메뉴 건너뛰기




Volumn 1853, Issue 4, 2015, Pages 858-871

Plasma membrane reorganization: A glycolipid gateway for microbes

Author keywords

Bacterium; Lipid rafts; Membrane invagination; Receptor clustering; Toxin; Virus

Indexed keywords

ACTIN; CAVEOLIN 1; CHOLERA TOXIN; CHOLESTEROL; GALECTIN 3; GLYCOLIPID; GLYCOPROTEIN; GUANOSINE TRIPHOSPHATASE; INTERNALIN A; INTERNALIN B; LECTIN; MEMBRANE LIPID; MEMBRANE PROTEIN; NEOLECTIN; SHIGA TOXIN; SPHINGOMYELIN; UNCLASSIFIED DRUG; LIGAND;

EID: 84923082197     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.11.014     Document Type: Article
Times cited : (54)

References (171)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer S.J., Nicolson G.L. The fluid mosaic model of the structure of cell membranes. Science 1972, 175:720-731.
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 84878846803 scopus 로고    scopus 로고
    • Pathogen and toxin entry - how pathogens and toxins induce and harness endocytotic mechanisms
    • InTech, B. Ceresa (Ed.)
    • Eierhoff T., Stechmann B., Römer W. Pathogen and toxin entry - how pathogens and toxins induce and harness endocytotic mechanisms. Mol. Regul. Endocytosis 2012, 249-276. InTech. 10.5772/45946. B. Ceresa (Ed.).
    • (2012) Mol. Regul. Endocytosis , pp. 249-276
    • Eierhoff, T.1    Stechmann, B.2    Römer, W.3
  • 3
    • 84898993452 scopus 로고    scopus 로고
    • The basic structure and dynamics of cell membranes: an update of the Singer-Nicolson model
    • Goñi F.M. The basic structure and dynamics of cell membranes: an update of the Singer-Nicolson model. Biochim. Biophys. Acta 2014, 1838:1467-1476. 10.1016/j.bbamem.2014.01.006.
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 1467-1476
    • Goñi, F.M.1
  • 4
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572. 10.1038/42408.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 5
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way: lipid modifications determine protein association with membrane rafts
    • Levental I., Grzybek M., Simons K. Greasing their way: lipid modifications determine protein association with membrane rafts. Biochemistry 2010, 49:6305-6316. 10.1021/bi100882y.
    • (2010) Biochemistry , vol.49 , pp. 6305-6316
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 6
    • 84862800913 scopus 로고    scopus 로고
    • Membrane mechanisms for signal transduction: the coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes
    • Kusumi A., Fujiwara T.K., Morone N., Yoshida K.J., Chadda R., Xie M., et al. Membrane mechanisms for signal transduction: the coupling of the meso-scale raft domains to membrane-skeleton-induced compartments and dynamic protein complexes. Semin. Cell Dev. Biol. 2012, 23:126-144. 10.1016/j.semcdb.2012.01.018.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 126-144
    • Kusumi, A.1    Fujiwara, T.K.2    Morone, N.3    Yoshida, K.J.4    Chadda, R.5    Xie, M.6
  • 7
    • 84892674236 scopus 로고    scopus 로고
    • Fluorescent probes for lipid rafts: from model membranes to living cells
    • Klymchenko A.S., Kreder R. Fluorescent probes for lipid rafts: from model membranes to living cells. Chem. Biol. 2014, 21:97-113. 10.1016/j.chembiol.2013.11.009.
    • (2014) Chem. Biol. , vol.21 , pp. 97-113
    • Klymchenko, A.S.1    Kreder, R.2
  • 8
    • 29144525990 scopus 로고    scopus 로고
    • The role of lipid rafts in the pathogenesis of bacterial infections
    • Zaas D.W., Duncan M., Rae Wright J., Abraham S.N. The role of lipid rafts in the pathogenesis of bacterial infections. Biochim. Biophys. Acta 2005, 1746:305-313. 10.1016/j.bbamcr.2005.10.003.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 305-313
    • Zaas, D.W.1    Duncan, M.2    Rae Wright, J.3    Abraham, S.N.4
  • 9
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2009, 327:46-50. 10.1126/science.1174621.
    • (2009) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 10
    • 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., et al. 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. 2005, 34:351-378. 10.1146/annurev.biophys.34.040204.144637.
    • (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
  • 11
    • 72249098633 scopus 로고    scopus 로고
    • Diffusion, transport, and cell membrane organization investigated by imaging fluorescence cross-correlation spectroscopy
    • Sankaran J., Manna M., Guo L., Kraut R., Wohland T. Diffusion, transport, and cell membrane organization investigated by imaging fluorescence cross-correlation spectroscopy. Biophys. J. 2009, 97:2630-2639. 10.1016/j.bpj.2009.08.025.
    • (2009) Biophys. J. , vol.97 , pp. 2630-2639
    • Sankaran, J.1    Manna, M.2    Guo, L.3    Kraut, R.4    Wohland, T.5
  • 12
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman S.J., Muncke C., Parton R.G., Hancock J.F. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:15500-15505. 10.1073/pnas.0504114102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 13
    • 84866881804 scopus 로고    scopus 로고
    • Mechanical feedback between membrane tension and dynamics
    • Gauthier N.C., Masters T.A., Sheetz M.P. Mechanical feedback between membrane tension and dynamics. Trends Cell Biol. 2012, 22:527-535. 10.1016/j.tcb.2012.07.005.
    • (2012) Trends Cell Biol. , vol.22 , pp. 527-535
    • Gauthier, N.C.1    Masters, T.A.2    Sheetz, M.P.3
  • 14
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: membrane-molding macromolecules
    • Frost A., Unger V.M., De Camilli P. The BAR domain superfamily: membrane-molding macromolecules. Cell 2009, 137:191-196. 10.1016/j.cell.2009.04.010.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 15
    • 84903370911 scopus 로고    scopus 로고
    • The inverse BAR domain protein IBARa drives membrane remodeling to control osmoregulation, phagocytosis and cytokinesis
    • Linkner J., Witte G., Zhao H., Junemann A., Nordholz B., Runge-Wollmann P., et al. The inverse BAR domain protein IBARa drives membrane remodeling to control osmoregulation, phagocytosis and cytokinesis. J. Cell Sci. 2014, 127:1279-1292. 10.1242/jcs.140756.
    • (2014) J. Cell Sci. , vol.127 , pp. 1279-1292
    • Linkner, J.1    Witte, G.2    Zhao, H.3    Junemann, A.4    Nordholz, B.5    Runge-Wollmann, P.6
  • 16
    • 84867274657 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) specifically induces membrane penetration and deformation by Bin/amphiphysin/Rvs (BAR) domains
    • Yoon Y., Zhang X., Cho W. Phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) specifically induces membrane penetration and deformation by Bin/amphiphysin/Rvs (BAR) domains. J. Biol. Chem. 2012, 287:34078-34090. 10.1074/jbc.M112.372789.
    • (2012) J. Biol. Chem. , vol.287 , pp. 34078-34090
    • Yoon, Y.1    Zhang, X.2    Cho, W.3
  • 17
    • 84893621437 scopus 로고    scopus 로고
    • Interplay between curvature and lateral organization of lipids and peptides/proteins in model membranes
    • Wu Q.-Y., Liang Q. Interplay between curvature and lateral organization of lipids and peptides/proteins in model membranes. Langmuir 2014, 30:1116-1122. 10.1021/la4039123.
    • (2014) Langmuir , vol.30 , pp. 1116-1122
    • Wu, Q.-Y.1    Liang, Q.2
  • 18
    • 84885848514 scopus 로고    scopus 로고
    • Membrane bending: the power of protein imbalance
    • Derganc J., Antonny B., Copič A. Membrane bending: the power of protein imbalance. Trends Biochem. Sci. 2013, 38:576-584. 10.1016/j.tibs.2013.08.006.
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 576-584
    • Derganc, J.1    Antonny, B.2    Copič, A.3
  • 19
    • 26944478236 scopus 로고    scopus 로고
    • Polymer-supported membranes as models of the cell surface
    • Tanaka M., Sackmann E. Polymer-supported membranes as models of the cell surface. Nature 2005, 437:656-663. 10.1038/nature04164.
    • (2005) Nature , vol.437 , pp. 656-663
    • Tanaka, M.1    Sackmann, E.2
  • 20
    • 30744456032 scopus 로고    scopus 로고
    • Visualizing association of N-ras in lipid microdomains: influence of domain structure and interfacial adsorption
    • Nicolini C., Baranski J., Schlummer S., Palomo J., Lumbierres-Burgues M., Kahms M., et al. Visualizing association of N-ras in lipid microdomains: influence of domain structure and interfacial adsorption. J. Am. Chem. Soc. 2006, 128:192-201. 10.1021/ja055779x.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 192-201
    • Nicolini, C.1    Baranski, J.2    Schlummer, S.3    Palomo, J.4    Lumbierres-Burgues, M.5    Kahms, M.6
  • 21
    • 84859809913 scopus 로고    scopus 로고
    • Direct evidence of lipid rafts by in situ atomic force microscopy
    • Cai M., Zhao W., Shang X., Jiang J., Ji H., Tang Z., et al. Direct evidence of lipid rafts by in situ atomic force microscopy. Small 2012, 8:1243-1250. 10.1002/smll.201102183.
    • (2012) Small , vol.8 , pp. 1243-1250
    • Cai, M.1    Zhao, W.2    Shang, X.3    Jiang, J.4    Ji, H.5    Tang, Z.6
  • 22
    • 33645967519 scopus 로고    scopus 로고
    • Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization
    • Shaw J.E., Epand R.F., Epand R.M., Li Z., Bittman R., Yip C.M. Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization. Biophys. J. 2006, 90:2170-2178. 10.1529/biophysj.105.073510.
