메뉴 건너뛰기




Volumn 88, Issue 6, 2005, Pages 4319-4336

Two-photon cross-correlation analysis of intracellular reactions with variable stoichiometry

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; PROTEIN KINASE (CALCIUM,CALMODULIN) II;

EID: 22244464837     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.055319     Document Type: Article
Times cited : (102)

References (51)
  • 2
    • 0001115948 scopus 로고
    • Laser photolysis of laser dyes and the influence of triplet quenchers
    • Asimov, M. M., V. N. Gavrilenko, and A. N. Rubinov. 1990. Laser photolysis of laser dyes and the influence of triplet quenchers. J. Luminesc. 46:243-249.
    • (1990) J. Luminesc. , vol.46 , pp. 243-249
    • Asimov, M.M.1    Gavrilenko, V.N.2    Rubinov, A.N.3
  • 4
    • 0035997078 scopus 로고    scopus 로고
    • Probing the endocytic pathway in live cells using dual-color fluorescence cross-correlation analysis
    • Bacia, K., I. V. Majoul, and P. Schwille. 2002. Probing the endocytic pathway in live cells using dual-color fluorescence cross-correlation analysis. Biophys. J. 83:1184-1193.
    • (2002) Biophys. J. , vol.83 , pp. 1184-1193
    • Bacia, K.1    Majoul, I.V.2    Schwille, P.3
  • 5
    • 0141884811 scopus 로고    scopus 로고
    • Excitation saturation in two-photon fluorescence correlation spectroscopy
    • Berland, K. M., and G. Shen. 2003. Excitation saturation in two-photon fluorescence correlation spectroscopy. Appl. Opt. 42:5566-5576.
    • (2003) Appl. Opt. , vol.42 , pp. 5566-5576
    • Berland, K.M.1    Shen, G.2
  • 6
    • 0028869663 scopus 로고
    • Two-photon fluorescence correlation spectroscopy: Method and application to the intracellular environment
    • Berland, K. M., P. T. So, and E. Gratton. 1995. Two-photon fluorescence correlation spectroscopy: method and application to the intracellular environment. Biophys. J. 68:694-701.
    • (1995) Biophys. J. , vol.68 , pp. 694-701
    • Berland, K.M.1    So, P.T.2    Gratton, E.3
  • 8
    • 0344603641 scopus 로고    scopus 로고
    • The photon counting histogram in fluorescence fluctuation spectroscopy
    • Chen, Y., J. D. Müller, P. T. 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.3    Gratton, E.4
  • 10
    • 0346734134 scopus 로고    scopus 로고
    • Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy
    • Chen, Y., L. N. Wei, and J. D. Müller. 2003. Probing protein oligomerization in living cells with fluorescence fluctuation spectroscopy. Proc. Natl. Acad. Sci. USA. 100:15492-15497.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15492-15497
    • Chen, Y.1    Wei, L.N.2    Müller, J.D.3
  • 11
    • 0035678612 scopus 로고    scopus 로고
    • Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two-photon excitation
    • Dittrich, P. S., and P. Schwille. 2001. Photobleaching and stabilization of fluorophores used for single-molecule analysis with one- and two-photon excitation. Appl. Phys. B. 73:829-837.
    • (2001) Appl. Phys. B , vol.73 , pp. 829-837
    • Dittrich, P.S.1    Schwille, P.2
  • 12
    • 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
  • 13
    • 0016379116 scopus 로고
    • Fluorescence correlation spectroscopy. I. Conceptual basis and theory
    • Elson, E. L., and D. Magde. 1974. Fluorescence correlation spectroscopy. I. Conceptual basis and theory. Biopolymers. 13:1-27.
    • (1974) Biopolymers , vol.13 , pp. 1-27
    • Elson, E.L.1    Magde, D.2
  • 15
    • 0033635801 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in small cytosolic compartments depends critically on the diffusion model used
    • Gennerich, A., and D. Schild. 2000. Fluorescence correlation spectroscopy in small cytosolic compartments depends critically on the diffusion model used. Biophys. J. 79:3294-3306.
