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Volumn 89, Issue 1, 2005, Pages 605-618

Rapid analysis of Förster resonance energy transfer by two-color global fluorescence correlation spectroscopy: Trypsin proteinase reaction

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE; TRYPSIN; PEPTIDE; SERINE PROTEINASE; TRYPSIN LIKE SERINE PROTEASE; TRYPSIN-LIKE SERINE PROTEASE;

EID: 23244451444     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.052753     Document Type: Article
Times cited : (47)

References (82)
  • 5
    • 0041876386 scopus 로고    scopus 로고
    • Methods of single-molecule fluorescence spectroscopy and microscopy
    • Moemer, W. E., and D. P. Fromm. 2003. Methods of single-molecule fluorescence spectroscopy and microscopy. Rev. Sci. Instrum. 74:3597-3619.
    • (2003) Rev. Sci. Instrum. , vol.74 , pp. 3597-3619
    • Moemer, W.E.1    Fromm, D.P.2
  • 6
    • 0001468698 scopus 로고    scopus 로고
    • Optical studies of single molecules at room temperature
    • Xie, X. S., and J. K. Trautmann. 1998. Optical studies of single molecules at room temperature. Annu. Rev. Phys. Chem. 49:441-480.
    • (1998) Annu. Rev. Phys. Chem. , vol.49 , pp. 441-480
    • Xie, X.S.1    Trautmann, J.K.2
  • 8
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system: Measurements by fluorescence correlation spectroscopy
    • Magde, D., E. L. Elson, and W. W. Webb. 1972. Thermodynamic fluctuations in a reacting system: measurements by fluorescence correlation spectroscopy. Phys. Rev. Lett. 29:705-708.
    • (1972) Phys. Rev. Lett. , vol.29 , pp. 705-708
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 9
    • 0033021689 scopus 로고    scopus 로고
    • Resolution of fluorescence correlation measurements
    • Meseth, U., T. Wohland, R. Rigler, and H. Vogel. 1999. Resolution of fluorescence correlation measurements. Biophys. J. 76:1619-1631.
    • (1999) Biophys. J. , vol.76 , pp. 1619-1631
    • Meseth, U.1    Wohland, T.2    Rigler, R.3    Vogel, H.4
  • 10
    • 0348155858 scopus 로고    scopus 로고
    • New fluorescence techniques for high-throughput drug discovery
    • Jäger, S., L. Brand, and C. Eggeling. 2003. New Fluorescence Techniques for High-Throughput Drug Discovery. Curr. Pharm. Biotechnol. 4:463-476.
    • (2003) Curr. Pharm. Biotechnol. , vol.4 , pp. 463-476
    • Jäger, S.1    Brand, L.2    Eggeling, C.3
  • 11
    • 0023395681 scopus 로고
    • Molecular aggregation characterized by high order autocorrelation in fluorescence correlation spectroscopy
    • Palmer, A. G., and N. L. Thompson. 1987. Molecular aggregation characterized by high order autocorrelation in fluorescence correlation spectroscopy. Biophys. J. 52:257-270.
    • (1987) Biophys. J. , vol.52 , pp. 257-270
    • Palmer, A.G.1    Thompson, N.L.2
  • 12
    • 0025056742 scopus 로고
    • On the analysis of high order moments of fluorescence fluctuations
    • Qian, H., and E. L. Elson. 1990. On the analysis of high order moments of fluorescence fluctuations. Biophys. J. 57:375-380.
    • (1990) Biophys. J. , vol.57 , pp. 375-380
    • Qian, H.1    Elson, E.L.2
  • 13
    • 0344603641 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy
    • Chen, Y., J. D. Müller, P. T. C. So, and E. Gratton. 1999. The photon counting histogram in fluorescence fluctuation spectroscopy. Biophys. J. 77:553-567.