    • (2006) Biophys. J. , vol.90 , pp. 2170-2178
    • Shaw, J.E.1    Epand, R.F.2    Epand, R.M.3    Li, Z.4    Bittman, R.5    Yip, C.M.6
  • 23
    • 34547181885 scopus 로고    scopus 로고
    • Raft domain reorganization driven by short- and long-chain ceramide: a combined AFM and FCS study
    • Chiantia S., Kahya N., Schwille P. Raft domain reorganization driven by short- and long-chain ceramide: a combined AFM and FCS study. Langmuir 2007, 23:7659-7665. 10.1021/la7010919.
    • (2007) Langmuir , vol.23 , pp. 7659-7665
    • Chiantia, S.1    Kahya, N.2    Schwille, P.3
  • 24
    • 84896508256 scopus 로고    scopus 로고
    • Changes in order parameters associated with ceramide-mediated membrane reorganization measured using pTIRFM
    • Ramirez D.M.C., Jakubek Z.J., Lu Z., Ogilvie W.W., Johnston L.J. Changes in order parameters associated with ceramide-mediated membrane reorganization measured using pTIRFM. Langmuir 2013, 29:15907-15918. 10.1021/la403585v.
    • (2013) Langmuir , vol.29 , pp. 15907-15918
    • Ramirez, D.M.C.1    Jakubek, Z.J.2    Lu, Z.3    Ogilvie, W.W.4    Johnston, L.J.5
  • 25
    • 84892761976 scopus 로고    scopus 로고
    • The molecular structure of the liquid-ordered phase of lipid bilayers
    • Sodt A.J., Sandar M.L., Gawrisch K., Pastor R.W., Lyman E. The molecular structure of the liquid-ordered phase of lipid bilayers. J. Am. Chem. Soc. 2014, 136:725-732. 10.1021/ja4105667.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 725-732
    • Sodt, A.J.1    Sandar, M.L.2    Gawrisch, K.3    Pastor, R.W.4    Lyman, E.5
  • 26
    • 79955563072 scopus 로고    scopus 로고
    • Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function
    • Watkins E.B., Miller C.E., Majewski J., Kuhl T.L. Membrane texture induced by specific protein binding and receptor clustering: active roles for lipids in cellular function. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:6975-6980. 10.1073/pnas.1014579108.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 6975-6980
    • Watkins, E.B.1    Miller, C.E.2    Majewski, J.3    Kuhl, T.L.4
  • 27
    • 84903907312 scopus 로고    scopus 로고
    • Influence of Gb3 glycosphingolipids differing in their fatty acid chain on the phase behaviour of solid supported membranes: chemical syntheses and impact of Shiga toxin binding
    • Schütte O.M., Ries A., Orth A., Patalag L.J., Römer W., Steinem C., et al. Influence of Gb3 glycosphingolipids differing in their fatty acid chain on the phase behaviour of solid supported membranes: chemical syntheses and impact of Shiga toxin binding. Chem. Sci. 2014, 10.1039/c4sc01290a.
    • (2014) Chem. Sci.
    • Schütte, O.M.1    Ries, A.2    Orth, A.3    Patalag, L.J.4    Römer, W.5    Steinem, C.6
  • 28
    • 67650924505 scopus 로고    scopus 로고
    • Lipid reorganization induced by Shiga toxin clustering on planar membranes
    • Windschiegl B., Orth A., Römer W., Berland L., Stechmann B., Bassereau P., et al. Lipid reorganization induced by Shiga toxin clustering on planar membranes. PLoS One 2009, 4:e6238. 10.1371/journal.pone.0006238.
    • (2009) PLoS One , vol.4 , pp. e6238
    • Windschiegl, B.1    Orth, A.2    Römer, W.3    Berland, L.4    Stechmann, B.5    Bassereau, P.6
  • 29
    • 84855701895 scopus 로고    scopus 로고
    • Creating and modulating microdomains in pore-spanning membranes
    • Orth A., Johannes L., Römer W., Steinem C. Creating and modulating microdomains in pore-spanning membranes. ChemPhysChem 2012, 13:108-114. 10.1002/cphc.201100644.
    • (2012) ChemPhysChem , vol.13 , pp. 108-114
    • Orth, A.1    Johannes, L.2    Römer, W.3    Steinem, C.4
  • 30
    • 77956409167 scopus 로고    scopus 로고
    • Coupling between clathrin-dependent endocytic budding and F-BAR-dependent tubulation in a cell-free system
    • Wu M., Huang B., Graham M., Raimondi A., Heuser J.E., Zhuang X., et al. Coupling between clathrin-dependent endocytic budding and F-BAR-dependent tubulation in a cell-free system. Nat. Cell Biol. 2010, 12:902-908. 10.1038/ncb2094.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 902-908
    • Wu, M.1    Huang, B.2    Graham, M.3    Raimondi, A.4    Heuser, J.E.5    Zhuang, X.6
  • 31
    • 77951900305 scopus 로고    scopus 로고
    • Globotriaosyl ceramide receptor function - where membrane structure and pathology intersect
    • Lingwood C.A., Binnington B., Manis A., Branch D.R. Globotriaosyl ceramide receptor function - where membrane structure and pathology intersect. FEBS Lett. 2010, 584:1879-1886. 10.1016/j.febslet.2009.11.089.
    • (2010) FEBS Lett. , vol.584 , pp. 1879-1886
    • Lingwood, C.A.1    Binnington, B.2    Manis, A.3    Branch, D.R.4
  • 32
    • 80053634217 scopus 로고    scopus 로고
    • Gangliosides and the multiscale modulation of membrane structure
    • Cantù L., Del Favero E., Sonnino S., Prinetti A. Gangliosides and the multiscale modulation of membrane structure. Chem. Phys. Lipids 2011, 164:796-810. 10.1016/j.chemphyslip.2011.09.005.
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 796-810
    • Cantù, L.1    Del Favero, E.2    Sonnino, S.3    Prinetti, A.4
  • 33
    • 36749032244 scopus 로고    scopus 로고
    • Shiga toxin induces tubular membrane invaginations for its uptake into cells
    • Römer W., Berland L., Chambon V., Gaus K., Windschiegl B., Tenza D., et al. Shiga toxin induces tubular membrane invaginations for its uptake into cells. Nature 2007, 450:670-675. 10.1038/nature05996.
    • (2007) Nature , vol.450 , pp. 670-675
    • Römer, W.1    Berland, L.2    Chambon, V.3    Gaus, K.4    Windschiegl, B.5    Tenza, D.6
  • 34
    • 84862989117 scopus 로고    scopus 로고
    • GM1 structure determines SV40-induced membrane invagination and infection
    • (sup)
    • Ewers H., Römer W., Smith A.E., Bacia K., Dmitrieff S., Chai W., et al. GM1 structure determines SV40-induced membrane invagination and infection. Nat. Cell Biol. 2010, 12:1-12. (sup). 10.1038/ncb1999.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1-12
    • Ewers, H.1    Römer, W.2    Smith, A.E.3    Bacia, K.4    Dmitrieff, S.5    Chai, W.6
  • 37
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins-from cell biology to biomedical applications
    • Johannes L., Römer W. Shiga toxins-from cell biology to biomedical applications. Nat. Rev. Microbiol. 2010, 8:105-116. 10.1038/nrmicro2279.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 105-116
    • Johannes, L.1    Römer, W.2
  • 40
    • 0032539645 scopus 로고    scopus 로고
    • Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3
    • Ling H., Boodhoo A., Hazes B., Cummings M.D., Armstrong G.D., Brunton J.L., et al. Structure of the shiga-like toxin I B-pentamer complexed with an analogue of its receptor Gb3. Biochemistry 1998, 37:1777-1788. 10.1021/bi971806n.
    • (1998) Biochemistry , vol.37 , pp. 1777-1788
    • Ling, H.1    Boodhoo, A.2    Hazes, B.3    Cummings, M.D.4    Armstrong, G.D.5    Brunton, J.L.6
  • 43
    • 78349250515 scopus 로고    scopus 로고
    • Lipid cosorting mediated by shiga toxin induced tubulation
    • Safouane M., Berland L., Callan-Jones A., Sorre B., Römer W., Johannes L., et al. Lipid cosorting mediated by shiga toxin induced tubulation. Traffic 2010, 11:1519-1529. 10.1111/j.1600-0854.2010.01116.x.
    • (2010) Traffic , vol.11 , pp. 1519-1529
    • Safouane, M.1    Berland, L.2    Callan-Jones, A.3    Sorre, B.4    Römer, W.5    Johannes, L.6
  • 44
    • 0033520914 scopus 로고    scopus 로고
    • Activation of Src family kinase yes induced by Shiga toxin binding to globotriaosyl ceramide (Gb3/CD77) in low density, detergent-insoluble microdomains
    • Katagiri Y.U., Mori T., Nakajima H., Katagiri C., Taguchi T., Takeda T., et al. Activation of Src family kinase yes induced by Shiga toxin binding to globotriaosyl ceramide (Gb3/CD77) in low density, detergent-insoluble microdomains. J. Biol. Chem. 1999, 274:35278-35282. 10.1074/jbc.274.49.35278.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35278-35282
    • Katagiri, Y.U.1    Mori, T.2    Nakajima, H.3    Katagiri, C.4    Taguchi, T.5    Takeda, T.6
  • 46
    • 84874086213 scopus 로고    scopus 로고
    • Association of Shiga toxin glycosphingolipid receptors with membrane microdomains of toxin-sensitive lymphoid and myeloid cells
    • Kouzel I.U., Pohlentz G., Storck W., Radamm L., Hoffmann P., Bielaszewska M., et al. Association of Shiga toxin glycosphingolipid receptors with membrane microdomains of toxin-sensitive lymphoid and myeloid cells. J. Lipid Res. 2013, 54:692-710. 10.1194/jlr.M031781.
