메뉴 건너뛰기




Volumn 478, Issue C, 2010, Pages 365-388

Intramolecular glycan-protein interactions in glycoproteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARAGINE LINKED OLIGOSACCHARIDE; CARBOHYDRATE; GLYCAN; GLYCOCONJUGATE; GLYCOPROTEIN; MUCIN; PROTEIN;

EID: 77956275854     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)78018-6     Document Type: Chapter
Times cited : (31)

References (106)
  • 1
    • 39049094267 scopus 로고    scopus 로고
    • Human IgG/Fc gamma R interactions are modulated by streptococcal IgG glycan hydrolysis
    • Allhorn M., Olin A.I., Nimmerjahn F., Collin M. Human IgG/Fc gamma R interactions are modulated by streptococcal IgG glycan hydrolysis. PLoS ONE 2008, 3:e1413.
    • (2008) PLoS ONE , vol.3
    • Allhorn, M.1    Olin, A.I.2    Nimmerjahn, F.3    Collin, M.4
  • 2
    • 0026638296 scopus 로고
    • A comprehensive procedure for preparation of partially methylated alditol acetates from glycoprotein carbohydrates
    • Anumula K.R., Taylor P.B. A comprehensive procedure for preparation of partially methylated alditol acetates from glycoprotein carbohydrates. Anal. Biochem. 1992, 203:101-108.
    • (1992) Anal. Biochem. , vol.203 , pp. 101-108
    • Anumula, K.R.1    Taylor, P.B.2
  • 3
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R., Hermjakob H., Sharon N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta Gen. Subj. 1999, 1473:4-8.
    • (1999) Biochim. Biophys. Acta Gen. Subj. , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 4
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold J.N., Wormald M.R., Sim R.B., Rudd P.M., Dwek R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25:21-50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 5
    • 70350055478 scopus 로고    scopus 로고
    • Branch-specific sialylation of IgG-Fc glycans by ST6Gal 1
    • Barb A.W., Brady E.K., Prestegard J.H. Branch-specific sialylation of IgG-Fc glycans by ST6Gal 1. Biochemistry 2009, 48:9705-9707.
    • (2009) Biochemistry , vol.48 , pp. 9705-9707
    • Barb, A.W.1    Brady, E.K.2    Prestegard, J.H.3
  • 6
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: From biosynthesis to pathogenesis of human disease
    • Barresi R., Campbell K.P. Dystroglycan: From biosynthesis to pathogenesis of human disease. J. Cell Sci. 2006, 119:199-207.
    • (2006) J. Cell Sci. , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 7
    • 0034066681 scopus 로고    scopus 로고
    • Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings
    • Barrientos L.G., Dolan C., Gronenborn A.M. Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings. J. Biomol. NMR 2000, 16:329-337.
    • (2000) J. Biomol. NMR , vol.16 , pp. 329-337
    • Barrientos, L.G.1    Dolan, C.2    Gronenborn, A.M.3
  • 8
    • 40849124080 scopus 로고    scopus 로고
    • The structural basis of the difference in sensitivity for PNGase F in the de-N-glycosylation of the native bovine pancreatic ribonucleases B and BS
    • Blanchard V., Frank M., Leeflang B.R., Boelens R., Kamerling J.P. The structural basis of the difference in sensitivity for PNGase F in the de-N-glycosylation of the native bovine pancreatic ribonucleases B and BS. Biochemistry 2008, 47:3435-3446.
    • (2008) Biochemistry , vol.47 , pp. 3435-3446
    • Blanchard, V.1    Frank, M.2    Leeflang, B.R.3    Boelens, R.4    Kamerling, J.P.5
  • 9
    • 0029063024 scopus 로고
    • Electron-microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan
    • Brancaccio A., Schulthess T., Gesemann M., Engel J. Electron-microscopic evidence for a mucin-like region in chick muscle alpha-dystroglycan. FEBS Lett. 1995, 368:139-142.
