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Volumn 26, Issue 1, 2006, Pages 43-79

Cell surface glycans: The why and how of their functionality as biochemical signals in lectin-mediated information transfer

Author keywords

Apoptosis; Cell adhesion; Galectin; Glycosylation; Glycosyltransferases; Integrin; Phagocytosis

Indexed keywords

CELL SURFACE PROTEIN; GALECTIN; GLYCAN; GLYCOSYLTRANSFERASE; INTEGRIN; LECTIN;

EID: 33646879955     PISSN: 10408401     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (134)

References (330)
  • 1
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R, Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem. 1985;54:631-64.
    • (1985) Annu Rev Biochem , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 2
    • 0026655996 scopus 로고
    • Structures and functions of the sugar chains of glycoproteins
    • Kobata A. Structures and functions of the sugar chains of glycoproteins. Eur J Biochem. 1992;209:483-501.
    • (1992) Eur J Biochem , vol.209 , pp. 483-501
    • Kobata, A.1
  • 3
    • 0002638114 scopus 로고    scopus 로고
    • Glycoproteins: Structure and function
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Sharon N, Lis H. Glycoproteins: structure and function. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 133-62.
    • (1997) Glycosciences: Status and Perspectives , pp. 133-162
    • Sharon, N.1    Lis, H.2
  • 4
    • 0032953692 scopus 로고    scopus 로고
    • Eukaryotic glycosylation - Whim of nature or multipurpose tool?
    • Reuter G, Gabius H-J. Eukaryotic glycosylation - whim of nature or multipurpose tool? Cell Mol Life Sci. 1999;55:368-422.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 368-422
    • Reuter, G.1    Gabius, H.-J.2
  • 5
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology. 2002;12:43R-56R.
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 6
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta. 1999;1473:4-8.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 8
    • 0037524357 scopus 로고    scopus 로고
    • O-GlcNAc turns twenty: Functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar
    • Wells L, Hart GW. O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar. FEBS Lett. 2003;546:154-8.
    • (2003) FEBS Lett , vol.546 , pp. 154-158
    • Wells, L.1    Hart, G.W.2
  • 9
    • 3042568878 scopus 로고    scopus 로고
    • Large clostridial cytotoxins: Cellular biology of Rho/Ras-glucosylating toxins
    • Schirmer J, Aktories K. Large clostridial cytotoxins: cellular biology of Rho/Ras-glucosylating toxins. Biochim Biophys Acta. 2004;1673:66-74.
    • (2004) Biochim Biophys Acta , vol.1673 , pp. 66-74
    • Schirmer, J.1    Aktories, K.2
  • 11
    • 0034577985 scopus 로고    scopus 로고
    • Protein C-mannosylation: Facts and questions
    • Furmanek A, Hofsteenge J. Protein C-mannosylation: facts and questions. Acta Biochim Pol. 2000;47:781-9.
    • (2000) Acta Biochim Pol , vol.47 , pp. 781-789
    • Furmanek, A.1    Hofsteenge, J.2
  • 13
    • 0037074006 scopus 로고    scopus 로고
    • Regulation of Notch signaling by O-linked fucose
    • Okajima T, Irvine KD. Regulation of Notch signaling by O-linked fucose. Cell. 2002;111:893-904.
    • (2002) Cell , vol.111 , pp. 893-904
    • Okajima, T.1    Irvine, K.D.2
  • 14
    • 0141995063 scopus 로고    scopus 로고
    • Glycosylation regulates Notch signalling
    • Haines N, Irvine KD. Glycosylation regulates Notch signalling. Nat Rev Mol Cell Biol. 2003;4:786-97.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 786-797
    • Haines, N.1    Irvine, K.D.2
  • 15
    • 0037300011 scopus 로고    scopus 로고
    • O-Fucose modifications of epidermal growth factor-like repeats and thrombospondin type 1 repeats: Unusual modifications in unusual places
    • Shao L, Haltiwanger RS. O-Fucose modifications of epidermal growth factor-like repeats and thrombospondin type 1 repeats: unusual modifications in unusual places. Cell Mol Life Sci. 2003;60:241-50.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 241-250
    • Shao, L.1    Haltiwanger, R.S.2
  • 16
    • 0037547158 scopus 로고    scopus 로고
    • Protein O-fucosyltransferase 1 is an essential component of Notch signaling pathways
    • U S A
    • Shi S, Stanley P. Protein O-fucosyltransferase 1 is an essential component of Notch signaling pathways. Proc Natl Acad Sci U S A. 2003;100:5234-9.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 5234-5239
    • Shi, S.1    Stanley, P.2
  • 18
  • 19
    • 0029797439 scopus 로고    scopus 로고
    • Sialic acids. Structure, analysis, metabolism, and recognition
    • Reuter G, Gabius H-J. Sialic acids. Structure, analysis, metabolism, and recognition. Biol Chem Hoppe-Seyler. 1996;377:325-42.
    • (1996) Biol Chem Hoppe-Seyler , vol.377 , pp. 325-342
    • Reuter, G.1    Gabius, H.-J.2
  • 20
    • 0035137134 scopus 로고    scopus 로고
    • Roles of O-linked oligosaccharides in immune responses
    • Tsuboi S, Fukuda M. Roles of O-linked oligosaccharides in immune responses. BioEssays. 2001;23:43-53.
    • (2001) BioEssays , vol.23 , pp. 43-53
    • Tsuboi, S.1    Fukuda, M.2
  • 21
    • 22844433667 scopus 로고    scopus 로고
    • The chemistry and biology of mucin-type O-linked glycosylation
    • Hang HC, Bertozzi CR. The chemistry and biology of mucin-type O-linked glycosylation. Bioorg Med Chem. 2005;13:5021-34.
    • (2005) Bioorg Med Chem , vol.13 , pp. 5021-5034
    • Hang, H.C.1    Bertozzi, C.R.2
  • 23
    • 1342306245 scopus 로고    scopus 로고
    • Biases and complex patterns in the residues flanking protein N-glycosylation sites
    • Ben-Dor S, Esterman N, Rubin E, Sharon N. Biases and complex patterns in the residues flanking protein N-glycosylation sites. Glycobiology. 2004;14:95-101.
    • (2004) Glycobiology , vol.14 , pp. 95-101
    • Ben-Dor, S.1    Esterman, N.2    Rubin, E.3    Sharon, N.4
  • 24
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • Petrescu A-J, Milac A-L, Petrescu SM, Dwek RA, Wormald MR. Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding. Glycobiology. 2004;14:103-14.
    • (2004) Glycobiology , vol.14 , pp. 103-114
    • Petrescu, A.-J.1    Milac, A.-L.2    Petrescu, S.M.3    Dwek, R.A.4    Wormald, M.R.5
  • 25
    • 0002468538 scopus 로고    scopus 로고
    • Glycolipids: Structure and function
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Kopitz J. Glycolipids: structure and function. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives, London (UK)/Weinheim (Germany): Chapman & Hall; p. 163-89.
    • Glycosciences: Status and Perspectives , pp. 163-189
    • Kopitz, J.1
  • 26
    • 0015521532 scopus 로고
    • The significance of glycosylated proteins
    • Winterburn PJ, Phelps CF. The significance of glycosylated proteins. Nature. 1972;236:147-51.
    • (1972) Nature , vol.236 , pp. 147-151
    • Winterburn, P.J.1    Phelps, C.F.2
  • 27
    • 0032160197 scopus 로고    scopus 로고
    • Lectins: From obscurity into the limelight
    • Sharon N. Lectins: from obscurity into the limelight. Protein Sci. 1998;7:2042-8.
    • (1998) Protein Sci , vol.7 , pp. 2042-2048
    • Sharon, N.1
  • 29
    • 0028789599 scopus 로고    scopus 로고
    • Galactofuranose-containing glycoconjugates in trypanosamatids
    • de Lederkremer RM, Colli W. Galactofuranose-containing glycoconjugates in trypanosamatids. Glycobiology. 2003;1995:547-52.
    • (2003) Glycobiology , vol.1995 , pp. 547-552
    • De Lederkremer, R.M.1    Colli, W.2
  • 30
    • 0037301077 scopus 로고    scopus 로고
    • Galactofuranose metabolism: A potential target for antimicrobial chemotherapy
    • Pedersen LL, Turco LJ. Galactofuranose metabolism: a potential target for antimicrobial chemotherapy. Cell Mol Life Sci. 2003;60:259-66.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 259-266
    • Pedersen, L.L.1    Turco, L.J.2
  • 31
    • 0001810168 scopus 로고    scopus 로고
    • The information-storing potential of the sugar code
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Laine RA. The information-storing potential of the sugar code. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives, London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 1-14.
    • (1997) Glycosciences: Status and Perspectives , pp. 1-14
    • Laine, R.A.1
  • 32
    • 0345304414 scopus 로고    scopus 로고
    • Why are there four letters in the genetic alphabet?
    • Szathmáry E. Why are there four letters in the genetic alphabet? Nat Rev Genet. 2003;4:995-1001.
    • (2003) Nat Rev Genet , vol.4 , pp. 995-1001
    • Szathmáry, E.1
  • 33
    • 0001811291 scopus 로고    scopus 로고
    • Glycosyltransferases involved in N- and O-glycan biosynthesis
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Brockhausen I, Schachter H. Glycosyltransferases involved in N- and O-glycan biosynthesis. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 79-113.
    • (1997) Glycosciences: Status and Perspectives , pp. 79-113
    • Brockhausen, I.1    Schachter, H.2
  • 37
    • 0036637625 scopus 로고    scopus 로고
    • The galactosyltransferase family
    • Hennet T. The galactosyltransferase family. Cell Mol Life Sci. 2002;59:1081-95.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1081-1095
    • Hennet, T.1
  • 38
    • 0345099482 scopus 로고    scopus 로고
    • A new superfamily of protein-O-fucosyltransferases, α2- fucosyltransferases, and α6-fucosyltransferases: Phylogeny and identification of conserved peptide motifs
    • Martinez-Duncker I, Mollicone R, Candelier J-J, Breton C, Oriol R. A new superfamily of protein-O-fucosyltransferases, α2-fucosyltransferases, and α6-fucosyltransferases: phylogeny and identification of conserved peptide motifs. Glycobiology. 2003;13:1C-5C.
    • (2003) Glycobiology , vol.13
    • Martinez-Duncker, I.1    Mollicone, R.2    Candelier, J.-J.3    Breton, C.4    Oriol, R.5
  • 39
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc:polypeptide N- acetylgalactosaminyltransferase
    • Ten Hagen KG, Fritz TA, Tabak LA. All in the family: the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Glycobiology. 2003;13:1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 40
    • 25144501600 scopus 로고    scopus 로고
    • The animal sialyltransferases and sialyltransferase-related genes: A phylogenetic approach
    • Harduin-Lepers A, Mollicone R, Delannoy P, Oriol R. The animal sialyltransferases and sialyltransferase-related genes: a phylogenetic approach. Glycobiology. 2005;15:805-17.
    • (2005) Glycobiology , vol.15 , pp. 805-817
    • Harduin-Lepers, A.1    Mollicone, R.2    Delannoy, P.3    Oriol, R.4
  • 41
    • 0038157153 scopus 로고    scopus 로고
    • Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: A new view of a large family
    • Young WW Jr, Holcomb DR, Ten Hagen KG, Tabak LA. Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family. Glycobiology. 2003;13:549-57.
    • (2003) Glycobiology , vol.13 , pp. 549-557
    • Young Jr., W.W.1    Holcomb, D.R.2    Ten Hagen, K.G.3    Tabak, L.A.4
  • 43
    • 0034646696 scopus 로고    scopus 로고
    • Control of O-glycan branch formation. Molecular cloning and characterization of a novel thymus associated core 2 β1,6-N- acetylglucosaminyltransferase
    • Schwientek T, Yeh JC, Levery SB, Keck B, Merkx G, van Kessel AG, Fukuda M, Clausen H. Control of O-glycan branch formation. Molecular cloning and characterization of a novel thymus associated core 2 β1,6-N- acetylglucosaminyltransferase. J Biol Chem. 2000;275:11106-13.
    • (2000) J Biol Chem , vol.275 , pp. 11106-11113
    • Schwientek, T.1    Yeh, J.C.2    Levery, S.B.3    Keck, B.4    Merkx, G.5    Van Kessel, A.G.6    Fukuda, M.7    Clausen, H.8
  • 44
    • 7944231564 scopus 로고    scopus 로고
    • Strategies for drug discovery by targeting sulfation pathways
    • Hemmerich S, Verdugo D, Rath VL. Strategies for drug discovery by targeting sulfation pathways. Drug Discov Today. 2004;9:967-75.
    • (2004) Drug Discov Today , vol.9 , pp. 967-975
    • Hemmerich, S.1    Verdugo, D.2    Rath, V.L.3
  • 45
    • 14844290268 scopus 로고    scopus 로고
    • Not core 2 β1,6-N-acetylglucosaminyltransferase-2 or -3 but -1 regulates sialyl-Lewis x expression in human precursor B cells
    • Kikuchi J, Shindohara H, Nonomura C, Ando H, Takaku S, Nojiri H, Nakamura M. Not core 2 β1,6-N-acetylglucosaminyltransferase-2 or -3 but -1 regulates sialyl-Lewis x expression in human precursor B cells. Glycobiology. 2005;15:271-80.
    • (2005) Glycobiology , vol.15 , pp. 271-280
    • Kikuchi, J.1    Shindohara, H.2    Nonomura, C.3    Ando, H.4    Takaku, S.5    Nojiri, H.6    Nakamura, M.7
  • 46
    • 14044262905 scopus 로고    scopus 로고
    • Regulation of PSGL-1 interactions with L-selectin, P-selectin, and E-selectin: Role of human fucosyltransferase-IV and -VII
    • Martinez M, Joffraud M, Giraud S, Baisse B, Bernimoulin MP, Schapira M, Spertini O. Regulation of PSGL-1 interactions with L-selectin, P-selectin, and E-selectin: role of human fucosyltransferase-IV and -VII. J Biol Chem. 2005;280:5378-90.
    • (2005) J Biol Chem , vol.280 , pp. 5378-5390
    • Martinez, M.1    Joffraud, M.2    Giraud, S.3    Baisse, B.4    Bernimoulin, M.P.5    Schapira, M.6    Spertini, O.7
  • 47
    • 15444372443 scopus 로고    scopus 로고
    • An alternate core 2 β1,6-N-acetylglucosaminyltransferase selectively contributes to P-selectin ligand formation in activated CD8 T cells
    • Merzaban JS, Zuccolo J, Corbel SY, Williams MJ, Ziltener HJ. An alternate core 2 β1,6-N-acetylglucosaminyltransferase selectively contributes to P-selectin ligand formation in activated CD8 T cells. J Immunol. 2005;174:4051-9.
