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Volumn 117, Issue 11, 2017, Pages 7457-7477

Super-Resolution Microscopy: Shedding Light on the Cellular Plasma Membrane

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; MAMMALS;

EID: 85017189143     PISSN: 00092665     EISSN: 15206890     Source Type: Journal    
DOI: 10.1021/acs.chemrev.6b00716     Document Type: Review
Times cited : (140)

References (245)
  • 1
    • 29144531904 scopus 로고    scopus 로고
    • Seeing Spots: Complex Phase Behavior in Simple Membranes
    • Veatch, S. L.; Keller, S. L. Seeing Spots: Complex Phase Behavior in Simple Membranes Biochim. Biophys. Acta, Mol. Cell Res. 2005, 1746 (3) 172-185 10.1016/j.bbamcr.2005.06.010
    • (2005) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1746 , Issue.3 , pp. 172-185
    • Veatch, S.L.1    Keller, S.L.2
  • 2
    • 38549173564 scopus 로고    scopus 로고
    • Membrane Lipids: Where They Are and How They Behave
    • van Meer, G.; Voelker, D. R.; Feigenson, G. W. Membrane Lipids: Where They Are and How They Behave Nat. Rev. Mol. Cell Biol. 2008, 9 (2) 112-124 10.1038/nrm2330
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , Issue.2 , pp. 112-124
    • Van Meer, G.1    Voelker, D.R.2    Feigenson, G.W.3
  • 3
    • 84884307854 scopus 로고    scopus 로고
    • Membrane Lipid Phase Transitions and Phase Organization Studied by Fourier Transform Infrared Spectroscopy
    • Lewis, R. N. A. H.; McElhaney, R. N. Membrane Lipid Phase Transitions and Phase Organization Studied by Fourier Transform Infrared Spectroscopy Biochim. Biophys. Acta, Biomembr. 2013, 1828 (10) 2347-2358 10.1016/j.bbamem.2012.10.018
    • (2013) Biochim. Biophys. Acta, Biomembr. , vol.1828 , Issue.10 , pp. 2347-2358
    • Lewis, R.N.A.H.1    McElhaney, R.N.2
  • 4
    • 77952898456 scopus 로고    scopus 로고
    • Phase Separation in Biological Membranes: Integration of Theory and Experiment
    • Elson, E. L.; Fried, E.; Dolbow, J. E.; Genin, G. M. Phase Separation in Biological Membranes: Integration of Theory and Experiment Annu. Rev. Biophys. 2010, 39 (1) 207-226 10.1146/annurev.biophys.093008.131238
    • (2010) Annu. Rev. Biophys. , vol.39 , Issue.1 , pp. 207-226
    • Elson, E.L.1    Fried, E.2    Dolbow, J.E.3    Genin, G.M.4
  • 6
    • 84921728247 scopus 로고    scopus 로고
    • A Comprehensive Review of the Lipid Cubic Phase or in Meso Method for Crystallizing Membrane and Soluble Proteins and Complexes
    • Caffrey, M. A Comprehensive Review of the Lipid Cubic Phase or in Meso Method for Crystallizing Membrane and Soluble Proteins and Complexes Acta Crystallogr., Sect. F: Struct. Biol. Commun. 2015, 71, 3-18 10.1107/S2053230X14026843
    • (2015) Acta Crystallogr., Sect. F: Struct. Biol. Commun. , vol.71 , pp. 3-18
    • Caffrey, M.1
  • 7
    • 0018797519 scopus 로고
    • Lipid Polymorphism and the Functional Roles of Lipids in Biological Membranes
    • Cullis, P. R.; de Kruijff, B. Lipid Polymorphism and the Functional Roles of Lipids in Biological Membranes Biochim. Biophys. Acta, Rev. Biomembr. 1979, 559 (4) 399-420 10.1016/0304-4157(79)90012-1
    • (1979) Biochim. Biophys. Acta, Rev. Biomembr. , vol.559 , Issue.4 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 9
    • 84901040347 scopus 로고    scopus 로고
    • Importance of the Hexagonal Lipid Phase in Biological Membrane Organization
    • Jouhet, J. Importance of the Hexagonal Lipid Phase in Biological Membrane Organization Front. Plant Sci. 2013, 10.3389/fpls.2013.00494
    • (2013) Front. Plant Sci.
    • Jouhet, J.1
  • 11
    • 0025134135 scopus 로고
    • Structure of the Inverted Hexagonal (HII) Phase, and Non-Lamellar Phase Transitions of Lipids
    • Seddon, J. M. Structure of the Inverted Hexagonal (HII) Phase, and Non-Lamellar Phase Transitions of Lipids Biochim. Biophys. Acta, Rev. Biomembr. 1990, 1031 (1) 1-69 10.1016/0304-4157(90)90002-T
    • (1990) Biochim. Biophys. Acta, Rev. Biomembr. , vol.1031 , Issue.1 , pp. 1-69
    • Seddon, J.M.1
  • 12
    • 0025981964 scopus 로고
    • On the Reversibility of the Phase Transitions in Lipid-Water Systems
    • Tenchov, B. On the Reversibility of the Phase Transitions in Lipid-Water Systems Chem. Phys. Lipids 1991, 57 (2) 165-177 10.1016/0009-3084(91)90074-L
    • (1991) Chem. Phys. Lipids , vol.57 , Issue.2 , pp. 165-177
    • Tenchov, B.1
  • 14
    • 0018181781 scopus 로고
    • Influence of Increased Membrane Cholesterol on Membrane Fluidity and Cell Function in Human Red Blood Cells
    • Cooper, R. A. Influence of Increased Membrane Cholesterol on Membrane Fluidity and Cell Function in Human Red Blood Cells J. Supramol. Struct. 1978, 8 (4) 413-430 10.1002/jss.400080404
    • (1978) J. Supramol. Struct. , vol.8 , Issue.4 , pp. 413-430
    • Cooper, R.A.1
  • 15
    • 0022389171 scopus 로고
    • Cholesterol and the Cell Membrane
    • Yeagle, P. L. Cholesterol and the Cell Membrane Biochim. Biophys. Acta, Rev. Biomembr. 1985, 822 (3) 267-287 10.1016/0304-4157(85)90011-5
    • (1985) Biochim. Biophys. Acta, Rev. Biomembr. , vol.822 , Issue.3 , pp. 267-287
    • Yeagle, P.L.1
  • 17
    • 77954956306 scopus 로고    scopus 로고
    • Lipidomics: Coming to Grips with Lipid Diversity
    • Shevchenko, A.; Simons, K. Lipidomics: Coming to Grips with Lipid Diversity Nat. Rev. Mol. Cell Biol. 2010, 11 (8) 593-598 10.1038/nrm2934
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.8 , pp. 593-598
    • Shevchenko, A.1    Simons, K.2
  • 18
    • 84994103566 scopus 로고    scopus 로고
    • Homeoviscous Adaptation and the Regulation of Membrane Lipids
    • Ernst, R.; Ejsing, C. S.; Antonny, B. Homeoviscous Adaptation and the Regulation of Membrane Lipids J. Mol. Biol. 2016, 428, 4776 10.1016/j.jmb.2016.08.013
    • (2016) J. Mol. Biol. , vol.428 , pp. 4776
    • Ernst, R.1    Ejsing, C.S.2    Antonny, B.3
  • 19
    • 50549175610 scopus 로고
    • The Preparation and Chemical Characteristics of Hemoglobin-Free Ghosts of Human Erythrocytes
    • Dodge, J. T.; Mitchell, C.; Hanahan, D. J. The Preparation and Chemical Characteristics of Hemoglobin-Free Ghosts of Human Erythrocytes Arch. Biochem. Biophys. 1963, 100 (1) 119-130 10.1016/0003-9861(63)90042-0
    • (1963) Arch. Biochem. Biophys. , vol.100 , Issue.1 , pp. 119-130
    • Dodge, J.T.1    Mitchell, C.2    Hanahan, D.J.3
  • 20
    • 0016226796 scopus 로고
    • The Organization of Proteins in the Human Red Blood Cell Membrane. A Review
    • Steck, T. L. The Organization of Proteins in the Human Red Blood Cell Membrane. A Review J. Cell Biol. 1974, 62 (1) 1-19 10.1083/jcb.62.1.1
    • (1974) J. Cell Biol. , vol.62 , Issue.1 , pp. 1-19
    • Steck, T.L.1
  • 21
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and Signaling by Fatty-Acylated and Prenylated Proteins
    • Resh, M. D. Trafficking and Signaling by Fatty-Acylated and Prenylated Proteins Nat. Chem. Biol. 2006, 2 (11) 584-590 10.1038/nchembio834
    • (2006) Nat. Chem. Biol. , vol.2 , Issue.11 , pp. 584-590
    • Resh, M.D.1
  • 22
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-Protein Interactions in Cell Signaling and Membrane Trafficking
    • Cho, W.; Stahelin, R. V. Membrane-Protein Interactions in Cell Signaling and Membrane Trafficking Annu. Rev. Biophys. Biomol. Struct. 2005, 34 (1) 119-151 10.1146/annurev.biophys.33.110502.133337
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , Issue.1 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 23
    • 38549092474 scopus 로고    scopus 로고
    • Membrane Recognition by Phospholipid-Binding Domains
    • Lemmon, M. A. Membrane Recognition by Phospholipid-Binding Domains Nat. Rev. Mol. Cell Biol. 2008, 9 (2) 99-111 10.1038/nrm2328
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , Issue.2 , pp. 99-111
    • Lemmon, M.A.1
  • 24
    • 0016001009 scopus 로고
    • The Molecular Organization of Membranes
    • Singer, S. J. The Molecular Organization of Membranes Annu. Rev. Biochem. 1974, 43 (1) 805-833 10.1146/annurev.bi.43.070174.004105
    • (1974) Annu. Rev. Biochem. , vol.43 , Issue.1 , pp. 805-833
    • Singer, S.J.1
  • 25
    • 58849092285 scopus 로고    scopus 로고
    • Membrane Fusion: Grappling with SNARE and SM Proteins
    • Südhof, T. C.; Rothman, J. E. Membrane Fusion: Grappling with SNARE and SM Proteins Science 2009, 323 (5913) 474-477 10.1126/science.1161748
    • (2009) Science , vol.323 , Issue.5913 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 26
  • 27
    • 84964959959 scopus 로고    scopus 로고
    • Lipidomics Analyses Reveal Temporal and Spatial Lipid Organization and Uncover Daily Oscillations in Intracellular Organelles
    • Aviram, R.; Manella, G.; Kopelman, N.; Neufeld-Cohen, A.; Zwighaft, Z.; Elimelech, M.; Adamovich, Y.; Golik, M.; Wang, C.; Han, X. et al. Lipidomics Analyses Reveal Temporal and Spatial Lipid Organization and Uncover Daily Oscillations in Intracellular Organelles Mol. Cell 2016, 62 (4) 636-648 10.1016/j.molcel.2016.04.002
    • (2016) Mol. Cell , vol.62 , Issue.4 , pp. 636-648
    • Aviram, R.1    Manella, G.2    Kopelman, N.3    Neufeld-Cohen, A.4    Zwighaft, Z.5    Elimelech, M.6    Adamovich, Y.7    Golik, M.8    Wang, C.9    Han, X.10
  • 28
    • 84949552712 scopus 로고    scopus 로고
    • Cytoskeletal Dynamics: A View from the Membrane
    • Bezanilla, M.; Gladfelter, A. S.; Kovar, D. R.; Lee, W.-L. Cytoskeletal Dynamics: A View from the Membrane J. Cell Biol. 2015, 209 (3) 329-337 10.1083/jcb.201502062
    • (2015) J. Cell Biol. , vol.209 , Issue.3 , pp. 329-337
    • Bezanilla, M.1    Gladfelter, A.S.2    Kovar, D.R.3    Lee, W.-L.4
  • 29
    • 0026497661 scopus 로고
    • Cytoskeleton - Plasma Membrane Interactions
    • Luna, E. J.; Hitt, A. L. Cytoskeleton - Plasma Membrane Interactions Science 1992, 258 (5084) 955-964 10.1126/science.1439807
    • (1992) Science , vol.258 , Issue.5084 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 30
    • 0035344650 scopus 로고    scopus 로고
    • Cell Control by Membrane-cytoskeleton Adhesion
    • Sheetz, M. P. Cell Control by Membrane-cytoskeleton Adhesion Nat. Rev. Mol. Cell Biol. 2001, 2 (5) 392-396 10.1038/35073095
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , Issue.5 , pp. 392-396
    • Sheetz, M.P.1
  • 31
    • 33745035202 scopus 로고    scopus 로고
    • Continuous Membrane-Cytoskeleton Adhesion Requires Continuous Accommodation to Lipid and Cytoskeleton Dynamics
    • Sheetz, M. P.; Sable, J. E.; Döbereiner, H.-G. Continuous Membrane-Cytoskeleton Adhesion Requires Continuous Accommodation to Lipid and Cytoskeleton Dynamics Annu. Rev. Biophys. Biomol. Struct. 2006, 35 (1) 417-434 10.1146/annurev.biophys.35.040405.102017
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , Issue.1 , pp. 417-434
    • Sheetz, M.P.1    Sable, J.E.2    Döbereiner, H.-G.3
  • 32
    • 33750057669 scopus 로고    scopus 로고
    • Conditions for Extreme Sensitivity of Protein Diffusion in Membranes to Cell Environments
    • Tserkovnyak, Y.; Nelson, D. R. Conditions for Extreme Sensitivity of Protein Diffusion in Membranes to Cell Environments Proc. Natl. Acad. Sci. U. S. A. 2006, 103 (41) 15002-15007 10.1073/pnas.0606992103
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.41 , pp. 15002-15007
    • Tserkovnyak, Y.1    Nelson, D.R.2
  • 33
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides
    • Saarikangas, J.; Zhao, H.; Lappalainen, P. Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides Physiol. Rev. 2010, 90 (1) 259-289 10.1152/physrev.00036.2009
    • (2010) Physiol. Rev. , vol.90 , Issue.1 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 34
    • 84866860428 scopus 로고    scopus 로고
    • Critical Casimir Forces in Cellular Membranes
    • Machta, B. B.; Veatch, S. L.; Sethna, J. P. Critical Casimir Forces in Cellular Membranes Phys. Rev. Lett. 2012, 109 (13) 138101 10.1103/PhysRevLett.109.138101
    • (2012) Phys. Rev. Lett. , vol.109 , Issue.13 , pp. 138101
    • Machta, B.B.1    Veatch, S.L.2    Sethna, J.P.3
  • 35
    • 34548506513 scopus 로고    scopus 로고
    • Fluorescence Probe Partitioning between Lo/Ld Phases in Lipid Membranes
    • Baumgart, T.; Hunt, G.; Farkas, E. R.; Webb, W. W.; Feigenson, G. W. Fluorescence Probe Partitioning between Lo/Ld Phases in Lipid Membranes Biochim. Biophys. Acta, Biomembr. 2007, 1768 (9) 2182-2194 10.1016/j.bbamem.2007.05.012
    • (2007) Biochim. Biophys. Acta, Biomembr. , vol.1768 , Issue.9 , pp. 2182-2194
    • Baumgart, T.1    Hunt, G.2    Farkas, E.R.3    Webb, W.W.4    Feigenson, G.W.5
  • 36
    • 0030949124 scopus 로고    scopus 로고
    • Functional Rafts in Cell Membranes
    • Simons, K.; Ikonen, E. Functional Rafts in Cell Membranes Nature 1997, 387 (6633) 569-572 10.1038/42408
    • (1997) Nature , vol.387 , Issue.6633 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 37
    • 44649160533 scopus 로고    scopus 로고
    • Have We Become Overly Reliant on Lipid Rafts? Talking Point on the Involvement of Lipid Rafts in T-Cell Activation
    • Kenworthy, A. K. Have We Become Overly Reliant on Lipid Rafts? Talking Point on the Involvement of Lipid Rafts in T-Cell Activation EMBO Rep. 2008, 9 (6) 531-535 10.1038/embor.2008.92
    • (2008) EMBO Rep. , vol.9 , Issue.6 , pp. 531-535
    • Kenworthy, A.K.1
  • 38
    • 0344585437 scopus 로고    scopus 로고
    • Lipid Rafts: Elusive or Illusive?