    • (1995) FEBS Lett. , vol.368 , pp. 139-142
    • Brancaccio, A.1    Schulthess, T.2    Gesemann, M.3    Engel, J.4
  • 10
    • 0022800346 scopus 로고
    • Conformation of the glycotripeptide repeating unit of antifreeze glycoprotein of polar fish as determined from the fully assigned proton NMR-spectrum
    • Bush C.A., Feeney R.E. Conformation of the glycotripeptide repeating unit of antifreeze glycoprotein of polar fish as determined from the fully assigned proton NMR-spectrum. Int. J. Pept. Protein Res. 1986, 28:386-397.
    • (1986) Int. J. Pept. Protein Res. , vol.28 , pp. 386-397
    • Bush, C.A.1    Feeney, R.E.2
  • 11
    • 33747873262 scopus 로고    scopus 로고
    • Glycopeptides as versatile tools for glycobiology
    • Buskas T., Ingale S., Boons G.J. Glycopeptides as versatile tools for glycobiology. Glycobiology 2006, 16:113R-136R.
    • (2006) Glycobiology , vol.16
    • Buskas, T.1    Ingale, S.2    Boons, G.J.3
  • 13
    • 0033179169 scopus 로고    scopus 로고
    • High prevalence of 2-mono- and 2, 6-di-substituted manol-terminating sequences among O-glycans released from brain glycopeptides by reductive alkaline hydrolysis
    • Chai W.G., Yuen C.T., Kogelberg H., Carruthers R.A., Margolis R.U., Feizi T., Lawson A.M. High prevalence of 2-mono- and 2, 6-di-substituted manol-terminating sequences among O-glycans released from brain glycopeptides by reductive alkaline hydrolysis. Eur. J. Biochem. 1999, 263:879-888.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 879-888
    • Chai, W.G.1    Yuen, C.T.2    Kogelberg, H.3    Carruthers, R.A.4    Margolis, R.U.5    Feizi, T.6    Lawson, A.M.7
  • 16
    • 13844267637 scopus 로고    scopus 로고
    • Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein
    • Chen B., Vogan E.M., Gong H.Y., Skehel J.J., Wiley D.C., Harrison S.C. Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein. Structure 2005, 13:197-211.
    • (2005) Structure , vol.13 , pp. 197-211
    • Chen, B.1    Vogan, E.M.2    Gong, H.Y.3    Skehel, J.J.4    Wiley, D.C.5    Harrison, S.C.6
  • 17
    • 33646071534 scopus 로고    scopus 로고
    • Galactosylation and sialylation of terminal glycan residues of human immunoglobulin G using bacterial glycosyltransferases with in situ regeneration of sugar-nucleotides
    • Chung S., Joo H., Jang K., Lee H., Lee S., Kim B. Galactosylation and sialylation of terminal glycan residues of human immunoglobulin G using bacterial glycosyltransferases with in situ regeneration of sugar-nucleotides. Enzyme Microb. Technol. 2006, 39:60-66.
    • (2006) Enzyme Microb. Technol. , vol.39 , pp. 60-66
    • Chung, S.1    Joo, H.2    Jang, K.3    Lee, H.4    Lee, S.5    Kim, B.6
  • 20
    • 33750970562 scopus 로고    scopus 로고
    • New insights into alpha-GalNAc-ser motif: Influence of hydrogen bonding versus solvent interactions on the preferred conformation
    • Corzana F., Busto J.H., Jimenez-Oses G., Asensio J.L., Jimenez-Barbero J., Peregrina J.M., Avenoza A. New insights into alpha-GalNAc-ser motif: Influence of hydrogen bonding versus solvent interactions on the preferred conformation. J. Am. Chem. Soc. 2006, 128:14640-14648.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14640-14648
    • Corzana, F.1    Busto, J.H.2    Jimenez-Oses, G.3    Asensio, J.L.4    Jimenez-Barbero, J.5    Peregrina, J.M.6    Avenoza, A.7
  • 21
    • 34547683219 scopus 로고    scopus 로고
    • Serine versus threonine glycosylation: The methyl group causes a drastic alteration on the carbohydrate orientation and on the surrounding water shell
    • Corzana F., Busto J.H., Jimenez-Oses G., de Luis M.G., Asensio J.L., Jimenez-Barbero J., Peregrina J.M., Avenoza A. Serine versus threonine glycosylation: The methyl group causes a drastic alteration on the carbohydrate orientation and on the surrounding water shell. J. Am. Chem. Soc. 2007, 129:9458-9467.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9458-9467
    • Corzana, F.1    Busto, J.H.2    Jimenez-Oses, G.3    de Luis, M.G.4    Asensio, J.L.5    Jimenez-Barbero, J.6    Peregrina, J.M.7    Avenoza, A.8
  • 22
    • 63849158824 scopus 로고    scopus 로고
    • The nature and sequence of the amino acid aglycone strongly modulates the conformation and dynamics effects of Tn antigen's clusters
    • Corzana F., Busto J.H., de Luis M.G., Jimenez-Barbero J., Avenoza A., Peregrina J.M. The nature and sequence of the amino acid aglycone strongly modulates the conformation and dynamics effects of Tn antigen's clusters. Chem. Eur. J. 2009, 15:3863-3874.