    • (2005) J Immunol , vol.174 , pp. 4051-4059
    • Merzaban, J.S.1    Zuccolo, J.2    Corbel, S.Y.3    Williams, M.J.4    Ziltener, H.J.5
  • 48
    • 13544268336 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein N-glycosylation
    • Yan A, Lennarz WJ. Unraveling the mechanism of protein N-glycosylation. J Biol Chem. 2005;280:3121-4.
    • (2005) J Biol Chem , vol.280 , pp. 3121-3124
    • Yan, A.1    Lennarz, W.J.2
  • 49
    • 0002784127 scopus 로고    scopus 로고
    • Topology of glycosylation - A histochemist's view
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Pavelka M. Topology of glycosylation - a histochemist's view. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 115-20.
    • (1997) Glycosciences: Status and Perspectives , pp. 115-120
    • Pavelka, M.1
  • 50
    • 2942672066 scopus 로고    scopus 로고
    • Structure-function analysis of human protein O-linked mannose β1,2-N-acetylglucosaminyltransferase 1, POMGnT1
    • Akasaka-Manya K, Manya H, Kobayashi K, Toda T, Endo T. Structure-function analysis of human protein O-linked mannose β1,2-N- acetylglucosaminyltransferase 1, POMGnT1. Biochem Biophys Res Commun. 2004;320:39-44.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 39-44
    • Akasaka-Manya, K.1    Manya, H.2    Kobayashi, K.3    Toda, T.4    Endo, T.5
  • 51
    • 0002460829 scopus 로고    scopus 로고
    • Proteoglycans: Structure and functions
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Kresse H. Proteoglycans: structure and functions. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 201-22.
    • (1997) Glycosciences: Status and Perspectives , pp. 201-222
    • Kresse, H.1
  • 52
    • 0001939486 scopus 로고    scopus 로고
    • Diverse functions and structures on heparan sulfate proteoglycan
    • Yanagishita M, Ishihara M, editors
    • Yanagishita M, Ishihara M, editors. Diverse functions and structures on heparan sulfate proteoglycan. Trends Glycosci Glycotechnol. 1998;10:51-233.
    • (1998) Trends Glycosci Glycotechnol , vol.10 , pp. 51-233
  • 53
    • 15244364003 scopus 로고    scopus 로고
    • Heparan sulfate-protein interactions: Therapeutic potential through structure-function insights
    • Coombe DR, Kett WC. Heparan sulfate-protein interactions: therapeutic potential through structure-function insights. Cell Mol Life Sci. 2005;62:410-24.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 410-424
    • Coombe, D.R.1    Kett, W.C.2
  • 54
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - As exemplified by chemokines
    • Handel TM, Johnson Z, Crown SE, Lau EK, Proudfoot AE. Regulation of protein function by glycosaminoglycans - as exemplified by chemokines. Annu Rev Biochem. 2005;74:385-410.
    • (2005) Annu Rev Biochem , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 56
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu B, Petitou M, Provasoli M, Sinay P. Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem Sci. 1988;13:221-5.
    • (1988) Trends Biochem Sci , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinay, P.4
  • 57
    • 0034191875 scopus 로고    scopus 로고
    • Proteoglycans and pattern formation: Sugar biochemistry meets developmental genetics
    • Selleck SB. Proteoglycans and pattern formation: sugar biochemistry meets developmental genetics. Trends Genet. 2000;16:206-12.
    • (2000) Trends Genet , vol.16 , pp. 206-212
    • Selleck, S.B.1
  • 58
    • 0035253193 scopus 로고    scopus 로고
    • Heparan sulfate: Decoding a dynamic multifunctional cell regulator
    • Turnbull J, Powell A, Guimond S. Heparan sulfate: decoding a dynamic multifunctional cell regulator. Trends Cell Biol. 2001;11:75-82.
    • (2001) Trends Cell Biol , vol.11 , pp. 75-82
    • Turnbull, J.1    Powell, A.2    Guimond, S.3
  • 59
    • 0031723937 scopus 로고    scopus 로고
    • Glycoproteins and their relationship to human disease
    • Brockhausen I, Schutzbach J, Kuhns W. Glycoproteins and their relationship to human disease. Acta Anat. 1998;161:36-78.
    • (1998) Acta Anat , vol.161 , pp. 36-78
    • Brockhausen, I.1    Schutzbach, J.2    Kuhns, W.3
  • 60
    • 0032830864 scopus 로고    scopus 로고
    • Molecular basis of glycoconjugate disease
    • Schachter H, editor
    • Schachter H, editor. Molecular basis of glycoconjugate disease. Biochim Biophys Acta. 1999;1455:61-418.
    • (1999) Biochim Biophys Acta , vol.1455 , pp. 61-418
  • 61
    • 0034092856 scopus 로고    scopus 로고
    • Essential roles of carbohydrate signals in development, immune response and tissue functions, as revealed by gene targeting
    • Muramatsu T. Essential roles of carbohydrate signals in development, immune response and tissue functions, as revealed by gene targeting. J Biochem. 2000;127:171-6.
    • (2000) J Biochem , vol.127 , pp. 171-176
    • Muramatsu, T.1
  • 62
    • 0035895782 scopus 로고    scopus 로고
    • Novel functions of complex carbohydrates elucidated by the mutant mice of glycosyltransferase genes
    • Furukawa K, Takamiya K, Okada M, Inoue M, Fukumoto S. Novel functions of complex carbohydrates elucidated by the mutant mice of glycosyltransferase genes. Biochim Biophys Acta. 2001;1525:1-12.
    • (2001) Biochim Biophys Acta , vol.1525 , pp. 1-12
    • Furukawa, K.1    Takamiya, K.2    Okada, M.3    Inoue, M.4    Fukumoto, S.5
  • 63
    • 0042266719 scopus 로고    scopus 로고
    • A genetic approach to mammalian glycan function
    • Lowe JJ, Marth JD. A genetic approach to mammalian glycan function. Annu Rev Biochem. 2003;72:643-91.
    • (2003) Annu Rev Biochem , vol.72 , pp. 643-691
    • Lowe, J.J.1    Marth, J.D.2
  • 64
    • 3943056897 scopus 로고    scopus 로고
    • Role of glycosylation in development
    • Haltiwanger RS, Lowe JB. Role of glycosylation in development. Annu Rev Biochem. 2004;73:491-537.
    • (2004) Annu Rev Biochem , vol.73 , pp. 491-537
    • Haltiwanger, R.S.1    Lowe, J.B.2
  • 65
    • 9444258592 scopus 로고    scopus 로고
    • When sugars guide axons: Insights from heparan sulphate proteoglycan mutants
    • Lee J-S, Chien C-B. When sugars guide axons: insights from heparan sulphate proteoglycan mutants. Nat Rev Genet. 2004;5:923-35.
    • (2004) Nat Rev Genet , vol.5 , pp. 923-935
    • Lee, J.-S.1    Chien, C.-B.2
  • 66
    • 0001072897 scopus 로고    scopus 로고
    • The biology of sulfated oligosaccharides
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Hooper LV, Manzella SM, Baenziger JU. The biology of sulfated oligosaccharides. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 261-76.
    • (1997) Glycosciences: Status and Perspectives , pp. 261-276
    • Hooper, L.V.1    Manzella, S.M.2    Baenziger, J.U.3
  • 67
    • 0037027336 scopus 로고    scopus 로고
    • Carbohydrate sulfotransferases of the GalNAc/Gal/GlcNAc6ST family
    • Grunwell JR, Bertozzi CR. Carbohydrate sulfotransferases of the GalNAc/Gal/GlcNAc6ST family. Biochemistry. 2002;41:13117-26.
    • (2002) Biochemistry , vol.41 , pp. 13117-13126
    • Grunwell, J.R.1    Bertozzi, C.R.2
  • 68
    • 0025726380 scopus 로고
    • Developmental abnormalities in transgenic mice expressing a sialic acid-specific 9-O-acetyltransferase
    • Varki A, Hooshmand F, Diaz S, Varki NM, Hedrick SM. Developmental abnormalities in transgenic mice expressing a sialic acid-specific 9-O-acetyltransferase. Cell. 1991;65:65-74.
    • (1991) Cell , vol.65 , pp. 65-74
    • Varki, A.1    Hooshmand, F.2    Diaz, S.3    Varki, N.M.4    Hedrick, S.M.5
  • 71
    • 0344393501 scopus 로고    scopus 로고
    • Conformational constraints on side chains in protein residues increase their information content
    • Bojarski AJ, Nowak M, Testa B. Conformational constraints on side chains in protein residues increase their information content. Cell Mol Life Sci. 2003;60:2526-31.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2526-2531
    • Bojarski, A.J.1    Nowak, M.2    Testa, B.3
  • 72
    • 0000815176 scopus 로고
    • Oligosaccharides: How can flexible molecules act as signals?
    • Carver JP. Oligosaccharides: how can flexible molecules act as signals? Pure Appl Chem. 1993;65:763-70.
    • (1993) Pure Appl Chem , vol.65 , pp. 763-770
    • Carver, J.P.1
  • 73
    • 0031915833 scopus 로고    scopus 로고
    • The how and why of protein-carbohydrate interaction: A primer to the theoretical concept and a guide to application in drug design
    • Gabius H-J. The how and why of protein-carbohydrate interaction: a primer to the theoretical concept and a guide to application in drug design. Pharmaceut Res. 1998;15:23-30.
    • (1998) Pharmaceut Res , vol.15 , pp. 23-30
    • Gabius, H.-J.1
  • 74
    • 0035208055 scopus 로고    scopus 로고
    • Towards defining the role of glycans as hardware in information storage and transfer: Basic principles, experimental approaches and recent progress
    • Solís D, Jiménez-Barbero J, Kaltner H, Romero A, Siebert H-C, von der Lieth C-W, Gabius H-J. Towards defining the role of glycans as hardware in information storage and transfer: basic principles, experimental approaches and recent progress. Cells Tissues Organs. 2001;168:5-23.
    • (2001) Cells Tissues Organs , vol.168 , pp. 5-23
    • Solís, D.1    Jiménez-Barbero, J.2    Kaltner, H.3    Romero, A.4    Siebert, H.-C.5    Von Der Lieth, C.-W.6    Gabius, H.-J.7
  • 77
    • 0042528660 scopus 로고    scopus 로고
    • Describing the topology of the bound ligand by transferred NOE spectroscopy and molecular modeling
    • Siebert H-C, Jiménez-Barbero J, André S, Kaltner H, Gabius H-J. Describing the topology of the bound ligand by transferred NOE spectroscopy and molecular modeling. Methods Enzymol. 2003;362:417-34.
    • (2003) Methods Enzymol , vol.362 , pp. 417-434
    • Siebert, H.-C.1    Jiménez-Barbero, J.2    André, S.3    Kaltner, H.4    Gabius, H.-J.5
  • 78
    • 0000098812 scopus 로고    scopus 로고
    • The glycosidic linkage flexibility and time-scale similarity hypotheses
    • Hardy BJ. The glycosidic linkage flexibility and time-scale similarity hypotheses. J Mol Struct. 1997;395-396:187-200.
    • (1997) J Mol Struct , vol.395-396 , pp. 187-200
    • Hardy, B.J.1
  • 79
    • 84892166712 scopus 로고
    • Einfluss der Configuration auf die Wirkung der Enzyme
    • Fischer E. Einfluss der Configuration auf die Wirkung der Enzyme. Ber Dt Chem Ges. 1894;27:2985-93.
    • (1894) Ber Dt Chem Ges , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 80
    • 0001022444 scopus 로고
    • Neutralisation of the anti-H agglutinin in eel serum by simple sugars
    • Watkins WM, Morgan WTJ. Neutralisation of the anti-H agglutinin in eel serum by simple sugars. Nature. 1952;169:825-6.
    • (1952) Nature , vol.169 , pp. 825-826
    • Watkins, W.M.1    Morgan, W.T.J.2
  • 81
    • 84965821924 scopus 로고
    • Phytohemagglutinin: An inhibitor of mitosis in cultures of normal human leukocytes
    • Nowell PC. Phytohemagglutinin: an inhibitor of mitosis in cultures of normal human leukocytes. Cancer Res. 1960;20:462-6.
    • (1960) Cancer Res , vol.20 , pp. 462-466
    • Nowell, P.C.1
  • 82
  • 83
    • 0033267884 scopus 로고    scopus 로고
    • A half century of blood-group antigen research: Some personal recollections
    • Watkins WM. A half century of blood-group antigen research: some personal recollections. Trends Glycosci Glycotechnol. 1999;11:391-411.
    • (1999) Trends Glycosci Glycotechnol , vol.11 , pp. 391-411
    • Watkins, W.M.1
  • 84
    • 0036703175 scopus 로고    scopus 로고
    • Plant lectins: Occurrence, biochemistry, functions and applications
    • Rüdiger H, Gabius H-J. Plant lectins: occurrence, biochemistry, functions and applications. Glycoconjugate J. 2001;18:589-613.
    • (2001) Glycoconjugate J , vol.18 , pp. 589-613
    • Rüdiger, H.1    Gabius, H.-J.2
  • 85
    • 0011452742 scopus 로고
    • The proteins of immune reactions
    • Neurath H, Bailey K, editors. New York: Academic Press
    • Boyd WC. The proteins of immune reactions. In: Neurath H, Bailey K, editors. The proteins, Vol. 2, Part 2. New York: Academic Press; 1954. p. 756-844.
    • (1954) The Proteins , vol.2 , Issue.2 PART , pp. 756-844
    • Boyd, W.C.1
  • 87
    • 0001124948 scopus 로고
    • Identification of snake venoms
    • Ogilvie ML, Gartner TK. Identification of snake venoms. J Herpetol. 1984;18:285-90.
    • (1984) J Herpetol , vol.18 , pp. 285-290
    • Ogilvie, M.L.1    Gartner, T.K.2
  • 88
    • 0035725755 scopus 로고    scopus 로고
    • Glycohistochemistry: The why and how of detection and localization of endogenous lectins
    • Gabius H-J. Glycohistochemistry: the why and how of detection and localization of endogenous lectins. Anat Histol Embryol. 2001;30:3-31.
