메뉴 건너뛰기




Volumn 2, Issue 5, 2006, Pages 238-248

Sweet spots in functional glycomics

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCAN; GLYCOPROTEIN;

EID: 33646457967     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio785     Document Type: Review
Times cited : (343)

References (137)
  • 1
    • 33646463732 scopus 로고    scopus 로고
    • eds. Taylor, M.E. & Drickamer, K. Oxford University Press, New York
    • Taylor, M.E. & Drickamer, K. in Introduction to Glycobiology (eds. Taylor, M.E. & Drickamer, K.) 1-224 (Oxford University Press, New York, 2003).
    • (2003) Introduction to Glycobiology , pp. 1-224
    • Taylor, M.E.1    Drickamer, K.2
  • 2
    • 0002495856 scopus 로고    scopus 로고
    • eds. Varki, A. et al. Cold Springs Harbor Laboratory Press, Plainview, NY, USA
    • Varki, A. et al. in Essentials of Glycobiology (eds. Varki, A. et al.) 1-653 (Cold Springs Harbor Laboratory Press, Plainview, NY, USA, 1999).
    • (1999) Essentials of Glycobiology , pp. 1-653
    • Varki, A.1
  • 3
    • 33646460726 scopus 로고    scopus 로고
    • eds. Sharon, N. & Lis, H. Kluwer Academic Publishers, Dordrecht, Boston
    • Sharon, N. & Lis, H. in Lectins (eds. Sharon, N. & Lis, H.) 470 (Kluwer Academic Publishers, Dordrecht, Boston, 2004).
    • (2004) Lectins , pp. 470
    • Sharon, N.1    Lis, H.2
  • 4
    • 0142025337 scopus 로고    scopus 로고
    • Bacterium-host protein-carbohydrate interactions
    • Ilver, D. et al. Bacterium-host protein-carbohydrate interactions. Methods Enzymol. 363, 134-157 (2003).
    • (2003) Methods Enzymol. , vol.363 , pp. 134-157
    • Ilver, D.1
  • 5
    • 10944268260 scopus 로고    scopus 로고
    • Sugar epitopes as potential universal disease transmission blocking targets
    • Dinglasan, R.R., Valenzuela, J.G. & Azad, A.F. Sugar epitopes as potential universal disease transmission blocking targets. Insect Biochem. Mol. Biol. 35, 1-10 (2005).
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 1-10
    • Dinglasan, R.R.1    Valenzuela, J.G.2    Azad, A.F.3
  • 6
    • 0032763888 scopus 로고    scopus 로고
    • Evolutionary considerations in relating oligosaccharide diversity to biological function
    • Gagneux, P. & Varki, A. Evolutionary considerations in relating oligosaccharide diversity to biological function. Glycobiology 9, 747-755 (1999).
    • (1999) Glycobiology , vol.9 , pp. 747-755
    • Gagneux, P.1    Varki, A.2
  • 7
    • 21644463169 scopus 로고    scopus 로고
    • Siglecs in innate immunity
    • Crocker, P.R. Siglecs in innate immunity. Curr. Opin. Pharmacol. 5, 431-437 (2005).
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 431-437
    • Crocker, P.R.1
  • 8
    • 29444437433 scopus 로고    scopus 로고
    • Siglecs - The major subfamily of I-type lectins
    • Varki, A. & Angata, T. Siglecs - the major subfamily of I-type lectins. Glycobiology 16, 1R-27R(2006).
    • (2006) Glycobiology , vol.16
    • Varki, A.1    Angata, T.2
  • 9
    • 3042643773 scopus 로고    scopus 로고
    • Phylogenetic analysis of the vertebrate galectin family
    • Houzelstein, D. et al. Phylogenetic analysis of the vertebrate galectin family. Mol. Biol. Evol. 21, 1177-1187 (2004).
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1177-1187
    • Houzelstein, D.1
  • 10
    • 11144241063 scopus 로고    scopus 로고
    • Galectins as modulators of tumour progression
    • Liu, F.T. & Rabinovich, G.A. Galectins as modulators of tumour progression. Nat. Rev. Cancer 5, 29-41 (2005).
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 29-41
    • Liu, F.T.1    Rabinovich, G.A.2
  • 11
    • 20444419772 scopus 로고    scopus 로고
    • Galectins as immunoregulators during infectious processes: From microbial invasion to the resolution of the disease
    • Rabinovich, G.A. & Gruppi, A. Galectins as immunoregulators during infectious processes: from microbial invasion to the resolution of the disease. Parasite Immunol. 27, 103-114 (2005).
    • (2005) Parasite Immunol. , vol.27 , pp. 103-114
    • Rabinovich, G.A.1    Gruppi, A.2
  • 12
    • 0000545033 scopus 로고
    • ed. Conn, P.M. Academic Press Inc., New York
    • Paulson, J.C. in The Receptors (ed. Conn, P.M.) 131-219 (Academic Press Inc., New York, 1985).
    • (1985) The Receptors , pp. 131-219
    • Paulson, J.C.1
  • 13
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith, A.E. & Helenius, A. How viruses enter animal cells. Science 304, 237-242 (2004).
    • (2004) Science , vol.304 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 14
    • 0036785609 scopus 로고    scopus 로고
    • Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core
    • Dormitzer, P.R. et al. Specificity and affinity of sialic acid binding by the rhesus rotavirus VP8* core. J. Virol. 76, 10512-10517 (2002).
    • (2002) J. Virol. , vol.76 , pp. 10512-10517
    • Dormitzer, P.R.1
  • 15
    • 0030839256 scopus 로고    scopus 로고
    • High-resolution structure of a polyomavirus VP1-oligosaccharide complex: Implications for assembly and receptor binding
    • Stehle, T. & Harrison, S.C. High-resolution structure of a polyomavirus VP1-oligosaccharide complex: implications for assembly and receptor binding. EMBO J. 16, 5139-5148 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5139-5148
    • Stehle, T.1    Harrison, S.C.2
  • 16
    • 31844438840 scopus 로고    scopus 로고
    • Uropathogenic Escherichia coli as a model of host-parasite interaction
    • Svanborg, C. et al. Uropathogenic Escherichia coli as a model of host-parasite interaction. Curr. Opin. Microbiol. 9, 33-39 (2006).
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 33-39
    • Svanborg, C.1
  • 17
    • 26444542946 scopus 로고    scopus 로고
    • Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays
    • Walz, A., Odenbreit, S., Mahdavi, J., Boren, T. & Ruhl, S. Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays. Glycobiology 15, 700-708 (2005).
    • (2005) Glycobiology , vol.15 , pp. 700-708
    • Walz, A.1    Odenbreit, S.2    Mahdavi, J.3    Boren, T.4    Ruhl, S.5
  • 19
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell, G. & Harford, J. Carbohydrate-specific receptors of the liver. Annu. Rev. Biochem. 51, 531-554 (1982).