    • (2009) Chem. Eur. J. , vol.15 , pp. 3863-3874
    • Corzana, F.1    Busto, J.H.2    de Luis, M.G.3    Jimenez-Barbero, J.4    Avenoza, A.5    Peregrina, J.M.6
  • 23
    • 70349326274 scopus 로고    scopus 로고
    • The repertoire of glycan determinants in the human glycome
    • Cummings R.D. The repertoire of glycan determinants in the human glycome. Mol. Biosyst. 2009, 5:1087-1104.
    • (2009) Mol. Biosyst. , vol.5 , pp. 1087-1104
    • Cummings, R.D.1
  • 24
    • 0037169646 scopus 로고    scopus 로고
    • NMR dipolar couplings for the structure determination of biopolymers in solution
    • de Alba E., Tjandra N. NMR dipolar couplings for the structure determination of biopolymers in solution. Prog. Nucl. Magn. Reson. Spectrosc. 2002, 40:175-197.
    • (2002) Prog. Nucl. Magn. Reson. Spectrosc. , vol.40 , pp. 175-197
    • de Alba, E.1    Tjandra, N.2
  • 25
    • 0028357376 scopus 로고
    • Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein-application of gradient-enhanced natural-abundance H-1-C-13 HSQC and HSQC-TOCSY to the alpha-subunit of human chorionic-gonadotropin
    • de Beer T., van Zuylen C.E.M., Hard K., Boelens R., Kaptein R., Kamerling J.P., Vliegenthart J.F.G. Rapid and simple approach for the NMR resonance assignment of the carbohydrate chains of an intact glycoprotein-application of gradient-enhanced natural-abundance H-1-C-13 HSQC and HSQC-TOCSY to the alpha-subunit of human chorionic-gonadotropin. FEBS Lett. 1994, 348:1-6.
    • (1994) FEBS Lett. , vol.348 , pp. 1-6
    • de Beer, T.1    van Zuylen, C.E.M.2    Hard, K.3    Boelens, R.4    Kaptein, R.5    Kamerling, J.P.6    Vliegenthart, J.F.G.7
  • 26
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 1981, 20:2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 27
    • 33745686511 scopus 로고    scopus 로고
    • Synthesis and structural model of an alpha(2, 6)-sialyl-T glycosylated MUC1 eicosapeptide under physiological conditions
    • Dziadek S., Griesinger C., Kunz H., Reinscheid U.M. Synthesis and structural model of an alpha(2, 6)-sialyl-T glycosylated MUC1 eicosapeptide under physiological conditions. Chem. Eur. J. 2006, 12:4981-4993.
    • (2006) Chem. Eur. J. , vol.12 , pp. 4981-4993
    • Dziadek, S.1    Griesinger, C.2    Kunz, H.3    Reinscheid, U.M.4
  • 29
    • 0023008168 scopus 로고
    • Structures of O-linked oligosaccharides isolated from normal granulocytes, chronic myelogenous leukemia-cells, and acute myelogenous leukemia-cells
    • Fukuda M., Carlsson S.R., Klock J.C., Dell A. Structures of O-linked oligosaccharides isolated from normal granulocytes, chronic myelogenous leukemia-cells, and acute myelogenous leukemia-cells. J. Biol. Chem. 1986, 261:2796-2806.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2796-2806
    • Fukuda, M.1    Carlsson, S.R.2    Klock, J.C.3    Dell, A.4
  • 30
    • 59149097542 scopus 로고    scopus 로고
    • Galectin-glycan lattices regulate cell-surface glycoprotein organization and signaling
    • Garner O.B., Baum L.G. Galectin-glycan lattices regulate cell-surface glycoprotein organization and signaling. Biochem. Soc. Trans. 2008, 36:1472-1477.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1472-1477
    • Garner, O.B.1    Baum, L.G.2
  • 31
    • 0023666952 scopus 로고
    • Structure and dynamics of porcine submaxillary mucin as determined by natural abundance C-13 NMR-spectroscopy
    • Gerken T.A., Jentoft N. Structure and dynamics of porcine submaxillary mucin as determined by natural abundance C-13 NMR-spectroscopy. Biochemistry 1987, 26:4689-4699.
