메뉴 건너뛰기




Volumn 33, Issue 3, 1998, Pages 151-208

Concepts and principles of O-linked glycosylation

Author keywords

Blood group; Glycosyl tranferase; Glycosylation; Immunological recognition; MHC; Mucin; O glycan; Oligosaccharide; Selectin; Sialyl Lewis X; ZP3

Indexed keywords

ALPHA N ACETYLGALACTOSAMINIDASE; ANTIBODY; CELL SURFACE PROTEIN; CYTOPLASM PROTEIN; GLYCAN; GLYCOPROTEIN; IMMUNOGLOBULIN; LIGAND; MUCIN; N ACETYLGLUCOSAMINYLTRANSFERASE; NUCLEAR PROTEIN; OLIGOSACCHARIDE; SELECTIN; SERINE; SUGAR; THREONINE;

EID: 0031858428     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409239891204198     Document Type: Review
Times cited : (659)

References (230)
  • 2
    • 0029001438 scopus 로고
    • Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy
    • Allen, A.C., Harper, S.J., and Feehally, J. 1995. Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy. Clin. Exp. Immunol. 100: 470-474.
    • (1995) Clin. Exp. Immunol. , vol.100 , pp. 470-474
    • Allen, A.C.1    Harper, S.J.2    Feehally, J.3
  • 4
    • 0029076738 scopus 로고
    • The P-selectin glycoprotein ligand functions as a common human leukocyte ligand for P- and E-selectins
    • Asa, D., Raycroft, L., Ma, L., Aeed, P.A., Kaytes, P.S., Elhammer, A.P., and Geng, J.G. 1995. The P-selectin glycoprotein ligand functions as a common human leukocyte ligand for P- and E-selectins. J. Biol. Chem. 270: 11662-11670.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11662-11670
    • Asa, D.1    Raycroft, L.2    Ma, L.3    Aeed, P.A.4    Kaytes, P.S.5    Elhammer, A.P.6    Geng, J.G.7
  • 7
    • 0028856492 scopus 로고
    • Evidence for a third component in neutrophil aggregation: Potential roles of O-linked glycoproteins as L-selectin counter-structures
    • Bennett, T.A., Schammel, C.M., Lynam, E.B., Guyer, D.A., Mellors, A., Edwards, B., Rogelj, S., and Sklar, L.A. 1995B. Evidence for a third component in neutrophil aggregation: potential roles of O-linked glycoproteins as L-selectin counter-structures. J. Leukoc. Biol. 58: 510-518.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 510-518
    • Bennett, T.A.1    Schammel, C.M.2    Lynam, E.B.3    Guyer, D.A.4    Mellors, A.5    Edwards, B.6    Rogelj, S.7    Sklar, L.A.8
  • 8
    • 0030035111 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3
    • Bennett, E.P., Hassan, H., and Clausen, H. 1996. cDNA cloning and expression of a novel human UDP-N-acetyl-(-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3. J. Biol. Chem. 271: 17006-17012.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17006-17012
    • Bennett, E.P.1    Hassan, H.2    Clausen, H.3
  • 9
    • 7344252951 scopus 로고    scopus 로고
    • Identification of a glyco-syltransferase gene family controlling the initiation of O-glycosylation: Cloning, expression and genomic organization of 5UDP-GalNAc:polypeptide N-Acetylgalactosaminyl transferase isoforms
    • Copenhagen
    • Bennett, E.P., Hassan, H., Geurts van Kessel, A., and Clausen, H. 1997. Identification of a glyco-syltransferase gene family controlling the initiation of O-glycosylation: cloning, expression and genomic organization of 5UDP-GalNAc:polypeptide N-Acetylgalactosaminyl transferase isoforms. Workshop on "Mucin O-glycosylation: sites and processing", Copenhagen.
    • (1997) Workshop on "Mucin O-glycosylation: Sites and Processing"
    • Bennett, E.P.1    Hassan, H.2    Van Geurts Kessel, A.3    Clausen, H.4
  • 11
    • 0028968261 scopus 로고
    • Enzymatic removal of sialic acid from human factor IX and factor X has no effect on their coagulant activity
    • Bharadwaj, D., Harris, R. J., Kisiel, W., and Smith, K.J. 1995. Enzymatic removal of sialic acid from human factor IX and factor X has no effect on their coagulant activity. J. Biol. Chem. 270: 6537-6542.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6537-6542
    • Bharadwaj, D.1    Harris, R.J.2    Kisiel, W.3    Smith, K.J.4
  • 12
    • 0028041217 scopus 로고
    • Expression of a differentiation antigen and poly-N-acetyllactosaminyl O-glycans directed by a cloned core 2 β-1,6-N-acetylglucosami-nyltransferase
    • Bierhuizen, M.F.A., Maemura, K., and Fukuda, M. 1994. Expression of a differentiation antigen and poly-N-acetyllactosaminyl O-glycans directed by a cloned core 2 β-1,6-N-acetylglucosami-nyltransferase. J. Biol. Chem. 269: 4473-4479.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4473-4479
    • Bierhuizen, M.F.A.1    Maemura, K.2    Fukuda, M.3
  • 13
    • 0025818351 scopus 로고
    • Differential glycosylation of N-POMC1-77 regulates the production of gamma 3-MSH by purified pro-opiomelanocortin converting enzyme. A possible mechanism for tissue-specific processing
    • Birch, N.P., Estivariz, F.E., Bennett, H.P., and Loh, Y.P. 1991. Differential glycosylation of N-POMC1-77 regulates the production of gamma 3-MSH by purified pro-opiomelanocortin converting enzyme. A possible mechanism for tissue-specific processing. FEBS Lett. 290: 191-194.
    • (1991) FEBS Lett. , vol.290 , pp. 191-194
    • Birch, N.P.1    Estivariz, F.E.2    Bennett, H.P.3    Loh, Y.P.4
  • 14
    • 0025764566 scopus 로고
    • Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine
    • Bjoern, S., Foster, D.C., Thim, L., Wiberg, F.C., Christensen, M., Komiyama, Y., Pedersen, A.H., and Kisiel, W. 1991. Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. J. Biol. Chem. 266: 11051-11057.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11051-11057
    • Bjoern, S.1    Foster, D.C.2    Thim, L.3    Wiberg, F.C.4    Christensen, M.5    Komiyama, Y.6    Pedersen, A.H.7    Kisiel, W.8
  • 15
    • 0026787015 scopus 로고
    • O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome
    • Blumenfeld, O.O., Lalezari, P., Khorshidi, M., Puglia, K., and Fukuda, M. 1992. O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome. Blood 80: 2388-2395.
    • (1992) Blood , vol.80 , pp. 2388-2395
    • Blumenfeld, O.O.1    Lalezari, P.2    Khorshidi, M.3    Puglia, K.4    Fukuda, M.5
  • 16
    • 0025851570 scopus 로고
    • Biosynthesis of O-glycans in leukocytes from normal donors and from patients with leukemia: Increase in O-glycan core 2 UDP-GIcNAc: GalβGalNAcα-R (GIcNAc to GalNAc) β(1-6)-N-Acetylglucosaminyltransferase in leukemic cells
    • Brockhausen, I., Kuhns, W., Schachter, H., Matta, K.L., Sutherland, D.R., and Baker, M.A. 1991. Biosynthesis of O-glycans in leukocytes from normal donors and from patients with leukemia: increase in O-glycan core 2 UDP-GIcNAc: GalβGalNAcα-R (GIcNAc to GalNAc) β(1-6)-N-Acetylglucosaminyltransferase in leukemic cells. Cancer Res. 51: 1257-1263.
    • (1991) Cancer Res. , vol.51 , pp. 1257-1263
    • Brockhausen, I.1    Kuhns, W.2    Schachter, H.3    Matta, K.L.4    Sutherland, D.R.5    Baker, M.A.6
  • 17
    • 0028817837 scopus 로고
    • Chicken oocytes and somatic cells express different splice variants of a multifunctional receptor
    • Bujo, H., Lindstedt, K.A., Hermann, M., Dalmau, L.M., Nimpf, J., and Schneider, W.J. 1995. Chicken oocytes and somatic cells express different splice variants of a multifunctional receptor. J. Biol. Chem. 270: 23546.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23546
    • Bujo, H.1    Lindstedt, K.A.2    Hermann, M.3    Dalmau, L.M.4    Nimpf, J.5    Schneider, W.J.6
  • 18
    • 0000297709 scopus 로고
    • Conformational energy calculations and proton nuclear overhauser enhancements reveal a unique conformation for blood group A oligosaccharides
    • Bush, C.A., Yan, Z.-Y., and Rao, B.N.N. 1986. Conformational energy calculations and proton nuclear overhauser enhancements reveal a unique conformation for blood group A oligosaccharides. J. Am. Chem. Soc. 108: 6168-6173.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 6168-6173
    • Bush, C.A.1    Yan, Z.-Y.2    Rao, B.N.N.3
  • 19
    • 0028520130 scopus 로고
    • Glycosylated boar spermadhesin A WN-1 isoforms. Biological origin, structural characterization by lectin mapping, localization of O-glycosylation sites, and effect of glycosylation on ligand binding
    • Calvete, J.J., Solis, D., Sanz, L., Diaz-Maurino, T., and Topfer-Petersen, E. 1994. Glycosylated boar spermadhesin A WN-1 isoforms. Biological origin, structural characterization by lectin mapping, localization of O-glycosylation sites, and effect of glycosylation on ligand binding. Biol. Chem. Hoppe-Seyler. 375: 667-673.
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 667-673
    • Calvete, J.J.1    Solis, D.2    Sanz, L.3    Diaz-Maurino, T.4    Topfer-Petersen, E.5
  • 20
    • 0029026052 scopus 로고
    • Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: Effect of glycosylation on its heparin- and gelatin-binding capabilities
    • Calvete, J.J., Mann, K., Schafer, W., Sanz, L., Reinert, M., Nessau, S., Raida, M., and Topfer-Petersen, E. 1995. Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities. Biochem. J. 310: 615-622.
    • (1995) Biochem. J. , vol.310 , pp. 615-622
    • Calvete, J.J.1    Mann, K.2    Schafer, W.3    Sanz, L.4    Reinert, M.5    Nessau, S.6    Raida, M.7    Topfer-Petersen, E.8
  • 21
    • 0025980339 scopus 로고
    • Cell surface mucin-type glycoproteins and mucin-like domains
    • Carraway, K.L. and Hull, S.R. 1991. Cell surface mucin-type glycoproteins and mucin-like domains. Glycobiology 1: 131-138.
    • (1991) Glycobiology , vol.1 , pp. 131-138
    • Carraway, K.L.1    Hull, S.R.2
  • 22
    • 0028178517 scopus 로고
    • Regulation of eIF-2 alpha-subunit phosphorylation in reticulocyte lysate
    • Chakraborty, A., Saha, D., Bose, A., Chatterjee, M., and Gupta, N.K. 1994. Regulation of eIF-2 alpha-subunit phosphorylation in reticulocyte lysate. Biochemistry 33: 6700-6706.
    • (1994) Biochemistry , vol.33 , pp. 6700-6706
    • Chakraborty, A.1    Saha, D.2    Bose, A.3    Chatterjee, M.4    Gupta, N.K.5
  • 23
    • 0029914496 scopus 로고    scopus 로고
    • O-linked oligosaccharide on the 75-kDa neurotrophin receptor
    • Chapman, B.S., Eckart, M.R., Kaufman, S.E., and Lapointe, G.R. 1996. O-linked oligosaccharide on the 75-kDa neurotrophin receptor. J. Neuro-chem.66: 1707-1716.
    • (1996) J. Neuro-chem. , vol.66 , pp. 1707-1716
    • Chapman, B.S.1    Eckart, M.R.2    Kaufman, S.E.3    Lapointe, G.R.4
  • 24
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin
    • Chiba, A., Matsumura, K., Yamada, H., Inazu, T., Shimizu, T., Kusunoki, S., Kanazawa, I., Kobata, A., and Endo, T. 1997. Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin, J. Biol. Chem. 272: 2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 25
    • 0027506091 scopus 로고
    • Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18
    • Chou, C.F. and Omary, M.B. 1993. Mitotic arrest-associated enhancement of O-linked glycosylation and phosphorylation of human keratins 8 and 18. J. Biol. Chem. 268: 4465-4472.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4465-4472
    • Chou, C.F.1    Omary, M.B.2
  • 26
    • 0029049198 scopus 로고
    • cMyc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas
    • Chou, T.-Y., Hart, G.W., and Dang, C.V. 1995. cMyc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas. J. Biol. Chem. 270: 18961-18965.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18961-18965
    • Chou, T.-Y.1    Hart, G.W.2    Dang, C.V.3
  • 27
    • 0029854393 scopus 로고    scopus 로고
    • A family of UDP-GalNAc: Polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation
    • Clausen, H. and Bennett, E.P. 1996. A family of UDP-GalNAc: polypeptide N-acetylgalactosaminyl-transferases control the initiation of mucin-type O-linked glycosylation. Glycobiology 6: 635-646.
