
    • Dynamic polymorphism of single actin molecules in the actin filament
    • Kozuka J., Yokota H., Arai Y., Ishii Y., and Yanagida T. Dynamic polymorphism of single actin molecules in the actin filament. Nat. Chem. Biol. 2 (2006) 83-86
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 83-86
    • Kozuka, J.1    Yokota, H.2    Arai, Y.3    Ishii, Y.4    Yanagida, T.5
  • 80
    • 0016802234 scopus 로고
    • A new immunoassay based on fluorescence excitation by internal reflection spectroscopy
    • Kronick M.N., and Little W.A. A new immunoassay based on fluorescence excitation by internal reflection spectroscopy. J. Immunol. Methods 8 (1975) 235-240
    • (1975) J. Immunol. Methods , vol.8 , pp. 235-240
    • Kronick, M.N.1    Little, W.A.2
  • 81
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • Kuhn J.R., and Pollard T.D. Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys. J. 88 (2005) 1387-1402
    • (2005) Biophys. J. , vol.88 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 82
    • 0034728349 scopus 로고    scopus 로고
    • Rebinding of IgE Fabs at haptenated planar membranes: Measurement by total internal reflection with fluorescence photobleaching recovery
    • Lagerholm B.C., Starr T.E., Volovyk Z.N., and Thompson N.L. Rebinding of IgE Fabs at haptenated planar membranes: Measurement by total internal reflection with fluorescence photobleaching recovery. Biochemistry 39 (2000) 2042-2051
    • (2000) Biochemistry , vol.39 , pp. 2042-2051
    • Lagerholm, B.C.1    Starr, T.E.2    Volovyk, Z.N.3    Thompson, N.L.4
  • 83
    • 0037286742 scopus 로고    scopus 로고
    • Cytomechanics applications of optical sectioning microscopy
    • Lagerholm B.C., Vanni S., Taylor D.L., and Lanni F. Cytomechanics applications of optical sectioning microscopy. Methods Enzymol. 361 (2003) 175-197
    • (2003) Methods Enzymol. , vol.361 , pp. 175-197
    • Lagerholm, B.C.1    Vanni, S.2    Taylor, D.L.3    Lanni, F.4
  • 84
    • 13244251098 scopus 로고    scopus 로고
    • Radiative decay engineering 5: Metal-enhanced fluorescence and plasmon emission
    • Lakowicz J.R. Radiative decay engineering 5: Metal-enhanced fluorescence and plasmon emission. Anal. Biochem. 337 (2005) 171-194
    • (2005) Anal. Biochem. , vol.337 , pp. 171-194
    • Lakowicz, J.R.1
  • 85
    • 0030612594 scopus 로고    scopus 로고
    • Ca2+-triggered peptide secretion neurotechnique in single cells imaged with green fluorescent protein and evanescent-wave microscopy
    • Lang T., Wacker I., Steyer J., Kaether C., Wunderlich I., Soldati T., Gerdes H.-H., and Almers W. Ca2+-triggered peptide secretion neurotechnique in single cells imaged with green fluorescent protein and evanescent-wave microscopy. Neuron 18 (1997) 857-863
    • (1997) Neuron , vol.18 , pp. 857-863
    • Lang, T.1    Wacker, I.2    Steyer, J.3    Kaether, C.4    Wunderlich, I.5    Soldati, T.6    Gerdes, H.-H.7    Almers, W.8
  • 86
    • 0034130493 scopus 로고    scopus 로고
    • Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells
    • Lang T., Wacker I., Wunderlich I., Rohrbach A., Giese G., Soldati T., and Almers W. Role of actin cortex in the subplasmalemmal transport of secretory granules in PC-12 cells. Biophys. J. 78 (2000) 2863-2877
    • (2000) Biophys. J. , vol.78 , pp. 2863-2877
    • Lang, T.1    Wacker, I.2    Wunderlich, I.3    Rohrbach, A.4    Giese, G.5    Soldati, T.6    Almers, W.7
  • 87
    • 4344629047 scopus 로고    scopus 로고
    • Single-molecule orientations determined by direct emission pattern imaging
    • Lieb M.A., Zavislan J.M., and Novotny L. Single-molecule orientations determined by direct emission pattern imaging. J. Opt. Soc. Am. B 21 (2004) 1210-1215
    • (2004) J. Opt. Soc. Am. B , vol.21 , pp. 1210-1215
    • Lieb, M.A.1    Zavislan, J.M.2    Novotny, L.3
  • 88
    • 0033624441 scopus 로고    scopus 로고
    • Super-resolution measurements with evanescent-wave fluorescence excitation using variable beam incidence
    • Loerke D., Preitz B., Stuhmer W., Oheim M., and Biomed J. Super-resolution measurements with evanescent-wave fluorescence excitation using variable beam incidence. Optics 5 (2000) 23-30
    • (2000) Optics , vol.5 , pp. 23-30
    • Loerke, D.1    Preitz, B.2    Stuhmer, W.3    Oheim, M.4    Biomed, J.5
  • 89
    • 0037107012 scopus 로고    scopus 로고
    • Quantifying axial secretory-granule motion with variable-angle evanescent-field excitation
    • Loerke D., Stuhmer W., and Oheim M. Quantifying axial secretory-granule motion with variable-angle evanescent-field excitation. J. Neurosci. Methods 119 (2002) 65-73
    • (2002) J. Neurosci. Methods , vol.119 , pp. 65-73
    • Loerke, D.1    Stuhmer, W.2    Oheim, M.3
  • 90
    • 33751229634 scopus 로고    scopus 로고
    • Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex
    • Mahaffey R.E., and Pollard T.D. Kinetics of the formation and dissociation of actin filament branches mediated by Arp2/3 complex. Biophys. J. 91 (2006) 3519-3528
    • (2006) Biophys. J. , vol.91 , pp. 3519-3528
    • Mahaffey, R.E.1    Pollard, T.D.2
  • 91
    • 32144433831 scopus 로고    scopus 로고
    • Use of TIRF microscopy to visualize actin and microtubules in migrating cells
    • Manneville J.B. Use of TIRF microscopy to visualize actin and microtubules in migrating cells. Methods Enzymol. 406 (2006) 520-532
