메뉴 건너뛰기




Volumn 7, Issue 1, 2017, Pages

N-glycan mediated adhesion strengthening during pathogen-receptor binding revealed by cell-cell force spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; CELL SURFACE RECEPTOR; DC-SPECIFIC ICAM-3 GRABBING NONINTEGRIN; LECTIN; POLYSACCHARIDE;

EID: 85026401827     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-017-07220-w     Document Type: Article
Times cited : (18)

References (62)
  • 1
    • 33749476819 scopus 로고    scopus 로고
    • Organization of the integrin LFA-1 in nanoclusters regulates its activity
    • Cambi, A. et al. Organization of the integrin LFA-1 in nanoclusters regulates its activity. Mol. Biol. Cell 17, 4270-4281 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4270-4281
    • Cambi, A.1
  • 2
    • 33747091892 scopus 로고    scopus 로고
    • Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering
    • Cairo, C. W., Mirchev, R., Golan, D. E. Cytoskeletal regulation couples LFA-1 conformational changes to receptor lateral mobility and clustering. Immunity 25, 297-308, doi: 10.1016/j.immuni.2006.06.012 (2006).
    • (2006) Immunity , vol.25 , pp. 297-308
    • Cairo, C.W.1    Mirchev, R.2    Golan, D.E.3
  • 3
    • 84859463286 scopus 로고    scopus 로고
    • Lateral mobility of individual integrin nanoclusters orchestrates the onset for leukocyte adhesion
    • Bakker, G. J. et al. Lateral mobility of individual integrin nanoclusters orchestrates the onset for leukocyte adhesion. Proc. Natl. Acad. Sci. USA 109, 4869-4874, doi: 10.1073/pnas.1116425109 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 4869-4874
    • Bakker, G.J.1
  • 4
    • 48749095948 scopus 로고    scopus 로고
    • Actin restricts FcepsilonRI diffusion and facilitates antigen-induced receptor immobilization
    • Andrews, N. L. et al. Actin restricts FcepsilonRI diffusion and facilitates antigen-induced receptor immobilization. Nat. Cell Biol. 10, 955-963, doi: 10.1038/ncb1755 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 955-963
    • Andrews, N.L.1
  • 5
    • 80555148149 scopus 로고    scopus 로고
    • ErbB1 dimerization is promoted by domain co-confinement and stabilized by ligand binding
    • Low-Nam, S. T. et al. ErbB1 dimerization is promoted by domain co-confinement and stabilized by ligand binding. Nat. Struct. Mol. Biol. 18, 1244-1249, doi: 10.1038/nsmb.2135 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1244-1249
    • Low-Nam, S.T.1
  • 6
    • 77949873936 scopus 로고    scopus 로고
    • CD169(+) macrophages present lipid antigens to mediate early activation of iNKT cells in lymph nodes
    • Barral, P. et al. CD169(+) macrophages present lipid antigens to mediate early activation of iNKT cells in lymph nodes. Nat. Immunol. 11, 303-312, doi: 10.1038/ni.1853 (2010).
    • (2010) Nat. Immunol. , vol.11 , pp. 303-312
    • Barral, P.1
  • 7
    • 84959574440 scopus 로고    scopus 로고
    • Dynamics of the actin cytoskeleton mediates receptor cross talk: An emerging concept in tuning receptor signaling
    • Mattila, P. K., Batista, F. D., Treanor, B. Dynamics of the actin cytoskeleton mediates receptor cross talk: An emerging concept in tuning receptor signaling. J. Cell Biol. 212, 267-280, doi: 10.1083/jcb.201504137 (2016).
    • (2016) J. Cell Biol. , vol.212 , pp. 267-280
    • Mattila, P.K.1    Batista, F.D.2    Treanor, B.3
  • 8
    • 84957837590 scopus 로고    scopus 로고
    • The actin cytoskeleton modulates the activation of iNKT cells by segregating CD1d nanoclusters on antigen-presenting cells
    • Torreno-Pina, J. A. et al. The actin cytoskeleton modulates the activation of iNKT cells by segregating CD1d nanoclusters on antigen-presenting cells. Proc. Natl. Acad. Sci. USA 113, E772-781, doi: 10.1073/pnas.1514530113 (2016).