    • (1996) Glycobiology , vol.6 , pp. 635-646
    • Clausen, H.1    Bennett, E.P.2
  • 30
    • 0029861773 scopus 로고    scopus 로고
    • The modern investigation of mucus glycoproteins and their role in gastrointestinal disease
    • Corfield, A.P. and Warren, B.F. 1996. The modern investigation of mucus glycoproteins and their role in gastrointestinal disease. J. Pathol. 180: 8-17.
    • (1996) J. Pathol. , vol.180 , pp. 8-17
    • Corfield, A.P.1    Warren, B.F.2
  • 33
    • 0026021936 scopus 로고
    • The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glyco-sylation
    • Cyster, J.G., Shotton, D.M., and Williams, A.F. 1991. The dimensions of the T lymphocyte glycoprotein leukosialin and identification of linear protein epitopes that can be modified by glyco-sylation. EMBO J. 10: 893-902.
    • (1991) EMBO J. , vol.10 , pp. 893-902
    • Cyster, J.G.1    Shotton, D.M.2    Williams, A.F.3
  • 34
    • 0027457979 scopus 로고
    • Regulation of UDP-GlcNAc:Galβ1-3GalNAc-R β1-6-N-Acetyl-glucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells
    • Datti, A. and Dennis, J.W. 1993. Regulation of UDP-GlcNAc:Galβ1-3GalNAc-R β1-6-N-Acetyl-glucosaminyltransferase (GlcNAc to GalNAc) in Chinese hamster ovary cells. J. Biol. Chem. 268: 5409-5416.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5409-5416
    • Datti, A.1    Dennis, J.W.2
  • 35
    • 0027278676 scopus 로고
    • Serum "big insulin-like growth factor II" from patients with tumor hypoglycemia lacks normal E-domain O-linked glycosylation, a possible determinant of normal propeptide processing
    • Daughaday, W.H., Trivedi, B., and Baxter, R.C. 1993. Serum "big insulin-like growth factor II" from patients with tumor hypoglycemia lacks normal E-domain O-linked glycosylation, a possible determinant of normal propeptide processing. Proc. Natl Acad. Sci U.S.A. 90: 5823-5827.
    • (1993) Proc. Natl Acad. Sci U.S.A. , vol.90 , pp. 5823-5827
    • Daughaday, W.H.1    Trivedi, B.2    Baxter, R.C.3
  • 36
    • 0028138630 scopus 로고
    • The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae
    • Dey, N.B., Bounelis, P., Fritz, T.A., Bedwell, D.M., and Marchase, R.B. 1994. The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 269: 27143-27148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27143-27148
    • Dey, N.B.1    Bounelis, P.2    Fritz, T.A.3    Bedwell, D.M.4    Marchase, R.B.5
  • 37
    • 0028924164 scopus 로고
    • Endocrinology of the carbohydrate-deficiënt glycoprotein syndrome type 1 from birth through adolescence
    • de Zegher, F. and Jaeken, J. 1995. Endocrinology of the carbohydrate-deficiënt glycoprotein syndrome type 1 from birth through adolescence. Pediatric Res. 37: 395-401.
    • (1995) Pediatric Res. , vol.37 , pp. 395-401
    • De Zegher, F.1    Jaeken, J.2
  • 38
    • 0028085881 scopus 로고
    • Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol
    • Dong, D.L. and Hart, G.W. 1994. Purification and characterization of an O-GlcNAc selective N-acetyl-beta-D-glucosaminidase from rat spleen cytosol. J. Biol. Chem. 269: 19321-19330.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19321-19330
    • Dong, D.L.1    Hart, G.W.2
  • 39
    • 0029058523 scopus 로고
    • Boar spermadhesin AWN-1. Oligosaccharide and zona pellucida binding characteristics
    • Dostalova, Z., Calvete, J.J., Sanz, L., and Topfer-Petersen, E. 1995. Boar spermadhesin AWN-1. Oligosaccharide and zona pellucida binding characteristics. Eur. J. Biochem. 230: 329-336.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 329-336
    • Dostalova, Z.1    Calvete, J.J.2    Sanz, L.3    Topfer-Petersen, E.4
  • 40
    • 0027327816 scopus 로고
    • Glycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) mucin is expressed by lactating mammary gland epithelial cells and is present in milk
    • Dowbenko, D., Kikuta, A., Fennie, C., Gillett, N., and Lasky, L.A. 1993. Glycosylation-dependent cell adhesion molecule 1 (GlyCAM 1) mucin is expressed by lactating mammary gland epithelial cells and is present in milk. J. Clin. Invest. 92: 952-960.
    • (1993) J. Clin. Invest. , vol.92 , pp. 952-960
    • Dowbenko, D.1    Kikuta, A.2    Fennie, C.3    Gillett, N.4    Lasky, L.A.5
  • 41
    • 0026342559 scopus 로고
    • Clearing up glycoprotein hormones
    • Drickamer, K. 1991. Clearing up glycoprotein hormones. Cell 67: 1029-1032.
    • (1991) Cell , vol.67 , pp. 1029-1032
    • Drickamer, K.1
  • 42
    • 0029015255 scopus 로고
    • Purification and partial characterization of acrosome reaction inhibiting glycoprotein from human seminal plasma
    • Drisdel, R.C., Mack, S.R., Anderson, R.A., and Zaneveld, L.J.D. 1995. Purification and partial characterization of acrosome reaction inhibiting glycoprotein from human seminal plasma. Bio. Reprod. 53: 201-208.
    • (1995) Bio. Reprod. , vol.53 , pp. 201-208
    • Drisdel, R.C.1    Mack, S.R.2    Anderson, R.A.3    Zaneveld, L.J.D.4
  • 43
    • 0030061494 scopus 로고    scopus 로고
    • Visualisation of human sCD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • Dustin, M.L., Ferguson, L.M., Chan, P.Y., Springer, T.A., and Golan, D. E. 1996. Visualisation of human sCD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area. J. Cell. Biol. 132: 456-474.
    • (1996) J. Cell. Biol. , vol.132 , pp. 456-474
    • Dustin, M.L.1    Ferguson, L.M.2    Chan, P.Y.3    Springer, T.A.4    Golan, D.E.5
  • 44
    • 0026517233 scopus 로고
    • The unique N-terminal sequence of testis angiotensin-converting enzyme is heavily O-glyco-sylated and unessential for activity or stability
    • Ehlers, M.R., Chen, Y.N., and Riordan, J.F. 1992. The unique N-terminal sequence of testis angiotensin-converting enzyme is heavily O-glyco-sylated and unessential for activity or stability. Biochem. Biophys. Res. Commun. 183: 199-205.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 199-205
    • Ehlers, M.R.1    Chen, Y.N.2    Riordan, J.F.3
  • 45
    • 0027280810 scopus 로고
    • The specificity of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides
    • Elhammer, A.P., Poorman, R.A., Brown, E., Maggiora, L.L., Hoogerheide, J.G., and Kézdy, F.J. 1993. The specificity of UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase as inferred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides. J. Biol. Chem. 268: 10029-10038.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10029-10038
    • Elhammer, A.P.1    Poorman, R.A.2    Brown, E.3    Maggiora, L.L.4    Hoogerheide, J.G.5    Kézdy, F.J.6
  • 46
    • 0028258920 scopus 로고
    • Biochemical and biologic characterization of murine monocyte chemoattractant protein-1. Identification of two functional domains
    • Ernst, C.A., Zhang, Y J., Hancock, P.R., Rutledge, B.J., Corless, C.L., and Rollins, B.J. 1994. Biochemical and biologic characterization of murine monocyte chemoattractant protein-1. Identification of two functional domains. J. Immunol. 152: 3541-3549.
    • (1994) J. Immunol. , vol.152 , pp. 3541-3549
    • Ernst, C.A.1    Zhang, Y.J.2    Hancock, P.R.3    Rutledge, B.J.4    Corless, C.L.5    Rollins, B.J.6
  • 47
    • 0028280439 scopus 로고
    • Structural analysis of the N-glycans from human immunoglobulin A1: Comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis
    • Field, M.C., Amatayakul-Chantler, S., Rademacher, T.W., Rudd, P.M. and Dwek, R.A. 1994, Structural analysis of the N-glycans from human immunoglobulin A1: comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid arthritis. Biochem. J. 299: 261-275.
    • (1994) Biochem. J. , vol.299 , pp. 261-275
    • Field, M.C.1    Amatayakul-Chantler, S.2    Rademacher, T.W.3    Rudd, P.M.4    Dwek, R.A.5
  • 48
    • 0029144380 scopus 로고
    • Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: A survey
    • Field, M.C. and Wainwright, L.J. 1995. Molecular cloning of eukaryotic glycoprotein and glycolipid glycosyltransferases: a survey. Glycobiology 5: 463-472.
    • (1995) Glycobiology , vol.5 , pp. 463-472
    • Field, M.C.1    Wainwright, L.J.2
  • 49
    • 0028871510 scopus 로고
    • The 220-kDa vitelline coat glycoprotein mediates sperm binding in the polarized egg of Unio elongatulus through O-linked oligosaccharides
    • Focarelli, R. and Rosati, F. 1995. The 220-kDa vitelline coat glycoprotein mediates sperm binding in the polarized egg of Unio elongatulus through O-linked oligosaccharides. Dev. Biol. 171: 606-614.
    • (1995) Dev. Biol. , vol.171 , pp. 606-614
    • Focarelli, R.1    Rosati, F.2
  • 50
    • 0023227217 scopus 로고
    • Primary defect of congenital dyserythropoietic anemia type II: Failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by a lowered N-acetylglucosaminyltransferase II
    • Fukuda, M.N., Dell, A., and Scartezzini, P. 1987. Primary defect of congenital dyserythropoietic anemia type II: failure in glycosylation of erythrocyte lactosaminoglycan proteins caused by a lowered N-acetylglucosaminyltransferase II. J. Biol. Chem. 262: 7195-7206.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7195-7206
    • Fukuda, M.N.1    Dell, A.2    Scartezzini, P.3
  • 51
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch, M. and Tanner, W. 1996. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J. 15: 5752-5759.
    • (1996) EMBO J. , vol.15 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 52
    • 43949151961 scopus 로고
    • Surface-bound cytokines - A possible effector mechanism in bacterial immunity?
    • George, A.J.T. 1994. Surface-bound cytokines - a possible effector mechanism in bacterial immunity? Immunol. Today 15: 88-89.
    • (1994) Immunol. Today , vol.15 , pp. 88-89
    • George, A.J.T.1
  • 53
    • 0024319438 scopus 로고
    • Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: Carbon-13 NMR studies of ovine submaxillary mucin
    • Gerken, T.A., Butenhof, K.J. and Shogren, R. 1989. Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins: carbon-13 NMR studies of ovine submaxillary mucin. Biochemistry 28: 5536-5543.
    • (1989) Biochemistry , vol.28 , pp. 5536-5543
    • Gerken, T.A.1    Butenhof, K.J.2    Shogren, R.3
  • 54
    • 0031025469 scopus 로고    scopus 로고
    • Mucin genes expressed by the ocular surface epithelium
    • Gipson, I.K. and Inatomi, T. 1997. Mucin genes expressed by the ocular surface epithelium. Prog. Retin. Eye Res. 16: 81-98.
    • (1997) Prog. Retin. Eye Res. , vol.16 , pp. 81-98
    • Gipson, I.K.1    Inatomi, T.2
  • 56
    • 0029094342 scopus 로고
    • Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm
    • Gong, X., Dubois, D.H., Miller, D.J., and Shur, B.D. 1995. Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm. Science 269: 1718-1721.
    • (1995) Science , vol.269 , pp. 1718-1721
    • Gong, X.1    Dubois, D.H.2    Miller, D.J.3    Shur, B.D.4
  • 57
    • 0031016884 scopus 로고    scopus 로고
    • How to find, identify and quantitate the sugars on proteins
    • Gooley, A.A. and Williams, K.L. 1997. How to find, identify and quantitate the sugars on proteins. Nature 385: 557-559.