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 20
    • 0036157926 scopus 로고    scopus 로고
    • Regulation of lutropin circulatory half-life by the mannose/N- acetylgalactosamine-4-SO4 receptor is critical for implantation in vivo
    • Mi, Y., Shapiro, S.D. & Baenziger, J.U. Regulation of lutropin circulatory half-life by the mannose/N-acetylgalactosamine-4-SO4 receptor is critical for implantation in vivo. J. Clin. Invest. 109, 269-276 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 269-276
    • Mi, Y.1    Shapiro, S.D.2    Baenziger, J.U.3
  • 22
    • 1642463804 scopus 로고    scopus 로고
    • The lectin-complement pathway - Its role in innate immunity and evolution
    • Fujita, T., Matsushita, M. & Endo, Y. The lectin-complement pathway - its role in innate immunity and evolution. Immunol. Rev. 198, 185-202 (2004).
    • (2004) Immunol. Rev. , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 24
    • 33644828798 scopus 로고    scopus 로고
    • Surfactant proteins SP-A and SP-D: Structure, function and receptors
    • Kishore, U. et al. Surfactant proteins SP-A and SP-D: structure, function and receptors. Mol. Immunol. 43, 1293-1315(2005).
    • (2005) Mol. Immunol. , vol.43 , pp. 1293-1315
    • Kishore, U.1
  • 25
    • 5144228482 scopus 로고    scopus 로고
    • Divergent roles for C-type lectins expressed by cells of the innate immune system
    • McGreal, E.P., Martinez-Pomares, L. & Gordon, S. Divergent roles for C-type lectins expressed by cells of the innate immune system. Mol. Immunol. 41, 1109-1121 (2004).
    • (2004) Mol. Immunol. , vol.41 , pp. 1109-1121
    • McGreal, E.P.1    Martinez-Pomares, L.2    Gordon, S.3
  • 26
    • 27744452942 scopus 로고    scopus 로고
    • The role of the mannose-binding lectin in innate immunity
    • Takahashi, K. & Ezekowitz, R.A. The role of the mannose-binding lectin in innate immunity. Clin. Infect. Dis. 41(Suppl.), S440-S444 (2005).
    • (2005) Clin. Infect. Dis. , vol.41 , Issue.SUPPL.
    • Takahashi, K.1    Ezekowitz, R.A.2
  • 27
    • 33144469842 scopus 로고    scopus 로고
    • Glycans modulate immune responses in helminth infections and allergy
    • Die, I. & Cummings, R.D. Glycans modulate immune responses in helminth infections and allergy. Chem. Immunol. Allergy 90, 91-112 (2006).
    • (2006) Chem. Immunol. Allergy , vol.90 , pp. 91-112
    • Die, I.1    Cummings, R.D.2
  • 28
    • 33244497571 scopus 로고    scopus 로고
    • Dectin-1: A signalling non-TLR pattern-recognition receptor
    • Brown, G.D. Dectin-1: a signalling non-TLR pattern-recognition receptor. Nat. Rev. Immunol. 6, 33-43 (2006).
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 33-43
    • Brown, G.D.1
  • 29
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharide-mediated cellular interactions
    • Brewer, C.F., Miceli, M.C. & Baum, L.G. Clusters, bundles, arrays and lattices: novel mechanisms for lectin-saccharide-mediated cellular interactions. Curr. Opin. Struct. Biol. 12, 616-623 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 30
  • 31
    • 12744279203 scopus 로고    scopus 로고
    • The mannose receptor: Linking homeostasis and immunity through sugar recognition
    • Taylor, P.R., Gordon, S. & Martinez-Pomares, L. The mannose receptor: linking homeostasis and immunity through sugar recognition. Trends Immunol. 26, 104-110 (2005).
    • (2005) Trends Immunol. , vol.26 , pp. 104-110
    • Taylor, P.R.1    Gordon, S.2    Martinez-Pomares, L.3
  • 32
    • 31344445556 scopus 로고    scopus 로고
    • Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling
    • Collins, B.E., Smith, B.A., Bengtson, P. & Paulson, J.C. Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling. Nat. Immunol. 7, 199-206 (2006).
    • (2006) Nat. Immunol. , vol.7 , pp. 199-206
    • Collins, B.E.1    Smith, B.A.2    Bengtson, P.3    Paulson, J.C.4
  • 33
    • 26644450721 scopus 로고    scopus 로고
    • CD22: A multifunctional receptor that regulates B lymphocyte survival and signal transduction
    • Tedder, T.F., Poe, J.C. & Haas, K.M. CD22: a multifunctional receptor that regulates B lymphocyte survival and signal transduction. Adv. Immunol. 88, 1-50 (2005).
    • (2005) Adv. Immunol. , vol.88 , pp. 1-50
    • Tedder, T.F.1    Poe, J.C.2    Haas, K.M.3
  • 34
    • 23844545174 scopus 로고    scopus 로고
    • Galectin-9 induces maturation of human monocyte-derived dendritic cells
    • Dai, S.Y. et al. Galectin-9 induces maturation of human monocyte-derived dendritic cells. J. Immunol. 175, 2974-2981 (2005).
    • (2005) J. Immunol. , vol.175 , pp. 2974-2981
    • Dai, S.Y.1
  • 35
    • 21044458257 scopus 로고    scopus 로고
    • Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells
    • Delacour, D. et al. Galectin-4 and sulfatides in apical membrane trafficking in enterocyte-like cells. J. Cell Biol. 169, 491-501 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 491-501
    • Delacour, D.1
  • 36
    • 0040620527 scopus 로고    scopus 로고
    • Glycosyltransferases and glycan structures contributing to the adhesive activities of L-, E- and P-selectin counter-receptors
    • Lowe, J.B. Glycosyltransferases and glycan structures contributing to the adhesive activities of L-, E- and P-selectin counter-receptors. Biochem. Soc. Symp. 69, 33-45 (2002).
    • (2002) Biochem. Soc. Symp. , vol.69 , pp. 33-45
    • Lowe, J.B.1
  • 37
    • 24944451114 scopus 로고    scopus 로고
    • Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses
    • Wang, L., Fuster, M., Sriramarao, P. & Esko, J.D. Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses. Nat. Immunol. 6, 902-910 (2005).
    • (2005) Nat. Immunol. , vol.6 , pp. 902-910
    • Wang, L.1    Fuster, M.2    Sriramarao, P.3    Esko, J.D.4
  • 38
    • 2942737261 scopus 로고    scopus 로고
    • Trafficking of natural killer cells
    • Morris, M.A. & Ley, K. Trafficking of natural killer cells. Curr. Mol. Med. 4, 431-438 (2004).
    • (2004) Curr. Mol. Med. , vol.4 , pp. 431-438
    • Morris, M.A.1    Ley, K.2
  • 41
    • 12844262132 scopus 로고    scopus 로고
    • The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor selective for myelin-associated glycoprotein
    • Venkatesh, K. et al. The Nogo-66 receptor homolog NgR2 is a sialic acid-dependent receptor selective for myelin-associated glycoprotein. J. Neurosci. 25, 808-822 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 808-822
    • Venkatesh, K.1
  • 43
    • 0036110074 scopus 로고    scopus 로고
    • Contribution of selectin ligands to eosinophil recruitment into the skin of patients with atopic dermatitis
    • Satoh, T., Kaneko, M., Wu, M.H., Yokozeki, H. & Nishioka, K. Contribution of selectin ligands to eosinophil recruitment into the skin of patients with atopic dermatitis. Eur. J. Immunol. 32, 1274-1281 (2002).
