메뉴 건너뛰기




Volumn 1572, Issue 2-3, 2002, Pages 165-177

The sugar code: Functional lectinomics

Author keywords

Agglutinin; Bioinformatics; Cell adhesion; Drug design; Glycoprotein; Lectin; Molecular modeling

Indexed keywords

ACROSIN; CALNEXIN; CALRETICULIN; CEREBELLAR SOLUBLE LECTIN PROTEIN; COLLECTIN; CYTOKINE; ELASTIN; GALECTIN; GLYCAN; GLYCOPROTEIN; HIGH MOBILITY GROUP B1 PROTEIN; HYALURONIC ACID BINDING PROTEIN; LAMININ BINDING PROTEIN; LANGERIN PROTEIN; LECTIN; OLIGOSACCHARIDE; P TYPE LECTIN PROTEIN; PENTRAXIN; PROTEIN; PROTEOGLYCAN CORE PROTEIN; SELECTIN; SUGAR; UNCLASSIFIED DRUG;

EID: 0037136404     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00306-9     Document Type: Review
Times cited : (302)

References (139)
  • 1
    • 0015521532 scopus 로고
    • The significance of glycosylated proteins
    • Winterburn P.J., Phelps C.F. The significance of glycosylated proteins. Nature. 236:1972;147-151.
    • (1972) Nature , vol.236 , pp. 147-151
    • Winterburn, P.J.1    Phelps, C.F.2
  • 3
    • 77956661991 scopus 로고
    • The history of glycoprotein research, a personal view
    • J. Montreuil, J.F.G. Vliegenthart, & H. Schachter. Amsterdam: Elsevier
    • Montreuil J. The history of glycoprotein research, a personal view. Montreuil J., Vliegenthart J.F.G., Schachter H. Glycoproteins. 1995;1-12 Elsevier, Amsterdam.
    • (1995) Glycoproteins , pp. 1-12
    • Montreuil, J.1
  • 4
    • 0035834665 scopus 로고    scopus 로고
    • Reflections of glycobiology
    • Roseman S. Reflections of glycobiology. J. Biol. Chem. 276:2001;41527-41542.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41527-41542
    • Roseman, S.1
  • 5
    • 0001022444 scopus 로고
    • Neutralisation of the anti-H agglutinin in eel serum by simple sugars
    • Watkins W.M., Morgan W.T.J. Neutralisation of the anti-H agglutinin in eel serum by simple sugars. Nature. 169:1952;825-826.
    • (1952) Nature , vol.169 , pp. 825-826
    • Watkins, W.M.1    Morgan, W.T.J.2
  • 6
    • 0033267884 scopus 로고    scopus 로고
    • A half century of blood-group antigen research: Some personal recollections
    • Watkins W.M. A half century of blood-group antigen research: some personal recollections. Trends Glycosci. Glycotechnol. 11:1999;391-411.
    • (1999) Trends Glycosci. Glycotechnol. , vol.11 , pp. 391-411
    • Watkins, W.M.1
  • 7
    • 0037136419 scopus 로고    scopus 로고
    • Animal lectins: A historical introduction and overview
    • Kilpatrick D.C. Animal lectins: a historical introduction and overview. Biochim. Biophys. Acta. 1572:2002;187-197.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 187-197
    • Kilpatrick, D.C.1
  • 8
    • 0000711134 scopus 로고
    • Specific precipitating activity of plant agglutinins (lectins)
    • Boyd W.C., Shapleigh E. Specific precipitating activity of plant agglutinins (lectins). Science. 119:1954;419.
    • (1954) Science , vol.119 , pp. 419
    • Boyd, W.C.1    Shapleigh, E.2
  • 9
    • 0015741344 scopus 로고
    • A molecular model for cell interactions
    • Roth S. A molecular model for cell interactions. Q. Rev. Biol. 48:1973;541-563.
    • (1973) Q. Rev. Biol. , vol.48 , pp. 541-563
    • Roth, S.1
  • 10
    • 0031029256 scopus 로고    scopus 로고
    • Animal lectins
    • Gabius H.-J. Animal lectins. Eur. J. Biochem. 243:1997;543-576.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 543-576
    • Gabius, H.-J.1
  • 12
    • 0035725755 scopus 로고    scopus 로고
    • Glycohistochemistry: The how and why of detection and localization of endogenous lectins
    • Gabius H.-J. Glycohistochemistry: the how and why of detection and localization of endogenous lectins. Anat. Histol. Embryol. 30:2001;3-31.
    • (2001) Anat. Histol. Embryol. , vol.30 , pp. 3-31
    • Gabius, H.-J.1
  • 13
    • 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. 87:2000;108-121.
    • (2000) Naturwissenschaften , vol.87 , pp. 108-121
    • Gabius, H.-J.1
  • 15
    • 0035260267 scopus 로고    scopus 로고
    • Glycome project: Concept, strategy and preliminary application to Caenorhabditis elegans
    • Hirabayashi J., Arata Y., Kasai K.-I. Glycome project: concept, strategy and preliminary application to Caenorhabditis elegans. Proteomics. 1:2001;295-303.