    • (2016) Proc. Natl. Acad. Sci. USA , vol.113 , pp. E772-781
    • Torreno-Pina, J.A.1
  • 9
    • 0347122962 scopus 로고    scopus 로고
    • Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells
    • Cambi, A. et al. Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells. J. Cell Biol. 164, 145-155, doi: 10.1083/jcb.200306112 (2004).
    • (2004) J. Cell Biol. , vol.164 , pp. 145-155
    • Cambi, A.1
  • 10
    • 84869031422 scopus 로고    scopus 로고
    • The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells
    • Manzo, C. et al. The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells. J. Biol. Chem. 287, 38946-38955, doi: 10.1074/jbc.M112.380121 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 38946-38955
    • Manzo, C.1
  • 11
    • 84914145217 scopus 로고    scopus 로고
    • Nanoclustering as a dominant feature of plasma membrane organization
    • Garcia-Parajo, M. F., Cambi, A., Torreno-Pina, J. A., Thompson, N., Jacobson, K. Nanoclustering as a dominant feature of plasma membrane organization. J. Cell Sci. 127, 4995-5005, doi: 10.1242/jcs.146340 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 4995-5005
    • Garcia-Parajo, M.F.1    Cambi, A.2    Torreno-Pina, J.A.3    Thompson, N.4    Jacobson, K.5
  • 12
    • 2942610580 scopus 로고    scopus 로고
    • Actin microdomains on endothelial cells: Association with CD44, ERM proteins, and signaling molecules during quiescence and wound healing
    • Jensen, P. V., Larsson, L. I. Actin microdomains on endothelial cells: Association with CD44, ERM proteins, and signaling molecules during quiescence and wound healing. Histochem. Cell Biol. 121, 361-369, doi: 10.1007/s00418-004-0648-2 (2004).
    • (2004) Histochem. Cell Biol. , vol.121 , pp. 361-369
    • Jensen, P.V.1    Larsson, L.I.2
  • 13
    • 0037227965 scopus 로고    scopus 로고
    • CD44: From adhesion molecules to signalling regulators
    • Ponta, H., Sherman, L., Herrlich, P. A. CD44: From adhesion molecules to signalling regulators. Nat. Rev. Mol. Cell Biol. 4, 33-45, doi: 10.1038/nrm1004 (2003).
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 33-45
    • Ponta, H.1    Sherman, L.2    Herrlich, P.A.3
  • 14
    • 0036521487 scopus 로고    scopus 로고
    • Constitutive and induced expression of DC-SIGN on dendritic cell and macrophage subpopulations in situ and in vitro
    • Soilleux, E. J. et al. Constitutive and induced expression of DC-SIGN on dendritic cell and macrophage subpopulations in situ and in vitro. J. Leukoc. Biol. 71, 445-457 (2002).
    • (2002) J. Leukoc. Biol. , vol.71 , pp. 445-457
    • Soilleux, E.J.1
  • 15
    • 0034598934 scopus 로고    scopus 로고
    • Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses
    • Geijtenbeek, T. B. et al. Identification of DC-SIGN, a novel dendritic cell-specific ICAM-3 receptor that supports primary immune responses. Cell 100, 575-585 (2000).
    • (2000) Cell , vol.100 , pp. 575-585
    • Geijtenbeek, T.B.1
  • 16
    • 0034598905 scopus 로고    scopus 로고
    • DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells
    • Geijtenbeek, T. B. et al. DC-SIGN, a dendritic cell-specific HIV-1-binding protein that enhances trans-infection of T cells. Cell 100, 587-597 (2000).
    • (2000) Cell , vol.100 , pp. 587-597
    • Geijtenbeek, T.B.1
  • 17
    • 0036278649 scopus 로고    scopus 로고
    • C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans
    • Alvarez, C. P. et al. C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans. J. Virol. 76, 6841-6844 (2002).
    • (2002) J. Virol. , vol.76 , pp. 6841-6844
    • Alvarez, C.P.1
  • 18
    • 3042788418 scopus 로고    scopus 로고
    • Hepatitis C virus targets DC-SIGN and L-SIGN to escape lysosomal degradation
    • Ludwig, I. S. et al. Hepatitis C virus targets DC-SIGN and L-SIGN to escape lysosomal degradation. J. Virol. 78, 8322-8332, doi: 10.1128/JVI.78.15.8322-8332.2004 (2004).
