메뉴 건너뛰기




Volumn 7, Issue 2, 1997, Pages 241-251

Differential recognition of glycoprotein acceptors by terminal glycosyltransferases

Author keywords

Galactosyltransferases; Glycoproteins; Glycosyltransferases; Sialyltransferases

Indexed keywords

GALACTOSYLTRANSFERASE; GLYCOPROTEIN; GLYCOSYLTRANSFERASE; SIALYLTRANSFERASE;

EID: 0030963571     PISSN: 09596658     EISSN: None     Source Type: Journal    
DOI: 10.1093/glycob/7.2.241     Document Type: Article
Times cited : (23)

References (82)
  • 2
    • 0028020550 scopus 로고
    • Protein-specific glycosyltransferases: How and why they do it!
    • Baenziger, J.U. (1994) Protein-specific glycosyltransferases: how and why they do it! FASEB J., 8, 1019-1025.
    • (1994) FASEB J. , vol.8 , pp. 1019-1025
    • Baenziger, J.U.1
  • 3
    • 0018787411 scopus 로고
    • Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides
    • Baenziger, J.U. and Fiete, D. (1979) Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides. J Biol. Chem., 254, 9795-9799.
    • (1979) J Biol. Chem. , vol.254 , pp. 9795-9799
    • Baenziger, J.U.1    Fiete, D.2
  • 4
    • 0026333687 scopus 로고
    • Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting
    • Baranski, T.J., Koelsch, G., Harsuck, J.A., and Kornfeld, S. (1991) Mapping and molecular modeling of a recognition domain for lysosomal enzyme targeting. J. Biol. Chem., 266, 23365-23372.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23365-23372
    • Baranski, T.J.1    Koelsch, G.2    Harsuck, J.A.3    Kornfeld, S.4
  • 5
    • 0026446324 scopus 로고
    • Lysosomal enzyme phosphorylation. I. Protein recognition determinants in both lobes of procathepsin D mediate its interaction with UDP-GlcNAc: Lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
    • Baranski, T.J., Cantor, A.B. and Kornfeld, S. (1992) Lysosomal enzyme phosphorylation. I. Protein recognition determinants in both lobes of procathepsin D mediate its interaction with UDP-GlcNAc: lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. J. Biol. Chem., 267, 23342-23348.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23342-23348
    • Baranski, T.J.1    Cantor, A.B.2    Kornfeld, S.3
  • 6
    • 0018592006 scopus 로고
    • Biosynthesis of mammalian glycoproteins. Glycosylation pathways in the synthesis of the nonreducing terminal sequences
    • Beyer, T.A., Rearick, J.I., Paulson, J.C, Prieels J.P., Sadler, J.E. and Hill, R.L. (1979) Biosynthesis of mammalian glycoproteins. Glycosylation pathways in the synthesis of the nonreducing terminal sequences. J. Biol. Chem., 254, 12531-12534.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12531-12534
    • Beyer, T.A.1    Rearick, J.I.2    Paulson, J.C.3    Prieels, J.P.4    Sadler, J.E.5    Hill, R.L.6
  • 7
    • 0019485676 scopus 로고
    • Glycosyltransferases and their use in assessing oligosaccharide structure and structure-function relationships
    • Beyer, T.A., Sadler, J.C., Rearick, J.I., Paulson, J.C., and Hill, R.L. (1981) Glycosyltransferases and their use in assessing oligosaccharide structure and structure-function relationships. Adv. Enzymol., 52, 23-175.