    • (2001) Proteomics , vol.1 , pp. 295-303
    • Hirabayashi, J.1    Arata, Y.2    Kasai, K.-I.3
  • 16
    • 0002488842 scopus 로고
    • A note on the recent discussion on definition of the term "lectin"
    • T.C. Bog-Hansen, & G.A. Spengler. Berlin: Walter de Gruyter
    • Kocourek J., Horejsi V. A note on the recent discussion on definition of the term "lectin" Bog-Hansen T.C., Spengler G.A. Lectins. Biology, Biochemistry, Clinical Biochemistry. vol. 3:1983;3-6 Walter de Gruyter, Berlin.
    • (1983) Lectins. Biology, Biochemistry, Clinical Biochemistry , vol.3 , pp. 3-6
    • Kocourek, J.1    Horejsi, V.2
  • 17
    • 0024159311 scopus 로고
    • Bifunctional properties of lectins: Lectins redefined
    • Barondes S.H. Bifunctional properties of lectins: lectins redefined. Trends Biochem. Sci. 13:1988;480-482.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 480-482
    • Barondes, S.H.1
  • 18
    • 0004895617 scopus 로고
    • The origin of the specificity in the recognition of oligosaccharides by proteins
    • Lemieux R.U. The origin of the specificity in the recognition of oligosaccharides by proteins. Chem. Soc. Rev. 18:1989;347-374.
    • (1989) Chem. Soc. Rev. , vol.18 , pp. 347-374
    • Lemieux, R.U.1
  • 19
    • 0003012148 scopus 로고    scopus 로고
    • How water provides the impetus for molecular recognition in aqueous solution
    • Lemieux R.U. How water provides the impetus for molecular recognition in aqueous solution. Acc. Chem. Res. 29:1996;373-380.
    • (1996) Acc. Chem. Res. , vol.29 , pp. 373-380
    • Lemieux, R.U.1
  • 20
    • 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. Pharm. Res. 15:1998;23-30.
    • (1998) Pharm. Res. , vol.15 , pp. 23-30
    • Gabius, H.-J.1
  • 21
    • 0001810168 scopus 로고    scopus 로고
    • The information-storing potential of the sugar code
    • H.-J. Gabius, & S. Gabius. London: Chapman & Hall
    • Laine R.A. The information-storing potential of the sugar code. Gabius H.-J., Gabius S. Glycosciences: Status and Perspectives. 1997;1-14 Chapman & Hall, London.
    • (1997) Glycosciences: Status and Perspectives , pp. 1-14
    • Laine, R.A.1
  • 23
    • 0001870839 scopus 로고    scopus 로고
    • Methods of glycoconjugate analysis
    • H.-J. Gabius, & S. Gabius. London: Chapman & Hall
    • Hounsell E.F. Methods of glycoconjugate analysis. Gabius H.-J., Gabius S. Glycosciences: Status and Perspectives. 1997;15-29 Chapman & Hall, London.
    • (1997) Glycosciences: Status and Perspectives , pp. 15-29
    • Hounsell, E.F.1
  • 24
    • 0031722559 scopus 로고    scopus 로고
    • Strategies for glycoconjugate analysis
    • Geyer H., Geyer R. Strategies for glycoconjugate analysis. Acta Anat. 161:1998;18-35.
    • (1998) Acta Anat. , vol.161 , pp. 18-35
    • Geyer, H.1    Geyer, R.2
  • 26
    • 0000815176 scopus 로고
    • Oligosaccharides: How can flexible molecules act as signals?
    • Carver J.P. Oligosaccharides: how can flexible molecules act as signals? Pure Appl. Chem. 65:1993;763-770.
    • (1993) Pure Appl. Chem. , vol.65 , pp. 763-770
    • Carver, J.P.1
  • 28
    • 0031935175 scopus 로고    scopus 로고
    • Computational carbohydrate chemistry: What theoretical methods can tell us
    • Woods R.J. Computational carbohydrate chemistry: what theoretical methods can tell us. Glycoconj. J. 15:1998;209-216.
    • (1998) Glycoconj. J. , vol.15 , pp. 209-216
    • Woods, R.J.1
  • 30
    • 0037681028 scopus 로고    scopus 로고
    • Structure, conformation, and dynamics of bioactive oligosaccharides: Theoretical approaches and experimental validations
    • Imberty A., Pérez S. Structure, conformation, and dynamics of bioactive oligosaccharides: theoretical approaches and experimental validations. Chem. Rev. 100:2000;4567-4588.
