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Volumn , Issue SUPPL. 10, 2008, Pages

Total Internal Reflection Fluorescence (TIRF) microscopy

Author keywords

Total internal reflection fluorescence microscopy

Indexed keywords

CLATHRIN; NEF PROTEIN; FLUORESCENT DYE;

EID: 51549109001     PISSN: 19348525     EISSN: 19348533     Source Type: Journal    
DOI: 10.1002/9780471729259.mc02a02s10     Document Type: Review
Times cited : (34)

References (46)
  • 1
    • 7944222012 scopus 로고    scopus 로고
    • Signal analysis of total internal reflection fluorescent speckle microscopy (TIR-FSM) and wide-field epifluorescence 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. 2004. Signal analysis of total internal reflection fluorescent speckle microscopy (TIR-FSM) and wide-field epifluorescence FSM of the actin cytoskeleton and focal adhesions in living cells. J. Microsc. 216:138-152.
    • (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
  • 2
    • 0002454697 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy
    • In (A. Periasamy, ed.) American Physiological Society, Bethesda, Md
    • Axelrod, D. 2001a. Total internal reflection fluorescence microscopy. In Methods in Cellular Imaging (A. Periasamy, ed.) pp. 362-380. American Physiological Society, Bethesda, Md.
    • (2001) Methods in Cellular Imaging , pp. 362-380
    • Axelrod, D.1
  • 3
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • Axelrod, D. 2001b. Total internal reflection fluorescence microscopy in cell biology. Traffic 2:764-774.
    • (2001) Traffic , vol.2 , pp. 764-774
    • Axelrod, D.1
  • 4
    • 0034745197 scopus 로고    scopus 로고
    • Selective imaging of surface fluorescence with very high aperture microscope objectives
    • Axelrod, D. 2001c. Selective imaging of surface fluorescence with very high aperture microscope objectives. J. Biomed. Opt. 6:6-13.
    • (2001) J. Biomed. Opt. , vol.6 , pp. 6-13
    • Axelrod, D.1
  • 5
    • 0020659058 scopus 로고
    • Total internal reflection fluorescent microscopy
    • Axelrod, D., Thompson, N.L., and Burghardt, T.P. 1983. Total internal reflection fluorescent microscopy. J Microsc. 129:19-28.
    • (1983) J Microsc. , vol.129 , pp. 19-28
    • Axelrod, D.1    Thompson, N.L.2    Burghardt, T.P.3
  • 7
    • 9544221857 scopus 로고
    • Adsorption kinetics on biological membranes: Measurements by total internal reflection fluorescence
    • (L. Taylor, A.S. Waggoner, R.F. Murphy, F. Lanni, and R.R. Birge, eds.) A.R. Liss, New York
    • Axelrod, D., Fulbright, R.M., and Hellen, E.H. 1986. Adsorption kinetics on biological membranes: Measurements by total internal reflection fluorescence. In Applications of Fluorescence in Biomedical Sciences (L. Taylor, A.S. Waggoner, R.F. Murphy, F. Lanni, and R.R. Birge, eds.) pp. 461-476. A.R. Liss, New York.
    • (1986) In Applications of Fluorescence in Biomedical Sciences , pp. 461-476
    • Axelrod, D.1    Fulbright, R.M.2    Hellen, E.H.3
  • 8
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J.S. and Traub, L.M. 2003. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 9
    • 0028003419 scopus 로고
    • Imaging of cell/substrate contacts on polymers by total internal reflection fluorescence microscopy
    • Burmeister, J.S., Truskey, G.A., Yarbrough, J.L., and Reichert, W.M. 1994. Imaging of cell/substrate contacts on polymers by total internal reflection fluorescence microscopy. Biotechnol. Prog. 10:26-31.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 26-31
    • Burmeister, J.S.1    Truskey, G.A.2    Yarbrough, J.L.3    Reichert, W.M.4
  • 10
    • 0032029808 scopus 로고    scopus 로고
    • Application of total internal reflection fluorescence microscopy to study cell adhesion to biomaterials