    • (2001) Anat Histol Embryol , vol.30 , pp. 3-31
    • Gabius, H.-J.1
  • 89
    • 7244258916 scopus 로고    scopus 로고
    • History of lectins: From hemagglutinins to biological recognition molecules
    • Sharon N, Lis H. History of lectins: from hemagglutinins to biological recognition molecules. Glycobiology. 2004;14:53R-62R.
    • (2004) Glycobiology , vol.14
    • Sharon, N.1    Lis, H.2
  • 90
    • 0014408285 scopus 로고
    • Physical and chemical studies on ceruloplasmin. V. Metabolic studies on sialic acid-free ceruloplasmin in vivo
    • Morell AG, Irvine RA, Sternlieb I, Scheinberg IH, Ashwell G. Physical and chemical studies on ceruloplasmin. V. Metabolic studies on sialic acid-free ceruloplasmin in vivo. J Biol Chem. 1968;243:155-9.
    • (1968) J Biol Chem , vol.243 , pp. 155-159
    • Morell, A.G.1    Irvine, R.A.2    Sternlieb, I.3    Scheinberg, I.H.4    Ashwell, G.5
  • 91
    • 0016304913 scopus 로고
    • The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins
    • Hudgin RL, Pricer WEJ, Ashwell G, Stockert RJ, Morell AG. The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins. J Biol Chem. 1974;249:5536-43.
    • (1974) J Biol Chem , vol.249 , pp. 5536-5543
    • Hudgin, R.L.1    Pricer, W.E.J.2    Ashwell, G.3    Stockert, R.J.4    Morell, A.G.5
  • 92
    • 0020021127 scopus 로고
    • Carbohydrate-specific receptors of the liver
    • Ashwell G, Harford J. Carbohydrate-specific receptors of the liver. Annu Rev Biochem. 1982;51:531-54.
    • (1982) Annu Rev Biochem , vol.51 , pp. 531-554
    • Ashwell, G.1    Harford, J.2
  • 93
    • 0026062477 scopus 로고
    • Detection and functions of mammalian lectins - with emphasis on membrane lectins
    • Gabius H-J. Detection and functions of mammalian lectins - with emphasis on membrane lectins. Biochim Biophys Acta. 1991;1071:1-18.
    • (1991) Biochim Biophys Acta , vol.1071 , pp. 1-18
    • Gabius, H.-J.1
  • 94
    • 0001620683 scopus 로고    scopus 로고
    • Glycoconjugate-mediated drug targeting
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Rice KG. Glycoconjugate-mediated drug targeting. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 471-83.
    • (1997) Glycosciences: Status and Perspectives , pp. 471-483
    • Rice, K.G.1
  • 96
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/ chondroitin sulfate receptors
    • Weigel PH, Yik JHN. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/ chondroitin sulfate receptors. Biochim Biophys Acta. 2002;1572:341-2.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 341-342
    • Weigel, P.H.1    Yik, J.H.N.2
  • 97
    • 84943994070 scopus 로고
    • Chemo-immunological studies on conjugated carbohydrate-proteins. I. The synthesis of p-aminophenyl β-glucoside, p-aminophenyl β-galactoside, and their coupling with serum globulin
    • Göbel WF, Avery OT. Chemo-immunological studies on conjugated carbohydrate-proteins. I. The synthesis of p-aminophenyl β-glucoside, p-aminophenyl β-galactoside, and their coupling with serum globulin. J Exp Med. 1929;50:521-31.
    • (1929) J Exp Med , vol.50 , pp. 521-531
    • Göbel, W.F.1    Avery, O.T.2
  • 98
    • 85025399590 scopus 로고
    • Chemo-immunological studies on conjugated carbohydrate-proteins. II. Immunological specificity of synthetic sugar-protein antigens
    • Avery OT, Göbel WF. Chemo-immunological studies on conjugated carbohydrate-proteins. II. Immunological specificity of synthetic sugar-protein antigens. J Exp Med. 1929;50:533-50.
    • (1929) J Exp Med , vol.50 , pp. 533-550
    • Avery, O.T.1    Göbel, W.F.2
  • 99
    • 0001559685 scopus 로고
    • Chemical and biochemical strategies for the preparation of glycohistochemical probes and their application in lectinology
    • Gabius H-J, Gabius S. Chemical and biochemical strategies for the preparation of glycohistochemical probes and their application in lectinology. Adv Lectin Res. 1992;5:123-57.
    • (1992) Adv Lectin Res , vol.5 , pp. 123-157
    • Gabius, H.-J.1    Gabius, S.2
  • 102
    • 0033428909 scopus 로고    scopus 로고
    • C-type lectin-like domains in Caenorhabditis elegans: Predictions from the complete genome sequence
    • Drickamer K, Dodd RB. C-type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence. Glycobiology. 1999;9:1357-69.
    • (1999) Glycobiology , vol.9 , pp. 1357-1369
    • Drickamer, K.1    Dodd, R.B.2
  • 103
    • 0002844682 scopus 로고
    • A familial, plasma-associated defect of phagocytosis: A new cause of recurrent bacterial infections
    • Miller ME, Seals J, Kaye R, Levitsky LC. A familial, plasma-associated defect of phagocytosis: a new cause of recurrent bacterial infections. Lancet. 1968;11:60-2.
    • (1968) Lancet , vol.11 , pp. 60-62
    • Miller, M.E.1    Seals, J.2    Kaye, R.3    Levitsky, L.C.4
  • 104
    • 0020577072 scopus 로고
    • A cell-surface molecule involved in organ-specific homing of lymphocytes
    • Gallatin WM, Weissman IL, Butcher EC. A cell-surface molecule involved in organ-specific homing of lymphocytes. Nature. 1983;304:30-4.
    • (1983) Nature , vol.304 , pp. 30-34
    • Gallatin, W.M.1    Weissman, I.L.2    Butcher, E.C.3
  • 105
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius H-J. Animal lectins. Eur J Biochem. 1997;243:543-76.
    • (1997) Eur J Biochem , vol.243 , pp. 543-576
    • Gabius, H.-J.1
  • 109
    • 0037136403 scopus 로고    scopus 로고
    • Molecular basis of non-self recognition by the horseshoe crab tachylectins
    • Kawabata S-I, Tsuda R. Molecular basis of non-self recognition by the horseshoe crab tachylectins. Biochim Biophys Acta. 2002;1572:414-21.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 414-421
    • Kawabata, S.-I.1    Tsuda, R.2
  • 110
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris R. Principles of structures of animal and plant lectins. Biochim Biophys Acta. 2002;1572:198-208.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 111
    • 0041819753 scopus 로고    scopus 로고
    • Evolutionary analysis reveals collective properties and specificity in the C-type lectin and lectin-like domain superfamily
    • Ebner S, Sharon N, Ben-Tal N. Evolutionary analysis reveals collective properties and specificity in the C-type lectin and lectin-like domain superfamily. PROTEINS. 2003;52:44-55.
    • (2003) Proteins , vol.52 , pp. 44-55
    • Ebner, S.1    Sharon, N.2    Ben-Tal, N.3
  • 112
    • 0035968315 scopus 로고    scopus 로고
    • Human intelectin is a novel lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall
    • Tsuji S, Uehori J, Matsumoto M, Suzuki J, Mutsuhisa A, Toyoshima K, Seya T. Human intelectin is a novel lectin that recognizes galactofuranose in carbohydrate chains of bacterial cell wall. J Biol Chem. 2001;276:23456-63.
    • (2001) J Biol Chem , vol.276 , pp. 23456-23463
    • Tsuji, S.1    Uehori, J.2    Matsumoto, M.3    Suzuki, J.4    Mutsuhisa, A.5    Toyoshima, K.6    Seya, T.7
  • 113
    • 3543015529 scopus 로고    scopus 로고
    • Nucleic acid is a novel ligand for innate, immune pattern recognition collectins surfactant proteins A and D and mannose-binding lectin
    • Palaniyar N, Nedesalingam J, Clark H, Shih MJ, Dodds AW, Reid KBM. Nucleic acid is a novel ligand for innate, immune pattern recognition collectins surfactant proteins A and D and mannose-binding lectin. J Biol Chem. 2004;279:32728-36.
    • (2004) J Biol Chem , vol.279 , pp. 32728-32736
    • Palaniyar, N.1    Nedesalingam, J.2    Clark, H.3    Shih, M.J.4    Dodds, A.W.5    Reid, K.B.M.6
  • 114
    • 0021684886 scopus 로고
    • Biochemical characterization of endogenous carbohydrate-binding proteins from spontaneous murine rhabdomyosarcoma, mammary adenocarcinoma, and ovarian teratoma
    • Gabius H-J, Engelhardt R, Rehm S, Cramer F. Biochemical characterization of endogenous carbohydrate-binding proteins from spontaneous murine rhabdomyosarcoma, mammary adenocarcinoma, and ovarian teratoma. J Natl Cancer Inst. 1984;73:1349-57.
    • (1984) J Natl Cancer Inst , vol.73 , pp. 1349-1357
    • Gabius, H.-J.1    Engelhardt, R.2    Rehm, S.3    Cramer, F.4
  • 115
    • 0022916592 scopus 로고
    • Localization of endogenous lectins in normal human breast, benign breast lesions and mammary carcinomas
    • Gabius H-J, Brehler R, Schauer A, Cramer F. Localization of endogenous lectins in normal human breast, benign breast lesions and mammary carcinomas. Virch Arch [Cell Pathol]. 1986;52:107-15.
    • (1986) Virch Arch [Cell Pathol] , vol.52 , pp. 107-115
    • Gabius, H.-J.1    Brehler, R.2    Schauer, A.3    Cramer, F.4
  • 116
    • 0030766193 scopus 로고    scopus 로고
    • Concepts of tumor lectinology
    • Gabius H-J. Concepts of tumor lectinology. Cancer Investig. 1997;15:454-64.
    • (1997) Cancer Investig , vol.15 , pp. 454-464
    • Gabius, H.-J.1
  • 117
    • 0002003782 scopus 로고    scopus 로고
    • Galectins in tumor cells
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Ohannesian DW, Lotan R. Galectins in tumor cells. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 459-69.
    • (1997) Glycosciences: Status and Perspectives , pp. 459-469
    • Ohannesian, D.W.1    Lotan, R.2
  • 118
    • 0035017215 scopus 로고    scopus 로고
    • Comprehensive galectin fingerprinting in a panel of 61 human tumor cell lines by RT-PCR and its implications for diagnostic and therapeutic procedures
    • Lahm H, André S, Höflich A, Fischer JR, Sordat B, Kaltner H, Wolf E, Gabius H-J. Comprehensive galectin fingerprinting in a panel of 61 human tumor cell lines by RT-PCR and its implications for diagnostic and therapeutic procedures. J Cancer Res Clin Oncol. 2001;127:375-86.
    • (2001) J Cancer Res Clin Oncol , vol.127 , pp. 375-386
    • Lahm, H.1    André, S.2    Höflich, A.3    Fischer, J.R.4    Sordat, B.5    Kaltner, H.6    Wolf, E.7    Gabius, H.-J.8
  • 119
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper DNW. Galectinomics: finding themes in complexity. Biochim Biophys Acta. 2002;1572:209-31.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 128
    • 0038127167 scopus 로고    scopus 로고
    • Combined analysis of tumor growth pattern and expression of endogenous lectins as a prognostic tool in primary testicular cancer and its lung metastases
    • Kayser K, Höft D, Hufnagl P, Caselitz J, Zick Y, André S, Kaltner H, Gabius H-J. Combined analysis of tumor growth pattern and expression of endogenous lectins as a prognostic tool in primary testicular cancer and its lung metastases. Histol Histopathol. 2003;18:771-9.
    • (2003) Histol Histopathol , vol.18 , pp. 771-779
    • Kayser, K.1    Höft, D.2    Hufnagl, P.3    Caselitz, J.4    Zick, Y.5    André, S.6    Kaltner, H.7    Gabius, H.-J.8
  • 129
    • 0142011059 scopus 로고    scopus 로고
    • Atypical adenomatous hyperplasia of lung: Its incidence and analysis of clinical, glycohistochemical and structural features including newly defined growth regulators and vascularization
    • Kayser K, Nwoye JO, Kosjerina S, Goldmann T, Vollmer E, Kaltner H, André S, Gabius H-J. Atypical adenomatous hyperplasia of lung: its incidence and analysis of clinical, glycohistochemical and structural features including newly defined growth regulators and vascularization. Lung Cancer. 2003;42:171-82.
    • (2003) Lung Cancer , vol.42 , pp. 171-182
    • Kayser, K.1    Nwoye, J.O.2    Kosjerina, S.3    Goldmann, T.4    Vollmer, E.5    Kaltner, H.6    André, S.7    Gabius, H.-J.8
  • 131
    • 16844381878 scopus 로고    scopus 로고
    • Monitoring the expression profiles of integrins and adhesion/growth- regulatory galectins in adamantinomatous craniopharyngiomas: Their ability to regulate tumor adhesiveness to surrounding tissue and their contribution to prognosis
    • Lefranc F, Mijatovic T, Decaestecker C, Kaltner H, André S, Brotchi J, Salmon I, Gabius H-J, Kiss R. Monitoring the expression profiles of integrins and adhesion/growth-regulatory galectins in adamantinomatous craniopharyngiomas: their ability to regulate tumor adhesiveness to surrounding tissue and their contribution to prognosis. Neurosurgery. 2005;56:763-76.
    • (2005) Neurosurgery , vol.56 , pp. 763-776
    • Lefranc, F.1    Mijatovic, T.2    Decaestecker, C.3    Kaltner, H.4    André, S.5    Brotchi, J.6    Salmon, I.7    Gabius, H.-J.8    Kiss, R.9
  • 132
    • 17544373394 scopus 로고    scopus 로고
    • New roles for galectins in brain tumors: From prognostic markers to therapeutic targets
    • Stillman BN, Mischel PS, Baum LG. New roles for galectins in brain tumors: from prognostic markers to therapeutic targets. Brain Pathol. 2005;15:124-32.
    • (2005) Brain Pathol , vol.15 , pp. 124-132
    • Stillman, B.N.1    Mischel, P.S.2    Baum, L.G.3
  • 133
    • 0031311618 scopus 로고    scopus 로고
    • Graph theory and the entropy concept in histochemistry. Theoretical considerations, application in histopathology and the combination with receptor-specific approaches
    • Kayser K, Gabius H-J. Graph theory and the entropy concept in histochemistry. Theoretical considerations, application in histopathology and the combination with receptor-specific approaches. Progr Histochem Cytochem. 1997;32(2):1-106.