    • (2004) J. Virol. , vol.78 , pp. 8322-8332
    • Ludwig, I.S.1
  • 19
    • 0037237593 scopus 로고    scopus 로고
    • Mycobacteria target DC-SIGN to suppress dendritic cell function
    • Geijtenbeek, T. B. et al. Mycobacteria target DC-SIGN to suppress dendritic cell function. J. Exp. Med. 197, 7-17 (2003).
    • (2003) J. Exp. Med. , vol.197 , pp. 7-17
    • Geijtenbeek, T.B.1
  • 20
    • 0037331548 scopus 로고    scopus 로고
    • The C-type lectin DC-SIGN (CD209) is an antigen-uptake receptor for Candida albicans on dendritic cells
    • Cambi, A. et al. The C-type lectin DC-SIGN (CD209) is an antigen-uptake receptor for Candida albicans on dendritic cells. Eur. J. Immunol. 33, 532-538 (2003).
    • (2003) Eur. J. Immunol. , vol.33 , pp. 532-538
    • Cambi, A.1
  • 21
    • 0035824446 scopus 로고    scopus 로고
    • Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR
    • Feinberg, H., Mitchell, D. A., Drickamer, K., Weis, W. I. Structural basis for selective recognition of oligosaccharides by DC-SIGN and DC-SIGNR. Science 294, 2163-2166, doi: 10.1126/science.1066371 (2001).
    • (2001) Science , vol.294 , pp. 2163-2166
    • Feinberg, H.1    Mitchell, D.A.2    Drickamer, K.3    Weis, W.I.4
  • 22
    • 0035800757 scopus 로고    scopus 로고
    • A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands
    • Mitchell, D. A., Fadden, A. J., Drickamer, K. A novel mechanism of carbohydrate recognition by the C-type lectins DC-SIGN and DC-SIGNR. Subunit organization and binding to multivalent ligands. J. Biol. Chem. 276, 28939-28945, doi: 10.1074/jbc.M104565200 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 23
    • 12444347833 scopus 로고    scopus 로고
    • Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR
    • Feinberg, H., Guo, Y., Mitchell, D. A., Drickamer, K., Weis, W. I. Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR. J. Biol. Chem. 280, 1327-1335, doi: 10.1074/jbc.M409925200 (2005).
    • (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
  • 24
    • 15244356948 scopus 로고    scopus 로고
    • Characterization of DC-SIGN/R interaction with human immunodeficiency virus type 1 gp120 and ICAM molecules favors the receptor's role as an antigen-capturing rather than an adhesion receptor
    • Snyder, G. A. et al. Characterization of DC-SIGN/R interaction with human immunodeficiency virus type 1 gp120 and ICAM molecules favors the receptor's role as an antigen-capturing rather than an adhesion receptor. J. Virol. 79, 4589-4598, doi: 10.1128/JVI.79.8.4589-4598.2005 (2005).
    • (2005) J. Virol. , vol.79 , pp. 4589-4598
    • Snyder, G.A.1
  • 25
    • 0035033755 scopus 로고    scopus 로고
    • DC-SIGN interactions with human immunodeficiency virus type 1 and 2 and simian immunodeficiency virus
    • Pohlmann, S. et al. DC-SIGN interactions with human immunodeficiency virus type 1 and 2 and simian immunodeficiency virus. J. Virol. 75, 4664-4672, doi: 10.1128/JVI.75.10.4664-4672.2001 (2001).
    • (2001) J. Virol. , vol.75 , pp. 4664-4672
    • Pohlmann, S.1
  • 26
    • 34447569554 scopus 로고    scopus 로고
    • Nanoscale organization of the pathogen receptor DC-SIGN mapped by single-molecule high-resolution fluorescence microscopy
    • de Bakker, B. I. et al. Nanoscale organization of the pathogen receptor DC-SIGN mapped by single-molecule high-resolution fluorescence microscopy. Chemphyschem 8, 1473-1480, doi: 10.1002/cphc.200700169 (2007).