    • Burmeister, J.S., Olivier, L.A., Truskey, G.A., and Reichert, W.M. 1998. Application of total internal reflection fluorescence microscopy to study cell adhesion to biomaterials. Biomaterials 19:307-325.
    • (1998) Biomaterials , vol.19 , pp. 307-325
    • Burmeister, J.S.1    Olivier, L.A.2    Truskey, G.A.3    Reichert, W.M.4
  • 12
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner, S.F. and Schmid, S.L. 2003. Regulated portals of entry into the cell. Nature 422:37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.F.1    Schmid, S.L.2
  • 13
    • 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. 2004. Imaging the activity and localization of single voltage-gated Ca2+ channels by total internal reflection fluorescence microscopy. Biophys. J. 86:3250-3259.
    • (2004) Biophys. J. , vol.86 , pp. 3250-3259
    • Demuro, A.1    Parker, I.2
  • 15
    • 15944425187 scopus 로고
    • Dynamics of nonspecific adsorption of insulin to erythrocyte membranes
    • Fulbright, R.M. and Axelrod, D. 1993. Dynamics of nonspecific adsorption of insulin to erythrocyte membranes. J. Fluoresc. 3:1-16.
    • (1993) J. Fluoresc. , vol.3 , pp. 1-16
    • Fulbright, R.M.1    Axelrod, D.2
  • 16
    • 7744246474 scopus 로고    scopus 로고
    • Uptake pathway of polyomavirus via ganglioside GD1a
    • Gilbert, J. and Benjamin, T. 2004. Uptake pathway of polyomavirus via ganglioside GD1a. J. Virol. 78:12259-12267.
    • (2004) J. Virol. , vol.78 , pp. 12259-12267
    • Gilbert, J.1    Benjamin, T.2
  • 17
    • 17044447869 scopus 로고
    • General electromagnetic theory of total internal reflection fluorescence: The quantitative basis for mapping cell-substratum topography
    • Gingell, D., Heavens, O.S., and Mellor, J.S. 1987. General electromagnetic theory of total internal reflection fluorescence: The quantitative basis for mapping cell-substratum topography. Cell Sci. 87:677-693.
    • (1987) Cell Sci. , vol.87 , pp. 677-693
    • Gingell, D.1    Heavens, O.S.2    Mellor, J.S.3
  • 18
    • 0035105080 scopus 로고    scopus 로고
    • Coupling of antibodies via protein Z on modified polyoma virus - Like particles
    • Gleiter, S. and Lilie, H. 2001. Coupling of antibodies via protein Z on modified polyoma virus - like particles. Protein Sci. 10:434-444.
    • (2001) Protein Sci. , vol.10 , pp. 434-444
    • Gleiter, S.1    Lilie, H.2
  • 19
    • 0001452103 scopus 로고
    • Total reflection fluorescence (TRF)
    • Hirschfeld, T. 1965. Total reflection fluorescence (TRF). Can. Spectrosc. 10:128.
    • (1965) Can. Spectrosc. , vol.10 , pp. 128
    • Hirschfeld, T.1
  • 20
    • 17444366080 scopus 로고    scopus 로고
    • Simultaneous, coincident optical trapping and single-molecule fluorescence
    • Lang, M.J., Fordyce, P.M., Engh, A.M., Neuman, K.C., and Block, S.M. 2004. Simultaneous, coincident optical trapping and single-molecule fluorescence. Nat. Methods 1:133-139.
    • (2004) Nat. Methods , vol.1 , pp. 133-139
    • Lang, M.J.1    Fordyce, P.M.2    Engh, A.M.3    Neuman, K.C.4    Block, S.M.5
  • 21
    • 0242385316 scopus 로고    scopus 로고
    • Ligand-receptor kinetics by total internal reflectionwith fluorescence correlation spectroscopy
    • Lieto, A.M., Randall, C.C., and Thompson, N.L. 2003. Ligand-receptor kinetics by total internal reflectionwith fluorescence correlation spectroscopy. Biophys. J. 85:3294-3302.
    • (2003) Biophys. J. , vol.85 , pp. 3294-3302
    • Lieto, A.M.1    Randall, C.C.2    Thompson, N.L.3
  • 22
    • 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. 2000. Atomic force and total internal reflection fluorescence microscopy for the study of force transmission in endothelial cells. Biophys. J. 78:1725-1735.
    • (2000) Biophys. J. , vol.78 , pp. 1725-1735
