메뉴 건너뛰기




Volumn , Issue SUPPL.62, 2012, Pages

Analysis of protein and lipid dynamics using confocal fluorescence recovery after photobleaching (FRAP)

Author keywords

Confocal laser scanning microscopes; Diffusion; Fluorescence microscopy; FRAP; GFP; Protein trafficking

Indexed keywords

LIPID; MEMBRANE PROTEIN; COMPLEMENTARY DNA; PROTEIN;

EID: 84874147884     PISSN: 19349297     EISSN: 19349300     Source Type: Journal    
DOI: 10.1002/0471142956.cy0219s62     Document Type: Article
Times cited : (66)

References (67)
  • 1
    • 70349207749 scopus 로고    scopus 로고
    • Single-particle tracking methods for the study of membrane receptors dynamics
    • Alcor, D., Gouzer, G., and Triller, A. 2009. Single-particle tracking methods for the study of membrane receptors dynamics. Eur. J. Neurosci. 30:987-997.
    • (2009) Eur. J. Neurosci. , vol.30 , pp. 987-997
    • Alcor, D.1    Gouzer, G.2    Triller, A.3
  • 3
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Biophys. J.
    • Axelrod, D., Koppel, D.E., Schlessinger, J., Elson, E., and Webb, W.W. 1976. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J.16:1055-1069.
    • (1976) , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 4
    • 0037282643 scopus 로고    scopus 로고
    • A dynamic view of cellular processes by in vivo fluorescence auto-and cross-correlation spectroscopy
    • Bacia, K. and Schwille, P. 2003. A dynamic view of cellular processes by in vivo fluorescence auto-and cross-correlation spectroscopy. Methods 29:74-85.
    • (2003) Methods , vol.29 , pp. 74-85
    • Bacia, K.1    Schwille, P.2
  • 5
    • 78650057290 scopus 로고    scopus 로고
    • Fluorescence perturbation techniques to study mobility and molecular dynamics of proteins in live cells: FRAP, photoactivation, photoconversion, and FLIP
    • pdb top
    • Bancaud, A., Huet, S., Rabut, G., and Ellenberg, J. 2010. Fluorescence perturbation techniques to study mobility and molecular dynamics of proteins in live cells: FRAP, photoactivation, photoconversion, and FLIP. Cold Spring Harb. Protoc. 2010:pdb top90.
    • (2010) Cold Spring Harb. Protoc. , vol.2010 , pp. 90
    • Bancaud, A.1    Huet, S.2    Rabut, G.3    Ellenberg, J.4
  • 6
    • 4644243088 scopus 로고    scopus 로고
    • Intracellular macromolecular mobility measured by fluorescence recovery after photobleaching with confocal laser scanning microscopes
    • Braga, J., Desterro, J.M.P., and Carmo-Fonseca, M. 2004. Intracellular macromolecular mobility measured by fluorescence recovery after photobleaching with confocal laser scanning microscopes. Mol. Biol. Cell 15:4749-4760.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4749-4760
    • Braga, J.1    Desterro, J.M.P.2    Carmo-Fonseca, M.3
  • 7
    • 7444240826 scopus 로고    scopus 로고
    • Characterizing fluorescence recovery curves for nuclear proteins undergoing binding events
    • Carrero, G., Crawford, E., Hendzel, M.J., and de Vries, G. 2004. Characterizing fluorescence recovery curves for nuclear proteins undergoing binding events. Bull. Math. Biol. 66:1515-1545.
    • (2004) Bull. Math. Biol. , vol.66 , pp. 1515-1545
    • Carrero, G.1    Crawford, E.2    Hendzel, M.J.3    de Vries, G.4
  • 8
    • 33746303104 scopus 로고    scopus 로고
    • Methods to measure the lateral diffusion of membrane lipids and proteins
    • Chen, Y., Lagerholm, B.C., Yang, B., and Jacobson, K. 2006. Methods to measure the lateral diffusion of membrane lipids and proteins. Methods 39:147-153.