    • (2006) Methods Enzymol. , vol.406 , pp. 520-532
    • Manneville, J.B.1
  • 92
    • 33947697260 scopus 로고    scopus 로고
    • Automatic detection of single fluorophores in live cells
    • Mashanov G.I., and Malloy J.E. Automatic detection of single fluorophores in live cells. Biophys. J. 92 (2007) 2199-2211
    • (2007) Biophys. J. , vol.92 , pp. 2199-2211
    • Mashanov, G.I.1    Malloy, J.E.2
  • 93
    • 0034114554 scopus 로고    scopus 로고
    • Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells
    • Mathur A.B., Truskey G.A., and Reichert W.M. Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells. Biophys. J. 78 (2000) 1725-1735
    • (2000) Biophys. J. , vol.78 , pp. 1725-1735
    • Mathur, A.B.1    Truskey, G.A.2    Reichert, W.M.3
  • 94
    • 33645459399 scopus 로고    scopus 로고
    • Fluorescence emission patterns near glass and metal-coated surfaces investigated with back focal plane imaging
    • Mattheyses A.L., and Axelrod D. Fluorescence emission patterns near glass and metal-coated surfaces investigated with back focal plane imaging. J. Biomed. Opt. 10 (2005) 054007/1-6
    • (2005) J. Biomed. Opt. , vol.10
    • Mattheyses, A.L.1    Axelrod, D.2
  • 95
    • 33744489651 scopus 로고    scopus 로고
    • Direct measurement of evanescent field profile and depth in TIRF microscopy
    • Mattheyses A.L., and Axelrod D. Direct measurement of evanescent field profile and depth in TIRF microscopy. J. Biomed. Opt. 11 (2005) 014006/1-7
    • (2005) J. Biomed. Opt. , vol.11
    • Mattheyses, A.L.1    Axelrod, D.2
  • 96
    • 33747891026 scopus 로고    scopus 로고
    • Effective elimination of laser interference fringing in fluorescence microscopy by spinning azimuthal incidence angle
    • Mattheyses A.L., Shaw K.D., and Axelrod D. Effective elimination of laser interference fringing in fluorescence microscopy by spinning azimuthal incidence angle. Microsc. Res. Tech. 69 (2006) 642-647
    • (2006) Microsc. Res. Tech. , vol.69 , pp. 642-647
    • Mattheyses, A.L.1    Shaw, K.D.2    Axelrod, D.3
  • 97
    • 5644282799 scopus 로고    scopus 로고
    • Metal-enhanced fluorescence immunoassays using total internal reflection and silver island-coated surfaces
    • Matveeva E., Gryczynski Z., Malicka J., Gryczynski I., and Lakowicz J.R. Metal-enhanced fluorescence immunoassays using total internal reflection and silver island-coated surfaces. Anal. Biochem. 334 (2004) 303-311
    • (2004) Anal. Biochem. , vol.334 , pp. 303-311
    • Matveeva, E.1    Gryczynski, Z.2    Malicka, J.3    Gryczynski, I.4    Lakowicz, J.R.5
  • 98
    • 0242586112 scopus 로고    scopus 로고
    • Total internal reflection fluorescence-correlation spectroscopy study of molecular transport in thin sol-gel films
    • McCain K.S., and Harris J.M. Total internal reflection fluorescence-correlation spectroscopy study of molecular transport in thin sol-gel films. Anal. Chem. 75 (2003) 3616-3624
    • (2003) Anal. Chem. , vol.75 , pp. 3616-3624
    • McCain, K.S.1    Harris, J.M.2
  • 99
    • 1242271265 scopus 로고    scopus 로고
    • Modifying the adsorption behavior of polyamidoamine dendrimers at silica surfaces investigated by total internal reflection fluorescence correlation spectroscopy
    • McCain K.S., Schluesche P., and Harris J.M. Modifying the adsorption behavior of polyamidoamine dendrimers at silica surfaces investigated by total internal reflection fluorescence correlation spectroscopy. Anal. Chem. 76 (2004) 930-938
    • (2004) Anal. Chem. , vol.76 , pp. 930-938
    • McCain, K.S.1    Schluesche, P.2    Harris, J.M.3
  • 100
    • 0343488536 scopus 로고    scopus 로고
    • Cytoskeletal protein binding kinetics at planar phospholipid membranes
    • McKiernan A.M., MacDonald R.C., MacDonald R.I., and Axelrod D. Cytoskeletal protein binding kinetics at planar phospholipid membranes. Biophys. J. 73 (1997) 1987-1998
    • (1997) Biophys. J. , vol.73 , pp. 1987-1998
    • McKiernan, A.M.1    MacDonald, R.C.2    MacDonald, R.I.3    Axelrod, D.4
  • 101
  • 102
    • 0034368539 scopus 로고    scopus 로고
    • Radiative absorption, fluorescence, and scattering of a classical dipole near a lossless interface: A unified description
    • Mertz J. Radiative absorption, fluorescence, and scattering of a classical dipole near a lossless interface: A unified description. J. Opt. Soc. Am. B 17 (2000) 1906-1913
    • (2000) J. Opt. Soc. Am. B , vol.17 , pp. 1906-1913
    • Mertz, J.1
  • 103
    • 23244445997 scopus 로고    scopus 로고
    • Micrometer-sized supported lipid bilayer arrays for bacterial toxin binding studies through total internal reflection fluorescence microscopy
    • Moran-Mirabal J.M., Edel J.B., Meyer G.D., Throckmorton D., Singh A.K., and Craighead H.G. Micrometer-sized supported lipid bilayer arrays for bacterial toxin binding studies through total internal reflection fluorescence microscopy. Biophys. J. 89 (2005) 296-305
    • (2005) Biophys. J. , vol.89 , pp. 296-305
    • Moran-Mirabal, J.M.1    Edel, J.B.2    Meyer, G.D.3    Throckmorton, D.4    Singh, A.K.5    Craighead, H.G.6
  • 104
    • 33646704772 scopus 로고    scopus 로고
    • Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo
    • Moseley J.B., Okada K., Balcer H.I., Kovar D.R., Pollard T.D., and Goode B.L. Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo. J. Cell Sci. 119 (2006) 1547-1557