    • (1981) Adv. Enzymol. , vol.52 , pp. 23-175
    • Beyer, T.A.1    Sadler, J.C.2    Rearick, J.I.3    Paulson, J.C.4    Hill, R.L.5
  • 8
    • 0026478889 scopus 로고
    • Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides
    • Cantor, A.B., Baranski, T.J. and Kornfeld, S. (1992) Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides. J. Biol. Chem., 267, 23349-23356.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23349-23356
    • Cantor, A.B.1    Baranski, T.J.2    Kornfeld, S.3
  • 9
    • 0026463870 scopus 로고
    • Phosphorylation of Asn-linked oligosaccharides located at novel sites on the lysosomal enzyme cathepsin D
    • Cantor, A.B. and Kornfeld, S. (1992) Phosphorylation of Asn-linked oligosaccharides located at novel sites on the lysosomal enzyme cathepsin D. J. Biol. Chem., 267, 23357-23363.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23357-23363
    • Cantor, A.B.1    Kornfeld, S.2
  • 10
    • 0030576058 scopus 로고    scopus 로고
    • Transcriptional regulation of α1,3-Galactosyltransferase in embryonal carcinoma cells by retinoic acid. Masking of Lewis x antigens by α-galactosylation
    • Cho, S.K., Yeh, J.-C., Cho, M. and Cummings, R.D. (1996) Transcriptional regulation of α1,3-Galactosyltransferase in embryonal carcinoma cells by retinoic acid. Masking of Lewis x antigens by α-galactosylation. J. Biol. Chem., 271, 3238-3246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3238-3246
    • Cho, S.K.1    Yeh, J.-C.2    Cho, M.3    Cummings, R.D.4
  • 11
    • 0002607662 scopus 로고
    • Synthesis of asparagine-linked oligosaccharides: Pathways, genetics and metabolic regulation
    • Allen, J.J. and Kisailus, E.C. (eds.), Marcel Dekker, New York
    • Cummings, R.D. (1992) Synthesis of asparagine-linked oligosaccharides: pathways, genetics and metabolic regulation. In Allen, J.J. and Kisailus, E.C. (eds.), Glycoconjugates: Composition, Structure and Function. Marcel Dekker, New York, pp. 333-360.
    • (1992) Glycoconjugates: Composition, Structure and Function , pp. 333-360
    • Cummings, R.D.1
  • 12
    • 0020368287 scopus 로고
    • Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography
    • Cummings, R.D. and Kornfeld, S. (1982) Fractionation of asparagine-linked oligosaccharides by serial lectin-agarose affinity chromatography. J. Biol. Chem., 257, 11235-11240.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11235-11240
    • Cummings, R.D.1    Kornfeld, S.2
  • 13
    • 0021227742 scopus 로고
    • R 2.1: Binding of oligosaccharides containing these sequences to immobilized Datura stramonium agglutinin
    • R 2.1: binding of oligosaccharides containing these sequences to immobilized Datura stramonium agglutinin. J. Biol. Chem., 259, 6253-6260.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6253-6260
    • Cummings, R.D.1    Kornfeld, S.2
  • 14
    • 0023946901 scopus 로고
    • Retinoic acid-induced differentiation of the mouse teratocarcinoma cell line F9 is accompanied by an increase in the activity of UDP-galactose:β-g-Galactosyl-α1,3-galactosyltransferase
    • Cummings, R.D. and Mattox, S.A. (1988) Retinoic acid-induced differentiation of the mouse teratocarcinoma cell line F9 is accompanied by an increase in the activity of UDP-galactose:β-g-Galactosyl-α1,3-galactosyltransferase. J. Biol. Chem., 263, 511-519.
    • (1988) J. Biol. Chem. , vol.263 , pp. 511-519
    • Cummings, R.D.1    Mattox, S.A.2
  • 15
    • 0029021007 scopus 로고
    • Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V
    • Demetriou, M., Nabi, I.R., Coppolino, M., Dedhar, S. and Dennis, J.W. (1995) Reduced contact-inhibition and substratum adhesion in epithelial cells expressing GlcNAc-transferase V. J. Cell Biol., 130, 383-392.
    • (1995) J. Cell Biol. , vol.130 , pp. 383-392
    • Demetriou, M.1    Nabi, I.R.2    Coppolino, M.3    Dedhar, S.4    Dennis, J.W.5
  • 16
    • 0021702358 scopus 로고
    • Translocation across Golgi vesicle membranes: A CHO glycosylation mutant deficient in CMP-sialic acid transport
    • Deutscher, S.L., Nuwayhid, N., Stanley, P., Briles, E.I. and Hirschberg, C.B. (1984) Translocation across Golgi vesicle membranes: a CHO glycosylation mutant deficient in CMP-sialic acid transport. Cell, 39, 295-299.
