메뉴 건너뛰기




Volumn 1798, Issue 4, 2010, Pages 777-787

A nanometer scale optical view on the compartmentalization of cell membranes

Author keywords

Lipid raft; Membrane nanodomain; Near field scanning optical microscopy; Single molecule detection; Super resolution optical microscopy

Indexed keywords

MEMBRANE PROTEIN;

EID: 77449114018     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2009.09.012     Document Type: Review
Times cited : (52)

References (116)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., and Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 175 (1972) 720-731
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson K., Sheets E.D., and Simon R. Revisiting the fluid mosaic model of membranes. Science 268 (1995) 1441-1442
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simon, R.3
  • 3
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • Maxfield F.R. Plasma membrane microdomains. Curr. Opin. Cell Biol. 14 (2002) 483-487
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 4
    • 33746303104 scopus 로고    scopus 로고
    • Methods to measure the lateral diffusion of membrane lipids and proteins
    • Chen Y., Lagerholm B.C., Yang B., and Jacobson K. Methods to measure the lateral diffusion of membrane lipids and proteins. Methods 39 (2006) 147-153
    • (2006) Methods , vol.39 , pp. 147-153
    • Chen, Y.1    Lagerholm, B.C.2    Yang, B.3    Jacobson, K.4
  • 5
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouritsen O.G., and Anderson R.G.W. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9 (2007) 7-14
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 6
    • 58149196187 scopus 로고    scopus 로고
    • Tracking microdomains in cells membranes
    • Day C.A., and Kenworthy A.K. Tracking microdomains in cells membranes. Biochim. Biophys. Acta 1788 (2009) 245-253
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 245-253
    • Day, C.A.1    Kenworthy, A.K.2
  • 7
    • 58149196402 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in membrane structure elucidation
    • Chiantia S., Ries J., and Schwille P. Fluorescence correlation spectroscopy in membrane structure elucidation. Biochim. Biophys. Acta 1788 (2009) 225-233
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 225-233
    • Chiantia, S.1    Ries, J.2    Schwille, P.3
  • 8
    • 0038557037 scopus 로고    scopus 로고
    • Lipids on the frontier: a century of cell membrane bilayers
    • Edidin M. Lipids on the frontier: a century of cell membrane bilayers. Nat. Rev. Mol. Cell Bio. 4 (2003) 414-418
    • (2003) Nat. Rev. Mol. Cell Bio. , vol.4 , pp. 414-418
    • Edidin, M.1
  • 10
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor S., and Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5 (2004) 231-240
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 11
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: contentious only from simplistic standpoints
    • Hancock J.F. Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Bio. 7 (2006) 456-462
    • (2006) Nat. Rev. Mol. Cell Bio. , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 12
    • 0036733284 scopus 로고    scopus 로고
    • Caveolae: from cell biology to animal physiology
    • Razani B., Woodman S.E., and Lisanti M.P. Caveolae: from cell biology to animal physiology. Pharmacol. Rev 54 (2002) 431-467
    • (2002) Pharmacol. Rev , vol.54 , pp. 431-467
    • Razani, B.1    Woodman, S.E.2    Lisanti, M.P.3
  • 13
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: a report on the Keystone symposium on lipid rafts and cell function
    • Pike L.J. Rafts defined: a report on the Keystone symposium on lipid rafts and cell function. J. Lipid Res. 47 (2006) 1597-1598
    • (2006) J. Lipid Res. , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 16
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor S., and Pagano R.E. Pathways of clathrin-independent endocytosis. Nat Rev. Mol. Cell Bio. 8 (2007) 603-612