    • (2006) J. Cell Sci. , vol.119 , pp. 1547-1557
    • Moseley, J.B.1    Okada, K.2    Balcer, H.I.3    Kovar, D.R.4    Pollard, T.D.5    Goode, B.L.6
  • 105
    • 33748440956 scopus 로고    scopus 로고
    • TIRF microscopy analysis of the mechanism of insulin exocytosis
    • Nagamatsu S. TIRF microscopy analysis of the mechanism of insulin exocytosis. Endocr. J. 53 (2006) 433-440
    • (2006) Endocr. J. , vol.53 , pp. 433-440
    • Nagamatsu, S.1
  • 106
    • 0000412790 scopus 로고    scopus 로고
    • Method of obtaining optical sectioning by using structured light in a conventional microscope
    • Neil M.A.A., Juskaitis R., and Wilson T. Method of obtaining optical sectioning by using structured light in a conventional microscope. Opt. Lett. 22 (1997) 1905-1907
    • (1997) Opt. Lett. , vol.22 , pp. 1905-1907
    • Neil, M.A.A.1    Juskaitis, R.2    Wilson, T.3
  • 107
    • 33746783857 scopus 로고    scopus 로고
    • Visualizing single fluorophores in live cells
    • Nenasheva T.A., and Mashanov G.L. Visualizing single fluorophores in live cells. Biofizika 51 (2006) 454-465
    • (2006) Biofizika , vol.51 , pp. 454-465
    • Nenasheva, T.A.1    Mashanov, G.L.2
  • 110
    • 33846942621 scopus 로고    scopus 로고
    • Primed vesicles can be distinguished from docked vesicles by analyzing their mobility
    • Nofal S., Becherer U., Hof D., Matti U., and Rettig J. Primed vesicles can be distinguished from docked vesicles by analyzing their mobility. J. Neurosci. 27 (2007) 1386-1395
    • (2007) J. Neurosci. , vol.27 , pp. 1386-1395
    • Nofal, S.1    Becherer, U.2    Hof, D.3    Matti, U.4    Rettig, J.5
  • 111
    • 0034951634 scopus 로고    scopus 로고
    • Imaging transmitter release. II. A practical guide to evanescent-wave imaging
    • Oheim M. Imaging transmitter release. II. A practical guide to evanescent-wave imaging. Lasers Med. Sci. 16 (2001) 159-170
    • (2001) Lasers Med. Sci. , vol.16 , pp. 159-170
    • Oheim, M.1
  • 112
    • 0031938792 scopus 로고    scopus 로고
    • The last few milliseconds in the life of a secretory granule: Docking, dynamics and fusion visualized by total internal reflection fluorescence microscopy (TIRFM)
    • Oheim M., Loerke D., Stuhmer W., and Chow R.H. The last few milliseconds in the life of a secretory granule: Docking, dynamics and fusion visualized by total internal reflection fluorescence microscopy (TIRFM). Eur. Biophys. J. 27 (1998) 83-98
    • (1998) Eur. Biophys. J. , vol.27 , pp. 83-98
    • Oheim, M.1    Loerke, D.2    Stuhmer, W.3    Chow, R.H.4
  • 113
    • 0032937795 scopus 로고    scopus 로고
    • Multiple stimulation dependent processes regulate the size of the releasable pool of vesicles
    • Oheim M., Loerke D., Stuhmer W., and Chow R.H. Multiple stimulation dependent processes regulate the size of the releasable pool of vesicles. Eur. Biophys. J. 28 (1999) 91-101
    • (1999) Eur. Biophys. J. , vol.28 , pp. 91-101
    • Oheim, M.1    Loerke, D.2    Stuhmer, W.3    Chow, R.H.4
  • 115
    • 0033826785 scopus 로고    scopus 로고
    • Tracking chromaffin granules on their way through the actin cortex
    • Oheim M., and Stuhmer W. Tracking chromaffin granules on their way through the actin cortex. Eur. Biophys. J. 29 (2000) 67-89
    • (2000) Eur. Biophys. J. , vol.29 , pp. 67-89
    • Oheim, M.1    Stuhmer, W.2
  • 116
    • 0034386996 scopus 로고    scopus 로고
    • Interaction of secretory organelles with the membrane
    • Oheim M., and Stuhmer W. Interaction of secretory organelles with the membrane. J. Membr. Biol. 178 (2000) 163-173
    • (2000) J. Membr. Biol. , vol.178 , pp. 163-173
    • Oheim, M.1    Stuhmer, W.2
  • 117
    • 0029985171 scopus 로고    scopus 로고
    • Membrane proximal calcium transients in stimulated neutrophils seen by total internal reflection fluorescence
    • Omann G.M., and Axelrod D. Membrane proximal calcium transients in stimulated neutrophils seen by total internal reflection fluorescence. Biophys. J. 71 (1996) 2885-2891
    • (1996) Biophys. J. , vol.71 , pp. 2885-2891
    • Omann, G.M.1    Axelrod, D.2
  • 118
    • 26844480981 scopus 로고    scopus 로고
    • Real-time dipole orientational imaging as a probe of ligand-protein interactions
    • Osborne M.A. Real-time dipole orientational imaging as a probe of ligand-protein interactions. J. Phys. Chem. B 109 (2005) 18153-18161
    • (2005) J. Phys. Chem. B , vol.109 , pp. 18153-18161
    • Osborne, M.A.1
  • 119
    • 26944460384 scopus 로고    scopus 로고
    • Time-resolved total internal reflection fluorescence spectroscopy-Part I. Photophysics of Coumarin 343 at liquid/liquid interface
    • Pant D., and Girault H.H. Time-resolved total internal reflection fluorescence spectroscopy-Part I. Photophysics of Coumarin 343 at liquid/liquid interface. Phys. Chem. Chem. Phys. 7 (2005) 3457-3463
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 3457-3463
    • Pant, D.1    Girault, H.H.2
  • 120
    • 33749464239 scopus 로고    scopus 로고
    • Initiation of attachment and generation of mature focal adhesions by integrin-containing filopodia in cell spreading
    • Partridge M.A., and Marcantonio E.E. Initiation of attachment and generation of mature focal adhesions by integrin-containing filopodia in cell spreading. Mol. Biol. Cell 17 (2006) 4237-4248
