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Volumn 8, Issue 6, 2004, Pages 617-625

Cell surface biology mediated by low affinity multivalent protein-glycan interactions

Author keywords

[No Author keywords available]

Indexed keywords

ANTITOXIN; BACTERIAL TOXIN; BINDING PROTEIN; CHOLERA TOXIN; CLATHRIN; GALECTIN; GLYCAN DERIVATIVE; LECTIN; LIGAND; PILIN; SHIGA TOXIN; STARFISH INHIBITOR; UNCLASSIFIED DRUG;

EID: 8844261143     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2004.10.004     Document Type: Review
Times cited : (287)

References (67)
  • 1
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharide-mediated cellular interactions
    • C.F. Brewer, M.C. Miceli, and L.G. Baum Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions Curr Opin Struct Biol 12 2002 616 623 This review covers galectin-mediated cross-linking of cell surface glycans, including a description of the two types of proposed lattice structures, and proposed biological significance.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 3
    • 0036815746 scopus 로고    scopus 로고
    • Siglecs: Sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling
    • P.R. Crocker Siglecs: sialic-acid-binding immunoglobulin-like lectins in cell-cell interactions and signalling Curr Opin Struct Biol 12 2002 609 615 A concise comprehensive review summarizing current aspects of siglec biology, particularly those of the immune system.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 609-615
    • Crocker, P.R.1
  • 6
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • A.E. Smith, and A. Helenius How viruses enter animal cells Science 304 2004 237 242
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 7
    • 0028787845 scopus 로고
    • Microbial recognition of target-cell glycoconjugates
    • K.A. Karlsson Microbial recognition of target-cell glycoconjugates Curr Opin Struct Biol 5 1995 622 635
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 622-635
    • Karlsson, K.A.1
  • 8
    • 0037333208 scopus 로고    scopus 로고
    • "Multivalent" saccharides: Development of new approaches for inhibiting the effects of glycosphingolipid-binding pathogens
    • C.L. Schengrund "Multivalent" saccharides: development of new approaches for inhibiting the effects of glycosphingolipid-binding pathogens Biochem Pharmacol 65 2003 699 707
    • (2003) Biochem Pharmacol , vol.65 , pp. 699-707
    • Schengrund, C.L.1
  • 9
    • 0346981999 scopus 로고    scopus 로고
    • Influencing receptor-ligand binding mechanisms with multivalent ligand architecture
    • J.E. Gestwicki, C.W. Cairo, L.E. Strong, K.A. Oetjen, and L.L. Kiessling Influencing receptor-ligand binding mechanisms with multivalent ligand architecture J Am Chem Soc 124 2002 14922 14933 These authors compare the effects of multivalency and spacing by synthesizing a series of 28 multivalent glycans including glyco-clusters, glyco-polymers, and glyco-dendrimers and analyzing their binding to the plant lectin Conconavalin A. Results are put in the context of potential uses of these constructs.