    • (2007) Nat Rev. Mol. Cell Bio. , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 17
    • 33645288264 scopus 로고    scopus 로고
    • Lipid rafts in lymphocyte activation and migration
    • Manes S., and Viola A. Lipid rafts in lymphocyte activation and migration. Mol. Mem. Biol. 23 (2006) 59-69
    • (2006) Mol. Mem. Biol. , vol.23 , pp. 59-69
    • Manes, S.1    Viola, A.2
  • 18
    • 33746732294 scopus 로고    scopus 로고
    • Virus infection and lipid rafts
    • Suzuki T., and Suzuki Y. Virus infection and lipid rafts. Biol. Pharma. Bull. 29 (2006) 1538-1541
    • (2006) Biol. Pharma. Bull. , vol.29 , pp. 1538-1541
    • Suzuki, T.1    Suzuki, Y.2
  • 19
    • 33847706096 scopus 로고    scopus 로고
    • Lipid rafts in health and disease
    • Michel V., and Bakovic M. Lipid rafts in health and disease. Biol. Cell 99 (2007) 129-140
    • (2007) Biol. Cell , vol.99 , pp. 129-140
    • Michel, V.1    Bakovic, M.2
  • 21
    • 1342306818 scopus 로고    scopus 로고
    • Mayor, Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P., Varma R., Sarasij R.C., Ira K., Gousset G., Krishnamoorthy M., and Rao S. Mayor, Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116 (2004) 577-589
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    Ira, K.4    Gousset, G.5    Krishnamoorthy, M.6    Rao, S.7
  • 24
    • 4644364556 scopus 로고    scopus 로고
    • Visualization of plasma membrane compartmentalization with patterned lipid bilayers
    • Wu M., Holowka D., Craighead H.G., and Baird B. Visualization of plasma membrane compartmentalization with patterned lipid bilayers. Proc. Natl. Acad. Sci. USA 101 (2004) 13798-13803
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13798-13803
    • Wu, M.1    Holowka, D.2    Craighead, H.G.3    Baird, B.4
  • 25
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro S. An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14 (1995) 4695-4704
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 26
    • 0037438349 scopus 로고    scopus 로고
    • Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling
    • Fragoso R., Ren D., Zhang X., Su M.W., Burakoff S.J., and Jin Y.J. Lipid raft distribution of CD4 depends on its palmitoylation and association with Lck, and evidence for CD4-induced lipid raft aggregation as an additional mechanism to enhance CD3 signaling. J. Immunol. 170 (2003) 913-921
    • (2003) J. Immunol. , vol.170 , pp. 913-921
    • Fragoso, R.1    Ren, D.2    Zhang, X.3    Su, M.W.4    Burakoff, S.J.5    Jin, Y.J.6
  • 27
    • 0037067715 scopus 로고    scopus 로고
    • Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts
    • Yamabhai M., and Anderson R.G. Second cysteine-rich region of epidermal growth factor receptor contains targeting information for caveolae/rafts. J. Bio. Chem. 277 (2002) 24843-24846
    • (2002) J. Bio. Chem. , vol.277 , pp. 24843-24846
    • Yamabhai, M.1    Anderson, R.G.2
  • 29
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass A.D., and Vale R.D. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121 (2005) 937-950
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 32
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: more than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 114 (2001) 4143-4151
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 34
    • 0036214457 scopus 로고    scopus 로고
    • Relationship of lipid rafts to transient confinement zones detected by single particle tracking
    • Dietrich C., Yang B., Fujiwara T., Kusumi A., and Jacobson K. Relationship of lipid rafts to transient confinement zones detected by single particle tracking. Biophys. J. 82 (2002) 274-284
    • (2002) Biophys. J. , vol.82 , pp. 274-284
    • Dietrich, C.1    Yang, B.2    Fujiwara, T.3    Kusumi, A.4    Jacobson, K.5
  • 35
    • 35548942611 scopus 로고    scopus 로고
    • Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins
    • Viola A., and Gupta N. Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins. Nat. Rev. Immunol. 7 (2007) 889-896
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 889-896
    • Viola, A.1    Gupta, N.2
  • 36
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara T., Ritchie K., Murakoshi H., Jacobson K., and Kusumi A. Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Bio. 157 (2002) 1071-1081
    • (2002) J. Cell Bio. , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 37
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules
    • Kusumi A., Nakada C., Ritchie K., Murase K., Suzuki K., Murakoshi H., Kasai R.S., Kondo J., and Fujiwara T. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34 (2005) 351-378
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 40
    • 0030956033 scopus 로고    scopus 로고
    • Single particle tracking: applications to membrane dynamics
    • Saxton M., and Jacobson K. Single particle tracking: applications to membrane dynamics. Annu. Rev. Biophys. Biomol. Struct. 26 (1997) 373-399
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.1    Jacobson, K.2
  • 41
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy A. Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24 (2001) 289-296
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.1
  • 42
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov O.O., and Nichols B.J. Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat. Cell. Bio. 6 (2004) 238-243
    • (2004) Nat. Cell. Bio. , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 43
    • 58149201036 scopus 로고    scopus 로고
    • FRET analysis of domain formation and properties in complex membrane systems
    • Loura L.M.S., de Almeida R.F.M., Silva L.C., and Pietro M. FRET analysis of domain formation and properties in complex membrane systems. Biochim. Biophys. Acta 1788 (2009) 209-224
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 209-224
    • Loura, L.M.S.1    de Almeida, R.F.M.2    Silva, L.C.3    Pietro, M.4
  • 45
    • 22344442585 scopus 로고    scopus 로고
    • Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutitin
    • Hess S.T., Kumar M., Verma A., Farrington J., Kenworthy A., and Zimmerberg J. Quantitative electron microscopy and fluorescence spectroscopy of the membrane distribution of influenza hemagglutitin. J. Cell Bio. 169 (2005) 965-976
    • (2005) J. Cell Bio. , vol.169 , pp. 965-976
    • Hess, S.T.1    Kumar, M.2    Verma, A.3    Farrington, J.4    Kenworthy, A.5    Zimmerberg, J.6
  • 46
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior I., Muncke C., Parton R., and Hancock J. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Bio. 160 (2003) 165-170
    • (2003) J. Cell Bio. , vol.160 , pp. 165-170
    • Prior, I.1    Muncke, C.2    Parton, R.3    Hancock, J.4
  • 47
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman S.J., Muncke C., Parton R., and Hancock J. H-ras, K-ras, and inner plasma raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. USA. 102 (2005) 15500-15505
    • (2005) Proc. Natl. Acad. Sci. USA. , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.3    Hancock, J.4
  • 48
    • 18144387991 scopus 로고    scopus 로고
    • Nanoscale resolution in the focal plane of an optical microscope
    • Westphal V., and Hell S.W. Nanoscale resolution in the focal plane of an optical microscope. Phys. Rev. Lett. 94 (2005) 143903
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 143903
    • Westphal, V.1    Hell, S.W.2
  • 50
    • 33645839858 scopus 로고    scopus 로고
    • STED microscopy reveals hat synaptotagmin remains clustered after synpatic vesicle exocytosis
    • Willig K.I., Rizzoli S.O., Wesphal V., Jahn R., and Hell S.W. STED microscopy reveals hat synaptotagmin remains clustered after synpatic vesicle exocytosis. Nature 440 (2006) 935-939