    • (1984) Cell , vol.39 , pp. 295-299
    • Deutscher, S.L.1    Nuwayhid, N.2    Stanley, P.3    Briles, E.I.4    Hirschberg, C.B.5
  • 17
    • 0025569426 scopus 로고
    • LAMP-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin
    • Do, K.-Y., Smith, D.F., and Cummings, R.D. (1990) LAMP-1 in CHO cells is a primary carrier of poly-N-acetyllactosamine chains and is bound preferentially by a mammalian S-type lectin. Biochem. Biophys. Res. Commun., 173, 1123-1128.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 1123-1128
    • Do, K.-Y.1    Smith, D.F.2    Cummings, R.D.3
  • 18
    • 0028093244 scopus 로고
    • Modification of glycoproteins by N-acetylglucosaminyltransferase V is greatly influenced by accessibility of the enzyme to oligosaccharide acceptors
    • Do, K.-Y., Fregien, N., Pierce, M. and Cummings, R.D. (1994) Modification of glycoproteins by N-acetylglucosaminyltransferase V is greatly influenced by accessibility of the enzyme to oligosaccharide acceptors. J. Biol. Chem., 269, 23456-23464.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23456-23464
    • Do, K.-Y.1    Fregien, N.2    Pierce, M.3    Cummings, R.D.4
  • 19
    • 0024494510 scopus 로고
    • Biosynthesis of bi-, tri-, and tetraantennary oligosaccharides containing α-D-galactosyl residues at their nonreducing termini. Branch specificity of the Ehrlich tumor cell α(1,3)-galactosyltransferase
    • Elices, M.J. and Goldstein, I.J. (1989) Biosynthesis of bi-, tri-, and tetraantennary oligosaccharides containing α-D-galactosyl residues at their nonreducing termini. Branch specificity of the Ehrlich tumor cell α(1,3)-galactosyltransferase. J. Biol. Chem., 264, 1375-1380.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1375-1380
    • Elices, M.J.1    Goldstein, I.J.2
  • 20
    • 0001601573 scopus 로고
    • Cell surface carbohydrates in hematopoietic cell differentiation and malignancy
    • Fukuda, M. (ed.), CRC Press, London
    • Fukuda, M. and Fukuda, M.N. (1992) Cell surface carbohydrates in hematopoietic cell differentiation and malignancy. In Fukuda, M. (ed.), Cell Surface Carbohydrates and Cell Development. CRC Press, London, pp. 127-160.
    • (1992) Cell Surface Carbohydrates and Cell Development , pp. 127-160
    • Fukuda, M.1    Fukuda, M.N.2
  • 21
    • 0018117205 scopus 로고
    • Release of oligosaccharides from various glycosphingolipids by endo-β-galactosidase
    • Fukuda, M.N., Watanabe, K. and Hakomori, S. (1978) Release of oligosaccharides from various glycosphingolipids by endo-β-galactosidase. J. Biol. Chem., 253, 6814-6819.
    • (1978) J. Biol. Chem. , vol.253 , pp. 6814-6819
    • Fukuda, M.N.1    Watanabe, K.2    Hakomori, S.3
  • 22
  • 23
    • 0028179379 scopus 로고
    • UDP-Galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase activity synthesizing O-glycan core 1 is controlled by the amino acid sequence and glycosylation of glycopeptide substrates
    • Granovsky, M., Bielfeldt, T., Peter, S., Paulsen, H., Meldal, M., Brockhausen, J. and Brockhausen, J. (1994) UDP-Galactose:glycoprotein-N-acetyl-D-galactosamine 3-β-D-galactosyltransferase activity synthesizing O-glycan core 1 is controlled by the amino acid sequence and glycosylation of glycopeptide substrates. Eur. J. Biochem., 221, 1039-1046.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 1039-1046
    • Granovsky, M.1    Bielfeldt, T.2    Peter, S.3    Paulsen, H.4    Meldal, M.5    Brockhausen, J.6    Brockhausen, J.7
  • 26
    • 0021919513 scopus 로고
    • Branch specificity of bovine colostrum CMPsialic acid: N-acetyllactosaminide α2-6-sialyltransferase. Interaction with biantennary oligosaccharides and glycopeptides of N-glycosylproteins
    • Joziasse, D.H., Schiphorst, W.E., van den Eijnden, D., van Kuik, J.A., van Halbeek, H. and Vliegenthart, J.F. (1985) Branch specificity of bovine colostrum CMPsialic acid: N-acetyllactosaminide α2-6-sialyltransferase. Interaction with biantennary oligosaccharides and glycopeptides of N-glycosylproteins. J. Biol. Chem. 260, 714-719.
    • (1985) J. Biol. Chem. , vol.260 , pp. 714-719
    • Joziasse, D.H.1    Schiphorst, W.E.2    Van Den Eijnden, D.3    Van Kuik, J.A.4    Van Halbeek, H.5    Vliegenthart, J.F.6
  • 27
    • 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, D.H., Schiphorst, W.E., van den Eijnden, D.H., van Kuik, J.A., van Halbeek, H. and Vliegenthart, J.F. (1987) 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., 262, 2025-33.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2025-2033
    • Joziasse, D.H.1    Schiphorst, W.E.2    Van Den Eijnden, D.H.3    Van Kuik, J.A.4    Van Halbeek, H.5    Vliegenthart, J.F.6
  • 28
    • 0028291625 scopus 로고
    • Differential expression of five sialyltransferase genes in human tissues
    • Kitagawa, H. and Paulson, J.C. (1994) Differential expression of five sialyltransferase genes in human tissues. J. Biol. Chem., 269, 17872-17878.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17872-17878
    • Kitagawa, H.1    Paulson, J.C.2
  • 29
    • 0013642280 scopus 로고
    • Structure and biosynthesis of cell surface carbohydrates
    • Fukuda, M. (ed.), CRC Press, London
    • Kobata, A. and Takasaki, S. (1992) Structure and biosynthesis of cell surface carbohydrates. In Fukuda, M. (ed.), Cell Surface Carbohydrates and Cell Developmen. CRC Press, London, pp. 1-24.