    • (1997) Nature , vol.385 , pp. 557-559
    • Gooley, A.A.1    Williams, K.L.2
  • 58
    • 85007856280 scopus 로고
    • Role of the carbohydrate moiety of a glucoamylase from Aspergillus awamori var. kawachi in the digestion of raw starch
    • Goto, M., Kuwano, E., Kanlayakrit, W., and Hayashida, S. 1995. Role of the carbohydrate moiety of a glucoamylase from Aspergillus awamori var. kawachi in the digestion of raw starch. Biosci. Biotechnol. Biochem. 59: 16-20.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 16-20
    • Goto, M.1    Kuwano, E.2    Kanlayakrit, W.3    Hayashida, S.4
  • 59
    • 0027931371 scopus 로고
    • Isolation and characterization of novel mucin-like glycoproteins from cobra venom
    • Gowda, D.C. and Davidson, E.A. 1994. Isolation and characterization of novel mucin-like glycoproteins from cobra venom. J. Biol. Chem. 269: 20031-20039.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20031-20039
    • Gowda, D.C.1    Davidson, E.A.2
  • 61
    • 0028988780 scopus 로고
    • Beta-amyloid precursor protein is modified with O-linked N-acetylglucosamine
    • Griffith, L.S., Mathes, and M., Schmitz, B. 1995. Beta-amyloid precursor protein is modified with O-linked N-acetylglucosamine. J. Neurosci. Res. 41: 270-278.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 270-278
    • Griffith, L.S.1    Mathes, M.2    Schmitz, B.3
  • 62
    • 0029120744 scopus 로고
    • O-linked N-acetylglucosamine is upregulated in Alzheimer brains
    • Griffith, L. S. and Schmitz, B. 1995. O-linked N-acetylglucosamine is upregulated in Alzheimer brains. Biochem. Biophys. Res. Commun. 213: 424-431.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 424-431
    • Griffith, L.S.1    Schmitz, B.2
  • 63
    • 0027244101 scopus 로고
    • Purification, cloning and expression of a bovine UDP-GalNAc: Polypeptide N-acetyl-galactosaminyltransferase
    • Hagen, F. K., Van Wuyckhuyse, B., and Tabak, L. A. 1993. Purification, cloning and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase. J. Biol. Chem. 268: 18960-18965.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18960-18965
    • Hagen, F.K.1    Van Wuyckhuyse, B.2    Tabak, L.A.3
  • 65
    • 0030922124 scopus 로고    scopus 로고
    • cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
    • Hagen, F. K., Ten Hagen, K. G., Beres, T. M., Balys, M. M., Van Wuyckhuyse, B. C., and Tabak, L. A. 1997. cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem. 272: 13843-13848.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13843-13848
    • Hagen, F.K.1    Ten Hagen, K.G.2    Beres, T.M.3    Balys, M.M.4    Van Wuyckhuyse, B.C.5    Tabak, L.A.6
  • 66
    • 0028177015 scopus 로고
    • Alpha-fucose-mediated binding and degradation of tissue-type plasminogen activator by HepG2 cells
    • Hajjar, K. A. and Reynolds, C. M. 1994. Alpha-fucose-mediated binding and degradation of tissue-type plasminogen activator by HepG2 cells. J. Clin. Invest. 93: 703-710.
    • (1994) J. Clin. Invest. , vol.93 , pp. 703-710
    • Hajjar, K.A.1    Reynolds, C.M.2
  • 67
    • 0025193520 scopus 로고
    • Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine::peptide β-N-acetylglucosaminyl-transferase
    • Haltiwanger, R. S., Holt, G. D., and Hart, G. W. 1990. Enzymatic addition of O-GlcNAc to nuclear and cytoplasmic proteins. Identification of a uridine diphospho-N-acetylglucosamine::peptide β-N-acetylglucosaminyl-transferase. J. Biol. Chem. 265: 2563-2568.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2563-2568
    • Haltiwanger, R.S.1    Holt, G.D.2    Hart, G.W.3
  • 68
    • 0029966497 scopus 로고    scopus 로고
    • MUC1 glycoforms in breast cancer. Cell line T47D as a model for carcinoma-associated alterations of O-glycosylation
    • Hanisch, F. G., Stadie, T. R., Deutzmann, F., and Peter-Katalinic, J. 1996. MUC1 glycoforms in breast cancer. Cell line T47D as a model for carcinoma-associated alterations of O-glycosylation. Eur. J. Biochem. 236: 318-327.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 318-327
    • Hanisch, F.G.1    Stadie, T.R.2    Deutzmann, F.3    Peter-Katalinic, J.4
  • 69
    • 0029003322 scopus 로고
    • Prediction of O-glycosylation of mammalian proteins: Specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Hansen, J. E., Lund, O., Engelbrecht, J., Bohr, H., Nielsen, J. O., Hansen, J.-E. S., and Brunak, S. 1995. Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. Biochem. J. 308: 801-813.
    • (1995) Biochem. J. , vol.308 , pp. 801-813
    • Hansen, J.E.1    Lund, O.2    Engelbrecht, J.3    Bohr, H.4    Nielsen, J.O.5    Hansen, J.-E.S.6    Brunak, S.7
  • 70
    • 0030860232 scopus 로고    scopus 로고
    • O-GLYCBASE version 2.0: A revised database of O-glycosylated proteins
    • Hansen, J. E., Lund, O., and Brunak, S. 1997. O-GLYCBASE version 2.0: a revised database of O-glycosylated proteins. Nucleic Acids Res. 25: 278-282.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 278-282
    • Hansen, J.E.1    Lund, O.2    Brunak, S.3
  • 71
    • 0025872471 scopus 로고
    • Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain
    • Harris, R. J., Leonard, C. K., Guzzetta, A. W., and Spellman, M. W. 1991. Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain. Biochemistry 30: 2311-2314.
    • (1991) Biochemistry , vol.30 , pp. 2311-2314
    • Harris, R.J.1    Leonard, C.K.2    Guzzetta, A.W.3    Spellman, M.W.4
  • 72
    • 0026700166 scopus 로고
    • O-linked fucose is present in the first epidermal growth factor domain of human factor XII but not protein C
    • Harris, R. J., Ling, V. T., and Spellman, M. W. 1992. O-linked fucose is present in the first epidermal growth factor domain of human factor XII but not protein C. J. Biol. Chem. 267: 5102-5107.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5102-5107
    • Harris, R.J.1    Ling, V.T.2    Spellman, M.W.3
  • 73
    • 0027203036 scopus 로고
    • Identification and structural analysis of of the tetrasaccharide NeuAcα(2-6)Galβ(1-4) GlcNAcβ(1-3)Fucα1-O linked to Ser-61 of human factor IX
    • Harris, R. J., van Halbeek, H., Glushka, J., Basa, L. J., Ling, V, T., Smith, K. J., and Spellman, M. W. 1993. Identification and structural analysis of of the tetrasaccharide NeuAcα(2-6)Galβ(1-4) GlcNAcβ(1-3)Fucα1-O linked to Ser-61 of human factor IX. Biochemistry 32: 6539-6547.
    • (1993) Biochemistry , vol.32 , pp. 6539-6547
    • Harris, R.J.1    Van Halbeek, H.2    Glushka, J.3    Basa, L.J.4    Ling, V.T.5    Smith, K.J.6    Spellman, M.W.7
  • 74
    • 0027205366 scopus 로고
    • O-linked fucose and other post-translational modifications unique to EGF-modules
    • Harris, R. J. and Spellman, M. W. 1993. O-linked fucose and other post-translational modifications unique to EGF-modules. Glycobiology 3:219-224.
    • (1993) Glycobiology , vol.3 , pp. 219-224
    • Harris, R.J.1    Spellman, M.W.2
  • 76
    • 0030943923 scopus 로고    scopus 로고
    • Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins
    • Hart, G. W. 1997. Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins. Annu. Rev. Biochem. 66: 315-335.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 315-335
    • Hart, G.W.1
  • 78
    • 0027718044 scopus 로고
    • A thermodynamic model for denaturation of granulocyte colony-stimulating factor: O-linked sugar chain suppresses not the triggering deprotonation but the succeeding denaturation
    • Hasegawa, M. 1993. A thermodynamic model for denaturation of granulocyte colony-stimulating factor: O-linked sugar chain suppresses not the triggering deprotonation but the succeeding denaturation. Biochim. Biophys. Acta. 1203: 295-297.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 295-297
    • Hasegawa, M.1
  • 79
    • 0028318850 scopus 로고
    • Recognition of carbohydrate by major histocompatibility complex class I-restricted, glycopeptide-specific cytotoxic T lymphocytes
    • Haurum, J. S., Arsequell, G., Lellouch, A. C., Wong, S. Y., Dwek, R. A., McMichael, A. J., and Elliott, T. 1994. Recognition of carbohydrate by major histocompatibility complex class I-restricted, glycopeptide-specific cytotoxic T lymphocytes. J. Exp. Med. 180: 739-744.
    • (1994) J. Exp. Med. , vol.180 , pp. 739-744
    • Haurum, J.S.1    Arsequell, G.2    Lellouch, A.C.3    Wong, S.Y.4    Dwek, R.A.5    McMichael, A.J.6    Elliott, T.7
  • 80
    • 0029616107 scopus 로고
    • Peptide anchor residue glycosylation: Effect on class I major histocompatibility complex binding and cytotoxic T lymphocyte recognition
    • Haurum, J.S., Tan, L., Arsequell, G., Frodsham, P., Lellouch, A.C., Moss, P.A., Dwek, R.A., McMichael, A.J., and Elliott, T. 1995. Peptide anchor residue glycosylation: effect on class I major histocompatibility complex binding and cytotoxic T lymphocyte recognition. Eur. J. Immunol. 25: 3270-3276.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 3270-3276
    • Haurum, J.S.1    Tan, L.2    Arsequell, G.3    Frodsham, P.4    Lellouch, A.C.5    Moss, P.A.6    Dwek, R.A.7    McMichael, A.J.8    Elliott, T.9
  • 81
    • 0026693093 scopus 로고
    • Yeast glycoprotein biosynthesis: MNT1 encodes an α-1,2-mannosyltransferase involved in O-glycosylation
    • Häusler, A., Ballou, L., Ballou, E.C., and Robbins, P.W. 1992. Yeast glycoprotein biosynthesis: MNT1 encodes an α-1,2-mannosyltransferase involved in O-glycosylation. Proc. Natl. Acad. Sci. U.S.A. 89: 6846-6850.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6846-6850
    • Häusler, A.1    Ballou, L.2    Ballou, E.C.3    Robbins, P.W.4
  • 82
    • 0027530462 scopus 로고
    • Branching β1-6N-acetylglucosaminylatransferases and polylactosamine expression in mouse F9 teratocarcinoma cells and differentiated counterparts
    • Heffernan, M, Lotan, R., Amos, B., Palcic, M., Takano, R., and Bennet, J.W. 1993. Branching β1-6N-acetylglucosaminylatransferases and polylactosamine expression in mouse F9 teratocarcinoma cells and differentiated counterparts. J. Biol. Chem. 268: 1242-1251.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1242-1251
    • Heffernan, M.1    Lotan, R.2    Amos, B.3    Palcic, M.4    Takano, R.5    Bennet, J.W.6
  • 83
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A. and Orlean, P. 1993. Glycoprotein biosynthesis in yeast. FASEB J. 7: 540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 85
    • 0025817137 scopus 로고
    • Aberrant O-linked oligosaccharide biosynthesis in lymphocytes and platelets from patients with the Wiskott-Aldrich syndrome
    • Higgins, E.A., Siminovitch, K.A., Zhuang, D.L., Brockhausen, I., and Dennis, J.W. 1991. Aberrant O-linked oligosaccharide biosynthesis in lymphocytes and platelets from patients with the Wiskott-Aldrich syndrome. J. Biol. Chem. 266: 6280-6290.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6280-6290
    • Higgins, E.A.1    Siminovitch, K.A.2    Zhuang, D.L.3    Brockhausen, I.4    Dennis, J.W.5
  • 86
    • 0027178358 scopus 로고
    • Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
    • Homa, F.L., Hollander, T., Lehman, D.J., Thomsen, D.R., and Elhammer, A.P. 1993. Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem. 268: 12609-12616.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12609-12616
    • Homa, F.L.1    Hollander, T.2    Lehman, D.J.3    Thomsen, D.R.4    Elhammer, A.P.5
  • 87
    • 0029820671 scopus 로고    scopus 로고
    • From legumes to leukocytes: Biological roles for sulfated carbohydrates
    • Hooper, L.V., Manzella, S.M., and Baenzinger, J.U. 1996. From legumes to leukocytes: biological roles for sulfated carbohydrates. FASEB. J. 10: 1137-1146.