    • (1999) Biophys. J. , vol.77 , pp. 553-567
    • Chen, Y.1    Müller, J.D.2    So, P.T.C.3    Gratton, E.4
  • 14
    • 0033598837 scopus 로고    scopus 로고
    • Fluorescence-intensity distribution analysis and its application in biomolecular detection technology
    • Kask, P., K. Palo, D. Ullmann, and K. Gall. 1999. Fluorescence-intensity distribution analysis and its application in biomolecular detection technology. Proc. Natl. Acad. Sci. USA. 96:13756-13761.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13756-13761
    • Kask, P.1    Palo, K.2    Ullmann, D.3    Gall, K.4
  • 15
    • 0034979380 scopus 로고    scopus 로고
    • Ligand binding to transmembrane receptors on intact cells or membrane vesicles measured in a homogeneous 1-microliter assay format
    • Klumpp, M., A. Scheel, E. Lopez-Calle, M. Busch, K. J. Murray, and A. J. Pope. 2001. Ligand binding to transmembrane receptors on intact cells or membrane vesicles measured in a homogeneous 1-microliter assay format. J. Biomol. Screen. 6:159-170.
    • (2001) J. Biomol. Screen. , vol.6 , pp. 159-170
    • Klumpp, M.1    Scheel, A.2    Lopez-Calle, E.3    Busch, M.4    Murray, K.J.5    Pope, A.J.6
  • 17
    • 0035070985 scopus 로고    scopus 로고
    • Molecular Heterogeneity of O-acetylserine sulfhydrylase by two-photon excited fluorescence fluctuation spectroscopy
    • Chirico, G., S. Bettati, A. Mozzarelli, Y. Chen, J. D. Müller, and E. Gratton. 2001. Molecular Heterogeneity of O-acetylserine sulfhydrylase by two-photon excited fluorescence fluctuation spectroscopy. Biophys. J. 80:1973-1985.
    • (2001) Biophys. J. , vol.80 , pp. 1973-1985
    • Chirico, G.1    Bettati, S.2    Mozzarelli, A.3    Chen, Y.4    Müller, J.D.5    Gratton, E.6
  • 18
    • 0036220117 scopus 로고    scopus 로고
    • Molecular brightness characterization of EGFP in vivo by fluorescence fluctuation spectroscopy
    • Chen, Y., J. D. Müller, Q. Ruan, and E. Gratton. 2002. Molecular brightness characterization of EGFP in vivo by fluorescence fluctuation spectroscopy. Biophys. J. 82:133-144.
    • (2002) Biophys. J. , vol.82 , pp. 133-144
    • Chen, Y.1    Müller, J.D.2    Ruan, Q.3    Gratton, E.4
  • 21
    • 0001594854 scopus 로고    scopus 로고
    • Quantitative identification of different single-molecules by selective time-resolved confocal fluorescence spectroscopy
    • Fries, J. R., L. Brand, C. Eggeling, M. Köllner, and C. A. M. Seidel. 1998. Quantitative identification of different single-molecules by selective time-resolved confocal fluorescence spectroscopy. J. Phys. Chem. A. 102:6601-6613.
    • (1998) J. Phys. Chem. A , vol.102 , pp. 6601-6613
    • Fries, J.R.1    Brand, L.2    Eggeling, C.3    Köllner, M.4    Seidel, C.A.M.5
  • 22
    • 0000664513 scopus 로고
    • Direct measurement of a distinct correlation function by fluorescence cross correlation
    • Ricka, J., and T. Binkert. 1989. Direct measurement of a distinct correlation function by fluorescence cross correlation. Phyx. Rev. A. 39:2646-2652.
    • (1989) Phyx. Rev. A , vol.39 , pp. 2646-2652
    • Ricka, J.1    Binkert, T.2
  • 23
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille, P., F. J. Meyer-Almes, and R. Rigler. 1997. Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys. J. 72:1878-1886.