    • (2013) J. Lipid Res. , vol.54 , pp. 692-710
    • Kouzel, I.U.1    Pohlentz, G.2    Storck, W.3    Radamm, L.4    Hoffmann, P.5    Bielaszewska, M.6
  • 47
    • 84872358862 scopus 로고    scopus 로고
    • Facing glycosphingolipid-Shiga toxin interaction: dire straits for endothelial cells of the human vasculature
    • Bauwens A., Betz J., Meisen I., Kemper B., Karch H., Müthing J. Facing glycosphingolipid-Shiga toxin interaction: dire straits for endothelial cells of the human vasculature. Cell. Mol. Life Sci. 2013, 70:425-457. 10.1007/s00018-012-1060-z.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 425-457
    • Bauwens, A.1    Betz, J.2    Meisen, I.3    Kemper, B.4    Karch, H.5    Müthing, J.6
  • 48
    • 79953313811 scopus 로고    scopus 로고
    • Shiga toxin glycosphingolipid receptors in microvascular and macrovascular endothelial cells: differential association with membrane lipid raft microdomains
    • Betz J., Bielaszewska M., Thies A., Humpf H.-U., Dreisewerd K., Karch H., et al. Shiga toxin glycosphingolipid receptors in microvascular and macrovascular endothelial cells: differential association with membrane lipid raft microdomains. J. Lipid Res. 2011, 52:618-634. 10.1194/jlr.M010819.
    • (2011) J. Lipid Res. , vol.52 , pp. 618-634
    • Betz, J.1    Bielaszewska, M.2    Thies, A.3    Humpf, H.-U.4    Dreisewerd, K.5    Karch, H.6
  • 49
    • 0024564286 scopus 로고
    • Endocytosis from coated pits of Shiga toxin: a glycolipid-binding protein from Shigella dysenteriae 1
    • Sandvig K., Olsnes S., Brown J.E., Petersen O.W., van Deurs B. Endocytosis from coated pits of Shiga toxin: a glycolipid-binding protein from Shigella dysenteriae 1. J. Cell Biol. 1989, 108:1331-1343.
    • (1989) J. Cell Biol. , vol.108 , pp. 1331-1343
    • Sandvig, K.1    Olsnes, S.2    Brown, J.E.3    Petersen, O.W.4    van Deurs, B.5
  • 50
    • 77749249684 scopus 로고    scopus 로고
    • Interplay between toxin transport and flotillin localization
    • Pust S., Dyve A.B., Torgersen M.L., van Deurs B., Sandvig K. Interplay between toxin transport and flotillin localization. PLoS One 2010, 5:e8844. 10.1371/journal.pone.0008844.
    • (2010) PLoS One , vol.5 , pp. e8844
    • Pust, S.1    Dyve, A.B.2    Torgersen, M.L.3    van Deurs, B.4    Sandvig, K.5
  • 53
  • 54
    • 0036800489 scopus 로고    scopus 로고
    • Lipid rafts unite signaling cascades with clathrin to regulate BCR internalization
    • Stoddart A., Dykstra M.L., Brown B.K., Song W., Pierce S.K., Brodsky F.M. Lipid rafts unite signaling cascades with clathrin to regulate BCR internalization. Immunity 2002, 17:451-462.
    • (2002) Immunity , vol.17 , pp. 451-462
    • Stoddart, A.1    Dykstra, M.L.2    Brown, B.K.3    Song, W.4    Pierce, S.K.5    Brodsky, F.M.6
  • 55
    • 40449122567 scopus 로고    scopus 로고
    • Syk associates with clathrin and mediates phosphatidylinositol 3-kinase activation during human rhinovirus internalization
    • Lau C., Wang X., Song L., North M., Wiehler S., Proud D., et al. Syk associates with clathrin and mediates phosphatidylinositol 3-kinase activation during human rhinovirus internalization. J. Immunol. 2008, 180:870-880. 10.4049/jimmunol.180.2.870.
    • (2008) J. Immunol. , vol.180 , pp. 870-880
    • Lau, C.1    Wang, X.2    Song, L.3    North, M.4    Wiehler, S.5    Proud, D.6
  • 57
    • 34347353315 scopus 로고    scopus 로고
    • The retromer complex and clathrin define an early endosomal retrograde exit site
    • Popoff V., Mardones G.A., Tenza D., Rojas R., Lamaze C., Bonifacino J.S., et al. The retromer complex and clathrin define an early endosomal retrograde exit site. J. Cell Sci. 2007, 120:2022-2031. 10.1242/jcs.003020.
    • (2007) J. Cell Sci. , vol.120 , pp. 2022-2031
    • Popoff, V.1    Mardones, G.A.2    Tenza, D.3    Rojas, R.4    Lamaze, C.5    Bonifacino, J.S.6
  • 59
    • 47349085612 scopus 로고    scopus 로고
    • Biophysical approaches to protein-induced membrane deformations in trafficking
    • Sens P., Johannes L., Bassereau P. Biophysical approaches to protein-induced membrane deformations in trafficking. Curr. Opin. Cell Biol. 2008, 20:476-482. 10.1016/j.ceb.2008.04.004.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 476-482
    • Sens, P.1    Johannes, L.2    Bassereau, P.3
  • 60
    • 35548942611 scopus 로고    scopus 로고
    • Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins
    • Viola A., Gupta N. Tether and trap: regulation of membrane-raft dynamics by actin-binding proteins. Nat. Rev. Immunol. 2007, 7:889-896. 10.1038/nri2193.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 889-896
    • Viola, A.1    Gupta, N.2
  • 61
    • 77955646459 scopus 로고    scopus 로고
    • Induced domain formation in endocytic invagination, lipid sorting, and scission
    • Johannes L., Mayor S. Induced domain formation in endocytic invagination, lipid sorting, and scission. Cell 2010, 142:507-510. 10.1016/j.cell.2010.08.007.
    • (2010) Cell , vol.142 , pp. 507-510
    • Johannes, L.1    Mayor, S.2
  • 62
    • 84878984989 scopus 로고    scopus 로고
    • The ERM proteins ezrin and moesin regulate retrograde Shiga toxin transport
    • Kvalvaag A.S., Pust S., Sundet K.I., Engedal N., Simm R., Sandvig K. The ERM proteins ezrin and moesin regulate retrograde Shiga toxin transport. Traffic 2013, 14:839-852. 10.1111/tra.12077.
    • (2013) Traffic , vol.14 , pp. 839-852
    • Kvalvaag, A.S.1    Pust, S.2    Sundet, K.I.3    Engedal, N.4    Simm, R.5    Sandvig, K.6
  • 63
    • 4444265798 scopus 로고    scopus 로고
    • Shiga toxin binding to globotriaosyl ceramide induces intracellular signals that mediate cytoskeleton remodeling in human renal carcinoma-derived cells
    • Takenouchi H., Kiyokawa N., Taguchi T., Matsui J., Katagiri Y.U., Okita H., et al. Shiga toxin binding to globotriaosyl ceramide induces intracellular signals that mediate cytoskeleton remodeling in human renal carcinoma-derived cells. J. Cell Sci. 2004, 117:3911-3922. 10.1242/jcs.01246.
    • (2004) J. Cell Sci. , vol.117 , pp. 3911-3922
    • Takenouchi, H.1    Kiyokawa, N.2    Taguchi, T.3    Matsui, J.4    Katagiri, Y.U.5    Okita, H.6
  • 64
    • 77049128273 scopus 로고    scopus 로고
    • Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis
    • Römer W., Pontani L.L., Sorre B., Rentero C., Berland L., Chambon V., et al. Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis. Cell 2010, 140:540-553. 10.1016/j.cell.2010.01.010.
    • (2010) Cell , vol.140 , pp. 540-553
    • Römer, W.1    Pontani, L.L.2    Sorre, B.3    Rentero, C.4    Berland, L.5    Chambon, V.6
  • 65
    • 0015795679 scopus 로고
    • Gangliosides and membrane receptors for cholera toxin
    • Cuatrecasas P. Gangliosides and membrane receptors for cholera toxin. Biochemistry 1973, 12:3558-3566.
    • (1973) Biochemistry , vol.12 , pp. 3558-3566
    • Cuatrecasas, P.1
  • 66
    • 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, 3:166-175. 10.1002/pro.5560030202.
    • (1994) Protein Sci. , vol.3 , 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
  • 67
    • 0025865722 scopus 로고
    • Neoglycolipid analogues of ganglioside GM1 as functional receptors of cholera toxin
    • Pacuszka T., Bradley R.M., Fishman P.H. Neoglycolipid analogues of ganglioside GM1 as functional receptors of cholera toxin. Biochemistry 1991, 30:2563-2570.
    • (1991) Biochemistry , vol.30 , pp. 2563-2570
    • Pacuszka, T.1    Bradley, R.M.2    Fishman, P.H.3
  • 68
    • 0026648267 scopus 로고
    • Intoxication of cultured cells by cholera toxin: evidence for different pathways when bound to ganglioside GM1 or neoganglioproteins
    • Pacuszka T., Fishman P.H. Intoxication of cultured cells by cholera toxin: evidence for different pathways when bound to ganglioside GM1 or neoganglioproteins. Biochemistry 1992, 31:4773-4778.
    • (1992) Biochemistry , vol.31 , pp. 4773-4778
    • Pacuszka, T.1    Fishman, P.H.2
  • 69
    • 0031802210 scopus 로고    scopus 로고
    • Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia
    • Wolf A.A., Jobling M.G., Wimer-Mackin S., Ferguson-Maltzman M., Madara J.L., Holmes R.K., et al. Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia. J. Cell Biol. 1998, 141:917-927.
    • (1998) J. Cell Biol. , vol.141 , pp. 917-927
    • Wolf, A.A.1    Jobling, M.G.2    Wimer-Mackin, S.3    Ferguson-Maltzman, M.4    Madara, J.L.5    Holmes, R.K.6
  • 70
    • 6044235526 scopus 로고    scopus 로고
    • Trafficking of cholera toxin-ganglioside G M1 complex into Golgi and induction of toxicity depend on actin cytoskeleton
    • (G. M.)