    • (2006) Methods , vol.39 , pp. 147-153
    • Chen, Y.1    Lagerholm, B.C.2    Yang, B.3    Jacobson, K.4
  • 10
    • 84871915537 scopus 로고    scopus 로고
    • Mechanisms underlying the confined diffusion of cholera toxin B-subunit in intact cell membranes
    • Day, C.A. and Kenworthy, A.K. 2012. Mechanisms underlying the confined diffusion of cholera toxin B-subunit in intact cell membranes. PLoS One 7:e34923.
    • (2012) PLoS On , vol.7
    • Day, C.A.1    Kenworthy, A.K.2
  • 11
    • 70349515538 scopus 로고    scopus 로고
    • The fluorescent protein palette: Tools for cellular imaging
    • Day, R.N. and Davidson, M.W. 2009. The fluorescent protein palette: Tools for cellular imaging. Chem. Soc. Rev. 38:2887-2921.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2887-2921
    • Day, R.N.1    Davidson, M.W.2
  • 12
    • 0033059157 scopus 로고    scopus 로고
    • Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum
    • Dayel, M.J., Hom, E.F., andVerkman, A.S. 1999. Diffusion of green fluorescent protein in the aqueous-phase lumen of endoplasmic reticulum. Biophys. J. 76:2843-2851.
    • (1999) Biophys. J. , vol.76 , pp. 2843-2851
    • Dayel, M.J.1    Hom, E.F.2    Verkman, A.S.3
  • 13
    • 0030832226 scopus 로고    scopus 로고
    • On/offblinking and switching behaviour of single molecules of green fluorescent protein
    • Dickson, R.M., Cubitt, A.B., Tsien, R.Y., andMoerner, W.E. 1997. On/offblinking and switching behaviour of single molecules of green fluorescent protein. Nature 388:355-358.
    • (1997) Nature , vol.388 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 14
    • 78349255372 scopus 로고    scopus 로고
    • Nucleocytoplasmic distribution and dynamics of the autophagosome marker EGFP-LC3
    • Drake, K.R., Kang, M., and Kenworthy, A.K. 2010. Nucleocytoplasmic distribution and dynamics of the autophagosome marker EGFP-LC3. PLoS One 5:e9806.
    • (2010) PLoS One , vol.5
    • Drake, K.R.1    Kang, M.2    Kenworthy, A.K.3
  • 16
    • 0036160561 scopus 로고    scopus 로고
    • Fluorescence localization after photobleaching (FLAP): A new method for studying protein dynamics in living cells
    • Dunn, G.A., Dobbie, I.M., Monypenny, J., Holt, M.R., and Zicha, D. 2002. Fluorescence localization after photobleaching (FLAP): A new method for studying protein dynamics in living cells. J. Microsc. 205:109-112.
    • (2002) J. Microsc. , vol.205 , pp. 109-112
    • Dunn, G.A.1    Dobbie, I.M.2    Monypenny, J.3    Holt, M.R.4    Zicha, D.5
  • 17
    • 0022196958 scopus 로고
    • Fluorescence correlation spectroscopy and photobleaching recovery
    • Elson, E.L. 1985. Fluorescence correlation spectroscopy and photobleaching recovery. Ann. Rev. Phys. Chem. 36:379-406.
    • (1985) Ann. Rev. Phys. Chem. , vol.36 , pp. 379-406
    • Elson, E.L.1
  • 18
    • 16544368010 scopus 로고    scopus 로고
    • Quick tour of fluorescence correlation spectroscopy from its inception
    • Elson, E.L. 2004. Quick tour of fluorescence correlation spectroscopy from its inception. J. Biomed. Opt. 9:857-864.
    • (2004) J. Biomed. Opt. , vol.9 , pp. 857-864
    • Elson, E.L.1
  • 19
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
    • Feder, T.J., Brust-Mascher, I., Slattery, J.P., Baird, B., and Webb, W.W. 1996. Constrained diffusion or immobile fraction on cell surfaces: A new interpretation. Biophys. J. 70:2767-2773.