    • Munro, S. Lipid Rafts: Elusive or Illusive? Cell 2003, 115 (4) 377-388 10.1016/S0092-8674(03)00882-1
    • (2003) Cell , vol.115 , Issue.4 , pp. 377-388
    • Munro, S.1
  • 39
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing Membrane Rafts: New Tools and Insights
    • Simons, K.; Gerl, M. J. Revitalizing Membrane Rafts: New Tools and Insights Nat. Rev. Mol. Cell Biol. 2010, 11 (10) 688-699 10.1038/nrm2977
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.10 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 40
    • 0040452793 scopus 로고    scopus 로고
    • Adhesion-Induced Domain Formation by Interplay of Long-Range Repulsion and Short-Range Attraction Force: A Model Membrane Study
    • Albersdörfer, A.; Feder, T.; Sackmann, E. Adhesion-Induced Domain Formation by Interplay of Long-Range Repulsion and Short-Range Attraction Force: A Model Membrane Study Biophys. J. 1997, 73 (1) 245-257 10.1016/S0006-3495(97)78065-2
    • (1997) Biophys. J. , vol.73 , Issue.1 , pp. 245-257
    • Albersdörfer, A.1    Feder, T.2    Sackmann, E.3
  • 41
    • 84939860220 scopus 로고    scopus 로고
    • Phase Transitions of Multivalent Proteins Can Promote Clustering of Membrane Receptors
    • Banjade, S.; Rosen, M. K. Phase Transitions of Multivalent Proteins Can Promote Clustering of Membrane Receptors eLife 2014, 3, e04123 10.7554/eLife.04123
    • (2014) ELife , vol.3 , pp. e04123
    • Banjade, S.1    Rosen, M.K.2
  • 42
    • 80052555773 scopus 로고    scopus 로고
    • Spatiotemporal Regulation of Chemical Reactions by Active Cytoskeletal Remodeling
    • Chaudhuri, A.; Bhattacharya, B.; Gowrishankar, K.; Mayor, S.; Rao, M. Spatiotemporal Regulation of Chemical Reactions by Active Cytoskeletal Remodeling Proc. Natl. Acad. Sci. U. S. A. 2011, 108 (36) 14825-14830 10.1073/pnas.1100007108
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , Issue.36 , pp. 14825-14830
    • Chaudhuri, A.1    Bhattacharya, B.2    Gowrishankar, K.3    Mayor, S.4    Rao, M.5
  • 44
    • 0019848925 scopus 로고
    • Fluorescent Low Density Lipoprotein for Observation of Dynamics of Individual Receptor Complexes on Cultured Human Fibroblasts
    • Barak, L. S.; Webb, W. W. Fluorescent Low Density Lipoprotein for Observation of Dynamics of Individual Receptor Complexes on Cultured Human Fibroblasts J. Cell Biol. 1981, 90 (3) 595-604 10.1083/jcb.90.3.595
    • (1981) J. Cell Biol. , vol.90 , Issue.3 , pp. 595-604
    • Barak, L.S.1    Webb, W.W.2
  • 45
    • 0020459573 scopus 로고
    • Diffusion of Low Density Lipoprotein-Receptor Complex on Human Fibroblasts
    • Barak, L. S.; Webb, W. W. Diffusion of Low Density Lipoprotein-Receptor Complex on Human Fibroblasts J. Cell Biol. 1982, 95 (3) 846-852 10.1083/jcb.95.3.846
    • (1982) J. Cell Biol. , vol.95 , Issue.3 , pp. 846-852
    • Barak, L.S.1    Webb, W.W.2
  • 46
    • 0022400414 scopus 로고
    • Probing Microtubule-Dependent Intracellular Motility with Nanometre Particle Video Ultramicroscopy (Nanovid Ultramicroscopy)
    • De Brabander, M.; Geuens, G.; Nuydens, R.; Moeremans, M.; De Mey, J. Probing Microtubule-Dependent Intracellular Motility with Nanometre Particle Video Ultramicroscopy (Nanovid Ultramicroscopy) Cytobios 1985, 43 (174S) 273-283
    • (1985) Cytobios , vol.43 , Issue.174 S , pp. 273-283
    • De Brabander, M.1    Geuens, G.2    Nuydens, R.3    Moeremans, M.4    De Mey, J.5
  • 47
    • 0023871621 scopus 로고
    • Tracking Kinesin-Driven Movements with Nanometre-Scale Precision
    • Gelles, J.; Schnapp, B. J.; Sheetz, M. P. Tracking Kinesin-Driven Movements with Nanometre-Scale Precision Nature 1988, 331 (6155) 450-453 10.1038/331450a0
    • (1988) Nature , vol.331 , Issue.6155 , pp. 450-453
    • Gelles, J.1    Schnapp, B.J.2    Sheetz, M.P.3
  • 48
    • 0023687725 scopus 로고
    • Nanometer-Scale Measurements Using Video Light Microscopy
    • Schnapp, B. J.; Gelles, J.; Sheetz, M. P. Nanometer-Scale Measurements Using Video Light Microscopy Cell Motil. Cytoskeleton 1988, 10 (1-2) 47-53 10.1002/cm.970100109
    • (1988) Cell Motil. Cytoskeleton , vol.10 , Issue.12 , pp. 47-53
    • Schnapp, B.J.1    Gelles, J.2    Sheetz, M.P.3
  • 49
    • 0026053736 scopus 로고
    • Lateral Diffusion and Retrograde Movements of Individual Cell Surface Components on Single Motile Cells Observed with Nanovid Microscopy
    • de Brabander, M.; Nuydens, R.; Ishihara, A.; Holifield, B.; Jacobson, K.; Geerts, H. Lateral Diffusion and Retrograde Movements of Individual Cell Surface Components on Single Motile Cells Observed with Nanovid Microscopy J. Cell Biol. 1991, 112 (1) 111-124 10.1083/jcb.112.1.111
    • (1991) J. Cell Biol. , vol.112 , Issue.1 , pp. 111-124
    • De Brabander, M.1    Nuydens, R.2    Ishihara, A.3    Holifield, B.4    Jacobson, K.5    Geerts, H.6
  • 50
    • 0029126377 scopus 로고
    • New Insights into Membrane Dynamics from the Analysis of Cell Surface Interactions by Physical Methods
    • Sheets, E. D.; Simson, R.; Jacobson, K. New Insights into Membrane Dynamics from the Analysis of Cell Surface Interactions by Physical Methods Curr. Opin. Cell Biol. 1995, 7 (5) 707-714 10.1016/0955-0674(95)80113-8
    • (1995) Curr. Opin. Cell Biol. , vol.7 , Issue.5 , pp. 707-714
    • Sheets, E.D.1    Simson, R.2    Jacobson, K.3
  • 51
    • 0028243194 scopus 로고
    • Compartmentalized Structure of the Plasma Membrane for Receptor Movements as Revealed by a Nanometer-Level Motion Analysis
    • Sako, Y.; Kusumi, A. Compartmentalized Structure of the Plasma Membrane for Receptor Movements as Revealed by a Nanometer-Level Motion Analysis J. Cell Biol. 1994, 125 (6) 1251-1264 10.1083/jcb.125.6.1251
    • (1994) J. Cell Biol. , vol.125 , Issue.6 , pp. 1251-1264
    • Sako, Y.1    Kusumi, A.2
  • 52
    • 0027504198 scopus 로고
    • Confined Lateral Diffusion of Membrane Receptors as Studied by Single Particle Tracking (Nanovid Microscopy). Effects of Calcium-Induced Differentiation in Cultured Epithelial Cells
    • Kusumi, A.; Sako, Y.; Yamamoto, M. Confined Lateral Diffusion of Membrane Receptors as Studied by Single Particle Tracking (Nanovid Microscopy). Effects of Calcium-Induced Differentiation in Cultured Epithelial Cells Biophys. J. 1993, 65 (5) 2021-2040 10.1016/S0006-3495(93)81253-0
    • (1993) Biophys. J. , vol.65 , Issue.5 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 53
    • 0030832226 scopus 로고    scopus 로고
    • On/off Blinking and Switching Behaviour of Single Molecules of Green Fluorescent Protein
    • Dickson, R. M.; Cubitt, A. B.; Tsien, R. Y.; Moerner, W. E. On/off Blinking and Switching Behaviour of Single Molecules of Green Fluorescent Protein Nature 1997, 388 (6640) 355-358 10.1038/41048
    • (1997) Nature , vol.388 , Issue.6640 , pp. 355-358
    • Dickson, R.M.1    Cubitt, A.B.2    Tsien, R.Y.3    Moerner, W.E.4
  • 54
    • 0028921834 scopus 로고
    • Improved Green Fluorescence
    • Heim, R.; Cubitt, A. B.; Tsien, R. Y. Improved Green Fluorescence Nature 1995, 373 (6516) 663-664 10.1038/373663b0
    • (1995) Nature , vol.373 , Issue.6516 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 55
    • 0039617818 scopus 로고    scopus 로고
    • Single Molecular Assay of Individual ATP Turnover by a Myosin-GFP Fusion Protein Expressed in Vitro
    • Iwane, A. H.; Funatsu, T.; Harada, Y.; Tokunaga, M.; Ohara, O.; Morimoto, S.; Yanagida, T. Single Molecular Assay of Individual ATP Turnover by a Myosin-GFP Fusion Protein Expressed in Vitro FEBS Lett. 1997, 407 (2) 235-238 10.1016/S0014-5793(97)00359-1
    • (1997) FEBS Lett. , vol.407 , Issue.2 , pp. 235-238
    • Iwane, A.H.1    Funatsu, T.2    Harada, Y.3    Tokunaga, M.4    Ohara, O.5    Morimoto, S.6    Yanagida, T.7
  • 56
    • 0030741606 scopus 로고    scopus 로고
    • Imaging Individual Green Fluorescent Proteins
    • Pierce, D. W.; Hom-Booher, N.; Vale, R. D. Imaging Individual Green Fluorescent Proteins Nature 1997, 388 (6640) 338-338 10.1038/41009
    • (1997) Nature , vol.388 , Issue.6640 , pp. 338
    • Pierce, D.W.1    Hom-Booher, N.2    Vale, R.D.3
  • 57
    • 0019494948 scopus 로고
    • Cell-Substrate Contacts Illuminated by Total Internal Reflection Fluorescence
    • Axelrod, D. Cell-Substrate Contacts Illuminated by Total Internal Reflection Fluorescence J. Cell Biol. 1981, 89 (1) 141-145 10.1083/jcb.89.1.141
    • (1981) J. Cell Biol. , vol.89 , Issue.1 , pp. 141-145
    • Axelrod, D.1
  • 60
    • 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 10.1146/annurev.biophys.26.1.373
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 62
    • 36849053761 scopus 로고    scopus 로고
    • Dynamic Clustered Distribution of Hemagglutinin Resolved at 40 Nm in Living Cell Membranes Discriminates between Raft Theories
    • Hess, S. T.; Gould, T. J.; Gudheti, M. V.; Maas, S. A.; Mills, K. D.; Zimmerberg, J. Dynamic Clustered Distribution of Hemagglutinin Resolved at 40 Nm in Living Cell Membranes Discriminates between Raft Theories Proc. Natl. Acad. Sci. U. S. A. 2007, 104 (44) 17370-17375 10.1073/pnas.0708066104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , Issue.44 , pp. 17370-17375
    • Hess, S.T.1    Gould, T.J.2    Gudheti, M.V.3    Maas, S.A.4    Mills, K.D.5    Zimmerberg, J.6
  • 63
    • 34648826792 scopus 로고    scopus 로고
    • Multicolor Super-Resolution Imaging with Photo-Switchable Fluorescent Probes
    • Bates, W. M.; Huang, B.; Dempsey, G. T.; Zhuang, X. Multicolor Super-Resolution Imaging with Photo-Switchable Fluorescent Probes Science 2007, 317 (5845) 1749-1753 10.1126/science.1146598
    • (2007) Science , vol.317 , Issue.5845 , pp. 1749-1753
    • Bates, W.M.1    Huang, B.2    Dempsey, G.T.3    Zhuang, X.4
  • 64
    • 38949216802 scopus 로고    scopus 로고
    • Three-Dimensional Super-Resolution Imaging by Stochastic Optical Reconstruction Microscopy
    • Huang, B.; Wang, W.; Bates, M.; Zhuang, X. Three-Dimensional Super-Resolution Imaging by Stochastic Optical Reconstruction Microscopy Science 2008, 319 (5864) 810-813 10.1126/science.1153529
    • (2008) Science , vol.319 , Issue.5864 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 65
    • 34248504534 scopus 로고    scopus 로고
    • Wide-Field Subdiffraction Imaging by Accumulated Binding of Diffusing Probes
    • Sharonov, A.; Hochstrasser, R. M. Wide-Field Subdiffraction Imaging by Accumulated Binding of Diffusing Probes Proc. Natl. Acad. Sci. U. S. A. 2006, 103 (50) 18911-18916 10.1073/pnas.0609643104
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.50 , pp. 18911-18916
    • Sharonov, A.1    Hochstrasser, R.M.2
  • 67
    • 42949083695 scopus 로고    scopus 로고
    • Live-Cell Photoactivated Localization Microscopy of Nanoscale Adhesion Dynamics
    • Shroff, H.; Galbraith, C. G.; Galbraith, J. A.; Betzig, E. Live-Cell Photoactivated Localization Microscopy of Nanoscale Adhesion Dynamics Nat. Methods 2008, 5 (5) 417-423 10.1038/nmeth.1202
    • (2008) Nat. Methods , vol.5 , Issue.5 , pp. 417-423
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 69
    • 17644402459 scopus 로고    scopus 로고
    • Transduction of Receptor Signals by ß-Arrestins
    • Lefkowitz, R. J.; Shenoy, S. K. Transduction of Receptor Signals by ß-Arrestins Science 2005, 308 (5721) 512-517 10.1126/science.1109237
    • (2005) Science , vol.308 , Issue.5721 , pp. 512-517