    • (2006) Nature , vol.440 , pp. 935-939
    • Willig, K.I.1    Rizzoli, S.O.2    Wesphal, V.3    Jahn, R.4    Hell, S.W.5
  • 52
    • 33751547691 scopus 로고    scopus 로고
    • Nanoscale organization of nicotinic acetylcholine receptors revealed by stimulated emission depletion microscopy
    • Kellner R.R., Baier C.J., Willig K.I., Hell S.W., and Barrantes F.J. Nanoscale organization of nicotinic acetylcholine receptors revealed by stimulated emission depletion microscopy. Neuroscience 144 (2007) 135-143
    • (2007) Neuroscience , vol.144 , pp. 135-143
    • Kellner, R.R.1    Baier, C.J.2    Willig, K.I.3    Hell, S.W.4    Barrantes, F.J.5
  • 53
    • 42049108013 scopus 로고    scopus 로고
    • Video-rate far-field optical nanoscopy dissects synaptic vesicle movement
    • Wesphal V., Rizzoli S.O., Lauterbach M.A., Kamin D., Jahn R., and Hell S.W. Video-rate far-field optical nanoscopy dissects synaptic vesicle movement. Science 320 (2008) 246-249
    • (2008) Science , vol.320 , pp. 246-249
    • Wesphal, V.1    Rizzoli, S.O.2    Lauterbach, M.A.3    Kamin, D.4    Jahn, R.5    Hell, S.W.6
  • 55
    • 24944539530 scopus 로고    scopus 로고
    • Non-linear structured-illumination microscopy: wide-field fluorescence imaging with theoretically unlimited resolution
    • Gustafsson M.G.L. Non-linear structured-illumination microscopy: wide-field fluorescence imaging with theoretically unlimited resolution. Proc. Natl. Acad. Sci. USA 102 (2005) 13081-13086
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 13081-13086
    • Gustafsson, M.G.L.1
  • 58
    • 42149171410 scopus 로고    scopus 로고
    • A presynaptic giant ankrin stabilizes the NMJ through regulation of presynaptics microtubules and transsynaptic cell adehesion
    • Pielage J., Cheng L., Fetter R.D., Carlton P.M., Sedat J.W., and Davis G.W. A presynaptic giant ankrin stabilizes the NMJ through regulation of presynaptics microtubules and transsynaptic cell adehesion. Neuron 58 (2008) 195-209
    • (2008) Neuron , vol.58 , pp. 195-209
    • Pielage, J.1    Cheng, L.2    Fetter, R.D.3    Carlton, P.M.4    Sedat, J.W.5    Davis, G.W.6
  • 60
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess S.T., Girirajan T.P.K., and Mason M.D. Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophys. J. 91 (2006) 4258-4272
    • (2006) Biophys. J. , vol.91 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.K.2    Mason, M.D.3
  • 61
    • 33749026335 scopus 로고    scopus 로고
    • Subdiffraction limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust M.J., Bates M., and Zhuang X. Subdiffraction limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3 (2006) 793-796
    • (2006) Nat. Methods , vol.3 , pp. 793-796
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 64
    • 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., and Zimmerberg J. Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories. Proc. Natl. Acad. Sci. USA 104 (2007) 17370-17375
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , 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
  • 65
    • 42949083695 scopus 로고    scopus 로고
    • Live cell photoactivated localization microscopy of nanoscale adhesion dynamics
    • Schroff H., Galbraith C.G., Galbraith J.A., and Betzig E. Live cell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat. Methods 5 (2008) 417-423
    • (2008) Nat. Methods , vol.5 , pp. 417-423
    • Schroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 66
    • 34648826792 scopus 로고    scopus 로고
    • Multicolor super-resolution imaging with photo-switchable fluorescent probes
    • Bates M., Huang B., Dempsey G.T., and Zhuang X. Multicolor super-resolution imaging with photo-switchable fluorescent probes. Science 317 (2007) 1749-1753
    • (2007) Science , vol.317 , pp. 1749-1753
    • Bates, M.1    Huang, B.2    Dempsey, G.T.3    Zhuang, X.4