    • Badizadegan K., Wheeler H.E., Fujinaga Y., Lencer W.I. Trafficking of cholera toxin-ganglioside G M1 complex into Golgi and induction of toxicity depend on actin cytoskeleton. Am. J. Physiol. Cell Physiol. 2004, 287:1453-1462. (G. M.). 10.1152/ajpcell.00189.2004.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287 , pp. 1453-1462
    • Badizadegan, K.1    Wheeler, H.E.2    Fujinaga, Y.3    Lencer, W.I.4
  • 71
    • 84866034926 scopus 로고    scopus 로고
    • Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1
    • Chinnapen D.J.-F., Hsieh W.-T., te Welscher Y.M., Saslowsky D.E., Kaoutzani L., Brandsma E., et al. Lipid sorting by ceramide structure from plasma membrane to ER for the cholera toxin receptor ganglioside GM1. Dev. Cell 2012, 23:573-586. 10.1016/j.devcel.2012.08.002.
    • (2012) Dev. Cell , vol.23 , pp. 573-586
    • Chinnapen, D.J.-F.1    Hsieh, W.-T.2    te Welscher, Y.M.3    Saslowsky, D.E.4    Kaoutzani, L.5    Brandsma, E.6
  • 73
    • 29144434531 scopus 로고    scopus 로고
    • Raft trafficking of AB5 subunit bacterial toxins
    • Lencer W.I., Saslowsky D. Raft trafficking of AB5 subunit bacterial toxins. Biochim. Biophys. Acta 2005, 1746:314-321. 10.1016/j.bbamcr.2005.07.007.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 314-321
    • Lencer, W.I.1    Saslowsky, D.2
  • 75
    • 42149118541 scopus 로고    scopus 로고
    • Attenuated endocytosis and toxicity of a mutant cholera toxin with decreased ability to cluster ganglioside GM1 molecules
    • Wolf A.A., Jobling M.G., Saslowsky D.E., Kern E., Drake K.R., Kenworthy A.K., et al. Attenuated endocytosis and toxicity of a mutant cholera toxin with decreased ability to cluster ganglioside GM1 molecules. Infect. Immun. 2008, 76:1476-1484. 10.1128/IAI. 01286-07.
    • (2008) Infect. Immun. , vol.76 , pp. 1476-1484
    • Wolf, A.A.1    Jobling, M.G.2    Saslowsky, D.E.3    Kern, E.4    Drake, K.R.5    Kenworthy, A.K.6
  • 76
    • 0035902550 scopus 로고    scopus 로고
    • A mutant cholera toxin B subunit that binds GM1-ganglioside but lacks immunomodulatory or toxic activity
    • Aman A.T., Fraser S., Merritt E.a, Rodigherio C., Kenny M., Ahn M., et al. A mutant cholera toxin B subunit that binds GM1-ganglioside but lacks immunomodulatory or toxic activity. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:8536-8541. 10.1073/pnas.161273098.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8536-8541
    • Aman, A.T.1    Fraser, S.2    Merritt, E.A.3    Rodigherio, C.4    Kenny, M.5    Ahn, M.6
  • 77
    • 84872143843 scopus 로고    scopus 로고
    • A single native ganglioside GM1-binding site is sufficient for cholera toxin to bind to cells and complete the intoxication pathway
    • Jobling M.G., Yang Z., Kam W.R., Lencer W.I., Holmes R.K. A single native ganglioside GM1-binding site is sufficient for cholera toxin to bind to cells and complete the intoxication pathway. MBio 2012, 3. 10.1128/mBio.00401-12.
    • (2012) MBio , vol.3
    • Jobling, M.G.1    Yang, Z.2    Kam, W.R.3    Lencer, W.I.4    Holmes, R.K.5
  • 78
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton R.G. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 1994, 42:155-166. 10.1177/42.2.8288861.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 79
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer J.E., McIntosh D.P., Dvorak A.M., Liu J., Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 1995, 269:1435-1439.
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 80
    • 22544450480 scopus 로고    scopus 로고
    • Endocytosis of cholera toxin by human enterocytes is developmentally regulated
    • Lu L., Khan S., Lencer W., Walker W.A. Endocytosis of cholera toxin by human enterocytes is developmentally regulated. Am. J. Physiol. Gastrointest. Liver Physiol. 2005, 289:G332-G341. 10.1152/ajpgi.00521.2004.
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.289 , pp. G332-G341
    • Lu, L.1    Khan, S.2    Lencer, W.3    Walker, W.A.4
  • 81
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi P.A., Fishman P.H. Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol. 1998, 141:905-915.
    • (1998) J. Cell Biol. , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 82
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen M.L., Skretting G., van Deurs B., Sandvig K. Internalization of cholera toxin by different endocytic mechanisms. J. Cell Sci. 2001, 114:3737-3747.
    • (2001) J. Cell Sci. , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    van Deurs, B.3    Sandvig, K.4
  • 83
    • 3343011405 scopus 로고    scopus 로고
    • Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways
    • Massol R.H., Larsen J.E., Fujinaga Y., Lencer W.I., Kirchhausen T. Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways. MBoC 2004, 15:3631-3641. 10.1091/mbc.E04.
    • (2004) MBoC , vol.15 , pp. 3631-3641
    • Massol, R.H.1    Larsen, J.E.2    Fujinaga, Y.3    Lencer, W.I.4    Kirchhausen, T.5
  • 84
    • 78649855802 scopus 로고    scopus 로고
    • Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2
    • Saslowsky D.E., Cho J.A., Chinnapen H., Massol R.H., Chinnapen D.J., Wagner J.S., et al. Intoxication of zebrafish and mammalian cells by cholera toxin depends on the flotillin/reggie proteins but not Derlin-1 or -2. J. Clin. Invest. 2010, 120:4399-4409. 10.1172/JCI42958DS1.
    • (2010) J. Clin. Invest. , vol.120 , pp. 4399-4409
    • Saslowsky, D.E.1    Cho, J.A.2    Chinnapen, H.3    Massol, R.H.4    Chinnapen, D.J.5    Wagner, J.S.6
  • 85
    • 34250851923 scopus 로고    scopus 로고
    • Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding
    • Frick M., Bright N.A., Riento K., Bray A., Merrified C., Nichols B.J. Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding. Curr. Biol. 2007, 17:1151-1156. 10.1016/j.cub.2007.05.078.
    • (2007) Curr. Biol. , vol.17 , pp. 1151-1156
    • Frick, M.1    Bright, N.A.2    Riento, K.3    Bray, A.4    Merrified, C.5    Nichols, B.J.6
  • 86
    • 34548664143 scopus 로고    scopus 로고
    • Linking membrane microdomains to the cytoskeleton: regulation of the lateral mobility of reggie-1/flotillin-2 by interaction with actin
    • Langhorst M.F., Solis G.P., Hannbeck S., Plattner H., Stuermer C.A.O. Linking membrane microdomains to the cytoskeleton: regulation of the lateral mobility of reggie-1/flotillin-2 by interaction with actin. FEBS Lett. 2007, 581:4697-4703. 10.1016/j.febslet.2007.08.074.
    • (2007) FEBS Lett. , vol.581 , pp. 4697-4703
    • Langhorst, M.F.1    Solis, G.P.2    Hannbeck, S.3    Plattner, H.4    Stuermer, C.A.O.5
  • 87
    • 13444310587 scopus 로고    scopus 로고
    • Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles
    • Kirkham M., Fujita A., Chadda R., Nixon S.J., Kurzchalia T.V., Sharma D.K., et al. Ultrastructural identification of uncoated caveolin-independent early endocytic vehicles. J. Cell Biol. 2005, 168:465-476. 10.1083/jcb.200407078.
    • (2005) J. Cell Biol. , vol.168 , pp. 465-476
    • Kirkham, M.1    Fujita, A.2    Chadda, R.3    Nixon, S.J.4    Kurzchalia, T.V.5    Sharma, D.K.6
  • 88
    • 0345490781 scopus 로고    scopus 로고
    • The intracellular voyage of cholera toxin: going retro
    • Lencer W.I., Tsai B. The intracellular voyage of cholera toxin: going retro. Trends Biochem. Sci. 2003, 28:639-645. 10.1016/j.tibs.2003.10.002.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 639-645
    • Lencer, W.I.1    Tsai, B.2
  • 89
    • 77956288440 scopus 로고    scopus 로고
    • Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum
    • Wernick N.L.B., Chinnapen D.J.-F., Cho J.A., Lencer W.I. Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum. Toxins (Basel) 2010, 2:310-325. 10.3390/toxins2030310.
    • (2010) Toxins (Basel) , vol.2 , pp. 310-325
    • Wernick, N.L.B.1    Chinnapen, D.J.-F.2    Cho, J.A.3    Lencer, W.I.4
  • 90
    • 66249127141 scopus 로고    scopus 로고
    • Sorting of lipids and proteins in membrane curvature gradients
    • Tian A., Baumgart T. Sorting of lipids and proteins in membrane curvature gradients. Biophys. J. 2009, 96:2676-2688. 10.1016/j.bpj.2008.11.067.
    • (2009) Biophys. J. , vol.96 , pp. 2676-2688
    • Tian, A.1    Baumgart, T.2
  • 91
    • 77952132277 scopus 로고    scopus 로고
    • Dynamic sorting of lipids and proteins in membrane tubes with a moving phase boundary
    • Heinrich M., Tian A., Esposito C., Baumgart T. Dynamic sorting of lipids and proteins in membrane tubes with a moving phase boundary. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:7208-7213. 10.1073/pnas.0913997107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 7208-7213
    • Heinrich, M.1    Tian, A.2    Esposito, C.3    Baumgart, T.4
  • 92
    • 34248582600 scopus 로고    scopus 로고
    • GM1 clustering inhibits cholera toxin binding in supported phospholipid membranes
    • Shi J., Yang T., Kataoka S., Zhang Y., Diaz A.J., Cremer P.S. GM1 clustering inhibits cholera toxin binding in supported phospholipid membranes. J. Am. Chem. Soc. 2007, 129:5954-5961. 10.1021/ja069375w.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5954-5961
    • Shi, J.1    Yang, T.2    Kataoka, S.3    Zhang, Y.4    Diaz, A.J.5    Cremer, P.S.6
  • 94
    • 84884659060 scopus 로고    scopus 로고
    • Reduction of lectin valency drastically changes glycolipid dynamics in membranes but not surface avidity
    • Arnaud J., Claudinon J., Tröndle K., Trovaslet M., Larson G., Thomas A., et al. Reduction of lectin valency drastically changes glycolipid dynamics in membranes but not surface avidity. ACS Chem. Biol. 2013, 8:1918-1924. 10.1021/cb400254b.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1918-1924
    • Arnaud, J.1    Claudinon, J.2    Tröndle, K.3    Trovaslet, M.4    Larson, G.5    Thomas, A.6
  • 95
    • 84877834849 scopus 로고    scopus 로고
    • Binding sugars: from natural lectins to synthetic receptors and engineered neolectins
    • Arnaud J., Audfray A., Imberty A. Binding sugars: from natural lectins to synthetic receptors and engineered neolectins. Chem. Soc. Rev. 2013, 42:4798-4813. 10.1039/c2cs35435g.