    • Lefkowitz, R.J.1    Shenoy, S.K.2
  • 70
    • 34447633368 scopus 로고    scopus 로고
    • Conformational Complexity of G-Protein-Coupled Receptors
    • Kobilka, B. K.; Deupi, X. Conformational Complexity of G-Protein-Coupled Receptors Trends Pharmacol. Sci. 2007, 28 (8) 397-406 10.1016/j.tips.2007.06.003
    • (2007) Trends Pharmacol. Sci. , vol.28 , Issue.8 , pp. 397-406
    • Kobilka, B.K.1    Deupi, X.2
  • 72
    • 66249144426 scopus 로고    scopus 로고
    • The Structure and Function of G-Protein-Coupled Receptors
    • Rosenbaum, D. M.; Rasmussen, S. G. F.; Kobilka, B. K. The Structure and Function of G-Protein-Coupled Receptors Nature 2009, 459 (7245) 356-363 10.1038/nature08144
    • (2009) Nature , vol.459 , Issue.7245 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 73
    • 85016554064 scopus 로고    scopus 로고
    • Labeling and Single-Molecule Methods to Monitor G Protein-Coupled Receptor Dynamics
    • Tian, H.; Fürstenberg, A.; Huber, T. Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics Chem. Rev. 2017, 117, 186-245 10.1021/acs.chemrev.6b00084
    • (2017) Chem. Rev. , vol.117 , pp. 186-245
    • Tian, H.1    Fürstenberg, A.2    Huber, T.3
  • 74
    • 0035318509 scopus 로고    scopus 로고
    • Oligomerization of G-Protein-Coupled Transmitter Receptors
    • Bouvier, M. Oligomerization of G-Protein-Coupled Transmitter Receptors Nat. Rev. Neurosci. 2001, 2 (4) 274-286 10.1038/35067575
    • (2001) Nat. Rev. Neurosci. , vol.2 , Issue.4 , pp. 274-286
    • Bouvier, M.1
  • 75
    • 41149127699 scopus 로고    scopus 로고
    • Dimerization and Oligomerization of G-Protein-Coupled Receptors: Debated Structures with Established and Emerging Functions
    • Szidonya, L.; Cserzö, M.; Hunyady, L. Dimerization and Oligomerization of G-Protein-Coupled Receptors: Debated Structures with Established and Emerging Functions J. Endocrinol. 2008, 196 (3) 435-453 10.1677/JOE-07-0573
    • (2008) J. Endocrinol. , vol.196 , Issue.3 , pp. 435-453
    • Szidonya, L.1    Cserzö, M.2    Hunyady, L.3
  • 76
    • 29244466321 scopus 로고    scopus 로고
    • Imaging Nanometer Domains of Beta-Adrenergic Receptor Complexes on the Surface of Cardiac Myocytes
    • Ianoul, A.; Grant, D. D.; Rouleau, Y.; Bani-Yaghoub, M.; Johnston, L. J.; Pezacki, J. P. Imaging Nanometer Domains of Beta-Adrenergic Receptor Complexes on the Surface of Cardiac Myocytes Nat. Chem. Biol. 2005, 1 (4) 196-202 10.1038/nchembio726
    • (2005) Nat. Chem. Biol. , vol.1 , Issue.4 , pp. 196-202
    • Ianoul, A.1    Grant, D.D.2    Rouleau, Y.3    Bani-Yaghoub, M.4    Johnston, L.J.5    Pezacki, J.P.6
  • 77
    • 79960806755 scopus 로고    scopus 로고
    • Quantitative Photo Activated Localization Microscopy: Unraveling the Effects of Photoblinking
    • Annibale, P.; Vanni, S.; Scarselli, M.; Rothlisberger, U.; Radenovic, A. Quantitative Photo Activated Localization Microscopy: Unraveling the Effects of Photoblinking PLoS One 2011, 6 (7) e22678 10.1371/journal.pone.0022678
    • (2011) PLoS One , vol.6 , Issue.7 , pp. e22678
    • Annibale, P.1    Vanni, S.2    Scarselli, M.3    Rothlisberger, U.4    Radenovic, A.5
  • 78
    • 84860877718 scopus 로고    scopus 로고
    • Cell Type-Specific β2-Adrenergic Receptor Clusters Identified Using Photoactivated Localization Microscopy Are Not Lipid Raft Related, but Depend on Actin Cytoskeleton Integrity
    • Scarselli, M.; Annibale, P.; Radenovic, A. Cell Type-Specific β2-Adrenergic Receptor Clusters Identified Using Photoactivated Localization Microscopy Are Not Lipid Raft Related, but Depend on Actin Cytoskeleton Integrity J. Biol. Chem. 2012, 287 (20) 16768-16780 10.1074/jbc.M111.329912
    • (2012) J. Biol. Chem. , vol.287 , Issue.20 , pp. 16768-16780
    • Scarselli, M.1    Annibale, P.2    Radenovic, A.3
  • 79
    • 84872195772 scopus 로고    scopus 로고
    • Single-Molecule Analysis of Fluorescently Labeled G-Protein-coupled Receptors Reveals Complexes with Distinct Dynamics and Organization
    • Calebiro, D.; Rieken, F.; Wagner, J.; Sungkaworn, T.; Zabel, U.; Borzi, A.; Cocucci, E.; Zürn, A.; Lohse, M. J. Single-Molecule Analysis of Fluorescently Labeled G-Protein-coupled Receptors Reveals Complexes with Distinct Dynamics and Organization Proc. Natl. Acad. Sci. U. S. A. 2013, 110 (2) 743-748 10.1073/pnas.1205798110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , Issue.2 , pp. 743-748
    • Calebiro, D.1    Rieken, F.2    Wagner, J.3    Sungkaworn, T.4    Zabel, U.5    Borzi, A.6    Cocucci, E.7    Zürn, A.8    Lohse, M.J.9
  • 80
    • 84890612981 scopus 로고    scopus 로고
    • Single-Molecule Imaging Revealed Dynamic GPCR Dimerization
    • Kasai, R. S.; Kusumi, A. Single-Molecule Imaging Revealed Dynamic GPCR Dimerization Curr. Opin. Cell Biol. 2014, 27, 78-86 10.1016/j.ceb.2013.11.008
    • (2014) Curr. Opin. Cell Biol. , vol.27 , pp. 78-86
    • Kasai, R.S.1    Kusumi, A.2
  • 81
    • 80051695489 scopus 로고    scopus 로고
    • Confinement of β(1)- and β(2)-Adrenergic Receptors in the Plasma Membrane of Cardiomyocyte-like H9c2 Cells Is Mediated by Selective Interactions with PDZ Domain and A-Kinase Anchoring Proteins but Not Caveolae
    • Valentine, C. D.; Haggie, P. M. Confinement of β(1)- and β(2)-Adrenergic Receptors in the Plasma Membrane of Cardiomyocyte-like H9c2 Cells Is Mediated by Selective Interactions with PDZ Domain and A-Kinase Anchoring Proteins but Not Caveolae Mol. Biol. Cell 2011, 22 (16) 2970-2982 10.1091/mbc.E11-01-0034
    • (2011) Mol. Biol. Cell , vol.22 , Issue.16 , pp. 2970-2982
    • Valentine, C.D.1    Haggie, P.M.2
  • 82
    • 84882265323 scopus 로고    scopus 로고
    • Improved Super-Resolution Microscopy with Oxazine Fluorophores in Heavy Water
    • Lee, S. F.; Vérolet, Q.; Fürstenberg, A. Improved Super-Resolution Microscopy with Oxazine Fluorophores in Heavy Water Angew. Chem., Int. Ed. 2013, 52 (34) 8948-8951 10.1002/anie.201302341
    • (2013) Angew. Chem., Int. Ed. , vol.52 , Issue.34 , pp. 8948-8951
    • Lee, S.F.1    Vérolet, Q.2    Fürstenberg, A.3
  • 83
    • 84903722378 scopus 로고    scopus 로고
    • Coordinate-Based Co-Localization-Mediated Analysis of Arrestin Clustering upon Stimulation of the C-C Chemokine Receptor 5 with RANTES/CCL5 Analogues
    • Tarancón Díez, L. T.; Bönsch, C.; Malkusch, S.; Truan, Z.; Munteanu, M.; Heilemann, M.; Hartley, O.; Endesfelder, U.; Fürstenberg, A. Coordinate-Based Co-Localization-Mediated Analysis of Arrestin Clustering upon Stimulation of the C-C Chemokine Receptor 5 with RANTES/CCL5 Analogues Histochem. Cell Biol. 2014, 142 (1) 69-77 10.1007/s00418-014-1206-1
    • (2014) Histochem. Cell Biol. , vol.142 , Issue.1 , pp. 69-77
    • Tarancón Díez, L.T.1    Bönsch, C.2    Malkusch, S.3    Truan, Z.4    Munteanu, M.5    Heilemann, M.6    Hartley, O.7    Endesfelder, U.8    Fürstenberg, A.9
  • 84
  • 86
    • 84922896573 scopus 로고    scopus 로고
    • Single Molecule Analysis of Functionally Asymmetric G Protein-Coupled Receptor (GPCR) Oligomers Reveals Diverse Spatial and Structural Assemblies
    • Jonas, K. C.; Fanelli, F.; Huhtaniemi, I. T.; Hanyaloglu, A. C. Single Molecule Analysis of Functionally Asymmetric G Protein-Coupled Receptor (GPCR) Oligomers Reveals Diverse Spatial and Structural Assemblies J. Biol. Chem. 2015, 290 (7) 3875-3892 10.1074/jbc.M114.622498
    • (2015) J. Biol. Chem. , vol.290 , Issue.7 , pp. 3875-3892
    • Jonas, K.C.1    Fanelli, F.2    Huhtaniemi, I.T.3    Hanyaloglu, A.C.4
  • 87
    • 0346244099 scopus 로고    scopus 로고
    • T-Cell-Antigen Recognition and the Immunological Synapse
    • Huppa, J. B.; Davis, M. M. T-Cell-Antigen Recognition and the Immunological Synapse Nat. Rev. Immunol. 2003, 3 (12) 973-983 10.1038/nri1245
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.12 , pp. 973-983
    • Huppa, J.B.1    Davis, M.M.2
  • 88
    • 84879647283 scopus 로고    scopus 로고
    • How B Cells Capture, Process and Present Antigens: A Crucial Role for Cell Polarity
    • Yuseff, M.-I.; Pierobon, P.; Reversat, A.; Lennon-Duménil, A.-M. How B Cells Capture, Process and Present Antigens: A Crucial Role for Cell Polarity Nat. Rev. Immunol. 2013, 13 (7) 475-486 10.1038/nri3469
    • (2013) Nat. Rev. Immunol. , vol.13 , Issue.7 , pp. 475-486
    • Yuseff, M.-I.1    Pierobon, P.2    Reversat, A.3    Lennon-Duménil, A.-M.4
  • 89
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat Are Expressed on Separate Protein Islands on T Cell Membranes and Concatenate during Activation
    • Lillemeier, B. F.; Mörtelmaier, M. A.; Forstner, M. B.; Huppa, J. B.; Groves, J. T.; Davis, M. M. TCR and Lat Are Expressed on Separate Protein Islands on T Cell Membranes and Concatenate during Activation Nat. Immunol. 2010, 11 (1) 90-96 10.1038/ni.1832
    • (2010) Nat. Immunol. , vol.11 , Issue.1 , pp. 90-96
    • Lillemeier, B.F.1    Mörtelmaier, M.A.2    Forstner, M.B.3    Huppa, J.B.4    Groves, J.T.5    Davis, M.M.6
  • 92
    • 79959373064 scopus 로고    scopus 로고
    • Pre-Existing Clusters of the Adaptor Lat Do Not Participate in Early T Cell Signaling Events
    • Williamson, D. J.; Owen, D. M.; Rossy, J.; Magenau, A.; Wehrmann, M.; Gooding, J. J.; Gaus, K. Pre-Existing Clusters of the Adaptor Lat Do Not Participate in Early T Cell Signaling Events Nat. Immunol. 2011, 12 (7) 655-662 10.1038/ni.2049
    • (2011) Nat. Immunol. , vol.12 , Issue.7 , pp. 655-662
    • Williamson, D.J.1    Owen, D.M.2    Rossy, J.3    Magenau, A.4    Wehrmann, M.5    Gooding, J.J.6    Gaus, K.7
  • 93
    • 84976575636 scopus 로고    scopus 로고
    • Superresolution Imaging Reveals Nanometer- and Micrometer-Scale Spatial Distributions of T-Cell Receptors in Lymph Nodes
    • Hu, Y. S.; Cang, H.; Lillemeier, B. F. Superresolution Imaging Reveals Nanometer- and Micrometer-Scale Spatial Distributions of T-Cell Receptors in Lymph Nodes Proc. Natl. Acad. Sci. U. S. A. 2016, 113 (26) 7201-7206 10.1073/pnas.1512331113
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , Issue.26 , pp. 7201-7206
    • Hu, Y.S.1    Cang, H.2    Lillemeier, B.F.3
  • 94
    • 84959574440 scopus 로고    scopus 로고
    • Dynamics of the Actin Cytoskeleton Mediates Receptor Cross Talk: An Emerging Concept in Tuning Receptor Signaling
    • Mattila, P. K.; Batista, F. D.; Treanor, B. Dynamics of the Actin Cytoskeleton Mediates Receptor Cross Talk: An Emerging Concept in Tuning Receptor Signaling J. Cell Biol. 2016, 212 (3) 267-280 10.1083/jcb.201504137
    • (2016) J. Cell Biol. , vol.212 , Issue.3 , pp. 267-280
    • Mattila, P.K.1    Batista, F.D.2    Treanor, B.3
  • 95
    • 84941799029 scopus 로고    scopus 로고
    • Cell Antigen Receptors of the IgM and IgD Classes Are Clustered in Different Protein Islands That Are Altered during B Cell Activation
    • Maity, P. C.; Blount, A.; Jumaa, H.; Ronneberger, O.; Lillemeier, B. F.; Reth, M. B. Cell Antigen Receptors of the IgM and IgD Classes Are Clustered in Different Protein Islands That Are Altered during B Cell Activation Sci. Signaling 2015, 8 (394) ra93-ra93 10.1126/scisignal.2005887
    • (2015) Sci. Signaling , vol.8 , Issue.394 , pp. ra93-ra93
    • Maity, P.C.1    Blount, A.2    Jumaa, H.3    Ronneberger, O.4    Lillemeier, B.F.5    Reth, M.B.6
  • 97
    • 85013287771 scopus 로고    scopus 로고
    • The Nanoscale Spatial Organization of B Cell Receptors on IgM- and IgG-Expressing Human B Cells