    • (2002) J Am Chem Soc , vol.124 , pp. 14922-14933
    • Gestwicki, J.E.1    Cairo, C.W.2    Strong, L.E.3    Oetjen, K.A.4    Kiessling, L.L.5
  • 10
    • 0028028246 scopus 로고
    • Polyacrylamides bearing pendant alpha-sialoside groups strongly inhibit agglutination of erythrocytes by influenza a virus: Multivalency and steric stabilization of particulate biological systems
    • W.J. Lees, A. Spaltenstein, J.E. Kingery-Wood, and G.M. Whitesides Polyacrylamides bearing pendant alpha-sialoside groups strongly inhibit agglutination of erythrocytes by influenza A virus: multivalency and steric stabilization of particulate biological systems J Med Chem 37 1994 3419 3433
    • (1994) J Med Chem , vol.37 , pp. 3419-3433
    • Lees, W.J.1    Spaltenstein, A.2    Kingery-Wood, J.E.3    Whitesides, G.M.4
  • 12
    • 0029731789 scopus 로고    scopus 로고
    • The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro
    • M.D. Bider, J.M. Wahlberg, R.A. Kammerer, and M. Spiess The oligomerization domain of the asialoglycoprotein receptor preferentially forms 2:2 heterotetramers in vitro J Biol Chem 271 1996 31996 32001
    • (1996) J Biol Chem , vol.271 , pp. 31996-32001
    • Bider, M.D.1    Wahlberg, J.M.2    Kammerer, R.A.3    Spiess, M.4
  • 13
    • 0038495788 scopus 로고    scopus 로고
    • Molecular characterization of the rat Kupffer cell glycoprotein receptor
    • A.J. Fadden, O.J. Holt, and K. Drickamer Molecular characterization of the rat Kupffer cell glycoprotein receptor Glycobiology 13 2003 529 537
    • (2003) Glycobiology , vol.13 , pp. 529-537
    • Fadden, A.J.1    Holt, O.J.2    Drickamer, K.3
  • 14
    • 0038394449 scopus 로고    scopus 로고
    • Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells
    • N.S. Stambach, and M.E. Taylor Characterization of carbohydrate recognition by langerin, a C-type lectin of Langerhans cells Glycobiology 13 2003 401 410
    • (2003) Glycobiology , vol.13 , pp. 401-410
    • Stambach, N.S.1    Taylor, M.E.2
  • 17
    • 0021099058 scopus 로고
    • Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin. Dependence on fine structural features
    • Y.C. Lee, R.R. Townsend, M.R. Hardy, J. Lonngren, J. Arnarp, M. Haraldsson, and H. Lonn Binding of synthetic oligosaccharides to the hepatic Gal/GalNAc lectin. Dependence on fine structural features J Biol Chem 258 1983 199 202
    • (1983) J Biol Chem , vol.258 , pp. 199-202
    • Lee, Y.C.1    Townsend, R.R.2    Hardy, M.R.3    Lonngren, J.4    Arnarp, J.5    Haraldsson, M.6    Lonn, H.7
  • 18
    • 0021772463 scopus 로고
    • New synthetic cluster ligands for galactose/N-acetylgalactosamine- specific lectin of mammalian liver
    • R.T. Lee, P. Lin, and Y.C. Lee New synthetic cluster ligands for galactose/N-acetylgalactosamine-specific lectin of mammalian liver Biochemistry 23 1984 4255 4261
    • (1984) Biochemistry , vol.23 , pp. 4255-4261
    • Lee, R.T.1    Lin, P.2    Lee, Y.C.3
  • 19
    • 0142011585 scopus 로고    scopus 로고
    • Application of a multivalent glycoprobe: Characterization of sugar-binding specificity of siglec family proteins
    • T. Yamaji, K. Nakamura, S. Amari, A. Suzuki, and Y. Hashimoto Application of a multivalent glycoprobe: characterization of sugar-binding specificity of siglec family proteins Methods Enzymol 363 2003 104 113
    • (2003) Methods Enzymol , vol.363 , pp. 104-113
    • Yamaji, T.1    Nakamura, K.2    Amari, S.3    Suzuki, A.4    Hashimoto, Y.5
  • 21
    • 0031830601 scopus 로고    scopus 로고
    • Polyacrylamide-based glycoconjugates as tools in glycobiology
    • N.V. Bovin Polyacrylamide-based glycoconjugates as tools in glycobiology Glycoconj J 15 1998 431 446
    • (1998) Glycoconj J , vol.15 , pp. 431-446
    • Bovin, N.V.1
  • 22
    • 0242712912 scopus 로고    scopus 로고
    • Dynamic multivalent lactosides displayed on cyclodextrin beads dangling from polymer strings
    • A. Nelson, and J.F. Stoddart Dynamic multivalent lactosides displayed on cyclodextrin beads dangling from polymer strings Org Lett 5 2003 3783 3786
    • (2003) Org Lett , vol.5 , pp. 3783-3786
    • Nelson, A.1    Stoddart, J.F.2
  • 23
    • 0344011988 scopus 로고    scopus 로고
