메뉴 건너뛰기




Volumn 12, Issue C, 2010, Pages 21-40

Measuring colocalization by dual color single molecule imaging. Thresholds, error rates, and sensitivity

Author keywords

Association; Diffusion; Fluorescence; Plasma membrane; Protein interaction; Single molecule microscopy; Single particle tracking

Indexed keywords


EID: 77958138174     PISSN: 15544516     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381266-7.00002-X     Document Type: Book
Times cited : (7)

References (77)
  • 1
    • 38549111882 scopus 로고    scopus 로고
    • Informatics and computational strategies for the study of lipids
    • Yetukuri L., et al. Informatics and computational strategies for the study of lipids. Mol. Biosyst. 2008, 4(2):121-127.
    • (2008) Mol. Biosyst. , vol.4 , Issue.2 , pp. 121-127
    • Yetukuri, L.1
  • 2
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., von Heijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 1998, 7(4):1029-1038.
    • (1998) Protein Sci. , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    von Heijne, G.2
  • 3
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • Kusumi A., Koyama-Honda I., Suzuki K. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic 2004, 5(4):213-230.
    • (2004) Traffic , vol.5 , Issue.4 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 4
    • 57049187658 scopus 로고    scopus 로고
    • Micropatterning for quantitative analysis of protein-protein interactions in living cells
    • Schwarzenbacher M., et al. Micropatterning for quantitative analysis of protein-protein interactions in living cells. Nat. Methods 2008, 5(12):1053-1060.
    • (2008) Nat. Methods , vol.5 , Issue.12 , pp. 1053-1060
    • Schwarzenbacher, M.1
  • 5
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte S., Cordelieres F.P. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 2006, 224(Pt 3):213-232.
    • (2006) J. Microsc. , vol.224 , Issue.PART 3 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 6
    • 0242574490 scopus 로고    scopus 로고
    • Co-localization analysis of complex formation among membrane proteins by computerized fluorescence microscopy: application to immunofluorescence co-patching studies
    • Lachmanovich E., et al. Co-localization analysis of complex formation among membrane proteins by computerized fluorescence microscopy: application to immunofluorescence co-patching studies. J. Microsc. 2003, 212(Pt 2):122-131.
    • (2003) J. Microsc. , vol.212 , Issue.PART 2 , pp. 122-131
    • Lachmanovich, E.1
  • 7
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and quantitative measurement of protein-protein colocalization in live cells
    • Costes S.V., et al. Automatic and quantitative measurement of protein-protein colocalization in live cells. Biophys. J. 2004, 86(6):3993-4003.
    • (2004) Biophys. J. , vol.86 , Issue.6 , pp. 3993-4003
    • Costes, S.V.1
  • 8
    • 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., Wiseman P.W. Advances in image correlation spectroscopy: measuring number densities, aggregation states, and dynamics of fluorescently labeled macromolecules in cells. Cell Biochem. Biophys. 2007, 49(3):141-164.
    • (2007) Cell Biochem. Biophys. , vol.49 , Issue.3 , pp. 141-164
    • Kolin, D.L.1    Wiseman, P.W.2
  • 9
    • 23244440556 scopus 로고    scopus 로고
    • Accuracy and dynamic range of spatial image correlation and cross-correlation spectroscopy
    • Costantino S., et al. Accuracy and dynamic range of spatial image correlation and cross-correlation spectroscopy. Biophys. J. 2005, 89(2):1251-1260.
    • (2005) Biophys. J. , vol.89 , Issue.2 , pp. 1251-1260
    • Costantino, S.1
  • 10
    • 33845432394 scopus 로고    scopus 로고
    • A guide to accurate fluorescence microscopy colocalization measurements
    • Comeau J.W., Costantino S., Wiseman P.W. A guide to accurate fluorescence microscopy colocalization measurements. Biophys. J. 2006, 91(12):4611-4622.
    • (2006) Biophys. J. , vol.91 , Issue.12 , pp. 4611-4622
    • Comeau, J.W.1    Costantino, S.2    Wiseman, P.W.3
  • 11
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy A.K. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 2001, 24(3):289-296.