    • Mathur, A.B.1    Truskey, G.A.2    Reichert, W.M.3
  • 24
    • 0024467376 scopus 로고
    • Evanscent detection of absorbed films: Assessment of optical considerations for absorbance and fluorescence spectroscopy at the crystal/solution and polymer/solution interfaces
    • Reichert, W.M. 1989. Evanscent detection of absorbed films: Assessment of optical considerations for absorbance and fluorescence spectroscopy at the crystal/solution and polymer/solution interfaces. Crit. Rev. Biocompat. 5:173-205.
    • (1989) Crit. Rev. Biocompat. , vol.5 , pp. 173-205
    • Reichert, W.M.1
  • 25
    • 0025330761 scopus 로고
    • Total internal reflection fluorescence (TIRF) microscopy. I. Modeling cell contact region fluorescence
    • Reichert,W.M. and Truskey, G.A. 1990. Total internal reflection fluorescence (TIRF) microscopy. I. Modeling cell contact region fluorescence. J. Cell Sci. 96:219-230.
    • (1990) J. Cell Sci. , vol.96 , pp. 219-230
    • Reichert, W.M.1    Truskey, G.A.2
  • 27
    • 0016800090 scopus 로고
    • A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase
    • Sanger, F. and Coulson, A.R. 1975. A rapid method for determining sequences in DNA by primed synthesis with DNA polymerase. J. Mol. Biol. 94:441-448.
    • (1975) J. Mol. Biol. , vol.94 , pp. 441-448
    • Sanger, F.1    Coulson, A.R.2
  • 28
    • 23044515069 scopus 로고    scopus 로고
    • Feature point tracking and trajectory analysis for video imaging in cell biology
    • Sbalzarini, I.F. and Koumoutsakos, P. 2005. Feature point tracking and trajectory analysis for video imaging in cell biology. J. Struct. Biol. 151:182-195.
    • (2005) J. Struct. Biol. , vol.151 , pp. 182-195
    • Sbalzarini, I.F.1    Koumoutsakos, P.2
  • 29
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection fluorescence microscopy
    • Schmoranzer, J., Goulian, M., Axelrod, D., and Simon, S.M. 2000. Imaging constitutive exocytosis with total internal reflection fluorescence microscopy. J. Cell Biol. 149:23-31.
    • (2000) J. Cell Biol. , vol.149 , pp. 23-31
    • Schmoranzer, J.1    Goulian, M.2    Axelrod, D.3    Simon, S.M.4
  • 30
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • Seong, J.A. and Almers,W. 2004. Tracking SNARE complex formation in live endocrine cells. Science 306:1042-1046.
    • (2004) Science , vol.306 , pp. 1042-1046
    • Seong, J.A.1    Almers, W.2
  • 31
    • 0028303852 scopus 로고
    • Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment
    • Stehle, T., Yan, Y., Benjamin, T.L., and Harrison, S.C. 1994. Structure of murine polyomavirus complexed with an oligosaccharide receptor fragment. Nature 369:160-163.
    • (1994) Nature , vol.369 , pp. 160-163
    • Stehle, T.1    Yan, Y.2    Benjamin, T.L.3    Harrison, S.C.4
  • 32
    • 0000710582 scopus 로고
    • Evanescent field excitation of fluorescence by epi-illumination microscopy
    • Stout, A.L. and Axelrod, D. 1989. Evanescent field excitation of fluorescence by epi-illumination microscopy. Appl. Optics 28:5237-5242.
    • (1989) Appl. Optics , vol.28 , pp. 5237-5242
    • Stout, A.L.1    Axelrod, D.2
  • 33
    • 0032866778 scopus 로고    scopus 로고
    • Cell membrane orientation visualized by polarized total internal reflection fluorescence
    • Sund, S.E., Swanson, J., and Axelrod, D. 1999. Cell membrane orientation visualized by polarized total internal reflection fluorescence. Biophys. J. 77:2266-2283.
    • (1999) Biophys. J. , vol.77 , pp. 2266-2283
    • Sund, S.E.1    Swanson, J.2    Axelrod, D.3
  • 34
    • 0019606838 scopus 로고
    • Total internal reflection microscopy: A surface inspection technique
    • Temple, P. 1981. Total internal reflection microscopy: A surface inspection technique. Appl. Optics 20:2656-2664.