    • Mannosyl glycodendritic structure inhibits DC-SIGN-mediated Ebola virus infection in cis and in trans
    • F. Lasala, E. Arce, J.R. Otero, J. Rojo, and R. Delgado Mannosyl glycodendritic structure inhibits DC-SIGN-mediated Ebola virus infection in cis and in trans Antimicrob Agents Chemother 47 2003 3970 3972
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3970-3972
    • Lasala, F.1    Arce, E.2    Otero, J.R.3    Rojo, J.4    Delgado, R.5
  • 24
    • 0347694971 scopus 로고    scopus 로고
    • On the nature of the multivalency effect: A thermodynamic model
    • P.I. Kitov, and D.R. Bundle On the nature of the multivalency effect: a thermodynamic model J Am Chem Soc 125 2003 16271 16284
    • (2003) J Am Chem Soc , vol.125 , pp. 16271-16284
    • Kitov, P.I.1    Bundle, D.R.2
  • 25
    • 0037442497 scopus 로고    scopus 로고
    • Assessment in mice of the therapeutic potential of tailored, multivalent Shiga toxin carbohydrate ligands
    • ••] describe the rational design and synthesis of multivalent inhibitors STARFISH, DAISY and SUPER TWIG, which bind with strong affinity to shiga toxin (Stx1 and Stx2). The dramatic efficacy of these inhibitors is illustrated in vivo using both purified Stx and enterohemorrhagic E. coli serotypes.
    • (2003) J Infect Dis , vol.187 , pp. 640-649
    • Mulvey, G.L.1    Marcato, P.2    Kitov, P.I.3    Sadowska, J.4    Bundle, D.R.5    Armstrong, G.D.6
  • 27
    • 0037032293 scopus 로고    scopus 로고
    • Solution and crystallographic studies of branched multivalent ligands that inhibit the receptor-binding of cholera toxin
    • Z. Zhang, E.A. Merritt, M. Ahn, C. Roach, Z. Hou, C.L. Verlinde, W.G. Hol, and E. Fan Solution and crystallographic studies of branched multivalent ligands that inhibit the receptor-binding of cholera toxin J Am Chem Soc 124 2002 12991 12998
    • (2002) J Am Chem Soc , vol.124 , pp. 12991-12998
    • Zhang, Z.1    Merritt, E.A.2    Ahn, M.3    Roach, C.4    Hou, Z.5    Verlinde, C.L.6    Hol, W.G.7    Fan, E.8
  • 28
    • 0035054508 scopus 로고    scopus 로고
    • Glycans as legislators of host-microbial interactions: Spanning the spectrum from symbiosis to pathogenicity
    • L.V. Hooper, and J.I. Gordon Glycans as legislators of host-microbial interactions: spanning the spectrum from symbiosis to pathogenicity Glycobiology 11 2001 1R 10R
    • (2001) Glycobiology , vol.11
    • Hooper, L.V.1    Gordon, J.I.2
  • 29
    • 0032239313 scopus 로고    scopus 로고
    • Oligosaccharide receptors for bacteria: A view to a kill
    • C.A. Lingwood Oligosaccharide receptors for bacteria: a view to a kill Curr Opin Chem Biol 2 1998 695 700
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 695-700
    • Lingwood, C.A.1
  • 30
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • J.J. Skehel, and D.C. Wiley Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin Annu Rev Biochem 69 2000 531 569
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 31
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual influenza viruses during viral entry
    • M.J. Rust, M. Lakadamyali, F. Zhang, and X. Zhuang Assembly of endocytic machinery around individual influenza viruses during viral entry Nat Struct Mol Biol 11 2004 567 573 This study describes the timing and use of clathrin-coated pits for influenza virus entry using real-time fluorescence microscopy. Significantly, the authors suggest that the highly multivalent interaction of the viral hemagglutanins with the cell surface glycans induce a local curvature in the membrane that then induces clathrin-coated pit formation.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 32
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • R.J. Connor, Y. Kawaoka, R.G. Webster, and J.C. Paulson Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates Virology 205 1994 17 23
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 33
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • •] describe the crystal structure of the pandemic 1918 influenza virus hemagglutinin. Both address the structural basis for the sialic acid specificity in the hemagglutinin and adaptation of the avian virus to humans.