    • (1992) Cell Surface Carbohydrates and Cell Developmen , pp. 1-24
    • Kobata, A.1    Takasaki, S.2
  • 30
    • 0022572229 scopus 로고
    • Trafficking of lysosomal enzymes in normal and disease states
    • Kornfeld, S. (1986) Trafficking of lysosomal enzymes in normal and disease states. J. Clin. Invest., 77, 1-6.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1-6
    • Kornfeld, S.1
  • 31
    • 0019877155 scopus 로고
    • The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant
    • Kornfeld, K., Reitman, M.L. and Kornfeld, R. (1981) The carbohydrate-binding specificity of pea and lentil lectins. Fucose is an important determinant. J. Biol. Chem., 256, 6633-6640.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6633-6640
    • Kornfeld, K.1    Reitman, M.L.2    Kornfeld, R.3
  • 32
    • 0016813441 scopus 로고
    • Interaction of immunoglobulin glycopeptides with concanavalin A
    • Kornfeld, R. and Ferris, C. (1975) Interaction of immunoglobulin glycopeptides with concanavalin A. J. Biol. Chem., 250, 2614-2619.
    • (1975) J. Biol. Chem. , vol.250 , pp. 2614-2619
    • Kornfeld, R.1    Ferris, C.2
  • 33
    • 0017146754 scopus 로고
    • The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin A-sepharose
    • Krusius, T., Finne, J. and Rauvala, H. (1976) The structural basis of the different affinities of two types of acidic N-glycosidic glycopeptides for concanavalin A-sepharose. FEBS Lett., 72, 117-120.
    • (1976) FEBS Lett. , vol.72 , pp. 117-120
    • Krusius, T.1    Finne, J.2    Rauvala, H.3
  • 34
    • 0344331265 scopus 로고
    • Isolation of a cDNA encoding a murine UDP-galactose:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide α1,3-galactosyltransferase: Expression cloning by gene transfer
    • Larsen, R.D., Rajan, V.P., Ruff, M.M., Kukowaska-Latallo, J., Cummings, R.D. and Lowe, J.B. (1989) Isolation of a cDNA encoding a murine UDP-galactose:β-D-galactosyl-1,4-N-acetyl-D-glucosaminide α1,3-galactosyltransferase: expression cloning by gene transfer. Proc. Natl. Acad. Sci. USA, 86, 8227-8231.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8227-8231
    • Larsen, R.D.1    Rajan, V.P.2    Ruff, M.M.3    Kukowaska-Latallo, J.4    Cummings, R.D.5    Lowe, J.B.6
  • 35
    • 0024321508 scopus 로고
    • Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α2,6-sialyltransferase
    • Lee., E.U., Roth., J. and Paulson., J.C. (1989) Alteration of terminal glycosylation sequences on N-linked oligosaccharides of Chinese hamster ovary cells by expression of β-galactoside α2,6-sialyltransferase. J. Biol. Chem., 264, 13848-13855.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13848-13855
    • Lee, E.U.1    Roth, J.2    Paulson, J.C.3
  • 36
    • 0018844844 scopus 로고
    • Structure of an unusual complex-type oligosaccharide isolated from Chinese hamster ovary cells
    • Li, E., Gibson, R. and Kornfeld, S. (1980) Structure of an unusual complex-type oligosaccharide isolated from Chinese hamster ovary cells. Arch. Biochem. Biophys. 199, 393-399.