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1274-1281
    • Satoh, T.1    Kaneko, M.2    Wu, M.H.3    Yokozeki, H.4    Nishioka, K.5
  • 44
    • 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
    • Somers, W.S., Tang, J., Shaw, G.D. & Camphausen, R.T. 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, 467-479 (2000).
    • (2000) Cell , vol.103 , pp. 467-479
    • Somers, W.S.1    Tang, J.2    Shaw, G.D.3    Camphausen, R.T.4
  • 45
    • 28444493924 scopus 로고    scopus 로고
    • Homo-multimeric complexes of CD22 in B cells revealed by protein-glycan crosslinking
    • Han, S., Collins, B.E., Bengston, P. & Paulson, J.C. Homo-multimeric complexes of CD22 in B cells revealed by protein-glycan crosslinking. Nat. Chem. Biol. 1, 93-97 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 93-97
    • Han, S.1    Collins, B.E.2    Bengston, P.3    Paulson, J.C.4
  • 46
    • 10644297503 scopus 로고    scopus 로고
    • The use of carbohydrate microarrays to study carbohydrate-cell interactions and to detect pathogens
    • Disney, M.D. & Seeberger, P.H. The use of carbohydrate microarrays to study carbohydrate-cell interactions and to detect pathogens. Chem. Biol. 11, 1701-1707 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 1701-1707
    • Disney, M.D.1    Seeberger, P.H.2
  • 47
    • 3042786282 scopus 로고    scopus 로고
    • Oligosaccharide microarrays to decipher the glyco code
    • Feizi, T. & Chai, W. Oligosaccharide microarrays to decipher the glyco code. Nat. Rev. Mol. Cell Biol. 5, 582-588 (2004).
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 582-588
    • Feizi, T.1    Chai, W.2
  • 48
    • 0141953233 scopus 로고    scopus 로고
    • Carbohydrate microarrays - A new set of technologies at the frontiers of glycomics
    • Feizi, T., Fazio, F., Chai, W. & Wong, C.H. Carbohydrate microarrays - a new set of technologies at the frontiers of glycomics. Curr. Opin. Struct. Biol. 13, 637-645 (2003).
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 637-645
    • Feizi, T.1    Fazio, F.2    Chai, W.3    Wong, C.H.4
  • 49
    • 18744400555 scopus 로고    scopus 로고
    • Carbohydrate microarrays: An advanced technology for functional studies of glycans
    • Shin, I., Park, S. & Lee, M.R. Carbohydrate microarrays: an advanced technology for functional studies of glycans. Chemistry (Easton) 11, 2894-2901 (2005).
    • (2005) Chemistry (Easton) , vol.11 , pp. 2894-2901
    • Shin, I.1    Park, S.2    Lee, M.R.3
  • 50
    • 10344224476 scopus 로고    scopus 로고
    • eds. Wang, P.G. & Ichikawa, Y. American Chemical Society, Washington, DC
    • Blixt, O. & Razi, N. in Synthesis of Carbohydrates through Biotechnology (eds. Wang, P.G. & Ichikawa, Y.) 93-112 (American Chemical Society, Washington, DC, 2004).
    • (2004) Synthesis of Carbohydrates Through Biotechnology , pp. 93-112
    • Blixt, O.1    Razi, N.2
  • 51
    • 8544283771 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of oligosaccharides and glycoproteins
    • Hanson, S., Best, M., Bryan, M.C. & Wong, C.H. Chemoenzymatic synthesis of oligosaccharides and glycoproteins. Trends Biochem. Sci. 29, 656-663 (2004).
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 656-663
    • Hanson, S.1    Best, M.2    Bryan, M.C.3    Wong, C.H.4
  • 52
    • 26044440288 scopus 로고    scopus 로고
    • Automated synthesis of oligosaccharides as a basis for drug discovery
    • Seeberger, P.H. & Werz, D.B. Automated synthesis of oligosaccharides as a basis for drug discovery. Nat. Rev. Drug Discov. 4, 751-763 (2005).
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 751-763
    • Seeberger, P.H.1    Werz, D.B.2
  • 53
    • 0019258021 scopus 로고
    • Detection of gangliosides that bind cholera toxin: Direct binding of 1251-labeled toxin to thin-layer chromatograms
    • Magnani, J.L., Smith, D.F. & Ginsburg, V. Detection of gangliosides that bind cholera toxin: direct binding of 1251-labeled toxin to thin-layer chromatograms. Anal. Biochem. 109, 399-402 (1980).
    • (1980) Anal. Biochem. , vol.109 , pp. 399-402
    • Magnani, J.L.1    Smith, D.F.2    Ginsburg, V.3
  • 54
    • 0023654128 scopus 로고
    • Neoglycolipid micro-immunoassays applied to the oligosaccharides of human milk galactosyltransferase detect blood-group related antigens on both O- and N-linked chains
    • Tang, P.W. & Feizi, T. Neoglycolipid micro-immunoassays applied to the oligosaccharides of human milk galactosyltransferase detect blood-group related antigens on both O- and N-linked chains. Carbohydr. Res. 161, 133-143 (1987).
    • (1987) Carbohydr. Res. , vol.161 , pp. 133-143
    • Tang, P.W.1    Feizi, T.2
  • 55
    • 0022399761 scopus 로고
    • Novel approach to the study of the antigenicities and receptor functions of carbohydrate chains of glycoproteins
    • Tang, P.W., Gool, H.C., Hardy, M., Lee, Y.C. & Feizi, T. Novel approach to the study of the antigenicities and receptor functions of carbohydrate chains of glycoproteins. Biochem. Biophys. Res. Commun. 132, 474-480 (1985).
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , pp. 474-480
    • Tang, P.W.1    Gool, H.C.2    Hardy, M.3    Lee, Y.C.4    Feizi, T.5
  • 56
    • 0036193564 scopus 로고    scopus 로고
    • Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells
    • Wang, D., Liu, S., Trummer, B.J., Deng, C. & Wang, A. Carbohydrate microarrays for the recognition of cross-reactive molecular markers of microbes and host cells. Nat. Biotechnol. 20, 275-281 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 275-281
    • Wang, D.1    Liu, S.2    Trummer, B.J.3    Deng, C.4    Wang, A.5
  • 57
    • 0036916176 scopus 로고    scopus 로고
    • Sugar-coated microarrays: A novel slide surface for the high-throughput analysis of glycans
    • Willats, W.G., Rasmussen, S.E., Kristensen, T., Mikkelsen, J.D. & Knox, J.P. Sugar-coated microarrays: a novel slide surface for the high-throughput analysis of glycans. Proteomics 2, 1666-1671 (2002).