    • (1987) Biochemistry , vol.26 , pp. 4689-4699
    • Gerken, T.A.1    Jentoft, N.2
  • 32
    • 0024319438 scopus 로고
    • Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins-C-13 NMR-studies of ovine submaxillary mucin
    • Gerken T.A., Butenhof K.J., Shogren R. Effects of glycosylation on the conformation and dynamics of O-linked glycoproteins-C-13 NMR-studies of ovine submaxillary mucin. Biochemistry 1989, 28:5536-5543.
    • (1989) Biochemistry , vol.28 , pp. 5536-5543
    • Gerken, T.A.1    Butenhof, K.J.2    Shogren, R.3
  • 34
    • 54849437907 scopus 로고    scopus 로고
    • Analysis of IgA1 N-glycosylation and its contribution to Fc alpha RI binding
    • Gomes M.M., Wall S.B., Takahashi K., Novak J., Renfrow M.B., Herr A.B. Analysis of IgA1 N-glycosylation and its contribution to Fc alpha RI binding. Biochemistry 2008, 47:11285-11299.
    • (2008) Biochemistry , vol.47 , pp. 11285-11299
    • Gomes, M.M.1    Wall, S.B.2    Takahashi, K.3    Novak, J.4    Renfrow, M.B.5    Herr, A.B.6
  • 35
    • 66149102040 scopus 로고    scopus 로고
    • Characterization of N-linked glycosylation on recombinant glycoproteins produced in Pichia pastoris using ESI-MS and MALDI-TOF
    • Gong B., Cukan M., Fisher R., Li H., Stadheim T.A., Gerngross T. Characterization of N-linked glycosylation on recombinant glycoproteins produced in Pichia pastoris using ESI-MS and MALDI-TOF. Meth. Mol. Biol. 2009, 534:213-223.
    • (2009) Meth. Mol. Biol. , vol.534 , pp. 213-223
    • Gong, B.1    Cukan, M.2    Fisher, R.3    Li, H.4    Stadheim, T.A.5    Gerngross, T.6
  • 36
    • 0037031255 scopus 로고    scopus 로고
    • Effect of glycosylation on muc1 humoral immune recognition: NMR studies of MUC1 glycopeptide-antibody interactions
    • Grinstead J.S., Koganty R.R., Krantz M.J., Longenecker B.M., Campbell A.P. Effect of glycosylation on muc1 humoral immune recognition: NMR studies of MUC1 glycopeptide-antibody interactions. Biochemistry 2002, 41:9946-9961.
    • (2002) Biochemistry , vol.41 , pp. 9946-9961
    • Grinstead, J.S.1    Koganty, R.R.2    Krantz, M.J.3    Longenecker, B.M.4    Campbell, A.P.5
  • 37
    • 62549107841 scopus 로고    scopus 로고
    • The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability
    • Hanson S.R., Culyba E.K., Hsu T.L., Wong C.H., Kelly J.W., Powers E.T. The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability. Proc. Natl. Acad. Sci. USA 2009, 106:3131-3136.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 3131-3136
    • Hanson, S.R.1    Culyba, E.K.2    Hsu, T.L.3    Wong, C.H.4    Kelly, J.W.5    Powers, E.T.6
  • 38
    • 0037497304 scopus 로고    scopus 로고
    • Insights into IgA-mediated immune responses from the crystal structures of human Fc alpha RI and its complex with IgA1-Fc
    • Herr A.B., Ballister E.R., Bjorkman P.J. Insights into IgA-mediated immune responses from the crystal structures of human Fc alpha RI and its complex with IgA1-Fc. Nature 2003, 423:614-620.