    • (2000) Chem. Rev. , vol.100 , pp. 4567-4588
    • Imberty, A.1    Pérez, S.2
  • 31
    • 7144254472 scopus 로고    scopus 로고
    • Conformer selection and differential restriction of ligand mobility by a plant lectin
    • Conformational behavior of Galβ1-3GlcNAcβ1-R, Galβ1-3GalNAcβ1-R and Galβ1-2Galβ1-R′ in the free state and complexed with mistletoe lectin as revealed by random walk and conformational clustering molecular mechanics calculations, molecular dynamics simulations and nuclear Overhauser experiments
    • Gilleron M., Siebert H.-C., Kaltner H., von der Lieth C.-W., Kozár T., Halkes K.M., Korchagina E.Y., Bovin N.V., Gabius H.-J., Vliegenthart J.F.G. Conformer selection and differential restriction of ligand mobility by a plant lectin. Conformational behavior of Galβ1-3GlcNAcβ1-R, Galβ1-3GalNAcβ1-R and Galβ1-2Galβ1-R′ in the free state and complexed with mistletoe lectin as revealed by random walk and conformational clustering molecular mechanics calculations, molecular dynamics simulations and nuclear Overhauser experiments. Eur. J. Biochem. 252:1998;416-427.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 416-427
    • Gilleron, M.1    Siebert, H.-C.2    Kaltner, H.3    Von der Lieth, C.-W.4    Kozár, T.5    Halkes, K.M.6    Korchagina, E.Y.7    Bovin, N.V.8    Gabius, H.-J.9    Vliegenthart, J.F.G.10
  • 32
    • 0002638114 scopus 로고    scopus 로고
    • Glycoproteins: Structure and function
    • H.-J. Gabius, & S. Gabius. London: Chapman & Hall
    • Sharon N., Lis H. Glycoproteins: structure and function. Gabius H.-J., Gabius S. Glycosciences: Status and Perspectives. 1997;133-162 Chapman & Hall, London.
    • (1997) Glycosciences: Status and Perspectives , pp. 133-162
    • Sharon, N.1    Lis, H.2
  • 33
    • 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. 55:1999;368-422.
    • (1999) Cell. Mol. Life Sci. , vol.55 , pp. 368-422
    • Reuter, G.1    Gabius, H.-J.2
  • 34
    • 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. 1473:1999;4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 35
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: Glycan presentation and protein-fold stability
    • Wormald M.R., Dwek R.A. Glycoproteins: glycan presentation and protein-fold stability. Structure. 7:1999;R155-R160.
    • (1999) Structure , vol.7
    • Wormald, M.R.1    Dwek, R.A.2
  • 36
    • 0023068345 scopus 로고
    • Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus
    • Hirschberg C.B., Snider M.D. Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus. Annu. Rev. Biochem. 56:1987;63-87.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 63-87
    • Hirschberg, C.B.1    Snider, M.D.2
  • 38
    • 0034851008 scopus 로고    scopus 로고
    • Nucleotide sugar transporters: Biological and functional aspects
    • Gerardy-Schahn R., Oelmann S., Bakker H. Nucleotide sugar transporters: biological and functional aspects. Biochimie. 83:2001;775-782.
    • (2001) Biochimie , vol.83 , pp. 775-782
    • Gerardy-Schahn, R.1    Oelmann, S.2    Bakker, H.3
  • 40
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology and genetics of the oligosaccharyltransferase
    • Silberstein S., Gilmore R. Biochemistry, molecular biology and genetics of the oligosaccharyltransferase. FASEB J. 10:1996;849-858.
    • (1996) FASEB J. , vol.10 , pp. 849-858
    • Silberstein, S.1    Gilmore, R.2
  • 41
    • 0032759101 scopus 로고    scopus 로고
    • Identification and characterization of large galactosyltransferase gene families: Galactosyltransferases for all functions
    • Amado M., Almeida R., Schwientek T., Clausen H. Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim. Biophys. Acta. 1473:1999;35-53.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 35-53
    • Amado, M.1    Almeida, R.2    Schwientek, T.3    Clausen, H.4
  • 42
    • 0032739349 scopus 로고    scopus 로고
    • β1,4-Galactosylation of N-glycans is a complex process
    • Furukawa K., Sato T. β1,4-Galactosylation of N-glycans is a complex process. Biochim. Biophys. Acta. 1473:1999;54-66.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 54-66
    • Furukawa, K.1    Sato, T.2
  • 43
    • 0035625597 scopus 로고    scopus 로고
    • Galactosyltransferases: A structural overview of their function and reaction mechanisms
    • Gastinel L.N. Galactosyltransferases: a structural overview of their function and reaction mechanisms. Trends Glycosci. Glycotechnol. 13:2001;131-145.
    • (2001) Trends Glycosci. Glycotechnol. , vol.13 , pp. 131-145
    • Gastinel, L.N.1
  • 45
    • 0032906430 scopus 로고    scopus 로고
    • Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates and bacteria
    • Oriol R., Mollicone R., Cailleau A., Balanzino L., Breton C. Divergent evolution of fucosyltransferase genes from vertebrates, invertebrates and bacteria. Glycobiology. 9:1999;323-334.
    • (1999) Glycobiology , vol.9 , pp. 323-334
    • Oriol, R.1    Mollicone, R.2    Cailleau, A.3    Balanzino, L.4    Breton, C.5
  • 47
    • 0034838654 scopus 로고    scopus 로고
    • Structural and functional features of glycosyltransferases
    • Breton C., Mucha J., Jeanneau C. Structural and functional features of glycosyltransferases. Biochimie. 83:2001;713-718.
    • (2001) Biochimie , vol.83 , pp. 713-718
    • Breton, C.1    Mucha, J.2    Jeanneau, C.3
  • 48
    • 0032392044 scopus 로고    scopus 로고
    • Biosynthesis of heparan sulfate and heparin: How are the multifunctional glycosaminoglycans built up?