    • (1996) FASEB. J. , vol.10 , pp. 1137-1146
    • Hooper, L.V.1    Manzella, S.M.2    Baenzinger, J.U.3
  • 88
    • 0030006293 scopus 로고    scopus 로고
    • O-linked protein glycosylation structure and function
    • Hounsell, E.F., Michael J.D., and Renouf, D.V. 1996. O-linked protein glycosylation structure and function. Glycoconj. J. 13: 19-26.
    • (1996) Glycoconj. J. , vol.13 , pp. 19-26
    • Hounsell, E.F.1    Michael, J.D.2    Renouf, D.V.3
  • 89
    • 0027964252 scopus 로고
    • Bacterial expression and in vitro folding of the beta-subunit of human chorionic gonadotropin (hCG beta) and functional assembly of recombinant hCG beta with hCG alpha
    • Huth, J.R., Norton, S.E., Lockridge, O., Shikone, T., Hsueh, A.J., and Ruddon, R.W. 1994. Bacterial expression and in vitro folding of the beta-subunit of human chorionic gonadotropin (hCG beta) and functional assembly of recombinant hCG beta with hCG alpha. Endocrinology 135: 911-918.
    • (1994) Endocrinology , vol.135 , pp. 911-918
    • Huth, J.R.1    Norton, S.E.2    Lockridge, O.3    Shikone, T.4    Hsueh, A.J.5    Ruddon, R.W.6
  • 90
    • 0027473659 scopus 로고
    • Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin
    • Imai, Y., Lasky, L.A., and Rosen, S.D. 1993. Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin. Nature 361: 555-557.
    • (1993) Nature , vol.361 , pp. 555-557
    • Imai, Y.1    Lasky, L.A.2    Rosen, S.D.3
  • 91
    • 0027426025 scopus 로고
    • Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X
    • Inoue, K. and Morita, T. 1993. Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X. Eur. J. Biochem. 218: 153-163.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 153-163
    • Inoue, K.1    Morita, T.2
  • 92
    • 0028809115 scopus 로고
    • Full active baculovirus-expressed human monocyte chemoattractant protein 1 with the intact N-terminus
    • Ishii, K., Yamagami, S., Tanaka, H., Motoki, M., Suwa, Y., and Endo, N. 1995, Full active baculovirus-expressed human monocyte chemoattractant protein 1 with the intact N-terminus. Biochem. Biophys. Res. Comm. 206: 955-961.
    • (1995) Biochem. Biophys. Res. Comm. , vol.206 , pp. 955-961
    • Ishii, K.1    Yamagami, S.2    Tanaka, H.3    Motoki, M.4    Suwa, Y.5    Endo, N.6
  • 93
    • 0029781201 scopus 로고    scopus 로고
    • Abundance of Galβ1,3GalNAc in O-linked oligosaccharide on hinge region of polymerized IgA1 and heat-aggregated IgA1 from normal human serum
    • Iwase, I., Tanaka, A., Hiki, Y., Kokubo, T., Ishii-Karakasa, I., Kobayashi, Y., and Hotta, K. 1996. Abundance of Galβ1,3GalNAc in O-linked oligosaccharide on hinge region of polymerized IgA1 and heat-aggregated IgA1 from normal human serum. J. Biochem. 120: 92-97.
    • (1996) J. Biochem. , vol.120 , pp. 92-97
    • Iwase, I.1    Tanaka, A.2    Hiki, Y.3    Kokubo, T.4    Ishii-Karakasa, I.5    Kobayashi, Y.6    Hotta, K.7
  • 94
    • 0027984467 scopus 로고
    • Modulation of complement regulatory function and measles virus receptor function by the serine-threonine-rich domains of membrane cofactor protein (CD46)
    • Iwata, K., Seya, T., Ueda, S., Ariga, H., and Nagasawa, S. 1994. Modulation of complement regulatory function and measles virus receptor function by the serine-threonine-rich domains of membrane cofactor protein (CD46). Biochem. J. 304: 169-175.
    • (1994) Biochem. J. , vol.304 , pp. 169-175
    • Iwata, K.1    Seya, T.2    Ueda, S.3    Ariga, H.4    Nagasawa, S.5
  • 95
    • 0028963272 scopus 로고
    • Characterization of human colon carcinoma variant cells selected for sialyl Lex carbohydrate antigen: Liver colonization and adhesion to vascular endothelial cells
    • Izumi, Y., Taniuchi, Y., Tsuji, T., Smith, C.W., Nakamori, S., Fidler, I.J., and Irimura, T. 1995. Characterization of human colon carcinoma variant cells selected for sialyl Lex carbohydrate antigen: liver colonization and adhesion to vascular endothelial cells. Exp. Cell. Res. 216: 215-221.
    • (1995) Exp. Cell. Res. , vol.216 , pp. 215-221
    • Izumi, Y.1    Taniuchi, Y.2    Tsuji, T.3    Smith, C.W.4    Nakamori, S.5    Fidler, I.J.6    Irimura, T.7
  • 96
    • 0000249979 scopus 로고
    • Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG deficiency, increased serum arylsulphatase A, and increased CSF-protein: A new syndrome?
    • Jaeken, J., Vanderschueren-Lodeweyckx, M., Casaer, P., Snoeck, L., Corbeel, L., Eggermont, E., and Eeckels, R. 1980. Familial psychomotor retardation with markedly fluctuating serum prolactin, FSH and GH levels, partial TBG deficiency, increased serum arylsulphatase A, and increased CSF-protein: a new syndrome? Pediatr. Res. 14: 170.
    • (1980) Pediatr. Res. , vol.14 , pp. 170
    • Jaeken, J.1    Vanderschueren-Lodeweyckx, M.2    Casaer, P.3    Snoeck, L.4    Corbeel, L.5    Eggermont, E.6    Eeckels, R.7
  • 97
    • 0027440619 scopus 로고
    • The carbohydrate-deficient glycoprotein syndromes: Pre-Golgi and Golgi disorders?
    • Jaeken, J., Carchon, H., and Stibler, H. 1993. The carbohydrate-deficient glycoprotein syndromes: pre-Golgi and Golgi disorders? Glycobiology 3: 423-428.
    • (1993) Glycobiology , vol.3 , pp. 423-428
    • Jaeken, J.1    Carchon, H.2    Stibler, H.3
  • 98
    • 0027930443 scopus 로고
    • Carbohydrate deficient glycoprotein syndrome type II: A deficiency in Golgi-localized N-acetylglucosaminyltransferase II
    • Jaeken, J., Schachter, H., Carchon, H., De Cock, P., Coddeville, B., and Spik, G. 1994. Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi-localized N-acetylglucosaminyltransferase II. Arch. Dis. Child. 71: 123-127.
    • (1994) Arch. Dis. Child. , vol.71 , pp. 123-127
    • Jaeken, J.1    Schachter, H.2    Carchon, H.3    De Cock, P.4    Coddeville, B.5    Spik, G.6
  • 99
    • 0028111088 scopus 로고
    • g-antigen: An example of modulation of antigenic properties of peptide by its glycosylation
    • g-antigen: an example of modulation of antigenic properties of peptide by its glycosylation. Blood 84: 2340-2345.
    • (1994) Blood , vol.84 , pp. 2340-2345
    • Jaskiewicz, E.1    Czerwinski, M.2    Syper, M.3    Lisowska, E.4
  • 100
    • 0028860624 scopus 로고
    • The gene encoding murine alpha 1,3-galactosyltransferase is expressed in female germ cells but not in male germ cells
    • Johnston, D.S., Shaper, J.H., Shaper, N.L., Joziasse, D.H., and Wright, W.W., 1995. The gene encoding murine alpha 1,3-galactosyltransferase is expressed in female germ cells but not in male germ cells. Dev. Biol. 171: 224-232.
    • (1995) Dev. Biol. , vol.171 , pp. 224-232
    • Johnston, D.S.1    Shaper, J.H.2    Shaper, N.L.3    Joziasse, D.H.4    Wright, W.W.5
  • 101
    • 0029166316 scopus 로고
    • Recombinant thyrotropin containing a beta-subunit chimera with the human chorionic gonadotropin-beta carboxy-terminus is biologically active, with a prolonged plasma half-life: Role of carbohydrate in bioactivity and metabolic clearance
    • Joshi, L., Murata, Y., Wondisford, F.E., Szkudlinski, M.W., Desai, R., and Weintraub, B.D. 1995. Recombinant thyrotropin containing a beta-subunit chimera with the human chorionic gonadotropin-beta carboxy-terminus is biologically active, with a prolonged plasma half-life: role of carbohydrate in bioactivity and metabolic clearance. Endocrinology 136: 3839-3848.
    • (1995) Endocrinology , vol.136 , pp. 3839-3848
    • Joshi, L.1    Murata, Y.2    Wondisford, F.E.3    Szkudlinski, M.W.4    Desai, R.5    Weintraub, B.D.6
  • 102
    • 0025911890 scopus 로고
    • Lysosomal alpha-N-acetylgalactosaminidase deficiency, the enzymatic defect in angiokeratoma corporis diffusum with glycopeptiduria
    • Kanzaki, T., Wang, A.M., and Desnick, R.J. 1991. Lysosomal alpha-N-acetylgalactosaminidase deficiency, the enzymatic defect in angiokeratoma corporis diffusum with glycopeptiduria. J. Clin. Invest. 88: 707-711.
    • (1991) J. Clin. Invest. , vol.88 , pp. 707-711
    • Kanzaki, T.1    Wang, A.M.2    Desnick, R.J.3
  • 103
    • 0029095821 scopus 로고
    • Glycosylation of CD44 negatively regulates its recognition of hyaluronan
    • Katoh, S., Zheng, Z., Oritani, K., Shimozato, T., and Kincade, P.W. 1995. Glycosylation of CD44 negatively regulates its recognition of hyaluronan. J. Exp. Med. 182: 419-429.
    • (1995) J. Exp. Med. , vol.182 , pp. 419-429
    • Katoh, S.1    Zheng, Z.2    Oritani, K.3    Shimozato, T.4    Kincade, P.W.5
  • 104
    • 0026030545 scopus 로고
    • Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins
    • Kearse, K.P. and Hart, G.W. 1991. Lymphocyte activation induces rapid changes in nuclear and cytoplasmic glycoproteins. Proc. Natl. Acad. Sci. U.S.A. 88: 1701-1705.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1701-1705
    • Kearse, K.P.1    Hart, G.W.2
  • 105
    • 0025083117 scopus 로고
    • Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase
    • Kentzer, E.J., Buko, A., Menon, G., and Sarin, V.K. 1990. Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase. Biochem. Biophys. Res. Commun. 171: 401-406.
    • (1990) Biochem. Biophys. Res. Commun. , vol.171 , pp. 401-406
    • Kentzer, E.J.1    Buko, A.2    Menon, G.3    Sarin, V.K.4
  • 106
    • 0028816610 scopus 로고
    • Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation
    • Kieliszewski, M.J., O'Neill, M., Leykam, J., and Orlando, R. 1995. Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation. J. Biol. Chem. 270: 2541-2549.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2541-2549
    • Kieliszewski, M.J.1    O'Neill, M.2    Leykam, J.3    Orlando, R.4
  • 107
    • 0001168093 scopus 로고
    • (Easmon, C.S.F. and Jeljaszewics, J., Eds.) Academic Press Inc., London
    • Killian, M. and Reinholdt, J. 1986. in Medical Microbiology (Easmon, C.S.F. and Jeljaszewics, J., Eds.) pp. 173-208, Academic Press Inc., London.
    • (1986) Medical Microbiology , pp. 173-208
    • Killian, M.1    Reinholdt, J.2
  • 108
    • 0028917849 scopus 로고
    • Mapping the mouse ZP3 combining site for sperm by exon swapping and site-directed mutagenesis
    • Kinloch, R.A., Sakai, Y., and Wassarman, P.M. 1995. Mapping the mouse ZP3 combining site for sperm by exon swapping and site-directed mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 92: 263-267.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 263-267
    • Kinloch, R.A.1    Sakai, Y.2    Wassarman, P.M.3
  • 109
    • 0027414938 scopus 로고
    • Role of sugar chains in the in-vitro activity of recombinant human interleukin 5
    • Kodama, S., Tsujimoto, M., Tsuruoka, N., Sugo, T., Endo, T., and Kobata, A. 1993. Role of sugar chains in the in-vitro activity of recombinant human interleukin 5. Eur. J. Biochem. 211: 903-908.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 903-908
    • Kodama, S.1    Tsujimoto, M.2    Tsuruoka, N.3    Sugo, T.4    Endo, T.5    Kobata, A.6
  • 110
    • 0028114079 scopus 로고
    • Role of cell surface O-linked oligosaccharides in adhesion of HL60 cells to fibronectin: Regulation of integrin-dependent cell adhesion by O-linked oligosaccharide elongation
    • Kojima, N., Saito, M., and Tsuji, S. 1994. Role of cell surface O-linked oligosaccharides in adhesion of HL60 cells to fibronectin: regulation of integrin-dependent cell adhesion by O-linked oligosaccharide elongation. Exp. Cell. Res. 214: 537-542.