    • (2002) Proteomics , vol.2 , pp. 1666-1671
    • Willats, W.G.1    Rasmussen, S.E.2    Kristensen, T.3    Mikkelsen, J.D.4    Knox, J.P.5
  • 58
    • 25444480799 scopus 로고    scopus 로고
    • Fluorous-based carbohydrate microarrays
    • Ko, K.S., Jaipuri, F.A. & Pohl, N.L. Fluorous-based carbohydrate microarrays. J. Am. Chem. Soc. 127, 13162-13163 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13162-13163
    • Ko, K.S.1    Jaipuri, F.A.2    Pohl, N.L.3
  • 59
    • 14244269760 scopus 로고    scopus 로고
    • Glycan array screening reveals a candidate ligand for Siglec-8
    • Bochner, B.S. et al. Glycan array screening reveals a candidate ligand for Siglec-8. J. Biol. Chem. 280, 4307-4312 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 4307-4312
    • Bochner, B.S.1
  • 61
    • 0037009016 scopus 로고    scopus 로고
    • Fabrication of carbohydrate chips for studying protein-carbohydrate interactions
    • Park, S. & Shin, I. Fabrication of carbohydrate chips for studying protein-carbohydrate interactions. Angew. Chem. Int. Edn. Engl. 41, 3180-3182 (2002).
    • (2002) Angew. Chem. Int. Edn. Engl. , vol.41 , pp. 3180-3182
    • Park, S.1    Shin, I.2
  • 62
    • 27744522187 scopus 로고    scopus 로고
    • Hydrogel glycan microarrays
    • Dyukova, V.I. et al. Hydrogel glycan microarrays. Anal. Biochem. 347, 94-105 (2005).
    • (2005) Anal. Biochem. , vol.347 , pp. 94-105
    • Dyukova, V.I.1
  • 63
    • 10344233222 scopus 로고    scopus 로고
    • Printed covalent glycan array for ligand profiling of diverse glycan binding proteins
    • Blixt, O. et al. Printed covalent glycan array for ligand profiling of diverse glycan binding proteins. Proc. Natl. Acad. Sci. USA 101, 17033-17038 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17033-17038
    • Blixt, O.1
  • 64
    • 2442580955 scopus 로고    scopus 로고
    • High-throughput identification of fucosyltransferase inhibitors using carbohydrate microarrays
    • Bryan, M.C., Lee, L.V. & Wong, C.H. High-throughput identification of fucosyltransferase inhibitors using carbohydrate microarrays. Bioorg. Med. Chem. Lett. 14, 3185-3188 (2004).
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 3185-3188
    • Bryan, M.C.1    Lee, L.V.2    Wong, C.H.3
  • 65
    • 3042682570 scopus 로고    scopus 로고
    • An early taste of functional glycomics
    • Mrksich, M. An early taste of functional glycomics. Chem. Biol. 11, 739-740 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 739-740
    • Mrksich, M.1
  • 66
    • 13444288243 scopus 로고    scopus 로고
    • Glycoprofiling with micro-arrays of glycoconjugates and lectins
    • Angeloni, S. et al. Glycoprofiling with micro-arrays of glycoconjugates and lectins. Glycobiology 15, 31-41 (2005).
    • (2005) Glycobiology , vol.15 , pp. 31-41
    • Angeloni, S.1
  • 67
    • 11144303670 scopus 로고    scopus 로고
    • Synthesis and reactions of glycosides
    • Garegg, P.J. Synthesis and reactions of glycosides. Adv. Carbohydr. Chem. Biochem. 59, 69-134 (2004).
    • (2004) Adv. Carbohydr. Chem. Biochem. , vol.59 , pp. 69-134
    • Garegg, P.J.1
  • 68
    • 0035805264 scopus 로고    scopus 로고
    • Adventures in carbohydrate chemistry: New synthetic technologies, chemical synthesis, molecular design, and chemical biology
    • Nicolaou, K.C. & Mitchell, H.J. Adventures in carbohydrate chemistry: new synthetic technologies, chemical synthesis, molecular design, and chemical biology. Angew. Chem. Int. Edn Engl. 40, 1576-1624 (2001).
    • (2001) Angew. Chem. Int. Edn Engl. , vol.40 , pp. 1576-1624
    • Nicolaou, K.C.1    Mitchell, H.J.2
  • 69
    • 13244249609 scopus 로고    scopus 로고
    • One-pot synthesis of sialo-containing glycosyl amino acids by use of an N-trichloroethoxycarbonyl-β-thiophenyl sialoside
    • Tanaka, H., Adachi, M. & Takahashi, T. One-pot synthesis of sialo-containing glycosyl amino acids by use of an N-trichloroethoxycarbonyl- β-thiophenyl sialoside. Chemistry (Easton) 11, 849-862 (2005).
    • (2005) Chemistry (Easton) , vol.11 , pp. 849-862
    • Tanaka, H.1    Adachi, M.2    Takahashi, T.3
  • 70
    • 0034697139 scopus 로고    scopus 로고
    • Anomeric reactivity-based one-pot oligosaccharide synthesis: A rapid route to oligosaccharide libraries
    • Ye, X.S. & Wong, C.H. Anomeric reactivity-based one-pot oligosaccharide synthesis: a rapid route to oligosaccharide libraries. J. Org. Chem. 65, 2410-2431 (2000).
    • (2000) J. Org. Chem. , vol.65 , pp. 2410-2431
    • Ye, X.S.1    Wong, C.H.2
  • 71
    • 0033032743 scopus 로고    scopus 로고
    • Large-scale production of N-acetyllactosamine through bacterial coupling
    • Endo, T., Koizumi, S., Tabata, K., Kakita, S. & Ozaki, A. Large-scale production of N-acetyllactosamine through bacterial coupling. Carbohydr. Res. 316, 179-183 (1999).
    • (1999) Carbohydr. Res. , vol.316 , pp. 179-183
    • Endo, T.1    Koizumi, S.2    Tabata, K.3    Kakita, S.4    Ozaki, A.5
  • 72
    • 0042232205 scopus 로고    scopus 로고
    • Sialoside specificity of the siglec family assessed using novel multivalent probes: Identification of potent inhibitors of myelin-associated glycoprotein
    • Blixt, O., Collins, B.E., van den Nieuwenhof, I.M., Crocker, P.R. & Paulson, J.C. Sialoside specificity of the siglec family assessed using novel multivalent probes: identification of potent inhibitors of myelin-associated glycoprotein. J. Biol. Chem. 278, 31007-31019 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 31007-31019
    • Blixt, O.1    Collins, B.E.2    Van Den Nieuwenhof, I.M.3    Crocker, P.R.4    Paulson, J.C.5
  • 73
    • 22744432702 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of 2-azidoethyl-ganglio-oligosaccharides GD3, GT3, GM2, GD2, GT2, GM1, and GD1a
    • Blixt, O. et al. Chemoenzymatic synthesis of 2-azidoethyl-ganglio- oligosaccharides GD3, GT3, GM2, GD2, GT2, GM1, and GD1a. Carbohydr. Res. 340, 1963-1972 (2005).
    • (2005) Carbohydr. Res. , vol.340 , pp. 1963-1972
    • Blixt, O.1
  • 74
    • 28444447140 scopus 로고    scopus 로고
    • Large-scale approaches for glycobiology
    • Campbell, C.T. & Yarema, K.J. Large-scale approaches for glycobiology. Genome Biol. 6, 236 (2005).
    • (2005) Genome Biol. , vol.6 , pp. 236
    • Campbell, C.T.1    Yarema, K.J.2
  • 75
    • 5444254250 scopus 로고    scopus 로고
    • Lectin-based structural glycomics: Glycoproteomics and glycan profiling
    • Hirabayashi, J. Lectin-based structural glycomics: glycoproteomics and glycan profiling. Glycoconj. J. 21, 35-40 (2004).