  • 67
    • 38949216802 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy
    • Huang B., Wang W., Bates M., and Zhuang X. Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy. Science 319 (2008) 810-813
    • (2008) Science , vol.319 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 71
    • 58149265015 scopus 로고    scopus 로고
    • Putting super-resolution fluorescence microscopy to work
    • Lippincott-Schwartz J., and Manley S. Putting super-resolution fluorescence microscopy to work. Nat. Methods 6 (2009) 21-23
    • (2009) Nat. Methods , vol.6 , pp. 21-23
    • Lippincott-Schwartz, J.1    Manley, S.2
  • 72
    • 65549088576 scopus 로고    scopus 로고
    • Advances in the speed and resolution of light microscopy
    • Ji N., Shroff H., Zhong H., and Betzig E. Advances in the speed and resolution of light microscopy. Curr. Opin. Neurobio. 18 (2008) 605-616
    • (2008) Curr. Opin. Neurobio. , vol.18 , pp. 605-616
    • Ji, N.1    Shroff, H.2    Zhong, H.3    Betzig, E.4
  • 73
    • 0021410769 scopus 로고
    • Optical stethoscopy: image recording with resolution λ/20
    • Pohl D.W., Denk W., and Lanz M. Optical stethoscopy: image recording with resolution λ/20. Appl. Phys. Lett. 44 (1984) 651-653
    • (1984) Appl. Phys. Lett. , vol.44 , pp. 651-653
    • Pohl, D.W.1    Denk, W.2    Lanz, M.3
  • 74
    • 12044259475 scopus 로고
    • Breaking the diffraction barrier: optical microscopy on a nanometric scale
    • Betzig E., Trautman J.K., Harris T.D., Weiner J.S., and Kostelak R.L. Breaking the diffraction barrier: optical microscopy on a nanometric scale. Science 251 (1991) 1468-1470
    • (1991) Science , vol.251 , pp. 1468-1470
    • Betzig, E.1    Trautman, J.K.2    Harris, T.D.3    Weiner, J.S.4    Kostelak, R.L.5
  • 76
    • 0000627596 scopus 로고    scopus 로고
    • Scanning near-field optical microscopy with aperture probes: fundamentals and applications
    • Hecht B., Sick B., Wild U.P., Deckert V., Zenobi R., Martin O.J.F., and Dieter D.W. Scanning near-field optical microscopy with aperture probes: fundamentals and applications. J. Chem. Phys. 112 (2000) 7761-7774
    • (2000) J. Chem. Phys. , vol.112 , pp. 7761-7774
    • Hecht, B.1    Sick, B.2    Wild, U.P.3    Deckert, V.4    Zenobi, R.5    Martin, O.J.F.6    Dieter, D.W.7
  • 77
    • 0029634150 scopus 로고
    • Piezo-electric tip-sample distance control for near field optical microscopes
    • Karrai K., and Grober R.D. Piezo-electric tip-sample distance control for near field optical microscopes. Appl. Phys. Lett. 66 (1995) 1842-1844
    • (1995) Appl. Phys. Lett. , vol.66 , pp. 1842-1844
    • Karrai, K.1    Grober, R.D.2
  • 80
    • 1542396457 scopus 로고
    • Scanning interferometric apertureless microscopy: optical imaging at 10 Angstrom resolution
    • Zenhausern F., Martin Y., and Wickramasinghe H.K. Scanning interferometric apertureless microscopy: optical imaging at 10 Angstrom resolution. Science 269 (1995) 1083-1085
    • (1995) Science , vol.269 , pp. 1083-1085
    • Zenhausern, F.1    Martin, Y.2    Wickramasinghe, H.K.3
  • 81
    • 33646717598 scopus 로고    scopus 로고
    • Near-field optical microscopy and spectroscopy with pointed probes
    • Novotny L., and Stranick S.J. Near-field optical microscopy and spectroscopy with pointed probes. Annu. Rev. Phys. Chem. 57 (2006) 303-331
    • (2006) Annu. Rev. Phys. Chem. , vol.57 , pp. 303-331
    • Novotny, L.1    Stranick, S.J.2
  • 82
    • 0001536175 scopus 로고    scopus 로고
    • Near-field fluorescence microscopy based on two-photon excitation with metal tips
    • Sanchez E.J., Novotny L., and Sunney-Xie X. Near-field fluorescence microscopy based on two-photon excitation with metal tips. Phys. Rev. Lett. 82 (1999) 4014-4017
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 4014-4017
    • Sanchez, E.J.1    Novotny, L.2    Sunney-Xie, X.3
  • 83