    • (2001) Methods , vol.24 , Issue.3 , pp. 289-296
    • Kenworthy, A.K.1
  • 12
    • 0036224370 scopus 로고    scopus 로고
    • Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse
    • Zal T., Zal M.A., Gascoigne N.R. Inhibition of T cell receptor-coreceptor interactions by antagonist ligands visualized by live FRET imaging of the T-hybridoma immunological synapse. Immunity 2002, 16(4):521-534.
    • (2002) Immunity , vol.16 , Issue.4 , pp. 521-534
    • Zal, T.1    Zal, M.A.2    Gascoigne, N.R.3
  • 13
    • 77952093185 scopus 로고    scopus 로고
    • Quantification of protein-lipid selectivity using FRET
    • Loura L.M., Prieto M., Fernandes F. Quantification of protein-lipid selectivity using FRET. Eur. Biophys. J. 2010, 39(4):565-578.
    • (2010) Eur. Biophys. J. , vol.39 , Issue.4 , pp. 565-578
    • Loura, L.M.1    Prieto, M.2    Fernandes, F.3
  • 14
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization
    • Maurel D., et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization. Nat. Methods 2008, 5(6):561-567.
    • (2008) Nat. Methods , vol.5 , Issue.6 , pp. 561-567
    • Maurel, D.1
  • 15
    • 0036909519 scopus 로고    scopus 로고
    • Imaging protein-protein interactions in living cells
    • Hink M.A., Bisselin T., Visser A.J. Imaging protein-protein interactions in living cells. Plant Mol. Biol. 2002, 50(6):871-883.
    • (2002) Plant Mol. Biol. , vol.50 , Issue.6 , pp. 871-883
    • Hink, M.A.1    Bisselin, T.2    Visser, A.J.3
  • 16
    • 34247863869 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between lipid probes detects nanoscopic heterogeneity in the plasma membrane of live cells
    • Sengupta P., Holowka D., Baird B. Fluorescence resonance energy transfer between lipid probes detects nanoscopic heterogeneity in the plasma membrane of live cells. Biophys. J. 2007, 92(10):3564-3574.
    • (2007) Biophys. J. , vol.92 , Issue.10 , pp. 3564-3574
    • Sengupta, P.1    Holowka, D.2    Baird, B.3
  • 17
  • 18
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 1978, 47:819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 19
    • 2942640371 scopus 로고    scopus 로고
    • Photobleaching-corrected FRET efficiency imaging of live cells
    • Zal T., Gascoigne N.R. Photobleaching-corrected FRET efficiency imaging of live cells. Biophys. J. 2004, 86(6):3923-3939.
    • (2004) Biophys. J. , vol.86 , Issue.6 , pp. 3923-3939
    • Zal, T.1    Gascoigne, N.R.2
  • 20
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100Å using imaging fluorescence resonance energy transfer
    • Kenworthy A.K., Edidin M. Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100Å using imaging fluorescence resonance energy transfer. J. Cell Biol. 1998, 142(1):69-84.
    • (1998) J. Cell Biol. , vol.142 , Issue.1 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 21
    • 35748931313 scopus 로고    scopus 로고
    • Practical guidelines for dual-color fluorescence cross-correlation spectroscopy
    • Bacia K., Schwille P. Practical guidelines for dual-color fluorescence cross-correlation spectroscopy. Nat. Protoc. 2007, 2(11):2842-2856.
    • (2007) Nat. Protoc. , vol.2 , Issue.11 , pp. 2842-2856
    • Bacia, K.1    Schwille, P.2
  • 22
    • 24144440917 scopus 로고    scopus 로고
    • Cross talk free fluorescence cross correlation spectroscopy in live cells
    • Thews E., et al. Cross talk free fluorescence cross correlation spectroscopy in live cells. Biophys. J. 2005, 89(3):2069-2076.
    • (2005) Biophys. J. , vol.89 , Issue.3 , pp. 2069-2076
    • Thews, E.1
  • 23
    • 33751318060 scopus 로고    scopus 로고
    • Dual-color total internal reflection fluorescence cross-correlation spectroscopy
    • Leutenegger M., et al. Dual-color total internal reflection fluorescence cross-correlation spectroscopy. J. Biomed. Opt. 2006, 11(4):040502.