    • Lee, J.; Sengupta, P.; Brzostowski, J.; Lippincott-Schwartz, J.; Pierce, S. K. The Nanoscale Spatial Organization of B Cell Receptors on IgM- and IgG-Expressing Human B Cells Mol. Biol. Cell 2016, 10.1091/mbc.E16-06-0452
    • (2016) Mol. Biol. Cell
    • Lee, J.1    Sengupta, P.2    Brzostowski, J.3    Lippincott-Schwartz, J.4    Pierce, S.K.5
  • 99
    • 84931274767 scopus 로고    scopus 로고
    • Steady-State Cross-Correlations for Live Two-Colour Super-Resolution Localization Data Sets
    • Stone, M. B.; Veatch, S. L. Steady-State Cross-Correlations for Live Two-Colour Super-Resolution Localization Data Sets Nat. Commun. 2015, 6, 7347 10.1038/ncomms8347
    • (2015) Nat. Commun. , vol.6 , pp. 7347
    • Stone, M.B.1    Veatch, S.L.2
  • 101
  • 102
    • 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.; Webb, W. W. Constrained Diffusion or Immobile Fraction on Cell Surfaces: A New Interpretation Biophys. J. 1996, 70 (6) 2767-2773 10.1016/S0006-3495(96)79846-6
    • (1996) Biophys. J. , vol.70 , Issue.6 , pp. 2767-2773
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 103
    • 27744432013 scopus 로고    scopus 로고
    • Temporally Resolved Interactions between Antigen-Stimulated IgE Receptors and Lyn Kinase on Living Cells
    • Larson, D. R.; Gosse, J. A.; Holowka, D. A.; Baird, B. A.; Webb, W. W. Temporally Resolved Interactions between Antigen-Stimulated IgE Receptors and Lyn Kinase on Living Cells J. Cell Biol. 2005, 171 (3) 527-536 10.1083/jcb.200503110
    • (2005) J. Cell Biol. , vol.171 , Issue.3 , pp. 527-536
    • Larson, D.R.1    Gosse, J.A.2    Holowka, D.A.3    Baird, B.A.4    Webb, W.W.5
  • 104
    • 84923322056 scopus 로고    scopus 로고
    • Fluorogen-Activating Proteins Provide Tunable Labeling Densities for Tracking FcϵRI Independent of IgE
    • Schwartz, S. L.; Yan, Q.; Telmer, C. A.; Lidke, K. A.; Bruchez, M. P.; Lidke, D. S. Fluorogen-Activating Proteins Provide Tunable Labeling Densities for Tracking FcϵRI Independent of IgE ACS Chem. Biol. 2015, 10 (2) 539-546 10.1021/cb5005146
    • (2015) ACS Chem. Biol. , vol.10 , Issue.2 , pp. 539-546
    • Schwartz, S.L.1    Yan, Q.2    Telmer, C.A.3    Lidke, K.A.4    Bruchez, M.P.5    Lidke, D.S.6
  • 105
    • 84887891725 scopus 로고    scopus 로고
    • Distinct Stages of Stimulated FcϵRI Receptor Clustering and Immobilization Are Identified through Superresolution Imaging
    • Shelby, S. A.; Holowka, D.; Baird, B.; Veatch, S. L. Distinct Stages of Stimulated FcϵRI Receptor Clustering and Immobilization Are Identified through Superresolution Imaging Biophys. J. 2013, 105 (10) 2343-2354 10.1016/j.bpj.2013.09.049
    • (2013) Biophys. J. , vol.105 , Issue.10 , pp. 2343-2354
    • Shelby, S.A.1    Holowka, D.2    Baird, B.3    Veatch, S.L.4
  • 107
    • 84994681140 scopus 로고    scopus 로고
    • Functional Nanoscale Coupling of Lyn Kinase with IgE-FcϵRI Is Restricted by the Actin Cytoskeleton in Early Antigen-Stimulated Signaling
    • Shelby, S. A.; Veatch, S. L.; Holowka, D. A.; Baird, B. A. Functional Nanoscale Coupling of Lyn Kinase with IgE-FcϵRI Is Restricted by the Actin Cytoskeleton in Early Antigen-Stimulated Signaling Mol. Biol. Cell 2016, 27, 3645 10.1091/mbc.E16-06-0425
    • (2016) Mol. Biol. Cell , vol.27 , pp. 3645
    • Shelby, S.A.1    Veatch, S.L.2    Holowka, D.A.3    Baird, B.A.4
  • 108
    • 84901025110 scopus 로고    scopus 로고
    • The Immune Receptor NOD1 and Kinase RIP2 Interact with Bacterial Peptidoglycan on Early Endosomes to Promote Autophagy and Inflammatory Signaling
    • Irving, A. T.; Mimuro, H.; Kufer, T. A.; Lo, C.; Wheeler, R.; Turner, L. J.; Thomas, B. J.; Malosse, C.; Gantier, M. P.; Casillas, L. N. et al. The Immune Receptor NOD1 and Kinase RIP2 Interact with Bacterial Peptidoglycan on Early Endosomes to Promote Autophagy and Inflammatory Signaling Cell Host Microbe 2014, 15 (5) 623-635 10.1016/j.chom.2014.04.001
    • (2014) Cell Host Microbe , vol.15 , Issue.5 , pp. 623-635
    • Irving, A.T.1    Mimuro, H.2    Kufer, T.A.3    Lo, C.4    Wheeler, R.5    Turner, L.J.6    Thomas, B.J.7    Malosse, C.8    Gantier, M.P.9    Casillas, L.N.10
  • 109
    • 84859415535 scopus 로고    scopus 로고
    • Super-Resolution Imaging of C-Type Lectin and Influenza Hemagglutinin Nanodomains on Plasma Membranes Using Blink Microscopy
    • Itano, M. S.; Steinhauer, C.; Schmied, J. J.; Forthmann, C.; Liu, P.; Neumann, A. K.; Thompson, N. L.; Tinnefeld, P.; Jacobson, K. Super-Resolution Imaging of C-Type Lectin and Influenza Hemagglutinin Nanodomains on Plasma Membranes Using Blink Microscopy Biophys. J. 2012, 102 (7) 1534-1542 10.1016/j.bpj.2012.02.022
    • (2012) Biophys. J. , vol.102 , Issue.7 , pp. 1534-1542
    • Itano, M.S.1    Steinhauer, C.2    Schmied, J.J.3    Forthmann, C.4    Liu, P.5    Neumann, A.K.6    Thompson, N.L.7    Tinnefeld, P.8    Jacobson, K.9
  • 112
    • 84922355071 scopus 로고    scopus 로고
    • Mechanistic Insights into EGFR Membrane Clustering Revealed by Super-Resolution Imaging
    • Gao, J.; Wang, Y.; Cai, M.; Pan, Y.; Xu, H.; Jiang, J.; Ji, H.; Wang, H. Mechanistic Insights into EGFR Membrane Clustering Revealed by Super-Resolution Imaging Nanoscale 2015, 7 (6) 2511-2519 10.1039/C4NR04962D
    • (2015) Nanoscale , vol.7 , Issue.6 , pp. 2511-2519
    • Gao, J.1    Wang, Y.2    Cai, M.3    Pan, Y.4    Xu, H.5    Jiang, J.6    Ji, H.7    Wang, H.8
  • 113
    • 80053325995 scopus 로고    scopus 로고
    • Remodelling of Cortical Actin Where Lytic Granules Dock at Natural Killer Cell Immune Synapses Revealed by Super-Resolution Microscopy
    • Brown, A. C. N.; Oddos, S.; Dobbie, I. M.; Alakoskela, J.-M.; Parton, R. M.; Eissmann, P.; Neil, M. A. A.; Dunsby, C.; French, P. M. W.; Davis, I. et al. Remodelling of Cortical Actin Where Lytic Granules Dock at Natural Killer Cell Immune Synapses Revealed by Super-Resolution Microscopy PLoS Biol. 2011, 9 (9) e1001152 10.1371/journal.pbio.1001152
    • (2011) PLoS Biol. , vol.9 , Issue.9 , pp. e1001152
    • Brown, A.C.N.1    Oddos, S.2    Dobbie, I.M.3    Alakoskela, J.-M.4    Parton, R.M.5    Eissmann, P.6    Neil, M.A.A.7    Dunsby, C.8    French, P.M.W.9    Davis, I.10
  • 114
    • 84868549451 scopus 로고    scopus 로고
    • Super-Resolution Imaging of Remodeled Synaptic Actin Reveals Different Synergies between NK Cell Receptors and Integrins
    • Brown, A. C. N.; Dobbie, I. M.; Alakoskela, J.-M.; Davis, I.; Davis, D. M. Super-Resolution Imaging of Remodeled Synaptic Actin Reveals Different Synergies between NK Cell Receptors and Integrins Blood 2012, 120 (18) 3729-3740 10.1182/blood-2012-05-429977
    • (2012) Blood , vol.120 , Issue.18 , pp. 3729-3740
    • Brown, A.C.N.1    Dobbie, I.M.2    Alakoskela, J.-M.3    Davis, I.4    Davis, D.M.5
  • 115
    • 34249325178 scopus 로고    scopus 로고
    • Aggregation and Vesiculation of Membrane Proteins by Curvature-Mediated Interactions
    • Reynwar, B. J.; Illya, G.; Harmandaris, V. A.; Müller, M. M.; Kremer, K.; Deserno, M. Aggregation and Vesiculation of Membrane Proteins by Curvature-Mediated Interactions Nature 2007, 447 (7143) 461-464 10.1038/nature05840
    • (2007) Nature , vol.447 , Issue.7143 , pp. 461-464
    • Reynwar, B.J.1    Illya, G.2    Harmandaris, V.A.3    Müller, M.M.4    Kremer, K.5    Deserno, M.6
  • 116
    • 84995467832 scopus 로고    scopus 로고
    • The Continuing Mystery of Lipid Rafts
    • Levental, I.; Veatch, S. L. The Continuing Mystery of Lipid Rafts J. Mol. Biol. 2016, 428, 4749 10.1016/j.jmb.2016.08.022
    • (2016) J. Mol. Biol. , vol.428 , pp. 4749
    • Levental, I.1    Veatch, S.L.2
  • 117
    • 84964977692 scopus 로고    scopus 로고
    • Micron-Scale Plasma Membrane Curvature Is Recognized by the Septin Cytoskeleton
    • Bridges, A. A.; Jentzsch, M. S.; Oakes, P. W.; Occhipinti, P.; Gladfelter, A. S. Micron-Scale Plasma Membrane Curvature Is Recognized by the Septin Cytoskeleton J. Cell Biol. 2016, 213, 23 10.1083/jcb.201512029
    • (2016) J. Cell Biol. , vol.213 , pp. 23
    • Bridges, A.A.1    Jentzsch, M.S.2    Oakes, P.W.3    Occhipinti, P.4    Gladfelter, A.S.5
  • 118
    • 84952690378 scopus 로고    scopus 로고
    • Negative Membrane Curvature Catalyzes Nucleation of Endosomal Sorting Complex Required for Transport (ESCRT)-III Assembly
    • Lee, I.-H.; Kai, H.; Carlson, L.-A.; Groves, J. T.; Hurley, J. H. Negative Membrane Curvature Catalyzes Nucleation of Endosomal Sorting Complex Required for Transport (ESCRT)-III Assembly Proc. Natl. Acad. Sci. U. S. A. 2015, 112 (52) 15892-15897 10.1073/pnas.1518765113
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , Issue.52 , pp. 15892-15897
    • Lee, I.-H.1    Kai, H.2    Carlson, L.-A.3    Groves, J.T.4    Hurley, J.H.5
  • 119
    • 33847181297 scopus 로고    scopus 로고
    • The Multiple Faces of Caveolae
    • Parton, R. G.; Simons, K. The Multiple Faces of Caveolae Nat. Rev. Mol. Cell Biol. 2007, 8 (3) 185-194 10.1038/nrm2122
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , Issue.3 , pp. 185-194
    • Parton, R.G.1    Simons, K.2
  • 120
    • 84922353014 scopus 로고    scopus 로고
    • Nanoscale Imaging of Caveolin-1 Membrane Domains in Vivo
    • Gabor, K. A.; Kim, D.; Kim, C. H.; Hess, S. T. Nanoscale Imaging of Caveolin-1 Membrane Domains In Vivo PLoS One 2015, 10 (2) e0117225 10.1371/journal.pone.0117225
    • (2015) PLoS One , vol.10 , Issue.2 , pp. e0117225
    • Gabor, K.A.1    Kim, D.2    Kim, C.H.3    Hess, S.T.4
  • 121
    • 84879899037 scopus 로고    scopus 로고
    • Super Resolution Microscopy Reveals That Caveolin-1 Is Required for Spatial Organization of CRFB1 and Subsequent Antiviral Signaling in Zebrafish
    • Gabor, K. A.; Stevens, C. R.; Pietraszewski, M. J.; Gould, T. J.; Shim, J.; Yoder, J. A.; Lam, S. H.; Gong, Z.; Hess, S. T.; Kim, C. H. Super Resolution Microscopy Reveals That Caveolin-1 Is Required for Spatial Organization of CRFB1 and Subsequent Antiviral Signaling in Zebrafish PLoS One 2013, 8 (7) e68759 10.1371/journal.pone.0068759
    • (2013) PLoS One , vol.8 , Issue.7 , pp. e68759
    • Gabor, K.A.1    Stevens, C.R.2    Pietraszewski, M.J.3    Gould, T.J.4    Shim, J.5    Yoder, J.A.6    Lam, S.H.7    Gong, Z.8    Hess, S.T.9    Kim, C.H.10
  • 122
    • 84875773685 scopus 로고    scopus 로고
    • Roles Played by Capsid-Dependent Induction of Membrane Curvature and Gag-ESCRT Interactions in Tetherin Recruitment to HIV-1 Assembly Sites
    • Grover, J. R.; Llewellyn, G. N.; Soheilian, F.; Nagashima, K.; Veatch, S. L.; Ono, A. Roles Played by Capsid-Dependent Induction of Membrane Curvature and Gag-ESCRT Interactions in Tetherin Recruitment to HIV-1 Assembly Sites J. Virol. 2013, 87, 4650 10.1128/JVI.03526-12
    • (2013) J. Virol. , vol.87 , pp. 4650
    • Grover, J.R.1    Llewellyn, G.N.2    Soheilian, F.3    Nagashima, K.4    Veatch, S.L.5    Ono, A.6
  • 124
    • 85087239202 scopus 로고    scopus 로고
    • Revealing Nanoscale Membrane Curvature with Polarized Localization Microscopy
    • Optical Society of America: paper NM3C.2. DOI
    • Maarouf, A.; Meerschaert, R. L.; Kelly, C. Revealing Nanoscale Membrane Curvature with Polarized Localization Microscopy. Novel Techniques in Microscopy 2015; Optical Society of America: 2015; paper NM3C.2. DOI: 10.1364/NTM.2015.NM3C.2.