    • (2003) Nature , vol.423 , pp. 614-620
    • Herr, A.B.1    Ballister, E.R.2    Bjorkman, P.J.3
  • 41
    • 70349999667 scopus 로고    scopus 로고
    • Recent departures in the synthesis of peptides and glycopeptides
    • Kan C., Danishefsky S.J. Recent departures in the synthesis of peptides and glycopeptides. Tetrahedron 2009, 65:9047-9065.
    • (2009) Tetrahedron , vol.65 , pp. 9047-9065
    • Kan, C.1    Danishefsky, S.J.2
  • 42
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y., Nimmerjahn F., Ravetch J.V. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006, 313:670-673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 43
    • 0034601779 scopus 로고    scopus 로고
    • Structural effects of O-glycosylation on a 15-residue peptide from the mucin (MUC1) core protein
    • Kirnarsky L., Prakash O., Vogen S.M., Nomoto M., Hollingsworth M.A., Sherman S. Structural effects of O-glycosylation on a 15-residue peptide from the mucin (MUC1) core protein. Biochemistry 2000, 39:12076-12082.
    • (2000) Biochemistry , vol.39 , pp. 12076-12082
    • Kirnarsky, L.1    Prakash, O.2    Vogen, S.M.3    Nomoto, M.4    Hollingsworth, M.A.5    Sherman, S.6
  • 44
    • 40749147518 scopus 로고    scopus 로고
    • The N-linked sugar chains of human immunoglobulin G: Their unique pattern, and their functional roles
    • Kobata A. The N-linked sugar chains of human immunoglobulin G: Their unique pattern, and their functional roles. Biochim. Biophys. Acta Gen. Subj. 2008, 1780:472-478.
    • (2008) Biochim. Biophys. Acta Gen. Subj. , vol.1780 , pp. 472-478
    • Kobata, A.1
  • 46
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S., Mimura Y., Jefferis R., Huber R., Sondermann P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 2003, 325:979-989.
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 47
    • 0031872222 scopus 로고    scopus 로고
    • Conformational and dynamic properties of a 14 residue antifreeze glycopeptide from antarctic cod
    • Lane A.N., Hays L.M., Feeney R.E., Crowe L.M., Crowe J.H. Conformational and dynamic properties of a 14 residue antifreeze glycopeptide from antarctic cod. Protein Sci. 1998, 7:1555-1563.
    • (1998) Protein Sci. , vol.7 , pp. 1555-1563
    • Lane, A.N.1    Hays, L.M.2    Feeney, R.E.3    Crowe, L.M.4    Crowe, J.H.5
  • 48
    • 0021866261 scopus 로고
    • Effector functions of a monoclonal aglycosylated mouse IgG2a: Binding and activation of complement component C1 and interaction with human monocyte Fc receptor
    • Leatherbarrow R.J., Rademacher T.W., Dwek R.A., Woof J.M., Clark A., Burton D.R., Richardson N., Feinstein A. Effector functions of a monoclonal aglycosylated mouse IgG2a: Binding and activation of complement component C1 and interaction with human monocyte Fc receptor. Mol. Immunol. 1985, 22:407-415.
    • (1985) Mol. Immunol. , vol.22 , pp. 407-415
    • Leatherbarrow, R.J.1    Rademacher, T.W.2    Dwek, R.A.3    Woof, J.M.4    Clark, A.5    Burton, D.R.6    Richardson, N.7    Feinstein, A.8
  • 49
    • 64749109053 scopus 로고    scopus 로고
    • An efficient platform for screening expression and crystallization of glycoproteins produced in human cells
    • Lee J.E., Fusco M.L., Saphire E.O. An efficient platform for screening expression and crystallization of glycoproteins produced in human cells. Nat. Protoc. 2009, 4:592-604.
    • (2009) Nat. Protoc. , vol.4 , pp. 592-604
    • Lee, J.E.1    Fusco, M.L.2    Saphire, E.O.3
  • 50
    • 0034886703 scopus 로고    scopus 로고
    • Glycosylated and phosphorylated proteins-expression in yeast and oocytes of xenopus: Prospects and challenges-relevance to expression of thermostable proteins
    • Li P.Z., Go X.G., Arellano R.O., Renugopalakrishnan V. Glycosylated and phosphorylated proteins-expression in yeast and oocytes of xenopus: Prospects and challenges-relevance to expression of thermostable proteins. Protein Expr. Purif. 2001, 22:369-380.