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4237-4248
    • Partridge, M.A.1    Marcantonio, E.E.2
  • 121
    • 7444263549 scopus 로고    scopus 로고
    • Recapture after exocytosis causes differential retention of protein in granules of bovine chromaffin cells
    • Perrais D., Kleppe I.C., Taraska J.W., and Almers W. Recapture after exocytosis causes differential retention of protein in granules of bovine chromaffin cells. J. Physiol. 560 (2004) 413-428
    • (2004) J. Physiol. , vol.560 , pp. 413-428
    • Perrais, D.1    Kleppe, I.C.2    Taraska, J.W.3    Almers, W.4
  • 122
    • 0026690278 scopus 로고
    • Binding kinetics of an anti-dinitrophenyl monoclonal Fab on supported phospholipid monolayers measured by total internal reflection with fluorescence photobleaching recovery
    • Pisarchick M.L., Gesty D., and Thompson N.L. Binding kinetics of an anti-dinitrophenyl monoclonal Fab on supported phospholipid monolayers measured by total internal reflection with fluorescence photobleaching recovery. Biophys. J. 63 (1992) 215-223
    • (1992) Biophys. J. , vol.63 , pp. 215-223
    • Pisarchick, M.L.1    Gesty, D.2    Thompson, N.L.3
  • 124
    • 0034022185 scopus 로고    scopus 로고
    • Observing secretory granules with a multiangle evanescent wave microscope
    • Rohrbach A. Observing secretory granules with a multiangle evanescent wave microscope. Biophys. J. 78 (2000) 2641-2654
    • (2000) Biophys. J. , vol.78 , pp. 2641-2654
    • Rohrbach, A.1
  • 125
    • 0041972289 scopus 로고    scopus 로고
    • Confocal total-internal-reflection fluorescence microscopy with a high-aperture parabolic mirror lens
    • Ruckstuhl T., and Seeger S. Confocal total-internal-reflection fluorescence microscopy with a high-aperture parabolic mirror lens. Appl. Opt. 42 (2003) 3277-3283
    • (2003) Appl. Opt. , vol.42 , pp. 3277-3283
    • Ruckstuhl, T.1    Seeger, S.2
  • 126
    • 1642588184 scopus 로고    scopus 로고
    • Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy
    • Ruckstuhl T., and Seeger S. Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy. Opt. Lett. 29 (2004) 569-571
    • (2004) Opt. Lett. , vol.29 , pp. 569-571
    • Ruckstuhl, T.1    Seeger, S.2
  • 127
    • 0031459220 scopus 로고    scopus 로고
    • Dual-colour microscopy of single fluorophores bound to myosin interacting with fluorescently labelled actin using anti-Stokes fluorescence
    • Saito K., Tokunaga M., Iwane A.H., and Yanagida T. Dual-colour microscopy of single fluorophores bound to myosin interacting with fluorescently labelled actin using anti-Stokes fluorescence. J. Microsc. Oxf. 188 (1997) 255-263
    • (1997) J. Microsc. Oxf. , vol.188 , pp. 255-263
    • Saito, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 128
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y., Miniguchi S., and Yanagida T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol. 2 (2000) 168-172
    • (2000) Nat. Cell Biol. , vol.2 , pp. 168-172
    • Sako, Y.1    Miniguchi, S.2    Yanagida, T.3
  • 129
    • 4444380329 scopus 로고    scopus 로고
    • Simultaneous atomic force microscope and fluorescence measurements of protein unfolding using a calibrated evanescent wave
    • Sarkar A., Robertson R.B., and Fernandez J.M. Simultaneous atomic force microscope and fluorescence measurements of protein unfolding using a calibrated evanescent wave. Proc. Natl. Acad. Sci. USA 101 (2004) 12882-12886
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12882-12886
    • Sarkar, A.1    Robertson, R.B.2    Fernandez, J.M.3
  • 130
    • 33646713911 scopus 로고    scopus 로고
    • How neurosecretory vesicles release their cargo
    • Scalettar B.A. How neurosecretory vesicles release their cargo. Neuroscientist 12 (2006) 164-176
    • (2006) Neuroscientist , vol.12 , pp. 164-176
    • Scalettar, B.A.1
  • 131
    • 0036591970 scopus 로고    scopus 로고
    • Neuronal calcium sensor-1 binds to regulated secretory organelles and functions in basal and stimulated exocytosis in PC12 cells
    • Scalettar B.A., Rosa P., Taverna E., Francolini M., Tsuboi T., Terekawa S., Koizumi S., Roder J., and Jeromin A. Neuronal calcium sensor-1 binds to regulated secretory organelles and functions in basal and stimulated exocytosis in PC12 cells. J. Cell Sci. 115 (2002) 2399-2412
    • (2002) J. Cell Sci. , vol.115 , pp. 2399-2412
    • Scalettar, B.A.1    Rosa, P.2    Taverna, E.3    Francolini, M.4    Tsuboi, T.5    Terekawa, S.6    Koizumi, S.7    Roder, J.8    Jeromin, A.9
  • 132
    • 0242695823 scopus 로고    scopus 로고
    • Fluorescence imaging with two-photon evanescent wave excitation
    • Schapper F., Goncalves J.T., and Oheim M. Fluorescence imaging with two-photon evanescent wave excitation. Eur. Biophys. J. 32 (2003) 635-643
    • (2003) Eur. Biophys. J. , vol.32 , pp. 635-643
    • Schapper, F.1    Goncalves, J.T.2    Oheim, M.3
  • 133
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection microscopy
    • Schmoranzer J., Goulian M., Axelrod D., and Simon S.M. Imaging constitutive exocytosis with total internal reflection microscopy. J. Cell Biol. 149 (2000) 23-31
    • (2000) J. Cell Biol. , vol.149 , pp. 23-31
    • Schmoranzer, J.1    Goulian, M.2    Axelrod, D.3    Simon, S.M.4
  • 134
    • 0344034726 scopus 로고    scopus 로고
    • Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge
    • Schmoranzer J., Kreitzer G., and Simon S.M. Migrating fibroblasts perform polarized, microtubule-dependent exocytosis towards the leading edge. J. Cell Sci. 116 (2003) 4513-4519
    • (2003) J. Cell Sci. , vol.116 , pp. 4513-4519
    • Schmoranzer, J.1    Kreitzer, G.2    Simon, S.M.3
  • 135
    • 13844267499 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy: Technical innovations and novel applications
    • Schneckenburger H. Total internal reflection fluorescence microscopy: Technical innovations and novel applications. Curr. Opin. Biotechnol. 16 (2005) 13-18
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 13-18
    • Schneckenburger, H.1
  • 136
    • 0043231283 scopus 로고    scopus 로고
    • Time-gated total internal reflection fluorescence spectroscopy (TG-TIRFS): Application to the membrane marker laurdan
    • Schneckenburger H., Stock K., Strauss W.S.L., Eickholz J., and Sailer R. Time-gated total internal reflection fluorescence spectroscopy (TG-TIRFS): Application to the membrane marker laurdan. J. Microsc. Oxf. 211 (2003) 30-36
    • (2003) J. Microsc. Oxf. , vol.211 , pp. 30-36
    • Schneckenburger, H.1    Stock, K.2    Strauss, W.S.L.3    Eickholz, J.4    Sailer, R.5
  • 137
    • 31444437864 scopus 로고    scopus 로고
    • Progressive movement of single kinesins on crowded microtubules visualized using quantum dots
    • Seitz A., and Surrey T. Progressive movement of single kinesins on crowded microtubules visualized using quantum dots. EMBO J. 25 (2006) 267-277
    • (2006) EMBO J. , vol.25 , pp. 267-277
    • Seitz, A.1    Surrey, T.2
  • 139
    • 33846787024 scopus 로고    scopus 로고
    • Imaging synaptosomal calcium concentration microdomains and vesicle fusion by using total internal reflection fluorescent microscopy
    • Serulle Y., Sugimori M., and Linas R.R. Imaging synaptosomal calcium concentration microdomains and vesicle fusion by using total internal reflection fluorescent microscopy. Proc. Natl. Acad. Sci. USA 104 (2007) 1697-1702
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1697-1702
    • Serulle, Y.1    Sugimori, M.2    Linas, R.R.3
  • 140
    • 33750919274 scopus 로고    scopus 로고
    • Coupling evanescent-wave fluorescence imaging and spectroscopy with scanning probe microscopy: Challenges and insights from TIRF-AFM
    • Shaw J.E., Oreopoulos J., Wong D., Hsu J.C.Y., and Yip C.M. Coupling evanescent-wave fluorescence imaging and spectroscopy with scanning probe microscopy: Challenges and insights from TIRF-AFM. Surf. Interface Anal. 38 (2006) 1459-1471
    • (2006) Surf. Interface Anal. , vol.38 , pp. 1459-1471
    • Shaw, J.E.1    Oreopoulos, J.2    Wong, D.3    Hsu, J.C.Y.4    Yip, C.M.5
  • 141
    • 33846695393 scopus 로고    scopus 로고
    • Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions
    • Shaw R.M., Fay A.J., Puthenveedu M.A., von Zastrow M., Jan Y.N., and Jan L.Y. Microtubule plus-end-tracking proteins target gap junctions directly from the cell interior to adherens junctions. Cell 128 (2007) 547-560
    • (2007) Cell , vol.128 , pp. 547-560
    • Shaw, R.M.1    Fay, A.J.2    Puthenveedu, M.A.3    von Zastrow, M.4    Jan, Y.N.5    Jan, L.Y.6
  • 142
    • 16244419347 scopus 로고    scopus 로고
    • Mechanisms of transport and exocytosis of dense-core-granules containing tissue plasminogen activator in developing hippocampal neurons
    • Silverman M.A., Johnson S., Gurkins D., Farmer M., Lochner J.E., Rosa P., and Scalettar B.A. Mechanisms of transport and exocytosis of dense-core-granules containing tissue plasminogen activator in developing hippocampal neurons. J. Neurosci. 25 (2005) 3095-3106
    • (2005) J. Neurosci. , vol.25 , pp. 3095-3106
    • Silverman, M.A.1    Johnson, S.2    Gurkins, D.3    Farmer, M.4    Lochner, J.E.5    Rosa, P.6    Scalettar, B.A.7
  • 143
    • 0035112321 scopus 로고    scopus 로고
    • Total internal reflection with fluorescence correlation spectroscopy: Combined surface reaction and solution diffusion
    • Starr T.E., and Thompson N.L. Total internal reflection with fluorescence correlation spectroscopy: Combined surface reaction and solution diffusion. Biophys. J. 80 (2001) 1575-1584
    • (2001) Biophys. J. , vol.80 , pp. 1575-1584
    • Starr, T.E.1    Thompson, N.L.2
  • 144
    • 0032995380 scopus 로고    scopus 로고
    • Tracking single secretory granules in live chromaffin cells by evanescent-field fluorescence microscopy
    • Steyer J.A., and Almers W. Tracking single secretory granules in live chromaffin cells by evanescent-field fluorescence microscopy. Biophys. J. 76 (1999) 2262-2271
    • (1999) Biophys. J. , vol.76 , pp. 2262-2271
    • Steyer, J.A.1    Almers, W.2
  • 145
    • 0035315984 scopus 로고    scopus 로고
    • A real-time view of life within 100 nm of the plasma membrane
    • Steyer J.A., and Almers W. A real-time view of life within 100 nm of the plasma membrane. Nat. Rev. Mol. Cell Biol. 2 (2001) 268-275
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 268-275
    • Steyer, J.A.1    Almers, W.2
  • 146
    • 0043231281 scopus 로고    scopus 로고
    • Variable-angle total internal reflection fluorescence microscopy (VA-TIRFM): Realization and application of a compact illumination device