    • (2007) Chemphyschem , vol.8 , pp. 1473-1480
    • De Bakker, B.I.1
  • 27
    • 42149114525 scopus 로고    scopus 로고
    • Distribution and lateral mobility of DC-SIGN on immature dendritic cells-implications for pathogen uptake
    • Neumann, A. K., Thompson, N. L., Jacobson, K. Distribution and lateral mobility of DC-SIGN on immature dendritic cells-implications for pathogen uptake. J. Cell Sci. 121, 634-643, doi: 10.1242/jcs.022418 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 634-643
    • Neumann, A.K.1    Thompson, N.L.2    Jacobson, K.3
  • 28
    • 79960298029 scopus 로고    scopus 로고
    • DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different
    • Itano, M. S. et al. DC-SIGN and influenza hemagglutinin dynamics in plasma membrane microdomains are markedly different. Biophys. J. 100, 2662-2670, doi: 10.1016/j.bpj.2011.04.044 (2011).
    • (2011) Biophys. J. , vol.100 , pp. 2662-2670
    • Itano, M.S.1
  • 29
    • 84904976236 scopus 로고    scopus 로고
    • Enhanced receptor-clathrin interactions induced by N-glycan-mediated membrane micropatterning
    • Torreno-Pina, J. A. et al. Enhanced receptor-clathrin interactions induced by N-glycan-mediated membrane micropatterning. Proc. Natl. Acad. Sci. USA 111, 11037-11042, doi: 10.1073/pnas.1402041111 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 11037-11042
    • Torreno-Pina, J.A.1
  • 30
    • 0033824065 scopus 로고    scopus 로고
    • Avidity regulation of integrins: The driving force in leukocyte adhesion
    • van Kooyk, Y., Figdor, C. G. Avidity regulation of integrins: The driving force in leukocyte adhesion. Curr. Opin. Cell Biol. 12, 542-547 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 542-547
    • Van Kooyk, Y.1    Figdor, C.G.2
  • 31
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • Parsons, J. T., Horwitz, A. R., Schwartz, M. A. Cell adhesion: Integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell Biol. 11, 633-643, doi: 10.1038/nrm2957 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 33
    • 84897401119 scopus 로고    scopus 로고
    • Dynamic coupling of ALCAM to the actin cortex strengthens cell adhesion to CD6
    • Te Riet, J. et al. Dynamic coupling of ALCAM to the actin cortex strengthens cell adhesion to CD6. J. Cell Sci. 127, 1595-1606, doi:10.1242/jcs.141077 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 1595-1606
    • Te Riet, J.1
  • 34
    • 84943820940 scopus 로고    scopus 로고
    • AFM force spectroscopy reveals how subtle structural differences affect the interaction strength between Candida albicans and DC-SIGN
    • Te Riet, J., Reinieren-Beeren, I., Figdor, C. G., Cambi, A. AFM force spectroscopy reveals how subtle structural differences affect the interaction strength between Candida albicans and DC-SIGN. J. Mol. Recognit. 28, 687-698, doi: 10.1002/jmr.2481 (2015).
    • (2015) J. Mol. Recognit. , vol.28 , pp. 687-698
    • Te Riet, J.1    Reinieren-Beeren, I.2    Figdor, C.G.3    Cambi, A.4
  • 35
    • 79958126320 scopus 로고    scopus 로고
    • Single-molecule binding of CD44 to fibrin versus P-selectin predicts their distinct shear-dependent interactions in cancer
    • Raman, P. S., Alves, C. S., Wirtz, D., Konstantopoulos, K. Single-molecule binding of CD44 to fibrin versus P-selectin predicts their distinct shear-dependent interactions in cancer. J. Cell Sci. 124, 1903-1910, doi: 10.1242/jcs.079814 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 1903-1910
    • Raman, P.S.1    Alves, C.S.2    Wirtz, D.3    Konstantopoulos, K.4
  • 36
    • 37249050958 scopus 로고    scopus 로고
    • Distinct kinetic and mechanical properties govern ALCAM-mediated interactions as shown by single-molecule force spectroscopy
    • Te Riet, J., et al. Distinct kinetic and mechanical properties govern ALCAM-mediated interactions as shown by single-molecule force spectroscopy. J. Cell Sci. 120, 3965-3976 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 3965-3976
    • Te Riet, J.1
  • 37
    • 84860546998 scopus 로고    scopus 로고
    • Dynamic cell adhesion and migration on nanoscale grooved substrates
    • Lamers, E. et al. Dynamic cell adhesion and migration on nanoscale grooved substrates. Eur. Cell. Mater. 23, 182-193 (2012).