    • Habuchi H., Habuchi O., Kimata K. Biosynthesis of heparan sulfate and heparin: how are the multifunctional glycosaminoglycans built up? Trends Glycosci. Glycotechnol. 10:1998;65-80.
    • (1998) Trends Glycosci. Glycotechnol. , vol.10 , pp. 65-80
    • Habuchi, H.1    Habuchi, O.2    Kimata, K.3
  • 49
    • 0032800522 scopus 로고    scopus 로고
    • Carbohydrate sulfotransferases: Mediators of extracellular communication
    • Bowman K.G., Bertozzi C.R. Carbohydrate sulfotransferases: mediators of extracellular communication. Chem. Biol. 6:1999;R9-R22.
    • (1999) Chem. Biol. , vol.6
    • Bowman, K.G.1    Bertozzi, C.R.2
  • 50
    • 0035930560 scopus 로고    scopus 로고
    • Carbohydrate-modifying sulfotransferases: Structure, function, and pathophysiology
    • Fukuda M., Hiraoka N., Akama T.O., Fukuda M.N. Carbohydrate-modifying sulfotransferases: structure, function, and pathophysiology. J. Biol. Chem. 276:2001;47747-47750.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47747-47750
    • Fukuda, M.1    Hiraoka, N.2    Akama, T.O.3    Fukuda, M.N.4
  • 53
    • 0017622781 scopus 로고
    • Detection of plasma membrane carbohydrates with lectin-peroxidase conjugates
    • D.M. Prescott. New York: Academic Press
    • Gonatas N.K., Avrameas S. Detection of plasma membrane carbohydrates with lectin-peroxidase conjugates. Prescott D.M. Methods in Cell Biology. vol. 15:1977;387-406 Academic Press, New York.
    • (1977) Methods in Cell Biology , vol.15 , pp. 387-406
    • Gonatas, N.K.1    Avrameas, S.2
  • 54
    • 0023253945 scopus 로고
    • Lectin cytochemistry and histrochemistry
    • Damjanov I. Lectin cytochemistry and histrochemistry. Lab. Invest. 57:1987;5-20.
    • (1987) Lab. Invest. , vol.57 , pp. 5-20
    • Damjanov, I.1
  • 55
    • 0023787466 scopus 로고
    • Detection and differentiation of glycoconjugates in various cell types by lectin histochemistry
    • Spicer S.S., Schulte B.A. Detection and differentiation of glycoconjugates in various cell types by lectin histochemistry. Basic Appl. Histochem. 32:1988;307-320.
    • (1988) Basic Appl. Histochem. , vol.32 , pp. 307-320
    • Spicer, S.S.1    Schulte, B.A.2
  • 56
    • 0028344684 scopus 로고
    • Contribution of carbohydrate histochemistry to glycobiology
    • Danguy A., Akif F., Pajak B., Gabius H.-J. Contribution of carbohydrate histochemistry to glycobiology. Histol. Histopathol. 9:1994;155-171.
    • (1994) Histol. Histopathol. , vol.9 , pp. 155-171
    • Danguy, A.1    Akif, F.2    Pajak, B.3    Gabius, H.-J.4
  • 57
    • 0002784127 scopus 로고    scopus 로고
    • Topology of glycosylation - A histochemist's view
    • H.-J. Gabius, & S. Gabius. London: Chapman & Hall
    • Pavelka M. Topology of glycosylation - a histochemist's view. Gabius H.-J., Gabius S. Glycosciences: Status and Perspectives. 1997;115-120 Chapman & Hall, London.
    • (1997) Glycosciences: Status and Perspectives , pp. 115-120
    • Pavelka, M.1
  • 58
    • 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. 95:1991;269-277.
    • (1991) Histochemistry , vol.95 , pp. 269-277
    • Gabius, H.-J.1    Wosgien, B.2    Hendrys, M.3    Bardosi, A.4
  • 59
    • 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. 39:1991;1249-1256.
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1249-1256
    • Gabius, H.-J.1    Kohnke-Godt, B.2    Leichsenring, M.3    Bardosi, A.4
  • 60
    • 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. 5:1992;123-157.
    • (1992) Adv. Lectin Res. , vol.5 , pp. 123-157
    • Gabius, H.-J.1    Gabius, S.2
  • 61
    • 0024342028 scopus 로고
    • Cell surface glycoproteins in embryonic development
    • Bourillon R., Aubery M. Cell surface glycoproteins in embryonic development. Int. Rev. Cytol. 116:1989;257-338.
    • (1989) Int. Rev. Cytol. , vol.116 , pp. 257-338
    • Bourillon, R.1    Aubery, M.2
  • 62
    • 0024269671 scopus 로고
    • Membrane oligosaccharides: Structure and function during differentiation
    • Mann P.L. Membrane oligosaccharides: structure and function during differentiation. Int. Rev. Cytol. 112:1988;67-96.
    • (1988) Int. Rev. Cytol. , vol.112 , pp. 67-96
    • Mann, P.L.1
  • 63
    • 0001033564 scopus 로고
    • Oligosaccharides in vertebrate development
    • Varki A., Marth J. Oligosaccharides in vertebrate development. Semin. Dev. Biol. 6:1995;127-138.