    • 33645057911 scopus 로고    scopus 로고
    • Enhancement and quenching of single-molecule fluorescence
    • Anger P., Bharadwaj P., and Novotny L. Enhancement and quenching of single-molecule fluorescence. Phys. Rev. Lett. 96 (2006) 1130021-1130024
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 1130021-1130024
    • Anger, P.1    Bharadwaj, P.2    Novotny, L.3
  • 84
    • 40449129184 scopus 로고    scopus 로고
    • 2+ transmembrane proteins in liquids
    • 2+ transmembrane proteins in liquids. Nano Lett. 8 (2008) 642-646
    • (2008) Nano Lett. , vol.8 , pp. 642-646
    • Höppener, C.1    Novotny, L.2
  • 85
    • 63649094330 scopus 로고    scopus 로고
    • Background suppression in near-field optical imaging
    • Höppener C., Beams R., and Novotny L. Background suppression in near-field optical imaging. Nano Lett. 9 (2009) 903-908
    • (2009) Nano Lett. , vol.9 , pp. 903-908
    • Höppener, C.1    Beams, R.2    Novotny, L.3
  • 88
    • 17844364215 scopus 로고    scopus 로고
    • High-resolution near-field optical imaging of single nuclear pore complexes under physiological conditions
    • Höppener C., Siebrasse J.P., Peters R., Kubitscheck U., and Naber A. High-resolution near-field optical imaging of single nuclear pore complexes under physiological conditions. Biophys. J. 88 (2005) 3681-3688
    • (2005) Biophys. J. , vol.88 , pp. 3681-3688
    • Höppener, C.1    Siebrasse, J.P.2    Peters, R.3    Kubitscheck, U.4    Naber, A.5
  • 89
    • 0034023562 scopus 로고    scopus 로고
    • Hybrid scanning ion conductance and scanning near-field optical microscopy for the study of living cells
    • Korchev Y.E., Raval M., Lab M.J., Gorelik J., Edwards C.R.W., Rayment T., and Klenerman D. Hybrid scanning ion conductance and scanning near-field optical microscopy for the study of living cells. Biophys. J. 78 (2000) 2675-2679
    • (2000) Biophys. J. , vol.78 , pp. 2675-2679
    • Korchev, Y.E.1    Raval, M.2    Lab, M.J.3    Gorelik, J.4    Edwards, C.R.W.5    Rayment, T.6    Klenerman, D.7
  • 90
    • 54949088235 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with sub-diffraction-limited resolution using near-field optical probes
    • Vobornik D., Banks D.S., Lu Z., Fradin C., Taylor R., and Johnston L.J. Fluorescence correlation spectroscopy with sub-diffraction-limited resolution using near-field optical probes. Appl. Phys. Lett. 93 (2008) 163904-163906
    • (2008) Appl. Phys. Lett. , vol.93 , pp. 163904-163906
    • Vobornik, D.1    Banks, D.S.2    Lu, Z.3    Fradin, C.4    Taylor, R.5    Johnston, L.J.6
  • 91
    • 41549145300 scopus 로고    scopus 로고
    • Optical antennas focus in on biology
    • Garcia-Parajo M.F. Optical antennas focus in on biology. Nature Photonics 2 (2008) 201-203
    • (2008) Nature Photonics , vol.2 , pp. 201-203
    • Garcia-Parajo, M.F.1
  • 92
    • 0028806195 scopus 로고
    • Nanoscale complexity of phospholipid monolayers investigated by near-field scanning optical microscopy
    • Hwang J., Tamm L.K., Bohm C., Ramalingam T.S., Betzig E., and Edidin M. Nanoscale complexity of phospholipid monolayers investigated by near-field scanning optical microscopy. Science 270 (1995) 610-614
    • (1995) Science , vol.270 , pp. 610-614
    • Hwang, J.1    Tamm, L.K.2    Bohm, C.3    Ramalingam, T.S.4    Betzig, E.5    Edidin, M.6
  • 93
    • 0031956655 scopus 로고    scopus 로고
    • Domains in cell plasma membranes investigated by near-field scanning optical microscopy
    • Hwang J., Gheber L.A., Margolis L., and Edidin M. Domains in cell plasma membranes investigated by near-field scanning optical microscopy. Biophys. J. 74 (1998) 2184-2190
    • (1998) Biophys. J. , vol.74 , pp. 2184-2190
    • Hwang, J.1    Gheber, L.A.2    Margolis, L.3    Edidin, M.4
  • 94
    • 0031835569 scopus 로고    scopus 로고
    • Submicron structure in l-α-dipalmitoylphosphatidyl-choline monolayers and bilayers probed with confocal, atomic force, and near-field microscopy