    • (1997) Progr Histochem Cytochem , vol.32 , Issue.2 , pp. 1-106
    • Kayser, K.1    Gabius, H.-J.2
  • 134
    • 0033020730 scopus 로고    scopus 로고
    • The application of thermodynamic principles to histochemical and morphometric tissue research: Principles and practical outline with focus on glycosciences
    • Kayser K, Gabius H-J. The application of thermodynamic principles to histochemical and morphometric tissue research: principles and practical outline with focus on glycosciences. Cell Tissue Res. 1999;296:443-55.
    • (1999) Cell Tissue Res , vol.296 , pp. 443-455
    • Kayser, K.1    Gabius, H.-J.2
  • 135
    • 0025812933 scopus 로고
    • Heparin-binding lectin of human placenta as a tool for histochemical ligand localization and ligand isolation
    • Gabius H-J, Kohnke-Godt B, Leichsenring M, Bardosi A. Heparin-binding lectin of human placenta as a tool for histochemical ligand localization and ligand isolation. J Histochem Cytochem. 1991;39:1249-56.
    • (1991) J Histochem Cytochem , vol.39 , pp. 1249-1256
    • Gabius, H.-J.1    Kohnke-Godt, B.2    Leichsenring, M.3    Bardosi, A.4
  • 136
    • 0026093104 scopus 로고
    • Lectin localization in human nerve by biochemically defined lectin-binding glycoproteins, neoglycoprotein and lectin-specific antibody
    • Gabius H-J, Wosgien B, Hendrys M, Bardosi A. Lectin localization in human nerve by biochemically defined lectin-binding glycoproteins, neoglycoprotein and lectin-specific antibody. Histochemistry. 1991;95:269-77.
    • (1991) Histochemistry , vol.95 , pp. 269-277
    • Gabius, H.-J.1    Wosgien, B.2    Hendrys, M.3    Bardosi, A.4
  • 139
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston AB, Bolam DN, Gilbert H-J, Davies GJ. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004;382:769-81.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.-J.3    Davies, G.J.4
  • 140
    • 0002438053 scopus 로고    scopus 로고
    • Lectins as tools for glycoconjugate purification and characterization
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Cummings RD. Lectins as tools for glycoconjugate purification and characterization. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 191-9.
    • (1997) Glycosciences: Status and Perspectives , pp. 191-199
    • Cummings, R.D.1
  • 141
    • 6344285924 scopus 로고    scopus 로고
    • Glycomic profiling of developmental changes in bovine testis by lectin histochemistry and further analysis of the most prominent alteration on the level of the glycoproteome by lectin blotting and lectin affinity chromatography
    • Manning JC, Seyrek K, Kaltner H, André S, Sinowatz F, Gabius H-J. Glycomic profiling of developmental changes in bovine testis by lectin histochemistry and further analysis of the most prominent alteration on the level of the glycoproteome by lectin blotting and lectin affinity chromatography. Histol Histopathol. 2004;19:1043-60.
    • (2004) Histol Histopathol , vol.19 , pp. 1043-1060
    • Manning, J.C.1    Seyrek, K.2    Kaltner, H.3    André, S.4    Sinowatz, F.5    Gabius, H.-J.6
  • 144
    • 0036436051 scopus 로고    scopus 로고
    • Thermodynamic binding studies of cell surface carbohydrate epitopes to galectin-1, -3 and -7. Evidence for differential binding specificities
    • Ahmad N, Gabius H-J, Kaltner H, André S, Kuwabara I, Liu F-T, Oscarson S, Norberg T, Brewer CF. Thermodynamic binding studies of cell surface carbohydrate epitopes to galectin-1, -3 and -7. Evidence for differential binding specificities. Can J Chem. 2002;80:1096-104.
    • (2002) Can J Chem , vol.80 , pp. 1096-1104
    • Ahmad, N.1    Gabius, H.-J.2    Kaltner, H.3    André, S.4    Kuwabara, I.5    Liu, F.-T.6    Oscarson, S.7    Norberg, T.8    Brewer, C.F.9
  • 147
    • 0345055811 scopus 로고    scopus 로고
    • Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning
    • Shin SW, Park SS, Park DS, Kim MG, Kim SC, Brey PT, Park HY. Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning. Insect Biochem Mol Biol. 1998;28:827-37.
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 827-837
    • Shin, S.W.1    Park, S.S.2    Park, D.S.3    Kim, M.G.4    Kim, S.C.5    Brey, P.T.6    Park, H.Y.7
  • 148
    • 0032993577 scopus 로고    scopus 로고
    • The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains
    • Koizumi N, Imamura M, Kadotani T, Yaoi K, Iwahana H, Sato R. The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains. FEBS Lett. 1999;443:139-43.
    • (1999) FEBS Lett , vol.443 , pp. 139-143
    • Koizumi, N.1    Imamura, M.2    Kadotani, T.3    Yaoi, K.4    Iwahana, H.5    Sato, R.6
  • 149
    • 0033166017 scopus 로고    scopus 로고
    • Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase
    • Yu X-Q, Gan H, Kanost MR. Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase. Insect Biochem Mol Biol. 1999;29:585-97.
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 585-597
    • Yu, X.-Q.1    Gan, H.2    Kanost, M.R.3
  • 150
    • 0034535375 scopus 로고    scopus 로고
    • Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to Gram-negative bacteria
    • Yu X-Q, Kanost MR. Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to Gram-negative bacteria. J Biol Chem. 2000;275:37373-81.
    • (2000) J Biol Chem , vol.275 , pp. 37373-37381
    • Yu, X.-Q.1    Kanost, M.R.2
  • 151
    • 14844282115 scopus 로고    scopus 로고
    • A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes
    • Yu X-Q, Tracy ME, Ling E, Scholz FR, Trenczek T. A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes. Insect Biochem Mol Biol. 2005;35:285-95.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 285-295
    • Yu, X.-Q.1    Tracy, M.E.2    Ling, E.3    Scholz, F.R.4    Trenczek, T.5
  • 152
    • 0035929631 scopus 로고    scopus 로고
    • Negative regulation of neuroblastoma cell growth by carbohydrate- dependent surface binding of galectin-1 and functional divergence from galectin-3
    • Kopitz J, von Reitzenstein C, André S, Kaltner H, Uhl J, Ehemann V, Cantz M, Gabius H-J. Negative regulation of neuroblastoma cell growth by carbohydrate-dependent surface binding of galectin-1 and functional divergence from galectin-3. J Biol Chem. 2001;276:35917-23.
    • (2001) J Biol Chem , vol.276 , pp. 35917-35923
    • Kopitz, J.1    Von Reitzenstein, C.2    André, S.3    Kaltner, H.4    Uhl, J.5    Ehemann, V.6    Cantz, M.7    Gabius, H.-J.8
  • 156
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • Ahmad N, Gabius H-J, André S, Kaltner H, Sabesan S, Liu B, Macaluso F, Brewer CF. Galectin-3 precipitates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J Biol Chem. 2004;279:10841-7.
    • (2004) J Biol Chem , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Sabesan, S.5    Liu, B.6    Macaluso, F.7    Brewer, C.F.8
  • 162
    • 0038044928 scopus 로고    scopus 로고
    • Ligation of siglec-8: A selective mechanism for induction of human eosinophil apoptosis
    • Nutku E, Aizawa H, Hudson SA, Bochner BS. Ligation of siglec-8: a selective mechanism for induction of human eosinophil apoptosis. Blood. 2003;101:5014-20.
    • (2003) Blood , vol.101 , pp. 5014-5020
    • Nutku, E.1    Aizawa, H.2    Hudson, S.A.3    Bochner, B.S.4
  • 163
    • 21644476233 scopus 로고    scopus 로고
    • Siglec-9 transduces apoptotic and nonapoptotic death signals into neutrophils depending on the proinflammatory cytokine environment
    • Von Gunten S, Yousefi S, Seitz M, Jakob SM, Schaffner T, Seger R, Takala J, Villiger PM, Simon H-U. Siglec-9 transduces apoptotic and nonapoptotic death signals into neutrophils depending on the proinflammatory cytokine environment. Blood. 2005;106:1423-31.
    • (2005) Blood , vol.106 , pp. 1423-1431
    • Von Gunten, S.1    Yousefi, S.2    Seitz, M.3    Jakob, S.M.4    Schaffner, T.5    Seger, R.6    Takala, J.7    Villiger, P.M.8    Simon, H.-U.9
  • 164
    • 0037136413 scopus 로고    scopus 로고
    • Mannan-binding lectin: Clinical significance and applications
    • Kilpatrick DC. Mannan-binding lectin: clinical significance and applications. Biochim Biophys Acta. 2002;1572:401-13.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 401-413
    • Kilpatrick, D.C.1
  • 165
    • 0037136421 scopus 로고    scopus 로고
    • Collectins and ficolins: Sugar pattern recognition molecules of the mammalian innate immune system
    • Lu J, Teh C, Kishore U, Reid KBM. Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system. Biochim Biophys Acta. 2002;1572:387-400.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 387-400
    • Lu, J.1    Teh, C.2    Kishore, U.3    Reid, K.B.M.4
  • 167
    • 2542423115 scopus 로고    scopus 로고
    • Mannan-binding lectin: A soluble pattern recognition molecule
    • Gadjeva M, Takahashi K, Thiel S. Mannan-binding lectin: a soluble pattern recognition molecule. Mol Immunol. 2004;41:113-21.
    • (2004) Mol Immunol , vol.41 , pp. 113-121
    • Gadjeva, M.1    Takahashi, K.2    Thiel, S.3
  • 168
    • 24744441296 scopus 로고    scopus 로고
    • Mannose-binding lectin: Biology and clinical implications
    • Worthley DL, Bardy PG, Mullighan CG. Mannose-binding lectin: biology and clinical implications. Intern Med J. 2005;35:548-55.
    • (2005) Intern Med J , vol.35 , pp. 548-555
    • Worthley, D.L.1    Bardy, P.G.2    Mullighan, C.G.3
  • 169
    • 0035797077 scopus 로고    scopus 로고
    • Biological activities of human mannose-binding lectin bound to two different ligand sugar structures, Lewis A and Lewis B antigens and high-mannose-type oligosaccharides
    • Muto S, Takada T, Matsumoto K. Biological activities of human mannose-binding lectin bound to two different ligand sugar structures, Lewis A and Lewis B antigens and high-mannose-type oligosaccharides. Biochim Biophys Acta. 2001;1527:39-46.
    • (2001) Biochim Biophys Acta , vol.1527 , pp. 39-46
    • Muto, S.1    Takada, T.2    Matsumoto, K.3
  • 170
    • 20144386133 scopus 로고    scopus 로고
    • Characterization of oligosaccharide ligands expressed on SW1116 cells recognized by mannan-binding protein. A highly fucosylated polylactosamine type N-glycan
    • Terada M, Khoo KH, Inoue R, Chen CI, Yamada K, Sakaguchi H, Kadowaki N, Ma BY, Oka S, Kawasaki T, Kawasaki N. Characterization of oligosaccharide ligands expressed on SW1116 cells recognized by mannan-binding protein. A highly fucosylated polylactosamine type N-glycan. J Biol Chem. 2005;280:10897-913.
    • (2005) J Biol Chem , vol.280 , pp. 10897-10913
    • Terada, M.1    Khoo, K.H.2    Inoue, R.3    Chen, C.I.4    Yamada, K.5    Sakaguchi, H.6    Kadowaki, N.7    Ma, B.Y.8    Oka, S.9    Kawasaki, T.10    Kawasaki, N.11
  • 171
    • 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. 2004;198:185-202.
    • (2004) Immunol Rev , vol.198 , pp. 185-202
    • Fujita, T.1    Matsushita, M.2    Endo, Y.3
  • 172
    • 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 DA, Fadden AJ, 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. 2001;276:28939-45.
    • (2001) J Biol Chem , vol.276 , pp. 28939-28945
    • Mitchell, D.A.1    Fadden, A.J.2    Drickamer, K.3
  • 173
    • 10644224262 scopus 로고    scopus 로고
    • Proteomic analysis of DC-SIGN on dendritic cells detects tetramers required for ligand binding but no association with CD4
    • Bernhard OK, Lai J, Wilkinson J, Sheil MM, Cunningham AL. Proteomic analysis of DC-SIGN on dendritic cells detects tetramers required for ligand binding but no association with CD4. J Biol Chem. 2004;279:51828-35.
    • (2004) J Biol Chem , vol.279 , pp. 51828-51835
    • Bernhard, O.K.1    Lai, J.2    Wilkinson, J.3    Sheil, M.M.4    Cunningham, A.L.5
  • 174
    • 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 GA, Colonna M, Sun PD. The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer. J Mol Biol. 2005;347:979-89.
    • (2005) J Mol Biol , vol.347 , pp. 979-989
    • Snyder, G.A.1    Colonna, M.2    Sun, P.D.3
  • 176
    • 12444347833 scopus 로고    scopus 로고
    • Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR
    • Feinberg H, Guo Y, Mitchell DA, Drickamer K, Weis WI. Extended neck regions stabilize tetramers of the receptors DC-SIGN and DC-SIGNR. J Biol Chem. 2005;280:1327-35.
    • (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
  • 177
    • 21344449731 scopus 로고    scopus 로고
    • Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin
    • Van Gisbergen KPJM, Aarnoudse CA, Meijer GA, Geijtenbeek TB, van Kooyk Y. Dendritic cells recognize tumor-specific glycosylation of carcinoembryonic antigen on colorectal cancer cells through dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin. Cancer Res. 2005;65:5935-44.
    • (2005) Cancer Res , vol.65 , pp. 5935-5944
    • Van Gisbergen, K.1    Aarnoudse, C.A.2    Meijer, G.A.3    Geijtenbeek, T.B.4    Van Kooyk, Y.5
  • 178
    • 0031784245 scopus 로고    scopus 로고
    • Animal lectins as cell adhesion molecules
    • Kaltner H, Stierstorfer B. Animal lectins as cell adhesion molecules. Acta Anat. 1998;161:162-79.
    • (1998) Acta Anat , vol.161 , pp. 162-179
    • Kaltner, H.1    Stierstorfer, B.2
  • 179
    • 0003070884 scopus 로고    scopus 로고
    • Neoglycoconjugates
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Lee RT, Lee YC. Neoglycoconjugates. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 55-77.