    • (2012) Eur. Cell. Mater. , vol.23 , pp. 182-193
    • Lamers, E.1
  • 38
    • 77954286695 scopus 로고    scopus 로고
    • Quantifying cellular adhesion to extracellular matrix components by single-cell force spectroscopy
    • Friedrichs, J., Helenius, J., Muller, D. J. Quantifying cellular adhesion to extracellular matrix components by single-cell force spectroscopy. Nat. Protoc. 5, 1353-1361, doi: 10.1038/nprot.2010.89 (2010).
    • (2010) Nat. Protoc. , vol.5 , pp. 1353-1361
    • Friedrichs, J.1    Helenius, J.2    Muller, D.J.3
  • 39
    • 84885596782 scopus 로고    scopus 로고
    • Investigating differential cell-matrix adhesion by directly comparative single-cell force spectroscopy
    • Dao, L., Gonnermann, C., Franz, C. M. Investigating differential cell-matrix adhesion by directly comparative single-cell force spectroscopy. J. Mol. Recognit. 26, 578-589, doi: 10.1002/jmr.2303 (2013).
    • (2013) J. Mol. Recognit. , vol.26 , pp. 578-589
    • Dao, L.1    Gonnermann, C.2    Franz, C.M.3
  • 40
    • 84949252234 scopus 로고    scopus 로고
    • Mast cells and dendritic cells form synapses that facilitate antigen transfer for T cell activation
    • Carroll-Portillo, A. et al. Mast cells and dendritic cells form synapses that facilitate antigen transfer for T cell activation. J. Cell Biol. 210, 851-864, doi: 10.1083/jcb.201412074 (2015).
    • (2015) J. Cell Biol. , vol.210 , pp. 851-864
    • Carroll-Portillo, A.1
  • 41
    • 79960401707 scopus 로고    scopus 로고
    • Mechanical interactions between dendritic cells and T cells correlate with T cell responsiveness
    • Lim, T. S., Mortellaro, A., Lim, C. T., Hammerling, G. J., Ricciardi-Castagnoli, P. Mechanical interactions between dendritic cells and T cells correlate with T cell responsiveness. J. Immunol. 187, 258-265, doi: 10.4049/jimmunol.1100267 (2011).
    • (2011) J. Immunol. , vol.187 , pp. 258-265
    • Lim, T.S.1    Mortellaro, A.2    Lim, C.T.3    Hammerling, G.J.4    Ricciardi-Castagnoli, P.5
  • 42
    • 79960924956 scopus 로고    scopus 로고
    • Atomic force microscopy: A nanoscopic window on the cell surface
    • Muller, D. J., Dufrene, Y. F. Atomic force microscopy: A nanoscopic window on the cell surface. Trends Cell Biol 21, 461-469, doi: 10.1016/j.tcb.2011.04.008 (2011).
    • (2011) Trends Cell Biol , vol.21 , pp. 461-469
    • Muller, D.J.1    Dufrene, Y.F.2
  • 43
    • 85009095769 scopus 로고    scopus 로고
    • Nanoscale adhesion forces between the fungal pathogen Candida albicans and macrophages
    • El-Kirat-Chatel, S., Dufrêne, Y. F. Nanoscale adhesion forces between the fungal pathogen Candida albicans and macrophages. Nanoscale Horizons 1, 69-74 (2016).
    • (2016) Nanoscale Horizons , vol.1 , pp. 69-74
    • El-Kirat-Chatel, S.1    Dufrêne, Y.F.2
  • 44
    • 84886499794 scopus 로고    scopus 로고
    • Adhesion and fusion efficiencies of human immunodeficiency virus type 1 (HIV-1) surface proteins
    • Dobrowsky, T. M. et al. Adhesion and fusion efficiencies of human immunodeficiency virus type 1 (HIV-1) surface proteins. Sci. Rep. 3, 3014, doi: 10.1038/srep03014 (2013).
    • (2013) Sci. Rep. , vol.3 , pp. 3014
    • Dobrowsky, T.M.1
  • 45
    • 84908230228 scopus 로고    scopus 로고
    • Atomic force microscopy in microbiology: New structural and functional insights into the microbial cell surface
    • Dufrene, Y. F. Atomic force microscopy in microbiology: New structural and functional insights into the microbial cell surface. MBio 5, e01363-01314, doi: 10.1128/mBio.01363-14 (2014).
