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Volumn 91, Issue 7, 2006, Pages 2626-2635

Application of surface plasmon coupled emission to study of muscle

Author keywords

[No Author keywords available]

Indexed keywords

GOLD; METAL;

EID: 33747779635     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.088369     Document Type: Article
Times cited : (80)

References (52)
  • 1
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • Minton, A. P. 1998. Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion. Methods Enzymol. 295:127-149.
    • (1998) Methods Enzymol , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 3
  • 4
    • 0031806323 scopus 로고    scopus 로고
    • Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers
    • Hopkins, S. C., C. Sabido-David, J. E. Corrie, M. Irving, and Y. E. Goldman. 1998. Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers. Biophys. J. 74:3093-3110.
    • (1998) Biophys. J. , vol.74 , pp. 3093-3110
    • Hopkins, S.C.1    Sabido-David, C.2    Corrie, J.E.3    Irving, M.4    Goldman, Y.E.5
  • 5
    • 0037382351 scopus 로고    scopus 로고
    • Orientational changes of cross-bridges during single turnover of ATP
    • Borejdo, J., and I. Akopova. 2003. Orientational changes of cross-bridges during single turnover of ATP. Biophys. J. 84:2450-2459.
    • (2003) Biophys. J. , vol.84 , pp. 2450-2459
    • Borejdo, J.1    Akopova, I.2
  • 6
    • 10044295196 scopus 로고    scopus 로고
    • Rotation of the lever-arm of myosin in contracting skeletal muscle fiber measured by two-photon anisotropy
    • Borejdo, J., A. A. Shepard, I. Akopova, W. Grudzinski, and J. Malicka. 2004. Rotation of the lever-arm of myosin in contracting skeletal muscle fiber measured by two-photon anisotropy. Biophys. J. 87:3912-3921.
    • (2004) Biophys. J. , vol.87 , pp. 3912-3921
    • Borejdo, J.1    Shepard, A.A.2    Akopova, I.3    Grudzinski, W.4    Malicka, J.5
  • 7
    • 0028229903 scopus 로고
    • Sorting single molecules: Application to diagnostics and evolutionary biotechnology
    • Eigen, M., and R. Rigler. 1994. Sorting single molecules: application to diagnostics and evolutionary biotechnology. Proc. Natl. Acad. Sci. USA. 91:5740-5747.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 8
  • 9
    • 22144456458 scopus 로고    scopus 로고
    • High spatial resolution observation of single-molecule dynamics in living cell membranes
    • Edel, J. B., M. Wu, B. Baird, and H. G. Craighead. 2005. High spatial resolution observation of single-molecule dynamics in living cell membranes. Biophys J. 88:L43-L45.
    • (2005) Biophys J. , vol.88
    • Edel, J.B.1    Wu, M.2    Baird, B.3    Craighead, H.G.4
  • 10
    • 0000627596 scopus 로고    scopus 로고
    • Scanning near-field optical microscopy with aperture probes: Fundamentals and applications
    • Hecht, B., B. Sick, U. P. Wild, V. Deckert, R. Zenobi, O. J. F. Martin, and D.W. Pohl. 2000. Scanning near-field optical microscopy with aperture probes: Fundamentals and applications. J. Chem. Phys. 112:7761-7774.
    • (2000) J. Chem. Phys. , vol.112 , pp. 7761-7774
    • Hecht, B.1    Sick, B.2    Wild, U.P.3    Deckert, V.4    Zenobi, R.5    Martin, O.J.F.6    Pohl, D.W.7
  • 11
    • 0000209278 scopus 로고    scopus 로고
    • Near-field scanning optical microscopy
    • Dunn, R. C. 1999. Near-field scanning optical microscopy. Chem. Rev. 99:2891-2927.
    • (1999) Chem. Rev. , vol.99 , pp. 2891-2927
    • Dunn, R.C.1
  • 12
    • 0027698450 scopus 로고
    • Single molecules observed by near field scanning optical microscopy
    • Betzig, E., and R. J. Chichester. 1993. Single molecules observed by near field scanning optical microscopy. Science. 262:1422-1425.
    • (1993) Science , vol.262 , pp. 1422-1425
    • Betzig, E.1    Chichester, R.J.2
  • 13
    • 1942484551 scopus 로고    scopus 로고
    • The essential light chains 1 and 3 rotate differently during muscle contraction
    • (Abstr.)
    • Borejdo, J., D. S. Ushakov, and I. Akopova. 2002. The essential light chains 1 and 3 rotate differently during muscle contraction. Biophys. J. 82:362a. (Abstr.)