    • (2000) Biophys. J. , vol.79 , pp. 3294-3306
    • Gennerich, A.1    Schild, D.2
  • 16
    • 0347319178 scopus 로고    scopus 로고
    • Triple-color coincidence analysis: One step further in following higher order molecular complex formation
    • Heinze, K. G., M. Jahnz, and P. Schwille. 2004. Triple-color coincidence analysis: one step further in following higher order molecular complex formation. Biophys. J. 86:506-516.
    • (2004) Biophys. J. , vol.86 , pp. 506-516
    • Heinze, K.G.1    Jahnz, M.2    Schwille, P.3
  • 17
    • 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
  • 18
    • 0035997377 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II: The role of structure and autoregulation in cellular function
    • 2+/calmodulin- dependent protein kinase II: the role of structure and autoregulation in cellular function. Annu. Rev. Biochem. 71:473-510.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 473-510
    • Hudmon, A.1    Schulman, H.2
  • 19
    • 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
  • 20
    • 0026020849 scopus 로고
    • Calmodulin-dependent protein kinase II. Kinetic studies on the interaction with substrates and calmodulin
    • Katoh, T., and H. Fujisawa. 1991. Calmodulin-dependent protein kinase II. Kinetic studies on the interaction with substrates and calmodulin. Biochim. Biophys. Acta. 1091:205-212.
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 205-212
    • Katoh, T.1    Fujisawa, H.2
  • 21
    • 0346458699 scopus 로고    scopus 로고
    • Intracellular calmodulin availability accessed with two-photon cross-correlation
    • Kim, S. A., K. G. Heinze, M. N. Waxham, and P. Schwille. 2004. Intracellular calmodulin availability accessed with two-photon cross-correlation. Proc. Natl. Acad. Sci. USA. 101:105-110.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 105-110
    • Kim, S.A.1    Heinze, K.G.2    Waxham, M.N.3    Schwille, P.4
  • 23
    • 0037125999 scopus 로고    scopus 로고
    • A protease assay for two-photon cross-correlation 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 cross-correlation 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
  • 24
    • 0032553432 scopus 로고    scopus 로고
    • Identification of domains essential for the assembly of calcium/calmodulin-dependent protein kinase II holoenzymes
    • Kolb, S. J., A. Hudmon, T. R. Ginsberg, and M. N. Waxham. 1998. Identification of domains essential for the assembly of calcium/calmodulin- dependent protein kinase II holoenzymes. J. Biol. Chem. 273:31555-31564.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31555-31564
    • Kolb, S.J.1    Hudmon, A.2    Ginsberg, T.R.3    Waxham, M.N.4
  • 25
    • 0034640259 scopus 로고    scopus 로고
    • Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains
    • Kolodziej, S. J., A. Hudmon, M. N. Waxham, and J. K. Stoops. 2000. Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains. J. Biol. Chem. 275:14354-14359.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14354-14359
    • Kolodziej, S.J.1    Hudmon, A.2    Waxham, M.N.3    Stoops, J.K.4
  • 26
    • 0021646776 scopus 로고
    • 2+/calmodulin- dependent protein kinase from Rat brain
    • 2+/calmodulin-dependent protein kinase from Rat brain. Biochemistry. 23:5495-5504.
    • (1984) Biochemistry , vol.23 , pp. 5495-5504
    • Kuret, J.1    Schulman, H.2
  • 27
    • 85030747053 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy to examine initial steps of IgE receptor signaling
    • Abstr.
    • Larson, D. R., J. A. Gosse, D. A. Holowka, B. A. Baird, and W. W. Webb. 2004. Dual-color fluorescence cross-correlation spectroscopy to examine initial steps of IgE receptor signaling. Biophys. J. 86:10a (Abstr.)