    • (2006) J. Biomed. Opt. , vol.11 , Issue.4 , pp. 040502
    • Leutenegger, M.1
  • 24
    • 69549126014 scopus 로고    scopus 로고
    • Modular scanning FCS quantifies receptor-ligand interactions in living multicellular organisms
    • Ries J., et al. Modular scanning FCS quantifies receptor-ligand interactions in living multicellular organisms. Nat. Methods 2009, 6(9):643-645.
    • (2009) Nat. Methods , vol.6 , Issue.9 , pp. 643-645
    • Ries, J.1
  • 25
    • 0344981490 scopus 로고    scopus 로고
    • Detecting and quantifying colocalization of cell surface molecules by single particle fluorescence imaging
    • Morrison I.E., et al. Detecting and quantifying colocalization of cell surface molecules by single particle fluorescence imaging. Biophys. J. 2003, 85(6):4110-4121.
    • (2003) Biophys. J. , vol.85 , Issue.6 , pp. 4110-4121
    • Morrison, I.E.1
  • 26
    • 0035866675 scopus 로고    scopus 로고
    • Statistical analysis of single-molecule colocalization assays
    • Trabesinger W., et al. Statistical analysis of single-molecule colocalization assays. Anal. Chem. 2001, 73(6):1100-1105.
    • (2001) Anal. Chem. , vol.73 , Issue.6 , pp. 1100-1105
    • Trabesinger, W.1
  • 27
    • 0039169542 scopus 로고    scopus 로고
    • Direct observation of ligand colocalization on individual receptor molecules
    • Schutz G.J., Trabesinger W., Schmidt T. Direct observation of ligand colocalization on individual receptor molecules. Biophys. J. 1998, 74(5):2223-2226.
    • (1998) Biophys. J. , vol.74 , Issue.5 , pp. 2223-2226
    • Schutz, G.J.1    Trabesinger, W.2    Schmidt, T.3
  • 28
    • 36749064485 scopus 로고    scopus 로고
    • Single-molecule level analysis of the subunit composition of the T cell receptor on live T cells
    • James J.R., et al. Single-molecule level analysis of the subunit composition of the T cell receptor on live T cells. Proc. Natl. Acad. Sci. USA 2007, 104(45):17662-17667.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.45 , pp. 17662-17667
    • James, J.R.1
  • 29
    • 20544457766 scopus 로고    scopus 로고
    • Fluorescence imaging for monitoring the colocalization of two single molecules in living cells
    • Koyama-Honda I., et al. Fluorescence imaging for monitoring the colocalization of two single molecules in living cells. Biophys. J. 2005, 88(3):2126-2136.
    • (2005) Biophys. J. , vol.88 , Issue.3 , pp. 2126-2136
    • Koyama-Honda, I.1
  • 30
    • 69349092619 scopus 로고    scopus 로고
    • DySCo: quantitating associations of membrane proteins using two-color single-molecule tracking
    • Dunne P.D., et al. DySCo: quantitating associations of membrane proteins using two-color single-molecule tracking. Biophys. J. 2009, 97(4):L5-L7.
    • (2009) Biophys. J. , vol.97 , Issue.4
    • Dunne, P.D.1
  • 31
    • 75949110393 scopus 로고    scopus 로고
    • Two-color single molecule tracking combined with photobleaching for the detection of rare molecular interactions in fluid biomembranes
    • Ruprecht V., Brameshuber M., Schütz G.J. Two-color single molecule tracking combined with photobleaching for the detection of rare molecular interactions in fluid biomembranes. Soft Matter 2010, 6(3):568-581.
    • (2010) Soft Matter , vol.6 , Issue.3 , pp. 568-581
    • Ruprecht, V.1    Brameshuber, M.2    Schütz, G.J.3
  • 32
    • 77249150932 scopus 로고    scopus 로고
    • Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
    • Hern J.A., et al. Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. Proc. Natl. Acad. Sci. USA 2010, 107(6):2693-2698.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , Issue.6 , pp. 2693-2698
    • Hern, J.A.1
  • 33
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1
    • Suzuki K.G., et al. GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1. J. Cell Biol. 2007, 177(4):717-730.