    • (1996) Biophys. J. , vol.70 , pp. 2767-2773
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 20
    • 23244457196 scopus 로고    scopus 로고
    • Ras diffusion is sensitive to plasma membrane viscosity
    • Goodwin, J.S., Drake, K.R., Remmert, C.L., and Kenworthy, A.K. 2005a. Ras diffusion is sensitive to plasma membrane viscosity. Biophys. J. 89:1398-1410.
    • (2005) Biophys. J. , vol.89 , pp. 1398-1410
    • Goodwin, J.S.1    Drake, K.R.2    Remmert, C.L.3    Kenworthy, A.K.4
  • 22
    • 55549127575 scopus 로고    scopus 로고
    • Fluorescence recovery kinetic analysis of gamma-tubulin binding to the mitotic spindle
    • Hallen, M.A., Ho, J., Yankel, C.D., and Endow, S.A. 2008. Fluorescence recovery kinetic analysis of gamma-tubulin binding to the mitotic spindle. Biophys. J. 95:3048-3058.
    • (2008) Biophys. J. , vol.95 , pp. 3048-3058
    • Hallen, M.A.1    Ho, J.2    Yankel, C.D.3    Endow, S.A.4
  • 23
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Novel variations of an established technique
    • Haustein, E. and Schwille, P. 2007. Fluorescence correlation spectroscopy: Novel variations of an established technique. Annu. Rev. Biophys. Biomol. Struct. 36:151-169.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 25
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson, K., Sheets, E.D., and Simson, R. 1995. Revisiting the fluid mosaic model of membranes. Science 268:1441-1442.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 27
    • 47749106407 scopus 로고    scopus 로고
    • A closed-form analytic expression for FRAP formula for the binding diffusion model
    • Kang, M. and Kenworthy, A.K. 2008. A closed-form analytic expression for FRAP formula for the binding diffusion model. Biophys. J. 95:L13-L15.
    • (2008) Biophys. J. , vol.95
    • Kang, M.1    Kenworthy, A.K.2
  • 28
    • 78349258393 scopus 로고    scopus 로고
    • Complex applications of simple FRAP on membranes
    • In Biomembrane Frontiers: Nanstructures, Models and the Design of Life, (R. Faller, T. Jue, M.L. Longo, andS.H. Risbud, eds.), New York
    • Kang, M. and Kenworthy, A.K. 2009. Complex applications of simple FRAP on membranes. In Biomembrane Frontiers: Nanstructures, Models and the Design of Life, Vol 2 (R. Faller, T. Jue, M.L. Longo, andS.H. Risbud, eds.) pp. 187-221. Humana Press, New York.
    • (2009) Humana Press , vol.4 , pp. 187-221
    • Kang, M.1    Kenworthy, A.K.2
  • 29
    • 70349589255 scopus 로고    scopus 로고
    • A generalization of theory for two-dimensional fluorescence recovery after photobleaching applicable to confocal laser scanning microscopes
    • Kang, M., Day, C.A., Drake, K., Kenworthy, A.K., and DiBenedetto, E. 2009. A generalization of theory for two-dimensional fluorescence recovery after photobleaching applicable to confocal laser scanning microscopes. Biophys. J. 97:1501-1511.
    • (2009) Biophys. J. , vol.97 , pp. 1501-1511
    • Kang, M.1    Day, C.A.2    Drake, K.3    Kenworthy, A.K.4    DiBenedetto, E.5
  • 30
    • 78349238937 scopus 로고    scopus 로고
    • A quantitative approach to analyze binding diffusion kinetics by confocal FRAP
    • Kang, M., Day, C.A., DiBenedetto, E., and Kenworthy, A.K. 2010. A quantitative approach to analyze binding diffusion kinetics by confocal FRAP. Biophys. J. 99:2737-2747.