    • (1995) Semin. Dev. Biol. , vol.6 , pp. 127-138
    • Varki, A.1    Marth, J.2
  • 64
    • 0031722439 scopus 로고    scopus 로고
    • Glycocoding as an information management system in embryonic development
    • Mann P.L., Waterman R.E. Glycocoding as an information management system in embryonic development. Acta Anat. 161:1998;153-161.
    • (1998) Acta Anat. , vol.161 , pp. 153-161
    • Mann, P.L.1    Waterman, R.E.2
  • 65
    • 0034444949 scopus 로고    scopus 로고
    • Protein-bound carbohydrates on cell-surface as targets of recognition: An odyssey in understanding them
    • Muramatsu T. Protein-bound carbohydrates on cell-surface as targets of recognition: an odyssey in understanding them. Glycoconj. J. 17:2000;577-595.
    • (2000) Glycoconj. J. , vol.17 , pp. 577-595
    • Muramatsu, T.1
  • 66
    • 0023517687 scopus 로고
    • Lectins and blood group substances as tumor markers
    • Caselitz J. Lectins and blood group substances as tumor markers. Curr. Top. Pathol. 77:1987;245-278.
    • (1987) Curr. Top. Pathol. , vol.77 , pp. 245-278
    • Caselitz, J.1
  • 67
    • 0024524840 scopus 로고
    • Malignant cell glycoproteins and glycolipids
    • Alhadeff J.A. Malignant cell glycoproteins and glycolipids. Crit. Rev. Oncol./Hematol. 9:1989;37-107.
    • (1989) Crit. Rev. Oncol./Hematol. , vol.9 , pp. 37-107
    • Alhadeff, J.A.1
  • 68
    • 0030766193 scopus 로고    scopus 로고
    • Concepts of tumor lectinology
    • Gabius H.-J. Concepts of tumor lectinology. Cancer Investig. 15:1997;454-464.
    • (1997) Cancer Investig. , vol.15 , pp. 454-464
    • Gabius, H.-J.1
  • 69
    • 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. 161:1998;36-78.
    • (1998) Acta Anat. , vol.161 , pp. 36-78
    • Brockhausen, I.1    Schutzbach, J.2    Kuhns, W.3
  • 70
    • 0031723411 scopus 로고    scopus 로고
    • Cancer-associated glycosphingolipid antigens: Their structure, organization and function
    • Hakomori S. Cancer-associated glycosphingolipid antigens: their structure, organization and function. Acta Anat. 161:1998;79-90.
    • (1998) Acta Anat. , vol.161 , pp. 79-90
    • Hakomori, S.1
  • 71
    • 0032186306 scopus 로고    scopus 로고
    • α-L-Fucose: A potentially critical molecule in pathologic processes including neoplasia
    • Listinsky J.J., Siegal G.P., Listinsky C.M. α-L-Fucose: a potentially critical molecule in pathologic processes including neoplasia. Am. J. Clin. Pathol. 110:1998;425-440.
    • (1998) Am. J. Clin. Pathol. , vol.110 , pp. 425-440
    • Listinsky, J.J.1    Siegal, G.P.2    Listinsky, C.M.3
  • 73
    • 0031754994 scopus 로고    scopus 로고
    • Application of lectins and neoglycoconjugates in histology and pathology
    • Danguy A., Decaestecker C., Genten F., Salmon I., Kiss R. Application of lectins and neoglycoconjugates in histology and pathology. Acta Anat. 161:1998;206-218.
    • (1998) Acta Anat. , vol.161 , pp. 206-218
    • Danguy, A.1    Decaestecker, C.2    Genten, F.3    Salmon, I.4    Kiss, R.5
  • 74
    • 0025132450 scopus 로고
    • Binding of T-antigen-bearing neoglycoprotein and peanut agglutinin to cultured tumor cells and breast carcinomas
    • Gabius H.-J., Schröter C., Gabius S., Brinck U., Tietze L.-F. Binding of T-antigen-bearing neoglycoprotein and peanut agglutinin to cultured tumor cells and breast carcinomas. J. Histochem. Cytochem. 38:1990;1625-1631.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1625-1631
    • Gabius, H.-J.1    Schröter, C.2    Gabius, S.3    Brinck, U.4    Tietze, L.-F.5
  • 76
    • 0033404665 scopus 로고    scopus 로고
    • The levels of expression of galectin-1, galectin-3, the Thomsen-Friedenreich antigen and their binding sites decrease as clinical aggressiveness increases in head and neck cancers
    • Choufani G., Nagy N., Saussez S., Marchant H., Bisschop P., Burchert M., Danguy A., Louryan S., Salmon I., Gabius H.-J., Kiss R., Hassid S. The levels of expression of galectin-1, galectin-3, the Thomsen-Friedenreich antigen and their binding sites decrease as clinical aggressiveness increases in head and neck cancers. Cancer. 86:1999;2353-2363.