    • (1994) Exp. Cell. Res. , vol.214 , pp. 537-542
    • Kojima, N.1    Saito, M.2    Tsuji, S.3
  • 111
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R. and Kornfeld, S. 1985. Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54: 631-664.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 112
    • 0030762901 scopus 로고    scopus 로고
    • High endothelial venules: Lymphocyte traffic control and controlled traffic
    • Kraal, G. and Mebius, R.E. 1996. High endothelial venules: lymphocyte traffic control and controlled traffic. Adv. Immunol. 65: 347-395.
    • (1996) Adv. Immunol. , vol.65 , pp. 347-395
    • Kraal, G.1    Mebius, R.E.2
  • 114
    • 0030959555 scopus 로고    scopus 로고
    • Dynamic glycosylation of nuclear and cytosolic proteins
    • Kreppel, L.K., Blomberg, M.A., and Hart, G.W. 1997. Dynamic glycosylation of nuclear and cytosolic proteins. J. Biol. Chem. 272: 9308-9315.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9308-9315
    • Kreppel, L.K.1    Blomberg, M.A.2    Hart, G.W.3
  • 115
    • 0030926584 scopus 로고    scopus 로고
    • 9-O-acetylation of sialomucins: A novel marker of murine CD4 T cells that is regulated during maturation and activation
    • Krishna, M. and Varki, A. 1997. 9-O-acetylation of sialomucins: a novel marker of murine CD4 T cells that is regulated during maturation and activation. J. Exp. Med. 185: 1997-2013.
    • (1997) J. Exp. Med. , vol.185 , pp. 1997-2013
    • Krishna, M.1    Varki, A.2
  • 116
    • 0031057323 scopus 로고    scopus 로고
    • Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA 1). The circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell derived protein 1 (SCP-1) cDNAs
    • Krogh, T. N., Bachmann, E., Teisner, B., Skjødt, K., and Højrup, P. 1997. Glycosylation analysis and protein structure determination of murine fetal antigen 1 (mFA 1). The circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell derived protein 1 (SCP-1) cDNAs. Eur. J. Biochem. 244: 334-342.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 334-342
    • Krogh, T.N.1    Bachmann, E.2    Teisner, B.3    Skjødt, K.4    Højrup, P.5
  • 117
    • 0022993925 scopus 로고
    • Identification of an O-glycosidic mannose-linked sialylated tetrasaccharide and keratan sulfate oligosaccharides in the chondroitin sulfate proteoglycan of brain
    • Krusius, T., Finne, J., Margolis, R.K., and Margolis, R.U. 1986. Identification of an O-glycosidic mannose-linked sialylated tetrasaccharide and keratan sulfate oligosaccharides in the chondroitin sulfate proteoglycan of brain. J. Biol. Chem. 261: 8237-8242.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8237-8242
    • Krusius, T.1    Finne, J.2    Margolis, R.K.3    Margolis, R.U.4
  • 118
    • 0029063952 scopus 로고
    • Identification and mutational analysis of the glycosylation sites of human keratin 18
    • Ku, N.O. and Omary, M.B. 1995. Identification and mutational analysis of the glycosylation sites of human keratin 18. J. Biol. Chem. 270: 11820-11827.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11820-11827
    • Ku, N.O.1    Omary, M.B.2
  • 119
    • 0029830192 scopus 로고    scopus 로고
    • Core 2 β-1,6-N-Acetyl-glucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin
    • Kumar, R., Camphausen, R.T., Sullivan, F.X., and Gumming, D.A. 1996. Core 2 β-1,6-N-Acetyl-glucosaminyltransferase enzyme activity is critical for P-selectin glycoprotein ligand-1 binding to P-selectin. Blood 88: 3872-3879.
    • (1996) Blood , vol.88 , pp. 3872-3879
    • Kumar, R.1    Camphausen, R.T.2    Sullivan, F.X.3    Gumming, D.A.4
  • 120
    • 0026161362 scopus 로고
    • High-level production of murine interleukin-5 (IL-5) utilizing recombinant baculovirus expression. Purification of the rIL-5 and its use in assessing the biological role of IL-5 glyco-sylation
    • Kunimoto, D. Y., Allison, K.C., Watson, C., Fuerst, T., Armstrong, G.D., Paul, W., and Strober, W. 1991. High-level production of murine interleukin-5 (IL-5) utilizing recombinant baculovirus expression. Purification of the rIL-5 and its use in assessing the biological role of IL-5 glyco-sylation. Cytokine 3: 224-230.
    • (1991) Cytokine , vol.3 , pp. 224-230
    • Kunimoto, D.Y.1    Allison, K.C.2    Watson, C.3    Fuerst, T.4    Armstrong, G.D.5    Paul, W.6    Strober, W.7
  • 121
    • 0025779352 scopus 로고
    • Tissue distribution of restricted leukocyte common antigens. A comprehensive study with proteinand carbohydrate-specific CD45R antibodies
    • Lai, R., Visser, L., and Poppema, S. 1991. Tissue distribution of restricted leukocyte common antigens. A comprehensive study with proteinand carbohydrate-specific CD45R antibodies. Lab. Invest. 64: 844-854.
    • (1991) Lab. Invest. , vol.64 , pp. 844-854
    • Lai, R.1    Visser, L.2    Poppema, S.3
  • 122
    • 0029069578 scopus 로고
    • Occurrence of multiple aberrantly spliced mRNAs of the LDL-receptor gene upon a donor splice site mutation that causes familial hypercholesterolemia (FHBenevento)
    • Lelli, N., Garuti, R., Ghisellini, M., Tiozzo, R., Rolleri, M., Aimale, V., Ginocchio, E., Naselli, A., Bertolini, S., and Calandra, S. 1995. Occurrence of multiple aberrantly spliced mRNAs of the LDL-receptor gene upon a donor splice site mutation that causes familial hypercholesterolemia (FHBenevento). J. Lipid. Res. 36: 1315-1324.
    • (1995) J. Lipid. Res. , vol.36 , pp. 1315-1324
    • Lelli, N.1    Garuti, R.2    Ghisellini, M.3    Tiozzo, R.4    Rolleri, M.5    Aimale, V.6    Ginocchio, E.7    Naselli, A.8    Bertolini, S.9    Calandra, S.10
  • 123
    • 0029865762 scopus 로고    scopus 로고
    • Visualization of P-selection glycoprotein ligand-1 as a highly extended molecule and mapping of protein epitopes for monoclonal antibodies
    • Li, F., Erickson, H.P., James, J.A., Moore, K.L., Cummings, R.D., and McEver, R.P. 1996A. Visualization of P-selection glycoprotein ligand-1 as a highly extended molecule and mapping of protein epitopes for monoclonal antibodies, J. Biol. Chem. 271: 6342-6348.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6342-6348
    • Li, F.1    Erickson, H.P.2    James, J.A.3    Moore, K.L.4    Cummings, R.D.5    McEver, R.P.6
  • 124
    • 0030041932 scopus 로고    scopus 로고
    • Post-translational modifications 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. 1996B. Post-translational modifications 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
  • 125
    • 0031029068 scopus 로고    scopus 로고
    • Germ cell-somatic cell dichotomy of a low density lipoprotein receptor gene family member in testis
    • Lindstedt, K.A., Bujo, H., Mahon, M.G., Nimpf, J., and Schneider, W.J. 1997. Germ cell-somatic cell dichotomy of a low density lipoprotein receptor gene family member in testis. DNA Cell. Biol. 16: 35-43.
    • (1997) DNA Cell. Biol. , vol.16 , pp. 35-43
    • Lindstedt, K.A.1    Bujo, H.2    Mahon, M.G.3    Nimpf, J.4    Schneider, W.J.5
  • 126
    • 0028902581 scopus 로고
    • Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro
    • Litscher, E.S., Juntunen, K., Seppo, A., Penttila, L., Niemela, R., Renkonen, O., and Wassarman, P.M. 1995. Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry 34: 4662-4669.
    • (1995) Biochemistry , vol.34 , pp. 4662-4669
    • Litscher, E.S.1    Juntunen, K.2    Seppo, A.3    Penttila, L.4    Niemela, R.5    Renkonen, O.6    Wassarman, P.M.7
  • 127
    • 0030466993 scopus 로고    scopus 로고
    • Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells
    • Lloyd, K. O., Burchell, J., Kudryashov, V., Yin, B.W.T., and Taylor-Papadimitriou, J. 1996. Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells. J. Biol. Chem. 271: 33325-33334.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33325-33334
    • Lloyd, K.O.1    Burchell, J.2    Kudryashov, V.3    Yin, B.W.T.4    Taylor-Papadimitriou, J.5
  • 128
    • 0028074734 scopus 로고
    • Specificity of the IgG response in mice and human breast cancer patients following immunization against synthetic sialyl-Tn, an epitope with possible functional significance in metastasis
    • Longenecker, B.M., Reddish, M., Koganty, R., and MacLean, G.D. 1994. Specificity of the IgG response in mice and human breast cancer patients following immunization against synthetic sialyl-Tn, an epitope with possible functional significance in metastasis. Adv. Exp. Med. Biol. 353: 105-124.
    • (1994) Adv. Exp. Med. Biol. , vol.353 , pp. 105-124
    • Longenecker, B.M.1    Reddish, M.2    Koganty, R.3    MacLean, G.D.4
  • 129
    • 0030944105 scopus 로고    scopus 로고
    • O-linked GlcNAc-transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats
    • Lubas, W.A., Frank, D.W., Krause, M., and Hanover, J. 1997. O-linked GlcNAc-transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272: 9316-9324.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9316-9324
    • Lubas, W.A.1    Frank, D.W.2    Krause, M.3    Hanover, J.4
  • 133
    • 0027211820 scopus 로고
    • Nervous tissue proteoglycans
    • Margolis, R.K., and Margolis, R.U. 1993. Nervous tissue proteoglycans. Experientia 49: 429-446.
    • (1993) Experientia , vol.49 , pp. 429-446
    • Margolis, R.K.1    Margolis, R.U.2
  • 134
    • 0027426024 scopus 로고
    • Mouse gelatinase B: cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation
    • Masure, S., Nys, G., Fiten, P., Van Damme, J., and Opdenakker, G. 1993. Mouse gelatinase B: cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation. Eur. J. Biochem. 218: 129-141.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 129-141
    • Masure, S.1    Nys, G.2    Fiten, P.3    Van Damme, J.4    Opdenakker, G.5
  • 135
    • 0031915973 scopus 로고    scopus 로고
    • The glyco-sylation and structure of human serum IgA1, Fab, and Fac regions and the role of N-glyco-sylation on Fcα receptor interactions
    • Mattu, T.S., Pleass, R.J., Willis, A.C., Kilian, M., Wormald, M.R., Lellouch, A.C., Rudd, P.M., Woof, J.M., and Dwek, R.A. 1998. The glyco-sylation and structure of human serum IgA1, Fab, and Fac regions and the role of N-glyco-sylation on Fcα receptor interactions. J. Biol. Chem. 273: 2260-2272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2260-2272
    • Mattu, T.S.1    Pleass, R.J.2    Willis, A.C.3    Kilian, M.4    Wormald, M.R.5    Lellouch, A.C.6    Rudd, P.M.7    Woof, J.M.8    Dwek, R.A.9
  • 139
    • 0029799513 scopus 로고    scopus 로고
    • Detection of UDP-D-xylose: α-D-xyloside α1-3xylosyltransferase activity in human hepatoma cell line HepG2
    • Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S., and Hase, S. 1996. Detection of UDP-D-xylose: α-D-xyloside α1-3xylosyltransferase activity in human hepatoma cell line HepG2. J. Biochem. 120: 1002-1006.