    • (2004) Science , vol.303 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 35
    • 0034721650 scopus 로고    scopus 로고
    • Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1
    • W.S. Somers, J. Tang, G.D. Shaw, and R.T. Camphausen Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P- and E-selectin bound to SLe(X) and PSGL-1 Cell 103 2000 467 479
    • (2000) Cell , vol.103 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 36
    • 0035943656 scopus 로고    scopus 로고
    • Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1
    • M.K. Wild, M.C. Huang, U. Schulze-Horsel, P.A. van der Merwe, and D. Vestweber Affinity, kinetics, and thermodynamics of E-selectin binding to E-selectin ligand-1 J Biol Chem 276 2001 31602 31612
    • (2001) J Biol Chem , vol.276 , pp. 31602-31612
    • Wild, M.K.1    Huang, M.C.2    Schulze-Horsel, U.3    Van Der Merwe, P.A.4    Vestweber, D.5
  • 37
    • 0030899123 scopus 로고    scopus 로고
    • Conformation of sLex tetrasaccharide, free in solution and bound to E-, P-, and L-selectin
    • L. Poppe, G.S. Brown, J.S. Philo, P.V. Nikrad, and B.H. Shah Conformation of sLex tetrasaccharide, free in solution and bound to E-, P-, and L-selectin J Am Chem Soc 119 1997 1727 1736
    • (1997) J Am Chem Soc , vol.119 , pp. 1727-1736
    • Poppe, L.1    Brown, G.S.2    Philo, J.S.3    Nikrad, P.V.4    Shah, B.H.5
  • 38
    • 2342525764 scopus 로고    scopus 로고
    • L-selectin-mediated leukocyte tethering in shear flow is controlled by multiple contacts and cytoskeletal anchorage facilitating fast rebinding events
    • U.S. Schwarz, and R. Alon L-selectin-mediated leukocyte tethering in shear flow is controlled by multiple contacts and cytoskeletal anchorage facilitating fast rebinding events Proc Natl Acad Sci USA 101 2004 6940 6945 This paper mathematically addresses and models the observed increase in selectin-dependent adherence with low shear force as compared with static adhesion. Current contrasting theories are compared and discussed.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6940-6945
    • Schwarz, U.S.1    Alon, R.2
  • 39
    • 0242425839 scopus 로고    scopus 로고
    • Avidity enhancement of L-selectin bonds by flow: Shear-promoted rotation of leukocytes turn labile bonds into functional tethers
    • O. Dwir, A. Solomon, S. Mangan, G.S. Kansas, U.S. Schwarz, and R. Alon Avidity enhancement of L-selectin bonds by flow: shear-promoted rotation of leukocytes turn labile bonds into functional tethers J Cell Biol 163 2003 649 659 A thorough description on the role of the cytoplasmic tail in stabilizing L-selectin-dependent rolling, especially as it relates to multivalency. Data are put in context of models describing the role of microvilli in selectin localization and rolling.