    • (1997) Biophys. J. , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer-Almes, F.J.2    Rigler, R.3
  • 26
    • 0842281277 scopus 로고    scopus 로고
    • Detection of specific DNA sequences using dual-color two-photon fluorescence correlation spectroscopy
    • Berland, K. M. 2004. Detection of specific DNA sequences using dual-color two-photon fluorescence correlation spectroscopy. J. Biotechnol. 108:127-136.
    • (2004) J. Biotechnol. , vol.108 , pp. 127-136
    • Berland, K.M.1
  • 27
    • 0034641711 scopus 로고    scopus 로고
    • Simultaneous two-photon excitation of distinct labels for dual-color fluorescence cross-correlation analysis
    • Heinze, K. G., A. Koltermann, and P. Schwille. 2000. Simultaneous two-photon excitation of distinct labels for dual-color fluorescence cross-correlation analysis. Proc. Natl. Acad. Sci. USA. 97:10377-10382.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10377-10382
    • Heinze, K.G.1    Koltermann, A.2    Schwille, P.3
  • 28
    • 2442583135 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy using single laser wavelength excitation
    • Hwang, L. C., and T. Wohland. 2004. Dual-color fluorescence cross-correlation spectroscopy using single laser wavelength excitation. Chem. Phys. Chem. 5:549-551.
    • (2004) Chem. Phys. Chem. , vol.5 , pp. 549-551
    • Hwang, L.C.1    Wohland, T.2
  • 29
    • 0032539688 scopus 로고    scopus 로고
    • Real-time enzyme kinetics monitored by dual-color fluorescence cross-correlation spectroscopy
    • Kettling, U., A. Koltermann, P. Schwille, and M. Eigen. 1998. Real-time enzyme kinetics monitored by dual-color fluorescence cross-correlation spectroscopy. Proc. Natl. Acad. Sci. USA. 95:1416-1420.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 1416-1420
    • Kettling, U.1    Koltermann, A.2    Schwille, P.3    Eigen, M.4
  • 31
    • 2942620251 scopus 로고    scopus 로고
    • Structure and dynamics of lipoplex formation examined using two-photon fluorescence cross-correlation spectroscopy
    • Merkte, D., S. P. Lees-Miller, and D. T. Cramb. 2004. Structure and dynamics of lipoplex formation examined using two-photon fluorescence cross-correlation spectroscopy. Biochemistry. 43:7263-7272.
    • (2004) Biochemistry , vol.43 , pp. 7263-7272
    • Merkte, D.1    Lees-Miller, S.P.2    Cramb, D.T.3
  • 33
    • 1542327697 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with high-order and dual-color correlation to probe nonequilibrium steady states
    • Qian, H., and E. L. Elson. 2004. Fluorescence correlation spectroscopy with high-order and dual-color correlation to probe nonequilibrium steady states. Proc. Natl. Acad. Sci. USA. 101:2828-2833.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2828-2833
    • Qian, H.1    Elson, E.L.2
  • 35
    • 0040182980 scopus 로고    scopus 로고
    • Simultaneous binding of two DNA duplexes to the NtrC-enhancer complex studied by two-color fluorescence cross-correlation
    • Rippe, K. 2000. Simultaneous binding of two DNA duplexes to the NtrC-enhancer complex studied by two-color fluorescence cross-correlation Biochemistry. 39:2131-2139.
    • (2000) Biochemistry , vol.39 , pp. 2131-2139
    • Rippe, K.1
  • 36
    • 0000545874 scopus 로고
    • Dual-beam incoherent cross-correlation spectroscopy
    • Xia, K.-Q., Y.-B. Xin. and P. Tong. 1995. Dual-beam incoherent cross-correlation spectroscopy. J. Opt. Soc. Am. A. 12:1571-1578.