    • Hollars C.W., and Dunn R.C. Submicron structure in l-α-dipalmitoylphosphatidyl-choline monolayers and bilayers probed with confocal, atomic force, and near-field microscopy. Biophys. J 75 (1998) 342-353
    • (1998) Biophys. J , vol.75 , pp. 342-353
    • Hollars, C.W.1    Dunn, R.C.2
  • 95
    • 0031209152 scopus 로고    scopus 로고
    • Submicron fluorescence, topography, and compliance measurements of phase-separated lipid monolayers using tapping-mode near-field scanning optical microscopy
    • Hollars C.W., and Dunn R.C. Submicron fluorescence, topography, and compliance measurements of phase-separated lipid monolayers using tapping-mode near-field scanning optical microscopy. J. Phys. Chem. B 101 (1997) 6313-6317
    • (1997) J. Phys. Chem. B , vol.101 , pp. 6313-6317
    • Hollars, C.W.1    Dunn, R.C.2
  • 96
    • 0141732123 scopus 로고    scopus 로고
    • Two-color near-field fluorescence microscopy studies of microdomains ("Rafts") in model membranes
    • Burgos P., Yuan C., Viriot M.-L., and Johnston L.J. Two-color near-field fluorescence microscopy studies of microdomains ("Rafts") in model membranes. Langmuir 19 (2003) 8002-8009
    • (2003) Langmuir , vol.19 , pp. 8002-8009
    • Burgos, P.1    Yuan, C.2    Viriot, M.-L.3    Johnston, L.J.4
  • 97
    • 0036729508 scopus 로고    scopus 로고
    • Physical and photophysical characterization of a BODIPY phos-phatidylcholine as a membrane probe
    • Dahim M., Mizuno N., Li X.M., Momsen W.E., Momsen M.M., and Brockman H.L. Physical and photophysical characterization of a BODIPY phos-phatidylcholine as a membrane probe. Biophys. J. 83 (2002) 1511-1524
    • (2002) Biophys. J. , vol.83 , pp. 1511-1524
    • Dahim, M.1    Mizuno, N.2    Li, X.M.3    Momsen, W.E.4    Momsen, M.M.5    Brockman, H.L.6
  • 98
    • 34250668824 scopus 로고    scopus 로고
    • Ganglioside partitioning and aggregation in phase-separated monolayers characterized by bodipy GM1 monomer/dimer emission
    • Coban O., Burger M., Laliberte M., Ianoul A., and Johnston L.J. Ganglioside partitioning and aggregation in phase-separated monolayers characterized by bodipy GM1 monomer/dimer emission. Langmuir 23 (2007) 6704-6711
    • (2007) Langmuir , vol.23 , pp. 6704-6711
    • Coban, O.1    Burger, M.2    Laliberte, M.3    Ianoul, A.4    Johnston, L.J.5
  • 99
    • 0242576753 scopus 로고    scopus 로고
    • Phase separation in supported phospholipid bilayers visualized by near-field scanning optical microscopy in aqueous solution
    • Ianoul A., Burgos P., Lu Z., Taylor R.S., and Johnston L.J. Phase separation in supported phospholipid bilayers visualized by near-field scanning optical microscopy in aqueous solution. Langmuir 19 (2003) 9246-9254
    • (2003) Langmuir , vol.19 , pp. 9246-9254
    • Ianoul, A.1    Burgos, P.2    Lu, Z.3    Taylor, R.S.4    Johnston, L.J.5
  • 100
    • 0036326281 scopus 로고    scopus 로고
    • A near-field microscopy study of submicron domain structure in a model lung surfactant monolayer
    • Flanders B.N., and Dunn R.C. A near-field microscopy study of submicron domain structure in a model lung surfactant monolayer. Ultramicroscopy 91 (2002) 245-251
    • (2002) Ultramicroscopy , vol.91 , pp. 245-251
    • Flanders, B.N.1    Dunn, R.C.2
  • 101
    • 12944307342 scopus 로고    scopus 로고
    • High-resolution studies of lung surfactant collapse
    • Sibug-Aga R., and Dunn R.C. High-resolution studies of lung surfactant collapse. Photochem. Photobiol. 80 (2004) 471-476
    • (2004) Photochem. Photobiol. , vol.80 , pp. 471-476
    • Sibug-Aga, R.1    Dunn, R.C.2
  • 102
    • 8844266908 scopus 로고    scopus 로고
    • Imaging the selective binding of synapsin to anionic membrane domains
    • Murray J., Cuccia L., Ianoul A., Cheetham J., and Johnston L.J. Imaging the selective binding of synapsin to anionic membrane domains. Chembiochem 5 (2004) 1489-1494