    • (1980) Arch. Biochem. Biophys. , vol.199 , pp. 393-399
    • Li, E.1    Gibson, R.2    Kornfeld, S.3
  • 37
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modification of recombinant P-selectin glycoprotein ligand-1 required for binding to P- and E-selectin
    • Li, F., Wilkins, P.P., Crawley, S., Weinstein, J., Cummings, R.D. and McEver, R.P. (1996) Post-translational modification of recombinant P-selectin glycoprotein ligand-1 required for binding to P-and E-selectin. J. Biol. Chem., 271, 3255-3264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3255-3264
    • Li, F.1    Wilkins, P.P.2    Crawley, S.3    Weinstein, J.4    Cummings, R.D.5    McEver, R.P.6
  • 38
    • 0026231669 scopus 로고
    • Molecular cloning, expression, and uses of mammalian glycosyltransferases
    • Lowe, J.B. (1991) Molecular cloning, expression, and uses of mammalian glycosyltransferases. Semin. Cell Biol., 2, 289-307.
    • (1991) Semin. Cell Biol. , vol.2 , pp. 289-307
    • Lowe, J.B.1
  • 39
    • 0029977263 scopus 로고    scopus 로고
    • Oligosaccharides containing 1,4-linked N-acetylgalactosamine, a paradigm for protein-specific glycosylation
    • Manzella, S.M., Hooper, L.V. and Baenziger, J.U. (1996) Oligosaccharides containing 1,4-linked N-acetylgalactosamine, a paradigm for protein-specific glycosylation. J. Biol. Chem., 271, 12117-12120.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12117-12120
    • Manzella, S.M.1    Hooper, L.V.2    Baenziger, J.U.3
  • 40
    • 0026452543 scopus 로고
    • A solid-phase assay for the activity of CMPNeuAc:Galβ1-4GlcNAc-R α2,6 sialyltransferase
    • Mattox, S., Walrath, K., Ceiler, D., Smith, D.F. and Cummings, R.D. (1992) A solid-phase assay for the activity of CMPNeuAc:Galβ1-4GlcNAc-R α2,6 sialyltransferase. Anal. Biochem., 206, 430-436.
    • (1992) Anal. Biochem. , vol.206 , pp. 430-436
    • Mattox, S.1    Walrath, K.2    Ceiler, D.3    Smith, D.F.4    Cummings, R.D.5
  • 41
    • 0029070815 scopus 로고
    • Leukocyte trafficking mediated by selectin-carbohydrate interactions
    • McEver, R.P., Moore, K.L. and Cummings, R.D. (1995) Leukocyte trafficking mediated by selectin-carbohydrate interactions. J. Biol. Chem., 270, 11025-11028.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11025-11028
    • McEver, R.P.1    Moore, K.L.2    Cummings, R.D.3
  • 42
    • 0023760470 scopus 로고
    • Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin
    • Merkle, R.K. and Cummings, R.D. (1988) Asparagine-linked oligosaccharides containing poly-N-acetyllactosamine chains are preferentially bound by immobilized calf heart agglutinin. J. Biol. Chem., 263, 16143-16149.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16143-16149
    • Merkle, R.K.1    Cummings, R.D.2
  • 43
    • 0021744087 scopus 로고
    • Spatial conformation of glycans and glycoproteins
    • Montreuil, J. (1984) Spatial conformation of glycans and glycoproteins. Biol. Cell. 51, 115-132.
    • (1984) Biol. Cell. , vol.51 , pp. 115-132
    • Montreuil, J.1
  • 44
    • 0027191058 scopus 로고
    • Enzymatic characterization of CMP-NeuAc:Galβ1-4GlcNAc-R α(2-3)-sialyltransferase from human placenta
    • Nemansky, M. and van den Eijnden, D.H. (1993) Enzymatic characterization of CMP-NeuAc:Galβ1-4GlcNAc-R α(2-3)-sialyltransferase from human placenta. Glycoconj. J., 10, 99-108.
    • (1993) Glycoconj. J. , vol.10 , pp. 99-108
    • Nemansky, M.1    Van Den Eijnden, D.H.2
  • 45
    • 0026544879 scopus 로고
    • The polypeptide part of human chorionic gonadotrophin affects the kinetics of α6-sialylation of its N-linked glycans but does not alter the branch specificity of CMP-NeuAc:Gal β1-4GlcNAc-R α2-6-sialyltransferase
    • Nemansky, M., Edzes, H.T., Wijnands, R.A. and van den Eijnden, D.H. (1992) The polypeptide part of human chorionic gonadotrophin affects the kinetics of α6-sialylation of its N-linked glycans but does not alter the branch specificity of CMP-NeuAc:Gal β1-4GlcNAc-R α2-6-sialyltransferase. Glycobiology, 2, 109-117.