    • (1995) J. Opt. Soc. Am. A , vol.12 , pp. 1571-1578
    • Xia, K.-Q.1    Xin, Y.-B.2    Tong, P.3
  • 37
    • 0034625009 scopus 로고    scopus 로고
    • Ultrasensitive detection of pathological priori protein aggregates by dual-color scanning for intensely fluorescent targets
    • Bieschke, J., A. Giese, W. Schulz-Schaeffer, I. Zerr, S. Poser, M. Eigen, and H. Kretzschmar. 2000. Ultrasensitive detection of pathological priori protein aggregates by dual-color scanning for intensely fluorescent targets. Proc. Natl. Acad. Sci. USA. 97:5468-5473.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5468-5473
    • Bieschke, J.1    Giese, A.2    Schulz-Schaeffer, W.3    Zerr, I.4    Poser, S.5    Eigen, M.6    Kretzschmar, H.7
  • 38
    • 0038350667 scopus 로고    scopus 로고
    • Highly sensitive fluorescence detection technology currently available for HTS
    • Eggeling, C., L. Brand, and S. Jäger. 2003. Highly sensitive fluorescence detection technology currently available for HTS. Drug Discov. Today. 8:632-641.
    • (2003) Drug Discov. Today , vol.8 , pp. 632-641
    • Eggeling, C.1    Brand, L.2    Jäger, S.3
  • 39
    • 1642339614 scopus 로고    scopus 로고
    • Single-nucleotide polymorphism detection using nanomolar nucleotides and single-molecule fluorescence
    • Twist, C. R., M. K. Winson, J. J. Rowland, and D. B. Kell. 2004. Single-nucleotide polymorphism detection using nanomolar nucleotides and single-molecule fluorescence. Anal. Biochem. 327:35-44.
    • (2004) Anal. Biochem. , vol.327 , pp. 35-44
    • Twist, C.R.1    Winson, M.K.2    Rowland, J.J.3    Kell, D.B.4
  • 41
    • 0033637148 scopus 로고    scopus 로고
    • Fluorescence intensity multiple distribution analysis. Concurrent determination of diffusion times and molecular brightness
    • Palo, K., Ü. Mets, S. Jäger, P. Kask, and K. Gall. 2000. Fluorescence intensity multiple distribution analysis. Concurrent determination of diffusion times and molecular brightness. Biophys. J. 79:2858-2866.
    • (2000) Biophys. J. , vol.79 , pp. 2858-2866
    • Palo, K.1    Mets, Ü.2    Jäger, S.3    Kask, P.4    Gall, K.5
  • 42
    • 33644478151 scopus 로고    scopus 로고
    • Resolving heterogeneity on the single molecule level with the photon-counting histogram
    • Müller, J. D., Y. Chen, and E. Gratton. 2000. Resolving heterogeneity on the single molecule level with the photon-counting histogram. Biophys. J. 82:133-144.
    • (2000) Biophys. J. , vol.82 , pp. 133-144
    • Müller, J.D.1    Chen, Y.2    Gratton, E.3
  • 43
    • 1542306618 scopus 로고    scopus 로고
    • Photon arrival-time interval distribution (PAID): A novel tool for analyzing molecular interactions
    • Laurence, T. A., A. N. Kapanidis, X. Kong, D. S. Chemla, and S. Weiss. 2004. Photon arrival-time interval distribution (PAID): a novel tool for analyzing molecular interactions. J. Phys. Chem. B. 108:3051-3067.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 3051-3067
    • Laurence, T.A.1    Kapanidis, A.N.2    Kong, X.3    Chemla, D.S.4    Weiss, S.5
  • 44
    • 0039025943 scopus 로고
    • Fluorescence correlation spectroscopy of triplet states in solution: A theoretical and experimental study
    • Widengren, J., Ü. Mets, and R. Rigler. 1995. Fluorescence correlation spectroscopy of triplet states in solution: a theoretical and experimental study. J. Phys. Chem. 99:13368-13379.