    • (2004) Glycoconj. J. , vol.21 , pp. 35-40
    • Hirabayashi, J.1
  • 76
    • 14744286126 scopus 로고    scopus 로고
    • Synthesis of diverse asparagine linked oligosaccharides and synthesis of sialylglycopeptide on solid phase
    • Kajihara, Y., Yamamoto, N., Miyazaki, T. & Sato, H. Synthesis of diverse asparagine linked oligosaccharides and synthesis of sialylglycopeptide on solid phase. Curr. Med. Chem. 12, 527-550 (2005).
    • (2005) Curr. Med. Chem. , vol.12 , pp. 527-550
    • Kajihara, Y.1    Yamamoto, N.2    Miyazaki, T.3    Sato, H.4
  • 77
    • 17744363690 scopus 로고    scopus 로고
    • Improving glycopeptide synthesis: A convenient protocol for the preparation of β-glycosylamines and the synthesis of glycopeptides
    • Hackenberger, C.P., O'Reilly, M.K. & Imperiali, B. Improving glycopeptide synthesis: a convenient protocol for the preparation of β-glycosylamines and the synthesis of glycopeptides. J. Org. Chem. 70, 3574-3578 (2005).
    • (2005) J. Org. Chem. , vol.70 , pp. 3574-3578
    • Hackenberger, C.P.1    O'Reilly, M.K.2    Imperiali, B.3
  • 78
    • 28544438397 scopus 로고    scopus 로고
    • Versatile fluorescent derivatization of glycans for glycomic analysis
    • Xia, B. et al. Versatile fluorescent derivatization of glycans for glycomic analysis. Nat. Methods 2, 845-850 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 845-850
    • Xia, B.1
  • 79
    • 3042637779 scopus 로고    scopus 로고
    • Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR
    • Guo, Y. et al. Structural basis for distinct ligand-binding and targeting properties of the receptors DC-SIGN and DC-SIGNR. Nat. Struct. Mol. Biol. 11, 591-598 (2004).
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 591-598
    • Guo, Y.1
  • 80
    • 25144506380 scopus 로고    scopus 로고
    • Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells
    • van Vliet, S.J. et al. Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells. Int. Immunol. 17, 661-669 (2005).
    • (2005) Int. Immunol. , vol.17 , pp. 661-669
    • Van Vliet, S.J.1
  • 81
    • 33646126940 scopus 로고    scopus 로고
    • The carbohydrate recognition domain of dectin-2 is a C-type lectin with specificity for high-mannose
    • published online 19 January doi:10.1093/glycob/cwj077
    • McGreal, E.P. et al. The carbohydrate recognition domain of dectin-2 is a C-type lectin with specificity for high-mannose. Glycobiology, published online 19 January 2006 (doi:10.1093/glycob/cwj077).
    • (2006) Glycobiology
    • McGreal, E.P.1
  • 82
    • 2942720454 scopus 로고    scopus 로고
    • High and low affinity carbohydrate ligands revealed for murine SIGN-R1 by carbohydrate array and cell binding approaches, and differing specificities for SIGN-R3 and langerin
    • Galustian, C. et al. High and low affinity carbohydrate ligands revealed for murine SIGN-R1 by carbohydrate array and cell binding approaches, and differing specificities for SIGN-R3 and langerin. Int. Immunol. 16, 853-866 (2004).
    • (2004) Int. Immunol. , vol.16 , pp. 853-866
    • Galustian, C.1
  • 83
    • 0141995591 scopus 로고    scopus 로고
    • A new kind of carbohydrate array, its use for profiling antiglycan antibodies, and the discovery of a novel human cellulose-binding antibody
    • Schwarz, M. et al. A new kind of carbohydrate array, its use for profiling antiglycan antibodies, and the discovery of a novel human cellulose-binding antibody. Glycobiology 13, 749-754 (2003).
    • (2003) Glycobiology , vol.13 , pp. 749-754
    • Schwarz, M.1
  • 84
    • 1342285016 scopus 로고    scopus 로고
    • Intact cell adhesion to glycan microarrays
    • Nimrichter, L. et al. Intact cell adhesion to glycan microarrays. Glycobiology 14, 197-203 (2004).
    • (2004) Glycobiology , vol.14 , pp. 197-203
    • Nimrichter, L.1
  • 85
    • 33644815187 scopus 로고    scopus 로고
    • A practical protocol for carbohydrate microarrays
    • Wang, R., Liu, S., Shah, D. & Wang, D. A practical protocol for carbohydrate microarrays. Methods Mol. Biol. 310, 241-252 (2005).
    • (2005) Methods Mol. Biol. , vol.310 , pp. 241-252
    • Wang, R.1    Liu, S.2    Shah, D.3    Wang, D.4
  • 86
    • 20744459138 scopus 로고    scopus 로고
    • Selective binding of the scavenger receptor C-type lectin to Lewis(x)trisaccharide and related glycan ligands
    • Coombs, P.J., Graham, S.A., Drickamer, K. & Taylor, M.E. Selective binding of the scavenger receptor C-type lectin to Lewis(x)trisaccharide and related glycan ligands. J. Biol. Chem. 280, 22993-22999 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 22993-22999
    • Coombs, P.J.1    Graham, S.A.2    Drickamer, K.3    Taylor, M.E.4
  • 87
    • 33646843444 scopus 로고    scopus 로고
    • Ligands for the β-glucan receptor, dectin-1, assigned using 'designer' microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides
    • Palma, A.S. et al. Ligands for the β-glucan receptor, dectin-1, assigned using 'designer' microarrays of oligosaccharide probes (neoglycolipids) generated from glucan polysaccharides. J. Biol. Chem. 281, 5771-5779 (2005).
    • (2005) J. Biol. Chem. , vol.281 , pp. 5771-5779
    • Palma, A.S.1
  • 88
    • 27944460432 scopus 로고    scopus 로고
    • Mouse Siglec-F and human Siglec-8 are functionally convergent paralogs that are selectively expressed on eosinophils and recognize 6′-sulfo- sialyl Lewis X as a preferred glycan ligand
    • Tateno, H., Crocker, P.R. & Paulson, J.C. Mouse Siglec-F and human Siglec-8 are functionally convergent paralogs that are selectively expressed on eosinophils and recognize 6′-sulfo-sialyl Lewis X as a preferred glycan ligand. Glycobiology 15, 1125-1135 (2005).
    • (2005) Glycobiology , vol.15 , pp. 1125-1135
    • Tateno, H.1    Crocker, P.R.2    Paulson, J.C.3
  • 89
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • Stevens, J. et al. Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J. Mol. Biol. 355, 1143-1155 (2006).
    • (2006) J. Mol. Biol. , vol.355 , pp. 1143-1155
    • Stevens, J.1
  • 90
    • 80255139730 scopus 로고    scopus 로고
    • Glycan array identifies specific signatures of anti-glycan autoantibodies in sera of breast cancer patients: Diagnostic, prognostic and therapeutic opportunities
    • Huflejt, M.E. et al. Glycan array identifies specific signatures of anti-glycan autoantibodies in sera of breast cancer patients: diagnostic, prognostic and therapeutic opportunities. Breast Cancer Res. Treat. 94, S85 (2005).