    • (2004) Biophys. J. , vol.86
    • Larson, D.R.1    Gosse, J.A.2    Holowka, D.A.3    Baird, B.A.4    Webb, W.W.5
  • 29
  • 30
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioral memory
    • Lisman, J., H. Schulman, and H. Cline. 2002. The molecular basis of CaMKII function in synaptic and behavioral memory. Nat. Rev. Neurosci. 3:175-190.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 31
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system-measurement by fluorescence correlation spectroscopy
    • Magde, D., E. L. Elson, and W. W. Webb. 1972. Thermodynamic fluctuations in a reacting system-measurement 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
  • 32
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures
    • Meador, W. E., A. R. Means, and F. A. Quiocho. 1993. Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Science. 262:1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 33
    • 0037452553 scopus 로고    scopus 로고
    • a receptors on hippocampal neurons monitored by fluorescence correlation spectroscopy
    • A receptors on hippocampal neurons monitored by fluorescence correlation spectroscopy. Biochemistry. 42:1667-1672.
    • (2003) Biochemistry , vol.42 , pp. 1667-1672
    • Meissner, O.1    Haberlein, H.2
  • 34
    • 0026718175 scopus 로고
    • Calmodulin trapping by calcium-calmodulin-dependent protein kinase
    • Meyer, T., P. I. Hanson, L. Stryer, and H. Schulman. 1992. Calmodulin trapping by calcium-calmodulin-dependent protein kinase. Science. 256:1199-1202.
    • (1992) Science , vol.256 , pp. 1199-1202
    • Meyer, T.1    Hanson, P.I.2    Stryer, L.3    Schulman, H.4
  • 35
    • 0001703536 scopus 로고    scopus 로고
    • Synthesis and photophysical properties of new conjugated fluorophores designed for two-photon-excited fluorescence
    • Mongin, O., L. Porres, L. Moreaux, J. Mertz, and M. Blanchard-Desce. 2002. Synthesis and photophysical properties of new conjugated fluorophores designed for two-photon-excited fluorescence. Org. Lett. 4:719-722.
    • (2002) Org. Lett. , vol.4 , pp. 719-722
    • Mongin, O.1    Porres, L.2    Moreaux, L.3    Mertz, J.4    Blanchard-Desce, M.5
  • 36
    • 0029965541 scopus 로고    scopus 로고
    • A peptide model for calmodulin trapping by calcium/calmodulin-dependent protein kinase II
    • Putkey, J. A., and M. N. Waxham. 1996. A peptide model for calmodulin trapping by calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 271:29619-29623.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29619-29623
    • Putkey, J.A.1    Waxham, M.N.2
  • 37
    • 0034847288 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for monitoring the kinetics of enzyme-catalyzed reactions
    • Rarbach, M., U. Kettling, A. Koltermann, and M. Eigen. 2001. Dual-color fluorescence cross-correlation spectroscopy for monitoring the kinetics of enzyme-catalyzed reactions. Methods. 24:104-116.
    • (2001) Methods , vol.24 , pp. 104-116
    • Rarbach, M.1    Kettling, U.2    Koltermann, A.3    Eigen, M.4
  • 38
    • 0000446663 scopus 로고    scopus 로고
    • Highly active two-photon dyes: Design, synthesis and characterization towards applications
    • Reinhard, B. A. 1998. Highly active two-photon dyes: design, synthesis and characterization towards applications. Chem. Mater. 10:1863-1874.
    • (1998) Chem. Mater. , vol.10 , pp. 1863-1874
    • Reinhard, B.A.1
  • 39
    • 0035778299 scopus 로고    scopus 로고
    • Cross-correlation analysis in FCS
    • E.L. Elson and R. Rigler, editors. Springer, Berlin, Germany
    • Schwille, P. 2001. Cross-correlation analysis in FCS. In Fluorescence Correlation Spectroscopy. Theory and Applications, E.L. Elson and R. Rigler, editors. Springer, Berlin, Germany. 360-378.