    • (2013) Chem. Soc. Rev. , vol.42 , pp. 4798-4813
    • Arnaud, J.1    Audfray, A.2    Imberty, A.3
  • 97
    • 80155164903 scopus 로고    scopus 로고
    • Interaction of single viruslike particles with vesicles containing glycosphingolipids
    • Bally M., Gunnarsson A., Svensson L., Larson G., Zhdanov V.P., Höök F. Interaction of single viruslike particles with vesicles containing glycosphingolipids. Phys. Rev. Lett. 2011, 107:188103. 10.1103/PhysRevLett.107.188103.
    • (2011) Phys. Rev. Lett. , vol.107 , pp. 188103
    • Bally, M.1    Gunnarsson, A.2    Svensson, L.3    Larson, G.4    Zhdanov, V.P.5    Höök, F.6
  • 98
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors
    • Mammen M., Choi S.-K., Whitesides G.M. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. ChemInform 1998, 37:2754-2794. 10.1002/chin.199909293.
    • (1998) ChemInform , vol.37 , pp. 2754-2794
    • Mammen, M.1    Choi, S.-K.2    Whitesides, G.M.3
  • 100
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L., Püntener D., Helenius A. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 2002, 296:535-539. 10.1126/science.1069784.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Püntener, D.2    Helenius, A.3
  • 101
    • 73349130473 scopus 로고    scopus 로고
    • High-speed nanoscopic tracking of the position and orientation of a single virus
    • Kukura P., Ewers H., Müller C., Renn A., Helenius A., Sandoghdar V. High-speed nanoscopic tracking of the position and orientation of a single virus. Nat. Methods 2009, 6:923-927. 10.1038/nmeth.1395.
    • (2009) Nat. Methods , vol.6 , pp. 923-927
    • Kukura, P.1    Ewers, H.2    Müller, C.3    Renn, A.4    Helenius, A.5    Sandoghdar, V.6
  • 103
    • 84873578370 scopus 로고    scopus 로고
    • Integrin-mediated signaling induced by simian virus 40 leads to transient uncoupling of cortical actin and the plasma membrane
    • Stergiou L., Bauer M., Mair W., Bausch-Fluck D., Drayman N., Wollscheid B., et al. Integrin-mediated signaling induced by simian virus 40 leads to transient uncoupling of cortical actin and the plasma membrane. PLoS One 2013, 8:e55799. 10.1371/journal.pone.0055799.
    • (2013) PLoS One , vol.8 , pp. e55799
    • Stergiou, L.1    Bauer, M.2    Mair, W.3    Bausch-Fluck, D.4    Drayman, N.5    Wollscheid, B.6
  • 104
    • 21844440569 scopus 로고    scopus 로고
    • Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis
    • Pelkmans L., Fava E., Grabner H., Hannus M., Habermann B., Krausz E., et al. Genome-wide analysis of human kinases in clathrin- and caveolae/raft-mediated endocytosis. Nature 2005, 436:78-86. 10.1038/nature03571.
    • (2005) Nature , vol.436 , pp. 78-86
    • Pelkmans, L.1    Fava, E.2    Grabner, H.3    Hannus, M.4    Habermann, B.5    Krausz, E.6
  • 106
    • 77958144531 scopus 로고    scopus 로고
    • Norovirus gastroenteritis, carbohydrate receptors, and animal models
    • Tan M., Jiang X. Norovirus gastroenteritis, carbohydrate receptors, and animal models. PLoS Pathog. 2010, 6:e1000983. 10.1371/journal.ppat.1000983.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000983
    • Tan, M.1    Jiang, X.2
  • 107
    • 84877057550 scopus 로고    scopus 로고
    • Human GII.4 norovirus VLP induces membrane invaginations on giant unilamellar vesicles containing secretor gene dependent α1,2-fucosylated glycosphingolipids
    • Rydell G.E., Svensson L., Larson G., Johannes L., Römer W. Human GII.4 norovirus VLP induces membrane invaginations on giant unilamellar vesicles containing secretor gene dependent α1,2-fucosylated glycosphingolipids. Biochim. Biophys. Acta 2013, 1828:1840-1845. 10.1016/j.bbamem.2013.03.016.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1840-1845
    • Rydell, G.E.1    Svensson, L.2    Larson, G.3    Johannes, L.4    Römer, W.5
  • 108
    • 32944462721 scopus 로고    scopus 로고
    • Bacterial adhesion and entry into host cells
    • Pizarro-Cerdá J., Cossart P. Bacterial adhesion and entry into host cells. Cell 2006, 124:715-727. 10.1016/j.cell.2006.02.012.
    • (2006) Cell , vol.124 , pp. 715-727
    • Pizarro-Cerdá, J.1    Cossart, P.2
  • 109
    • 9144254025 scopus 로고    scopus 로고
    • Rafts can trigger contact-mediated secretion of bacterial effectors via a lipid-based mechanism
    • van der Goot F.G., Tran van Nhieu G., Allaoui A., Sansonetti P., Lafont F. Rafts can trigger contact-mediated secretion of bacterial effectors via a lipid-based mechanism. J. Biol. Chem. 2004, 279:47792-47798. 10.1074/jbc.M406824200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47792-47798
    • van der Goot, F.G.1    Tran van Nhieu, G.2    Allaoui, A.3    Sansonetti, P.4    Lafont, F.5
  • 110
    • 34247119640 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa exploits a PIP3-dependent pathway to transform apical into basolateral membrane
    • Kierbel A., Gassama-Diagne A., Rocha C., Radoshevich L., Olson J., Mostov K., et al. Pseudomonas aeruginosa exploits a PIP3-dependent pathway to transform apical into basolateral membrane. J. Cell Biol. 2007, 177:21-27. 10.1083/jcb.200605142.
    • (2007) J. Cell Biol. , vol.177 , pp. 21-27
    • Kierbel, A.1    Gassama-Diagne, A.2    Rocha, C.3    Radoshevich, L.4    Olson, J.5    Mostov, K.6
  • 111
    • 15744393649 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase is required for intracellular Listeria monocytogenes actin-based motility and filopod formation
    • Sidhu G., Li W., Laryngakis N., Bishai E., Balla T., Southwick F. Phosphoinositide 3-kinase is required for intracellular Listeria monocytogenes actin-based motility and filopod formation. J. Biol. Chem. 2005, 280:11379-11386. 10.1074/jbc.M414533200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11379-11386
    • Sidhu, G.1    Li, W.2    Laryngakis, N.3    Bishai, E.4    Balla, T.5    Southwick, F.6
  • 112
    • 22144435517 scopus 로고    scopus 로고
    • Phosphoinositide3-kinase regulates actin polymerization during delayed phagocytosis of Helicobacter pylori
    • Allen L.H., Allgood J.A., Han X., Wittine L.M. Phosphoinositide3-kinase regulates actin polymerization during delayed phagocytosis of Helicobacter pylori. J. Leukoc. Biol. 2005, 78:220-230.
    • (2005) J. Leukoc. Biol. , vol.78 , pp. 220-230
    • Allen, L.H.1    Allgood, J.A.2    Han, X.3    Wittine, L.M.4
  • 113
    • 0030691027 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator is an epithelial cell receptor for clearance of Pseudomonas aeruginosa from the lung
    • Pier G.B., Grout M., Zaidi T.S. Cystic fibrosis transmembrane conductance regulator is an epithelial cell receptor for clearance of Pseudomonas aeruginosa from the lung. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:12088-12093.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 12088-12093
    • Pier, G.B.1    Grout, M.2    Zaidi, T.S.3
  • 114
    • 85056061766 scopus 로고    scopus 로고
    • Glycolipid-dependent, protease sensitive internalization of Pseudomonas aeruginosa into cultured human respiratory epithelial cells
    • Emam A., Carter W.G., Lingwood C. Glycolipid-dependent, protease sensitive internalization of Pseudomonas aeruginosa into cultured human respiratory epithelial cells. Open Microbiol. J. 2010, 4:106-115. 10.2174/1874285801004010106.
    • (2010) Open Microbiol. J. , vol.4 , pp. 106-115
    • Emam, A.1    Carter, W.G.2    Lingwood, C.3
  • 115
    • 0032588051 scopus 로고    scopus 로고
    • Fibronectin and alpha5beta1 integrin mediate binding of Pseudomonas aeruginosa to repairing airway epithelium
    • Roger P., Puchelle E., Bajolet-Laudinat O., Tournier J.M., Debordeaux C., Plotkowski M.C., et al. Fibronectin and alpha5beta1 integrin mediate binding of Pseudomonas aeruginosa to repairing airway epithelium. Eur. Respir. J. 1999, 13:1301-1309.
    • (1999) Eur. Respir. J. , vol.13 , pp. 1301-1309
    • Roger, P.1    Puchelle, E.2    Bajolet-Laudinat, O.3    Tournier, J.M.4    Debordeaux, C.5    Plotkowski, M.C.6
  • 116
    • 0029920335 scopus 로고    scopus 로고
    • Asialo GM1 is a receptor for Pseudomonas aeruginosa adherence to regenerating respiratory epithelial cells
    • De Bentzmann S., Roger P., Dupuit F., Bajolet-Laudinet O., Fuchey C., Plotkowski M.C., et al. Asialo GM1 is a receptor for Pseudomonas aeruginosa adherence to regenerating respiratory epithelial cells. Infect. Immun. 1996, 64:1582-1588.