    • (2005) Breast Cancer Res. Treat. , vol.94
    • Huflejt, M.E.1
  • 91
    • 30444458986 scopus 로고    scopus 로고
    • Carbohydrate microarray for profiling the antibodies interacting with Globo H tumor antigen
    • Huang, C.Y. et al. Carbohydrate microarray for profiling the antibodies interacting with Globo H tumor antigen. Proc. Natl. Acad. Sci. USA 103, 15-20 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 15-20
    • Huang, C.Y.1
  • 92
    • 33646400026 scopus 로고    scopus 로고
    • Cancer-associated carbohydrate identification in Hodgkin's lymphoma by carbohydrate array profiling
    • published online 4 January doi:10.1002/iij.21762
    • Lawrie, C.H. et al. Cancer-associated carbohydrate identification in Hodgkin's lymphoma by carbohydrate array profiling. Int. J. Cancer, published online 4 January 2006 (doi:10.1002/iij.21762).
    • (2006) Int. J. Cancer
    • Lawrie, C.H.1
  • 93
    • 33646458337 scopus 로고    scopus 로고
    • Carbohydrate array analysis of anti-Tn antibodies and lectins reveals unexpected specificities: Implications for diagnostic and vaccine development
    • Manimala, J.C., Li, Z., Jain, A., Vedbrat, S. & Gildersleeve, J.C. Carbohydrate array analysis of anti-Tn antibodies and lectins reveals unexpected specificities: implications for diagnostic and vaccine development. Chembiochem 6, 2229-2241 (2005).
    • (2005) Chembiochem , vol.6 , pp. 2229-2241
    • Manimala, J.C.1    Li, Z.2    Jain, A.3    Vedbrat, S.4    Gildersleeve, J.C.5
  • 94
    • 20444501805 scopus 로고    scopus 로고
    • Development of a lectin microarray for the rapid analysis of protein glycopatterns
    • Pilobello, K.T., Krishnamoorthy, L., Slawek, D. & Mahal, L.K. Development of a lectin microarray for the rapid analysis of protein glycopatterns. ChemBioChem 6, 985-989 (2005).
    • (2005) ChemBioChem , vol.6 , pp. 985-989
    • Pilobello, K.T.1    Krishnamoorthy, L.2    Slawek, D.3    Mahal, L.K.4
  • 95
    • 22244436325 scopus 로고    scopus 로고
    • Lectin arrays for profiling cell surface carbohydrate expression
    • Zheng, T., Peelen, D. & Smith, L.M. Lectin arrays for profiling cell surface carbohydrate expression. J. Am. Chem. Soc. 127, 9982-9983 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9982-9983
    • Zheng, T.1    Peelen, D.2    Smith, L.M.3
  • 96
    • 33646452547 scopus 로고    scopus 로고
    • Analyzing the dynamic bacterial glycome with a lectin microarray approach
    • Hsu, K.L., Pilobello, K.T. & Mahal, L.K. Analyzing the dynamic bacterial glycome with a lectin microarray approach. Nat. Chem. Biol. 2, 153-157 (2006).
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 153-157
    • Hsu, K.L.1    Pilobello, K.T.2    Mahal, L.K.3
  • 97
    • 0026799439 scopus 로고
    • Biosynthesis of a nonphysiological sialic acid in different rat organs, using N-propanoyl-D-hexosamines as precursors
    • Kayser, H. et al. Biosynthesis of a nonphysiological sialic acid in different rat organs, using N-propanoyl-D-hexosamines as precursors. J. Biol. Chem. 267, 16934-16938 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 16934-16938
    • Kayser, H.1
  • 98
    • 0026548021 scopus 로고
    • Incorporation of N-acyl-2-amino-2-deoxy-hexoses into glycosphingolipids of the pheochromocytoma cell line PC 12
    • Kayser, H., Geilen, C.C., Paul, C., Zeitler, R. & Reutter, W. Incorporation of N-acyl-2-amino-2-deoxy-hexoses into glycosphingolipids of the pheochromocytoma cell line PC 12. FEBS Lett. 301, 137-140 (1992).
    • (1992) FEBS Lett. , vol.301 , pp. 137-140
    • Kayser, H.1    Geilen, C.C.2    Paul, C.3    Zeitler, R.4    Reutter, W.5
  • 99
    • 0028893933 scopus 로고
    • Biosynthetic modulation of sialic acid-dependent virus-receptor interactions of two primate polyoma viruses
    • Keppler, O.T. et al. Biosynthetic modulation of sialic acid-dependent virus-receptor interactions of two primate polyoma viruses. J. Biol. Chem. 270, 1308-1314 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 1308-1314
    • Keppler, O.T.1
  • 100
    • 0142199949 scopus 로고    scopus 로고
    • Metabolic oligosaccharide engineering as a tool for glycobiology
    • Dube, D.H. & Bertozzi, C.R. Metabolic oligosaccharide engineering as a tool for glycobiology. Curr. Opin. Chem. Biol. 7, 616-625 (2003).
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 616-625
    • Dube, D.H.1    Bertozzi, C.R.2
  • 101
    • 0035937499 scopus 로고    scopus 로고
    • Chemical glycobiology
    • Bertozzi, C.R. & Kiessling, L.L. Chemical glycobiology. Science 291, 2357-2364 (2001).
    • (2001) Science , vol.291 , pp. 2357-2364
    • Bertozzi, C.R.1    Kiessling, L.L.2
  • 102
    • 0035054528 scopus 로고    scopus 로고
    • Biochemical engineering of the N-acyl side chain of sialic acid: Biological implications
    • Keppler, O.T., Horstkorte, R., Pawlita, M., Schmidt, C. & Reutter, W. Biochemical engineering of the N-acyl side chain of sialic acid: biological implications. Glycobiology 11, 11R-18R (2001).
    • (2001) Glycobiology , vol.11
    • Keppler, O.T.1    Horstkorte, R.2    Pawlita, M.3    Schmidt, C.4    Reutter, W.5
  • 103
    • 4344704630 scopus 로고    scopus 로고
    • Chemical remodelling of cell surfaces in living animals
    • Prescher, J.A., Dube, D.H. & Bertozzi, C.R. Chemical remodelling of cell surfaces in living animals. Nature 430, 873-877 (2004).
    • (2004) Nature , vol.430 , pp. 873-877
    • Prescher, J.A.1    Dube, D.H.2    Bertozzi, C.R.3
  • 104
    • 4544310350 scopus 로고    scopus 로고
    • Expanding the diversity of unnatural cell-surface sialic acids
    • Luchansky, S.J., Goon, S. & Bertozzi, C.R. Expanding the diversity of unnatural cell-surface sialic acids. ChemBioChem 5, 371-374 (2004).
    • (2004) ChemBioChem , vol.5 , pp. 371-374
    • Luchansky, S.J.1    Goon, S.2    Bertozzi, C.R.3
  • 106
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alpha-keto acids: An evolutionary perspective
    • Angata, T. & Varki, A. Chemical diversity in the sialic acids and related alpha-keto acids: an evolutionary perspective. Chem. Rev. 102, 439-469 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 107
    • 0442294020 scopus 로고    scopus 로고
    • Characterization of the cellular uptake and metabolic conversion of acetylated N-acetylmannosamine (ManNAc) analogues to sialic acids
    • Jones, M.B. et al. Characterization of the cellular uptake and metabolic conversion of acetylated N-acetylmannosamine (ManNAc) analogues to sialic acids. Biotechnol. Bioeng. 85, 394-405 (2004).