    • (2015) Novel Techniques in Microscopy 2015
    • Maarouf, A.1    Meerschaert, R.L.2    Kelly, C.3
  • 125
    • 76349086678 scopus 로고    scopus 로고
    • Localized Topological Changes of the Plasma Membrane upon Exocytosis Visualized by Polarized TIRFM
    • Anantharam, A.; Onoa, B.; Edwards, R. H.; Holz, R. W.; Axelrod, D. Localized Topological Changes of the Plasma Membrane upon Exocytosis Visualized by Polarized TIRFM J. Cell Biol. 2010, 188 (3) 415-428 10.1083/jcb.200908010
    • (2010) J. Cell Biol. , vol.188 , Issue.3 , pp. 415-428
    • Anantharam, A.1    Onoa, B.2    Edwards, R.H.3    Holz, R.W.4    Axelrod, D.5
  • 127
    • 84938742317 scopus 로고    scopus 로고
    • Super-Resolution Imaging and Quantitative Analysis of Membrane Protein/Lipid Raft Clustering Mediated by Cell-Surface Self-Assembly of Hybrid Nanoconjugates
    • Hartley, J. M.; Chu, T.-W.; Peterson, E. M.; Zhang, R.; Yang, J.; Harris, J.; Kopeček, J. Super-Resolution Imaging and Quantitative Analysis of Membrane Protein/Lipid Raft Clustering Mediated by Cell-Surface Self-Assembly of Hybrid Nanoconjugates ChemBioChem 2015, 16 (12) 1725-1729 10.1002/cbic.201500278
    • (2015) ChemBioChem , vol.16 , Issue.12 , pp. 1725-1729
    • Hartley, J.M.1    Chu, T.-W.2    Peterson, E.M.3    Zhang, R.4    Yang, J.5    Harris, J.6    Kopeček, J.7
  • 128
    • 77954630046 scopus 로고    scopus 로고
    • PALM Imaging and Cluster Analysis of Protein Heterogeneity at the Cell Surface
    • Owen, D. M.; Rentero, C.; Rossy, J.; Magenau, A.; Williamson, D.; Rodriguez, M.; Gaus, K. PALM Imaging and Cluster Analysis of Protein Heterogeneity at the Cell Surface J. Biophotonics 2010, 3 (7) 446-454 10.1002/jbio.200900089
    • (2010) J. Biophotonics , vol.3 , Issue.7 , pp. 446-454
    • Owen, D.M.1    Rentero, C.2    Rossy, J.3    Magenau, A.4    Williamson, D.5    Rodriguez, M.6    Gaus, K.7
  • 129
    • 84871789466 scopus 로고    scopus 로고
    • Sub-Resolution Lipid Domains Exist in the Plasma Membrane and Regulate Protein Diffusion and Distribution
    • Owen, D. M.; Williamson, D. J.; Magenau, A.; Gaus, K. Sub-Resolution Lipid Domains Exist in the Plasma Membrane and Regulate Protein Diffusion and Distribution Nat. Commun. 2012, 3, 1256 10.1038/ncomms2273
    • (2012) Nat. Commun. , vol.3 , pp. 1256
    • Owen, D.M.1    Williamson, D.J.2    Magenau, A.3    Gaus, K.4
  • 130
    • 78650664669 scopus 로고    scopus 로고
    • Palmitoylation Regulates Raft Affinity for the Majority of Integral Raft Proteins
    • Levental, I.; Lingwood, D.; Grzybek, M.; Coskun, U.; Simons, K. Palmitoylation Regulates Raft Affinity for the Majority of Integral Raft Proteins Proc. Natl. Acad. Sci. U. S. A. 2010, 107 (51) 22050-22054 10.1073/pnas.1016184107
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.51 , pp. 22050-22054
    • Levental, I.1    Lingwood, D.2    Grzybek, M.3    Coskun, U.4    Simons, K.5
  • 131
    • 80255137569 scopus 로고    scopus 로고
    • Probing Protein Heterogeneity in the Plasma Membrane Using PALM and Pair Correlation Analysis
    • Sengupta, P.; Jovanovic-Talisman, T.; Skoko, D.; Renz, M.; Veatch, S. L.; Lippincott-Schwartz, J. Probing Protein Heterogeneity in the Plasma Membrane Using PALM and Pair Correlation Analysis Nat. Methods 2011, 8 (11) 969-975 10.1038/nmeth.1704
    • (2011) Nat. Methods , vol.8 , Issue.11 , pp. 969-975
    • Sengupta, P.1    Jovanovic-Talisman, T.2    Skoko, D.3    Renz, M.4    Veatch, S.L.5    Lippincott-Schwartz, J.6
  • 132
    • 84895116509 scopus 로고    scopus 로고
    • Nanoscale Effects of Ethanol and Naltrexone on Protein Organization in the Plasma Membrane Studied by Photoactivated Localization Microscopy (PALM)
    • Tobin, S. J.; Cacao, E. E.; Hong, D. W. W.; Terenius, L.; Vukojevic, V.; Jovanovic-Talisman, T. Nanoscale Effects of Ethanol and Naltrexone on Protein Organization in the Plasma Membrane Studied by Photoactivated Localization Microscopy (PALM) PLoS One 2014, 9 (2) e87225 10.1371/journal.pone.0087225
    • (2014) PLoS One , vol.9 , Issue.2 , pp. e87225
    • Tobin, S.J.1    Cacao, E.E.2    Hong, D.W.W.3    Terenius, L.4    Vukojevic, V.5    Jovanovic-Talisman, T.6
  • 134
    • 58149196187 scopus 로고    scopus 로고
    • Tracking Microdomain Dynamics in Cell Membranes
    • Day, C. A.; Kenworthy, A. K. Tracking Microdomain Dynamics in Cell Membranes Biochim. Biophys. Acta, Biomembr. 2009, 1788 (1) 245-253 10.1016/j.bbamem.2008.10.024
    • (2009) Biochim. Biophys. Acta, Biomembr. , vol.1788 , Issue.1 , pp. 245-253
    • Day, C.A.1    Kenworthy, A.K.2
  • 135
    • 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. N.; Fujiwara, T. K. Hierarchical Organization of the Plasma Membrane: Investigations by Single-Molecule Tracking vs. Fluorescence Correlation Spectroscopy FEBS Lett. 2010, 584 (9) 1814-1823 10.1016/j.febslet.2010.02.047
    • (2010) FEBS Lett. , vol.584 , Issue.9 , pp. 1814-1823
    • Kusumi, A.1    Shirai, Y.M.2    Koyama-Honda, I.3    Suzuki, K.G.N.4    Fujiwara, T.K.5
  • 136
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-Cholesterol Rafts Diffuse as Small Entities in the Plasma Membrane of Mammalian Cells
    • Pralle, A.; Keller, P.; Florin, E.-L.; Simons, K.; Hörber, J. K. H. Sphingolipid-Cholesterol Rafts Diffuse as Small Entities in the Plasma Membrane of Mammalian Cells J. Cell Biol. 2000, 148 (5) 997-1008 10.1083/jcb.148.5.997
    • (2000) J. Cell Biol. , vol.148 , Issue.5 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.-L.3    Simons, K.4    Hörber, J.K.H.5
  • 137
    • 84928404203 scopus 로고    scopus 로고
    • GPI-Anchored Proteins Do Not Reside in Ordered Domains in the Live Cell Plasma Membrane
    • Sevcsik, E.; Brameshuber, M.; Fölser, M.; Weghuber, J.; Honigmann, A.; Schütz, G. J. GPI-Anchored Proteins Do Not Reside in Ordered Domains in the Live Cell Plasma Membrane Nat. Commun. 2015, 6, 6969 10.1038/ncomms7969
    • (2015) Nat. Commun. , vol.6 , pp. 6969
    • Sevcsik, E.1    Brameshuber, M.2    Fölser, M.3    Weghuber, J.4    Honigmann, A.5    Schütz, G.J.6
  • 138
    • 84922460988 scopus 로고    scopus 로고
    • Scanning STED-FCS Reveals Spatiotemporal Heterogeneity of Lipid Interaction in the Plasma Membrane of Living Cells
    • Honigmann, A.; Mueller, V.; Ta, H.; Schoenle, A.; Sezgin, E.; Hell, S. W.; Eggeling, C. Scanning STED-FCS Reveals Spatiotemporal Heterogeneity of Lipid Interaction in the Plasma Membrane of Living Cells Nat. Commun. 2014, 5, 5412 10.1038/ncomms6412
    • (2014) Nat. Commun. , vol.5 , pp. 5412
    • Honigmann, A.1    Mueller, V.2    Ta, H.3    Schoenle, A.4    Sezgin, E.5    Hell, S.W.6    Eggeling, C.7
  • 139
    • 79959655729 scopus 로고    scopus 로고
    • Minimal Model of Plasma Membrane Heterogeneity Requires Coupling Cortical Actin to Criticality
    • Machta, B. B.; Papanikolaou, S.; Sethna, J. P.; Veatch, S. L. Minimal Model of Plasma Membrane Heterogeneity Requires Coupling Cortical Actin to Criticality Biophys. J. 2011, 100 (7) 1668-1677 10.1016/j.bpj.2011.02.029
    • (2011) Biophys. J. , vol.100 , Issue.7 , pp. 1668-1677
    • Machta, B.B.1    Papanikolaou, S.2    Sethna, J.P.3    Veatch, S.L.4
  • 140
    • 84898717364 scopus 로고    scopus 로고
    • A Lipid Bound Actin Meshwork Organizes Liquid Phase Separation in Model Membranes
    • Honigmann, A.; Sadeghi, S.; Keller, J.; Hell, S. W.; Eggeling, C.; Vink, R. A Lipid Bound Actin Meshwork Organizes Liquid Phase Separation in Model Membranes eLife 2014, 3, e01671 10.7554/eLife.01671
    • (2014) ELife , vol.3 , pp. e01671
    • Honigmann, A.1    Sadeghi, S.2    Keller, J.3    Hell, S.W.4    Eggeling, C.5    Vink, R.6
  • 141
    • 84905234209 scopus 로고    scopus 로고
    • Counterion-Mediated Cluster Formation by Polyphosphoinositides
    • Wang, Y.-H.; Slochower, D. R.; Janmey, P. A. Counterion-Mediated Cluster Formation by Polyphosphoinositides Chem. Phys. Lipids 2014, 182, 38-51 10.1016/j.chemphyslip.2014.01.001
    • (2014) Chem. Phys. Lipids , vol.182 , pp. 38-51
    • Wang, Y.-H.1    Slochower, D.R.2    Janmey, P.A.3
  • 143
    • 66349122907 scopus 로고    scopus 로고
    • Clustering of Syntaxin-1A in Model Membranes Is Modulated by Phosphatidylinositol 4,5-Bisphosphate and Cholesterol
    • Murray, D. H.; Tamm, L. K. Clustering of Syntaxin-1A in Model Membranes Is Modulated by Phosphatidylinositol 4,5-Bisphosphate and Cholesterol Biochemistry 2009, 48 (21) 4617-4625 10.1021/bi9003217
    • (2009) Biochemistry , vol.48 , Issue.21 , pp. 4617-4625
    • Murray, D.H.1    Tamm, L.K.2
  • 144
    • 84964808703 scopus 로고    scopus 로고
    • Segregation of PIP2 and PIP3 into Distinct Nanoscale Regions within the Plasma Membrane
    • Wang, J.; Richards, D. A. Segregation of PIP2 and PIP3 into Distinct Nanoscale Regions within the Plasma Membrane Biol. Open 2012, 1 (9) 857-862 10.1242/bio.20122071
    • (2012) Biol. Open , vol.1 , Issue.9 , pp. 857-862
    • Wang, J.1    Richards, D.A.2
  • 145
    • 84946780726 scopus 로고    scopus 로고
    • Nanoscale Landscape of Phosphoinositides Revealed by Specific Pleckstrin Homology (PH) Domains Using Single-Molecule Superresolution Imaging in the Plasma Membrane
    • Ji, C.; Zhang, Y.; Xu, P.; Xu, T.; Lou, X. Nanoscale Landscape of Phosphoinositides Revealed by Specific Pleckstrin Homology (PH) Domains Using Single-Molecule Superresolution Imaging in the Plasma Membrane J. Biol. Chem. 2015, 290 (45) 26978-26993 10.1074/jbc.M115.663013
    • (2015) J. Biol. Chem. , vol.290 , Issue.45 , pp. 26978-26993
    • Ji, C.1    Zhang, Y.2    Xu, P.3    Xu, T.4    Lou, X.5
  • 146
    • 84856479181 scopus 로고    scopus 로고
    • Dual-Objective STORM Reveals Three-Dimensional Filament Organization in the Actin Cytoskeleton
    • Xu, K.; Babcock, H. P.; Zhuang, X. Dual-Objective STORM Reveals Three-Dimensional Filament Organization in the Actin Cytoskeleton Nat. Methods 2012, 9 (2) 185-188 10.1038/nmeth.1841
    • (2012) Nat. Methods , vol.9 , Issue.2 , pp. 185-188
    • Xu, K.1    Babcock, H.P.2    Zhuang, X.3
  • 147
    • 84934344305 scopus 로고    scopus 로고
    • Cortical Actin Networks Induce Spatio-Temporal Confinement of Phospholipids in the Plasma Membrane - A Minimally Invasive Investigation by STED-FCS
    • Andrade, D. M.; Clausen, M. P.; Keller, J.; Mueller, V.; Wu, C.; Bear, J. E.; Hell, S. W.; Lagerholm, B. C.; Eggeling, C. Cortical Actin Networks Induce Spatio-Temporal Confinement of Phospholipids in the Plasma Membrane-a Minimally Invasive Investigation by STED-FCS Sci. Rep. 2015, 5, 11454 10.1038/srep11454
    • (2015) Sci. Rep. , vol.5 , pp. 11454
    • Andrade, D.M.1    Clausen, M.P.2    Keller, J.3    Mueller, V.4    Wu, C.5    Bear, J.E.6    Hell, S.W.7    Lagerholm, B.C.8    Eggeling, C.9
  • 148
    • 84946763639 scopus 로고    scopus 로고
    • Multimodal Super-Resolution Optical Microscopy Visualizes the Close Connection between Membrane and the Cytoskeleton in Liver Sinusoidal Endothelial Cell Fenestrations
    • Mönkemöller, V.; Øie, C.; Hübner, W.; Huser, T.; McCourt, P. Multimodal Super-Resolution Optical Microscopy Visualizes the Close Connection between Membrane and the Cytoskeleton in Liver Sinusoidal Endothelial Cell Fenestrations Sci. Rep. 2015, 5, 16279 10.1038/srep16279
    • (2015) Sci. Rep. , vol.5 , pp. 16279
    • Mönkemöller, V.1    Øie, C.2    Hübner, W.3    Huser, T.4    McCourt, P.5
  • 149
    • 84872796017 scopus 로고    scopus 로고
    • Actin, Spectrin and Associated Proteins Form a Periodic Cytoskeletal Structure in Axons
    • Xu, K.; Zhong, G.; Zhuang, X. Actin, Spectrin and Associated Proteins Form a Periodic Cytoskeletal Structure in Axons Science 2013, 339, 452 10.1126/science.1232251
    • (2013) Science , vol.339 , pp. 452
    • Xu, K.1    Zhong, G.2    Zhuang, X.3
  • 150
    • 84924619572 scopus 로고    scopus 로고
    • STED Nanoscopy Reveals the Ubiquity of Subcortical Cytoskeleton Periodicity in Living Neurons
    • D'Este, E.; Kamin, D.; Göttfert, F.; El-Hady, A.; Hell, S. W. STED Nanoscopy Reveals the Ubiquity of Subcortical Cytoskeleton Periodicity in Living Neurons Cell Rep. 2015, 10 (8) 1246-1251 10.1016/j.celrep.2015.02.007
    • (2015) Cell Rep. , vol.10 , Issue.8 , pp. 1246-1251
    • D'Este, E.1    Kamin, D.2    Göttfert, F.3    El-Hady, A.4    Hell, S.W.5
  • 156
    • 0026675654 scopus 로고
    • Transmembrane Signaling: The Joy of Aggregation