    • (1981) Appl. Optics , vol.20 , pp. 2656-2664
    • Temple, P.1
  • 36
    • 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. 2000. Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy. J. Cell Biol. 149:33-40.
    • (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
  • 37
    • 33645220584 scopus 로고    scopus 로고
    • An atomic force - Multi optical imaging integrated microscope for monitoring molecular dynamics in live cells
    • 064023
    • Trache, A. and Meininger, G.A. 2005. An atomic force - multi optical imaging integrated microscope for monitoring molecular dynamics in live cells. J. Biomed. Opt. 10:064023:1-17.
    • (2005) J. Biomed. Opt. , vol.10 , pp. 1-17
    • Trache, A.1    Meininger, G.A.2
  • 38
    • 0026437513 scopus 로고
    • Total internal reflection fluorescence microscopy (TIRFM). II. Topographical mapping of relative cell/substratum separation distances
    • Truskey, G.A., Burmeister, J.S., Grapa, E., and Reichert, W.M. 1992. Total internal reflection fluorescence microscopy (TIRFM). II. Topographical mapping of relative cell/substratum separation distances. J. Cell Sci. 103:491-499.
    • (1992) J. Cell Sci. , vol.103 , pp. 491-499
    • Truskey, G.A.1    Burmeister, J.S.2    Grapa, E.3    Reichert, W.M.4
  • 40
    • 0028314370 scopus 로고
    • DNA fingerprinting of medically important microorganisms by use of PCR
    • van Belkum, A. 1994. DNA fingerprinting of medically important microorganisms by use of PCR. Clin. Microbiol. Rev. 7:174-184.
    • (1994) Clin. Microbiol. Rev. , vol.7 , pp. 174-184
    • van Belkum, A.1
  • 41
    • 0037731315 scopus 로고    scopus 로고
    • Combined single-molecule force and fluorescence measurements for biology
    • Wallace, M.I., Molloy, J.E., and Trentham, D.R. 2003. Combined single-molecule force and fluorescence measurements for biology. J. Biol. 2(1): 4.
    • (2003) J. Biol. , vol.2 , Issue.1 , pp. 4
    • Wallace, M.I.1    Molloy, J.E.2    Trentham, D.R.3
  • 42
    • 0028169684 scopus 로고
    • Time-lapse total internal reflection fluorescence video of acetylcholine receptor cluster formation on myotubes
    • Wang, M.D. and Axelrod, D. 1994. Time-lapse total internal reflection fluorescence video of acetylcholine receptor cluster formation on myotubes. Dev. Dynam. 201:29-40.
    • (1994) Dev. Dynam. , vol.201 , pp. 29-40
    • Wang, M.D.1    Axelrod, D.2
  • 43
    • 0020121742 scopus 로고
    • The morphologic pathway of exocytosis of the vesicular somatitis virus G protein in cultured fibrolasts
    • Wehland, J., Willingham, M.C., Gallo, M.G., and Pastan, I. 1982. The morphologic pathway of exocytosis of the vesicular somatitis virus G protein in cultured fibrolasts. Cell 28:831-841.
    • (1982) Cell , vol.28 , pp. 831-841
    • Wehland, J.1    Willingham, M.C.2    Gallo, M.G.3    Pastan, I.4
  • 44
    • 0030924693 scopus 로고    scopus 로고
    • Multiple-complete-digest restriction fragment mapping: Generating sequence-ready maps for large scale DNA sequencing
    • Wong, G.K., Yu, J., Thayer, E.C., and Olson, M.V. 1997. Multiple-complete-digest restriction fragment mapping: Generating sequence-ready maps for large scale DNA sequencing. Proc. Natl. Acad. Sci. U.S.A. 94:5225-5230.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 5225-5230
    • Wong, G.K.1    Yu, J.2    Thayer, E.C.3    Olson, M.V.4
  • 46
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5 nm localization
    • Yildiz, A., Forkey, J.N., McKinney, S.A., Ha, T., Goldman, Y.E., and Selvin, P.R. 2003. Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5 nm localization. Science 300:2061-2065.
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6


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