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 394-405
    • Jones, M.B.1
  • 108
    • 3342965895 scopus 로고    scopus 로고
    • Biochemical engineering of the N-acyl side chain of sialic acid leads to increased calcium influx from intracellular compartments and promotes differentiation of HL60 cells
    • Horstkorte, R., Rau, K., Laabs, S., Danker, K. & Reutter, W. Biochemical engineering of the N-acyl side chain of sialic acid leads to increased calcium influx from intracellular compartments and promotes differentiation of HL60 cells. FEBS Lett. 571, 99-102 (2004).
    • (2004) FEBS Lett. , vol.571 , pp. 99-102
    • Horstkorte, R.1    Rau, K.2    Laabs, S.3    Danker, K.4    Reutter, W.5
  • 109
    • 0033998936 scopus 로고    scopus 로고
    • Conversion of cellular sialic acid expression from N-acetyl- to N-glycolylneuraminic acid using a synthetic precursor, N-glycolylmannosamine pentaacetate: Inhibition of myelin-associated glycoprotein binding to neural cells
    • Collins, B.E., Fralich, T.J., Itonori, S., Ichikawa, Y. & Schnaar, R.L. Conversion of cellular sialic acid expression from N-acetyl- to N-glycolylneuraminic acid using a synthetic precursor, N-glycolylmannosamine pentaacetate: inhibition of myelin-associated glycoprotein binding to neural cells. Glycobiology 10, 11-20 (2000).
    • (2000) Glycobiology , vol.10 , pp. 11-20
    • Collins, B.E.1    Fralich, T.J.2    Itonori, S.3    Ichikawa, Y.4    Schnaar, R.L.5
  • 110
    • 0033793732 scopus 로고    scopus 로고
    • Biosynthetic incorporation of unnatural sialic acids into polysialic acid on neural cells
    • Charter, N.W., Mahal, L.K., Koshland, D.E., Jr & Bertozzi, C.R. Biosynthetic incorporation of unnatural sialic acids into polysialic acid on neural cells. Glycobiology 10, 1049-1056 (2000).
    • (2000) Glycobiology , vol.10 , pp. 1049-1056
    • Charter, N.W.1    Mahal, L.K.2    Koshland Jr., D.E.3    Bertozzi, C.R.4
  • 111
    • 0037088575 scopus 로고    scopus 로고
    • Differential effects of unnatural sialic acids on the polysialylation of the neural cell adhesion molecule and neuronal behavior
    • Charter, N.W., Mahal, L.K., Koshland, D.E., Jr & Bertozzi, C.R. Differential effects of unnatural sialic acids on the polysialylation of the neural cell adhesion molecule and neuronal behavior. J. Biol. Chem. 277, 9255-9261 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 9255-9261
    • Charter, N.W.1    Mahal, L.K.2    Koshland Jr., D.E.3    Bertozzi, C.R.4
  • 112
    • 0037453019 scopus 로고    scopus 로고
    • Metabolic incorporation of unnatural sialic acids into Haemophilus ducreyi lipooligosaccharides
    • Goon, S., Schilling, B., Tullius, M.V., Gibson, B.W. & Bertozzi, C.R. Metabolic incorporation of unnatural sialic acids into Haemophilus ducreyi lipooligosaccharides. Proc. Natl. Acad. Sci. USA 100, 3089-3094 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3089-3094
    • Goon, S.1    Schilling, B.2    Tullius, M.V.3    Gibson, B.W.4    Bertozzi, C.R.5
  • 113
    • 1842861739 scopus 로고    scopus 로고
    • Increased expression of the selectin ligand sialyl-Lewis(x) by biochemical engineering of sialic acids
    • Horstkorte, R., Rau, K., Reutter, W., Nohring, S. & Lucka, L. Increased expression of the selectin ligand sialyl-Lewis(x) by biochemical engineering of sialic acids. Exp. Cell Res. 295, 549-554 (2004).
    • (2004) Exp. Cell Res. , vol.295 , pp. 549-554
    • Horstkorte, R.1    Rau, K.2    Reutter, W.3    Nohring, S.4    Lucka, L.5
  • 114
    • 10844273227 scopus 로고    scopus 로고
    • Azido sialic acids can modulate cell-surface interactions
    • Luchansky, S.J. & Bertozzi, C.R. Azido sialic acids can modulate cell-surface interactions. ChemBioChem 5, 1706-1709 (2004).
    • (2004) ChemBioChem , vol.5 , pp. 1706-1709
    • Luchansky, S.J.1    Bertozzi, C.R.2
  • 116
    • 0345598906 scopus 로고    scopus 로고
    • A metabolic label ing approach toward proteomic analysis of mucin-type O-linked glycosylation
    • Hang, H.C., Yu, C., Kato, D.L. & Bertozzi, C.R. A metabolic label ing approach toward proteomic analysis of mucin-type O-linked glycosylation. Proc. Natl. Acad. Sci. USA 100, 14846-14851 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14846-14851
    • Hang, H.C.1    Yu, C.2    Kato, D.L.3    Bertozzi, C.R.4
  • 117
    • 0037132659 scopus 로고    scopus 로고
    • Investigating cellular metabolism of synthetic azidosugars with the Staudinger ligation
    • Saxon, E. et al. Investigating cellular metabolism of synthetic azidosugars with the Staudinger ligation. J. Am. Chem. Soc. 124, 14893-14902 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14893-14902
    • Saxon, E.1
  • 118
    • 21744431575 scopus 로고    scopus 로고
    • The sweet and sour of cancer: Glycans as novel therapeutic targets
    • Fuster, M.M. & Esko, J.D. The sweet and sour of cancer: glycans as novel therapeutic targets. Nat. Rev. Cancer 5, 526-542 (2005).
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 526-542
    • Fuster, M.M.1    Esko, J.D.2
  • 119
    • 0038615922 scopus 로고    scopus 로고
    • A disaccharide precursor of sialyl Lewis X inhibits metastatic potential of tumor cells
    • Fuster, M.M., Brown, J.R., Wang, L. & Esko, J.D. A disaccharide precursor of sialyl Lewis X inhibits metastatic potential of tumor cells. Cancer Res. 63, 2775-2781 (2003).
    • (2003) Cancer Res. , vol.63 , pp. 2775-2781
    • Fuster, M.M.1    Brown, J.R.2    Wang, L.3    Esko, J.D.4
  • 120
    • 8844261143 scopus 로고    scopus 로고
    • Cell surface biology mediated by low affinity multivalent protein-glycan interactions
    • Collins, B.E. & Paulson, J.C. Cell surface biology mediated by low affinity multivalent protein-glycan interactions. Curr. Opin. Chem. Biol. 8, 617-625 (2004).
