메뉴 건너뛰기




Volumn 45, Issue 13, 2006, Pages 4058-4068

In situ single-molecule imaging with attoliter detection using objective total internal reflection confocal microscopy

Author keywords

[No Author keywords available]

Indexed keywords

BIOMEDICAL ENGINEERING; CHROMOPHORES; DIFFRACTION; ELECTROMAGNETIC FIELD EFFECTS; FLUORESCENCE; MICROSCOPIC EXAMINATION; PROTEINS;

EID: 33645550945     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052097d     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 18144399250 scopus 로고    scopus 로고
    • Exploring life by single-molecule fluorescence spectroscopy
    • Neuweiler, H., and Sauer, M. (2005) Exploring life by single-molecule fluorescence spectroscopy, Anal. Chem. 179A-185A.
    • (2005) Anal. Chem.
    • Neuweiler, H.1    Sauer, M.2
  • 2
    • 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
  • 3
    • 23244457898 scopus 로고    scopus 로고
    • Rotational motions of macromolecules by single-molecule fluorescence microscopy
    • Rosenberg, S. A., Quinlan, M. E., Forkey, J. N., and Goldman, Y. E. (2005) Rotational motions of macromolecules by single-molecule fluorescence microscopy, Acc. Chem. Res. 38, 583-593.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 583-593
    • Rosenberg, S.A.1    Quinlan, M.E.2    Forkey, J.N.3    Goldman, Y.E.4
  • 5
    • 0035815743 scopus 로고    scopus 로고
    • The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media
    • Minton, A. P. (2001) The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media, J. Biol. Chem. 276, 10577-10580.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10577-10580
    • Minton, A.P.1
  • 6
    • 0037162456 scopus 로고    scopus 로고
    • Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components
    • Timasheff, S. N. (2002) Protein-solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components, Proc. Natl. Acad. Sci. U.S.A. 99, 9721-9726.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9721-9726
    • Timasheff, S.N.1
  • 7
    • 0014685163 scopus 로고
    • The mechanism of muscular contraction
    • Huxley, H. E. (1969) The mechanism of muscular contraction, Science 164, 1356-1366.
    • (1969) Science , vol.164 , pp. 1356-1366
    • Huxley, H.E.1
  • 8
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley, A. F., and Simmons, R. M. (1971) Proposed mechanism of force generation in striated muscle, Nature 233, 533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 10
    • 0013537731 scopus 로고    scopus 로고
    • Three-dimensional super-resolution with a 4Pi-confocal microscope using image restoration
    • Schrader, M., Hell, S. W., and van der Voort, H. T. M. (1998) Three-dimensional super-resolution with a 4Pi-confocal microscope using image restoration, J. Appl. Phys. 84, 4033-4042.
    • (1998) J. Appl. Phys. , vol.84 , pp. 4033-4042
    • Schrader, M.1    Hell, S.W.2    Van Der Voort, H.T.M.3
  • 11
    • 0034682512 scopus 로고    scopus 로고
    • Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission
    • Klar, T. A., Jakobs, S., Dyba, M., Egner, A., and Hell, S. W. (2000) Fluorescence microscopy with diffraction resolution barrier broken by stimulated emission, Proc. Natl. Acad. Sci. U.S.A. 97, 8206-8210.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8206-8210
    • Klar, T.A.1    Jakobs, S.2    Dyba, M.3    Egner, A.4    Hell, S.W.5
  • 12
    • 0242290929 scopus 로고    scopus 로고
    • Immunofluorescence stimulated emission depletion microscopy
    • Dyba, M., Jakobs, S., and Hell, S. W. (2003) Immunofluorescence stimulated emission depletion microscopy, Nat. Biotechnol. 21, 1303-1304.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1303-1304
    • Dyba, M.1    Jakobs, S.2    Hell, S.W.3
  • 13
    • 0037474152 scopus 로고    scopus 로고
    • Zero-mode waveguides for single-molecule analysis at high concentrations
    • Levene, M. J., Korlach, J., Turner, S. W., Foquet, M., Craighead, H. G., and Webb, W. W. (2003) Zero-mode waveguides for single-molecule analysis at high concentrations, Science 299, 682-686.
    • (2003) Science , vol.299 , pp. 682-686
