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Volumn 127, Issue 23, 2014, Pages 4995-5005

Nanoclustering as a dominant feature of plasma membrane organization

Author keywords

Plasma membrane; Protein nanoclustering; Super resolution microscopy

Indexed keywords

B LYMPHOCYTE RECEPTOR; CD209 ANTIGEN; CELL MEMBRANE PROTEIN; F ACTIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; HEMAGGLUTININ; LIPID LINKED PROTEIN; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; MEMBRANE PROTEIN; RAS PROTEIN; T LYMPHOCYTE RECEPTOR; IMMUNOGLOBULIN RECEPTOR; MEMBRANE LIPID; NANOPARTICLE; PROTEIN AGGREGATE;

EID: 84914145217     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.146340     Document Type: Article
Times cited : (226)

References (80)
  • 1
    • 22944475303 scopus 로고    scopus 로고
    • Protein oligomerization: how and why
    • Ali, M. H. and Imperiali, B. (2005). Protein oligomerization: how and why. Bioorg. Med. Chem. 13, 5013-5020.
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 5013-5020
    • Ali, M.H.1    Imperiali, B.2
  • 2
    • 0037036135 scopus 로고    scopus 로고
    • A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    • Anderson, R. G. W. and Jacobson, K. (2002). A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science 296, 1821-1825.
    • (2002) Science , vol.296 , pp. 1821-1825
    • Anderson, R.G.W.1    Jacobson, K.2
  • 4
    • 44949124597 scopus 로고    scopus 로고
    • Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters
    • Belanis, L., Plowman, S. J., Rotblat, B., Hancock, J. F. and Kloog, Y. (2008). Galectin-1 is a novel structural component and a major regulator of h-ras nanoclusters. Mol. Biol. Cell 19, 1404-1414.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1404-1414
    • Belanis, L.1    Plowman, S.J.2    Rotblat, B.3    Hancock, J.F.4    Kloog, Y.5
  • 7
    • 76649135799 scopus 로고    scopus 로고
    • Signalling complexes and clusters: functional advantages and methodological hurdles
    • Cebecauer, M., Spitaler, M., Sergé, A. and Magee, A. I. (2010). Signalling complexes and clusters: functional advantages and methodological hurdles. J. Cell Sci. 123, 309-320.
    • (2010) J. Cell Sci. , vol.123 , pp. 309-320
    • Cebecauer, M.1    Spitaler, M.2    Sergé, A.3    Magee, A.I.4
  • 8
    • 33749544508 scopus 로고    scopus 로고
    • Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides
    • Chen, Y., Thelin, W. R., Yang, B., Milgram, S. L. and Jacobson, K. (2006). Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides. J. Cell Biol. 175, 169-178.
    • (2006) J. Cell Biol. , vol.175 , pp. 169-178
    • Chen, Y.1    Thelin, W.R.2    Yang, B.3    Milgram, S.L.4    Jacobson, K.5
  • 9
    • 70450236974 scopus 로고    scopus 로고
    • The transmembrane protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored protein, to the cytoskeleton
    • Chen, Y., Veracini, L., Benistant, C. and Jacobson, K. (2009). The transmembrane protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored protein, to the cytoskeleton. J. Cell Sci. 122, 3966-3972.
    • (2009) J. Cell Sci. , vol.122 , pp. 3966-3972
    • Chen, Y.1    Veracini, L.2    Benistant, C.3    Jacobson, K.4
  • 11
    • 9444291849 scopus 로고    scopus 로고
    • Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: relevance to co-stimulation
    • Delaguillaumie, A., Harriague, J., Kohanna, S., Bismuth, G., Rubinstein, E., Seigneuret, M. and Conjeaud, H. (2004). Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: relevance to co-stimulation. J. Cell Sci. 117, 5269-5282.
    • (2004) J. Cell Sci. , vol.117 , pp. 5269-5282
    • Delaguillaumie, A.1    Harriague, J.2    Kohanna, S.3    Bismuth, G.4    Rubinstein, E.5    Seigneuret, M.6    Conjeaud, H.7
  • 13
    • 12444347833 scopus 로고    scopus 로고
    • Extended neck regions stabilize tetramers of the receptors DC-SIGN and DCSIGNR
    • Feinberg, H., Guo, Y., Mitchell, D. A., Drickamer, K. and Weis, W. I. (2005). Extended neck regions stabilize tetramers of the receptors DC-SIGN and DCSIGNR. J. Biol. Chem. 280, 1327-1335.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1327-1335
    • Feinberg, H.1    Guo, Y.2    Mitchell, D.A.3    Drickamer, K.4    Weis, W.I.5
  • 14
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson, T. and Kurzchalia, T. V. (1998). Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394, 802-805.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 16
    • 84861991991 scopus 로고    scopus 로고
    • Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules
    • Gowrishankar, K., Ghosh, S., Saha, S., C, R., Mayor, S. and Rao, M. (2012). Active remodeling of cortical actin regulates spatiotemporal organization of cell surface molecules. Cell 149, 1353-1367.
    • (2012) Cell , vol.149 , pp. 1353-1367
    • Gowrishankar, K.1    Ghosh, S.2    Saha, S.3    Mayor, C.R.S.4    Rao, M.5
  • 18
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding, A. S. and Hancock, J. F. (2008). Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol. 18, 364-371.
    • (2008) Trends Cell Biol. , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 19
    • 79956188298 scopus 로고    scopus 로고
    • Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization
    • Hashimoto, K., Nishi, H., Bryant, S. and Panchenko, A. R. (2011). Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization. Phys. Biol. 8, 035007.
    • (2011) Phys. Biol. , vol.8 , pp. 035007
    • Hashimoto, K.1    Nishi, H.2    Bryant, S.3    Panchenko, A.R.4
  • 20
    • 3543071011 scopus 로고    scopus 로고
    • Transmembrane adaptor proteins: organizers of immunoreceptor signalling
    • Hořejší, V., Zhang, W. and Schraven, B. (2004). Transmembrane adaptor proteins: organizers of immunoreceptor signalling. Nat. Rev. Immunol. 4, 603-616.
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 603-616
    • Hořejší, V.1    Zhang, W.2    Schraven, B.3
  • 21
    • 79960298029 scopus 로고    scopus 로고
    • DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different
    • Itano, M. S., Neumann, A. K., Liu, P., Zhang, F., Gratton, E., Parak, W. J., Thompson, N. L. and Jacobson, K. (2011). DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different. Biophys. J. 100, 2662-2670.
    • (2011) Biophys. J. , vol.100 , pp. 2662-2670
    • Itano, M.S.1    Neumann, A.K.2    Liu, P.3    Zhang, F.4    Gratton, E.5    Parak, W.J.6    Thompson, N.L.7    Jacobson, K.8
  • 23
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson, K., Mouritsen, O. G. and Anderson, R. G. (2007). Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9, 7-14.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.3
  • 25
    • 80051978813 scopus 로고    scopus 로고
    • Cytoskeletal control of CD36 diffusion promotes its receptor and signaling function
    • Jaqaman, K., Kuwata, H., Touret, N., Collins, R., Trimble, W. S., Danuser, G. and Grinstein, S. (2011). Cytoskeletal control of CD36 diffusion promotes its receptor and signaling function. Cell 146, 593-606.
    • (2011) Cell , vol.146 , pp. 593-606
    • Jaqaman, K.1    Kuwata, H.2    Touret, N.3    Collins, R.4    Trimble, W.S.5    Danuser, G.6    Grinstein, S.7
  • 26
    • 84871703344 scopus 로고    scopus 로고
    • A critical survey of methods to detect plasma membrane rafts
    • Klotzsch, E. and Schütz, G. J. (2013). A critical survey of methods to detect plasma membrane rafts. Philos. Trans. R. Soc. B 368, 20120033.
    • (2013) Philos. Trans. R. Soc. B , vol.368 , pp. 20120033
    • Klotzsch, E.1    Schütz, G.J.2
  • 28
    • 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. (2005). 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, 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
  • 30
    • 0031910469 scopus 로고    scopus 로고
    • Theory for ligand rebinding at cell membrane surfaces
    • Lagerholm, B. C. and Thompson, N. L. (1998). Theory for ligand rebinding at cell membrane surfaces. Biophys. J. 74, 1215-1228.
    • (1998) Biophys. J. , vol.74 , pp. 1215-1228
    • Lagerholm, B.C.1    Thompson, N.L.2
  • 31
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
    • Lajoie, P., Goetz, J. G., Dennis, J. W. and Nabi, I. R. (2009). Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane. J. Cell Biol. 185, 381-385.
    • (2009) J. Cell Biol. , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 33
    • 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. and Davis, M. M. (2010). TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nat. Immunol. 11, 90-96.
    • (2010) Nat. Immunol. , vol.11 , 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
  • 35
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D. and Simons, K. (2010). Lipid rafts as a membrane-organizing principle. Science 327, 46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 36
    • 84862777193 scopus 로고    scopus 로고
    • The formation and stability of DC-SIGN microdomains require its extracellular moiety
    • Liu, P., Wang, X., Itano, M. S., Neumann, A. K., Jacobson, K. and Thompson, N. L. (2012). The formation and stability of DC-SIGN microdomains require its extracellular moiety. Traffic 13, 715-726.