    • (1996) Infect. Immun. , vol.64 , pp. 1582-1588
    • De Bentzmann, S.1    Roger, P.2    Dupuit, F.3    Bajolet-Laudinet, O.4    Fuchey, C.5    Plotkowski, M.C.6
  • 117
    • 77949522346 scopus 로고    scopus 로고
    • Gangliosides and beta1-integrin are required for caveolae and membrane domains
    • Singh R.D., Marks D.L., Holicky E.L., Wheatley C.L., Kaptzan T., Sato S.B., et al. Gangliosides and beta1-integrin are required for caveolae and membrane domains. Traffic 2010, 11:348-360. 10.1111/j.1600-0854.2009.01022.x.
    • (2010) Traffic , vol.11 , pp. 348-360
    • Singh, R.D.1    Marks, D.L.2    Holicky, E.L.3    Wheatley, C.L.4    Kaptzan, T.5    Sato, S.B.6
  • 118
    • 84900563188 scopus 로고    scopus 로고
    • Reduced GM1 ganglioside in CFTR-deficient human airway cells results in decreased 1-integrin signaling and delayed wound repair
    • Itokazu Y., Pagano R.E., Schroeder A.S., O'Grady S.M., Limper A.H., Marks D.L. Reduced GM1 ganglioside in CFTR-deficient human airway cells results in decreased 1-integrin signaling and delayed wound repair. Am. J. Physiol. Cell Physiol. 2014, 306:C819-C830. 10.1152/ajpcell.00168.2013.
    • (2014) Am. J. Physiol. Cell Physiol. , vol.306 , pp. C819-C830
    • Itokazu, Y.1    Pagano, R.E.2    Schroeder, A.S.3    O'Grady, S.M.4    Limper, A.H.5    Marks, D.L.6
  • 119
    • 84861213684 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa pili and flagella mediate distinct binding and signaling events at the apical and basolateral surface of airway epithelium
    • Bucior I., Pielage J.F., Engel J.N. Pseudomonas aeruginosa pili and flagella mediate distinct binding and signaling events at the apical and basolateral surface of airway epithelium. PLoS Pathog. 2012, 8:e1002616. 10.1371/journal.ppat.1002616.
    • (2012) PLoS Pathog. , vol.8 , pp. e1002616
    • Bucior, I.1    Pielage, J.F.2    Engel, J.N.3
  • 120
    • 0041322625 scopus 로고    scopus 로고
    • Characterization of Pseudomonas aeruginosa exoenzyme S as a bifunctional enzyme in J774A. 1 macrophages
    • Rocha C.L., Coburn J., Rucks E.A., Olson J.C. Characterization of Pseudomonas aeruginosa exoenzyme S as a bifunctional enzyme in J774A. 1 macrophages. Infect. Immun. 2003, 71:5296-5305. 10.1128/IAI.71.9.5296.
    • (2003) Infect. Immun. , vol.71 , pp. 5296-5305
    • Rocha, C.L.1    Coburn, J.2    Rucks, E.A.3    Olson, J.C.4
  • 121
    • 0032036504 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa invasion and cytotoxicity are independent events, both of which involve protein tyrosine kinase activity
    • Evans D.J., Frank D.W., Finck-Barbançon V., Wu C., Fleiszig S.M. Pseudomonas aeruginosa invasion and cytotoxicity are independent events, both of which involve protein tyrosine kinase activity. Infect. Immun. 1998, 66:1453-1459.
    • (1998) Infect. Immun. , vol.66 , pp. 1453-1459
    • Evans, D.J.1    Frank, D.W.2    Finck-Barbançon, V.3    Wu, C.4    Fleiszig, S.M.5
  • 122
    • 0035162799 scopus 로고    scopus 로고
    • Invasion of human epithelial cells by Pseudomonas aeruginosa involves Src-like tyrosine kinases p60Src and p59Fyn
    • Kinases T., Esen M., Grassmé H., Riethmüller J., Fassbender K., Gulbins E., et al. Invasion of human epithelial cells by Pseudomonas aeruginosa involves Src-like tyrosine kinases p60Src and p59Fyn. Infect. Immun. 2001, 69:281-287. 10.1128/IAI.69.1.281.
    • (2001) Infect. Immun. , vol.69 , pp. 281-287
    • Kinases, T.1    Esen, M.2    Grassmé, H.3    Riethmüller, J.4    Fassbender, K.5    Gulbins, E.6
  • 123
    • 33746256896 scopus 로고    scopus 로고
    • Src kinase Lyn is crucial for Pseudomonas aeruginosa internalization into lung cells
    • Kannan S., Audet A., Knittel J., Mullegama S., Gao G.F., Wu M. Src kinase Lyn is crucial for Pseudomonas aeruginosa internalization into lung cells. Eur. J. Immunol. 2006, 36:1739-1752. 10.1002/eji.200635973.
    • (2006) Eur. J. Immunol. , vol.36 , pp. 1739-1752
    • Kannan, S.1    Audet, A.2    Knittel, J.3    Mullegama, S.4    Gao, G.F.5    Wu, M.6
  • 124
    • 42149147975 scopus 로고    scopus 로고
    • Cholesterol-rich membrane rafts and Lyn are involved in phagocytosis during Pseudomonas aeruginosa infection
    • Kannan S., Audet A., Huang H., Chen L.J., Wu M. Cholesterol-rich membrane rafts and Lyn are involved in phagocytosis during Pseudomonas aeruginosa infection. J. Immunol. 2008, 180:2396-2408. 10.4049/jimmunol.180.4.2396.
    • (2008) J. Immunol. , vol.180 , pp. 2396-2408
    • Kannan, S.1    Audet, A.2    Huang, H.3    Chen, L.J.4    Wu, M.5
  • 125
    • 18244410381 scopus 로고    scopus 로고
    • The phosphoinositol-3-kinase-protein kinase B/Akt pathway is critical for Pseudomonas aeruginosa strain PAK internalization
    • Kierbel A., Gassama-Diagne A., Mostov K., Engel J.N. The phosphoinositol-3-kinase-protein kinase B/Akt pathway is critical for Pseudomonas aeruginosa strain PAK internalization. Mol. Biol. Cell 2005, 16:2577-2585. 10.1091/mbc.E04.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2577-2585
    • Kierbel, A.1    Gassama-Diagne, A.2    Mostov, K.3    Engel, J.N.4
  • 126
    • 79960435080 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa interacts with epithelial cells rapidly forming aggregates that are internalized by a Lyn-dependent mechanism
    • Lepanto P., Bryant D.M., Rossello J., Datta A., Mostov K.E., Kierbel A. Pseudomonas aeruginosa interacts with epithelial cells rapidly forming aggregates that are internalized by a Lyn-dependent mechanism. Cell. Microbiol. 2011, 13:1212-1222. 10.1111/j.1462-5822.2011.01611.x.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1212-1222
    • Lepanto, P.1    Bryant, D.M.2    Rossello, J.3    Datta, A.4    Mostov, K.E.5    Kierbel, A.6
  • 127
    • 42949162611 scopus 로고    scopus 로고
    • RNAi screen reveals an Abl kinase-dependent host cell pathway involved in Pseudomonas aeruginosa internalization
    • Pielage J.F., Powell K.R., Kalman D., Engel J.N. RNAi screen reveals an Abl kinase-dependent host cell pathway involved in Pseudomonas aeruginosa internalization. PLoS Pathog. 2008, 4:e1000031. 10.1371/journal.ppat.1000031.
    • (2008) PLoS Pathog. , vol.4 , pp. e1000031
    • Pielage, J.F.1    Powell, K.R.2    Kalman, D.3    Engel, J.N.4
  • 128
    • 0142095498 scopus 로고    scopus 로고
    • Host defense against Pseudomonas aeruginosa requires ceramide-rich membrane rafts
    • Grassmé H., Jendrossek V., Riehle A., Kürthy G.V., Berger J.B., Schwarz H. Host defense against Pseudomonas aeruginosa requires ceramide-rich membrane rafts. Nat. Med. 2003, 9:322-330. 10.1038/nm.
    • (2003) Nat. Med. , vol.9 , pp. 322-330
    • Grassmé, H.1    Jendrossek, V.2    Riehle, A.3    Kürthy, G.V.4    Berger, J.B.5    Schwarz, H.6
  • 129
    • 65449143628 scopus 로고    scopus 로고
    • Role of LecA and LecB lectins in Pseudomonas aeruginosa-induced lung injury and effect of carbohydrate ligands
    • Chemani C., Imberty A., de Bentzmann S., Pierre M., Wimmerová M., Guery B.P., et al. Role of LecA and LecB lectins in Pseudomonas aeruginosa-induced lung injury and effect of carbohydrate ligands. Infect. Immun. 2009, 77:2065-2075. 10.1128/IAI. 01204-08.
    • (2009) Infect. Immun. , vol.77 , pp. 2065-2075
    • Chemani, C.1    Imberty, A.2    de Bentzmann, S.3    Pierre, M.4    Wimmerová, M.5    Guery, B.P.6
  • 131
    • 83755177932 scopus 로고    scopus 로고
    • Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes
    • Cossart P. Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:19484-19491. 10.1073/pnas.1112371108.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 19484-19491
    • Cossart, P.1
  • 132
    • 64049117000 scopus 로고    scopus 로고
    • Listeria monocytogenes internalin and E-cadherin: from structure to pathogenesis
    • Bonazzi M., Lecuit M., Cossart P. Listeria monocytogenes internalin and E-cadherin: from structure to pathogenesis. Cell. Microbiol. 2009, 11:693-702. 10.1111/j.1462-5822.2009.01293.x.
    • (2009) Cell. Microbiol. , vol.11 , pp. 693-702
    • Bonazzi, M.1    Lecuit, M.2    Cossart, P.3
  • 133
    • 0037009369 scopus 로고    scopus 로고
    • Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interaction
    • Lafont F., Tran Van Nhieu G., Hanada K., Sansonetti P., van der Goot F.G. Initial steps of Shigella infection depend on the cholesterol/sphingolipid raft-mediated CD44-IpaB interaction. EMBO J. 2002, 21:4449-4457.