    • (2002) Biophys. J. , vol.82
    • Borejdo, J.1    Ushakov, D.S.2    Akopova, I.3
  • 14
    • 33644982036 scopus 로고    scopus 로고
    • Rotations of a few cross-bridges in muscle by confocal total internal reflection microscopy
    • Borejdo, J., J. Talent, I. Akopova, and T. P. Burghardt. 2006. Rotations of a few cross-bridges in muscle by confocal total internal reflection microscopy. Biochim. Biophys. Acta. 1763:137-140.
    • (2006) Biochim. Biophys. Acta. , vol.1763 , pp. 137-140
    • Borejdo, J.1    Talent, J.2    Akopova, I.3    Burghardt, T.P.4
  • 15
    • 1642588184 scopus 로고    scopus 로고
    • Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy
    • Ruckstuhl, T., and S. Seeger. 2004. Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy. Optic Lett. 29:569-571.
    • (2004) Optic Lett. , vol.29 , pp. 569-571
    • Ruckstuhl, T.1    Seeger, S.2
  • 18
    • 3242783234 scopus 로고    scopus 로고
    • Attomolar sensitivity in bioessays based on Surface Plasmon Fluorescence Spectroscopy
    • Yu, F., B. Persson, S. Lofas, and W. Knoll. 2004. Attomolar sensitivity in bioessays based on Surface Plasmon Fluorescence Spectroscopy. J. Am. Chem. Soc. 126:8902-8903.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8902-8903
    • Yu, F.1    Persson, B.2    Lofas, S.3    Knoll, W.4
  • 21
    • 33744822157 scopus 로고    scopus 로고
    • In situ fluorescent protein imaging with metal film enhanced total internal reflection microscopy
    • Burghardt, T. P., J. E. Charlesworth, M. F. Halsetad, J. E. Tarara, and K. Ajtai. 2006. In situ fluorescent protein imaging with metal film enhanced total internal reflection microscopy. Biophys. J. 90:4662-4671.
    • (2006) Biophys. J. , vol.90 , pp. 4662-4671
    • Burghardt, T.P.1    Charlesworth, J.E.2    Halsetad, M.F.3    Tarara, J.E.4    Ajtai, K.5
  • 22
    • 27544478136 scopus 로고    scopus 로고
    • The efficiency of surface-plasmon coupled emission for sensitive fluorescence detection
    • Enderlein, J., and T. Ruckstuhl. 2005. The efficiency of surface-plasmon coupled emission for sensitive fluorescence detection. Opt. Express. 13:8855-8865.
    • (2005) Opt. Express. , vol.13 , pp. 8855-8865
    • Enderlein, J.1    Ruckstuhl, T.2
  • 23
    • 7644240095 scopus 로고    scopus 로고
    • Myoglobin immunoassay utilizing directional surface plasmon-coupled emission
    • Matveeva, E., Z. Gryczynski, I. Gryczynski, J. Malicka, and J. R. Lakowicz. 2004. Myoglobin immunoassay utilizing directional surface plasmon-coupled emission. Anal. Chem. 76:6287-6292.
    • (2004) Anal. Chem. , vol.76 , pp. 6287-6292
    • Matveeva, E.1    Gryczynski, Z.2    Gryczynski, I.3    Malicka, J.4    Lakowicz, J.R.5
  • 24
    • 10944228204 scopus 로고    scopus 로고
    • Surface plasmon-coupled ultraviolet emission of 2,5-diphenyl-1,3,4- oxadiazole
    • Malicka, J., I. Gryczynski, Z. Gryczynski, and J. R. Lakowicz. 2004. Surface plasmon-coupled ultraviolet emission of 2,5-diphenyl-1,3,4-oxadiazole. J. Phys. Chem. B. 108:19114-19118.
    • (2004) J. Phys. Chem. B. , vol.108 , pp. 19114-19118
    • Malicka, J.1    Gryczynski, I.2    Gryczynski, Z.3    Lakowicz, J.R.4
  • 26
    • 0020327766 scopus 로고
    • Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore
    • Borejdo, J., O. Assulin, T. Ando, and S. Putnam. 1982. Cross-bridge orientation in skeletal muscle measured by linear dichroism of an extrinsic chromophore. J. Mol. Biol. 158:391-414.
    • (1982) J. Mol. Biol. , vol.158 , pp. 391-414
    • Borejdo, J.1    Assulin, O.2    Ando, T.3    Putnam, S.4
  • 27
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • Harada, Y., K. Sakurada, T. Aoki, D. D. Thomas, and T. Yanagida. 1990. Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216:49-68.
    • (1990) J. Mol. Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 29
    • 0346278794 scopus 로고    scopus 로고
    • Radiative decay engineering 4. Experimental studies of surface plasmon-coupled directional emission
    • Gryczynski, I., J. Malicka, Z. Gryczynski, and J. R. Lakowicz. 2004. Radiative decay engineering 4. Experimental studies of surface plasmon-coupled directional emission. Anal. Biochem. 324:170-182.