    • Stock K., Sailer R., Strauss W.S.L., Lyttek M., Steiner R., and Schneckenburger H. Variable-angle total internal reflection fluorescence microscopy (VA-TIRFM): Realization and application of a compact illumination device. J. Microsc. Oxf. 211 (2003) 19-29
    • (2003) J. Microsc. Oxf. , vol.211 , pp. 19-29
    • Stock, K.1    Sailer, R.2    Strauss, W.S.L.3    Lyttek, M.4    Steiner, R.5    Schneckenburger, H.6
  • 147
    • 0000710582 scopus 로고
    • Evanescent field excitation of fluorescence by epi-illumination microscopy
    • Stout A.L., and Axelrod D. Evanescent field excitation of fluorescence by epi-illumination microscopy. Appl. Opt. 28 (1989) 5237-5242
    • (1989) Appl. Opt. , vol.28 , pp. 5237-5242
    • Stout, A.L.1    Axelrod, D.2
  • 148
    • 0028038109 scopus 로고
    • Reversible binding kinetics of a cytoskeletal protein at the erythrocyte submembrane
    • Stout A.L., and Axelrod D. Reversible binding kinetics of a cytoskeletal protein at the erythrocyte submembrane. Biophys. J. 67 (1994) 1324-1334
    • (1994) Biophys. J. , vol.67 , pp. 1324-1334
    • Stout, A.L.1    Axelrod, D.2
  • 149
    • 0033850088 scopus 로고    scopus 로고
    • Actin dynamics at the living cell submembrane imaged by total internal reflection fluorescence photobleaching
    • Sund S.E., and Axelrod D. Actin dynamics at the living cell submembrane imaged by total internal reflection fluorescence photobleaching. Biophys. J. 79 (2000) 1655-1669
    • (2000) Biophys. J. , vol.79 , pp. 1655-1669
    • Sund, S.E.1    Axelrod, D.2
  • 150
    • 0032866778 scopus 로고    scopus 로고
    • Cell membrane orientation visualized by polarized total internal reflection fluorescence
    • Sund S.E., Swanson J.A., and Axelrod D. Cell membrane orientation visualized by polarized total internal reflection fluorescence. Biophys. J. 77 (1999) 2266-2283
    • (1999) Biophys. J. , vol.77 , pp. 2266-2283
    • Sund, S.E.1    Swanson, J.A.2    Axelrod, D.3
  • 151
    • 2942562098 scopus 로고    scopus 로고
    • Bilayers merge even when exocytosis is transient
    • Taraska J.W., and Almers W. Bilayers merge even when exocytosis is transient. Proc. Natl. Acad. Sci. USA 101 (2004) 8780-8785
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8780-8785
    • Taraska, J.W.1    Almers, W.2
  • 152
    • 0032740355 scopus 로고    scopus 로고
    • Attachment of growth cones on substrate observed by multi-mode light microscopy
    • Tatsumi H., Katayama Y., and Sokabe M. Attachment of growth cones on substrate observed by multi-mode light microscopy. Neurosci. Res. 35 (1999) 197-206
    • (1999) Neurosci. Res. , vol.35 , pp. 197-206
    • Tatsumi, H.1    Katayama, Y.2    Sokabe, M.3
  • 153
    • 0020794259 scopus 로고
    • Immunoglobulin surface binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy
    • Thompson N.L., and Axelrod D. Immunoglobulin surface binding kinetics studied by total internal reflection with fluorescence correlation spectroscopy. Biophys. J. 43 (1983) 103-114
    • (1983) Biophys. J. , vol.43 , pp. 103-114
    • Thompson, N.L.1    Axelrod, D.2
  • 154
    • 0019366933 scopus 로고
    • Measuring surface dynamics of biomolecules by total internal reflection with photobleaching recovery or correlation spectroscopy
    • Thompson N.L., Burghardt T.P., and Axelrod D. Measuring surface dynamics of biomolecules by total internal reflection with photobleaching recovery or correlation spectroscopy. Biophys. J. 33 (1981) 435-454
    • (1981) Biophys. J. , vol.33 , pp. 435-454
    • Thompson, N.L.1    Burghardt, T.P.2    Axelrod, D.3
  • 155
    • 0021701783 scopus 로고
    • Order in supported phospholipid monolayers detected by the dichroism of fluorescence excited by polarized evanescent illumination
    • Thompson N.L., McConnell H.M., and Burghardt T.P. Order in supported phospholipid monolayers detected by the dichroism of fluorescence excited by polarized evanescent illumination. Biophys. J. 46 (1984) 739-747
    • (1984) Biophys. J. , vol.46 , pp. 739-747
    • Thompson, N.L.1    McConnell, H.M.2    Burghardt, T.P.3
  • 156
    • 0027525336 scopus 로고
    • Total internal reflection fluorescence microscopy-application to substrate-supported planar membranes
    • Thompson N.L., Pearce K.H., and Hsieh H.V. Total internal reflection fluorescence microscopy-application to substrate-supported planar membranes. Eur. Biophys. J. 22 (1993) 367-378
    • (1993) Eur. Biophys. J. , vol.22 , pp. 367-378
    • Thompson, N.L.1    Pearce, K.H.2    Hsieh, H.V.3
  • 157
    • 0025087323 scopus 로고
    • Surface diffusion of interacting proteins. Effect of concentration on the lateral mobility of adsorbed bovine serum albumin
    • Tilton R.D., Gast A.P., and Robertson C.R. Surface diffusion of interacting proteins. Effect of concentration on the lateral mobility of adsorbed bovine serum albumin. Biophys. J. 58 (1990) 1321-1326
    • (1990) Biophys. J. , vol.58 , pp. 1321-1326
    • Tilton, R.D.1    Gast, A.P.2    Robertson, C.R.3
  • 158
    • 0023705217 scopus 로고
    • Mapping of cell-glass contacts of Dictyostelium amoebae by total internal reflection aqueous fluorescence overcomes a basic ambiguity of interference reflection microscopy