    • (2003) J Cell Biol , vol.163 , pp. 649-659
    • Dwir, O.1    Solomon, A.2    Mangan, S.3    Kansas, G.S.4    Schwarz, U.S.5    Alon, R.6
  • 40
    • 0033521607 scopus 로고    scopus 로고
    • L-selectin-mediated leukocyte adhesion in vivo: Microvillous distribution determines tethering efficiency, but not rolling velocity
    • J.V. Stein, G. Cheng, B.M. Stockton, B.P. Fors, E.C. Butcher, and U.H. von Andrian L-selectin-mediated leukocyte adhesion in vivo: microvillous distribution determines tethering efficiency, but not rolling velocity J Exp Med 189 1999 37 50
    • (1999) J Exp Med , vol.189 , pp. 37-50
    • Stein, J.V.1    Cheng, G.2    Stockton, B.M.3    Fors, B.P.4    Butcher, E.C.5    Von Andrian, U.H.6
  • 41
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: Lectins that initiate cell adhesion under flow
    • R.P. McEver Selectins: lectins that initiate cell adhesion under flow Curr Opin Cell Biol 14 2002 581 586
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 42
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • B.T. Marshall, M. Long, J.W. Piper, T. Yago, R.P. McEver, and C. Zhu Direct observation of catch bonds involving cell-adhesion molecules Nature 423 2003 190 193 Using atomic force microscopy and flow chamber rolling this group describes a novel mechanism of 'catch bonds' for selectin mediated adherence at low shear force. Included is a discussion of the conversion between 'catch' and 'slip' bond types and their relevance to rolling.
    • (2003) Nature , vol.423 , pp. 190-193
    • Marshall, B.T.1    Long, M.2    Piper, J.W.3    Yago, T.4    McEver, R.P.5    Zhu, C.6
  • 44
    • 0346732920 scopus 로고    scopus 로고
    • Signal-dependent distribution of cell surface P-selectin in clathrin-coated pits affects leukocyte rolling under flow
    • H. Setiadi, and R.P. McEver Signal-dependent distribution of cell surface P-selectin in clathrin-coated pits affects leukocyte rolling under flow J Cell Biol 163 2003 1385 1395
    • (2003) J Cell Biol , vol.163 , pp. 1385-1395
    • Setiadi, H.1    McEver, R.P.2
  • 45
    • 0036775462 scopus 로고    scopus 로고
    • Immune escape through C-type lectins on dendritic cells
    • A. Engering, T.B. Geijtenbeek, and Y. van Kooyk Immune escape through C-type lectins on dendritic cells Trends Immunol 23 2002 480 485 An excellent concise review that covers all known dendritic cell C-type lectins and their roles in pathogen recognition.
    • (2002) Trends Immunol , vol.23 , pp. 480-485
    • Engering, A.1    Geijtenbeek, T.B.2    Van Kooyk, Y.3
  • 47
    • 0037184995 scopus 로고    scopus 로고
    • Pattern recognition receptors: Doubling up for the innate immune response
    • S. Gordon Pattern recognition receptors: doubling up for the innate immune response Cell 111 2002 927 930
    • (2002) Cell , vol.111 , pp. 927-930
    • Gordon, S.1
  • 48
    • 3042637779 scopus 로고    scopus 로고
    • Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR
    • Y. Guo, H. Feinberg, E. Conroy, D.A. Mitchell, R. Alvarez, O. Blixt, M.E. Taylor, W.I. Weis, and K. Drickamer Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR Nat Struct Mol Biol 11 2004 591 598 This study describes the use of multivalent glycan arrays to differentiate the carbohydrate specificity of DC-SIGN and DC-SIGNR to 135 distinct glycan structures. The authors suggest the difference in binding specificities may relate to adhesive or endocytic properties of the lectins.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 591-598
    • Guo, Y.1    Feinberg, H.2    Conroy, E.3    Mitchell, D.A.4    Alvarez, R.5    Blixt, O.6    Taylor, M.E.7    Weis, W.I.8    Drickamer, K.9
  • 49