    • (2001) Protein Expr. Purif. , vol.22 , pp. 369-380
    • Li, P.Z.1    Go, X.G.2    Arellano, R.O.3    Renugopalakrishnan, V.4
  • 51
    • 23744474504 scopus 로고    scopus 로고
    • Parallel solid-phase synthesis of mucin-like glycopeptides
    • Liu M., Barany G., Live D. Parallel solid-phase synthesis of mucin-like glycopeptides. Carbohydr. Res. 2005, 340:2111-2122.
    • (2005) Carbohydr. Res. , vol.340 , pp. 2111-2122
    • Liu, M.1    Barany, G.2    Live, D.3
  • 52
    • 34247184796 scopus 로고    scopus 로고
    • Spin-labeled analogs of CMP-NeuAc as NMR probes of the alpha-2, 6-sialyltransferase ST6Gal 1
    • Liu S., Venot A., Meng L., Tian F., Moremen K.W., Boons G.J., Prestegard J.H. Spin-labeled analogs of CMP-NeuAc as NMR probes of the alpha-2, 6-sialyltransferase ST6Gal 1. Chem. Biol. 2007, 14:409-418.
    • (2007) Chem. Biol. , vol.14 , pp. 409-418
    • Liu, S.1    Venot, A.2    Meng, L.3    Tian, F.4    Moremen, K.W.5    Boons, G.J.6    Prestegard, J.H.7
  • 53
    • 46749098419 scopus 로고    scopus 로고
    • Conformational consequences of protein glycosylation: Preparation of O-mannosyl serine and threonine building blocks, and their incorporation into glycopeptide sequences derived from alpha-dystroglycan
    • Liu M., Borgert A., Barany G., Live D. Conformational consequences of protein glycosylation: Preparation of O-mannosyl serine and threonine building blocks, and their incorporation into glycopeptide sequences derived from alpha-dystroglycan. Biopolymers 2008, 90:358-368.
    • (2008) Biopolymers , vol.90 , pp. 358-368
    • Liu, M.1    Borgert, A.2    Barany, G.3    Live, D.4
  • 54
    • 0030470557 scopus 로고    scopus 로고
    • Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma receptor i and influence the synthesis of its oligosaccharide chains
    • Lund J., Takahashi N., Pound J.D., Goodall M., Jefferis R. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma receptor i and influence the synthesis of its oligosaccharide chains. J. Immunol. 1996, 157:4963-4969.
    • (1996) J. Immunol. , vol.157 , pp. 4963-4969
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Jefferis, R.5
  • 55
    • 0030167995 scopus 로고    scopus 로고
    • Expression of human chorionic gonadotropin uniformly labeled with NMR isotopes in Chinese hamster ovary cells: An advance toward rapid determination of glycoprotein structures
    • Lustbader J.W., Birken S., Pollak S., Pound A., Chait B.T., Mirza U.A., Ramnarain S., Canfield R.E., Brown J.M. Expression of human chorionic gonadotropin uniformly labeled with NMR isotopes in Chinese hamster ovary cells: An advance toward rapid determination of glycoprotein structures. J. Biomol. NMR 1996, 7:295-304.
    • (1996) J. Biomol. NMR , vol.7 , pp. 295-304
    • Lustbader, J.W.1    Birken, S.2    Pollak, S.3    Pound, A.4    Chait, B.T.5    Mirza, U.A.6    Ramnarain, S.7    Canfield, R.E.8    Brown, J.M.9
  • 56
    • 58849162321 scopus 로고    scopus 로고
    • Analysis and validation of carbohydrate three-dimensional structures
    • Lutteke T. Analysis and validation of carbohydrate three-dimensional structures. Acta Crystallogr. D Biol. Crystallogr. 2009, 65:156-168.