    • (1997) Glycosciences: Status and Perspectives , pp. 55-77
    • Lee, R.T.1    Lee, Y.C.2
  • 180
    • 0015212069 scopus 로고
    • Hepatic uptake of proteins coupled to fetuin glycopeptide
    • Rogers JC, Kornfeld S. Hepatic uptake of proteins coupled to fetuin glycopeptide. Biochem Biophys Res Commun. 1971;45:622-9.
    • (1971) Biochem Biophys Res Commun , vol.45 , pp. 622-629
    • Rogers, J.C.1    Kornfeld, S.2
  • 181
    • 0033805014 scopus 로고    scopus 로고
    • Lectin-mediated drug targeting. Selection of valency, sugar type (Gal/Lac) and spacer length for cluster glycosides as parameters to distinguish ligand binding to C-type asialoglycoprotein receptors and galectins
    • André S, Frisch B, Kaltner H, Desouza DL, Schuber F, Gabius H-J. Lectin-mediated drug targeting. Selection of valency, sugar type (Gal/Lac) and spacer length for cluster glycosides as parameters to distinguish ligand binding to C-type asialoglycoprotein receptors and galectins. Pharmaceut Res. 2000;17:985-90.
    • (2000) Pharmaceut Res , vol.17 , pp. 985-990
    • André, S.1    Frisch, B.2    Kaltner, H.3    Desouza, D.L.4    Schuber, F.5    Gabius, H.-J.6
  • 182
    • 6944224067 scopus 로고    scopus 로고
    • From pattern recognition receptor to regulator of homeostasis: The double-faced macrophage mannose receptor
    • Allavena P, Chieppa M, Monti P, Piemonti L. From pattern recognition receptor to regulator of homeostasis: the double-faced macrophage mannose receptor. Crit Rev Immunol. 2004;24:179-92.
    • (2004) Crit Rev Immunol , vol.24 , pp. 179-192
    • Allavena, P.1    Chieppa, M.2    Monti, P.3    Piemonti, L.4
  • 183
    • 12744279203 scopus 로고    scopus 로고
    • The mannose receptor: Linking homeostasis and immunity through sugar recognition
    • Taylor PR, Gordon S, Martinez-Pomares L. The mannose receptor: linking homeostasis and immunity through sugar recognition. Trends Immunol. 2005;26:104-10.
    • (2005) Trends Immunol , vol.26 , pp. 104-110
    • Taylor, P.R.1    Gordon, S.2    Martinez-Pomares, L.3
  • 184
    • 0033569567 scopus 로고    scopus 로고
    • Multiple interactions between pituitary hormones and the mannose receptor
    • Simpson DZ, Hitchen PG, Elmhirst EL, Taylor ME. Multiple interactions between pituitary hormones and the mannose receptor. Biochem J. 1999;343:403-11.
    • (1999) Biochem J , vol.343 , pp. 403-411
    • Simpson, D.Z.1    Hitchen, P.G.2    Elmhirst, E.L.3    Taylor, M.E.4
  • 185
    • 0032514687 scopus 로고    scopus 로고
    • Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy
    • U S A
    • Fritz J, Katopodis AG, Kolbinger F, Anselmetti D. Force-mediated kinetics of single P-selectin/ligand complexes observed by atomic force microscopy. Proc Natl Acad Sci U S A. 1998;95:12283-8.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 12283-12288
    • Fritz, J.1    Katopodis, A.G.2    Kolbinger, F.3    Anselmetti, D.4
  • 186
    • 0034669526 scopus 로고    scopus 로고
    • Differences in zero-force and force-driven kinetics of ligand dissociation from β-galactoside-specific proteins (plant and animal lectins, immunoglobulin G) monitored by plasmon resonance and dynamic single molecule force microscopy
    • Dettmann W, Grandbois M, André S, Benoit M, Wehle AK, Kaltner H, Gabius H-J, Gaub HE. Differences in zero-force and force-driven kinetics of ligand dissociation from β-galactoside-specific proteins (plant and animal lectins, immunoglobulin G) monitored by plasmon resonance and dynamic single molecule force microscopy. Arch Biochem Biophys. 2000;383:157-70.
    • (2000) Arch Biochem Biophys , vol.383 , pp. 157-170
    • Dettmann, W.1    Grandbois, M.2    André, S.3    Benoit, M.4    Wehle, A.K.5    Kaltner, H.6    Gabius, H.-J.7    Gaub, H.E.8
  • 187
    • 0036775765 scopus 로고    scopus 로고
    • Selectins: Lectins that initiate cell adhesion under flow
    • McEver RP. Selectins: lectins that initiate cell adhesion under flow. Curr Opin Cell Biol. 2002;14:581-6.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 581-586
    • McEver, R.P.1
  • 188
    • 0242290221 scopus 로고    scopus 로고
    • Leukocyte adhesion: An exquisite balance of hydrodynamic and molecular forces
    • Tees DFJ, Goetz DJ. Leukocyte adhesion: an exquisite balance of hydrodynamic and molecular forces. News Physiol Sci. 2003;18:186-90.
    • (2003) News Physiol Sci , vol.18 , pp. 186-190
    • Tees, D.F.J.1    Goetz, D.J.2
  • 190
    • 0030010512 scopus 로고    scopus 로고
    • Proteoglycans of the extracellular environment: Clues from the gene and protein side offer novel perspectives in molecular diversity and function
    • Iozzo RV, Murdoch AD. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 1996;10:598-614.
    • (1996) FASEB J , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 191
    • 0030963839 scopus 로고    scopus 로고
    • The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety
    • U S A
    • Aspberg A, Miura R, Bourdoulous S, Shimonaka M, Heinegård D, Schachner M, Ruoslahti E, Yamaguchi Y. The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety. Proc Natl Acad Sci U S A. 1997;94:10116-21.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 10116-10121
    • Aspberg, A.1    Miura, R.2    Bourdoulous, S.3    Shimonaka, M.4    Heinegård, D.5    Schachner, M.6    Ruoslahti, E.7    Yamaguchi, Y.8
  • 192
    • 0033575208 scopus 로고    scopus 로고
    • Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican
    • Aspberg A, Adam S, Kostka G, Timpl R, Heinegård D. Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican. J Biol Chem. 1999;274:20444-9.
    • (1999) J Biol Chem , vol.274 , pp. 20444-20449
    • Aspberg, A.1    Adam, S.2    Kostka, G.3    Timpl, R.4    Heinegård, D.5
  • 193
    • 4143100146 scopus 로고    scopus 로고
    • Structural basis for interactions between tenascins and lectican C-type lectin domains: Evidence for a crosslinking role for tenascins
    • Lundell A, Olin AI, Mörgelin M, al-Karadaghi S, Aspberg A, Logan DT. Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins. Structure. 2004;12:1495-1506.
    • (2004) Structure , vol.12 , pp. 1495-1506
    • Lundell, A.1    Olin, A.I.2    Mörgelin, M.3    Al-Karadaghi, S.4    Aspberg, A.5    Logan, D.T.6
  • 194
    • 0034079042 scopus 로고    scopus 로고
    • Biological information transfer beyond the genetic code: The sugar code
    • Gabius H-J. Biological information transfer beyond the genetic code: the sugar code. Naturwissenschaften. 2000;87:108-21.
    • (2000) Naturwissenschaften , vol.87 , pp. 108-121
    • Gabius, H.-J.1
  • 195
    • 0041289900 scopus 로고
    • A β-D-galactoside binding protein from electric organ tissue of Electrophorus dectricus
    • U S A
    • Teichberg VI, Silman I, Beitsch DD, Resheff G. A β-D-galactoside binding protein from electric organ tissue of Electrophorus dectricus. Proc Natl Acad Sci U S A. 1975;72:1383-7.
    • (1975) Proc Natl Acad Sci , vol.72 , pp. 1383-1387
    • Teichberg, V.I.1    Silman, I.2    Beitsch, D.D.3    Resheff, G.4
  • 196
    • 0026920652 scopus 로고
    • Sialic acid-binding proteins: Characterization, biological functions and application
    • Zeng F-Y, Gabius H-J. Sialic acid-binding proteins: characterization, biological functions and application. Z Naturforsch. 1992;47c:641-53.
    • (1992) Z Naturforsch , vol.47 , pp. 641-653
    • Zeng, F.-Y.1    Gabius, H.-J.2
  • 197
    • 0035884413 scopus 로고    scopus 로고
    • Carbohydrate specificity of a galectin from chicken liver (CG-16)
    • Wu AM, Wu JH, Tsai M-S, Kaltner H, Gabius H-J. Carbohydrate specificity of a galectin from chicken liver (CG-16). Biochem J. 2001;358:529-38.
    • (2001) Biochem J , vol.358 , pp. 529-538
    • Wu, A.M.1    Wu, J.H.2    Tsai, M.-S.3    Kaltner, H.4    Gabius, H.-J.5
  • 198
    • 0036846884 scopus 로고    scopus 로고
    • Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • Wu AM, Wu JH, Tsai M-S, Liu J-H, André S, Wasano K, Kaltner H, Gabius H-J. Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochem J. 2002;367:653-64.
    • (2002) Biochem J , vol.367 , pp. 653-664
    • Wu, A.M.1    Wu, J.H.2    Tsai, M.-S.3    Liu, J.-H.4    André, S.5    Wasano, K.6    Kaltner, H.7    Gabius, H.-J.8
  • 199
  • 201
    • 1942542931 scopus 로고    scopus 로고
    • Ligands for L-selectin: Homing, inflammation, and beyond
    • Rosen SD. Ligands for L-selectin: homing, inflammation, and beyond. Annu Rev Immunol. 2004;22:129-56.
    • (2004) Annu Rev Immunol , vol.22 , pp. 129-156
    • Rosen, S.D.1
  • 202
    • 2942640032 scopus 로고    scopus 로고
    • Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galb1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)
    • Wu AM, Wu JH, Liu J-H, Singh T, André S, Kaltner H, Gabius H-J. Effects of polyvalency of glycotopes and natural modifications of human blood group ABH/Lewis sugars at the Galb1-terminated core saccharides on the binding of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N). Biochimie. 2004;86:317-26.
    • (2004) Biochimie , vol.86 , pp. 317-326
    • Wu, A.M.1    Wu, J.H.2    Liu, J.-H.3    Singh, T.4    André, S.5    Kaltner, H.6    Gabius, H.-J.7
  • 203
    • 14244257721 scopus 로고    scopus 로고
    • Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells
    • Ideo H, Seko A, Yamashita K. Galectin-4 binds to sulfated glycosphingolipids and carcinoembryonic antigen in patches on the cell surface of human colon adenocarcinoma cells. J Biol Chem. 2005;280:4730-7.
    • (2005) J Biol Chem , vol.280 , pp. 4730-4737
    • Ideo, H.1    Seko, A.2    Yamashita, K.3
  • 206
    • 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 JD. Endothelial heparan sulfate deficiency impairs L-selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses. Nat Immunol. 2005;6:902-10.
    • (2005) Nat Immunol , vol.6 , pp. 902-910
    • Wang, L.1    Fuster, M.2    Sriramarao, P.3    Esko, J.D.4
  • 208
    • 0037635976 scopus 로고    scopus 로고
    • Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and X-ray scattering
    • He L, André S, Siebert H-C, Helmholz H, Niemeyer B, Gabius H-J. Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and X-ray scattering. Biophys J. 2003;85:511-24.
    • (2003) Biophys J , vol.85 , pp. 511-524
    • He, L.1    André, S.2    Siebert, H.-C.3    Helmholz, H.4    Niemeyer, B.5    Gabius, H.-J.6
  • 209
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: Crystallographic characterization of structural changes induced by single-site mutations and their impact on thermodynamics of ligand binding increasing entropie penalty
    • López-Lucendo MF, Solís D, André S, Hirabayashi J, Kasai K-I, Kaltner H, Gabius H-J, Romero A. Growth-regulatory human galectin-1: crystallographic characterization of structural changes induced by single-site mutations and their impact on thermodynamics of ligand binding increasing entropie penalty. J Mol Biol. 2004;343:957-70.
    • (2004) J Mol Biol , vol.343 , pp. 957-970
    • López-Lucendo, M.F.1    Solís, D.2    André, S.3    Hirabayashi, J.4    Kasai, K.-I.5    Kaltner, H.6    Gabius, H.-J.7    Romero, A.8
  • 210
    • 0036176858 scopus 로고    scopus 로고
    • Molecular dynamics simulations of α2,8-linked disialoside: Conformational analysis and implications for binding to proteins
    • Vasudevan SV, Balaji PV. Molecular dynamics simulations of α2,8-linked disialoside: conformational analysis and implications for binding to proteins. Biopolymers. 2002;63:168-80.
    • (2002) Biopolymers , vol.63 , pp. 168-180
    • Vasudevan, S.V.1    Balaji, P.V.2
  • 212
    • 0032080122 scopus 로고    scopus 로고
    • 1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture
    • 1, a product of the growth-controlling activity of a cell surface ganglioside sialidase, on human neuroblastoma cells in culture. J Biol Chem. 1998;273:11205-11.
    • (1998) J Biol Chem , vol.273 , pp. 11205-11211
    • Kopitz, J.1    Von Reitzenstein, C.2    Burchert, M.3    Cantz, M.4    Gabius, H.-J.5
  • 215
    • 0021749885 scopus 로고
    • A dominant mutation to ricin resistance in Chinese hamster ovary cells induces UDP-GlcNAc:glycopeptide β-4-N-acetylglucosaminyltransferase III activity
    • Campbell C, Stanley P. A dominant mutation to ricin resistance in Chinese hamster ovary cells induces UDP-GlcNAc:glycopeptide β-4-N- acetylglucosaminyltransferase III activity. J Biol Chem. 1984;259:13370-8.
    • (1984) J Biol Chem , vol.259 , pp. 13370-13378
    • Campbell, C.1    Stanley, P.2
  • 217
    • 1642499128 scopus 로고    scopus 로고
    • Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo
    • André S, Unverzagt C, Kojima S, Frank M, Seifert J, Fink C, Kayser K, von der Lieth C-W, Gabius H-J. Determination of modulation of ligand properties of synthetic complex-type biantennary N-glycans by introduction of bisecting GlcNAc in silico, in vitro and in vivo. Eur J Biochem. 2004;271:118-34.