    • (2002) EMBO J. , vol.21 , pp. 4449-4457
    • Lafont, F.1    Tran Van Nhieu, G.2    Hanada, K.3    Sansonetti, P.4    van der Goot, F.G.5
  • 134
    • 0032506002 scopus 로고    scopus 로고
    • Involvement of focal adhesion kinase in invasin-mediated uptake
    • Alrutz M.A., Isberg R.R. Involvement of focal adhesion kinase in invasin-mediated uptake. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:13658-13663.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 13658-13663
    • Alrutz, M.A.1    Isberg, R.R.2
  • 135
    • 0033105366 scopus 로고    scopus 로고
    • A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association
    • Dersch P., Isberg R.R. A region of the Yersinia pseudotuberculosis invasin protein enhances integrin-mediated uptake into mammalian cells and promotes self-association. EMBO J. 1999, 18:1199-1213. 10.1093/emboj/18.5.1199.
    • (1999) EMBO J. , vol.18 , pp. 1199-1213
    • Dersch, P.1    Isberg, R.R.2
  • 136
    • 33750565408 scopus 로고    scopus 로고
    • Functionally different pools of Shiga toxin receptor, globotriaosyl ceramide, in HeLa cells
    • Falguières T., Römer W., Amessou M., Afonso C., Wolf C., Tabet J.-C., et al. Functionally different pools of Shiga toxin receptor, globotriaosyl ceramide, in HeLa cells. FEBS J. 2006, 273:5205-5218. 10.1111/j.1742-4658.2006.05516.x.
    • (2006) FEBS J. , vol.273 , pp. 5205-5218
    • Falguières, T.1    Römer, W.2    Amessou, M.3    Afonso, C.4    Wolf, C.5    Tabet, J.-C.6
  • 137
    • 84886030991 scopus 로고    scopus 로고
    • Identification of TLR4 as the receptor that recognizes Shiga toxins in human neutrophils
    • Brigotti M., Carnicelli D., Arfilli V., Tamassia N., Borsetti F., Fabbri E., et al. Identification of TLR4 as the receptor that recognizes Shiga toxins in human neutrophils. J. Immunol. 2013, 191:4748-4758. 10.4049/jimmunol.1300122.
    • (2013) J. Immunol. , vol.191 , pp. 4748-4758
    • Brigotti, M.1    Carnicelli, D.2    Arfilli, V.3    Tamassia, N.4    Borsetti, F.5    Fabbri, E.6
  • 138
    • 84902672939 scopus 로고    scopus 로고
    • Rab12 localizes to Shiga toxin-induced plasma membrane invaginations and controls toxin transport
    • Rydell G.E., Renard H.-F., Garcia-Castillo M.-D., Dingli F., Loew D., Lamaze C., et al. Rab12 localizes to Shiga toxin-induced plasma membrane invaginations and controls toxin transport. Traffic 2014, 15:772-787. 10.1111/tra.12173.
    • (2014) Traffic , vol.15 , pp. 772-787
    • Rydell, G.E.1    Renard, H.-F.2    Garcia-Castillo, M.-D.3    Dingli, F.4    Loew, D.5    Lamaze, C.6
  • 139
    • 66649097426 scopus 로고    scopus 로고
    • Caveolin-1 regulation of dynamin-dependent, raft-mediated endocytosis of cholera toxin-B sub-unit occurs independently of caveolae
    • Lajoie P., Kojic L.D., Nim S., Li L., Dennis J.W., Nabi I.R. Caveolin-1 regulation of dynamin-dependent, raft-mediated endocytosis of cholera toxin-B sub-unit occurs independently of caveolae. J. Cell. Mol. Med. 2009, 13:3218-3225. 10.1111/j.1582-4934.2009.00732.x.
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 3218-3225
    • Lajoie, P.1    Kojic, L.D.2    Nim, S.3    Li, L.4    Dennis, J.W.5    Nabi, I.R.6
  • 140
    • 10744224620 scopus 로고    scopus 로고
    • Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulum
    • Fujinaga Y., Wolf A.A., Rodighiero C., Wheeler H., Tsai B., Allen L., et al. Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulum. Mol. Biol. Cell 2003, 14:4783-4793. 10.1091/mbc.E03.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4783-4793
    • Fujinaga, Y.1    Wolf, A.A.2    Rodighiero, C.3    Wheeler, H.4    Tsai, B.5    Allen, L.6
  • 142
    • 0028860250 scopus 로고
    • Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diptheria toxin receptor and inhibits specifically its mitogenic activity
    • Toshihide M., Higashiyama S., Taniguchi N., Klagsbrun M., Mekada E. Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diptheria toxin receptor and inhibits specifically its mitogenic activity. J. Biol. Chem. 1995, 270:1015-1019.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1015-1019
    • Toshihide, M.1    Higashiyama, S.2    Taniguchi, N.3    Klagsbrun, M.4    Mekada, E.5
  • 143
    • 84955185136 scopus 로고    scopus 로고
    • Molecular aspects of botulinum neurotoxin
    • Springer, New York, New York, NY, K.A. Foster (Ed.)
    • Popoff M.R., Connan C. Molecular aspects of botulinum neurotoxin. Curr. Top. Neurotox 2014, 4:35-68. Springer, New York, New York, NY. 10.1007/978-1-4614-9454-6. K.A. Foster (Ed.).
    • (2014) Curr. Top. Neurotox , vol.4 , pp. 35-68
    • Popoff, M.R.1    Connan, C.2
  • 144
    • 80052994116 scopus 로고    scopus 로고
    • Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly.
    • Sun S., Suresh S., Liu H., Tepp W.H., Johnson E.a, Edwardson J.M., et al. Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly. Cell Host Microbe 2011, 10:237-247. 10.1016/j.chom.2011.06.012.
    • (2011) Cell Host Microbe , vol.10 , pp. 237-247
    • Sun, S.1    Suresh, S.2    Liu, H.3    Tepp, W.H.4    Johnson, E.A.5    Edwardson, J.M.6
  • 146
    • 33746618384 scopus 로고    scopus 로고
    • Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1
    • Deinhardt K., Berninghausen O., Willison H.J., Hopkins C.R., Schiavo G. Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1. J. Cell Biol. 2006, 174:459-471. 10.1083/jcb.200508170.
    • (2006) J. Cell Biol. , vol.174 , pp. 459-471
    • Deinhardt, K.1    Berninghausen, O.2    Willison, H.J.3    Hopkins, C.R.4    Schiavo, G.5
  • 147
    • 84879537235 scopus 로고    scopus 로고
    • Tetanus toxin Hc fragment induces the formation of ceramide platforms and protects neuronal cells against oxidative stress
    • Cubí R., Candalija A., Ortega A., Gil C., Aguilera J. Tetanus toxin Hc fragment induces the formation of ceramide platforms and protects neuronal cells against oxidative stress. PLoS One 2013, 8:e68055. 10.1371/journal.pone.0068055.
    • (2013) PLoS One , vol.8 , pp. e68055
    • Cubí, R.1    Candalija, A.2    Ortega, A.3    Gil, C.4    Aguilera, J.5
  • 148
    • 33644871336 scopus 로고    scopus 로고
    • Internalized Pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum.
    • Smith D.C., Spooner R.a, Watson P.D., Murray J.L., Hodge T.W., Amessou M., et al. Internalized Pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum. Traffic 2006, 7:379-393. 10.1111/j.1600-0854.2006.00391.x.
    • (2006) Traffic , vol.7 , pp. 379-393
    • Smith, D.C.1    Spooner, R.A.2    Watson, P.D.3    Murray, J.L.4    Hodge, T.W.5    Amessou, M.6
  • 149
    • 0022005540 scopus 로고
    • Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin toxin
    • Moya M., Dautry-Varsat A., Goud B., Louvard D., Boquet P. Inhibition of coated pit formation in Hep2 cells blocks the cytotoxicity of diphtheria toxin but not that of ricin toxin. J. Cell Biol. 1985, 101:548-559.
    • (1985) J. Cell Biol. , vol.101 , pp. 548-559
    • Moya, M.1    Dautry-Varsat, A.2    Goud, B.3    Louvard, D.4    Boquet, P.5
  • 150
    • 0019309042 scopus 로고
    • Entry of lethal doses of abrin, ricin and modeccin into the cytosol of HeLa Cells
    • Eiklid K., Olsnes S., Pihl A. Entry of lethal doses of abrin, ricin and modeccin into the cytosol of HeLa Cells. Exp. Cell Res. 1980, 126:321-326.
    • (1980) Exp. Cell Res. , vol.126 , pp. 321-326
    • Eiklid, K.1    Olsnes, S.2    Pihl, A.3
  • 151
    • 84893565146 scopus 로고    scopus 로고
    • Ricin and ricin-containing immunotoxins: insights into intracellular transport and mechanism of action in vitro
    • Słomińska-Wojewódzka M., Sandvig K. Ricin and ricin-containing immunotoxins: insights into intracellular transport and mechanism of action in vitro. Antibodies 2013, 2:236-269. 10.3390/antib2020236.
    • (2013) Antibodies , vol.2 , pp. 236-269
    • Słomińska-Wojewódzka, M.1    Sandvig, K.2
  • 154
    • 84878783726 scopus 로고    scopus 로고
    • N-way FRET microscopy of multiple protein-protein interactions in live cells
    • Hoppe A.D., Scott B.L., Welliver T.P., Straight S.W., Swanson J.a N-way FRET microscopy of multiple protein-protein interactions in live cells. PLoS One 2013, 8:e64760. 10.1371/journal.pone.0064760.
    • (2013) PLoS One , vol.8 , pp. e64760
    • Hoppe, A.D.1    Scott, B.L.2    Welliver, T.P.3    Straight, S.W.4    Swanson, J.A.5
  • 155
    • 84892608409 scopus 로고    scopus 로고
    • Entry of influenza A virus: host factors and antiviral targets
    • Edinger T.O., Pohl M.O., Stertz S. Entry of influenza A virus: host factors and antiviral targets. J. Gen. Virol. 2014, 95:263-277. 10.1099/vir. 0.059477-0.