    • (1996) J. Biochem. , vol.120 , pp. 1002-1006
    • Minamida, S.1    Aoki, K.2    Natsuka, S.3    Omichi, K.4    Fukase, K.5    Kusumoto, S.6    Hase, S.7
  • 140
    • 0027992114 scopus 로고
    • The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine
    • Moore, K.L., Eaton, S.F., Lyons, D.E., Lichenstein, H.S., Cummings, R.D., and McEver, R.P. 1994. The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine, J. Biol. Chem. 269: 23318-23327.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23318-23327
    • Moore, K.L.1    Eaton, S.F.2    Lyons, D.E.3    Lichenstein, H.S.4    Cummings, R.D.5    McEver, R.P.6
  • 141
    • 0028832978 scopus 로고
    • The activation of type 1 and type 2 plasminogen by type 1 and type 2 tissue plasminogen activator
    • Mori, K., Dwek, R.A., Downing, A.K., Opdenakker, G., and Rudd, P.M. 1995. The activation of type 1 and type 2 plasminogen by type 1 and type 2 tissue plasminogen activator. J. Biol. Chem. 270: 3261-3267.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3261-3267
    • Mori, K.1    Dwek, R.A.2    Downing, A.K.3    Opdenakker, G.4    Rudd, P.M.5
  • 142
    • 0029070422 scopus 로고
    • Expression of tumor-associated polymorphic epithelial mucin and carcinoembryonic antigen in gastrointestinal carcinoid tumors. Implications for immunodiagnosis and immunotherapy
    • Moyana, T.N. and Xiang, J. 1995. Expression of tumor-associated polymorphic epithelial mucin and carcinoembryonic antigen in gastrointestinal carcinoid tumors. Implications for immunodiagnosis and immunotherapy. Cancer 75: 2836-2843.
    • (1995) Cancer , vol.75 , pp. 2836-2843
    • Moyana, T.N.1    Xiang, J.2
  • 143
    • 0027171780 scopus 로고
    • Protective effects of oligosaccharides in P-selectin-dependent lung injury
    • Mulligan, M.S., Paulson, J.C., De Frees, S., Zheng, Z.-L., Lowe, J.B., and Ward, P.A. 1993. Protective effects of oligosaccharides in P-selectin-dependent lung injury. Nature 364: 149-151.
    • (1993) Nature , vol.364 , pp. 149-151
    • Mulligan, M.S.1    Paulson, J.C.2    De Frees, S.3    Zheng, Z.-L.4    Lowe, J.B.5    Ward, P.A.6
  • 144
    • 0028182854 scopus 로고
    • Bacterial immunoglobulin A1 proteases
    • Mulks, M.H. and Shoberg, R.J. 1994. Bacterial immunoglobulin A1 proteases. Methods Enzymol. 235: 543-554.
    • (1994) Methods Enzymol. , vol.235 , pp. 543-554
    • Mulks, M.H.1    Shoberg, R.J.2
  • 145
    • 0026491215 scopus 로고
    • Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition
    • Naim, H.Y. and Lentze, M.J. 1992. Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterization of glycoforms varying in enzyme activity and localization of O-glycoside addition. J. Biol. Chem. 267: 25494-25504.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25494-25504
    • Naim, H.Y.1    Lentze, M.J.2
  • 146
    • 0028817807 scopus 로고
    • The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22
    • Nath, D., van der Merwe, P.A., Kelm, S., Bradfield, P., and Crocker, P.R. 1995. The amino-terminal immunoglobulin-like domain of sialoadhesin contains the sialic acid binding site. Comparison with CD22. J. Biol. Chem. 270: 26184-26191.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26184-26191
    • Nath, D.1    Van Der Merwe, P.A.2    Kelm, S.3    Bradfield, P.4    Crocker, P.R.5
  • 147
    • 0028982008 scopus 로고
    • Enzymic remodelling of the N- and O-linked carbohydrate chains of human chorionic gonadotropin. Effects on biological activity and receptor binding
    • Nemansky, M., de Leeuw, R., Wijnands, R.A., and Van den Eijnden, D.H. 1995. Enzymic remodelling 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    De Leeuw, R.2    Wijnands, R.A.3    Van Den Eijnden, D.H.4
  • 149
    • 0027771655 scopus 로고
    • Characterization of the invariant chain C-terminus (Glu183-Glu193) epitope which is obscured in processed Ii, MHC alpha,beta trimers
    • Nguyen, Q.V., Knapp, W., and Humphreys, R.E. 1993. Characterization of the invariant chain C-terminus (Glu183-Glu193) epitope which is obscured in processed Ii, MHC alpha,beta trimers. Mol. Immunol. 30: 1679-1684.
    • (1993) Mol. Immunol. , vol.30 , pp. 1679-1684
    • Nguyen, Q.V.1    Knapp, W.2    Humphreys, R.E.3
  • 151
    • 0026606075 scopus 로고
    • Evidence for the existence of O-linked sugar chains consisting of glucose and xylose in bovine thrombospondin
    • Nishimura, H., Yamashita, S., Zeng, Z., Walz, D.A., and Iwanaga, S. 1992A. Evidence for the existence of O-linked sugar chains consisting of glucose and xylose in bovine thrombospondin. J. Biochem. (Tokyo) 111: 460-464.
    • (1992) J. Biochem. (Tokyo) , vol.111 , pp. 460-464
    • Nishimura, H.1    Yamashita, S.2    Zeng, Z.3    Walz, D.A.4    Iwanaga, S.5
  • 152
    • 0026701391 scopus 로고
    • Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue
    • Nishimura, H., Takao, T., Hase, S., Shimonishi, Y., and Iwanaga, S. 1992B. Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. J. Biol. Chem. 267: 17520-17525.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17520-17525
    • Nishimura, H.1    Takao, T.2    Hase, S.3    Shimonishi, Y.4    Iwanaga, S.5
  • 153
    • 0028863499 scopus 로고
    • Identification and characterization of a gene regulating enzymatic glycosylation which is induced by diabetes and hyperglycemia specifically in rat cardiac tissue
    • Nishio, Y., Warren, C.E., Buczek-Thomas, J.A., Rulfs, J., Koya, D., Aiello, L.P., Feener, E.P., Miller, T.B., Jr., Dennis, J.W., and King, G.L. 1995. Identification and characterization of a gene regulating enzymatic glycosylation which is induced by diabetes and hyperglycemia specifically in rat cardiac tissue. J. Clin. Invest. 96: 1759-1767.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1759-1767
    • Nishio, Y.1    Warren, C.E.2    Buczek-Thomas, J.A.3    Rulfs, J.4    Koya, D.5    Aiello, L.P.6    Feener, E.P.7    Miller Jr., T.B.8    Dennis, J.W.9    King, G.L.10
  • 154
    • 0028289809 scopus 로고
    • In vitro comparison of the biological potency of glycosylated versus nonglycosylated rG-CSF
    • Nissen, C., Dalle Carbonare, V., and Moser, Y. 1994. In vitro comparison of the biological potency of glycosylated versus nonglycosylated rG-CSF. Drug Invest. 7: 346-352.
    • (1994) Drug Invest. , vol.7 , pp. 346-352
    • Nissen, C.1    Dalle Carbonare, V.2    Moser, Y.3
  • 155
    • 0025736040 scopus 로고
    • Investigation of the structural requirements for peptide precursor processing in AtT-20 cells using site-directed mutagenesis of proadrenocorticotropin/endorphin
    • Noel, G., Keutmann, H.T., and Mains, R.E. 1991. Investigation of the structural requirements for peptide precursor processing in AtT-20 cells using site-directed mutagenesis of proadrenocorticotropin/endorphin. Mol. Endocrinol. 5: 404-413.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 404-413
    • Noel, G.1    Keutmann, H.T.2    Mains, R.E.3
  • 156
    • 0025284968 scopus 로고
    • O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity
    • Oh'eda, M., Hasegawa, M., Hattori, K., Kuboniwa, H., Kojima, T., Orita, T., Tomonou, K., Yamazaki, T., and Ochi, N. 1990. O-linked sugar chain of human granulocyte colony-stimulating factor protects it against polymerization and denaturation allowing it to retain its biological activity. J. Biol. Chem. 265: 11432-11435.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11432-11435
    • Oh'eda, M.1    Hasegawa, M.2    Hattori, K.3    Kuboniwa, H.4    Kojima, T.5    Orita, T.6    Tomonou, K.7    Yamazaki, T.8    Ochi, N.9
  • 159
  • 161
    • 0029012040 scopus 로고
    • Comparison of the effects of amino acid substitutions and beta-N- vs. alpha-O-glycosylation on the T-cell stimulatory activity and conformation of an epitope on the rabies virus glycoprotein
    • Otvos, L. Jr., Krivulka, G.R., Urge, L., Szendrei, G.I., Nagy, L., Xiang, Z.Q., and Ertl, H.C. 1995. Comparison of the effects of amino acid substitutions and beta-N- vs. alpha-O-glycosylation on the T-cell stimulatory activity and conformation of an epitope on the rabies virus glycoprotein. Biochim. Biophys. Acta 1267: 55-64.
    • (1995) Biochim. Biophys. Acta , vol.1267 , pp. 55-64
    • Otvos Jr., L.1    Krivulka, G.R.2    Urge, L.3    Szendrei, G.I.4    Nagy, L.5    Xiang, Z.Q.6    Ertl, H.C.7
  • 163
    • 0027441378 scopus 로고
    • Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins
    • Patel, T., Bruce, J., Merry, A., Bigge, C., Wormald, M., Jaques, A., and Parekh, R. 1993. Use of hydrazine to release in intact and unreduced form both N- and O-linked oligosaccharides from glycoproteins. Biochemistry 32: 679-693.
    • (1993) Biochemistry , vol.32 , pp. 679-693
    • Patel, T.1    Bruce, J.2    Merry, A.3    Bigge, C.4    Wormald, M.5    Jaques, A.6    Parekh, R.7
  • 164
    • 0026340756 scopus 로고
    • Presence of terminal N-acetylgalactosamine residues in subrogions of the endoplasmic reticulum is influenced by cell differentiation in culture
    • Perez-Vilar, J., Hidalgo, J., and Velasco, A. 1991. Presence of terminal N-acetylgalactosamine residues in subrogions of the endoplasmic reticulum is influenced by cell differentiation in culture. J. Biol. Chem. 266: 23967-23976.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23967-23976
    • Perez-Vilar, J.1    Hidalgo, J.2    Velasco, A.3
  • 165
    • 0030098246 scopus 로고    scopus 로고
    • Stabilization of the T1 fragment of glycophorin A(N) through interactions with N-and O-linked glycans
    • Pieper, J., Ott, K.H., and Meyer, B. 1996. Stabilization of the T1 fragment of glycophorin A(N) through interactions with N-and O-linked glycans. Nat. Struct. Biol. 3: 228-232.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 228-232
    • Pieper, J.1    Ott, K.H.2    Meyer, B.3
  • 166
    • 0020656366 scopus 로고
    • The IgA1 proteases of pathogenic bacteria
    • Plaut, A.G. 1983. The IgA1 proteases of pathogenic bacteria. Annu. Rev. Microbiol. 37: 603-622.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 603-622
    • Plaut, A.G.1
  • 167
    • 0025736633 scopus 로고
    • Membrane cofactor protein of the complement system: Alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlates with protein phenotype
    • Post, T.W., Lyszewsky, M.K., Adams, E.M., Tedja, I., Miller, E.A., and Atkinson, J.P. 1991. Membrane cofactor protein of the complement system: alternative splicing of serine/threonine/proline-rich exons and cytoplasmic tails produces multiple isoforms that correlates with protein phenotype. J. Exp. Med. 174: 93-102.
    • (1991) J. Exp. Med. , vol.174 , pp. 93-102
    • Post, T.W.1    Lyszewsky, M.K.2    Adams, E.M.3    Tedja, I.4    Miller, E.A.5    Atkinson, J.P.6
  • 168
    • 0028206055 scopus 로고
    • The oligosaccharide binding specificities of CD22 beta, a sialic acid-specific lectin of B cells
    • Powell, L.D. and Varki, A. 1994. The oligosaccharide binding specificities of CD22 beta, 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
  • 169
    • 0028962757 scopus 로고
    • Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22. Evidence for a minimal structural recognition motif and the potential importance of multisite binding
    • Powell, L.D., Jain, R.K., Matta, K.L., Sabesan, S., and Varki, A. 1995. Characterization of sialyloligosaccharide binding by recombinant soluble and native cell-associated CD22. Evidence for a minimal structural recognition motif and the potential importance of multisite binding. J. Biol. Chem. 270: 7523-7535.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7523-7535
    • Powell, L.D.1    Jain, R.K.2    Matta, K.L.3    Sabesan, S.4    Varki, A.5
  • 171
    • 0028177865 scopus 로고
    • Simple mucins (T, sialosyl-T, Tn and sialosyl-Tn) are not diagnostic for malignant breast lesions
    • Reed, W., Bryne, M., Clausen, H., Dabelsteen, E., and Nesland, J.M. 1994. Simple mucins (T, sialosyl-T, Tn and sialosyl-Tn) are not diagnostic for malignant breast lesions. Anticancer Res. 14: 609-616.