    • (1992) Glycobiology , vol.2 , pp. 109-117
    • Nemansky, M.1    Edzes, H.T.2    Wijnands, R.A.3    Van Den Eijnden, D.H.4
  • 46
    • 0028982008 scopus 로고
    • Enzymic remodeling of the N- and O-linked carbohydrate chains of human chorionic gonadotropin. Effects on biological activity and receptor binding
    • Nemansky, M., DeLeeuw, R., Wijnands, R.A. and van den Eijnden, D.H (1995) Enzymic remodeling of the N-and O-linked carbohydrate chains of human chorionic gonadotropin. Effects on biological activity and receptor binding. Eur. J. Biochem., 227, 880-888.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 880-888
    • Nemansky, M.1    DeLeeuw, R.2    Wijnands, R.A.3    Van Den Eijnden, D.H.4
  • 47
    • 0016772320 scopus 로고
    • Fractionation of glycopeptides by affinity column chromatography on concanavalin A-sepharose
    • Ogata, S., Muramatsu, T. and Kobata, A. (1975) Fractionation of glycopeptides by affinity column chromatography on concanavalin A-sepharose. J. Biochem. (Tokyo), 78, 687-696.
    • (1975) J. Biochem. (Tokyo) , vol.78 , pp. 687-696
    • Ogata, S.1    Muramatsu, T.2    Kobata, A.3
  • 48
    • 0027369489 scopus 로고
    • Enzymatic modeling of the oligosaccharide chains of glycoproteins immobilized onto polystyrene surfaces
    • Orberger, G., Gessner, R., Fuchs, H., Volz, B., Kottgen, E. and Tauber, R. (1993) Enzymatic modeling of the oligosaccharide chains of glycoproteins immobilized onto polystyrene surfaces. Anal. Biochem., 214, 195-204.
    • (1993) Anal. Biochem. , vol.214 , pp. 195-204
    • Orberger, G.1    Gessner, R.2    Fuchs, H.3    Volz, B.4    Kottgen, E.5    Tauber, R.6
  • 49
    • 0024278682 scopus 로고
    • Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures
    • Passaniti, A. and Hart, G.W. (1988) Cell surface sialylation and tumor metastasis. Metastatic potential of B16 melanoma variants correlates with their relative numbers of specific penultimate oligosaccharide structures. J. Biol. Chem., 263, 7591-7603.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7591-7603
    • Passaniti, A.1    Hart, G.W.2
  • 51
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation
    • Paulson, J.C. and Colley, K.J. (1989) Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. J. Biol. Chem., 264, 17615-17618.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 52
    • 0028206055 scopus 로고
    • The oligosaccharide binding specificities of CD22β, a sialic acid-specific lectin of B cells
    • Powell, L.D. and Varki, A. (1994) The oligosaccharide binding specificities of CD22β, a sialic acid-specific lectin of B cells. J. Biol. Chem., 269, 10628-10636.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10628-10636
    • Powell, L.D.1    Varki, A.2
  • 53
    • 0029054907 scopus 로고
    • I-Type lectins
    • Powell, L.D. and Varki, A. (1995) I-Type lectins. J. Biol. Chem., 270, 14243-14246.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14243-14246
    • Powell, L.D.1    Varki, A.2
  • 54
    • 0027511875 scopus 로고
    • Natural ligands of the B cell adhesion molecule CD22 β carry N-linked oligosaccharides with α-2,6 -linked sialic acids that are required for recognition
    • Powell, L.D., Sgroi, D., Sjoberg, E.R., Stamenkovic, I. and Varki, A. (1993) Natural ligands of the B cell adhesion molecule CD22 β carry N-linked oligosaccharides with α-2,6 -linked sialic acids that are required for recognition. J. Biol. Chem., 268, 7019-7027.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7019-7027
    • Powell, L.D.1    Sgroi, D.2    Sjoberg, E.R.3    Stamenkovic, I.4    Varki, A.5
  • 56
    • 0027136155 scopus 로고
    • Structural study of the sugar chains of human leukocyte common antigen CD45
    • Sato, T., Furukawa, K., Autero, M., Gahmberg, C.G. and Kobata, A. (1993) Structural study of the sugar chains of human leukocyte common antigen CD45. Biochemistry, 32, 12694-12704.
    • (1993) Biochemistry , vol.32 , pp. 12694-12704
    • Sato, T.1    Furukawa, K.2    Autero, M.3    Gahmberg, C.G.4    Kobata, A.5
  • 57
    • 0022462129 scopus 로고
    • Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides
    • Schachter, H. (1986) Biosynthetic controls that determine the branching and microheterogeneity of protein-bound oligosaccharides. Biochem. Cell Biol. 64, 163-181.