    • (2004) Eur J Biochem , vol.271 , pp. 118-134
    • André, S.1    Unverzagt, C.2    Kojima, S.3    Frank, M.4    Seifert, J.5    Fink, C.6    Kayser, K.7    Von Der Lieth, C.-W.8    Gabius, H.-J.9
  • 218
    • 0031281271 scopus 로고    scopus 로고
    • Neoglycoproteins with the synthetic complex biantennary nonasaccharide or its α2,3/α2,6-sialylated derivatives: Their preparation, the assessment of their ligand properties for purified lectins, for tumor cells in vitro and in tissue sections and their biodistribution in tumor-bearing mice
    • André S, Unverzagt C, Kojima S, Dong X, Fink C, Kayser K, Gabius H-J. Neoglycoproteins with the synthetic complex biantennary nonasaccharide or its α2,3/α2,6-sialylated derivatives: their preparation, the assessment of their ligand properties for purified lectins, for tumor cells in vitro and in tissue sections and their biodistribution in tumor-bearing mice. Bioconjugate Chem. 1997;8:845-55.
    • (1997) Bioconjugate Chem , vol.8 , pp. 845-855
    • André, S.1    Unverzagt, C.2    Kojima, S.3    Dong, X.4    Fink, C.5    Kayser, K.6    Gabius, H.-J.7
  • 219
    • 0037122782 scopus 로고    scopus 로고
    • Structure-activity profiles of complex biantennary glycans with core fucosylation and with/without additional α2,3/α2,6-sialylation: Synthesis of neoglycoproteins and their properties in lectin assays, cell binding, and organ uptake
    • Unverzagt C, André S, Seifert J, Kojima S, Fink C, Srikrishna G, Freeze H, Kayser K, Gabius H-J. Structure-activity profiles of complex biantennary glycans with core fucosylation and with/without additional α2,3/α2,6-sialylation: synthesis of neoglycoproteins and their properties in lectin assays, cell binding, and organ uptake. J Med Chem. 2002;45:478-91.
    • (2002) J Med Chem , vol.45 , pp. 478-491
    • Unverzagt, C.1    André, S.2    Seifert, J.3    Kojima, S.4    Fink, C.5    Srikrishna, G.6    Freeze, H.7    Kayser, K.8    Gabius, H.-J.9
  • 220
    • 17444365412 scopus 로고    scopus 로고
    • Introduction of extended LEC14-type branching into core-fucosylated biantennary N-glycan: Glycoengineering for enhanced cell binding and serum clearance of the neoglycoprotein
    • André S, Kojima S, Prahl I, Lensch M, Unverzagt C, Gabius H-J. Introduction of extended LEC14-type branching into core-fucosylated biantennary N-glycan: glycoengineering for enhanced cell binding and serum clearance of the neoglycoprotein. FEBS J. 2005;272:1986-98.
    • (2005) FEBS J , vol.272 , pp. 1986-1998
    • André, S.1    Kojima, S.2    Prahl, I.3    Lensch, M.4    Unverzagt, C.5    Gabius, H.-J.6
  • 221
    • 0025147414 scopus 로고
    • Defined geometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat hepatocytes
    • Rice KG, Weisz OA, Barthel T, Lee RT, Lee YC. Defined geometry of binding between triantennary glycopeptide and the asialoglycoprotein receptor of rat hepatocytes. J Biol Chem. 1990;265:18429-34.
    • (1990) J Biol Chem , vol.265 , pp. 18429-18434
    • Rice, K.G.1    Weisz, O.A.2    Barthel, T.3    Lee, R.T.4    Lee, Y.C.5
  • 222
    • 0027344590 scopus 로고
    • Oligosaccharide valency and conformations in determining binding to the asialoglycoprotein receptor of rat hepatocytes
    • Rice KG, Lee YC. Oligosaccharide valency and conformations in determining binding to the asialoglycoprotein receptor of rat hepatocytes. Adv Enzymol. 1993;66:41-83.
    • (1993) Adv Enzymol , vol.66 , pp. 41-83
    • Rice, K.G.1    Lee, Y.C.2
  • 223
    • 0025887737 scopus 로고
    • Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer
    • Rice KG, Wu P, Brand L, Lee YC. Interterminal distance and flexibility of a triantennary glycopeptide as measured by resonance energy transfer. Biochemistry. 1991;30:6646-55.
    • (1991) Biochemistry , vol.30 , pp. 6646-6655
    • Rice, K.G.1    Wu, P.2    Brand, L.3    Lee, Y.C.4
  • 224
    • 0026052393 scopus 로고
    • Differential flexibilities in three branches of an N-linked triantennary glycopeptide
    • U S A
    • Wu P, Rice KG, Brand L, Lee YC. Differential flexibilities in three branches of an N-linked triantennary glycopeptide. Proc Natl Acad Sci U S A. 1991;88:9355-9.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 9355-9359
    • Wu, P.1    Rice, K.G.2    Brand, L.3    Lee, Y.C.4
  • 225
    • 0027308234 scopus 로고
    • Modification of oligosaccharide antenna flexibility induced by exoglycosidase trimming
    • Rice KG, Wu P, Brand L, Lee YC. Modification of oligosaccharide antenna flexibility induced by exoglycosidase trimming. Biochemistry. 1993;32:7264-70.
    • (1993) Biochemistry , vol.32 , pp. 7264-7270
    • Rice, K.G.1    Wu, P.2    Brand, L.3    Lee, Y.C.4
  • 226
    • 0030064740 scopus 로고    scopus 로고
    • Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide
    • Stubbs HJ, Lih JJ, Gustafson TL, Rice KG. Influence of core fucosylation on the flexibility of a biantennary N-linked oligosaccharide. Biochemistry. 1996;35:937-47.
    • (1996) Biochemistry , vol.35 , pp. 937-947
    • Stubbs, H.J.1    Lih, J.J.2    Gustafson, T.L.3    Rice, K.G.4
  • 227
    • 13344269017 scopus 로고    scopus 로고
    • Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues
    • Wu P, Lee KB, Lee YC, Brand L. Solution conformations of a biantennary glycopeptide and a series of its exoglycosidase products from sequential trimming of sugar residues. J Biol Chem. 1996;271:1470-4.
    • (1996) J Biol Chem , vol.271 , pp. 1470-1474
    • Wu, P.1    Lee, K.B.2    Lee, Y.C.3    Brand, L.4
  • 228
    • 0021208290 scopus 로고
    • Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis
    • Yamashita K, Ohkura T, Tachibana Y, Takasaki S, Kobata A. Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis. J Biol Chem. 1984;259:10834-40.
    • (1984) J Biol Chem , vol.259 , pp. 10834-10840
    • Yamashita, K.1    Ohkura, T.2    Tachibana, Y.3    Takasaki, S.4    Kobata, A.5
  • 229
    • 0023654072 scopus 로고
    • Branch specificity of bovine colostrum CMP-sialic acid: Galβ1-4GlcNAc-R α2-6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type
    • Joziasse DH, Schiphorst WECM, van den Eijnden DH, van Kuik JA, van Halbeek H, Vliegenthart JFG. Branch specificity of bovine colostrum CMP-sialic acid: Galβ1-4GlcNAc-R α2-6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type. J Biol Chem. 1987;262:2025-33.
    • (1987) J Biol Chem , vol.262 , pp. 2025-2033
    • Joziasse, D.H.1    Schiphorst, W.E.C.M.2    Van Den Eijnden, D.H.3    Van Kuik, J.A.4    Van Halbeek, H.5    Vliegenthart, J.F.G.6
  • 230
    • 0033546414 scopus 로고    scopus 로고
    • Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of i-extension enzyme and β1,4- galactosyltransferase I
    • Ujita M, McAuliffe J, Hindsgaul O, Sasaki K, Fukuda MN, Fukuda M. Poly-N-acetyllactosamine synthesis in branched N-glycans is controlled by complemental branch specificity of i-extension enzyme and β1,4- galactosyltransferase I. J Biol Chem. 1999;274:16717-26.
    • (1999) J Biol Chem , vol.274 , pp. 16717-16726
    • Ujita, M.1    McAuliffe, J.2    Hindsgaul, O.3    Sasaki, K.4    Fukuda, M.N.5    Fukuda, M.6
  • 231
    • 27244458793 scopus 로고    scopus 로고
    • Characterization of a novel galactose β1,3-N- acetylglucosaminyltransferase (β3Gn-T8): The complex formation of β3Gn-T2 and β3Gn-T8 enhances enzymatic activity
    • Seko A, Yamashita K. Characterization of a novel galactose β1,3-N-acetylglucosaminyltransferase (β3Gn-T8): the complex formation of β3Gn-T2 and β3Gn-T8 enhances enzymatic activity. Glycobiology. 2005;15:943-51.
    • (2005) Glycobiology , vol.15 , pp. 943-951
    • Seko, A.1    Yamashita, K.2
  • 232
    • 1642576028 scopus 로고    scopus 로고
    • Core 2 branching β1,6-N-acetylglucosaminyltransferase and high endothelial venule-restricted sulfotransferase collaboratively control lymphocyte homing
    • Hiraoka N, Kawashima H, Petryniak B, Nakayama J, Mitoma J, Marth JD, Lowe JB, Fukuda M. Core 2 branching β1,6-N-acetylglucosaminyltransferase and high endothelial venule-restricted sulfotransferase collaboratively control lymphocyte homing. J Biol Chem. 2004;279:3058-67.
    • (2004) J Biol Chem , vol.279 , pp. 3058-3067
    • Hiraoka, N.1    Kawashima, H.2    Petryniak, B.3    Nakayama, J.4    Mitoma, J.5    Marth, J.D.6    Lowe, J.B.7    Fukuda, M.8
  • 233
    • 0036793242 scopus 로고    scopus 로고
    • Sweet 'n' sour: The impact of differential glycosylation on T cell responses
    • Daniels MA, Hogquist KA, Stephen CJ. Sweet 'n' sour: the impact of differential glycosylation on T cell responses. Nat Immunol. 2002;3:903-10.
    • (2002) Nat Immunol , vol.3 , pp. 903-910
    • Daniels, M.A.1    Hogquist, K.A.2    Stephen, C.J.3
  • 234
    • 12344315867 scopus 로고    scopus 로고
    • Galectin-1 supports survival of naive T cells without promoting cell proliferation
    • Endharti AT, Zhou YW, Nakashima I, Suzuki H. Galectin-1 supports survival of naive T cells without promoting cell proliferation. Eur J Immunol. 2005;35:86-97.
    • (2005) Eur J Immunol , vol.35 , pp. 86-97
    • Endharti, A.T.1    Zhou, Y.W.2    Nakashima, I.3    Suzuki, H.4
  • 235
    • 0012061680 scopus 로고    scopus 로고
    • Lactose-containing starburst dendrimers: Influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties
    • André S, Cejas Ortega PJ, Alamino Perez M, Roy R, Gabius H-J. Lactose-containing starburst dendrimers: influence of dendrimer generation and binding-site orientation of receptors (plant/animal lectins and immunoglobulins) on binding properties. Glycobiology. 1999;9:1253-61.
    • (1999) Glycobiology , vol.9 , pp. 1253-1261
    • André, S.1    Cejas Ortega, P.J.2    Alamino Perez, M.3    Roy, R.4    Gabius, H.-J.5
  • 236
    • 0035814138 scopus 로고    scopus 로고
    • Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates
    • André S, Pieters RJ, Vrasidas I, Kaltner H, Kuwabara I, Liu F-T, Liskamp RMJ, Gabius H-J. Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates. ChemBioChem. 2001;2:822-30.
    • (2001) ChemBioChem , vol.2 , pp. 822-830
    • André, S.1    Pieters, R.J.2    Vrasidas, I.3    Kaltner, H.4    Kuwabara, I.5    Liu, F.-T.6    Liskamp, R.M.J.7    Gabius, H.-J.8
  • 237
    • 0036462596 scopus 로고    scopus 로고
    • Thermodynamic studies of lectin-carbohydrate interactions by isothermal titration calorimetry
    • Dam TK, Brewer CF. Thermodynamic studies of lectin-carbohydrate interactions by isothermal titration calorimetry. Chem Rev. 2002;102:387-429.
    • (2002) Chem Rev , vol.102 , pp. 387-429
    • Dam, T.K.1    Brewer, C.F.2
  • 238
    • 0347946755 scopus 로고    scopus 로고
    • A decade of glycodendrimer chemistry
    • Roy R. A decade of glycodendrimer chemistry. Trends Glycosci Glycotechnol. 2003;15:291-310.
    • (2003) Trends Glycosci Glycotechnol , vol.15 , pp. 291-310
    • Roy, R.1
  • 239
    • 0842328412 scopus 로고    scopus 로고
    • Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets
    • André S, Kaltner H, Furuike T, Nishimura S-I, Gabius H-J. Persubstituted cyclodextrin-based glycoclusters as inhibitors of protein-carbohydrate recognition using purified plant and mammalian lectins and wild-type and lectin-gene-transfected tumor cells as targets. Bioconjugate Chem. 2004;15:87-98.
    • (2004) Bioconjugate Chem , vol.15 , pp. 87-98
    • André, S.1    Kaltner, H.2    Furuike, T.3    Nishimura, S.-I.4    Gabius, H.-J.5
  • 240
    • 24944450621 scopus 로고    scopus 로고
    • Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants
    • Dam TK, Gabius H-J, André S, Kaltner H, Lensch M, Brewer CF. Galectins bind to the multivalent glycoprotein asialofetuin with enhanced affinities and a gradient of decreasing binding constants. Biochemistry. 2005;44:12564-71.
    • (2005) Biochemistry , vol.44 , pp. 12564-12571
    • Dam, T.K.1    Gabius, H.-J.2    André, S.3    Kaltner, H.4    Lensch, M.5    Brewer, C.F.6
  • 241
    • 0028206055 scopus 로고
    • The oligosaccharide binding specificities of CD22b, a sialic acid-specific lectin of B cells
    • Powell LD, Varki A. The oligosaccharide binding specificities of CD22b, a sialic acid-specific lectin of B cells. J Biol Chem. 1994;169:10628-36.
    • (1994) J Biol Chem , vol.169 , pp. 10628-10636
    • Powell, L.D.1    Varki, A.2
  • 242
    • 0028292786 scopus 로고
    • Differential recognition by conglutinin and mannan-binding protein of N-glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B
    • Solís D, Feizi T, Yuen CT, Lawson AM, Harrison RA, Loveless RW. Differential recognition by conglutinin and mannan-binding protein of N-glycans presented on neoglycolipids and glycoproteins with special reference to complement glycoprotein C3 and ribonuclease B. J Biol Chem. 1994;269:11555-62.