    • (2001) Fluorescence Correlation Spectroscopy. Theory and Applications , pp. 360-378
    • Schwille, P.1
  • 40
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation
    • Schwille, P., U. Haupts, S. Maiti, and W. W. Webb. 1999. Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one- and two-photon excitation. Biophys. J. 77:2251-2265.
    • (1999) Biophys. J. , vol.77 , pp. 2251-2265
    • Schwille, P.1    Haupts, U.2    Maiti, S.3    Webb, W.W.4
  • 41
    • 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
  • 42
    • 0347810033 scopus 로고    scopus 로고
    • Singlet molecular oxygen photosensitized by Rhodamine dyes: Correlation with photophysical properties of the sensitizers
    • Stracke, F., M. Heupel, and E. Thiel. 1999. Singlet molecular oxygen photosensitized by Rhodamine dyes: correlation with photophysical properties of the sensitizers. J. Photochem. Photobiol. A Chem. 126:51-58.
    • (1999) J. Photochem. Photobiol. A Chem. , vol.126 , pp. 51-58
    • Stracke, F.1    Heupel, M.2    Thiel, E.3
  • 43
    • 0027157723 scopus 로고
    • 2+/calmodulin-dependent protein kinase II with calmodulin
    • 2+/calmodulin-dependent protein kinase II with calmodulin. Biochim. Biophys. Acta. 1177:270-274.
    • (1993) Biochim. Biophys. Acta , vol.1177 , pp. 270-274
    • Sugiura, H.1    Yamauchi, T.2
  • 44
    • 0019366933 scopus 로고
    • Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy
    • Thompson, N. L., T. P. Burghardt, and D. Axelrod. 1981. Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy. Biophys. J. 33:435-454.
    • (1981) Biophys. J. , vol.33 , pp. 435-454
    • Thompson, N.L.1    Burghardt, T.P.2    Axelrod, D.3
  • 46
    • 84941102391 scopus 로고    scopus 로고
    • Calmodulin and calcium signal transduction: An introduction
    • L.J. van Eldik and D.M. Watterson, editors. Academic Press, New York
    • van Eldik, L. J., and D. M. Watterson. 1998. Calmodulin and calcium signal transduction: an introduction. In Calmodulin and Signal Transduction. L.J. van Eldik and D.M. Watterson, editors. Academic Press, New York. 1-15.
    • (1998) Calmodulin and Signal Transduction , pp. 1-15
    • Van Eldik, L.J.1    Watterson, D.M.2
  • 48
    • 0036106455 scopus 로고    scopus 로고
    • Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy
    • Weidemann, T., M. Wachsmuth, M. Tewes, K. Rippe, and J. Langowski. 2002. Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy. Single Mol. 3:49-61.
    • (2002) Single Mol. , vol.3 , pp. 49-61
    • Weidemann, T.1    Wachsmuth, M.2    Tewes, M.3    Rippe, K.4    Langowski, J.5
  • 49
    • 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
  • 50
    • 0024789308 scopus 로고
    • Expression and characterization of calmodulin-dependent protein kinase II from cloned cDNAs in Chinese Hamster ovary cells
    • Yamauchi, T., S. Ohsako, and T. Deguchi. 1989. Expression and characterization of calmodulin-dependent protein kinase II from cloned cDNAs in Chinese Hamster ovary cells. J. Biol. Chem. 264:19108-19116.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19108-19116
    • Yamauchi, T.1    Ohsako, S.2    Deguchi, T.3
  • 51
    • 1842637652 scopus 로고    scopus 로고
    • New caged Coumarin fluorophores with extraordinary uncaging cross section suitable for biological imaging applications
    • Zhao, Y., Q. Zheng, K. Dakin, K. Xu, M. L. Martinez, and W.-H. Li. 2004. New caged Coumarin fluorophores with extraordinary uncaging cross section suitable for biological imaging applications. J. Am. Chem. Soc. 126:4653-4663.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4653-4663
    • Zhao, Y.1    Zheng, Q.2    Dakin, K.3    Xu, K.4    Martinez, M.L.5    Li, W.-H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.