    • (1994) Anticancer Res. , vol.14 , pp. 609-616
    • Reed, W.1    Bryne, M.2    Clausen, H.3    Dabelsteen, E.4    Nesland, J.M.5
  • 172
    • 0026333518 scopus 로고
    • Expression of human glycophorin A in wild type and glycosylation-deficient Chinese hamster ovary cells. Role of N-and O-linked glycosylation in cell surface expression
    • Remaley, A.T., Ugorski, M., Wu, N., Litzky, L., Burger, S.R., Moore, J.S., Fukuda, M., and Spitalnik, S.L. 1991. Expression of human glycophorin A in wild type and glycosylation-deficient Chinese hamster ovary cells. Role of N-and O-linked glycosylation in cell surface expression J. Biol. Chem. 266: 24176-24183.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24176-24183
    • Remaley, A.T.1    Ugorski, M.2    Wu, N.3    Litzky, L.4    Burger, S.R.5    Moore, J.S.6    Fukuda, M.7    Spitalnik, S.L.8
  • 173
    • 0025807832 scopus 로고
    • Characterisation of human IFN-γ and human interleukin-2 from recombinant mammalian cell lines and peripheral blood lymphocytes
    • Riske, F.J., Cullen, B.R., and Chizzonite, R. 1991. Characterisation of human IFN-γ and human interleukin-2 from recombinant mammalian cell lines and peripheral blood lymphocytes. Lymphokine Cytokine Res. 10: 213-218.
    • (1991) Lymphokine Cytokine Res. , vol.10 , pp. 213-218
    • Riske, F.J.1    Cullen, B.R.2    Chizzonite, R.3
  • 175
    • 0021356148 scopus 로고
    • Effects of deglycosylation on the architecture of ovine submaxillary mucin glycoprotein
    • Rose, M.C., Voter, W.A., Sage, H., Brown, C.F., and Kaufman, B. 1984. Effects of deglycosylation on the architecture of ovine submaxillary mucin glycoprotein. J. Biol. Chem. 259: 3167-3172.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3167-3172
    • Rose, M.C.1    Voter, W.A.2    Sage, H.3    Brown, C.F.4    Kaufman, B.5
  • 176
    • 0023024461 scopus 로고
    • Diffferential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells
    • Roth, J., Taatjes, D.J., Weinstein, J., Paulson, J.C., Greenwell, P., Watkins, W.M. 1986. Diffferential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells. J. Biol. Chem. 261: 14307-14312.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14307-14312
    • Roth, J.1    Taatjes, D.J.2    Weinstein, J.3    Paulson, J.C.4    Greenwell, P.5    Watkins, W.M.6
  • 177
    • 0028587240 scopus 로고
    • Subcellular localization of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetyl-galactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland
    • Roth, J., Wang, Y., Eckhardt, A.E., and Hill, R.L. 1994. Subcellular localization of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetyl-galactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland. Proc. Natl. Acad. Sci. U.S.A. 91: 8935-8939.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8935-8939
    • Roth, J.1    Wang, Y.2    Eckhardt, A.E.3    Hill, R.L.4
  • 178
    • 0000810848 scopus 로고
    • Biosynthesis. 4c. Compartmentation of glycoprotein biosynthesis
    • Montreuil, J., Schachter, H., and Vliegenthart, J.F.G., Eds., Elsevier
    • Roth, J. 1995. Biosynthesis. 4c. Compartmentation of glycoprotein biosynthesis. In: Glycoproteins, Montreuil, J., Schachter, H., and Vliegenthart, J.F.G., Eds., Elsevier.
    • (1995) Glycoproteins
    • Roth, J.1
  • 180
    • 0028129261 scopus 로고
    • Human T-cell receptor recognizes 'O'-linked sugars from the hinge region of human IgA1 and IgD
    • Rudd, P.M., Fortune, F., Patel, T., Parekh, R.B., Dwek, R.A., and Lehner, T. 1994B. Human T-cell receptor recognizes 'O'-linked sugars from the hinge region of human IgA1 and IgD. Immunology 83: 99-106.
    • (1994) Immunology , vol.83 , pp. 99-106
    • Rudd, P.M.1    Fortune, F.2    Patel, T.3    Parekh, R.B.4    Dwek, R.A.5    Lehner, T.6
  • 181
    • 0028921674 scopus 로고
    • The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator
    • Rudd, P. M., Woods, R. J., Wormald, M. R., Opdenakker, G., Downing, A.K., Campbell, I. D., and Dwek, R. A. 1995A. The effects of variable glycosylation on the functional activities of ribonuclease, plasminogen and tissue plasminogen activator. Biochim. Biophys. Acta 1248: 1-10.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 1-10
    • Rudd, P.M.1    Woods, R.J.2    Wormald, M.R.3    Opdenakker, G.4    Downing, A.K.5    Campbell, I.D.6    Dwek, R.A.7
  • 182
    • 0028867358 scopus 로고
    • Lectin-carbohydrate interactions in disease. T-cell recognition of IgA and IgD; mannose binding protein recognition of IgGO
    • Rudd, P. M., Fortune, F., Lehner, T., Parekh, R., Patel, T., Wormald, M., Malhotra, R., Sim, R., and Dwek, R. 1995B. Lectin-carbohydrate interactions in disease. T-cell recognition of IgA and IgD; mannose binding protein recognition of IgGO. Adv. Exp. Med. Biol. 376: 147-152.
    • (1995) Adv. Exp. Med. Biol. , vol.376 , pp. 147-152
    • Rudd, P.M.1    Fortune, F.2    Lehner, T.3    Parekh, R.4    Patel, T.5    Wormald, M.6    Malhotra, R.7    Sim, R.8    Dwek, R.9
  • 183
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and the 3D structure of proteins
    • Rudd., P.M. and Dwek, R.A. 1997. Glycosylation: heterogeneity and the 3D structure of proteins. Crit. Rev. Biochem. Mol. Biol. 32: 1-100.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 185
    • 0027976177 scopus 로고
    • Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor
    • Rutledge, E.A., Root, B.J., Lucas, J.J., and Enns, C.A. 1994A. Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor. Blood 83: 580-586.
    • (1994) Blood , vol.83 , pp. 580-586
    • Rutledge, E.A.1    Root, B.J.2    Lucas, J.J.3    Enns, C.A.4
  • 186
    • 0027970890 scopus 로고
    • Generation of the soluble transferrin receptor requires cycling through an endosomal compartment
    • Rutledge, E.A., Green, F.A., and Enns, C.A. 1994B. Generation of the soluble transferrin receptor requires cycling through an endosomal compartment. J. Biol. Chem. 269: 31864-31868.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31864-31868
    • Rutledge, E.A.1    Green, F.A.2    Enns, C.A.3
  • 187
    • 0029780466 scopus 로고    scopus 로고
    • Cleavage of the transferrin receptor is influenced by the composition of the O-linked carbohydrate chain at position 104
    • Rutledge, E.A. and Enns, C.A. 1996. Cleavage of the transferrin receptor is influenced by the composition of the O-linked carbohydrate chain at position 104. J. Cell. Physiol. 168: 284-293.
    • (1996) J. Cell. Physiol. , vol.168 , pp. 284-293
    • Rutledge, E.A.1    Enns, C.A.2
  • 188
    • 0028953466 scopus 로고
    • Enhancement in accessibility to macrophages by modification of mucin-type carbohydrate chains on a tumor cell line: Role of a C-type lectin of macrophages
    • Sakamaki, T., Imai, Y., and Irimura, T. 1995. Enhancement in accessibility to macrophages by modification of mucin-type carbohydrate chains on a tumor cell line: role of a C-type lectin of macrophages. J. Leukoc. Biol. 57: 407-414.
    • (1995) J. Leukoc. Biol. , vol.57 , pp. 407-414
    • Sakamaki, T.1    Imai, Y.2    Irimura, T.3
  • 189
    • 0026022265 scopus 로고
    • UDP-GlcNAc:Galβ3GalNAc-mucin: (GlcNAc to GalNAc) β6-N-Acetylglucosaminyltransferase and UDP-GlcNAc: Galβ3(GlcNAcβ6)Gal NAc-mucin: (GlcNAc to GalNAc) β6-N-Acetylglucosaminyltransferase from swine trachea epithelium
    • Sangadala, S., Sivakami, S., and Mendicino, J. 1991. UDP-GlcNAc:Galβ3GalNAc-mucin: (GlcNAc to GalNAc) β6-N-Acetylglucosaminyltransferase and UDP-GlcNAc: Galβ3(GlcNAcβ6)Gal NAc-mucin: (GlcNAc to GalNAc) β6-N-Acetylglucosaminyltransferase from swine trachea epithelium. Mol Cell. Biochem. 101: 125-143.
    • (1991) Mol Cell. Biochem. , vol.101 , pp. 125-143
    • Sangadala, S.1    Sivakami, S.2    Mendicino, J.3
  • 190
    • 0028931740 scopus 로고
    • Biochemical characterization of a bovine oviduct-specific sialo-glycoprotein that sustains sperm viability in vitro
    • Satoh, T., Abe, H., Sendai, Y., Iwata, H., and Hoshi, H. 1995. Biochemical characterization of a bovine oviduct-specific sialo-glycoprotein that sustains sperm viability in vitro. Biochim, Biophys. Acta. 1266: 117-123.
    • (1995) Biochim, Biophys. Acta , vol.1266 , pp. 117-123
    • Satoh, T.1    Abe, H.2    Sendai, Y.3    Iwata, H.4    Hoshi, H.5
  • 193
    • 0028947585 scopus 로고
    • b subsets to serve as TCR-ligands for allo-specific CTL-clones: Potential role for N-linked glycosylation
    • b subsets to serve as TCR-ligands for allo-specific CTL-clones: potential role for N-linked glycosylation. J. Exp. Med. 181: 1773-1783.
    • (1995) J. Exp. Med. , vol.181 , pp. 1773-1783
    • Shen, L.1    Kane, K.P.2
  • 194
  • 195
    • 0029856391 scopus 로고    scopus 로고
    • Regulation of sialic acid 9-O-acetylation during the growth and differentiation of murine erythroleukemia cells
    • Shi, W.-X., Chammas, R., and Varki, A. 1996A. Regulation of sialic acid 9-O-acetylation during the growth and differentiation of murine erythroleukemia cells. J. Biol. Chem. 271: 31517-31525.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31517-31525
    • Shi, W.-X.1    Chammas, R.2    Varki, A.3
  • 196
    • 0029950416 scopus 로고    scopus 로고
    • Sialic acid 9-O-acetylation on murine erythroleukemia cells affects complement activation, binding to I-type lectins, and tissue homing
    • Shi, W.-X., Chammas, R., Varki, N.M., Powell, L., and Varki, A. 1996B. Sialic acid 9-O-acetylation on murine erythroleukemia cells affects complement activation, binding to I-type lectins, and tissue homing. J. Biol. Chem. 271: 31526-31532.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31526-31532
    • Shi, W.-X.1    Chammas, R.2    Varki, N.M.3    Powell, L.4    Varki, A.5
  • 197
    • 0027996391 scopus 로고
    • Cytokeratin peptide SFGSGFGGGY mimics N-acetyl-beta-D-glucosamine in reaction with antibodies and lectins, and induces in vivo anti-carbohydrate antibody response
    • Shikhman, A.R., Greenspan, N.S., and Cunningham, M.W. 1994. Cytokeratin peptide SFGSGFGGGY mimics N-acetyl-beta-D-glucosamine in reaction with antibodies and lectins, and induces in vivo anti-carbohydrate antibody response. J. Immunol. 153: 5593-5606.
    • (1994) J. Immunol. , vol.153 , pp. 5593-5606
    • Shikhman, A.R.1    Greenspan, N.S.2    Cunningham, M.W.3
  • 198
    • 0028181891 scopus 로고
    • Immunological mimicry between N-acetyl-beta-D-glucosamine and cytokeratin peptides. Evidence for a microbially driven anti-keratin antibody response
    • Shikhman, A.R. and Cunningham, M.W. 1994. Immunological mimicry between N-acetyl-beta-D-glucosamine and cytokeratin peptides. Evidence for a microbially driven anti-keratin antibody response. J. Immunol. 152: 4375-4387.
    • (1994) J. Immunol. , vol.152 , pp. 4375-4387
    • Shikhman, A.R.1    Cunningham, M.W.2
  • 199
    • 0027754171 scopus 로고
    • Mucins in the mainstream
    • Shimizu, Y. and Shaw, S. 1993. Mucins in the mainstream. Nature 366: 630-631.
    • (1993) Nature , vol.366 , pp. 630-631
    • Shimizu, Y.1    Shaw, S.2
  • 200
    • 0022759530 scopus 로고
    • Conformation of mucous glycoproteins in aqueous solvents
    • Shogren, R.L., Jamieson, A.M., Blackwell, J., and Jentoft, N. 1986. Conformation of mucous glycoproteins in aqueous solvents. Biopol. 25: 1505-1517.