    • (1995) J. Phys. Chem. , vol.99 , pp. 13368-13379
    • Widengren, J.1    Mets, Ü.2    Rigler, R.3
  • 45
    • 0029977148 scopus 로고    scopus 로고
    • Scanning two-photon fluctuation correlation spectroscopy: Particle counting measurements for detection of molecular aggregates
    • Berland, K., P. T. C. So, Y. Chen, W. W. Mantulin, and E. Gratton. 1996. Scanning two-photon fluctuation correlation spectroscopy: particle counting measurements for detection of molecular aggregates. Biophys. J. 71:410-420.
    • (1996) Biophys. J. , vol.71 , pp. 410-420
    • Berland, K.1    So, P.T.C.2    Chen, Y.3    Mantulin, W.W.4    Gratton, E.5
  • 46
    • 0033869619 scopus 로고    scopus 로고
    • Probing ligand protein binding equilibria with fluorescence fluctuation spectroscopy
    • Chen, Y., J. D. Müller, S. Y. Tetin, J. D. Tyner, and E. Gratton. 2000. Probing ligand protein binding equilibria with fluorescence fluctuation spectroscopy. Biophys. J. 79:1074-1084.
    • (2000) Biophys. J. , vol.79 , pp. 1074-1084
    • Chen, Y.1    Müller, J.D.2    Tetin, S.Y.3    Tyner, J.D.4    Gratton, E.5
  • 47
    • 84981779372 scopus 로고
    • Zwischenmolekulare energiewanderung und fluoreszenz
    • in German
    • Förster, T. 1948. Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann. Phys. 2:55-75. [in German].
    • (1948) Ann. Phys. , vol.2 , pp. 55-75
    • Förster, T.1
  • 48
    • 0003667153 scopus 로고    scopus 로고
    • D. L. Andrews and A. A. Demidov, editors. John Wiley & Sons, Chicester, UK
    • Andrews, D. L., and A. A. Demidov. 1999. Resonance Energy Transfer, D. L. Andrews and A. A. Demidov, editors. John Wiley & Sons, Chicester, UK.
    • (1999) Resonance Energy Transfer
    • Andrews, D.L.1    Demidov, A.A.2
  • 49
    • 0026687952 scopus 로고
    • Fluorescence resonance energy transfer and nucleic acids
    • Clegg, R. M. 1992. Fluorescence resonance energy transfer and nucleic acids. Methods Enzymol. 211:353-388.
    • (1992) Methods Enzymol. , vol.211 , pp. 353-388
    • Clegg, R.M.1
  • 50
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • Ha, T. 2001. Single-molecule fluorescence resonance energy transfer. Methods. 25:78-86.
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 52
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localization
    • Sekar, R. B., and A. Periasamy. 2003. Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localization. J. Cell Biol. 160:629-633.
    • (2003) J. Cell Biol. , vol.160 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 54
    • 20644431583 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonant energy transfer in calcium concentration dependent cameleon
    • Brasselet, S., E. J. G. Peterman, A. Miyawaki, and W. E. Moerner. 2000. Single-molecule fluorescence resonant energy transfer in calcium concentration dependent cameleon. J. Phys. Chem. B. 104:3676-3682.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3676-3682
    • Brasselet, S.1    Peterman, E.J.G.2    Miyawaki, A.3    Moerner, W.E.4
  • 55
    • 0021508431 scopus 로고
    • Intramolecular dynamics of chain molecules monitored by fluctuations in efficiency of excitation energy transfer
    • Haas, E., and I. Z. Steinberg. 1984. Intramolecular dynamics of chain molecules monitored by fluctuations in efficiency of excitation energy transfer. Biophys. J. 46:429-437.
    • (1984) Biophys. J. , vol.46 , pp. 429-437
    • Haas, E.1    Steinberg, I.Z.2
  • 56
    • 0036283241 scopus 로고    scopus 로고
    • Analysis of coupled bimolecular reaction kinetics and diffusion by two-color fluorescence correlation spectroscopy: Enhanced resolution of kinetics by resonance energy transfer
    • Horn, E. F. Y., and A. S. Verkman. 2002. Analysis of coupled bimolecular reaction kinetics and diffusion by two-color fluorescence correlation spectroscopy: enhanced resolution of kinetics by resonance energy transfer. Biophys. J. 83:533-546.