    • (1986) Biochem. Cell Biol. , vol.64 , pp. 163-181
    • Schachter, H.1
  • 58
    • 0028043159 scopus 로고
    • Bi-antennary oligo-(N-acetyllactosamino) glycans of I-type are galactosylated preferentially at the GlcNAc β1-6Gal linked arms by α 1,3-galactosyltransferase of bovine thymus
    • Seppo, A., Penttila, L., Leppanen, A., Maaheimo, H., Niemela, R., Helin, J., Wieruszeski, J.M. and Renkonen, O. (1994) Bi-antennary oligo-(N-acetyllactosamino) glycans of I-type are galactosylated preferentially at the GlcNAc β1-6Gal linked arms by α 1,3-galactosyltransferase of bovine thymus. Glycoconj. J., 11, 217-225.
    • (1994) Glycoconj. J. , vol.11 , pp. 217-225
    • Seppo, A.1    Penttila, L.2    Leppanen, A.3    Maaheimo, H.4    Niemela, R.5    Helin, J.6    Wieruszeski, J.M.7    Renkonen, O.8
  • 59
  • 60
    • 0028889103 scopus 로고
    • The effect of the protein matrix proximity on glycan reactivity in a glycoprotein model
    • Shao, M.C. and Wold, F. (1995) The effect of the protein matrix proximity on glycan reactivity in a glycoprotein model. Eur. J. Biochem., 228, 79-85.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 79-85
    • Shao, M.C.1    Wold, F.2
  • 61
    • 0028762195 scopus 로고
    • Specificity studies of the GDP-L-fucose: 2-acetamido-2-deoxy-β-D-glucoside (FucvAsn-linked GlcNAc) 6-α-L-fucosyltransferase from rat-liver Golgi membranes
    • Shao, M.C., Sokolik, C.W. and Wold, F. (1994) Specificity studies of the GDP-L-fucose: 2-acetamido-2-deoxy-β-D-glucoside (FucvAsn-linked GlcNAc) 6-α-L-fucosyltransferase from rat-liver Golgi membranes. Carbohydrate Res., 251, 163-173.
    • (1994) Carbohydrate Res. , vol.251 , pp. 163-173
    • Shao, M.C.1    Sokolik, C.W.2    Wold, F.3
  • 63
    • 0026604570 scopus 로고
    • Molecular basis of recognition by the glycoprotein hormone-specific N-acetylgalactosamine-transferase
    • Smith, P.L. and Baenziger, J.U. (1992) Molecular basis of recognition by the glycoprotein hormone-specific N-acetylgalactosamine-transferase. Proc. Natl. Acad. Sci. USA, 89, 329-333.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 329-333
    • Smith, P.L.1    Baenziger, J.U.2
  • 64
    • 0025240089 scopus 로고
    • Transfer and expression of a murine UDP-Gal:β-D-Gal-α 1,3-galactosyltransferase gene in transfected Chinese hamster ovary cells. Competition reactions between the α 1,3-galactosyltransferase and the endogenous α 2,3-sialyltransferase
    • Smith., D.F., Larsen., R.D., Mattox., S., Lowe., J.B. and Cummings., R.D. (1990) Transfer and expression of a murine UDP-Gal:β-D-Gal-α 1,3-galactosyltransferase gene in transfected Chinese hamster ovary cells. Competition reactions between the α 1,3-galactosyltransferase and the endogenous α 2,3-sialyltransferase. J. Biol. Chem., 265, 6225-6234.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6225-6234
    • Smith, D.F.1    Larsen, R.D.2    Mattox, S.3    Lowe, J.B.4    Cummings, R.D.5
  • 65
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa, M.C., Ferrero-Garcia, M.A. and Parodi, A.J. (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry, 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 66
    • 84878788105 scopus 로고
    • Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin
    • Spik, G., Bayard, B., Fourner, B., Strecker, G., Bouquelet, S. and Montreuil, J. (1975) Studies on glycoconjugates. LXIV. Complete structure of two carbohydrate units of human serotransferrin. FEBS Lett., 50, 296-299.
    • (1975) FEBS Lett. , vol.50 , pp. 296-299
    • Spik, G.1    Bayard, B.2    Fourner, B.3    Strecker, G.4    Bouquelet, S.5    Montreuil, J.6
  • 68
    • 0021004081 scopus 로고
    • Labeling of plasma membrane glycoconjugates by terminal glycosylation (galactosyltransferase and glycosidase)
    • Thilo, L. (1983) Labeling of plasma membrane glycoconjugates by terminal glycosylation (galactosyltransferase and glycosidase). Methods Enzymol., 98, 415-421.