    • Levene, M.J.1    Korlach, J.2    Turner, S.W.3    Foquet, M.4    Craighead, H.G.5    Webb, W.W.6
  • 14
    • 21244458506 scopus 로고    scopus 로고
    • λ-repressor oligomerization kinetics at high concentrations using fluorescence correlation spectroscopy in zero-mode waveguides
    • Samiee, K. T., Foquet, M., Guo, L., Cox, E. C., and Craighead, H. G. (2005) λ-Repressor oligomerization kinetics at high concentrations using fluorescence correlation spectroscopy in zero-mode waveguides, Biophys. J. 88, 2145-2153.
    • (2005) Biophys. J. , vol.88 , pp. 2145-2153
    • Samiee, K.T.1    Foquet, M.2    Guo, L.3    Cox, E.C.4    Craighead, H.G.5
  • 18
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • Axelrod, D. (2001) Total internal reflection fluorescence microscopy in cell biology. Traffic 2, 764-774.
    • (2001) Traffic , vol.2 , pp. 764-774
    • Axelrod, D.1
  • 19
    • 1642588184 scopus 로고    scopus 로고
    • Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy
    • Ruckstuhl, T., and Seeger, S. (2004) Attoliter detection volumes by confocal total-internal-reflection fluorescence microscopy, Opt. Lett. 29, 569-571.
    • (2004) Opt. Lett. , vol.29 , pp. 569-571
    • Ruckstuhl, T.1    Seeger, S.2
  • 20
    • 0041972289 scopus 로고    scopus 로고
    • Confocal total-internal-reflection fluorescence microscopy with a high-aperture parabolic mirror lens
    • Ruckstuhl, T., and Seeger, S. (2003) Confocal total-internal-reflection fluorescence microscopy with a high-aperture parabolic mirror lens, Appl. Opt. 42, 3277-3283.
    • (2003) Appl. Opt. , vol.42 , pp. 3277-3283
    • Ruckstuhl, T.1    Seeger, S.2
  • 21
    • 25444499946 scopus 로고    scopus 로고
    • Sometimes less is more: Parabolic optics improve analytical sensitivity
    • Ruckstuhl, T. (2005) Sometimes less is more: Parabolic optics improve analytical sensitivity, Biophotonics 12, 48-51.
    • (2005) Biophotonics , vol.12 , pp. 48-51
    • Ruckstuhl, T.1
  • 22
    • 0037035205 scopus 로고    scopus 로고
    • Local diffusion and concentration of IgG near planar membranes: Measurement by total internal reflection with fluorescence correlation spectroscopy
    • Starr, T. E., and Thompson, N. L. (2002) Local diffusion and concentration of IgG near planar membranes: Measurement by total internal reflection with fluorescence correlation spectroscopy, J. Phys. Chem. B 106, 2365-2371.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 2365-2371
    • Starr, T.E.1    Thompson, N.L.2
  • 23
    • 0026985623 scopus 로고
    • Stereospecific reaction of muscle fiber proteins with the 5′ or 6′ isomer of iodoacetamidetetramethyl rhodamine
    • Ajtai, K., Ilich, P. J. K., Ringler, A., Sedarous, S. S., Toft, D. J., and Burghardt, T. P. (1992) Stereospecific reaction of muscle fiber proteins with the 5′ or 6′ isomer of iodoacetamidetetramethyl rhodamine, Biochemistry 31, 12431-12440.
    • (1992) Biochemistry , vol.31 , pp. 12431-12440
    • Ajtai, K.1    Ilich, P.J.K.2    Ringler, A.3    Sedarous, S.S.4    Toft, D.J.5    Burghardt, T.P.6
  • 24
    • 33644982036 scopus 로고    scopus 로고
    • Rotations of a few cross-bridges in muscle by confocal total internal reflection microscopy
    • in press
    • Borejdo, J., Talent, J., Akopova, I., and Burghardt, T. P. (2006) Rotations of a few cross-bridges in muscle by confocal total internal reflection microscopy, Biochim. Biophys. Acta, in press.
    • (2006) Biochim. Biophys. Acta
    • Borejdo, J.1    Talent, J.2    Akopova, I.3    Burghardt, T.P.4
  • 25
    • 0040238077 scopus 로고
    • Fluctuations in polarized fluorescence: Evidence that muscle cross bridges rotate repetitively during contraction
    • Borejdo, J., Putnam, S., and Morales, M. F. (1979) Fluctuations in polarized fluorescence: Evidence that muscle cross bridges rotate repetitively during contraction, Proc. Natl. Acad. Sci. U.S.A. 76, 6346-6350.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 6346-6350
    • Borejdo, J.1    Putnam, S.2    Morales, M.F.3
  • 26
    • 0024561651 scopus 로고
    • Fluorescent modification and orientation of myosin sulfhydryl 2 in skeletal muscle fibers