    • (2002) Biophys. J. , vol.83 , pp. 533-546
    • Horn, E.F.Y.1    Verkman, A.S.2
  • 57
    • 0037125999 scopus 로고    scopus 로고
    • A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins
    • Kohl, T., K. G. Heinze, R. Kuhlemann, A. Koltermann, and P. Schwille. 2002. A protease assay for two-photon crosscorrelation and FRET analysis based solely on fluorescent proteins. Proc. Natl. Acad. Sci. USA. 99:12161-12166.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12161-12166
    • Kohl, T.1    Heinze, K.G.2    Kuhlemann, R.3    Koltermann, A.4    Schwille, P.5
  • 58
    • 0035913541 scopus 로고    scopus 로고
    • Two new concepts to measure fluorescence resonance energy transfer via fluorescence correlation spectroscopy: Theory and experimental realizations
    • Widengren, J., E. Schweinberger, S. Berger, and C. A. M. Seidel. 2001. Two new concepts to measure fluorescence resonance energy transfer via fluorescence correlation spectroscopy: theory and experimental realizations. J. Phys. Chem. 105:6851-6866.
    • (2001) J. Phys. Chem. , vol.105 , pp. 6851-6866
    • Widengren, J.1    Schweinberger, E.2    Berger, S.3    Seidel, C.A.M.4
  • 60
    • 0029832603 scopus 로고    scopus 로고
    • Trypsin: A case study in the structural determinants of enzyme specificity
    • Hedstrom, L. 1996. Trypsin: a case study in the structural determinants of enzyme specificity. Biol. Chem. 377:465-470.
    • (1996) Biol. Chem. , vol.377 , pp. 465-470
    • Hedstrom, L.1
  • 61
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J. J., and C. S. Craik. 1995. Structural basis of substrate specificity in the serine proteases. Protein Sci. 4:337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 62
    • 0032535442 scopus 로고    scopus 로고
    • Design and synthesis of fluorogenic trypsin peptide substrates based on resonance energy transfer
    • Grahn, S., D. Ullmann, and H.-D. Jakubke. 1998. Design and synthesis of fluorogenic trypsin peptide substrates based on resonance energy transfer. anal. Biochem. 265:225-231.
    • (1998) Anal. Biochem. , vol.265 , pp. 225-231
    • Grahn, S.1    Ullmann, D.2    Jakubke, H.-D.3
  • 64
    • 23244442940 scopus 로고    scopus 로고
    • Comparison of different fluorescence fluctuation methods for their use in FRET assays. Monitoring a protease reaction
    • In press
    • Eggeling, C., S. Jäger, D. Winkler, and P. Kask. 2005. Comparison of different fluorescence fluctuation methods for their use in FRET assays. Monitoring a protease reaction. Curr. Pharm. Biotechnol. In press.
    • (2005) Curr. Pharm. Biotechnol.
    • Eggeling, C.1    Jäger, S.2    Winkler, D.3    Kask, P.4
  • 65
    • 0036708472 scopus 로고    scopus 로고
    • Two-photon fluorescence coincidence analysis: Rapid measurements of enzyme kinetics
    • Heinze, K. G., M. Rarbach, M. Jahnz, and P. Schwille. 2002. Two-photon fluorescence coincidence analysis: rapid measurements of enzyme kinetics. Biophys. J. 83:1671-1681.
    • (2002) Biophys. J. , vol.83 , pp. 1671-1681
    • Heinze, K.G.1    Rarbach, M.2    Jahnz, M.3    Schwille, P.4
  • 66
    • 0017801658 scopus 로고
    • Fluorescence correlation spectroscopy. III. Uniform translation and laminar flow
    • Magde, D., W. W. Webb, and E. L. Elson. 1978. Fluorescence correlation spectroscopy. III. Uniform translation and laminar flow. Biopolymers. 17:361-376.