    • (2007) J. Cell Biol. , vol.177 , Issue.4 , pp. 717-730
    • Suzuki, K.G.1
  • 34
    • 34249074042 scopus 로고    scopus 로고
    • 2+ signaling: single-molecule tracking study 2
    • 2+ signaling: single-molecule tracking study 2. J. Cell Biol. 2007, 177(4):731-742.
    • (2007) J. Cell Biol. , vol.177 , Issue.4 , pp. 731-742
    • Suzuki, K.G.1
  • 35
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass A.D., Vale R.D. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 2005, 121(6):937-950.
    • (2005) Cell , vol.121 , Issue.6 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 36
    • 70350501513 scopus 로고    scopus 로고
    • Single molecule imaging reveals differences in microtubule track selection between Kinesin motors
    • Cai D., et al. Single molecule imaging reveals differences in microtubule track selection between Kinesin motors. PLoS Biol. 2009, 7(10):e1000216.
    • (2009) PLoS Biol. , vol.7 , Issue.10
    • Cai, D.1
  • 37
    • 77952059303 scopus 로고    scopus 로고
    • Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells
    • Subach F.V., et al. Bright monomeric photoactivatable red fluorescent protein for two-color super-resolution sptPALM of live cells. J. Am. Chem. Soc. 2010, 132(18):6481-6491.
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.18 , pp. 6481-6491
    • Subach, F.V.1
  • 38
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M., et al. Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 2003, 302(5644):442-445.
    • (2003) Science , vol.302 , Issue.5644 , pp. 442-445
    • Dahan, M.1
  • 39
    • 48449104310 scopus 로고    scopus 로고
    • Dynamic multiple-target tracing to probe spatiotemporal cartography of cell membranes
    • Serge A., et al. Dynamic multiple-target tracing to probe spatiotemporal cartography of cell membranes. Nat. Methods 2008, 5(8):687-694.
    • (2008) Nat. Methods , vol.5 , Issue.8 , pp. 687-694
    • Serge, A.1
  • 40
    • 42149087060 scopus 로고    scopus 로고
    • Nanometer-scale mapping and single-molecule detection with color-coded nanoparticle probes
    • Agrawal A., et al. Nanometer-scale mapping and single-molecule detection with color-coded nanoparticle probes. Proc. Natl. Acad. Sci. USA 2008, 105(9):3298-3303.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.9 , pp. 3298-3303
    • Agrawal, A.1
  • 41
    • 77951643876 scopus 로고    scopus 로고
    • Probing cellular events, one quantum dot at a time
    • Pinaud F., et al. Probing cellular events, one quantum dot at a time. Nat. Methods 2010, 7(4):275-285.
    • (2010) Nat. Methods , vol.7 , Issue.4 , pp. 275-285
    • Pinaud, F.1
  • 42
    • 70349200987 scopus 로고    scopus 로고
    • Investigating biological processes at the single molecule level using luminescent quantum dots
    • Pons T., Mattoussi H. Investigating biological processes at the single molecule level using luminescent quantum dots. Ann. Biomed. Eng. 2009, 37(10):1934-1959.
    • (2009) Ann. Biomed. Eng. , vol.37 , Issue.10 , pp. 1934-1959
    • Pons, T.1    Mattoussi, H.2
  • 43
    • 34447508103 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals heterogeneous dynamics of lipid raft components upon TCR engagement
    • Drbal K., et al. Single-molecule microscopy reveals heterogeneous dynamics of lipid raft components upon TCR engagement. Int. Immunol. 2007, 19(5):675-684.
    • (2007) Int. Immunol. , vol.19 , Issue.5 , pp. 675-684
    • Drbal, K.1
  • 44
    • 36749082903 scopus 로고    scopus 로고
    • Single nitrogen vacancy centers in chemical vapor deposited diamond nanocrystals
    • Rabeau J.R., et al. Single nitrogen vacancy centers in chemical vapor deposited diamond nanocrystals. Nano Lett. 2007, 7(11):3433-3437.