    • Todd I., Mellor J.S., and Gingell D. Mapping of cell-glass contacts of Dictyostelium amoebae by total internal reflection aqueous fluorescence overcomes a basic ambiguity of interference reflection microscopy. J. Cell Sci. 89 (1988) 107-114
    • (1988) J. Cell Sci. , vol.89 , pp. 107-114
    • Todd, I.1    Mellor, J.S.2    Gingell, D.3
  • 159
    • 84884864308 scopus 로고    scopus 로고
    • Total internal reflection fluorescent microscopy
    • Celis J.E. (Ed), Elsevier Science, Elsevier Academic Press, New York Chapter 2
    • Toomre D., and Axelrod D. Total internal reflection fluorescent microscopy. In: Celis J.E. (Ed). Cell Biology: A Laboratory Handbook Vol. 3 (2005), Elsevier Science, Elsevier Academic Press, New York Chapter 2
    • (2005) Cell Biology: A Laboratory Handbook , vol.3
    • Toomre, D.1    Axelrod, D.2
  • 160
    • 0035399557 scopus 로고    scopus 로고
    • Lighting up the cell surface with evanescent wave microscopy
    • Toomre D., and Manstein D.J. Lighting up the cell surface with evanescent wave microscopy. Trends Cell Biol. 11 (2001) 298-303
    • (2001) Trends Cell Biol. , vol.11 , pp. 298-303
    • Toomre, D.1    Manstein, D.J.2
  • 161
    • 0034599547 scopus 로고    scopus 로고
    • Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy
    • Toomre D., Steyer J.A., Keller P., Almers W., and Simons K. Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy. J. Cell Biol. 149 (2000) 33-40
    • (2000) J. Cell Biol. , vol.149 , pp. 33-40
    • Toomre, D.1    Steyer, J.A.2    Keller, P.3    Almers, W.4    Simons, K.5
  • 163
    • 33645220584 scopus 로고    scopus 로고
    • Atomic force-multi-optical imaging integrated microscope for monitoring molecular dynamics in live cells
    • Trache A., and Meininger G.A. Atomic force-multi-optical imaging integrated microscope for monitoring molecular dynamics in live cells. J. Biomed. Opt. 10 (2005) 064023
    • (2005) J. Biomed. Opt. , vol.10 , pp. 064023
    • Trache, A.1    Meininger, G.A.2
  • 164
    • 0034804586 scopus 로고    scopus 로고
    • Protein kinase C-dependent supply of secretory granules to the plasma membrane
    • Tsuboi T., Kikuta T., Warashina A., and Terakawa S. Protein kinase C-dependent supply of secretory granules to the plasma membrane. Biochem. Biophys. Res. Commun. 282 (2001) 621-628
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 621-628
    • Tsuboi, T.1    Kikuta, T.2    Warashina, A.3    Terakawa, S.4
  • 165
    • 0037013208 scopus 로고    scopus 로고
    • Sweeping model of dynamin activity-Visualization of coupling between exocytosis and endocytosis under an evanescent wave microscope with green fluorescent proteins
    • Tsuboi T., Terakawa S., Scalettar B.A., Fantus C., Roder J., and Jeromin A. Sweeping model of dynamin activity-Visualization of coupling between exocytosis and endocytosis under an evanescent wave microscope with green fluorescent proteins. J. Biol. Chem. 277 (2002) 15957-15961
    • (2002) J. Biol. Chem. , vol.277 , pp. 15957-15961
    • Tsuboi, T.1    Terakawa, S.2    Scalettar, B.A.3    Fantus, C.4    Roder, J.5    Jeromin, A.6
  • 166
    • 0034687214 scopus 로고    scopus 로고
    • Simultaneous evanescent wave imaging of insulin vesicle membrane and cargo during a single exocytotic event
    • Tsuboi T., Zhao C., Terakawa S., and Rutter G.A. Simultaneous evanescent wave imaging of insulin vesicle membrane and cargo during a single exocytotic event. Curr. Biol. 10 (2000) 1307-1310
    • (2000) Curr. Biol. , vol.10 , pp. 1307-1310
    • Tsuboi, T.1    Zhao, C.2    Terakawa, S.3    Rutter, G.A.4
  • 167
    • 0009234279 scopus 로고
    • Fluorescence of chlorophyll alpha in monolayers
    • Tweet A.G., Gaines G.L., and Bellamy W.D. Fluorescence of chlorophyll alpha in monolayers. J. Chem. Phys. 40 (1964) 2596-2600
    • (1964) J. Chem. Phys. , vol.40 , pp. 2596-2600
    • Tweet, A.G.1    Gaines, G.L.2    Bellamy, W.D.3
  • 168
    • 0029879228 scopus 로고    scopus 로고
    • Direct observation of single kinesin molecules moving along microtubules
    • Vale R.D., Funatsu T., Pierce D.W., Romberg L., Harada Y., and Yanagida T. Direct observation of single kinesin molecules moving along microtubules. Nature 380 (1996) 451-453
    • (1996) Nature , vol.380 , pp. 451-453
    • Vale, R.D.1    Funatsu, T.2    Pierce, D.W.3    Romberg, L.4    Harada, Y.5    Yanagida, T.6
  • 169
    • 0023921894 scopus 로고
    • Polarized fluorescence photobleaching recovery for measuring rotational diffusion in solutions and membranes
    • Velez M., and Axelrod D. Polarized fluorescence photobleaching recovery for measuring rotational diffusion in solutions and membranes. Biophys. J. 53 (1988) 575-591
    • (1988) Biophys. J. , vol.53 , pp. 575-591
    • Velez, M.1    Axelrod, D.2
  • 170
    • 0037328047 scopus 로고    scopus 로고
    • A prism combination for near isotropic fluorescence excitation by total internal reflection
    • Wakelin S., and Bagshaw C.R. A prism combination for near isotropic fluorescence excitation by total internal reflection. J. Microsc. Oxf. 209 (2003) 143-148
    • (2003) J. Microsc. Oxf. , vol.209 , pp. 143-148
    • Wakelin, S.1    Bagshaw, C.R.2
  • 171
    • 2442533907 scopus 로고    scopus 로고
    • A new method for determining dipole moment orientation of single molecules
    • Wang C., Liu L., Wang G.Y., and Xu Z.Z. A new method for determining dipole moment orientation of single molecules. Chinese Phys. Lett. 21 (2004) 843-845