    • (2012) Traffic , vol.13 , pp. 715-726
    • Liu, P.1    Wang, X.2    Itano, M.S.3    Neumann, A.K.4    Jacobson, K.5    Thompson, N.L.6
  • 37
    • 84892511726 scopus 로고    scopus 로고
    • Low copy numbers of DC-SIGN in cell membrane microdomains: implications for structure and function
    • Liu, P., Wang, X., Itano, M. S., Neumann, A. K., de Silva, A. M., Jacobson, K. and Thompson, N. L. (2014). Low copy numbers of DC-SIGN in cell membrane microdomains: implications for structure and function. Traffic 15, 179-196.
    • (2014) Traffic , vol.15 , pp. 179-196
    • Liu, P.1    Wang, X.2    Itano, M.S.3    Neumann, A.K.4    de Silva, A.M.5    Jacobson, K.6    Thompson, N.L.7
  • 38
    • 84886286196 scopus 로고    scopus 로고
    • Molecular mechanisms of cellular mechanosensing
    • Luo, T., Mohan, K., Iglesias, P. A. and Robinson, D. N. (2013). Molecular mechanisms of cellular mechanosensing. Nat. Mater. 12, 1064-1071.
    • (2013) Nat. Mater. , vol.12 , pp. 1064-1071
    • Luo, T.1    Mohan, K.2    Iglesias, P.A.3    Robinson, D.N.4
  • 39
    • 84880659609 scopus 로고    scopus 로고
    • Evolutionary diversification of the multimeric states of proteins
    • Lynch, M. (2013). Evolutionary diversification of the multimeric states of proteins. Proc. Natl. Acad. Sci. USA 110, E2821-E2828.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E2821-E2828
    • Lynch, M.1
  • 42
    • 0036702299 scopus 로고    scopus 로고
    • Plasma membrane microdomains
    • Maxfield, F. R. (2002). Plasma membrane microdomains. Curr. Opin. Cell Biol. 14, 483-487.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 483-487
    • Maxfield, F.R.1
  • 43
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor, S. and Rao, M. (2004). Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5, 231-240.
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 47
    • 84899444997 scopus 로고    scopus 로고
    • The Fluid-Mosaic Model of Membrane Structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years
    • Nicolson, G. L. (2013). The Fluid-Mosaic Model of Membrane Structure: still relevant to understanding the structure, function and dynamics of biological membranes after more than 40 years. Biochim. Biophys. Acta. 1838, 1451-1466.
    • (2013) Biochim. Biophys. Acta. , vol.1838 , pp. 1451-1466
    • Nicolson, G.L.1
  • 48
    • 1442274700 scopus 로고    scopus 로고
    • Lipid rafts and plasma membrane microorganization: insights from Ras
    • Parton, R. G. and Hancock, J. F. (2004). Lipid rafts and plasma membrane microorganization: insights from Ras. Trends Cell Biol. 14, 141-147.
    • (2004) Trends Cell Biol. , vol.14 , pp. 141-147
    • Parton, R.G.1    Hancock, J.F.2
  • 49
    • 33746085241 scopus 로고    scopus 로고
    • Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function
    • Pike, L. J. (2006). Rafts defined: a report on the Keystone Symposium on Lipid Rafts and Cell Function. J. Lipid Res. 47, 1597-1598.
    • (2006) J. Lipid Res. , vol.47 , pp. 1597-1598
    • Pike, L.J.1
  • 50
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, Kras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman, S. J., Muncke, C., Parton, R. G. and Hancock, J. F. (2005). H-ras, Kras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. USA 102, 15500-15505.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 51
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior, I. A., Muncke, C., Parton, R. G. and Hancock, J. F. (2003). Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 160, 165-170.
    • (2003) J. Cell Biol. , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 53
    • 84871424424 scopus 로고    scopus 로고
    • Organization of the resting TCR in nanoscale oligomers
    • Schamel, W. W. and Alarcón, B. (2013). Organization of the resting TCR in nanoscale oligomers. Immunol. Rev. 251, 13-20.
    • (2013) Immunol. Rev. , vol.251 , pp. 13-20
    • Schamel, W.W.1    Alarcón, B.2
  • 57
  • 58
    • 0020790863 scopus 로고
    • Membrane skeletal dynamics: role in modulation of red cell deformability, mobility of transmembrane proteins, and shape
    • Sheetz, M. P. (1983). Membrane skeletal dynamics: role in modulation of red cell deformability, mobility of transmembrane proteins, and shape. Semin. Hematol. 20, 175-188.
    • (1983) Semin. Hematol. , vol.20 , pp. 175-188
    • Sheetz, M.P.1
  • 60
  • 61
    • 0017657279 scopus 로고
    • Thermodynamics, the structure of integral membrane proteins, and transport