    • (2007) Nano Lett. , vol.7 , Issue.11 , pp. 3433-3437
    • Rabeau, J.R.1
  • 45
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • Schütz G.J., et al. Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J. 2000, 19(5):892-901.
    • (2000) EMBO J. , vol.19 , Issue.5 , pp. 892-901
    • Schütz, G.J.1
  • 46
    • 33746725960 scopus 로고    scopus 로고
    • Single-molecule diffusion reveals similar mobility for the Lck, H-ras, and K-ras membrane anchors
    • Lommerse P.H., et al. Single-molecule diffusion reveals similar mobility for the Lck, H-ras, and K-ras membrane anchors. Biophys. J. 2006, 91(3):1090-1097.
    • (2006) Biophys. J. , vol.91 , Issue.3 , pp. 1090-1097
    • Lommerse, P.H.1
  • 47
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y., Minoghchi S., Yanagida T. Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol. 2000, 2(3):168-172.
    • (2000) Nat. Cell Biol. , vol.2 , Issue.3 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 48
    • 0034759494 scopus 로고    scopus 로고
    • Single-molecule imaging of l-type Ca(2+) channels in live cells
    • Harms G.S., et al. Single-molecule imaging of l-type Ca(2+) channels in live cells. Biophys. J. 2001, 81(5):2639-2646.
    • (2001) Biophys. J. , vol.81 , Issue.5 , pp. 2639-2646
    • Harms, G.S.1
  • 49
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger G., et al. Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 2001, 294(5548):1929-1932.
    • (2001) Science , vol.294 , Issue.5548 , pp. 1929-1932
    • Seisenberger, G.1
  • 50
    • 33749243938 scopus 로고    scopus 로고
    • Visualizing odorant receptor trafficking in living cells down to the single-molecule level
    • Jacquier V., et al. Visualizing odorant receptor trafficking in living cells down to the single-molecule level. Proc. Natl. Acad. Sci. USA 2006, 103(39):14325-14330.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.39 , pp. 14325-14330
    • Jacquier, V.1
  • 51
    • 14344253281 scopus 로고    scopus 로고
    • Non-exponential bleaching of single bioconjugated Cy5 molecules
    • Füreder-Kitzmüller E., et al. Non-exponential bleaching of single bioconjugated Cy5 molecules. Chem. Phys. Lett. 2005, 404:13-18.
    • (2005) Chem. Phys. Lett. , vol.404 , pp. 13-18
    • Füreder-Kitzmüller, E.1
  • 52
    • 0036382531 scopus 로고    scopus 로고
    • Single molecule microscopy in living cells: subtraction of autofluorescence based on two color recording
    • Moertelmaier M.A., et al. Single molecule microscopy in living cells: subtraction of autofluorescence based on two color recording. Single Mol. 2002, 3(4):225-231.
    • (2002) Single Mol. , vol.3 , Issue.4 , pp. 225-231
    • Moertelmaier, M.A.1
  • 53
    • 34547687408 scopus 로고    scopus 로고
    • Systematic colocalization errors between acridine orange and EGFP in astrocyte vesicular organelles
    • Nadrigny F., et al. Systematic colocalization errors between acridine orange and EGFP in astrocyte vesicular organelles. Biophys. J. 2007, 93(3):969-980.
    • (2007) Biophys. J. , vol.93 , Issue.3 , pp. 969-980
    • Nadrigny, F.1
  • 54
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: applications to membrane dynamics
    • Saxton M.J., Jacobson K. Single-particle tracking: applications to membrane dynamics. Annu. Rev. Biophys. Biomol. Struct. 1997, 26:373-399.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 55
    • 55649112026 scopus 로고    scopus 로고
    • Tracking single molecules in the live cell plasma membrane-Do's and Don't's
    • Wieser S., Schutz G.J. Tracking single molecules in the live cell plasma membrane-Do's and Don't's. Methods 2008, 46(2):131-140.