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , pp. 156-168
    • Lutteke, T.1
  • 58
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia-coli ribonuclease H1-correlations with structure and function in an active enzyme
    • Mandel A.M., Akke M., Palmer A.G. Backbone dynamics of Escherichia-coli ribonuclease H1-correlations with structure and function in an active enzyme. J. Mol. Biol. 1995, 246:144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 59
    • 33645781487 scopus 로고    scopus 로고
    • Construction of highly glycosylated mucin-type glycopeptides based on microwave-assisted solid-phase syntheses and enzymatic modifications
    • Matsushita T., Hinou H., Fumoto M., Kurogochi M., Fujitani N., Shimizu H., Nishimura S.I. Construction of highly glycosylated mucin-type glycopeptides based on microwave-assisted solid-phase syntheses and enzymatic modifications. J. Org. Chem. 2006, 71:3051-3063.
    • (2006) J. Org. Chem. , vol.71 , pp. 3051-3063
    • Matsushita, T.1    Hinou, H.2    Fumoto, M.3    Kurogochi, M.4    Fujitani, N.5    Shimizu, H.6    Nishimura, S.I.7
  • 60
    • 85014310281 scopus 로고    scopus 로고
    • Conformation of glycopeptides and glycoproteins
    • Meyer B., Moller H. Conformation of glycopeptides and glycoproteins. Top. Curr. Chem. 2007, 267:187-251.
    • (2007) Top. Curr. Chem. , vol.267 , pp. 187-251
    • Meyer, B.1    Moller, H.2
  • 61
    • 0026726624 scopus 로고
    • NMR-study of interaction between sugar and peptide moieties in mucin-type model glycopeptides
    • Mimura Y., Yamamoto Y., Inoue Y., Chujo R. NMR-study of interaction between sugar and peptide moieties in mucin-type model glycopeptides. Int. J. Biol. Macromol. 1992, 14:242-248.
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 242-248
    • Mimura, Y.1    Yamamoto, Y.2    Inoue, Y.3    Chujo, R.4
  • 63
    • 0032887723 scopus 로고    scopus 로고
    • NMR analysis of human salivary mucin (MUC7) derived O-linked model glycopeptides: Comparison of structural features and carbohydrate-peptide interactions
    • Naganagowda G.A., Gururaja T.L., Satyanarayana J., Levine M.J. NMR analysis of human salivary mucin (MUC7) derived O-linked model glycopeptides: Comparison of structural features and carbohydrate-peptide interactions. J. Pept. Res. 1999, 54:290-310.
    • (1999) J. Pept. Res. , vol.54 , pp. 290-310
    • Naganagowda, G.A.1    Gururaja, T.L.2    Satyanarayana, J.3    Levine, M.J.4
  • 66
    • 33748195979 scopus 로고    scopus 로고
    • Glycosylation in cellular mechanisms of health and disease
    • Ohtsubo K., Marth J.D. Glycosylation in cellular mechanisms of health and disease. Cell 2006, 126:855-867.
    • (2006) Cell , vol.126 , pp. 855-867
    • Ohtsubo, K.1    Marth, J.D.2
  • 67
    • 0033026167 scopus 로고    scopus 로고
    • Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values
    • Ottiger M., Bax A. Bicelle-based liquid crystals for NMR-measurement of dipolar couplings at acidic and basic pH values. J. Biomol. NMR 1999, 13:187-191.
    • (1999) J. Biomol. NMR , vol.13 , pp. 187-191
    • Ottiger, M.1    Bax, A.2
  • 69
    • 72149096309 scopus 로고    scopus 로고
    • Advances in chemical ligation strategies for the synthesis of glycopeptides and glycoproteins
    • Payne R.J., Wong C.H. Advances in chemical ligation strategies for the synthesis of glycopeptides and glycoproteins. Chem. Commun. 2010, 46:21-43.
    • (2010) Chem. Commun. , vol.46 , pp. 21-43
    • Payne, R.J.1    Wong, C.H.2
  • 70
    • 1342327544 scopus 로고    scopus 로고
    • Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding
    • Petrescu A.J., Milac A.L., Petrescu S.M., Dwek R.A., Wormald M.R. Statistical analysis of the protein environment of N-glycosylation sites: Implications for occupancy, structure, and folding. Glycobiology 2004, 14:103-114.