    • 0037592165 scopus 로고    scopus 로고
    • Oligolysine-based oligosaccharide clusters: Selective recognition and endocytosis by the mannose receptor and dendritic cell-specific intercellular adhesion molecule 3 (ICAM-3)-grabbing nonintegrin
    • N. Frison, M.E. Taylor, E. Soilleux, M.T. Bousser, R. Mayer, M. Monsigny, K. Drickamer, and A.C. Roche Oligolysine-based oligosaccharide clusters: selective recognition and endocytosis by the mannose receptor and dendritic cell-specific intercellular adhesion molecule 3 (ICAM-3)-grabbing nonintegrin J Biol Chem 278 2003 23922 23929
    • (2003) J Biol Chem , vol.278 , pp. 23922-23929
    • Frison, N.1    Taylor, M.E.2    Soilleux, E.3    Bousser, M.T.4    Mayer, R.5    Monsigny, M.6    Drickamer, K.7    Roche, A.C.8
  • 50
    • 4043082787 scopus 로고    scopus 로고
    • Molecular basis of the differences in binding properties of the highly related C-type lectins DC-SIGN and L-SIGN to Lewis X trisaccharide and schistosoma mansoni egg antigens
    • E. Van Liempt, A. Imberty, C.M. Bank, S.J. Van Vliet, Y. Van Kooyk, T.B. Geijtenbeek, and I. Van Die Molecular basis of the differences in binding properties of the highly related C-type lectins DC-SIGN and L-SIGN to Lewis X trisaccharide and schistosoma mansoni egg antigens J Biol Chem 279 2004 33161 33167
    • (2004) J Biol Chem , vol.279 , pp. 33161-33167
    • Van Liempt, E.1    Imberty, A.2    Bank, C.M.3    Van Vliet, S.J.4    Van Kooyk, Y.5    Geijtenbeek, T.B.6    Van Die, I.7
  • 51
    • 0038407687 scopus 로고    scopus 로고
    • DC-SIGN: A novel HIV receptor on DCs that mediates HIV-1 transmission
    • T.B. Geijtenbeek, and Y. van Kooyk DC-SIGN: a novel HIV receptor on DCs that mediates HIV-1 transmission Curr Top Microbiol Immunol 276 2003 31 54
    • (2003) Curr Top Microbiol Immunol , vol.276 , pp. 31-54
    • Geijtenbeek, T.B.1    Van Kooyk, Y.2
  • 53
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • N. Ahmad, H.J. Gabius, S. Andre, H. Kaltner, S. Sabesan, R. Roy, B. Liu, F. Macaluso, and C.F. Brewer Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes J Biol Chem 279 2004 10841 10847
    • (2004) J Biol Chem , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.J.2    Andre, S.3    Kaltner, H.4    Sabesan, S.5    Roy, R.6    Liu, B.7    MacAluso, F.8    Brewer, C.F.9
  • 54
    • 4444329794 scopus 로고    scopus 로고
    • Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3
    • N. Ahmad, H.J. Gabius, S. Sabesan, S. Oscarson, and C.F. Brewer Thermodynamic binding studies of bivalent oligosaccharides to galectin-1, galectin-3, and the carbohydrate recognition domain of galectin-3 Glycobiology 2004
    • (2004) Glycobiology
    • Ahmad, N.1    Gabius, H.J.2    Sabesan, S.3    Oscarson, S.4    Brewer, C.F.5
  • 55
    • 0037470066 scopus 로고    scopus 로고
    • The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death
    • M. Amano, M. Galvan, J. He, and L.G. Baum The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death J Biol Chem 278 2003 7469 7475
    • (2003) J Biol Chem , vol.278 , pp. 7469-7475
    • Amano, M.1    Galvan, M.2    He, J.3    Baum, L.G.4
  • 57
    • 0346034779 scopus 로고    scopus 로고
    • The B cell coreceptor CD22 associates with AP50, a clathrin-coated pit adapter protein, via tyrosine-dependent interaction
    • B. John, B.R. Herrin, C. Raman, Y.N. Wang, K.R. Bobbitt, B.A. Brody, and L.B. Justement The B cell coreceptor CD22 associates with AP50, a clathrin-coated pit adapter protein, via tyrosine-dependent interaction J Immunol 170 2003 3534 3543
    • (2003) J Immunol , vol.170 , pp. 3534-3543
    • John, B.1    Herrin, B.R.2    Raman, C.3    Wang, Y.N.4    Bobbitt, K.R.5    Brody, B.A.6    Justement, L.B.7