    • (1999) Cancer , vol.86 , pp. 2353-2363
    • Choufani, G.1    Nagy, N.2    Saussez, S.3    Marchant, H.4    Bisschop, P.5    Burchert, M.6    Danguy, A.7    Louryan, S.8    Salmon, I.9    Gabius, H.-J.10    Kiss, R.11    Hassid, S.12
  • 77
    • 0032830864 scopus 로고    scopus 로고
    • Molecular basis of glycoconjugate disease
    • Schachter H. Molecular basis of glycoconjugate disease. Biochim. Biophys. Acta. 1455:1999;61-418.
    • (1999) Biochim. Biophys. Acta , vol.1455 , pp. 61-418
    • Schachter, H.1
  • 78
    • 0003969391 scopus 로고    scopus 로고
    • J. Montreuil, J.F.G. Vliegenthart, & H. Schachter. Amsterdam: Elsevier
    • Montreuil J., Vliegenthart J.F.G., Schachter H. Glycoproteins and Disease. 1996;Elsevier, Amsterdam.
    • (1996) Glycoproteins and Disease
  • 79
    • 0034515822 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency II-from A to almost Z
    • Etzioni A., Tonetti M. Leukocyte adhesion deficiency II-from A to almost Z. Immunol. Rev. 178:2000;138-147.
    • (2000) Immunol. Rev. , vol.178 , pp. 138-147
    • Etzioni, A.1    Tonetti, M.2
  • 80
    • 0032833063 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency type II
    • Becker D.J., Lowe J.B. Leukocyte adhesion deficiency type II. Biochim. Biophys. Acta. 1455:1999;193-204.
    • (1999) Biochim. Biophys. Acta , vol.1455 , pp. 193-204
    • Becker, D.J.1    Lowe, J.B.2
  • 81
    • 0034939074 scopus 로고    scopus 로고
    • Golgi nucleotide sugar transport and leukocyte adhesion deficiency II
    • Hirschberg C.B. Golgi nucleotide sugar transport and leukocyte adhesion deficiency II. J. Clin. Invest. 108:2001;3-6.
    • (2001) J. Clin. Invest. , vol.108 , pp. 3-6
    • Hirschberg, C.B.1
  • 82
    • 0031784245 scopus 로고    scopus 로고
    • Animal lectins as cell adhesion molecules
    • Kaltner H., Stierstorfer B. Animal lectins as cell adhesion molecules. Acta Anat. 161:1998;162-179.
    • (1998) Acta Anat. , vol.161 , pp. 162-179
    • Kaltner, H.1    Stierstorfer, B.2
  • 83
    • 0033229717 scopus 로고    scopus 로고
    • x oligosaccharides: Versatile roles in cell-cell interaction
    • x oligosaccharides: versatile roles in cell-cell interaction. J. Cell Biol. 147:1999;467-470.
    • (1999) J. Cell Biol. , vol.147 , pp. 467-470
    • Fukuda, M.1    Hiraoka, N.2    Yeh, J.-C.3
  • 84
    • 0033573884 scopus 로고    scopus 로고
    • Human glycosylation disorders and sugar supplement therapy
    • Freeze H.H. Human glycosylation disorders and sugar supplement therapy. Biochem. Biophys. Res. Commun. 255:1999;189-193.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 189-193
    • Freeze, H.H.1
  • 85
    • 0035279221 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation: Genetic model systems lead the way
    • Aebi M., Hennet T. Congenital disorders of glycosylation: genetic model systems lead the way. Trends Cell Biol. 11:2001;136-141.
    • (2001) Trends Cell Biol. , vol.11 , pp. 136-141
    • Aebi, M.1    Hennet, T.2
  • 86
    • 0035716899 scopus 로고    scopus 로고
    • Update and perspectives on congenital disorders of glycosylation
    • Freeze H.H. Update and perspectives on congenital disorders of glycosylation. Glycobiology. 11:2001;129R-143R.
    • (2001) Glycobiology , vol.11
    • Freeze, H.H.1
  • 87
    • 0033543696 scopus 로고    scopus 로고
    • Cloning and expression of a proteoglycan UDP-galactose:β-xylose β1,4-galactosyltransferase I. A seventh member of the human β4-galactosyltransferase gene family
    • Almeida R., Levery S.B., Mandel U., Kresse H., Schwientek T., Bennett E.P., Clausen H. Cloning and expression of a proteoglycan UDP-galactose:β-xylose β1,4-galactosyltransferase I. A seventh member of the human β4-galactosyltransferase gene family. J. Biol. Chem. 274:1999;26165-26171.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26165-26171
    • Almeida, R.1    Levery, S.B.2    Mandel, U.3    Kresse, H.4    Schwientek, T.5    Bennett, E.P.6    Clausen, H.7
  • 88
    • 0032857187 scopus 로고    scopus 로고
    • Molecular basis for the progeroid variant of Ehlers-Danlos syndrome. Identification and characterization of two mutations in galactosyltransferase I gene
    • Okajima T., Fukumoto S., Furukawa K., Urano T., Furukawa K. Molecular basis for the progeroid variant of Ehlers-Danlos syndrome. Identification and characterization of two mutations in galactosyltransferase I gene. J. Biol. Chem. 274:1999;28841-28844.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28841-28844
    • Okajima, T.1    Fukumoto, S.2    Furukawa, K.3    Urano, T.4    Furukawa, K.5
  • 89
    • 0035213888 scopus 로고    scopus 로고
    • The clinical relevance of glycobiology
    • Schachter H. The clinical relevance of glycobiology. J. Clin. Invest. 108:2001;1579-1582.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1579-1582
    • Schachter, H.1
  • 91
    • 0034018612 scopus 로고    scopus 로고
    • The missing link in lysosomal enzyme targeting
    • Sly W.S. The missing link in lysosomal enzyme targeting. J. Clin. Invest. 105:2000;563-564.