    • (2004) Chembiochem , vol.5 , pp. 1489-1494
    • Murray, J.1    Cuccia, L.2    Ianoul, A.3    Cheetham, J.4    Johnston, L.J.5
  • 103
    • 33744804799 scopus 로고    scopus 로고
    • Effects of ceramide on liquid-ordered domains investigated by simultaneous AFM and FCS
    • Chiantia S., Kahya N., Ries J., and Schwille P. Effects of ceramide on liquid-ordered domains investigated by simultaneous AFM and FCS. Biophys. J. 90 (2006) 4500-4508
    • (2006) Biophys. J. , vol.90 , pp. 4500-4508
    • Chiantia, S.1    Kahya, N.2    Ries, J.3    Schwille, P.4
  • 108
    • 43249113149 scopus 로고    scopus 로고
    • NSOM/QD-based nanoscale immunofluorescence imaging of antigen-specific T-cell receptor responses during an in vivo clonal Vγ2Vδ2 T-cell expansion
    • Chen Y., Shao L., Ali Z., Cai J., and Chen Z.W. NSOM/QD-based nanoscale immunofluorescence imaging of antigen-specific T-cell receptor responses during an in vivo clonal Vγ2Vδ2 T-cell expansion. Blood 111 (2008) 4220-4232
    • (2008) Blood , vol.111 , pp. 4220-4232
    • Chen, Y.1    Shao, L.2    Ali, Z.3    Cai, J.4    Chen, Z.W.5
  • 109
    • 0033014064 scopus 로고    scopus 로고
    • Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy
    • Nagy P., Jenei A., Kirsch A.K., Sazollosi J., Damjanovich S., and Jovin T.M. Activation-dependent clustering of the erbB2 receptor tyrosine kinase detected by scanning near-field optical microscopy. J. Cell Sci. 112 (1999) 1733-1741
    • (1999) J. Cell Sci. , vol.112 , pp. 1733-1741
    • Nagy, P.1    Jenei, A.2    Kirsch, A.K.3    Sazollosi, J.4    Damjanovich, S.5    Jovin, T.M.6
  • 110
    • 0031017575 scopus 로고    scopus 로고
    • Membrane specific mapping and colocalization of malarial and host skeletal proteins in the Plasmodium falciparum infected erythrocyte by dual-color near-field scanning optical microscopy
    • Enderle T., Ha T., Ogletree D.F., Chemla D.S., Magowan C., and Weiss S. Membrane specific mapping and colocalization of malarial and host skeletal proteins in the Plasmodium falciparum infected erythrocyte by dual-color near-field scanning optical microscopy. Proc. Natl. Acad. Sci. USA 94 (1997) 520-525
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 520-525
    • Enderle, T.1    Ha, T.2    Ogletree, D.F.3    Chemla, D.S.4    Magowan, C.5    Weiss, S.6
  • 113
    • 63049139536 scopus 로고    scopus 로고
    • Fluorescence-topographic NSOM directly visualizes peak-valley polarities of GM1/GM3 rafts in cell membrane fluctuations
    • Chen Y., Qin J., and Chen Z. Fluorescence-topographic NSOM directly visualizes peak-valley polarities of GM1/GM3 rafts in cell membrane fluctuations. J. Lipid Res. 49 (2008) 2268-2275
    • (2008) J. Lipid Res. , vol.49 , pp. 2268-2275
    • Chen, Y.1    Qin, J.2    Chen, Z.3
  • 115
    • 36048946627 scopus 로고    scopus 로고
    • Neurite imaging of living PC12 cells with scanning electrochemical/near-field optical/atomic force microscopy
    • Ueda A., Niwa O., Maruyama K., Shindo Y., Oka K., and Suzuki K. Neurite imaging of living PC12 cells with scanning electrochemical/near-field optical/atomic force microscopy. Angew. Chem. Int. Ed. Engl. 46 (2007) 8238-8241
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 8238-8241
    • Ueda, A.1    Niwa, O.2    Maruyama, K.3    Shindo, Y.4    Oka, K.5    Suzuki, K.6
  • 116
    • 40549122287 scopus 로고    scopus 로고
    • Implementation of a bimorph-based aperture tapping-SNOM with an incubator to study the evolution of cultured living cells
    • Longo G., Girasole M., and Cricenti A. Implementation of a bimorph-based aperture tapping-SNOM with an incubator to study the evolution of cultured living cells. J. Microsc. 229 (2008) 433-439
    • (2008) J. Microsc. , vol.229 , pp. 433-439
    • Longo, G.1    Girasole, M.2    Cricenti, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.