    • Metzger, H. Transmembrane Signaling: The Joy of Aggregation J. Immunol. 1992, 149 (5) 1477-1487
    • (1992) J. Immunol. , vol.149 , Issue.5 , pp. 1477-1487
    • Metzger, H.1
  • 157
    • 84867912638 scopus 로고    scopus 로고
    • Counting Protein Molecules Using Quantitative Fluorescence Microscopy
    • Coffman, V. C.; Wu, J.-Q. Counting Protein Molecules Using Quantitative Fluorescence Microscopy Trends Biochem. Sci. 2012, 37 (11) 499-506 10.1016/j.tibs.2012.08.002
    • (2012) Trends Biochem. Sci. , vol.37 , Issue.11 , pp. 499-506
    • Coffman, V.C.1    Wu, J.-Q.2
  • 158
    • 44049105523 scopus 로고    scopus 로고
    • Mapping the Number of Molecules and Brightness in the Laser Scanning Microscope
    • Digman, M. A.; Dalal, R.; Horwitz, A. F.; Gratton, E. Mapping the Number of Molecules and Brightness in the Laser Scanning Microscope Biophys. J. 2008, 94 (6) 2320-2332 10.1529/biophysj.107.114645
    • (2008) Biophys. J. , vol.94 , Issue.6 , pp. 2320-2332
    • Digman, M.A.1    Dalal, R.2    Horwitz, A.F.3    Gratton, E.4
  • 160
    • 84941339381 scopus 로고    scopus 로고
    • One, Two or Three? Probing the Stoichiometry of Membrane Proteins by Single-Molecule Localization Microscopy
    • Fricke, F.; Beaudouin, J.; Eils, R.; Heilemann, M. One, Two or Three? Probing the Stoichiometry of Membrane Proteins by Single-Molecule Localization Microscopy Sci. Rep. 2015, 5, 14072 10.1038/srep14072
    • (2015) Sci. Rep. , vol.5 , pp. 14072
    • Fricke, F.1    Beaudouin, J.2    Eils, R.3    Heilemann, M.4
  • 161
    • 33748926752 scopus 로고    scopus 로고
    • Stoichiometry and Turnover in Single, Functioning Membrane Protein Complexes
    • Leake, M. C.; Chandler, J. H.; Wadhams, G. H.; Bai, F.; Berry, R. M.; Armitage, J. P. Stoichiometry and Turnover in Single, Functioning Membrane Protein Complexes Nature 2006, 443 (7109) 355-358 10.1038/nature05135
    • (2006) Nature , vol.443 , Issue.7109 , pp. 355-358
    • Leake, M.C.1    Chandler, J.H.2    Wadhams, G.H.3    Bai, F.4    Berry, R.M.5    Armitage, J.P.6
  • 162
    • 84907820473 scopus 로고    scopus 로고
    • Challenges in Quantitative Single Molecule Localization Microscopy
    • Shivanandan, A.; Deschout, H.; Scarselli, M.; Radenovic, A. Challenges in Quantitative Single Molecule Localization Microscopy FEBS Lett. 2014, 588 (19) 3595-3602 10.1016/j.febslet.2014.06.014
    • (2014) FEBS Lett. , vol.588 , Issue.19 , pp. 3595-3602
    • Shivanandan, A.1    Deschout, H.2    Scarselli, M.3    Radenovic, A.4
  • 164
    • 0036138908 scopus 로고    scopus 로고
    • A Variant of Yellow Fluorescent Protein with Fast and Efficient Maturation for Cell-Biological Applications
    • Nagai, T.; Ibata, K.; Park, E. S.; Kubota, M.; Mikoshiba, K.; Miyawaki, A. A Variant of Yellow Fluorescent Protein with Fast and Efficient Maturation for Cell-Biological Applications Nat. Biotechnol. 2002, 20 (1) 87-90 10.1038/nbt0102-87
    • (2002) Nat. Biotechnol. , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 165
    • 11144267737 scopus 로고    scopus 로고
    • Improved Monomeric Red, Orange and Yellow Fluorescent Proteins Derived from Discosoma Sp. Red Fluorescent Protein
    • Shaner, N. C.; Campbell, R. E.; Steinbach, P. A.; Giepmans, B. N. G.; Palmer, A. E.; Tsien, R. Y. Improved Monomeric Red, Orange and Yellow Fluorescent Proteins Derived from Discosoma Sp. Red Fluorescent Protein Nat. Biotechnol. 2004, 22 (12) 1567-1572 10.1038/nbt1037
    • (2004) Nat. Biotechnol. , vol.22 , Issue.12 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.G.4    Palmer, A.E.5    Tsien, R.Y.6
  • 166
    • 0031663369 scopus 로고    scopus 로고
    • The Green Fluorescent Protein
    • Tsien, R. Y. The Green Fluorescent Protein Annu. Rev. Biochem. 1998, 67 (1) 509-544 10.1146/annurev.biochem.67.1.509
    • (1998) Annu. Rev. Biochem. , vol.67 , Issue.1 , pp. 509-544
    • Tsien, R.Y.1
  • 167
    • 84902172298 scopus 로고    scopus 로고
    • Characterization and Development of Photoactivatable Fluorescent Proteins for Single-Molecule-based Superresolution Imaging
    • Wang, S.; Moffitt, J. R.; Dempsey, G. T.; Xie, X. S.; Zhuang, X. Characterization and Development of Photoactivatable Fluorescent Proteins for Single-Molecule-based Superresolution Imaging Proc. Natl. Acad. Sci. U. S. A. 2014, 111 (23) 8452-8457 10.1073/pnas.1406593111
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , Issue.23 , pp. 8452-8457
    • Wang, S.1    Moffitt, J.R.2    Dempsey, G.T.3    Xie, X.S.4    Zhuang, X.5
  • 168
    • 84870785240 scopus 로고    scopus 로고
    • Ultrabright Photoactivatable Fluorophores Created by Reductive Caging
    • Vaughan, J. C.; Jia, S.; Zhuang, X. Ultrabright Photoactivatable Fluorophores Created by Reductive Caging Nat. Methods 2012, 9 (12) 1181-1184 10.1038/nmeth.2214
    • (2012) Nat. Methods , vol.9 , Issue.12 , pp. 1181-1184
    • Vaughan, J.C.1    Jia, S.2    Zhuang, X.3
  • 169
    • 84905018413 scopus 로고    scopus 로고
    • Tryptophan and ATTO 590: Mutual Fluorescence Quenching and Exciplex Formation
    • Bhattacharjee, U.; Beck, C.; Winter, A.; Wells, C.; Petrich, J. W. Tryptophan and ATTO 590: Mutual Fluorescence Quenching and Exciplex Formation J. Phys. Chem. B 2014, 118 (29) 8471-8477 10.1021/jp412045m
    • (2014) J. Phys. Chem. B , vol.118 , Issue.29 , pp. 8471-8477
    • Bhattacharjee, U.1    Beck, C.2    Winter, A.3    Wells, C.4    Petrich, J.W.5
  • 170
    • 0033795017 scopus 로고    scopus 로고
    • Anomalous Fluorescence Enhancement of Cy3 and cy3.5 versus Anomalous Fluorescence Loss of Cy5 and Cy7 upon Covalent Linking to IgG and Noncovalent Binding to Avidin
    • Gruber, H. J.; Hahn, C. D.; Kada, G.; Riener, C. K.; Harms, G. S.; Ahrer, W.; Dax, T. G.; Knaus, H. G. Anomalous Fluorescence Enhancement of Cy3 and cy3.5 versus Anomalous Fluorescence Loss of Cy5 and Cy7 upon Covalent Linking to IgG and Noncovalent Binding to Avidin Bioconjugate Chem. 2000, 11 (5) 696-704 10.1021/bc000015m
    • (2000) Bioconjugate Chem. , vol.11 , Issue.5 , pp. 696-704
    • Gruber, H.J.1    Hahn, C.D.2    Kada, G.3    Riener, C.K.4    Harms, G.S.5    Ahrer, W.6    Dax, T.G.7    Knaus, H.G.8
  • 171
    • 0344494656 scopus 로고    scopus 로고
    • Inter- and Intramolecular Fluorescence Quenching of Organic Dyes by Tryptophan
    • Marmé, N.; Knemeyer, J.-P.; Sauer, M.; Wolfrum, J. Inter- and Intramolecular Fluorescence Quenching of Organic Dyes by Tryptophan Bioconjugate Chem. 2003, 14 (6) 1133-1139 10.1021/bc0341324
    • (2003) Bioconjugate Chem. , vol.14 , Issue.6 , pp. 1133-1139
    • Marmé, N.1    Knemeyer, J.-P.2    Sauer, M.3    Wolfrum, J.4
  • 172
    • 84883442783 scopus 로고    scopus 로고
    • Localization Microscopy Coming of Age: From Concepts to Biological Impact
    • Sauer, M. Localization Microscopy Coming of Age: From Concepts to Biological Impact J. Cell Sci. 2013, 126 (16) 3505-3513 10.1242/jcs.123612
    • (2013) J. Cell Sci. , vol.126 , Issue.16 , pp. 3505-3513
    • Sauer, M.1
  • 173
    • 85170282443 scopus 로고    scopus 로고
    • A Density-Based Algorithm for Discovering Clusters in Large Spatial Databases with Noise
    • AAAI
    • Ester, M.; Kriegel, H.-P.; Sander, J.; Xu, X. A Density-Based Algorithm for Discovering Clusters in Large Spatial Databases with Noise. KDD-96 Proceedings; AAAI: 1996; pp 226-231.
    • (1996) KDD-96 Proceedings , pp. 226-231
    • Ester, M.1    Kriegel, H.-P.2    Sander, J.3    Xu, X.4
  • 174
    • 84964354489 scopus 로고    scopus 로고
    • ClusterViSu, a Method for Clustering of Protein Complexes by Voronoi Tessellation in Super-Resolution Microscopy
    • Andronov, L.; Orlov, I.; Lutz, Y.; Vonesch, J.-L.; Klaholz, B. P. ClusterViSu, a Method for Clustering of Protein Complexes by Voronoi Tessellation in Super-Resolution Microscopy Sci. Rep. 2016, 6, 24084 10.1038/srep24084
    • (2016) Sci. Rep. , vol.6 , pp. 24084
    • Andronov, L.1    Orlov, I.2    Lutz, Y.3    Vonesch, J.-L.4    Klaholz, B.P.5
  • 176
    • 84994638560 scopus 로고    scopus 로고
    • Model-Independent Counting of Molecules in Single-Molecule Localization Microscopy
    • Hummer, G.; Fricke, F.; Heilemann, M. Model-Independent Counting of Molecules in Single-Molecule Localization Microscopy Mol. Biol. Cell 2016, 27, 3637 10.1091/mbc.E16-07-0525
    • (2016) Mol. Biol. Cell , vol.27 , pp. 3637
    • Hummer, G.1    Fricke, F.2    Heilemann, M.3
  • 177
    • 84920972458 scopus 로고    scopus 로고
    • Stochastic Approach to the Molecular Counting Problem in Superresolution Microscopy
    • Rollins, G. C.; Shin, J. Y.; Bustamante, C.; Pressé, S. Stochastic Approach to the Molecular Counting Problem in Superresolution Microscopy Proc. Natl. Acad. Sci. U. S. A. 2015, 112 (2) E110-E118 10.1073/pnas.1408071112
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , Issue.2 , pp. E110-E118
    • Rollins, G.C.1    Shin, J.Y.2    Bustamante, C.3    Pressé, S.4
  • 178
    • 84871246277 scopus 로고    scopus 로고
    • Accurate Construction of Photoactivated Localization Microscopy (PALM) Images for Quantitative Measurements
    • Coltharp, C.; Kessler, R. P.; Xiao, J. Accurate Construction of Photoactivated Localization Microscopy (PALM) Images for Quantitative Measurements PLoS One 2012, 7 (12) e51725 10.1371/journal.pone.0051725
    • (2012) PLoS One , vol.7 , Issue.12 , pp. e51725
    • Coltharp, C.1    Kessler, R.P.2    Xiao, J.3
  • 179
    • 84867912724 scopus 로고    scopus 로고
    • Counting Single Photoactivatable Fluorescent Molecules by Photoactivated Localization Microscopy (PALM)
    • Lee, S.-H.; Shin, J. Y.; Lee, A.; Bustamante, C. Counting Single Photoactivatable Fluorescent Molecules by Photoactivated Localization Microscopy (PALM) Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (43) 17436-17441 10.1073/pnas.1215175109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.43 , pp. 17436-17441
    • Lee, S.-H.1    Shin, J.Y.2    Lee, A.3    Bustamante, C.4
  • 180
    • 84857580744 scopus 로고    scopus 로고
    • Correlation Functions Quantify Super-Resolution Images and Estimate Apparent Clustering due to over-Counting
    • Veatch, S. L.; Machta, B. B.; Shelby, S. A.; Chiang, E. N.; Holowka, D. A.; Baird, B. A. Correlation Functions Quantify Super-Resolution Images and Estimate Apparent Clustering due to over-Counting PLoS One 2012, 7 (2) e31457 10.1371/journal.pone.0031457
    • (2012) PLoS One , vol.7 , Issue.2 , pp. e31457
    • Veatch, S.L.1    Machta, B.B.2    Shelby, S.A.3    Chiang, E.N.4    Holowka, D.A.5    Baird, B.A.6
  • 182
    • 84879826657 scopus 로고    scopus 로고
    • Multiscale Spatial Organization of RNA Polymerase in Escherichia coli
    • Endesfelder, U.; Finan, K.; Holden, S. J.; Cook, P. R.; Kapanidis, A. N.; Heilemann, M. Multiscale Spatial Organization of RNA Polymerase in Escherichia Coli Biophys. J. 2013, 105 (1) 172-181 10.1016/j.bpj.2013.05.048
    • (2013) Biophys. J. , vol.105 , Issue.1 , pp. 172-181
    • Endesfelder, U.1    Finan, K.2    Holden, S.J.3    Cook, P.R.4    Kapanidis, A.N.5    Heilemann, M.6
  • 183
    • 84999738001 scopus 로고    scopus 로고
    • Engineering Lipid Structure for Recognition of the Liquid Ordered Membrane Phase
    • Bordovsky, S. S.; Wong, C. S.; Bachand, G. D.; Stachowiak, J. C.; Sasaki, D. Y. Engineering Lipid Structure for Recognition of the Liquid Ordered Membrane Phase Langmuir 2016, 32, 12527 10.1021/acs.langmuir.6b02636
    • (2016) Langmuir , vol.32 , pp. 12527
    • Bordovsky, S.S.1    Wong, C.S.2    Bachand, G.D.3    Stachowiak, J.C.4    Sasaki, D.Y.5
  • 184
    • 0020183511 scopus 로고
    • Use of a Fluorescent Cholesterol Derivative to Measure Lateral Mobility of Cholesterol in Membranes
    • Alecio, M. R.; Golan, D. E.; Veatch, W. R.; Rando, R. R. Use of a Fluorescent Cholesterol Derivative to Measure Lateral Mobility of Cholesterol in Membranes Proc. Natl. Acad. Sci. U. S. A. 1982, 79 (17) 5171-5174 10.1073/pnas.79.17.5171
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , Issue.17 , pp. 5171-5174
    • Alecio, M.R.1    Golan, D.E.2    Veatch, W.R.3    Rando, R.R.4
  • 185
    • 84872008437 scopus 로고    scopus 로고
    • STED Microscopy Detects and Quantifies Liquid Phase Separation in Lipid Membranes Using a New Far-Red Emitting Fluorescent Phosphoglycerolipid Analogue
    • Honigmann, A.; Mueller, V.; Hell, S. W.; Eggeling, C. STED Microscopy Detects and Quantifies Liquid Phase Separation in Lipid Membranes Using a New Far-Red Emitting Fluorescent Phosphoglycerolipid Analogue Faraday Discuss. 2013, 161, 77-89 10.1039/C2FD20107K