    • Singer, S. J. (1977). Thermodynamics, the structure of integral membrane proteins, and transport. J. Supramol. Struct. 6, 313-323.
    • (1977) J. Supramol. Struct. , vol.6 , pp. 313-323
    • Singer, S.J.1
  • 62
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S. J. and Nicolson, G. L. (1972). The fluid mosaic model of the structure of cell membranes. Science 175, 720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 63
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1
    • Suzuki, K. G. N., Fujiwara, T. K., Sanematsu, F., Iino, R., Edidin, M. and Kusumi, A. (2007). GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1. J. Cell Biol. 177, 717-730.
    • (2007) J. Cell Biol. , vol.177 , pp. 717-730
    • Suzuki, K.G.N.1    Fujiwara, T.K.2    Sanematsu, F.3    Iino, R.4    Edidin, M.5    Kusumi, A.6
  • 65
  • 68
    • 0023432865 scopus 로고
    • Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells
    • van Meer, G., Stelzer, E. H., Wijnaendts-van-Resandt, R. W. and Simons, K. (1987). Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells. J. Cell Biol. 105, 1623-1635.
    • (1987) J. Cell Biol. , vol.105 , pp. 1623-1635
    • van Meer, G.1    Stelzer, E.H.2    Wijnaendts-van-Resandt, R.W.3    Simons, K.4
  • 69
  • 70
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R. and Mayor, S. (1998). GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394, 798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 71
    • 65649109738 scopus 로고    scopus 로고
    • Roles of galectins in infection
    • Vasta, G. R. (2009). Roles of galectins in infection. Nat. Rev. Microbiol. 7, 424-438.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 424-438
    • Vasta, G.R.1
  • 72
    • 84862274274 scopus 로고    scopus 로고
    • Quantitative nanoscale analysis of IgE-FceRI clustering and coupling to early signaling proteins
    • Veatch, S. L., Chiang, E. N., Sengupta, P., Holowka, D. A. and Baird, B. A. (2012). Quantitative nanoscale analysis of IgE-FceRI clustering and coupling to early signaling proteins. J. Phys. Chem. B 116, 6923-6935.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 6923-6935
    • Veatch, S.L.1    Chiang, E.N.2    Sengupta, P.3    Holowka, D.A.4    Baird, B.A.5
  • 73
    • 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. and Gaus, K. (2011). Pre-existing clusters of the adaptor Lat do not participate in early T cell signaling events. Nat. Immunol. 12, 655-662.
    • (2011) Nat. Immunol. , vol.12 , 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
  • 74
    • 84899890442 scopus 로고    scopus 로고
    • Recent applications of superresolution microscopy in neurobiology
    • Willig, K. I. and Barrantes, F. J. (2014). Recent applications of superresolution microscopy in neurobiology. Curr. Opin. Chem. Biol. 20, 16-21.
    • (2014) Curr. Opin. Chem. Biol. , vol.20 , pp. 16-21
    • Willig, K.I.1    Barrantes, F.J.2
  • 75
    • 0035817631 scopus 로고    scopus 로고
    • High resolution mapping of mast cell membranes reveals primary and secondary domains of Fc(epsilon)RI and LAT
    • Wilson, B. S., Pfeiffer, J. R., Surviladze, Z., Gaudet, E. A. and Oliver, J. M. (2001). High resolution mapping of mast cell membranes reveals primary and secondary domains of Fc(epsilon)RI and LAT. J. Cell Biol. 154, 645-658.
    • (2001) J. Cell Biol. , vol.154 , pp. 645-658
    • Wilson, B.S.1    Pfeiffer, J.R.2    Surviladze, Z.3    Gaudet, E.A.4    Oliver, J.M.5
  • 76
    • 84872796017 scopus 로고    scopus 로고
    • Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons
    • Xu, K., Zhong, G. and Zhuang, X. (2013). Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons. Science 339, 452-456.
    • (2013) Science , vol.339 , pp. 452-456
    • Xu, K.1    Zhong, G.2    Zhuang, X.3
  • 78
    • 77957125242 scopus 로고    scopus 로고
    • Oligomeric organization of the B-cell antigen receptor on resting cells
    • Yang, J. and Reth, M. (2010). Oligomeric organization of the B-cell antigen receptor on resting cells. Nature 467, 465-469.
    • (2010) Nature , vol.467 , pp. 465-469
    • Yang, J.1    Reth, M.2
  • 80
    • 84864920732 scopus 로고    scopus 로고
    • Spatial-temporal reorganization of activated integrins
    • Yu, C. H., Luo, W. and Sheetz, M. P. (2012). Spatial-temporal reorganization of activated integrins. Cell Adh. Migr. 6, 280-284
    • (2012) Cell Adh. Migr , vol.6 , pp. 280-284
    • Yu, C.H.1    Luo, W.2    Sheetz, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.