    • (1978) Biopolymers. , vol.17 , pp. 361-376
    • Magde, D.1    Webb, W.W.2    Elson, E.L.3
  • 67
    • 0023286051 scopus 로고
    • Theory of sample translation in fluorescence correlation spectroscopy
    • Palmer, A. G., and N. L. Thompson. 1987. Theory of sample translation in fluorescence correlation spectroscopy. Biophys. J. 51:339-343.
    • (1987) Biophys. J. , vol.51 , pp. 339-343
    • Palmer, A.G.1    Thompson, N.L.2
  • 68
    • 0022545162 scopus 로고
    • Scanning fluorescence correlation spectroscopy. I. Theory and simulation of aggregation measurements
    • Petersen, N. O. 1986. Scanning fluorescence correlation spectroscopy. I. Theory and simulation of aggregation measurements. Biophys. J. 49:809-815.
    • (1986) Biophys. J. , vol.49 , pp. 809-815
    • Petersen, N.O.1
  • 69
    • 4143135216 scopus 로고    scopus 로고
    • Spatial-temporal studies of membrane dynamics: Scanning fluorescence correlation spectroscopy (SFCS)
    • Ruan, Q., M. A. Cheng, M. Levi, E. Gratton, and W. W. Mantulin. 2004. Spatial-temporal studies of membrane dynamics: scanning fluorescence correlation spectroscopy (SFCS). Biophys. J. 87:1260-1267.
    • (2004) Biophys. J. , vol.87 , pp. 1260-1267
    • Ruan, Q.1    Cheng, M.A.2    Levi, M.3    Gratton, E.4    Mantulin, W.W.5
  • 70
    • 0033573989 scopus 로고    scopus 로고
    • Confocal fluorescence coincidence analysis: An approach to ultra high throughput screening
    • Winkler, T., U. Kettling, A. Koltermann, and M. Eigen. 1999. Confocal fluorescence coincidence analysis: an approach to ultra high throughput screening. Proc. Natl. Acad. Sci. USA. 96:1375-1378.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1375-1378
    • Winkler, T.1    Kettling, U.2    Koltermann, A.3    Eigen, M.4
  • 71
    • 23244465393 scopus 로고    scopus 로고
    • Fluorescence intensity distribution analysis (FIDA) and related fluorescence fluctuation techniques: Theory and practice
    • R. Kraayenhof, A. J. W. G. Visser, and H. C. Gerritsen, editors. Springer. New York, NY
    • Kask, P., C. Eggeling, K. Palo, Ü. Mets, M. Cole, and K. Gall. 2002. Fluorescence intensity distribution analysis (FIDA) and related fluorescence fluctuation techniques: theory and practice. In Fluorescence Spectroscopy, Imaging and Probes: New Tools in Chemical, Physical and Life Sciences. R. Kraayenhof, A. J. W. G. Visser, and H. C. Gerritsen, editors. Springer. New York, NY. 153-181.
    • (2002) Fluorescence Spectroscopy, Imaging and Probes: New Tools in Chemical, Physical and Life Sciences , pp. 153-181
    • Kask, P.1    Eggeling, C.2    Palo, K.3    Mets, Ü.4    Cole, M.5    Gall, K.6
  • 72
    • 0032544218 scopus 로고    scopus 로고
    • Engineering the S1′ subsite of trypsin: Design of a protease which cleaves between dibasic residues
    • Kurth, T., S. Grahn, M. Thormann, D. Ullmann, H.-J. Hofmann, H.-D. Jakubke, and L. Hedstrom. 1998. Engineering the S1′ subsite of trypsin: design of a protease which cleaves between dibasic residues. Biochemistry. 37:11434-11440.