    • (2014) J. Gen. Virol. , vol.95 , pp. 263-277
    • Edinger, T.O.1    Pohl, M.O.2    Stertz, S.3
  • 156
    • 84878119333 scopus 로고    scopus 로고
    • Actin mediates the nanoscale membrane organization of the clustered membrane protein influenza hemagglutinin
    • Gudheti M.V., Curthoys N.M., Gould T.J., Kim D., Gunewardene M.S., Gabor K.a, et al. Actin mediates the nanoscale membrane organization of the clustered membrane protein influenza hemagglutinin. Biophys. J. 2013, 104:2182-2192. 10.1016/j.bpj.2013.03.054.
    • (2013) Biophys. J. , vol.104 , pp. 2182-2192
    • Gudheti, M.V.1    Curthoys, N.M.2    Gould, T.J.3    Kim, D.4    Gunewardene, M.S.5    Gabor, K.A.6
  • 157
    • 1942489100 scopus 로고    scopus 로고
    • Rotavirus RRV associates with lipid membrane microdomains during cell entry
    • Isa P., Realpe M., Romero P., López S., Arias C.F. Rotavirus RRV associates with lipid membrane microdomains during cell entry. Virology 2004, 322:370-381. 10.1016/j.virol.2004.02.018.
    • (2004) Virology , vol.322 , pp. 370-381
    • Isa, P.1    Realpe, M.2    Romero, P.3    López, S.4    Arias, C.F.5
  • 158
    • 84888605265 scopus 로고    scopus 로고
    • Molecular arrangement between multivalent glycocluster and Pseudomonas aeruginosa LecA (PA-IL) by atomic force microscopy: influence of the glycocluster concentration
    • Sicard D., Chevolot Y., Souteyrand E., Imberty A., Vidal S., Phaner-Goutorbe M. Molecular arrangement between multivalent glycocluster and Pseudomonas aeruginosa LecA (PA-IL) by atomic force microscopy: influence of the glycocluster concentration. J. Mol. Recognit. 2013, 26:694-699. 10.1002/jmr.2333.
    • (2013) J. Mol. Recognit. , vol.26 , pp. 694-699
    • Sicard, D.1    Chevolot, Y.2    Souteyrand, E.3    Imberty, A.4    Vidal, S.5    Phaner-Goutorbe, M.6
  • 159
    • 79953311518 scopus 로고    scopus 로고
    • Type VI secretion system in Pseudomonas aeruginosa: secretion and multimerization of VgrG proteins
    • Hachani A., Lossi N.S., Hamilton A., Jones C., Bleves S., Albesa-Jové D., et al. Type VI secretion system in Pseudomonas aeruginosa: secretion and multimerization of VgrG proteins. J. Biol. Chem. 2011, 286:12317-12327. 10.1074/jbc.M110.193045.
    • (2011) J. Biol. Chem. , vol.286 , pp. 12317-12327
    • Hachani, A.1    Lossi, N.S.2    Hamilton, A.3    Jones, C.4    Bleves, S.5    Albesa-Jové, D.6
  • 160
    • 84866060723 scopus 로고    scopus 로고
    • Involvement of c-Src tyrosine kinase upstream of class I phosphatidylinositol (PI) 3-kinases in Salmonella Enteritidis Rck protein-mediated invasion
    • Wiedemann A., Rosselin M., Mijouin L., Bottreau E., Velge P. Involvement of c-Src tyrosine kinase upstream of class I phosphatidylinositol (PI) 3-kinases in Salmonella Enteritidis Rck protein-mediated invasion. J. Biol. Chem. 2012, 287:31148-31154. 10.1074/jbc.M112.392134.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31148-31154
    • Wiedemann, A.1    Rosselin, M.2    Mijouin, L.3    Bottreau, E.4    Velge, P.5
  • 161
    • 77953288100 scopus 로고    scopus 로고
    • Rck of Salmonella enterica, subspecies enterica serovar enteritidis, mediates zipper-like internalization
    • Rosselin M., Virlogeux-Payant I., Roy C., Bottreau E., Sizaret P.-Y., Mijouin L., et al. Rck of Salmonella enterica, subspecies enterica serovar enteritidis, mediates zipper-like internalization. Cell Res. 2010, 20:647-664. 10.1038/cr.2010.45.
    • (2010) Cell Res. , vol.20 , pp. 647-664
    • Rosselin, M.1    Virlogeux-Payant, I.2    Roy, C.3    Bottreau, E.4    Sizaret, P.-Y.5    Mijouin, L.6
  • 162
    • 38549126641 scopus 로고    scopus 로고
    • Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion.
    • Schroeder G.N., Hilbi H. Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion. Clin. Microbiol. Rev. 2008, 21:134-156. 10.1128/CMR. 00032-07.
    • (2008) Clin. Microbiol. Rev. , vol.21 , pp. 134-156
    • Schroeder, G.N.1    Hilbi, H.2
  • 163
    • 0029005239 scopus 로고
    • Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp6Oc-src-mediated signalling pathway
    • Dehio C., Prevost M., Sansonetti P.J. Invasion of epithelial cells by Shigella flexneri induces tyrosine phosphorylation of cortactin by a pp6Oc-src-mediated signalling pathway. EMBO J. 1995, 14:2471-2482.
    • (1995) EMBO J. , vol.14 , pp. 2471-2482
    • Dehio, C.1    Prevost, M.2    Sansonetti, P.J.3
  • 164
    • 0034604515 scopus 로고    scopus 로고
    • Involvement of cellular caveolae in bacterial entry into mast cells
    • (80-.)
    • Shin J.-S. Involvement of cellular caveolae in bacterial entry into mast cells. Science 2000, 289:785-788. (80-.). 10.1126/science.289.5480.785.
    • (2000) Science , vol.289 , pp. 785-788
    • Shin, J.-S.1
  • 165
    • 4444329588 scopus 로고    scopus 로고
    • Role of lipid rafts in E-cadherin- and HGF-R/Met-mediated entry of Listeria monocytogenes into host cells
    • Seveau S., Bierne H., Giroux S., Prévost M.-C., Cossart P. Role of lipid rafts in E-cadherin- and HGF-R/Met-mediated entry of Listeria monocytogenes into host cells. J. Cell Biol. 2004, 166:743-753. 10.1083/jcb.200406078.
    • (2004) J. Cell Biol. , vol.166 , pp. 743-753
    • Seveau, S.1    Bierne, H.2    Giroux, S.3    Prévost, M.-C.4    Cossart, P.5
  • 166
    • 83755183062 scopus 로고    scopus 로고
    • Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization
    • Bonazzi M., Vasudevan L., Mallet A., Sachse M., Sartori A., Prevost M.-C., et al. Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization. J. Cell Biol. 2011, 195:525-536. 10.1083/jcb.201105152.
    • (2011) J. Cell Biol. , vol.195 , pp. 525-536
    • Bonazzi, M.1    Vasudevan, L.2    Mallet, A.3    Sachse, M.4    Sartori, A.5    Prevost, M.-C.6
  • 167
    • 8744233911 scopus 로고    scopus 로고
    • Early signaling events involved in the entry of Rickettsia conorii into mammalian cells
    • Martinez J.J., Cossart P. Early signaling events involved in the entry of Rickettsia conorii into mammalian cells. J. Cell Sci. 2004, 117:5097-5106. 10.1242/jcs.01382.
    • (2004) J. Cell Sci. , vol.117 , pp. 5097-5106
    • Martinez, J.J.1    Cossart, P.2
  • 168
    • 28944447801 scopus 로고    scopus 로고
    • Ku70, a component of DNA-dependent protein kinase, is a mammalian receptor for Rickettsia conorii
    • Martinez J.J., Seveau S., Veiga E., Matsuyama S., Cossart P. Ku70, a component of DNA-dependent protein kinase, is a mammalian receptor for Rickettsia conorii. Cell 2005, 123:1013-1023. 10.1016/j.cell.2005.08.046.
    • (2005) Cell , vol.123 , pp. 1013-1023
    • Martinez, J.J.1    Seveau, S.2    Veiga, E.3    Matsuyama, S.4    Cossart, P.5
  • 169
    • 0036307071 scopus 로고    scopus 로고
    • Modulation of Brucella-induced macropinocytosis by lipid rafts mediates intracellular replication
    • Watarai M., Makino S.-I., Fujii Y., Okamoto K., Shirahata T. Modulation of Brucella-induced macropinocytosis by lipid rafts mediates intracellular replication. Cell. Microbiol. 2002, 4:341-355.
    • (2002) Cell. Microbiol. , vol.4 , pp. 341-355
    • Watarai, M.1    Makino, S.-I.2    Fujii, Y.3    Okamoto, K.4    Shirahata, T.5
  • 170
    • 77950662773 scopus 로고    scopus 로고
    • Molecular pathogenesis of infections caused by Legionella pneumophila
    • Newton H.J., Ang D.K.Y., van Driel I.R., Hartland E.L. Molecular pathogenesis of infections caused by Legionella pneumophila. Clin. Microbiol. Rev. 2010, 23:274-298. 10.1128/CMR. 00052-09.
    • (2010) Clin. Microbiol. Rev. , vol.23 , pp. 274-298
    • Newton, H.J.1    Ang, D.K.Y.2    van Driel, I.R.3    Hartland, E.L.4
  • 171
    • 84900539372 scopus 로고    scopus 로고
    • Early sequence of events triggered by the interaction of Neisseria meningitidis with endothelial cells
    • Soyer M., Charles-Orszag A., Lagache T., Machata S., Imhaus A.-F., Dumont A., et al. Early sequence of events triggered by the interaction of Neisseria meningitidis with endothelial cells. Cell. Microbiol. 2013, 10.1111/cmi.12248.
    • (2013) Cell. Microbiol.
    • Soyer, M.1    Charles-Orszag, A.2    Lagache, T.3    Machata, S.4    Imhaus, A.-F.5    Dumont, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.