    • (2010) Biophys. J. , vol.99 , pp. 2737-2747
    • Kang, M.1    Day, C.A.2    DiBenedetto, E.3    Kenworthy, A.K.4
  • 31
    • 84873254599 scopus 로고    scopus 로고
    • Simplified equation to extract diffusion coefficients from confocal FRAP data
    • Kang, M., Day, C.A., Kenworthy, A.K., and DiBenedetto, E. 2012. Simplified equation to extract diffusion coefficients from confocal FRAP data. Traffic. In press.
    • (2012) Traffic. In press
    • Kang, M.1    Day, C.A.2    Kenworthy, A.K.3    DiBenedetto, E.4
  • 32
    • 33748969315 scopus 로고    scopus 로고
    • Fluorescence-based methods to image palmitoylated proteins
    • Kenworthy, A.K. 2006. Fluorescence-based methods to image palmitoylated proteins. Methods 40:198-205.
    • (2006) Methods , vol.40 , pp. 198-205
    • Kenworthy, A.K.1
  • 33
    • 58149199087 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching studies of lipid rafts
    • T. McIntosh, ed. Humana Press, Totowa, N.J
    • Kenworthy, A.K. 2007. Fluorescence recovery after photobleaching studies of lipid rafts. In Lipid Rafts, Vol. 398 (T. McIntosh, ed.). Humana Press, Totowa, N.J.
    • (2007) Lipid Rafts , vol.398
    • Kenworthy, A.K.1
  • 35
    • 36949010581 scopus 로고    scopus 로고
    • Advances in image correlation spectroscopy: measuring number densities, aggregation states, and dynamics of fluorescently labeled macromolecules in cells
    • Kolin, D.L. andWiseman, P.W. 2007. Advances in image correlation spectroscopy: measuring number densities, aggregation states, and dynamics of fluorescently labeled macromolecules in cells. Cell Biochem. Biophys. 49:141-164.
    • (2007) Cell Biochem. Biophys. , vol.49 , pp. 141-164
    • Kolin, D.L.1    Wiseman, P.W.2
  • 36
    • 84861434988 scopus 로고    scopus 로고
    • Imaging protein complex formation in the autophagy pathway: Analysis of the interaction of LC3 and Atg4B(C74A) in live cells using F"orster resonance energy transfer and fluorescence recovery after photobleaching
    • Kraft, L.J. and Kenworthy, A.K. 2012. Imaging protein complex formation in the autophagy pathway: Analysis of the interaction of LC3 and Atg4B(C74A) in live cells using F"orster resonance energy transfer and fluorescence recovery after photobleaching. J. Biomed. Opt. 17:011008.
    • (2012) J. Biomed. Opt. , vol.17 , pp. 011008
    • Kraft, L.J.1    Kenworthy, A.K.2
  • 39
    • 77951923713 scopus 로고    scopus 로고
    • Hierarchical organization of the plasma membrane: Investigations by single-molecule tracking vs fluorescence correlation spectroscopy
    • Kusumi, A., Shirai, Y.M., Koyama-Honda, I., Suzuki, K.G., and Fujiwara, T.K. 2010. Hierarchical organization of the plasma membrane: Investigations by single-molecule tracking vs. fluorescence correlation spectroscopy. FEBS Lett. 584:1814-1823.
    • (2010) FEBS Lett. , vol.584 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.4    Fujiwara, T.K.5
  • 41
    • 34548305123 scopus 로고    scopus 로고
    • Exploring dynamics in living cells by tracking single particles
    • Levi, V. and Gratton, E. 2007. Exploring dynamics in living cells by tracking single particles. Cell Biochem. Biophys. 48:1-15.
    • (2007) Cell Biochem. Biophys. , vol.48 , pp. 1-15
    • Levi, V.1    Gratton, E.2
  • 42
  • 44
    • 0042338695 scopus 로고    scopus 로고
    • Photobleaching and photoactivation: Following protein dynamics in living cells
    • Lippincott-Schwartz, J., Altan-Bonnet, N., and Patterson, G.H. 2003. Photobleaching and photoactivation: Following protein dynamics in living cells. Nat. Cell Biol. Suppl.:S7-S14.