    • (2004) Anal. Biochem. , vol.324 , pp. 170-182
    • Gryczynski, I.1    Malicka, J.2    Gryczynski, Z.3    Lakowicz, J.R.4
  • 30
    • 0024490584 scopus 로고
    • Total internal reflection fluorescence microscopy
    • Axelrod, D. 1989. Total internal reflection fluorescence microscopy. Methods Cell Biol. 30:245-270.
    • (1989) Methods Cell Biol. , vol.30 , pp. 245-270
    • Axelrod, D.1
  • 31
    • 23844501274 scopus 로고    scopus 로고
    • Surface plasmon-coupled emission and Fabry-Perot resonance in the sample layer: A theoretical approach
    • Calander, N. 2005. Surface plasmon-coupled emission and Fabry-Perot resonance in the sample layer: A theoretical approach. J. Phys. Chem. B. 109:13957-13963.
    • (2005) J. Phys. Chem. B. , vol.109 , pp. 13957-13963
    • Calander, N.1
  • 32
    • 85030609253 scopus 로고    scopus 로고
    • TFC-Calc. Software Spectra, Portland, OR
    • TFC-Calc. Optical Coating Design Software. Software Spectra, Portland, OR.
    • Optical Coating Design Software
  • 33
    • 0028811462 scopus 로고
    • Phalloidin unzips nebulin from thin filaments in skeletal myofibrils
    • Ao, X., and S. S. Lehrer. 1995. Phalloidin unzips nebulin from thin filaments in skeletal myofibrils. J. Cell Sci. 108:3397-3403.
    • (1995) J. Cell Sci. , vol.108 , pp. 3397-3403
    • Ao, X.1    Lehrer, S.S.2
  • 35
    • 84975602255 scopus 로고
    • Energy transfer from an excited dye molecule to the surface plasmons of an adjacent metal
    • Weber, W. H., and C. F. Eagen. 1979. Energy transfer from an excited dye molecule to the surface plasmons of an adjacent metal. Opt. Lett. 4:236-238.
    • (1979) Opt. Lett. , vol.4 , pp. 236-238
    • Weber, W.H.1    Eagen, C.F.2
  • 36
    • 48549114117 scopus 로고
    • Electromagnetic interactions of molecules with metal surfaces
    • Ford, G. W., and W. H. Weber. 1984. Electromagnetic interactions of molecules with metal surfaces. Phys. Rep. 113:195-287.
    • (1984) Phys. Rep. , vol.113 , pp. 195-287
    • Ford, G.W.1    Weber, W.H.2
  • 37
    • 0021668349 scopus 로고
    • Effect of planar dielectric interfaces on fluorescence emission and detection. Evanescent excitation with high-aperture collection
    • Burghardt, T. P., and N. L. Thompson. 1984. Effect of planar dielectric interfaces on fluorescence emission and detection. Evanescent excitation with high-aperture collection. Biophys. J. 46:729-737.
    • (1984) Biophys. J. , vol.46 , pp. 729-737
    • Burghardt, T.P.1    Thompson, N.L.2
  • 38
    • 84975574862 scopus 로고
    • Fluorescence emission at dielectric and metal-film interfaces
    • E. H. Hellen and D. Axelrod. 1987. Fluorescence emission at dielectric and metal-film interfaces. J. Opt. Soc. Am. B. 4:337-350.
    • (1987) J. Opt. Soc. Am. B. , vol.4 , pp. 337-350
    • Hellen, E.H.1    Axelrod, D.2
  • 39
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • Magde, D., E. L. Elson, and W. W. Webb. 1974. Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers. 13:29-61.
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 40
    • 0027943305 scopus 로고
    • Effects of pH on myofibrillar ATPase activity in fast and slow skeletal muscle fibers of the rabbit
    • Potma, E. J., I. A. van Graas, and G. J. Stienen. 1994. Effects of pH on myofibrillar ATPase activity in fast and slow skeletal muscle fibers of the rabbit. Biophys. J. 67:2404-2410.
    • (1994) Biophys. J. , vol.67 , pp. 2404-2410
    • Potma, E.J.1    Van Graas, I.A.2    Stienen, G.J.3
  • 42
    • 0030002263 scopus 로고    scopus 로고
    • A study on the mechanism of phalloidin-induced tension changes in skinned rabbit psoas muscle fibres
    • Bukatina, A. E., F. Fuchs, and S. C. Watkins. 1996. A study on the mechanism of phalloidin-induced tension changes in skinned rabbit psoas muscle fibres. J. Muscle Res. Cell Motil. 17:365-371.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 365-371
    • Bukatina, A.E.1    Fuchs, F.2    Watkins, S.C.3
  • 43
    • 0021015221 scopus 로고