    • (1983) Methods Enzymol. , vol.98 , pp. 415-421
    • Thilo, L.1
  • 70
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology, 3, 97-130.
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 72
    • 0022555844 scopus 로고
    • Lysosomal enzymes and their receptors
    • Von Figura, K. and Hasilik, A. (1986) Lysosomal enzymes and their receptors. Annu. Rev. Biochem., 55, 167-193.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 167-193
    • Von Figura, K.1    Hasilik, A.2
  • 73
    • 0024278423 scopus 로고
    • The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing sialic acid-linked α2,3 to penultimate galactose residues
    • Wang, W.-C. and Cummings, R.D. (1988) The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing sialic acid-linked α2,3 to penultimate galactose residues. J. Biol. Chem., 263, 4576-4585.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4576-4585
    • Wang, W.-C.1    Cummings, R.D.2
  • 74
    • 0020491372 scopus 로고
    • Purification of a Galβ1-4GlcNAc α2-6 sialyltransferase and a Galβ1-3(4)GlcNAc α2-3sialyltransferase to homogeneity from rat liver
    • Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. (1982a) Purification of a Galβ1-4GlcNAc α2-6 sialyltransferase and a Galβ1-3(4)GlcNAc α2-3sialyltransferase to homogeneity from rat liver. J. Biol. Chem., 257, 13835-13844.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13835-13844
    • Weinstein, J.1    De Souza-e-Silva, U.2    Paulson, J.C.3
  • 75
    • 0020491419 scopus 로고
    • Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Galβ1-3(4)GlcNAc α2-3sialyltransferase and a Galβ1-4GlcNAc α2-6 sialyltransferase from rat liver
    • Weinstein, J., de Souza-e-Silva, U. and Paulson, J.C. (1982b) Sialylation of glycoprotein oligosaccharides N-linked to asparagine. Enzymatic characterization of a Galβ1-3(4)GlcNAc α2-3sialyltransferase and a Galβ1-4GlcNAc α2-6 sialyltransferase from rat liver. J. Biol. Chem., 257, 13845-13853.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13845-13853
    • Weinstein, J.1    De Souza-e-Silva, U.2    Paulson, J.C.3
  • 76
    • 0023192786 scopus 로고
    • Sialyltransferases as specific cell surface probes of terminal and penultimate saccharide structures on living cells
    • Whiteheart, S.W. and Hart, G.W. (1987) Sialyltransferases as specific cell surface probes of terminal and penultimate saccharide structures on living cells. Anal. Biochem., 163, 123-135.
    • (1987) Anal. Biochem. , vol.163 , pp. 123-135
    • Whiteheart, S.W.1    Hart, G.W.2
  • 78
    • 0025021141 scopus 로고
    • Surface of murine lymphocyte subsets differ in sialylation states and antigen distribution of a major N-linked penultimate saccharide structure
    • Whiteheart, S.W., McLenithan, J.C., and Hart, G.W. (1990) Surface of murine lymphocyte subsets differ in sialylation states and antigen distribution of a major N-linked penultimate saccharide structure. Cell Immunol., 125, 337-353.
    • (1990) Cell Immunol. , vol.125 , pp. 337-353
    • Whiteheart, S.W.1    McLenithan, J.C.2    Hart, G.W.3
  • 79
    • 0029763034 scopus 로고    scopus 로고
    • Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells
    • Wilkins, P., McEver, R.P. and Cummings, R.D. (1996) Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells. J. Biol. Chem., 271, 18732-18742.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18732-18742
    • Wilkins, P.1    McEver, R.P.2    Cummings, R.D.3
  • 80
    • 0029972452 scopus 로고    scopus 로고
    • Absorbance- and light-based solid-phase assays for CMPNueAc:Galβ1-4GlcNAc-R α-2,3-sialyltransferase
    • Yeh, J.-C. and Cummings, R.D. (1996) Absorbance-and light-based solid-phase assays for CMPNueAc:Galβ1-4GlcNAc-R α-2,3-sialyltransferase. Anal. Biochem., 236, 126-133.
    • (1996) Anal. Biochem. , vol.236 , pp. 126-133
    • Yeh, J.-C.1    Cummings, R.D.2
  • 81
    • 0027508349 scopus 로고
    • Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system
    • Yeh, J.-C., Seals, J.R., Murphy, C.I., van Halbeek, H., and Cummings, R.D. (1993) Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system. Biochemistry 32, 11087-11099.
    • (1993) Biochemistry , vol.32 , pp. 11087-11099
    • Yeh, J.-C.1    Seals, J.R.2    Murphy, C.I.3    Van Halbeek, H.4    Cummings, R.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.