    • (2013) Faraday Discuss. , vol.161 , pp. 77-89
    • Honigmann, A.1    Mueller, V.2    Hell, S.W.3    Eggeling, C.4
  • 186
    • 0036082665 scopus 로고    scopus 로고
    • PIP(2) and Proteins: Interactions, Organization, and Information Flow
    • McLaughlin, S.; Wang, J.; Gambhir, A.; Murray, D. PIP(2) and Proteins: Interactions, Organization, and Information Flow Annu. Rev. Biophys. Biomol. Struct. 2002, 31, 151-175 10.1146/annurev.biophys.31.082901.134259
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 151-175
    • McLaughlin, S.1    Wang, J.2    Gambhir, A.3    Murray, D.4
  • 187
    • 38849098376 scopus 로고    scopus 로고
    • A Gouy-Chapman-Stern Model of the Double Layer at a (Metal)/(ionic Liquid) Interface
    • Oldham, K. B. A Gouy-Chapman-Stern Model of the Double Layer at a (Metal)/(ionic Liquid) Interface J. Electroanal. Chem. 2008, 613 (2) 131-138 10.1016/j.jelechem.2007.10.017
    • (2008) J. Electroanal. Chem. , vol.613 , Issue.2 , pp. 131-138
    • Oldham, K.B.1
  • 188
    • 84863145014 scopus 로고    scopus 로고
    • Divalent Cation-Induced Cluster Formation by Polyphosphoinositides in Model Membranes
    • Wang, Y.-H.; Collins, A.; Guo, L.; Smith-Dupont, K. B.; Gai, F.; Svitkina, T.; Janmey, P. A. Divalent Cation-Induced Cluster Formation by Polyphosphoinositides in Model Membranes J. Am. Chem. Soc. 2012, 134 (7) 3387-3395 10.1021/ja208640t
    • (2012) J. Am. Chem. Soc. , vol.134 , Issue.7 , pp. 3387-3395
    • Wang, Y.-H.1    Collins, A.2    Guo, L.3    Smith-Dupont, K.B.4    Gai, F.5    Svitkina, T.6    Janmey, P.A.7
  • 189
    • 84961364349 scopus 로고    scopus 로고
    • Charge Shielding of PIP 2 by Cations Regulates Enzyme Activity of Phospholipase C
    • Seo, J. B.; Jung, S.-R.; Huang, W.; Zhang, Q.; Koh, D.-S. Charge Shielding of PIP 2 by Cations Regulates Enzyme Activity of Phospholipase C PLoS One 2015, 10 (12) e0144432 10.1371/journal.pone.0144432
    • (2015) PLoS One , vol.10 , Issue.12 , pp. e0144432
    • Seo, J.B.1    Jung, S.-R.2    Huang, W.3    Zhang, Q.4    Koh, D.-S.5
  • 190
    • 0028267231 scopus 로고
    • Crystal Structure of Cholera Toxin B-Pentamer Bound to Receptor GM1 Pentasaccharide
    • Merritt, E. A.; Sarfaty, S.; van den Akker, F.; L'Hoir, C.; Martial, J. A.; Hol, W. G. Crystal Structure of Cholera Toxin B-Pentamer Bound to Receptor GM1 Pentasaccharide Protein Sci. 1994, 3 (2) 166-175 10.1002/pro.5560030202
    • (1994) Protein Sci. , vol.3 , Issue.2 , pp. 166-175
    • Merritt, E.A.1    Sarfaty, S.2    Van Den Akker, F.3    L'Hoir, C.4    Martial, J.A.5    Hol, W.G.6
  • 191
    • 18144417503 scopus 로고    scopus 로고
    • Crosslinking a Lipid Raft Component Triggers Liquid Ordered-Liquid Disordered Phase Separation in Model Plasma Membranes
    • Hammond, A. T.; Heberle, F. A.; Baumgart, T.; Holowka, D.; Baird, B.; Feigenson, G. W. Crosslinking a Lipid Raft Component Triggers Liquid Ordered-Liquid Disordered Phase Separation in Model Plasma Membranes Proc. Natl. Acad. Sci. U. S. A. 2005, 102 (18) 6320-6325 10.1073/pnas.0405654102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.18 , pp. 6320-6325
    • Hammond, A.T.1    Heberle, F.A.2    Baumgart, T.3    Holowka, D.4    Baird, B.5    Feigenson, G.W.6
  • 192
    • 85006707326 scopus 로고    scopus 로고
    • Glycolipid Crosslinking Is Required for Cholera Toxin to Partition into and Stabilize Ordered Domains
    • Raghunathan, K.; Wong, T. H.; Chinnapen, D. J.; Lencer, W. I.; Jobling, M. G.; Kenworthy, A. K. Glycolipid Crosslinking Is Required for Cholera Toxin to Partition Into and Stabilize Ordered Domains Biophys. J. 2016, 111 (12) 2547-2550 10.1016/j.bpj.2016.11.008
    • (2016) Biophys. J. , vol.111 , Issue.12 , pp. 2547-2550
    • Raghunathan, K.1    Wong, T.H.2    Chinnapen, D.J.3    Lencer, W.I.4    Jobling, M.G.5    Kenworthy, A.K.6
  • 193
    • 0033431772 scopus 로고    scopus 로고
    • A Role for Lipid Rafts in B Cell Antigen Receptor Signaling and Antigen Targeting
    • Cheng, P. C.; Dykstra, M. L.; Mitchell, R. N.; Pierce, S. K. A Role for Lipid Rafts in B Cell Antigen Receptor Signaling and Antigen Targeting J. Exp. Med. 1999, 190 (11) 1549-1560 10.1084/jem.190.11.1549
    • (1999) J. Exp. Med. , vol.190 , Issue.11 , pp. 1549-1560
    • Cheng, P.C.1    Dykstra, M.L.2    Mitchell, R.N.3    Pierce, S.K.4
  • 194
    • 0026554220 scopus 로고
    • Cyclic AMP-Independent Effects of Cholera Toxin on B Cell Activation. II. Binding of Ganglioside GM1 Induces B Cell Activation
    • Francis, M. L.; Ryan, J.; Jobling, M. G.; Holmes, R. K.; Moss, J.; Mond, J. J. Cyclic AMP-Independent Effects of Cholera Toxin on B Cell Activation. II. Binding of Ganglioside GM1 Induces B Cell Activation J. Immunol. 1992, 148 (7) 1999-2005
    • (1992) J. Immunol. , vol.148 , Issue.7 , pp. 1999-2005
    • Francis, M.L.1    Ryan, J.2    Jobling, M.G.3    Holmes, R.K.4    Moss, J.5    Mond, J.J.6
  • 195
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of Glycolipid and Glycosylphosphatidylinositol-Anchored Proteins in Lymphoid Cells: Accumulation of Actin Regulated by Local Tyrosine Phosphorylation
    • Harder, T.; Simons, K. Clusters of Glycolipid and Glycosylphosphatidylinositol-Anchored Proteins in Lymphoid Cells: Accumulation of Actin Regulated by Local Tyrosine Phosphorylation Eur. J. Immunol. 1999, 29 (2) 556-562 10.1002/(SICI)1521-4141(199902)29:02<556::AID-IMMU556>3.0.CO;2-2
    • (1999) Eur. J. Immunol. , vol.29 , Issue.2 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 196
    • 84856713971 scopus 로고    scopus 로고
    • Analysis of Cholesterol Trafficking with Fluorescent Probes
    • Maxfield, F. R.; Wüstner, D. Analysis of Cholesterol Trafficking with Fluorescent Probes Methods Cell Biol. 2012, 108, 367-393 10.1016/B978-0-12-386487-1.00017-1
    • (2012) Methods Cell Biol. , vol.108 , pp. 367-393
    • Maxfield, F.R.1    Wüstner, D.2
  • 197
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of Phosphoinositides That Bind Pleckstrin Homology Domains: Calcium- and Agonist-Induced Dynamic Changes and Relationship to Myo-[3H]inositol-Labeled Phosphoinositide Pools
    • Várnai, P.; Balla, T. Visualization of Phosphoinositides That Bind Pleckstrin Homology Domains: Calcium- and Agonist-Induced Dynamic Changes and Relationship to Myo-[3H]inositol-Labeled Phosphoinositide Pools J. Cell Biol. 1998, 143 (2) 501-510 10.1083/jcb.143.2.501
    • (1998) J. Cell Biol. , vol.143 , Issue.2 , pp. 501-510
    • Várnai, P.1    Balla, T.2
  • 198
    • 84928141099 scopus 로고    scopus 로고
    • CRISPR/Cas9-Mediated Endogenous Protein Tagging for RESOLFT Super-Resolution Microscopy of Living Human Cells
    • Ratz, M.; Testa, I.; Hell, S. W.; Jakobs, S. CRISPR/Cas9-Mediated Endogenous Protein Tagging for RESOLFT Super-Resolution Microscopy of Living Human Cells Sci. Rep. 2015, 5, 9592 10.1038/srep09592
    • (2015) Sci. Rep. , vol.5 , pp. 9592
    • Ratz, M.1    Testa, I.2    Hell, S.W.3    Jakobs, S.4
  • 199
    • 79955544152 scopus 로고    scopus 로고
    • Chemically Induced Photoswitching of Fluorescent Probes - A General Concept for Super-Resolution Microscopy
    • Endesfelder, U.; Malkusch, S.; Flottmann, B.; Mondry, J.; Liguzinski, P.; Verveer, P. J.; Heilemann, M. Chemically Induced Photoswitching of Fluorescent Probes-A General Concept for Super-Resolution Microscopy Molecules 2011, 16 (4) 3106-3118 10.3390/molecules16043106
    • (2011) Molecules , vol.16 , Issue.4 , pp. 3106-3118
    • Endesfelder, U.1    Malkusch, S.2    Flottmann, B.3    Mondry, J.4    Liguzinski, P.5    Verveer, P.J.6    Heilemann, M.7
  • 200
    • 84863208605 scopus 로고    scopus 로고
    • Rational Design of True Monomeric and Bright Photoactivatable Fluorescent Proteins
    • Zhang, M.; Chang, H.; Zhang, Y.; Yu, J.; Wu, L.; Ji, W.; Chen, J.; Liu, B.; Lu, J.; Liu, Y. et al. Rational Design of True Monomeric and Bright Photoactivatable Fluorescent Proteins Nat. Methods 2012, 9 (7) 727-729 10.1038/nmeth.2021
    • (2012) Nat. Methods , vol.9 , Issue.7 , pp. 727-729
    • Zhang, M.1    Chang, H.2    Zhang, Y.3    Yu, J.4    Wu, L.5    Ji, W.6    Chen, J.7    Liu, B.8    Lu, J.9    Liu, Y.10
  • 201
    • 0028295474 scopus 로고
    • Reduction-of-Dimensionality Kinetics at Reaction-Limited Cell Surface Receptors
    • Axelrod, D.; Wang, M. D. Reduction-of-Dimensionality Kinetics at Reaction-Limited Cell Surface Receptors Biophys. J. 1994, 66 (3) 588-600 10.1016/S0006-3495(94)80834-3
    • (1994) Biophys. J. , vol.66 , Issue.3 , pp. 588-600
    • Axelrod, D.1    Wang, M.D.2
  • 202
    • 0022625444 scopus 로고
    • Rates of Membrane-Associated Reactions: Reduction of Dimensionality Revisited
    • McCloskey, M. A.; Poo, M. M. Rates of Membrane-Associated Reactions: Reduction of Dimensionality Revisited J. Cell Biol. 1986, 102 (1) 88-96 10.1083/jcb.102.1.88
    • (1986) J. Cell Biol. , vol.102 , Issue.1 , pp. 88-96
    • McCloskey, M.A.1    Poo, M.M.2
  • 204
    • 0036841874 scopus 로고    scopus 로고
    • Triton Promotes Domain Formation in Lipid Raft Mixtures
    • Heerklotz, H. Triton Promotes Domain Formation in Lipid Raft Mixtures Biophys. J. 2002, 83 (5) 2693-2701 10.1016/S0006-3495(02)75278-8
    • (2002) Biophys. J. , vol.83 , Issue.5 , pp. 2693-2701
    • Heerklotz, H.1
  • 205
    • 0038730762 scopus 로고    scopus 로고
    • The Sensitivity of Lipid Domains to Small Perturbations Demonstrated by the Effect of Triton
    • Heerklotz, H.; Szadkowska, H.; Anderson, T.; Seelig, J. The Sensitivity of Lipid Domains to Small Perturbations Demonstrated by the Effect of Triton J. Mol. Biol. 2003, 329 (4) 793-799 10.1016/S0022-2836(03)00504-7
    • (2003) J. Mol. Biol. , vol.329 , Issue.4 , pp. 793-799
    • Heerklotz, H.1    Szadkowska, H.2    Anderson, T.3    Seelig, J.4
  • 207
    • 34247861082 scopus 로고    scopus 로고
    • Plasma Membrane-Associated Proteins Are Clustered into Islands Attached to the Cytoskeleton
    • Lillemeier, B. F.; Pfeiffer, J. R.; Surviladze, Z.; Wilson, B. S.; Davis, M. M. Plasma Membrane-Associated Proteins Are Clustered into Islands Attached to the Cytoskeleton Proc. Natl. Acad. Sci. U. S. A. 2006, 103 (50) 18992-18997 10.1073/pnas.0609009103
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.50 , pp. 18992-18997
    • Lillemeier, B.F.1    Pfeiffer, J.R.2    Surviladze, Z.3    Wilson, B.S.4    Davis, M.M.5
  • 208
    • 84895513092 scopus 로고    scopus 로고
    • Correlative Super-Resolution Fluorescence and Metal-Replica Transmission Electron Microscopy
    • Sochacki, K. A.; Shtengel, G.; van Engelenburg, S. B.; Hess, H. F.; Taraska, J. W. Correlative Super-Resolution Fluorescence and Metal-Replica Transmission Electron Microscopy Nat. Methods 2014, 11 (3) 305-308 10.1038/nmeth.2816
    • (2014) Nat. Methods , vol.11 , Issue.3 , pp. 305-308
    • Sochacki, K.A.1    Shtengel, G.2    Van Engelenburg, S.B.3    Hess, H.F.4    Taraska, J.W.5
  • 209
    • 84990866214 scopus 로고    scopus 로고
    • Critical Importance of Appropriate Fixation Conditions for Faithful Imaging of Receptor Microclusters
    • Stanly, T. A.; Fritzsche, M.; Banerji, S.; García, E.; de la Serna, J. B.; Jackson, D. G.; Eggeling, C. Critical Importance of Appropriate Fixation Conditions for Faithful Imaging of Receptor Microclusters Biol. Open 2016, 5 (9) 1343-1350 10.1242/bio.019943
    • (2016) Biol. Open , vol.5 , Issue.9 , pp. 1343-1350
    • Stanly, T.A.1    Fritzsche, M.2    Banerji, S.3    García, E.4    De La Serna, J.B.5    Jackson, D.G.6    Eggeling, C.7
  • 211
    • 75249105436 scopus 로고    scopus 로고
    • Fast STED Microscopy with Continuous Wave Fiber Lasers
    • Moneron, G.; Medda, R.; Hein, B.; Giske, A.; Westphal, V.; Hell, S. W. Fast STED Microscopy with Continuous Wave Fiber Lasers Opt. Express 2010, 18 (2) 1302-1309 10.1364/OE.18.001302
    • (2010) Opt. Express , vol.18 , Issue.2 , pp. 1302-1309
    • Moneron, G.1    Medda, R.2    Hein, B.3    Giske, A.4    Westphal, V.5    Hell, S.W.6
  • 213
    • 84908281743 scopus 로고    scopus 로고
    • Oxygen Depletion Speeds and Simplifies Diffusion in HeLa Cells
    • Edwald, E.; Stone, M. B.; Gray, E. M.; Wu, J.; Veatch, S. L. Oxygen Depletion Speeds and Simplifies Diffusion in HeLa Cells Biophys. J. 2014, 107 (8) 1873-1884 10.1016/j.bpj.2014.08.023
    • (2014) Biophys. J. , vol.107 , Issue.8 , pp. 1873-1884