    • (2014) MBio , vol.5 , pp. e01363-01314
    • Dufrene, Y.F.1
  • 46
    • 0035451130 scopus 로고    scopus 로고
    • Trends in mortality due to invasive mycotic diseases in the United States 1980-1997
    • McNeil, M. M. et al. Trends in mortality due to invasive mycotic diseases in the United States, 1980-1997. Clin. Infect. Dis. 33, 641-647 (2001).
    • (2001) Clin. Infect. Dis. , vol.33 , pp. 641-647
    • McNeil, M.M.1
  • 47
    • 50649113319 scopus 로고    scopus 로고
    • Dendritic cell interaction with Candida albicans critically depends on N-linked mannan
    • Cambi, A. et al. Dendritic cell interaction with Candida albicans critically depends on N-linked mannan. J. Biol. Chem. 283, 20590-20599 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 20590-20599
    • Cambi, A.1
  • 48
    • 34248228113 scopus 로고    scopus 로고
    • Ligand-conjugated quantum dots monitor antigen uptake and processing by dendritic cells
    • Cambi, A., Lidke, D. S., Arndt-Jovin, D. J., Figdor, C. G., Jovin, T. M. Ligand-conjugated quantum dots monitor antigen uptake and processing by dendritic cells. Nano Lett. 7, 970-977, doi: 10.1021/nl0700503 (2007).
    • (2007) Nano Lett. , vol.7 , pp. 970-977
    • Cambi, A.1    Lidke, D.S.2    Arndt-Jovin, D.J.3    Figdor, C.G.4    Jovin, T.M.5
  • 49
    • 15244352448 scopus 로고    scopus 로고
    • The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer
    • Snyder, G. A., Colonna, M., Sun, P. D. The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer. J. Mol. Biol. 347, 979-989 (2005).
    • (2005) J. Mol. Biol. , vol.347 , pp. 979-989
    • Snyder, G.A.1    Colonna, M.2    Sun, P.D.3
  • 50
    • 57049166474 scopus 로고    scopus 로고
    • A bond for a lifetime: Employing membrane nanotubes from living cells to determine receptor-ligand kinetics
    • Krieg, M., Helenius, J., Heisenberg, C. P., Muller, D. J. A bond for a lifetime: Employing membrane nanotubes from living cells to determine receptor-ligand kinetics. Angew. Chem. 47, 9775-9777, doi: 10.1002/anie.200803552 (2008).
    • (2008) Angew. Chem. , vol.47 , pp. 9775-9777
    • Krieg, M.1    Helenius, J.2    Heisenberg, C.P.3    Muller, D.J.4
  • 51
    • 28444450194 scopus 로고    scopus 로고
    • Multiple membrane tethers probed by atomic force microscopy
    • Sun, M. et al. Multiple membrane tethers probed by atomic force microscopy. Biophys. J. 89, 4320-4329, doi: 10.1529/biophysj.104.058180 (2005).
    • (2005) Biophys. J. , vol.89 , pp. 4320-4329
    • Sun, M.1
  • 52
    • 70449533662 scopus 로고    scopus 로고
    • Segmented helical structure of the neck region of the glycan-binding receptor DC-SIGNR
    • Feinberg, H., Tso, C. K., Taylor, M. E., Drickamer, K., Weis, W. I. Segmented helical structure of the neck region of the glycan-binding receptor DC-SIGNR. J. Mol. Biol. 394, 613-620 (2009).
    • (2009) J. Mol. Biol. , vol.394 , pp. 613-620
    • Feinberg, H.1    Tso, C.K.2    Taylor, M.E.3    Drickamer, K.4    Weis, W.I.5
  • 53
    • 0037420289 scopus 로고    scopus 로고
    • Analytical descriptions of dynamic force spectroscopy: Behaviour of multiple connections
    • Williams, P. M. Analytical descriptions of dynamic force spectroscopy: Behaviour of multiple connections. Anal. Chim. Acta. 479(107), 115 (2003).