    • (1998) Biochemistry , vol.37 , pp. 11434-11440
    • Kurth, T.1    Grahn, S.2    Thormann, M.3    Ullmann, D.4    Hofmann, H.-J.5    Jakubke, H.-D.6    Hedstrom, L.7
  • 73
    • 0010012322 scopus 로고    scopus 로고
    • Photostabilities of fluorescent dyes for single-molecule spectroscopy: Mechanisms and experimental methods for estimating photobleaching in aqueous solution
    • W. Rettig, B. Strehmel, M. Schrader, and H. Seifert, editors. Springer, Berlin, Germany
    • Eggeling, C., J. Widengren, R. Rigler, and C. A. M. Seidel. 1999. Photostabilities of fluorescent dyes for single-molecule spectroscopy: mechanisms and experimental methods for estimating photobleaching in aqueous solution. In Applied Fluorescence in Chemistry, Biology and Medicine. W. Rettig, B. Strehmel, M. Schrader, and H. Seifert, editors. Springer, Berlin, Germany. 193-240.
    • (1999) Applied Fluorescence in Chemistry, Biology and Medicine , pp. 193-240
    • Eggeling, C.1    Widengren, J.2    Rigler, R.3    Seidel, C.A.M.4
  • 74
    • 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
  • 76
    • 23244453017 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang, J. H., T. D. Chung, and K. R. Oldenburg. 1999. A simple statistical parameter for use in evaluation and validation of high throughput screening assays. J. Biomol. Screen. 7:275-290.
    • (1999) J. Biomol. Screen. , vol.7 , pp. 275-290
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 77
    • 0033616580 scopus 로고    scopus 로고
    • Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Förster distance dependence and subpopulations
    • Deniz, A. A., M. Dahan, J. R. Grunwell, T. Ha, A. E. Faulhaber, D. S. Chemla, S. Weiss, and P. G. Schultz. 1999. Single-pair fluorescence resonance energy transfer on freely diffusing molecules: observation of Förster distance dependence and subpopulations. Proc. Natl. Acad. Sci. USA. 96:3670-3675.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3670-3675
    • Deniz, A.A.1    Dahan, M.2    Grunwell, J.R.3    Ha, T.4    Faulhaber, A.E.5    Chemla, D.S.6    Weiss, S.7    Schultz, P.G.8
  • 78
    • 0037126290 scopus 로고    scopus 로고
    • Probing the free energy surface for protein folding with single molecule fluorescence spectroscopy
    • Schuler, B., E. A. Lipman, and W. A. Eaton. 2002. Probing the free energy surface for protein folding with single molecule fluorescence spectroscopy. Nature. 419:743-747.
    • (2002) Nature , vol.419 , pp. 743-747
    • Schuler, B.1    Lipman, E.A.2    Eaton, W.A.3
  • 79
    • 0242322565 scopus 로고    scopus 로고
    • Toward fluorescence nanoscopy
    • Hell, S. W. 2003. Toward fluorescence nanoscopy. Nat. Biotechnol. 21:1347-1355.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 1347-1355
    • Hell, S.W.1
  • 80
  • 81
    • 0037474104 scopus 로고    scopus 로고
    • How to detect weak pairs
    • Laurence, T. A., and S. Weiss. 2003. How to detect weak pairs. Science. 299:667-668.
    • (2003) Science , vol.299 , pp. 667-668
    • Laurence, T.A.1    Weiss, S.2
  • 82
    • 0035996964 scopus 로고    scopus 로고
    • Fluorescence intensity and lifetime distribution analysis: Toward higher accuracy in fluorescence fluctuation spectroscopy
    • Palo, K., L. Brand, C. Eggeling, S. Jäger, P. Kask, and K. Gall. 2002. Fluorescence intensity and lifetime distribution analysis: toward higher accuracy in fluorescence fluctuation spectroscopy. Biophys. J. 83:605-618.
    • (2002) Biophys. J. , vol.83 , pp. 605-618
    • Palo, K.1    Brand, L.2    Eggeling, C.3    Jäger, S.4    Kask, P.5    Gall, K.6


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