    • (1994) J Biol Chem , vol.269 , pp. 11555-11562
    • Solís, D.1    Feizi, T.2    Yuen, C.T.3    Lawson, A.M.4    Harrison, R.A.5    Loveless, R.W.6
  • 243
    • 0028928442 scopus 로고
    • Binding of human plasma sialoglycoproteins by the B cell-specific lectin CD22
    • Hanasaki K, Powell LD, Varki A. Binding of human plasma sialoglycoproteins by the B cell-specific lectin CD22. J Biol Chem. 1995;270:7543-50.
    • (1995) J Biol Chem , vol.270 , pp. 7543-7550
    • Hanasaki, K.1    Powell, L.D.2    Varki, A.3
  • 244
    • 0032518583 scopus 로고    scopus 로고
    • Role of carbohydrate and protein in the binding of tissue-type plasminogen activator to the human mannose receptor
    • Moorman F, Barrett-Bergshoeff MM, Rijken DC. Role of carbohydrate and protein in the binding of tissue-type plasminogen activator to the human mannose receptor. Eur J Biochem. 1998;251:107-13.
    • (1998) Eur J Biochem , vol.251 , pp. 107-113
    • Moorman, F.1    Barrett-Bergshoeff, M.M.2    Rijken, D.C.3
  • 247
    • 18244389671 scopus 로고    scopus 로고
    • Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN
    • Van Gisbergen KP, Sanchez-Hernandez M, Geijtenbeek TB, van Kooyk Y. Neutrophils mediate immune modulation of dendritic cells through glycosylation-dependent interactions between Mac-1 and DC-SIGN. J Exp Med. 2005;201:1281-92.
    • (2005) J Exp Med , vol.201 , pp. 1281-1292
    • Van Gisbergen, K.P.1    Sanchez-Hernandez, M.2    Geijtenbeek, T.B.3    Van Kooyk, Y.4
  • 248
    • 0031572518 scopus 로고    scopus 로고
    • Cell type-specific glycoforms of FcγRIIIa (CD16): Differential ligand binding
    • Edberg JC, Kimberly RP. Cell type-specific glycoforms of FcγRIIIa (CD16): differential ligand binding. J Immunol. 1997;159:3849-57.
    • (1997) J Immunol , vol.159 , pp. 3849-3857
    • Edberg, J.C.1    Kimberly, R.P.2
  • 249
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • Rabinovich GA, Rubinstein N, Toscano M. Role of galectins in inflammatory and immunomodulatory processes. Biochim Biophys Acta. 2002;1572:274-84.
    • (2002) Biochim Biophys Acta , vol.1572 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.3
  • 250
    • 0037137493 scopus 로고    scopus 로고
    • UDP-N-acetylglucosamine: α-6-D-mannoside β1,6 N-acetylglucosaminyltransferase V (Mgat5) deficient mice
    • Dennis JW, Pawling J, Cheung P, Partridge E, Demetriou M. UDP-N-acetylglucosamine: α-6-D-mannoside β1,6 N- acetylglucosaminyltransferase V (Mgat5) deficient mice. Biochim Biophys Acta. 2002;1573:414-22.
    • (2002) Biochim Biophys Acta , vol.1573 , pp. 414-422
    • Dennis, J.W.1    Pawling, J.2    Cheung, P.3    Partridge, E.4    Demetriou, M.5
  • 251
    • 0037039367 scopus 로고    scopus 로고
    • The glycosynapse
    • U S A
    • Hakomori S-I. The glycosynapse. Proc Natl Acad Sci U S A. 2002;99:225-32.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 225-232
    • Hakomori, S.-I.1
  • 252
    • 0036462601 scopus 로고    scopus 로고
    • Protein N-glycosylation along the secretory pathway: Relationship to organelle topography and function, protein quality control, and cell interactions
    • Roth J. Protein N-glycosylation along the secretory pathway: relationship to organelle topography and function, protein quality control, and cell interactions. Chem Rev. 2002;102:285-303.
    • (2002) Chem Rev , vol.102 , pp. 285-303
    • Roth, J.1
  • 254
    • 0141814712 scopus 로고    scopus 로고
    • A novel role for N-glycans in the ERAD system
    • Yoshida Y. A novel role for N-glycans in the ERAD system. J Biochem. 2003;134:183-90.
    • (2003) J Biochem , vol.134 , pp. 183-190
    • Yoshida, Y.1
  • 255
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem. 2004;73:1019-49.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 256
    • 20444429745 scopus 로고    scopus 로고
    • A window of opportunity: Timing protein degradation by trimming of sugars and ubiquitins
    • Lederkremer GZ, Glickman MH. A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem Sci. 2005;30:297-303.
    • (2005) Trends Biochem Sci , vol.30 , pp. 297-303
    • Lederkremer, G.Z.1    Glickman, M.H.2
  • 258
    • 18244371937 scopus 로고    scopus 로고
    • Thermodynamic analysis oi interactions between N-linked sugar chains and F-box protein Fbs1
    • Hagihara S, Totani K, Matsuo I, Ito Y. Thermodynamic analysis oi interactions between N-linked sugar chains and F-box protein Fbs1. J Med Chem. 2005;48:3126-9.
    • (2005) J Med Chem , vol.48 , pp. 3126-3129
    • Hagihara, S.1    Totani, K.2    Matsuo, I.3    Ito, Y.4
  • 259
    • 16844369621 scopus 로고    scopus 로고
    • Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates
    • Yoshida Y, Adachi E, Fukiya K, Iwai K, Tanaka K. Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates. EMBO Rep. 2005;6:239-44.
    • (2005) EMBO Rep , vol.6 , pp. 239-244
    • Yoshida, Y.1    Adachi, E.2    Fukiya, K.3    Iwai, K.4    Tanaka, K.5
  • 260
    • 0035478934 scopus 로고    scopus 로고
    • Dissecting glycoprotein quality control in the secretory pathway
    • Cabral CM, Liu Y, Sifers RN. Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci. 2001;26:619-24.
    • (2001) Trends Biochem Sci , vol.26 , pp. 619-624
    • Cabral, C.M.1    Liu, Y.2    Sifers, R.N.3
  • 261
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags
    • Hebert DN, Garman SC, Molinari M. The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 2005;15:364-70.
    • (2005) Trends Cell Biol , vol.15 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 262
    • 0026756506 scopus 로고
    • Sequence and expression oi a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120
    • U S A
    • Curtis BM, Scharnowske S, Watson AJ. Sequence and expression oi a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120. Proc Natl Acad Sci U S A. 1992;89:8356-60.
    • (1992) Proc Natl Acad Sci , vol.89 , pp. 8356-8360
    • Curtis, B.M.1    Scharnowske, S.2    Watson, A.J.3
  • 265
    • 13844322103 scopus 로고    scopus 로고
    • Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation
    • Koppel EA, van Gisbergen KP, Geijtenbeek TB, van Kooyk Y. Distinct functions of DC-SIGN and its homologues L-SIGN (DC-SIGNR) and mSIGNR1 in pathogen recognition and immune regulation. Cell Microbiol. 2005;7:157-65.
    • (2005) Cell Microbiol , vol.7 , pp. 157-165
    • Koppel, E.A.1    Van Gisbergen, K.P.2    Geijtenbeek, T.B.3    Van Kooyk, Y.4
  • 267
    • 0038558249 scopus 로고    scopus 로고
    • Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2
    • Gantner BN, Simmons RM, Canavera SJ, Akira S, Underhill DM. Collaborative induction of inflammatory responses by dectin-1 and Toll-like receptor 2. J Exp Med. 2003;197:1107-17.
    • (2003) J Exp Med , vol.197 , pp. 1107-1117
    • Gantner, B.N.1    Simmons, R.M.2    Canavera, S.J.3    Akira, S.4    Underhill, D.M.5
  • 271
    • 18844412640 scopus 로고    scopus 로고
    • The human β-glucan receptor is widely expressed and functionally equivalent to murine dectin-1 on primary cells
    • Willment JA, Marshall AS, Reid DM, Williams DL, Wong SY, Gordon S, Brown GD. The human β-glucan receptor is widely expressed and functionally equivalent to murine dectin-1 on primary cells. Eur J Immunol. 2005;35:1539-47.
    • (2005) Eur J Immunol , vol.35 , pp. 1539-1547
    • Willment, J.A.1    Marshall, A.S.2    Reid, D.M.3    Williams, D.L.4    Wong, S.Y.5    Gordon, S.6    Brown, G.D.7
  • 273
    • 0028178318 scopus 로고
    • Non-carbohydrate binding partners/domains of animal lectins
    • Gabius H-J. Non-carbohydrate binding partners/domains of animal lectins. Int J Biochem. 1994;26:469-77.
    • (1994) Int J Biochem , vol.26 , pp. 469-477
    • Gabius, H.-J.1
  • 274
    • 0034650484 scopus 로고    scopus 로고
    • A peptide mimic of E-selectin ligand inhibits sialyl Lewis X-dependent lung colonization of tumor cells
    • Fukuda MN, Ohyama C, Lowitz K, Matsuo O, Pasqualini R, Ruoslahti E, Fukuda M. A peptide mimic of E-selectin ligand inhibits sialyl Lewis X-dependent lung colonization of tumor cells. Cancer Res. 2000;60:450-6.
    • (2000) Cancer Res , vol.60 , pp. 450-456
    • Fukuda, M.N.1    Ohyama, C.2    Lowitz, K.3    Matsuo, O.4    Pasqualini, R.5    Ruoslahti, E.6    Fukuda, M.7
  • 275
    • 0034671747 scopus 로고    scopus 로고
    • The enamel protein amelogenin binds to the N-acetyl-D-glucosamine- mimicking peptide motif of cytokeratins
    • Ravindranath RM, Tam WY, Nguyen P, Fincham AG. The enamel protein amelogenin binds to the N-acetyl-D-glucosamine-mimicking peptide motif of cytokeratins. J Biol Chem. 2000;275:39654-61.
    • (2000) J Biol Chem , vol.275 , pp. 39654-39661
    • Ravindranath, R.M.1    Tam, W.Y.2    Nguyen, P.3    Fincham, A.G.4
  • 278
    • 2342508517 scopus 로고    scopus 로고
    • Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP
    • Rotblat B, Niv H, André S, Kaltner H, Gabius H-J, Kloog Y. Galectin-1(L11A) predicted from a computed galectin-1 farnesyl-binding pocket selectively inhibits Ras-GTP. Cancer Res. 2004;64:3112-8.
    • (2004) Cancer Res , vol.64 , pp. 3112-3118
    • Rotblat, B.1    Niv, H.2    André, S.3    Kaltner, H.4    Gabius, H.-J.5    Kloog, Y.6
  • 280
    • 10444275602 scopus 로고    scopus 로고
    • Identification of peptide ligands for malignancy- and growth-regulating galectins using random phage-display and designed peptide libraries
    • André S, Arnusch CJ, Kuwabara I, Russwurm R, Kaltner H, Gabius H-J, Pieters RJ. Identification of peptide ligands for malignancy- and growth-regulating galectins using random phage-display and designed peptide libraries. BioorgMed Chem. 2005;13:563-73.
    • (2005) BioorgMed Chem , vol.13 , pp. 563-573
    • André, S.1    Arnusch, C.J.2    Kuwabara, I.3    Russwurm, R.4    Kaltner, H.5    Gabius, H.-J.6    Pieters, R.J.7
  • 281
    • 33646554216 scopus 로고    scopus 로고
    • A guide to signaling pathways connecting protein-glycan interaction with the emerging verstile effector functionality of mammalian lectins
    • In press
    • Villalobo A, Nogales-Gonzalés A, Gabius H-J. A guide to signaling pathways connecting protein-glycan interaction with the emerging verstile effector functionality of mammalian lectins. Trends Glycosci Glycotechnol. In press 2006.
    • (2006) Trends Glycosci Glycotechnol
    • Villalobo, A.1    Nogales-Gonzalés, A.2    Gabius, H.-J.3
  • 282
    • 0029054487 scopus 로고
    • Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading
    • White TK, Zhu Q, Tanzer ML. Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J Biol Chem. 1995;270:15926-8.
    • (1995) J Biol Chem , vol.270 , pp. 15926-15928
    • White, T.K.1    Zhu, Q.2    Tanzer, M.L.3
  • 283
    • 2342513408 scopus 로고    scopus 로고
    • Calreticulin on the mouse egg surface mediates transmembrane signaling linked to cell cycle resumption
    • Tutuncu L, Stein P, Ord TS, Jorgez CJ, Williams CJ. Calreticulin on the mouse egg surface mediates transmembrane signaling linked to cell cycle resumption. Dev Biol. 2004;270:246-60.
    • (2004) Dev Biol , vol.270 , pp. 246-260
    • Tutuncu, L.1    Stein, P.2    Ord, T.S.3    Jorgez, C.J.4    Williams, C.J.5
  • 286
    • 0037020243 scopus 로고    scopus 로고
    • Galectin-1 augments Ras activation and diverts Ras signals to Raf-1 at the expense of phosphoinositide 3-kinase
    • Elad-Sfadia G, Haklai R, Ballan E, Gabius H-J, Kloog Y. Galectin-1 augments Ras activation and diverts Ras signals to Raf-1 at the expense of phosphoinositide 3-kinase. J Biol Chem. 2002;277:37169-75.
    • (2002) J Biol Chem , vol.277 , pp. 37169-37175
    • Elad-Sfadia, G.1    Haklai, R.2    Ballan, E.3    Gabius, H.-J.4    Kloog, Y.5
  • 287
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J Cell Biol. 2003;160:165-70.
    • (2003) J Cell Biol , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 290
    • 0022132140 scopus 로고
    • Receptor for the cell binding site of discoidin I
    • Gabius H-J, Springer WR, Barondes SH. Receptor for the cell binding site of discoidin I. Cell. 1985;42:449-56.
    • (1985) Cell , vol.42 , pp. 449-456
    • Gabius, H.-J.1    Springer, W.R.2    Barondes, S.H.3
  • 291
    • 0030029478 scopus 로고    scopus 로고
    • Analysis of the sugar specificity and molecular location of the β-glucan-binding lectin site of complement receptor type 3
    • Thornton BP, Vetvicka V, Pitman M, Goldman RC, Ross GD. Analysis of the sugar specificity and molecular location of the β-glucan-binding lectin site of complement receptor type 3. J Immunol. 1996;156:1235-46.
    • (1996) J Immunol , vol.156 , pp. 1235-1246
    • Thornton, B.P.1    Vetvicka, V.2    Pitman, M.3    Goldman, R.C.4    Ross, G.D.5
  • 294
    • 0037235543 scopus 로고    scopus 로고
    • Multifunctional proteins: Examples of gene sharing
    • Jeffery CJ. Multifunctional proteins: examples of gene sharing. Ann Med. 2003;35:28-35.