    • (1986) Biopol. , vol.25 , pp. 1505-1517
    • Shogren, R.L.1    Jamieson, A.M.2    Blackwell, J.3    Jentoft, N.4
  • 201
    • 0024389522 scopus 로고
    • Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: Light-scattering studies of ovine submaxillary mucin
    • Shogren, R., Gerken, T.A., and Jentoft, N. 1989. Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins: light-scattering studies of ovine submaxillary mucin. Biochemistry 28: 5525-5536.
    • (1989) Biochemistry , vol.28 , pp. 5525-5536
    • Shogren, R.1    Gerken, T.A.2    Jentoft, N.3
  • 202
    • 0027537465 scopus 로고
    • Carbohydrate residues modulate the activation of coagulation factor X
    • Sinha, U. and Wolf, D.L. 1993. Carbohydrate residues modulate the activation of coagulation factor X. J. Biol. Chem. 268: 3048-3051.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3048-3051
    • Sinha, U.1    Wolf, D.L.2
  • 203
    • 0028972060 scopus 로고
    • UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, identification and separation of two distinct transferase activities
    • Sørensen, T., White, T., Wandall, H.H., Kristensen, A.K., Roepstorff, P, and Henrik, C. 1995. UDP-N-acetyl-α-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, identification and separation of two distinct transferase activities. J. Biol. Chem. 270: 24166-24173.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24166-24173
    • Sørensen, T.1    White, T.2    Wandall, H.H.3    Kristensen, A.K.4    Roepstorff, P.5    Henrik, C.6
  • 204
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T.A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 76: 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 206
    • 0025973305 scopus 로고
    • Protein O-glycosylation in Saccharomyces cerevisiae, purification and characterization of the dolichyl-phosphate-D-mannose-protein O-D-mannosyltransferase
    • Strahl-Bolsinger, S., and Tanner, W. 1991. Protein O-glycosylation in Saccharomyces cerevisiae, purification and characterization of the dolichyl-phosphate-D-mannose-protein O-D-mannosyltransferase. J. Biochem. 196: 185-190.
    • (1991) J. Biochem. , vol.196 , pp. 185-190
    • Strahl-Bolsinger, S.1    Tanner, W.2
  • 210
    • 0028012360 scopus 로고
    • Aberrant regulation of complement by the erythrocytes of hereditary erythroblastic multinuclearity with a positive acidified serum lysis test (HEMPAS)
    • Tomita, A. and Parker, C.J. 1994. Aberrant regulation of complement by the erythrocytes of hereditary erythroblastic multinuclearity with a positive acidified serum lysis test (HEMPAS). Blood 83: 250-259.
    • (1994) Blood , vol.83 , pp. 250-259
    • Tomita, A.1    Parker, C.J.2
  • 211
    • 0030778823 scopus 로고    scopus 로고
    • Branched O-linked oligosaccharides ectopically expressed in transgenic mice reduce primary T-cell immune responses
    • Tsuboi, S. and Fukuda, M. 1997. Branched O-linked oligosaccharides ectopically expressed in transgenic mice reduce primary T-cell immune responses. EMBO J. 16: 6364-6373.
    • (1997) EMBO J. , vol.16 , pp. 6364-6373
    • Tsuboi, S.1    Fukuda, M.2
  • 212
    • 0028891332 scopus 로고
    • Purification and characterization of two forms of beta-o-galactosidase from rat epididymal luminal fluid: Evidence for their role in the modification of sperm plasma membrane glycoprotein(s)
    • Tulsiani, D.R., Skudlarek, M.D., Araki, Y., and Orgebin-Crist, M.C. 1995. Purification and characterization of two forms of beta-o-galactosidase from rat epididymal luminal fluid: evidence for their role in the modification of sperm plasma membrane glycoprotein(s). Biochem. J. 305: 41-50.
    • (1995) Biochem. J. , vol.305 , pp. 41-50
    • Tulsiani, D.R.1    Skudlarek, M.D.2    Araki, Y.3    Orgebin-Crist, M.C.4
  • 214
    • 0027290454 scopus 로고
    • Recombinant Miltenberger I and II human blood group antigens: The role of glycosylation in cell surface expression and antigenicity of glycophorin A
    • Ugorski, M., Blackall, D.P., Pahlsson, P., Shakin-Eshleman, S.H., Moore, J., and Spitalnik, S.L. 1993. Recombinant Miltenberger I and II human blood group antigens: the role of glycosylation in cell surface expression and antigenicity of glycophorin A. Blood 82: 1913-1920.
    • (1993) Blood , vol.82 , pp. 1913-1920
    • Ugorski, M.1    Blackall, D.P.2    Pahlsson, P.3    Shakin-Eshleman, S.H.4    Moore, J.5    Spitalnik, S.L.6
  • 215
    • 0026721539 scopus 로고
    • Structural and functional identification of two human, tumor-derived monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the chemokine family
    • Van Damme, J., Proost, P., Lenaerts, J.-P., and Opdenakker, G. 1992. Structural and functional identification of two human, tumor-derived monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the chemokine family. J. Exp. Med. 176: 59-65.
    • (1992) J. Exp. Med. , vol.176 , pp. 59-65
    • Van Damme, J.1    Proost, P.2    Lenaerts, J.-P.3    Opdenakker, G.4
  • 216
    • 0029140842 scopus 로고
    • Topology of the CD2-CD48 cell-adhesion molecule complex: Implications for antigen recognition by T cells
    • van der Merwe, P.A., McNamee, P.N., Davies, E.A., Barclay, A.N., and Davis, S.J. 1995. Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells. Curr. Biol. 5: 74-84.
    • (1995) Curr. Biol. , vol.5 , pp. 74-84
    • Van Der Merwe, P.A.1    McNamee, P.N.2    Davies, E.A.3    Barclay, A.N.4    Davis, S.J.5
  • 217
    • 0029585865 scopus 로고
    • Phospho-mannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I
    • Van Schaftingen, E., and Jaeken, J. 1995. Phospho-mannomutase deficiency is a cause of carbohydrate-deficient glycoprotein syndrome type I. FEBS Lett. 377: 318-320.
    • (1995) FEBS Lett. , vol.377 , pp. 318-320
    • Van Schaftingen, E.1    Jaeken, J.2
  • 218
    • 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
  • 220
    • 0030472840 scopus 로고    scopus 로고
    • Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF-domains
    • Wang, Y., Lee, G. F., Kelley, R. F., and Spellman, M. W. 1996. Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF-domains. Glycobiology 6: 837-842.
    • (1996) Glycobiology , vol.6 , pp. 837-842
    • Wang, Y.1    Lee, G.F.2    Kelley, R.F.3    Spellman, M.W.4
  • 221
    • 0028803582 scopus 로고
    • Purification and cDNA cloning of a human UDP-N-acetyl-α-C-galactosamine:polypeptide N-acetylgalactosaminyltransferase
    • White, T., Bennett, E.P., Takio, K., Sørensen, T., Bonding, N., and Clausen, H. 1995. Purification and cDNA cloning of a human UDP-N-acetyl-α-C-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem. 270: 24156-24165.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24156-24165
    • White, T.1    Bennett, E.P.2    Takio, K.3    Sørensen, T.4    Bonding, N.5    Clausen, H.6
  • 222
    • 0027494242 scopus 로고
    • Rotaviruses preferentially bind O-linked sialylglycoconjugates and sialomucins
    • Willoughby, R.E. 1993. Rotaviruses preferentially bind O-linked sialylglycoconjugates and sialomucins. Glycobiology 3: 437-445.
    • (1993) Glycobiology , vol.3 , pp. 437-445
    • Willoughby, R.E.1
  • 223
    • 0027641048 scopus 로고
    • The systematic use of negative nuclear Overhauser constraints in the determination of oligosaccharide conformations: Application to sialyl Lewis X
    • Wormald, M.R. and Edge, C.J. 1993. The systematic use of negative nuclear Overhauser constraints in the determination of oligosaccharide conformations: application to sialyl Lewis X. Carbohyd. Res. 246: 337-344.
    • (1993) Carbohyd. Res. , vol.246 , pp. 337-344
    • Wormald, M.R.1    Edge, C.J.2
  • 224
    • 0028901083 scopus 로고
    • Alterations in gastric cin with malignant transformation: Novel path-way for mucin synthesis
    • Yamashita, Y., Chung, Y.S., Horie, R., Kannagi, R., and Sowa, M. 1995. Alterations in gastric cin with malignant transformation: novel path-way for mucin synthesis. J. Natl. Cancer Inst. 87: 441-446.
    • (1995) J. Natl. Cancer Inst. , vol.87 , pp. 441-446
    • Yamashita, Y.1    Chung, Y.S.2    Horie, R.3    Kannagi, R.4    Sowa, M.5
  • 225
    • 0029145205 scopus 로고
    • Construction and adhesive properties of a soluble MadCAM-1-Fc chimera expressed in a baculovirus system: Phylogenetic conservation of receptor-ligand interaction
    • Yang, Y., Sammar, M., Harrison, J.E., Lehnert, K., Print, C.G., Leung, E., Prestidge, R., and Krissansen, G.W. 1995. Construction and adhesive properties of a soluble MadCAM-1-Fc chimera expressed in a baculovirus system: phylogenetic conservation of receptor-ligand interaction. Scand. J. Immunol. 42: 235-247.
    • (1995) Scand. J. Immunol. , vol.42 , pp. 235-247
    • Yang, Y.1    Sammar, M.2    Harrison, J.E.3    Lehnert, K.4    Print, C.G.5    Leung, E.6    Prestidge, R.7    Krissansen, G.W.8
  • 226
    • 0028877229 scopus 로고
    • Involvement of N-linked carbohydrate chains of pig zona pellucida in sperm-egg binding
    • Yonezawa, N., Aoki, H., Hatanaka, Y., and Nakano, M. 1995. Involvement of N-linked carbohydrate chains of pig zona pellucida in sperm-egg binding. Eur. J. Biochem. 233: 35-41.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 35-41
    • Yonezawa, N.1    Aoki, H.2    Hatanaka, Y.3    Nakano, M.4
  • 227
    • 0028832270 scopus 로고
    • Thyrotropic action of human chorionic gonadotropin
    • Yoshimura, M. and Hershman, J.M. 1995. Thyrotropic action of human chorionic gonadotropin. Thyroid 5: 425-434.
    • (1995) Thyroid , vol.5 , pp. 425-434
    • Yoshimura, M.1    Hershman, J.M.2
  • 228
    • 0028016498 scopus 로고
    • Overexpressing sperm surface beta 1,4-galactosyltransferase in transgenic mice affects multiple aspects of spermegg interactions
    • Youakim, A., Hathaway, H.J., Miller, D.J., Gong, X., and Shur, B.D. 1994. Overexpressing sperm surface beta 1,4-galactosyltransferase in transgenic mice affects multiple aspects of spermegg interactions. J. Cell. Biol. 126: 1573-1583.
    • (1994) J. Cell. Biol. , vol.126 , pp. 1573-1583
    • Youakim, A.1    Hathaway, H.J.2    Miller, D.J.3    Gong, X.4    Shur, B.D.5
  • 229
    • 0026086828 scopus 로고
    • Increased UDP-GlcNAc:Galβ1-3GalNAc-R (Glc NAc to GalNAc) β-1,6-N-Acetylglucosaminyltransferase activity in metastatic murine tumor cell lines. Control of polylactosamine biosynthesis
    • Yousefi, S., Higgins, E., Daoling, Z., Pollex-Kruger, A., Hindsgaul, O., and Dennis, J.W. 1991. Increased UDP-GlcNAc:Galβ1-3GalNAc-R (Glc NAc to GalNAc) β-1,6-N-Acetylglucosaminyltransferase activity in metastatic murine tumor cell lines. Control of polylactosamine biosynthesis. J. Biol. Chem. 266: 1772-1782.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1772-1782
    • Yousefi, S.1    Higgins, E.2    Daoling, Z.3    Pollex-Kruger, A.4    Hindsgaul, O.5    Dennis, J.W.6
  • 230
    • 0025984497 scopus 로고
    • Isolation, composition, and biological activity of sugar chains of porcine oocyte zona pellucida 55K glycoproteins
    • Yurewicz, E.G., Pack, B.A., and Sacco, A.G. 1991. Isolation, composition, and biological activity of sugar chains of porcine oocyte zona pellucida 55K glycoproteins. Mol. Reprod. Dev. 30: 126-134.
    • (1991) Mol. Reprod. Dev. , vol.30 , pp. 126-134
    • Yurewicz, E.G.1    Pack, B.A.2    Sacco, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.