    • Ajtai, K., and Burghardt, T. P. (1989) Fluorescent modification and orientation of myosin sulfhydryl 2 in skeletal muscle fibers, Biochemistry 28, 2204-2210.
    • (1989) Biochemistry , vol.28 , pp. 2204-2210
    • Ajtai, K.1    Burghardt, T.P.2
  • 27
    • 0030928755 scopus 로고    scopus 로고
    • Probes bound to myosin Cys-707 rotate during length transients in contraction
    • Burghardt, T. P., Garamszegi, S. P., and Ajtai, K. (1997) Probes bound to myosin Cys-707 rotate during length transients in contraction, Proc. Natl. Acad. Sci. U.S.A. 94, 9631-9636.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9631-9636
    • Burghardt, T.P.1    Garamszegi, S.P.2    Ajtai, K.3
  • 28
    • 0004232671 scopus 로고
    • Princeton University Press, Princeton, NJ
    • Berg, H. C. (1983) Random Walks in Biology, Princeton University Press, Princeton, NJ.
    • (1983) Random Walks in Biology
    • Berg, H.C.1
  • 29
    • 0042322244 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy with non-ideal photodetectors
    • Hillesheim, L. N., and Müller, J. D. (2003) The photon counting histogram in fluorescence fluctuation spectroscopy with non-ideal photodetectors, Bioophys. J. 85, 1948-1958.
    • (2003) Bioophys. J. , vol.85 , pp. 1948-1958
    • Hillesheim, L.N.1    Müller, J.D.2
  • 30
    • 0000890319 scopus 로고
    • (Wilson, T., Ed.), Academic Press, New York
    • Wilson, T. (1990) in Confocal Microscopy (Wilson, T., Ed.) pp 1-64, Academic Press, New York.
    • (1990) Confocal Microscopy , pp. 1-64
    • Wilson, T.1
  • 31
    • 0000235622 scopus 로고    scopus 로고
    • Optimized pupil-plane filters for confocal microscope point-spread function engineering
    • Neu, M. A. A., Juškaitis, R., Wilson, T., Laczik, Z. J., and Sarafis, V. (2000) Optimized pupil-plane filters for confocal microscope point-spread function engineering, Opt. Lett. 25, 245-247.
    • (2000) Opt. Lett. , vol.25 , pp. 245-247
    • Neu, M.A.A.1    Juškaitis, R.2    Wilson, T.3    Laczik, Z.J.4    Sarafis, V.5
  • 32
    • 0012112253 scopus 로고    scopus 로고
    • Orientational imaging of single molecules by annular illumination
    • Sick, B., Hecht, B., and Novotny, L. (2000) Orientational imaging of single molecules by annular illumination, Phys. Rev. Lett. 85, 4482-4485.
    • (2000) Phys. Rev. Lett. , vol.85 , pp. 4482-4485
    • Sick, B.1    Hecht, B.2    Novotny, L.3
  • 33
    • 4644233568 scopus 로고    scopus 로고
    • Capabilities and limitations of pupil-plane filters for superresolution and image enhancement
    • Davis, B. J., Karl, W. C., Swan, A. K., and Ünlü, M. S. (2004) Capabilities and limitations of pupil-plane filters for superresolution and image enhancement, Optics Express 12, 4150-4156.
    • (2004) Optics Express , vol.12 , pp. 4150-4156
    • Davis, B.J.1    Karl, W.C.2    Swan, A.K.3    Ünlü, M.S.4
  • 34
    • 0001106323 scopus 로고
    • Electromagnetic diffraction in optical systems. II. Structure of the image field in an aplanatic system
    • Richards, B., and Wolf, E. (1959) Electromagnetic diffraction in optical systems. II. Structure of the image field in an aplanatic system, Proc. R. Soc. London, Ser. A 253, 358-379.
    • (1959) Proc. R. Soc. London, Ser. A , vol.253 , pp. 358-379
    • Richards, B.1    Wolf, E.2
  • 35
    • 0037306093 scopus 로고    scopus 로고
    • Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever arm movement
    • Muhlrad, A., Peyser, Y. M., Nili, M., Ajtai, K., Reisler, E., and Burghardt, T. P. (2003) Chemical decoupling of ATPase activation and force production from the contractile cycle in myosin by steric hindrance of lever arm movement, Biophys. J. 84, 1047-1056.
    • (2003) Biophys. J. , vol.84 , pp. 1047-1056
    • Muhlrad, A.1    Peyser, Y.M.2    Nili, M.3    Ajtai, K.4    Reisler, E.5    Burghardt, T.P.6
  • 36
    • 0016125864 scopus 로고
    • Electromagnetic field near the focus of Gaussian beams
    • Yoshida, A., and Asakura, T. (1974) Electromagnetic field near the focus of Gaussian beams, Optik 41, 281-292.
    • (1974) Optik , vol.41 , pp. 281-292
    • Yoshida, A.1    Asakura, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.