    • Studies on conformation of F-actin in muscle fibers in the relaxed state, rigor, and during contraction using fluorescent phalloidin
    • Prochniewicz-Nakayama, E., T. Yanagida, and F. Oosawa. 1983. Studies on conformation of F-actin in muscle fibers in the relaxed state, rigor, and during contraction using fluorescent phalloidin. J. Cell Biol. 97:1663-1667.
    • (1983) J. Cell Biol. , vol.97 , pp. 1663-1667
    • Prochniewicz-Nakayama, E.1    Yanagida, T.2    Oosawa, F.3
  • 44
    • 0032128026 scopus 로고    scopus 로고
    • Photobleaching of fluorescent dyes under conditions used for single-molecule detection: Evidence of two-step photolysis
    • Eggeling, C., J. Widengren, R. Rigler, and C. A. M. Seidel. 1998. Photobleaching of fluorescent dyes under conditions used for single-molecule detection: evidence of two-step photolysis. Anal. Chem. 70:2651-2659.
    • (1998) Anal. Chem. , vol.70 , pp. 2651-2659
    • Eggeling, C.1    Widengren, J.2    Rigler, R.3    Seidel, C.A.M.4
  • 45
    • 0033167917 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes
    • Schwille, P., J. Korlach, and W. W. Webb. 1999. Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes. Cytometry. 36:176-182.
    • (1999) Cytometry , vol.36 , pp. 176-182
    • Schwille, P.1    Korlach, J.2    Webb, W.W.3
  • 46
    • 2342467974 scopus 로고    scopus 로고
    • Ligand-receptor interactions in live cells by fluorescence correlation spectroscopy
    • Pramanik, A. 2004. Ligand-receptor interactions in live cells by fluorescence correlation spectroscopy. Curr. Pharm. Biotechnol. 5:205-212.
    • (2004) Curr. Pharm. Biotechnol. , vol.5 , pp. 205-212
    • Pramanik, A.1
  • 48
    • 0035845662 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy detects galanin receptor diversity on insulinoma cells
    • Pramanik, A., M. Olsson, U. Langel, T. Bartfai, and R. Rigler. 2001. Fluorescence correlation spectroscopy detects galanin receptor diversity on insulinoma cells. Biochemistry. 40:10839-10845.
    • (2001) Biochemistry , vol.40 , pp. 10839-10845
    • Pramanik, A.1    Olsson, M.2    Langel, U.3    Bartfai, T.4    Rigler, R.5
  • 49
    • 0031029922 scopus 로고    scopus 로고
    • Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells
    • Duensing, T. D., and J. P. van Putten. 1997. Vitronectin mediates internalization of Neisseria gonorrhoeae by Chinese hamster ovary cells. Infect. Immun. 65:964-970.
    • (1997) Infect. Immun. , vol.65 , pp. 964-970
    • Duensing, T.D.1    Van Putten, J.P.2
  • 50
    • 0034789580 scopus 로고    scopus 로고
    • Monitoring the conformational fluctuations of DNA hairpins using single-pair fluorescence resonance energy transfer
    • Grunwell, J. R., J. L. Glass, T. D. Lacoste, A. A. Deniz, D. S. Chemla, and P. G. Schultz. 2001. Monitoring the conformational fluctuations of DNA hairpins using single-pair fluorescence resonance energy transfer. J. Am. Chem. Soc. 123:4295-4303.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4295-4303
    • Grunwell, J.R.1    Glass, J.L.2    Lacoste, T.D.3    Deniz, A.A.4    Chemla, D.S.5    Schultz, P.G.6
  • 51
    • 0032126375 scopus 로고    scopus 로고
    • Single-molecule analysis of restriction DNA fragments using fluorescence correlation spectroscopy
    • Kinjo, M., G. Nishimura, T. Koyama, U. Mets, and R. Rigler. 1998. Single-molecule analysis of restriction DNA fragments using fluorescence correlation spectroscopy. Anal. Biochem. 260:166-172.
    • (1998) Anal. Biochem. , vol.260 , pp. 166-172
    • Kinjo, M.1    Nishimura, G.2    Koyama, T.3    Mets, U.4    Rigler, R.5
  • 52
    • 28444454589 scopus 로고    scopus 로고
    • Putting prions into focus: Application of single molecule detection to the diagnosis of prion diseases
    • Giese, A., J. Bieschke, M. Eigen, and H. A. Kretzschmar. 2000. Putting prions into focus: application of single molecule detection to the diagnosis of prion diseases. Arch. Virol. Suppl. 16:161-71.
    • (2000) Arch. Virol. Suppl. , vol.16 , pp. 161-171
    • Giese, A.1    Bieschke, J.2    Eigen, M.3    Kretzschmar, H.A.4


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