    • (2003) Nat. Cell Biol. , Issue.SUPPL
    • Lippincott-Schwartz, J.1    Altan-Bonnet, N.2    Patterson, G.H.3
  • 47
    • 37249044282 scopus 로고    scopus 로고
    • Quantitative FRAP in analysis of molecular binding dynamics in vivo
    • McNally, J.G. 2008. Quantitative FRAP in analysis of molecular binding dynamics in vivo. Methods Cell Biol. 85:329-351.
    • (2008) Methods Cell Biol. , vol.85 , pp. 329-351
    • McNally, J.G.1
  • 48
    • 43149119497 scopus 로고    scopus 로고
    • Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching
    • Mueller, F., Wach, P., and McNally, J.G. 2008. Evidence for a common mode of transcription factor interaction with chromatin as revealed by improved quantitative fluorescence recovery after photobleaching. Biophys. J. 94:3323-3339.
    • (2008) Biophys. J. , vol.94 , pp. 3323-3339
    • Mueller, F.1    Wach, P.2    McNally, J.G.3
  • 49
    • 77954815037 scopus 로고    scopus 로고
    • FRAP and kinetic modeling in the analysis of nuclear protein dynamics: What do we really know? Curr
    • Mueller, F., Mazza, D., Stasevich, T.J., and McNally, J.G. 2010. FRAP and kinetic modeling in the analysis of nuclear protein dynamics: What do we really know? Curr. Opin. Cell Biol. 22:403-411.
    • (2010) Opin. Cell Biol. , vol.22 , pp. 403-411
    • Mueller, F.1    Mazza, D.2    Stasevich, T.J.3    McNally, J.G.4
  • 50
    • 84859378171 scopus 로고    scopus 로고
    • Minimizing the impact of photoswitching of fluorescent proteins on FRAP analysis
    • Mueller, F., Morisaki, T., Mazza, D., and McNally, J.G. 2012. Minimizing the impact of photoswitching of fluorescent proteins on FRAP analysis. Biophys. J. 102:1656-1665.
    • (2012) Biophys. J. , vol.102 , pp. 1656-1665
    • Mueller, F.1    Morisaki, T.2    Mazza, D.3    McNally, J.G.4
  • 51
    • 57549090632 scopus 로고    scopus 로고
    • Photoactivation and imaging of photoactivatable fluorescent proteins
    • Patterson, G.H. 2008. Photoactivation and imaging of photoactivatable fluorescent proteins. Curr. Protoc. Cell Biol. 38:21.6.1-21.6.10.
    • (2008) Curr. Protoc. Cell Biol. , vol.38
    • Patterson, G.H.1
  • 52
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson, G.H. and Lippincott-Schwartz, J. 2002. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297:1873-1877.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 53
    • 0021100162 scopus 로고
    • Nuclear envelope permeability measured by fluorescence microphotolysis of single liver cell nuclei
    • Peters, R. 1983. Nuclear envelope permeability measured by fluorescence microphotolysis of single liver cell nuclei. J. Biol. Chem. 258:11427-11429.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11427-11429
    • Peters, R.1
  • 54
    • 77957043923 scopus 로고    scopus 로고
    • Scanning FCS for the characterization of protein dynamics in live cells
    • Petrasek, Z., Ries, J., and Schwille, P. 2010. Scanning FCS for the characterization of protein dynamics in live cells. Methods Enzymol. 472:317-343.