    • (2008) Methods , vol.46 , Issue.2 , pp. 131-140
    • Wieser, S.1    Schutz, G.J.2
  • 56
    • 0029981248 scopus 로고    scopus 로고
    • Imaging of single molecule diffusion
    • Schmidt T., et al. Imaging of single molecule diffusion. Proc. Natl. Acad. Sci. USA 1996, 93(7):2926-2929.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , Issue.7 , pp. 2926-2929
    • Schmidt, T.1
  • 57
    • 33947697260 scopus 로고    scopus 로고
    • Automatic detection of single fluorophores in live cells
    • Mashanov G.I., Molloy J.E. Automatic detection of single fluorophores in live cells. Biophys. J. 2007, 92(6):2199-2211.
    • (2007) Biophys. J. , vol.92 , Issue.6 , pp. 2199-2211
    • Mashanov, G.I.1    Molloy, J.E.2
  • 58
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson R.E., Larson D.R., Webb W.W. Precise nanometer localization analysis for individual fluorescent probes. Biophys. J. 2002, 82(5):2775-2783.
    • (2002) Biophys. J. , vol.82 , Issue.5 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 59
    • 33746727710 scopus 로고    scopus 로고
    • RNA expression profiling at the single molecule level
    • Hesse J., et al. RNA expression profiling at the single molecule level. Genome Res. 2006, 16(8):1041-1045.
    • (2006) Genome Res. , vol.16 , Issue.8 , pp. 1041-1045
    • Hesse, J.1
  • 60
    • 0033529248 scopus 로고    scopus 로고
    • Time-resolved analysis and visualization of dynamic processes in living cells
    • Tvarusko W., et al. Time-resolved analysis and visualization of dynamic processes in living cells. Proc. Natl. Acad. Sci. USA 1999, 96(14):7950-7955.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.14 , pp. 7950-7955
    • Tvarusko, W.1
  • 61
    • 45849092940 scopus 로고    scopus 로고
    • Bayesian inference for improved single molecule fluorescence tracking
    • Yoon J.W., et al. Bayesian inference for improved single molecule fluorescence tracking. Biophys. J. 2008.
    • (2008) Biophys. J.
    • Yoon, J.W.1
  • 62
    • 77952215650 scopus 로고    scopus 로고
    • Optimized localization analysis for single-molecule tracking and super-resolution microscopy
    • Mortensen K.I., et al. Optimized localization analysis for single-molecule tracking and super-resolution microscopy. Nat. Methods 2010, 7(5):377-381.
    • (2010) Nat. Methods , vol.7 , Issue.5 , pp. 377-381
    • Mortensen, K.I.1
  • 63
    • 77952216273 scopus 로고    scopus 로고
    • Fast, single-molecule localization that achieves theoretically minimum uncertainty
    • Smith C.S., et al. Fast, single-molecule localization that achieves theoretically minimum uncertainty. Nat. Methods 2010, 7(5):373-375.
    • (2010) Nat. Methods , vol.7 , Issue.5 , pp. 373-375
    • Smith, C.S.1
  • 64
    • 0000534160 scopus 로고
    • Position measurement with a resolution and noise-limited instrument
    • Bobroff N. Position measurement with a resolution and noise-limited instrument. Rev. Sci. Instrum. 1986, 57(6):1152-1157.
    • (1986) Rev. Sci. Instrum. , vol.57 , Issue.6 , pp. 1152-1157
    • Bobroff, N.1
  • 65
    • 65149084148 scopus 로고    scopus 로고
    • Accurately determining single molecule trajectories of molecular motion on surfaces
    • Claytor K., et al. Accurately determining single molecule trajectories of molecular motion on surfaces. J. Chem. Phys. 2009, 130(16):164710.
    • (2009) J. Chem. Phys. , vol.130 , Issue.16 , pp. 164710
    • Claytor, K.1
  • 66
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement?
    • Kural C., et al. Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement?. Science 2005, 308(5727):1469-1472.
    • (2005) Science , vol.308 , Issue.5727 , pp. 1469-1472
    • Kural, C.1
  • 67
    • 34247886012 scopus 로고    scopus 로고
    • (Un)confined diffusion of CD59 in the plasma membrane determined by high-resolution single molecule microscopy
    • Wieser S., et al. (Un)confined diffusion of CD59 in the plasma membrane determined by high-resolution single molecule microscopy. Biophys. J. 2007, 92(10):3719-3728.