  • 58
    • 0037029637 scopus 로고    scopus 로고
    • Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling
    • L. Jin, P.A. McLean, B.G. Neel, and H.H. Wortis Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling J Exp Med 195 2002 1199 1205
    • (2002) J Exp Med , vol.195 , pp. 1199-1205
    • Jin, L.1    McLean, P.A.2    Neel, B.G.3    Wortis, H.H.4
  • 59
    • 0037029667 scopus 로고    scopus 로고
    • The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound
    • S. Kelm, J. Gerlach, R. Brossmer, C.P. Danzer, and L. Nitschke The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound J Exp Med 195 2002 1207 1213
    • (2002) J Exp Med , vol.195 , pp. 1207-1213
    • Kelm, S.1    Gerlach, J.2    Brossmer, R.3    Danzer, C.P.4    Nitschke, L.5
  • 61
    • 0036259295 scopus 로고    scopus 로고
    • Lymph node macrophages, but not spleen macrophages, express high levels of unmasked sialoadhesin: Implication for the adhesive properties of macrophages in vivo
    • K. Nakamura, T. Yamaji, P.R. Crocker, A. Suzuki, and Y. Hashimoto Lymph node macrophages, but not spleen macrophages, express high levels of unmasked sialoadhesin: implication for the adhesive properties of macrophages in vivo Glycobiology 12 2002 209 216
    • (2002) Glycobiology , vol.12 , pp. 209-216
    • Nakamura, K.1    Yamaji, T.2    Crocker, P.R.3    Suzuki, A.4    Hashimoto, Y.5
  • 62
    • 0032560557 scopus 로고    scopus 로고
    • Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes
    • N. Razi, and A. Varki Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes Proc Natl Acad Sci USA 95 1998 7469 7474
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7469-7474
    • Razi, N.1    Varki, A.2
  • 63
    • 0037744803 scopus 로고    scopus 로고
    • Ganglioside GD3 expression on target cells can modulate NK cell cytotoxicity via siglec-7-dependent and -independent mechanisms
    • G. Nicoll, T. Avril, K. Lock, K. Furukawa, N. Bovin, and P.R. Crocker Ganglioside GD3 expression on target cells can modulate NK cell cytotoxicity via siglec-7-dependent and -independent mechanisms Eur J Immunol 33 2003 1642 1648
    • (2003) Eur J Immunol , vol.33 , pp. 1642-1648
    • Nicoll, G.1    Avril, T.2    Lock, K.3    Furukawa, K.4    Bovin, N.5    Crocker, P.R.6
  • 64
    • 1942437467 scopus 로고    scopus 로고
    • Masking of CD22 by cis ligands does not prevent redistribution of CD22 to sites of cell contact
    • ••] demonstrate that despite being masked by cis ligands, CD22 can redistribute to sites of cell contact such as between the B cell and a cancer cell, via ligands presented in trans, resulting in suppression of B cell activation in response to antigens presented on the apposing cell.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 6104-6109
    • Collins, B.E.1    Blixt, O.2    Desieno, A.R.3    Bovin, N.4    Marth, J.D.5    Paulson, J.C.6
  • 66
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c: Can low affinity systems be studied by isothermal titration calorimetry?
    • W.B. Turnbull, and A.H. Daranas On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J Am Chem Soc 125 2003 14859 14866
    • (2003) J Am Chem Soc , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 67
    • 0036312180 scopus 로고    scopus 로고
    • Comparison of CD22 binding to native CD45 and synthetic oligosaccharide
    • T.R. Bakker, C. Piperi, E.A. Davies, and P.A. Merwe Comparison of CD22 binding to native CD45 and synthetic oligosaccharide Eur J Immunol 32 2002 1924 1932
    • (2002) Eur J Immunol , vol.32 , pp. 1924-1932
    • Bakker, T.R.1    Piperi, C.2    Davies, E.A.3    Merwe, P.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.