    • (2004) Chinese Phys. Lett. , vol.21 , pp. 843-845
    • Wang, C.1    Liu, L.2    Wang, G.Y.3    Xu, Z.Z.4
  • 172
    • 0028169684 scopus 로고
    • Time-lapse total internal reflection fluorescence video of acetylcholine receptor cluster formation on myotubes
    • Wang M.D., and Axelrod D. Time-lapse total internal reflection fluorescence video of acetylcholine receptor cluster formation on myotubes. Dev. Dyn. 201 (1994) 29-40
    • (1994) Dev. Dyn. , vol.201 , pp. 29-40
    • Wang, M.D.1    Axelrod, D.2
  • 173
    • 33747140741 scopus 로고    scopus 로고
    • Imaging of dynamic secretory vesicles in living pollen tubes of Picea meyeri using evanescent wave microscopy
    • Wang X.H., Teng Y., Wang Q.L., Li X.J., Sheng X.Y., Zheng M.Z., Samaj J., Baluska F., and Lin J.X. Imaging of dynamic secretory vesicles in living pollen tubes of Picea meyeri using evanescent wave microscopy. Plant Physiol. 141 (2006) 1591-1603
    • (2006) Plant Physiol. , vol.141 , pp. 1591-1603
    • Wang, X.H.1    Teng, Y.2    Wang, Q.L.3    Li, X.J.4    Sheng, X.Y.5    Zheng, M.Z.6    Samaj, J.7    Baluska, F.8    Lin, J.X.9
  • 174
    • 0017557557 scopus 로고
    • Total internal reflection fluorescence technique for the study of protein adsorption
    • Watkins R.W., and Robertson C.R. Total internal reflection fluorescence technique for the study of protein adsorption. J. Biomed. Mater. Res. 11 (1977) 915-938
    • (1977) J. Biomed. Mater. Res. , vol.11 , pp. 915-938
    • Watkins, R.W.1    Robertson, C.R.2
  • 175
    • 23944503359 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in single molecule nanobioscience
    • Wazawa T., and Ueda M. Total internal reflection fluorescence microscopy in single molecule nanobioscience. Adv. Biochem. Eng. Biotechnol. 95 (2005) 77-106
    • (2005) Adv. Biochem. Eng. Biotechnol. , vol.95 , pp. 77-106
    • Wazawa, T.1    Ueda, M.2
  • 176
    • 0020316252 scopus 로고
    • Stimulation of fluorescence in a small contact region between rat basophile leukemia cells and planar lipid membrane targets by coherent evanescent radiation
    • Weis R.M., Balakrishnan K., Smith B., and McConnell H.M. Stimulation of fluorescence in a small contact region between rat basophile leukemia cells and planar lipid membrane targets by coherent evanescent radiation. J. Biol. Chem. 257 (1982) 6440-6445
    • (1982) J. Biol. Chem. , vol.257 , pp. 6440-6445
    • Weis, R.M.1    Balakrishnan, K.2    Smith, B.3    McConnell, H.M.4
  • 177
    • 0037567239 scopus 로고    scopus 로고
    • New and versatile optical-immunoassay instrumentation for water monitoring
    • Willard D., Proll G., Reder S., and Gauglitz G. New and versatile optical-immunoassay instrumentation for water monitoring. Environ. Sci. Pollut. Res. 10 (2003) 188-191
    • (2003) Environ. Sci. Pollut. Res. , vol.10 , pp. 188-191
    • Willard, D.1    Proll, G.2    Reder, S.3    Gauglitz, G.4
  • 178
    • 3042691206 scopus 로고    scopus 로고
    • High sensitivity detection of protein molecules picked up on a probe of atomic force microscope based on the fluorescence detection by a total internal reflection fluorescence microscope
    • Yamada T., Afrin R., Arakawa H., and Ikai A. High sensitivity detection of protein molecules picked up on a probe of atomic force microscope based on the fluorescence detection by a total internal reflection fluorescence microscope. FEBS Lett. 569 (2004) 59-64
    • (2004) FEBS Lett. , vol.569 , pp. 59-64
    • Yamada, T.1    Afrin, R.2    Arakawa, H.3    Ikai, A.4
  • 180
    • 33846099490 scopus 로고    scopus 로고
    • Fibronectin matrix assembly requires distinct contributions from rho kinases I and II
    • Yoneda A., Ushakov D., Multhaupt H.A.B., and Couchman J.R. Fibronectin matrix assembly requires distinct contributions from rho kinases I and II. Mol. Biol. Cell 18 (2007) 66-75
    • (2007) Mol. Biol. Cell , vol.18 , pp. 66-75
    • Yoneda, A.1    Ushakov, D.2    Multhaupt, H.A.B.3    Couchman, J.R.4
  • 181
    • 0022748104 scopus 로고
    • Protein rotational motion in solution measured by polarized fluorescence depletion
    • Yoshida T.M., and Barisas B.G. Protein rotational motion in solution measured by polarized fluorescence depletion. Biophys. J. 50 (1986) 41-53
    • (1986) Biophys. J. , vol.50 , pp. 41-53
    • Yoshida, T.M.1    Barisas, B.G.2
  • 182
    • 0029135025 scopus 로고
    • Subnanosecond polarized fluorescence photobleaching: Rotational diffusion of acetylcholine receptors on developing muscle cells
    • Yuan Y., and Axelrod D. Subnanosecond polarized fluorescence photobleaching: Rotational diffusion of acetylcholine receptors on developing muscle cells. Biophys. J. 69 (1995) 690-700
    • (1995) Biophys. J. , vol.69 , pp. 690-700
    • Yuan, Y.1    Axelrod, D.2
  • 183
    • 33845580046 scopus 로고    scopus 로고
    • Surface-plasmon microscopy with a two-piece solid immersion lens: Bright and dark fields
    • Zhang J., Pitter M.C., Liu S.G., See C., and Somekh M.G. Surface-plasmon microscopy with a two-piece solid immersion lens: Bright and dark fields. Appl. Opt. 45 (2006) 7977-7986
    • (2006) Appl. Opt. , vol.45 , pp. 7977-7986
    • Zhang, J.1    Pitter, M.C.2    Liu, S.G.3    See, C.4    Somekh, M.G.5


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