    • (2007) Biophys. J. , vol.92 , Issue.10 , pp. 3719-3728
    • Wieser, S.1
  • 68
    • 13444292841 scopus 로고    scopus 로고
    • Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time
    • Churchman L.S., et al. Single molecule high-resolution colocalization of Cy3 and Cy5 attached to macromolecules measures intramolecular distances through time. Proc. Natl. Acad. Sci. USA 2005, 102(5):1419-1423.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.5 , pp. 1419-1423
    • Churchman, L.S.1
  • 69
    • 0346788868 scopus 로고    scopus 로고
    • Co-localization of cell surface receptors at high spatial resolution by single-particle fluorescence imaging
    • Karakikes I., et al. Co-localization of cell surface receptors at high spatial resolution by single-particle fluorescence imaging. Biochem. Soc. Trans. 2003, 31(Pt 6):1453-1455.
    • (2003) Biochem. Soc. Trans. , vol.31 , Issue.PART 6 , pp. 1453-1455
    • Karakikes, I.1
  • 70
    • 65749107160 scopus 로고    scopus 로고
    • Dynamic partitioning of a glycosyl-phosphatidylinositol-anchored protein in glycosphingolipid-rich microdomains imaged by single-quantum dot tracking
    • Pinaud F., et al. Dynamic partitioning of a glycosyl-phosphatidylinositol-anchored protein in glycosphingolipid-rich microdomains imaged by single-quantum dot tracking. Traffic 2009, 10(6):691-712.
    • (2009) Traffic , vol.10 , Issue.6 , pp. 691-712
    • Pinaud, F.1
  • 71
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias D.A., et al. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 2002, 296(5569):913-916.
    • (2002) Science , vol.296 , Issue.5569 , pp. 913-916
    • Zacharias, D.A.1
  • 72
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • Eggeling C., et al. Direct observation of the nanoscale dynamics of membrane lipids in a living cell. Nature 2009, 457(7233):1159-1162.
    • (2009) Nature , vol.457 , Issue.7233 , pp. 1159-1162
    • Eggeling, C.1
  • 73
    • 34548256844 scopus 로고    scopus 로고
    • Anatomy and dynamics of a supramolecular membrane protein cluster
    • Sieber J.J., et al. Anatomy and dynamics of a supramolecular membrane protein cluster. Science 2007, 317(5841):1072-1076.
    • (2007) Science , vol.317 , Issue.5841 , pp. 1072-1076
    • Sieber, J.J.1
  • 74
    • 33645839858 scopus 로고    scopus 로고
    • STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis
    • Willig K.I., et al. STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis. Nature 2006, 440(7086):935-939.
    • (2006) Nature , vol.440 , Issue.7086 , pp. 935-939
    • Willig, K.I.1
  • 75
    • 36849053761 scopus 로고    scopus 로고
    • Dynamic clustered distribution of hemagglutinin resolved at 40nm in living cell membranes discriminates between raft theories
    • Hess S.T., et al. Dynamic clustered distribution of hemagglutinin resolved at 40nm in living cell membranes discriminates between raft theories. Proc. Natl. Acad. Sci. USA 2007, 104(44):17370-17375.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.44 , pp. 17370-17375
    • Hess, S.T.1
  • 76
    • 33645520476 scopus 로고    scopus 로고
    • A non-Gaussian distribution quantifies distances measured with fluorescence localization techniques
    • Churchman L.S., Flyvbjerg H., Spudich J.A. A non-Gaussian distribution quantifies distances measured with fluorescence localization techniques. Biophys. J. 2006, 90(2):668-671.
    • (2006) Biophys. J. , vol.90 , Issue.2 , pp. 668-671
    • Churchman, L.S.1    Flyvbjerg, H.2    Spudich, J.A.3
  • 77
    • 0032939154 scopus 로고    scopus 로고
    • Detection of individual oligonucleotide pairing by single-molecule microscopy
    • Trabesinger W., et al. Detection of individual oligonucleotide pairing by single-molecule microscopy. Anal. Chem. 1999, 71(1):279-283.
    • (1999) Anal. Chem. , vol.71 , Issue.1 , pp. 279-283
    • Trabesinger, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.