    • Edwald, E.1    Stone, M.B.2    Gray, E.M.3    Wu, J.4    Veatch, S.L.5
  • 215
    • 84891864540 scopus 로고    scopus 로고
    • Bayesian Total Internal Reflection Fluorescence Correlation Spectroscopy Reveals hIAPP-Induced Plasma Membrane Domain Organization in Live Cells
    • Guo, S.-M.; Bag, N.; Mishra, A.; Wohland, T.; Bathe, M. Bayesian Total Internal Reflection Fluorescence Correlation Spectroscopy Reveals hIAPP-Induced Plasma Membrane Domain Organization in Live Cells Biophys. J. 2014, 106 (1) 190-200 10.1016/j.bpj.2013.11.4458
    • (2014) Biophys. J. , vol.106 , Issue.1 , pp. 190-200
    • Guo, S.-M.1    Bag, N.2    Mishra, A.3    Wohland, T.4    Bathe, M.5
  • 216
    • 84880675693 scopus 로고    scopus 로고
    • Fast Spatiotemporal Correlation Spectroscopy to Determine Protein Lateral Diffusion Laws in Live Cell Membranes
    • Di Rienzo, C.; Gratton, E.; Beltram, F.; Cardarelli, F. Fast Spatiotemporal Correlation Spectroscopy to Determine Protein Lateral Diffusion Laws in Live Cell Membranes Proc. Natl. Acad. Sci. U. S. A. 2013, 110 (30) 12307-12312 10.1073/pnas.1222097110
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , Issue.30 , pp. 12307-12312
    • Di Rienzo, C.1    Gratton, E.2    Beltram, F.3    Cardarelli, F.4
  • 217
    • 21044433334 scopus 로고    scopus 로고
    • Podosomes at a Glance
    • Linder, S.; Kopp, P. Podosomes at a Glance J. Cell Sci. 2005, 118 (10) 2079-2082 10.1242/jcs.02390
    • (2005) J. Cell Sci. , vol.118 , Issue.10 , pp. 2079-2082
    • Linder, S.1    Kopp, P.2
  • 219
    • 4444310711 scopus 로고    scopus 로고
    • Lymphocyte Microvilli Are Dynamic, Actin-Dependent Structures That Do Not Require Wiskott-Aldrich Syndrome Protein (WASp) for Their Morphology
    • Majstoravich, S.; Zhang, J.; Nicholson-Dykstra, S.; Linder, S.; Friedrich, W.; Siminovitch, K. A.; Higgs, H. N. Lymphocyte Microvilli Are Dynamic, Actin-Dependent Structures That Do Not Require Wiskott-Aldrich Syndrome Protein (WASp) for Their Morphology Blood 2004, 104 (5) 1396-1403 10.1182/blood-2004-02-0437
    • (2004) Blood , vol.104 , Issue.5 , pp. 1396-1403
    • Majstoravich, S.1    Zhang, J.2    Nicholson-Dykstra, S.3    Linder, S.4    Friedrich, W.5    Siminovitch, K.A.6    Higgs, H.N.7
  • 222
    • 55049135085 scopus 로고    scopus 로고
    • Stimulated Emission Depletion (STED) Nanoscopy of a Fluorescent Protein-Labeled Organelle inside a Living Cell
    • Hein, B.; Willig, K. I.; Hell, S. W. Stimulated Emission Depletion (STED) Nanoscopy of a Fluorescent Protein-Labeled Organelle inside a Living Cell Proc. Natl. Acad. Sci. U. S. A. 2008, 105 (38) 14271-14276 10.1073/pnas.0807705105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , Issue.38 , pp. 14271-14276
    • Hein, B.1    Willig, K.I.2    Hell, S.W.3
  • 223
    • 84964380497 scopus 로고    scopus 로고
    • Axial Superresolution via Multiangle TIRF Microscopy with Sequential Imaging and Photobleaching
    • Fu, Y.; Winter, P. W.; Rojas, R.; Wang, V.; McAuliffe, M.; Patterson, G. H. Axial Superresolution via Multiangle TIRF Microscopy with Sequential Imaging and Photobleaching Proc. Natl. Acad. Sci. U. S. A. 2016, 113 (16) 4368-4373 10.1073/pnas.1516715113
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , Issue.16 , pp. 4368-4373
    • Fu, Y.1    Winter, P.W.2    Rojas, R.3    Wang, V.4    McAuliffe, M.5    Patterson, G.H.6
  • 224
    • 84878763652 scopus 로고    scopus 로고
    • Consequences of Membrane Topography
    • Parmryd, I.; Önfelt, B. Consequences of Membrane Topography FEBS J. 2013, 280 (12) 2775-2784 10.1111/febs.12209
    • (2013) FEBS J. , vol.280 , Issue.12 , pp. 2775-2784
    • Parmryd, I.1    Önfelt, B.2
  • 225
    • 61449194210 scopus 로고    scopus 로고
    • Binding Specificity of SH2 Domains: Insight from Free Energy Simulations
    • Gan, W.; Roux, B. Binding Specificity of SH2 Domains: Insight from Free Energy Simulations Proteins: Struct., Funct., Genet. 2009, 74 (4) 996-1007 10.1002/prot.22209
    • (2009) Proteins: Struct., Funct., Genet. , vol.74 , Issue.4 , pp. 996-1007
    • Gan, W.1    Roux, B.2
  • 226
    • 0037070567 scopus 로고    scopus 로고
    • High Free Energy of Lipid/protein Interaction in Biological Membranes
    • Sandermann, H., Jr. High Free Energy of Lipid/protein Interaction in Biological Membranes FEBS Lett. 2002, 514 (2-3) 340-342 10.1016/S0014-5793(02)02400-6
    • (2002) FEBS Lett. , vol.514 , Issue.23 , pp. 340-342
    • Sandermann, Jr.H.1
  • 227
    • 84904966494 scopus 로고    scopus 로고
    • Far-Red Organic Fluorophores Contain a Fluorescent Impurity
    • Stone, M. B.; Veatch, S. L. Far-Red Organic Fluorophores Contain a Fluorescent Impurity ChemPhysChem 2014, 15 (11) 2240-2246 10.1002/cphc.201402002
    • (2014) ChemPhysChem , vol.15 , Issue.11 , pp. 2240-2246
    • Stone, M.B.1    Veatch, S.L.2
  • 229
    • 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 10.1016/S0006-3495(02)75618-X
    • (2002) Biophys. J. , vol.82 , Issue.5 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 230
    • 84947576482 scopus 로고    scopus 로고
    • Optimal Drift Correction for Superresolution Localization Microscopy with Bayesian Inference
    • Elmokadem, A.; Yu, J. Optimal Drift Correction for Superresolution Localization Microscopy with Bayesian Inference Biophys. J. 2015, 109 (9) 1772-1780 10.1016/j.bpj.2015.09.017
    • (2015) Biophys. J. , vol.109 , Issue.9 , pp. 1772-1780
    • Elmokadem, A.1    Yu, J.2
  • 231
    • 84968558081 scopus 로고    scopus 로고
    • Removing Orientation-Induced Localization Biases in Single-Molecule Microscopy Using a Broadband Metasurface Mask
    • Backlund, M. P.; Arbabi, A.; Petrov, P. N.; Arbabi, E.; Saurabh, S.; Faraon, A.; Moerner, W. E. Removing Orientation-Induced Localization Biases in Single-Molecule Microscopy Using a Broadband Metasurface Mask Nat. Photonics 2016, 10 (7) 459-462 10.1038/nphoton.2016.93
    • (2016) Nat. Photonics , vol.10 , Issue.7 , pp. 459-462
    • Backlund, M.P.1    Arbabi, A.2    Petrov, P.N.3    Arbabi, E.4    Saurabh, S.5    Faraon, A.6    Moerner, W.E.7
  • 232
    • 84861979783 scopus 로고    scopus 로고
    • A Simple, Versatile Method for GFP-Based Super-Resolution Microscopy via Nanobodies
    • Ries, J.; Kaplan, C.; Platonova, E.; Eghlidi, H.; Ewers, H. A Simple, Versatile Method for GFP-Based Super-Resolution Microscopy via Nanobodies Nat. Methods 2012, 9 (6) 582-584 10.1038/nmeth.1991
    • (2012) Nat. Methods , vol.9 , Issue.6 , pp. 582-584
    • Ries, J.1    Kaplan, C.2    Platonova, E.3    Eghlidi, H.4    Ewers, H.5
  • 233
    • 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.; Ökten, Z.; Rock, R. S.; Dawson, J. F.; Spudich, J. A. Single Molecule High-Resolution Colocalization of Cy3 and Cy5 Attached to Macromolecules Measures Intramolecular Distances through Time Proc. Natl. Acad. Sci. U. S. A. 2005, 102 (5) 1419-1423 10.1073/pnas.0409487102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.5 , pp. 1419-1423
    • Churchman, L.S.1    Ökten, Z.2    Rock, R.S.3    Dawson, J.F.4    Spudich, J.A.5
  • 235
    • 84907857741 scopus 로고    scopus 로고
    • Twinkle, Twinkle Little Star: Photoswitchable Fluorophores for Super-Resolution Imaging
    • Chozinski, T. J.; Gagnon, L. A.; Vaughan, J. C. Twinkle, Twinkle Little Star: Photoswitchable Fluorophores for Super-Resolution Imaging FEBS Lett. 2014, 588 (19) 3603-3612 10.1016/j.febslet.2014.06.043
    • (2014) FEBS Lett. , vol.588 , Issue.19 , pp. 3603-3612
    • Chozinski, T.J.1    Gagnon, L.A.2    Vaughan, J.C.3
  • 237
    • 84940501708 scopus 로고    scopus 로고
    • Extended-Resolution Structured Illumination Imaging of Endocytic and Cytoskeletal Dynamics
    • Li, D.; Shao, L.; Chen, B.-C.; Zhang, X.; Zhang, M.; Moses, B.; Milkie, D. E.; Beach, J. R.; Hammer, J. A.; Pasham, M. et al. Extended-Resolution Structured Illumination Imaging of Endocytic and Cytoskeletal Dynamics Science 2015, 349 (6251) aab3500 10.1126/science.aab3500
    • (2015) Science , vol.349 , Issue.6251 , pp. aab3500
    • Li, D.1    Shao, L.2    Chen, B.-C.3    Zhang, X.4    Zhang, M.5    Moses, B.6    Milkie, D.E.7    Beach, J.R.8    Hammer, J.A.9    Pasham, M.10
  • 238
    • 84879747564 scopus 로고    scopus 로고
    • Light-Sheet Confined Super-Resolution Using Two-Photon Photoactivation
    • Cella Zanacchi, F.; Lavagnino, Z.; Faretta, M.; Furia, L.; Diaspro, A. Light-Sheet Confined Super-Resolution Using Two-Photon Photoactivation PLoS One 2013, 8 (7) e67667 10.1371/journal.pone.0067667
    • (2013) PLoS One , vol.8 , Issue.7 , pp. e67667
    • Cella Zanacchi, F.1    Lavagnino, Z.2    Faretta, M.3    Furia, L.4    Diaspro, A.5
  • 239
    • 84929095475 scopus 로고    scopus 로고
    • Super-Resolution Two-Photon Microscopy via Scanning Patterned Illumination
    • Urban, B. E.; Yi, J.; Chen, S.; Dong, B.; Zhu, Y.; DeVries, S. H.; Backman, V.; Zhang, H. F. Super-Resolution Two-Photon Microscopy via Scanning Patterned Illumination Phys. Rev. E 2015, 91 (4) 042703 10.1103/PhysRevE.91.042703
    • (2015) Phys. Rev. e , vol.91 , Issue.4 , pp. 042703
    • Urban, B.E.1    Yi, J.2    Chen, S.3    Dong, B.4    Zhu, Y.5    DeVries, S.H.6    Backman, V.7    Zhang, H.F.8
  • 240
    • 84897462187 scopus 로고    scopus 로고
    • Correction of Depth-Dependent Aberrations in 3D Single Molecule Localization and Super-Resolution Microscopy
    • McGorty, R.; Schnitzbauer, J.; Zhang, W.; Huang, B. Correction of Depth-Dependent Aberrations in 3D Single Molecule Localization and Super-Resolution Microscopy Opt. Lett. 2014, 39 (2) 275-278 10.1364/OL.39.000275
    • (2014) Opt. Lett. , vol.39 , Issue.2 , pp. 275-278
    • McGorty, R.1    Schnitzbauer, J.2    Zhang, W.3    Huang, B.4
  • 241
    • 84890076034 scopus 로고    scopus 로고
    • Three Dimensional Single Molecule Localization Using a Phase Retrieved Pupilfunction
    • Liu, S.; Kromann, E. B.; Krueger, W. D.; Bewersdorf, J.; Lidke, K. A. Three Dimensional Single Molecule Localization Using a Phase Retrieved Pupilfunction Opt. Express 2013, 21 (24) 29462-29487 10.1364/OE.21.029462
    • (2013) Opt. Express , vol.21 , Issue.24 , pp. 29462-29487
    • Liu, S.1    Kromann, E.B.2    Krueger, W.D.3    Bewersdorf, J.4    Lidke, K.A.5
  • 242
    • 0037572308 scopus 로고    scopus 로고
    • Phase Retrieval for High-Numerical-Aperture Optical Systems
    • Hanser, B. M.; Gustafsson, M. G. L.; Agard, D. A.; Sedat, J. W. Phase Retrieval for High-Numerical-Aperture Optical Systems Opt. Lett. 2003, 28 (10) 801-803 10.1364/OL.28.000801
    • (2003) Opt. Lett. , vol.28 , Issue.10 , pp. 801-803
    • Hanser, B.M.1    Gustafsson, M.G.L.2    Agard, D.A.3    Sedat, J.W.4
  • 243
    • 84935838542 scopus 로고    scopus 로고
    • Precise Three-Dimensional Scan-Free Multiple-Particle Tracking over Large Axial Ranges with Tetrapod Point Spread Functions
    • Shechtman, Y.; Weiss, L. E.; Backer, A. S.; Sahl, S. J.; Moerner, W. E. Precise Three-Dimensional Scan-Free Multiple-Particle Tracking over Large Axial Ranges with Tetrapod Point Spread Functions Nano Lett. 2015, 15 (6) 4194-4199 10.1021/acs.nanolett.5b01396
    • (2015) Nano Lett. , vol.15 , Issue.6 , pp. 4194-4199
    • Shechtman, Y.1    Weiss, L.E.2    Backer, A.S.3    Sahl, S.J.4    Moerner, W.E.5
  • 244
    • 84856386755 scopus 로고    scopus 로고
    • Optimal 3D Single-Molecule Localization for Superresolution Microscopy with Aberrations and Engineered Point Spread Functions
    • Quirin, S.; Pavani, S. R. P.; Piestun, R. Optimal 3D Single-Molecule Localization for Superresolution Microscopy with Aberrations and Engineered Point Spread Functions Proc. Natl. Acad. Sci. U. S. A. 2012, 109 (3) 675-679 10.1073/pnas.1109011108
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.3 , pp. 675-679
    • Quirin, S.1    Pavani, S.R.P.2    Piestun, R.3
  • 245
    • 84902968088 scopus 로고    scopus 로고
    • Imaging Cellular Ultrastructure by PALM, iPALM, and Correlative iPALM-EM
    • Shtengel, G.; Wang, Y.; Zhang, Z.; Goh, W. I.; Hess, H. F.; Kanchanawong, P. Imaging Cellular Ultrastructure by PALM, iPALM, and Correlative iPALM-EM Methods Cell Biol. 2014, 123, 273-294 10.1016/B978-0-12-420138-5.00015-X
    • (2014) Methods Cell Biol. , vol.123 , pp. 273-294
    • Shtengel, G.1    Wang, Y.2    Zhang, Z.3    Goh, W.I.4    Hess, H.F.5    Kanchanawong, P.6


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