    • (2003) Anal. Chim. Acta. , vol.479 , Issue.107 , pp. 115
    • Williams, P.M.1
  • 54
    • 84856317475 scopus 로고    scopus 로고
    • Unraveling the human dendritic cell phagosome proteome by organellar enrichment ranking
    • Buschow, S. I. et al. Unraveling the human dendritic cell phagosome proteome by organellar enrichment ranking. J. Proteomics 75, 1547-1562, doi: 10.1016/j.jprot.2011.11.024 (2012).
    • (2012) J. Proteomics , vol.75 , pp. 1547-1562
    • Buschow, S.I.1
  • 55
    • 0023957304 scopus 로고
    • Structural studies of mannans from the cell walls of the pathogenic yeasts Candida albicans serotypes A and B and Candida parapsilosis
    • Kogan, G., Pavliak, V., Masler, L. Structural studies of mannans from the cell walls of the pathogenic yeasts Candida albicans serotypes A and B and Candida parapsilosis. Carbohydr. Res. 172, 243-253 (1988).
    • (1988) Carbohydr. Res. , vol.172 , pp. 243-253
    • Kogan, G.1    Pavliak, V.2    Masler, L.3
  • 56
    • 0030014583 scopus 로고    scopus 로고
    • Lymphocytes utilize CD11b/CD18 for adhesion to Candida albicans
    • Forsyth, C. B., Mathews, H. L. Lymphocytes utilize CD11b/CD18 for adhesion to Candida albicans. Cell. Immunol. 170, 91-100 (1996).
    • (1996) Cell. Immunol. , vol.170 , pp. 91-100
    • Forsyth, C.B.1    Mathews, H.L.2
  • 57
    • 18044382736 scopus 로고    scopus 로고
    • Surface hydrophobicity changes of two Candida albicans serotype B mnn4delta mutants
    • Singleton, D. R., Masuoka, J., Hazen, K. C. Surface hydrophobicity changes of two Candida albicans serotype B mnn4delta mutants. Eukaryot. Cell 4, 639-648 (2005).
    • (2005) Eukaryot. Cell , vol.4 , pp. 639-648
    • Singleton, D.R.1    Masuoka, J.2    Hazen, K.C.3
  • 58
    • 69249154681 scopus 로고    scopus 로고
    • The C-type lectin DC-SIGN internalizes soluble antigens and HIV-1 virions via a clathrin-dependent mechanism
    • Cambi, A., Beeren, I., Joosten, B., Fransen, J. A., Figdor, C. G. The C-type lectin DC-SIGN internalizes soluble antigens and HIV-1 virions via a clathrin-dependent mechanism. Eur. J. Immunol. 39, 1923-1928, doi: 10.1002/eji.200939351 (2009).
    • (2009) Eur. J. Immunol. , vol.39 , pp. 1923-1928
    • Cambi, A.1    Beeren, I.2    Joosten, B.3    Fransen, J.A.4    Figdor, C.G.5
  • 59
    • 81055138892 scopus 로고    scopus 로고
    • Interlaboratory round robin on cantilever calibration for AFM force spectroscopy
    • Te Riet, J. et al. Interlaboratory round robin on cantilever calibration for AFM force spectroscopy. Ultramicroscopy 111, 1659-1669, doi:10.1016/j.ultramic.2011.09.012 (2011).
    • (2011) Ultramicroscopy , vol.111 , pp. 1659-1669
    • Te Riet, J.1
  • 60
    • 36449007442 scopus 로고
    • Calibration of atomic-force microscope tips
    • Bechhoefer, J., Hutter, J. L. Calibration of atomic-force microscope tips. Rev. Sci. Instrum. 64, 1868-1873 (1993).
    • (1993) Rev. Sci. Instrum. , vol.64 , pp. 1868-1873
    • Bechhoefer, J.1    Hutter, J.L.2
  • 61
    • 27144462660 scopus 로고    scopus 로고
    • Measuring cell adhesion forces of primary gastrulating cells from zebrafish using atomic force microscopy
    • Puech, P. H. et al. Measuring cell adhesion forces of primary gastrulating cells from zebrafish using atomic force microscopy. J. Cell Sci. 118, 4199-4206 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 4199-4206
    • Puech, P.H.1
  • 62
    • 30744445427 scopus 로고    scopus 로고
    • Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death
    • Stillman, B. N. et al. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death. J. Immunol. 176, 778-789 (2006).
    • (2006) J. Immunol. , vol.176 , pp. 778-789
    • Stillman, B.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.