    • (2003) Ann Med , vol.35 , pp. 28-35
    • Jeffery, C.J.1
  • 296
    • 8444221915 scopus 로고    scopus 로고
    • Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase
    • Wang W, Roach PJ. Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase. Biochem Biophys Res Commun. 2004;325:726-30.
    • (2004) Biochem Biophys Res Commun , vol.325 , pp. 726-730
    • Wang, W.1    Roach, P.J.2
  • 297
    • 0034888753 scopus 로고    scopus 로고
    • β-Galactosidases with a lectin-like domain are expressed in strawberry
    • Trainotti L, Spinello R, Piovan A, Spolaore S, Casadoro G. β-Galactosidases with a lectin-like domain are expressed in strawberry. J Exp Bot. 2001;361:1635-45.
    • (2001) J Exp Bot , vol.361 , pp. 1635-1645
    • Trainotti, L.1    Spinello, R.2    Piovan, A.3    Spolaore, S.4    Casadoro, G.5
  • 298
    • 4544286792 scopus 로고    scopus 로고
    • Signaling and immune regulatory role of the dendritic cell immunoreceptor (DCIR) family lectins: DCIR, DCAR, dectin-2 and BDCA-2
    • Kanazawa N, Tashiro K, Miyachi Y. Signaling and immune regulatory role of the dendritic cell immunoreceptor (DCIR) family lectins: DCIR, DCAR, dectin-2 and BDCA-2. Immunobiology. 2004;209:179-90.
    • (2004) Immunobiology , vol.209 , pp. 179-190
    • Kanazawa, N.1    Tashiro, K.2    Miyachi, Y.3
  • 300
    • 0042572077 scopus 로고    scopus 로고
    • Receptor-like protein kinases: The keys to response
    • Morris ER, Walker JC. Receptor-like protein kinases: the keys to response. Curr Opin Plant Biol. 2003;6:339-42.
    • (2003) Curr Opin Plant Biol , vol.6 , pp. 339-342
    • Morris, E.R.1    Walker, J.C.2
  • 301
    • 24344466922 scopus 로고    scopus 로고
    • Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms
    • André S, Siebert H-C, Nishiguchi M, Tazaki K, Gabius H-J. Evidence for lectin activity of a plant receptor-like protein kinase by application of neoglycoproteins and bioinformatic algorithms. Biochim Biophys Acta. 2005;1725:222-32.
    • (2005) Biochim Biophys Acta , vol.1725 , pp. 222-232
    • André, S.1    Siebert, H.-C.2    Nishiguchi, M.3    Tazaki, K.4    Gabius, H.-J.5
  • 302
    • 0347302952 scopus 로고    scopus 로고
    • Cytokines in cancer pathogenesis and cancer therapy
    • Dranoff G. Cytokines in cancer pathogenesis and cancer therapy. Nat Rev Cancer. 2004;4:11-22.
    • (2004) Nat Rev Cancer , vol.4 , pp. 11-22
    • Dranoff, G.1
  • 303
    • 0347123433 scopus 로고    scopus 로고
    • Tumour-educated macrophages promote tumour progression and metastasis
    • Pollard JW. Tumour-educated macrophages promote tumour progression and metastasis. Nat Rev Cancer. 2004;4:71-8.
    • (2004) Nat Rev Cancer , vol.4 , pp. 71-78
    • Pollard, J.W.1
  • 304
    • 18144374219 scopus 로고    scopus 로고
    • Revisiting immunosurveillance and immunostimulation: Implications for cancer immunotherapy
    • Ichim CV. Revisiting immunosurveillance and immunostimulation: implications for cancer immunotherapy. J Transl Med. 2005;3:8.
    • (2005) J Transl Med , vol.3 , pp. 8
    • Ichim, C.V.1
  • 305
    • 0034053785 scopus 로고    scopus 로고
    • Long-term administration of galactoside-specific mistletoe lectin in an animal model: No protection against N-butyl-N-(4-hydroxybutyl)-nitrosamine- induced urinary bladder carcinogenesis in rats and no induction of a relevant local cellular immune response
    • Kunze E, Schulz H, Adamek M, Gabius H-J. Long-term administration of galactoside-specific mistletoe lectin in an animal model: no protection against N-butyl-N-(4-hydroxybutyl)-nitrosamine-induced urinary bladder carcinogenesis in rats and no induction of a relevant local cellular immune response. J Cancer Res Clin Oncol. 2000;126:125-38.
    • (2000) J Cancer Res Clin Oncol , vol.126 , pp. 125-138
    • Kunze, E.1    Schulz, H.2    Adamek, M.3    Gabius, H.-J.4
  • 306
    • 0034850491 scopus 로고    scopus 로고
    • Probing the cons and pros of lectin-induced immunomodulation: Case studies for the mistletoe lectin and galectin-1
    • Gabius H-J. Probing the cons and pros of lectin-induced immunomodulation: case studies for the mistletoe lectin and galectin-1. Biochimie. 2001;83:659-66.
    • (2001) Biochimie , vol.83 , pp. 659-666
    • Gabius, H.-J.1
  • 307
    • 0035070675 scopus 로고    scopus 로고
    • Evidence for stimulation of tumor proliferation in cell lines and histotypic cultures by clinically relevant low doses of the galactoside-binding mistletoe lectin, a component of proprietary extracts
    • Gabius H-J, Darro F, Remmelink M, André S, Kopitz J, Danguy A, Gabius S, Salmon I, Kiss R. Evidence for stimulation of tumor proliferation in cell lines and histotypic cultures by clinically relevant low doses of the galactoside-binding mistletoe lectin, a component of proprietary extracts. Cancer Invest. 2001;19:114-26.
    • (2001) Cancer Invest , vol.19 , pp. 114-126
    • Gabius, H.-J.1    Darro, F.2    Remmelink, M.3    André, S.4    Kopitz, J.5    Danguy, A.6    Gabius, S.7    Salmon, I.8    Kiss, R.9
  • 308
    • 0034813262 scopus 로고    scopus 로고
    • Immunotherapy of C3H/HeJ mammary adenocarcinoma with interleukin-2, mistletoe lectin or their combination: Effects on tumour growth, capillary leakage and nitric oxide (NO) production
    • Timoshenko AV, Lan Y, Gabius H-J, Lala PK. Immunotherapy of C3H/HeJ mammary adenocarcinoma with interleukin-2, mistletoe lectin or their combination: effects on tumour growth, capillary leakage and nitric oxide (NO) production. Eur J Cancer. 2001;37:1910-20.
    • (2001) Eur J Cancer , vol.37 , pp. 1910-1920
    • Timoshenko, A.V.1    Lan, Y.2    Gabius, H.-J.3    Lala, P.K.4
  • 310
    • 23944439856 scopus 로고    scopus 로고
    • Genome-wide association study to identify SNPs conferring risk of myocardial infarction and their functional analyses
    • Ozaki K, Tanaka T. Genome-wide association study to identify SNPs conferring risk of myocardial infarction and their functional analyses. Cell Mol Life Sci. 2005;62:1804-13.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1804-1813
    • Ozaki, K.1    Tanaka, T.2
  • 311
    • 0035834665 scopus 로고    scopus 로고
    • Reflections on glycobiology
    • Roseman S. Reflections on glycobiology. J Biol Chem. 2001;276:41527-42.
    • (2001) J Biol Chem , vol.276 , pp. 41527-41542
    • Roseman, S.1
  • 312
    • 77956661991 scopus 로고
    • The history of glycoprotein research, a personal view
    • Montreuil J, Vliegenthart JFG, Schachter H, editors. Amsterdam: Elsevier
    • Montreuil J. The history of glycoprotein research, a personal view. In: Montreuil J, Vliegenthart JFG, Schachter H, editors. Glycoproteins. Amsterdam: Elsevier; 1995. p. 1-12.
    • (1995) Glycoproteins , pp. 1-12
    • Montreuil, J.1
  • 313
    • 0001870839 scopus 로고    scopus 로고
    • Methods of glycoconjugate analysis
    • Gabius H-J, Gabius S, editors. London (UK)/Weinheim (Germany): Chapman & Hall
    • Hounsell EF. Methods of glycoconjugate analysis. In: Gabius H-J, Gabius S, editors. Glycosciences: status and perspectives. London (UK)/Weinheim (Germany): Chapman & Hall; 1997. p. 15-29.
    • (1997) Glycosciences: Status and Perspectives , pp. 15-29
    • Hounsell, E.F.1
  • 314
    • 0031722559 scopus 로고    scopus 로고
    • Strategies for glycoconjugate analysis
    • Geyer H, Geyer R. Strategies for glycoconjugate analysis. Acta Anat. 1998;161:18-35.
    • (1998) Acta Anat , vol.161 , pp. 18-35
    • Geyer, H.1    Geyer, R.2
  • 315
    • 15744372996 scopus 로고    scopus 로고
    • O-Fucosylation of Notch occurs in the endoplasmic reticulum
    • Luo Y, Haltiwanger RS. O-Fucosylation of Notch occurs in the endoplasmic reticulum. J Biol Chem. 2005;280:11289-94.
    • (2005) J Biol Chem , vol.280 , pp. 11289-11294
    • Luo, Y.1    Haltiwanger, R.S.2
  • 317
    • 0037370699 scopus 로고    scopus 로고
    • Insights into leukocyte adhesion deficiency type 2 from a novel mutation in the GDP-fucose transporter gene
    • Hidalgo A, Ma S, Peired AJ, Weiss LA, Cunningham-Rundles C, Frenette PS. Insights into leukocyte adhesion deficiency type 2 from a novel mutation in the GDP-fucose transporter gene. Blood. 2003;101:1705-12.
    • (2003) Blood , vol.101 , pp. 1705-1712
    • Hidalgo, A.1    Ma, S.2    Peired, A.J.3    Weiss, L.A.4    Cunningham-Rundles, C.5    Frenette, P.S.6
  • 318
    • 0003969391 scopus 로고    scopus 로고
    • Montreuil J, Vliegenthart JFG, Schachter H, editors. Amsterdam: Elsevier
    • Montreuil J, Vliegenthart JFG, Schachter H, editors. Glycoproteins and disease. Amsterdam: Elsevier; 1996.
    • (1996) Glycoproteins and Disease
  • 320
    • 1842467267 scopus 로고    scopus 로고
    • Glycosylation in congenital muscular dystrophies
    • Endo T, Toda T. Glycosylation in congenital muscular dystrophies. Biol Pharm Bull. 2003;26:1641-7.
    • (2003) Biol Pharm Bull , vol.26 , pp. 1641-1647
    • Endo, T.1    Toda, T.2
  • 321
    • 0037605951 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Review of their molecular bases, clinical presentations and specific therapies
    • Marquardt T, Denecke J. Congenital disorders of glycosylation: review of their molecular bases, clinical presentations and specific therapies. Eur J Pediatr. 2003;162:359-79.
    • (2003) Eur J Pediatr , vol.162 , pp. 359-379
    • Marquardt, T.1    Denecke, J.2
  • 322
    • 0038182574 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex: Post-translational processing and dystroglycan function
    • Michele DE, Campbell KP. Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. J Biol Chem. 2003;278:15457-60.
    • (2003) J Biol Chem , vol.278 , pp. 15457-15460
    • Michele, D.E.1    Campbell, K.P.2
  • 323
    • 0021861315 scopus 로고
    • Endogenous tumor lectins: A new class of tumor markers and targets for therapy?
    • Gabius H-J, Engelhardt R, Cramer F. Endogenous tumor lectins: a new class of tumor markers and targets for therapy? Med Hypotheses. 1985;18:47-50.
    • (1985) Med Hypotheses , vol.18 , pp. 47-50
    • Gabius, H.-J.1    Engelhardt, R.2    Cramer, F.3
  • 324
    • 0023187733 scopus 로고
    • Endogenous lectins in tumors and the immune system
    • Gabius H-J. Endogenous lectins in tumors and the immune system. Cancer Investig. 1987;5:39-46.
    • (1987) Cancer Investig , vol.5 , pp. 39-46
    • Gabius, H.-J.1
  • 325
    • 0344256483 scopus 로고    scopus 로고
    • Leukocyte and endothelial cell adhesion molecules as targets for therapeutic interventions in inflammatory disease
    • Ulbrich H, Eriksson EE, Lindbom L. Leukocyte and endothelial cell adhesion molecules as targets for therapeutic interventions in inflammatory disease. Trends Pharmacol Sci. 2003;24:640-7.
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 640-647
    • Ulbrich, H.1    Eriksson, E.E.2    Lindbom, L.3
  • 326
    • 0242490176 scopus 로고    scopus 로고
    • The molecular basis of lymphocyte recruitment to the skin: Clues for pathogenesis and selective therapies of inflammatory disorders
    • Schön MP, Zollner TM, Boehncke W-H. The molecular basis of lymphocyte recruitment to the skin: clues for pathogenesis and selective therapies of inflammatory disorders. J Invest Dermatol. 2003;121:951-62.
    • (2003) J Invest Dermatol , vol.121 , pp. 951-962
    • Schön, M.P.1    Zollner, T.M.2    Boehncke, W.-H.3
  • 327
    • 2542472337 scopus 로고    scopus 로고
    • Norovirus disease: Changing epidemiology and host susceptibility factors
    • Hutson AM, Atmar RL, Estes MK. Norovirus disease: changing epidemiology and host susceptibility factors. Trends Microbiol. 2004;12:279-87.
    • (2004) Trends Microbiol , vol.12 , pp. 279-287
    • Hutson, A.M.1    Atmar, R.L.2    Estes, M.K.3
  • 328
    • 20344381822 scopus 로고    scopus 로고
    • Glycoconjugate glycans as viral receptors
    • Olofsson S, Bergström T. Glycoconjugate glycans as viral receptors. Ann Med. 2005;37:154-72.
    • (2005) Ann Med , vol.37 , pp. 154-172
    • Olofsson, S.1    Bergström, T.2
  • 330
    • 0036687864 scopus 로고    scopus 로고
    • Active conformations of glycosaminoglycans. NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution
    • Hricovíni M, Guerrini M, Bisio A, Torri G, Naggi A, Casu B. Active conformations of glycosaminoglycans. NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution. Semin Thromb Hemost. 2002;28:325-34.
    • (2002) Semin Thromb Hemost , vol.28 , pp. 325-334
    • Hricovíni, M.1    Guerrini, M.2    Bisio, A.3    Torri, G.4    Naggi, A.5    Casu, B.6


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