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 617-625
    • Collins, B.E.1    Paulson, J.C.2
  • 121
    • 0346981999 scopus 로고    scopus 로고
    • Influencing receptor-ligand binding mechanisms with multivalent ligand architecture
    • Gestwicki, J.E., Cairo, C.W., Strong, L.E., Oetjen, K.A. & Kiessling, L.L. Influencing receptor-ligand binding mechanisms with multivalent ligand architecture. J. Am. Chem. Soc. 124, 14922-14933 (2002).
    • (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
  • 122
    • 0036462602 scopus 로고    scopus 로고
    • The cluster glycoside effect
    • Lundquist, J.J. & Toone, E.J. The cluster glycoside effect. Chem. Rev. 102, 555-578 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 555-578
    • Lundquist, J.J.1    Toone, E.J.2
  • 123
    • 0037188488 scopus 로고    scopus 로고
    • A therapeutic agent with oriented carbohydrates for treatment of infections by Shiga toxin-producing Escherichia coli O157:H7
    • Nishikawa, K. et al. A therapeutic agent with oriented carbohydrates for treatment of infections by Shiga toxin-producing Escherichia coli O157:H7. Proc. Natl. Acad. Sci. USA 199, 7669-7674 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.199 , pp. 7669-7674
    • Nishikawa, K.1
  • 124
    • 2142770270 scopus 로고    scopus 로고
    • Novel polysulfated galactose-derivatized dendrimers as binding antagonists of human immunodeficiency virus type 1 infection
    • Kensinger, R.D., Catalone, B.J., Krebs, F.C., Wigdahl, B. & Schengrund, C.L. Novel polysulfated galactose-derivatized dendrimers as binding antagonists of human immunodeficiency virus type 1 infection. Antimicrob. Agents Chemother. 48, 1614-1623 (2004).
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 1614-1623
    • Kensinger, R.D.1    Catalone, B.J.2    Krebs, F.C.3    Wigdahl, B.4    Schengrund, C.L.5
  • 125
    • 27744545243 scopus 로고    scopus 로고
    • Polymer-bound 6′ sialyl-N-acetyllactosamine protects mice infected by influenza virus
    • Gambaryan, A.S. et al. Polymer-bound 6′ sialyl-N-acetyllactosamine protects mice infected by influenza virus. Antiviral Res. 68, 116-123 (2005).
    • (2005) Antiviral Res. , vol.68 , pp. 116-123
    • Gambaryan, A.S.1
  • 126
    • 22944488021 scopus 로고    scopus 로고
    • Dendrimer-like PEO glycopolymers exhibit anti-inflammatory properties
    • Rele, S.M. et al. Dendrimer-like PEO glycopolymers exhibit anti-inflammatory properties. J. Am. Chem. Soc. 127, 10132-10133 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10132-10133
    • Rele, S.M.1
  • 127
    • 1342310803 scopus 로고    scopus 로고
    • Polymers bearing sLex-mimetics are superior inhibitors of E-selectin-dependent leukocyte rolling in vivo
    • Ali, M., Hicks, A.E., Hellewell, P.G., Thoma, G. & Norman, K.E. Polymers bearing sLex-mimetics are superior inhibitors of E-selectin-dependent leukocyte rolling in vivo. FASEB J. 18, 152-154 (2004).
    • (2004) FASEB J. , vol.18 , pp. 152-154
    • Ali, M.1    Hicks, A.E.2    Hellewell, P.G.3    Thoma, G.4    Norman, K.E.5
  • 128
    • 2642575134 scopus 로고    scopus 로고
    • Synthetic glycoprotein mimics inhibit L-selectin-mediated rolling and promote L-selectin shedding
    • Mowery, P. et al. Synthetic glycoprotein mimics inhibit L-selectin-mediated rolling and promote L-selectin shedding. Chem. Biol. 11, 725-732 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 725-732
    • Mowery, P.1
  • 129
    • 0021772463 scopus 로고
    • New synthetic cluster ligands for galactose/N-acetylgalactosamine- specific lectin of mammalian liver
    • Lee, R.T., Lin, P. & Lee, Y.C. New synthetic cluster ligands for galactose/N-acetylgalactosamine-specific lectin of mammalian liver. Biochemistry 23, 4255-4261 (1984).
    • (1984) Biochemistry , vol.23 , pp. 4255-4261
    • Lee, R.T.1    Lin, P.2    Lee, Y.C.3
  • 130
    • 0034628502 scopus 로고    scopus 로고
    • Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands
    • Kitov, P.I. et al. Shiga-like toxins are neutralized by tailored multivalent carbohydrate ligands. Nature 403, 669-672 (2000).
    • (2000) Nature , vol.403 , pp. 669-672
    • Kitov, P.I.1
  • 131
    • 0242417566 scopus 로고    scopus 로고
    • Optimization of tether length in nonglycosidically linked bivalent ligands that target sites 2 and 1 of a Shiga-like toxin
    • Kitov, P.I., Shimizu, H., Homans, S.W. & Bundle, D.R. Optimization of tether length in nonglycosidically linked bivalent ligands that target sites 2 and 1 of a Shiga-like toxin. J. Am. Chem. Soc. 125, 3284-3294 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 3284-3294
    • Kitov, P.I.1    Shimizu, H.2    Homans, S.W.3    Bundle, D.R.4
  • 132
    • 0037442497 scopus 로고    scopus 로고
    • Assessment in mice of the therapeutic potential of tailored, multivalent Shiga toxin carbohydrate ligands
    • Mulvey, G.L. et al. Assessment in mice of the therapeutic potential of tailored, multivalent Shiga toxin carbohydrate ligands. J. Infect. Dis. 187, 640-649 (2003).
    • (2003) J. Infect. Dis. , vol.187 , pp. 640-649
    • Mulvey, G.L.1
  • 133
    • 4644331825 scopus 로고    scopus 로고
    • A self-assembled multivalent pseudopolyrotaxane for binding galectin-1
    • Nelson, A. et al. A self-assembled multivalent pseudopolyrotaxane for binding galectin-1. J. Am. Chem. Soc. 126, 11914-11922 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 11914-11922
    • Nelson, A.1
  • 135
    • 13944283259 scopus 로고    scopus 로고
    • Protein heterodimerization through ligand-bridged multivalent pre-organization: Enhancing ligand binding toward both protein targets
    • Liu, J. et al. Protein heterodimerization through ligand-bridged multivalent pre-organization: enhancing ligand binding toward both protein targets. J. Am. Chem. Soc. 127, 2044-2045 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2044-2045
    • Liu, J.1
  • 136
    • 26444601733 scopus 로고    scopus 로고
    • Heterobifunctional multivalent inhibitor-adaptor mediates specific aggregation between Shiga toxin and a pentraxin
    • Solomon, D. et al. Heterobifunctional multivalent inhibitor-adaptor mediates specific aggregation between Shiga toxin and a pentraxin. Org. Lett. 7, 4369-4372 (2005).
    • (2005) Org. Lett. , vol.7 , pp. 4369-4372
    • Solomon, D.1
  • 137
    • 0036788485 scopus 로고    scopus 로고
    • Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions
    • Fukui, S., Feizi, T., Galustian, C., Lawson, A.M. & Chai, W. Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions. Nat. Biotechnol. 20, 1011-1017 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1011-1017
    • Fukui, S.1    Feizi, T.2    Galustian, C.3    Lawson, A.M.4    Chai, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.