    • (2000) J. Clin. Invest. , vol.105 , pp. 563-564
    • Sly, W.S.1
  • 92
    • 0032739350 scopus 로고    scopus 로고
    • The remodeling of glycoconjugates in mice
    • Hennet T., Ellies L.G. The remodeling of glycoconjugates in mice. Biochim. Biophys. Acta. 1473:1999;123-136.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 123-136
    • Hennet, T.1    Ellies, L.G.2
  • 93
    • 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. 127:2000;171-176.
    • (2000) J. Biochem. , vol.127 , pp. 171-176
    • Muramatsu, T.1
  • 94
    • 0001622821 scopus 로고    scopus 로고
    • Functions of carbohydrates revealed by transgenic technology
    • M. Fukuda, & O. Hindsgaul. Oxford: Oxford Univ. Press
    • Stanley P. Functions of carbohydrates revealed by transgenic technology. Fukuda M., Hindsgaul O. Molecular and Cellular Glycobiology (Frontiers in Molecular Biology). vol. 30:2000;169-198 Oxford Univ. Press, Oxford.
    • (2000) Molecular and Cellular Glycobiology (Frontiers in Molecular Biology) , vol.30 , pp. 169-198
    • Stanley, P.1
  • 95
    • 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. 1525:2001;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
  • 96
    • 0032725993 scopus 로고    scopus 로고
    • New discoveries with mice mutant in endothelial and platelet selectins
    • Hartwell D.W., Wagner D.D. New discoveries with mice mutant in endothelial and platelet selectins. Thromb. Haemost. 82:1999;850-857.
    • (1999) Thromb. Haemost. , vol.82 , pp. 850-857
    • Hartwell, D.W.1    Wagner, D.D.2
  • 97
    • 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. 1572:2002;198-208.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 98
    • 0034710157 scopus 로고    scopus 로고
    • The evolution of cell adhesion
    • Hynes R.O., Zhao Q. The evolution of cell adhesion. J. Cell Biol. 150:2000;F89-F95.
    • (2000) J. Cell Biol. , vol.150
    • Hynes, R.O.1    Zhao, Q.2
  • 99
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • Dodd R.B., Drickamer K. Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology. 11:2001;71R-79R.
    • (2001) Glycobiology , vol.11
    • Dodd, R.B.1    Drickamer, K.2
  • 100
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • The C. elegans Sequencing Consortium Genome sequence of the nematode C. elegans: a platform for investigating biology. Science. 282:1998;2012-2018.
    • (1998) Science , vol.282 , pp. 2012-2018
  • 101
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • Weigel P.H., Yik J.H.N. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim. Biophys. Acta. 1572:2002;341-363.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.N.2
  • 103
    • 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 K.B.M. Collectins and ficolins: sugar pattern recognition molecules of the mammalian innate immune system. Biochim. Biophys. Acta. 1572:2002;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
  • 104
    • 0037136413 scopus 로고    scopus 로고
    • Mannan-binding lectin: Clinical significance and applications
    • Kilpatrick D.C. Mannan-binding lectin: clinical significance and applications. Biochim. Biophys. Acta. 1572:2002;401-413.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 401-413
    • Kilpatrick, D.C.1
  • 105
    • 0037136416 scopus 로고    scopus 로고
    • Galectinomics: Finding themes in complexity
    • Cooper D.N.W. Galectinomics: finding themes in complexity. Biochim. Biophys. Acta. 1572:2002;209-231.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 209-231
    • Cooper, D.N.W.1
  • 107
    • 0037136412 scopus 로고    scopus 로고
    • Binding and cross-linking properties of galectins
    • Brewer C.F., Dam T.K. Binding and cross-linking properties of galectins. Biochim. Biophys. Acta. 1572:2002;252-262.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 252-262
    • Brewer, C.F.1    Dam, T.K.2
  • 109
    • 0037136408 scopus 로고    scopus 로고
    • Role of galectins in inflammatory and immunomodulatory processes
    • Rabinovich G.A., Rubinstein N., Toscano M. Role of galectins in inflammatory and immunomodulatory processes. Biochim. Biophys. Acta. 1572:2002;274-284.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 274-284
    • Rabinovich, G.A.1    Rubinstein, N.2    Toscano, M.3
  • 113
    • 17544377102 scopus 로고    scopus 로고
    • Different architecture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives
    • Solís D., Romero A., Kaltner H., Gabius H.-J., Díaz-Mauriño T. Different architecture of the combining sites of two chicken galectins revealed by chemical-mapping studies with synthetic ligand derivatives. J. Biol. Chem. 271:1996;12744-12748.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12744-12748
    • Solís, D.1    Romero, A.2    Kaltner, H.3    Gabius, H.-J.4    Díaz-Mauriño, T.5
  • 114
    • 0035884413 scopus 로고    scopus 로고
    • Carbohydrate specificity of a galectin from chicken liver (CG-16)
    • Wu A.M., Wu J.H., Tsai M.S., Kaltner H., Gabius H.-J. Carbohydrate specificity of a galectin from chicken liver (CG-16). Biochem. J. 358:2001;529-538.