    • (2010) Methods Enzymol. , vol.472 , pp. 317-343
    • Petrasek, Z.1    Ries, J.2    Schwille, P.3
  • 55
    • 33750417953 scopus 로고    scopus 로고
    • 2-color photobleaching experiments reveal distinct intracellular dynamics of two components of the Hsp90 complex
    • Picard, D., Suslova, E., and Briand, P.A. 2006. 2-color photobleaching experiments reveal distinct intracellular dynamics of two components of the Hsp90 complex. Exp. Cell Res. 312:3949-3958.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3949-3958
    • Picard, D.1    Suslova, E.2    Briand, P.A.3
  • 56
    • 0033168491 scopus 로고    scopus 로고
    • Use of caged fluorochromes to track macromolecular movement in living cells
    • Politz, J.C. 1999. Use of caged fluorochromes to track macromolecular movement in living cells. Trends Cell Biol. 9:284-287.
    • (1999) Trends Cell Biol. , vol.9 , pp. 284-287
    • Politz, J.C.1
  • 57
    • 0034976147 scopus 로고    scopus 로고
    • From fixed to FRAP: Measuring protein mobility and activity in living cells
    • Reits, E.A. and Neefjes, J.J. 2001. From fixed to FRAP: Measuring protein mobility and activity in living cells. Nat. Cell Biol. 3:E145-E147.
    • (2001) Nat. Cell Biol. , vol.3
    • Reits, E.A.1    Neefjes, J.J.2
  • 59
    • 68049110292 scopus 로고    scopus 로고
    • Modulation of nucleocytoplasmic trafficking by retention in cytoplasm or nucleus
    • Roth, D.M., Harper, I., Pouton, C.W., and Jans, D.A. 2009. Modulation of nucleocytoplasmic trafficking by retention in cytoplasm or nucleus. J. Cell. Biochem. 107:1160-1167.
    • (2009) J. Cell. Biochem. , vol.107 , pp. 1160-1167
    • Roth, D.M.1    Harper, I.2    Pouton, C.W.3    Jans, D.A.4
  • 61
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: Applications to membrane dynamics
    • Saxton, M.J. and Jacobson, K. 1997. Single-particle tracking: Applications to membrane dynamics. Annu. Rev. Biophys. Biomol. Struct. 26:373-399.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 62
    • 18244362575 scopus 로고    scopus 로고
    • Reversible photobleaching of enhanced green fluorescent proteins
    • Sinnecker, D., Voigt, P., Hellwig, N., and Schaefer, M. 2005. Reversible photobleaching of enhanced green fluorescent proteins. Biochemistry 44:7085-7094.
    • (2005) Biochemistry , vol.44 , pp. 7085-7094
    • Sinnecker, D.1    Voigt, P.2    Hellwig, N.3    Schaefer, M.4
  • 63
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • Sprague, B.L., Pego, R.L., Stavreva, D.A., and McNally, J.G. 2004. Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys. J. 86:3473-3495.
    • (2004) Biophys. J. , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 64
    • 0019366933 scopus 로고
    • Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy
    • Thompson, N.L., Burghardt, T.P., and Axelrod, D. 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
  • 65
    • 34347240880 scopus 로고    scopus 로고
    • New fluorescent tools for watching nanometer-scale conformational changes of single molecules
    • Toprak, E. and Selvin, P.R. 2007. New fluorescent tools for watching nanometer-scale conformational changes of single molecules. Annu. Rev. Biophys. Biomol. Struct. 36:349-369.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 349-369
    • Toprak, E.1    Selvin, P.R.2
  • 66
    • 2142762991 scopus 로고    scopus 로고
    • Probing plasma membrane microdomains in cowpea protoplasts using lipidated GFP-fusion proteins and multimode FRET microscopy
    • Vermeer, J.E., VanMunster, E.B., Vischer, N.O., and Gadella, T.W. Jr. 2004. Probing plasma membrane microdomains in cowpea protoplasts using lipidated GFP-fusion proteins and multimode FRET microscopy. J. Microsc. 214:190-200.
    • (2004) J. Microsc. , vol.214 , pp. 190-200
    • Vermeer, J.E.1    VanMunster, E.B.2    Vischer, N.O.3    Gadella, T.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.