    • (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
  • 115
    • 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 R.J., Vrasidas I., Kaltner H., Kuwabara I., Liu F.-T., Liskamp R.M.J., Gabius H.-J. Wedgelike glycodendrimers as inhibitors of binding of mammalian galectins to various glycoproteins, lactose maxiclusters and cell surface glycoconjugates. CHEMBIOCHEM. 2:2001;822-830.
    • (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
  • 116
    • 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 J.R., 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. 127:2001;375-386.
    • (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
    • 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. 273:1998;11205-11211.
    • (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
  • 120
    • 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. 276:2001;35917-35923.
    • (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
  • 122
    • 0034698092 scopus 로고    scopus 로고
    • Cloning, characterization and phylogenetic analysis of siglec-9, a new member of the CD33-related group of siglecs. Evidence for co-evolution with sialic acid synthesis pathways
    • Angata T., Varki A. Cloning, characterization and phylogenetic analysis of siglec-9, a new member of the CD33-related group of siglecs. Evidence for co-evolution with sialic acid synthesis pathways. J. Biol. Chem. 275:2000;22127-22135.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22127-22135
    • Angata, T.1    Varki, A.2
  • 123
    • 0030045734 scopus 로고    scopus 로고
    • NMR-based, molecular dynamics- and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galβ1-2Galβ1-R) for an animal galectin in the free and in the bound state
    • Siebert H.-C., Gilleron M., Kaltner H., von der Lieth C.-W., Kozár T., Bovin N.V., Korchagina E.Y., Vliegenthart J.F.G., Gabius H.-J. NMR-based, molecular dynamics- and random walk molecular mechanics-supported study of conformational aspects of a carbohydrate ligand (Galβ1-2Galβ1-R) for an animal galectin in the free and in the bound state. Biochem. Biophys. Res. Commun. 219:1996;205-212.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 205-212
    • Siebert, H.-C.1    Gilleron, M.2    Kaltner, H.3    Von der Lieth, C.-W.4    Kozár, T.5    Bovin, N.V.6    Korchagina, E.Y.7    Vliegenthart, J.F.G.8    Gabius, H.-J.9
  • 131
    • 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 R.V., Murdoch A.D. Proteoglycans of the extracellular environment: clues from the gene and protein side offer novel perspectives in molecular diversity and function. FASEB J. 10:1996;598-614.
    • (1996) FASEB J. , vol.10 , pp. 598-614
    • Iozzo, R.V.1    Murdoch, A.D.2
  • 132
    • 4243877714 scopus 로고    scopus 로고
    • Molecular basis of non-self recognition by the horseshoe crab tachylectins
    • in press
    • S. Kawabata, R. Tsuda, Molecular basis of non-self recognition by the horseshoe crab tachylectins, Biochim. Biophys. Acta, in press.
    • Biochim. Biophys. Acta
    • Kawabata, S.1    Tsuda, R.2
  • 133
    • 0037136409 scopus 로고    scopus 로고
    • Lectin activities of cytokines: Functions and putative carbohydrate recognition domains
    • Cebo C., Vergoten G., Zanetta J.-P. Lectin activities of cytokines: functions and putative carbohydrate recognition domains. Biochim. Biophys. Acta. 1572:2002;422-434.
    • (2002) Biochim. Biophys. Acta , vol.1572 , pp. 422-434
    • Cebo, C.1    Vergoten, G.2    Zanetta, J.-P.3
  • 134
    • 0035358554 scopus 로고    scopus 로고
    • Combinatorial syntheses of sugar derivatives
    • Nishimura S.-I. Combinatorial syntheses of sugar derivatives. Curr. Opin. Chem. Biol. 5:2001;325-335.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 325-335
    • Nishimura, S.-I.1
  • 136
    • 0031722560 scopus 로고    scopus 로고
    • Signaling pathways for transduction of the initial message of the glycocode into cellular responses
    • Villalobo A., Gabius H.-J. Signaling pathways for transduction of the initial message of the glycocode into cellular responses. Acta Anat. 161:1998;110-129.
    • (1998) Acta Anat. , vol.161 , pp. 110-129
    • Villalobo, A.1    Gabius, H.-J.2
  • 137
    • 0032714187 scopus 로고    scopus 로고
    • Intracellular lectins associated with N-linked glycoprotein traffic
    • Yamashita K., Hara-Kuge S., Ohkura T. Intracellular lectins associated with N-linked glycoprotein traffic. Biochim. Biophys. Acta. 1473:1999;147-160.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 147-160
    • Yamashita, K.1    Hara-Kuge, S.2    Ohkura, T.3
  • 138
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A., Aebi M. Intracellular functions of N-linked glycans. Science. 291:2001;2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 139
    • 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. 168:2001;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.