    • (2004) Glycobiology , vol.14 , pp. 103-114
    • Petrescu, A.J.1    Milac, A.L.2    Petrescu, S.M.3    Dwek, R.A.4    Wormald, M.R.5
  • 71
    • 33749071408 scopus 로고    scopus 로고
    • Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding
    • Petrescu A.J., Wormald M.R., Dwek R.A. Structural aspects of glycomes with a focus on N-glycosylation and glycoprotein folding. Curr. Opin. Struct. Biol. 2006, 16:600-607.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 600-607
    • Petrescu, A.J.1    Wormald, M.R.2    Dwek, R.A.3
  • 73
    • 0025804150 scopus 로고
    • Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum
    • Plummer T.H., Tarentino A.L. Purification of the oligosaccharide-cleaving enzymes of Flavobacterium meningosepticum. Glycobiology 1991, 1:257-263.
    • (1991) Glycobiology , vol.1 , pp. 257-263
    • Plummer, T.H.1    Tarentino, A.L.2
  • 74
  • 75
    • 0035979377 scopus 로고    scopus 로고
    • Glycoengineering of therapeutic glycoproteins: In vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues
    • Raju T.S., Briggs J.B., Chamow S.M., Winkler M.E., Jones A.J. Glycoengineering of therapeutic glycoproteins: In vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues. Biochemistry 2001, 40:8868-8876.
    • (2001) Biochemistry , vol.40 , pp. 8868-8876
    • Raju, T.S.1    Briggs, J.B.2    Chamow, S.M.3    Winkler, M.E.4    Jones, A.J.5
  • 76
    • 0034661578 scopus 로고    scopus 로고
    • Derivatization strategies for preparing N-glycan probes
    • Rice K.G. Derivatization strategies for preparing N-glycan probes. Anal. Biochem. 2000, 283:10-16.
    • (2000) Anal. Biochem. , vol.283 , pp. 10-16
    • Rice, K.G.1
  • 77
    • 62649171202 scopus 로고    scopus 로고
    • Emerging methods for the production of homogeneous human glycoproteins
    • Rich J.R., Withers S.G. Emerging methods for the production of homogeneous human glycoproteins. Nat. Chem. Biol. 2009, 5:206-215.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 206-215
    • Rich, J.R.1    Withers, S.G.2
  • 79
    • 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., Kaufman B. Effects of deglycosylation on the architecture of ovine submaxillary mucin glycoprotein. J. Biol. Chem. 1984, 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
  • 80
    • 0033583320 scopus 로고    scopus 로고
    • Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules
    • Sanchez L.M., Chirino A.J., Bjorkman P. Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules. Science 1999, 283:1914-1919.
    • (1999) Science , vol.283 , pp. 1914-1919
    • Sanchez, L.M.1    Chirino, A.J.2    Bjorkman, P.3
  • 82
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • Scallon B.J., Tam S.H., McCarthy S.G., Cai A.N., Raju T.S. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol. Immunol. 2007, 44:1524-1534.
    • (2007) Mol. Immunol. , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 83
    • 0033136832 scopus 로고    scopus 로고
    • 'Wave-type' structure of a synthetic hexaglycosylated decapeptide: A part of the extracellular domain of human glycophorin A
    • Schuster O., Klich G., Sinnwell V., Kranz H., Paulsen H., Meyer B. 'Wave-type' structure of a synthetic hexaglycosylated decapeptide: A part of the extracellular domain of human glycophorin A. J. Biomol. NMR 1999, 14:33-45.
    • (1999) J. Biomol. NMR , vol.14 , pp. 33-45
    • Schuster, O.1    Klich, G.2    Sinnwell, V.3    Kranz, H.4    Paulsen, H.5    Meyer, B.6
  • 86
    • 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., Jentoft N. Role of glycosylation on the conformation and chain dimensions of O-linked glycoproteins-light-scattering-studies of ovine submaxillary mucin. Biochemistry 1989, 28:5525-5536.
    • (1989) Biochemistry , vol.28 , pp. 5525-5536
    • Shogren, R.1    Gerken, T.A.2    Jentoft, N.3
  • 87
    • 0032544933 scopus 로고    scopus 로고
    • Glycosylation of threonine of the repeating unit of RNA polymerase II with beta-linked N-acetylglucosame leads to a turnlike structure
    • Simanek E.E., Huang D.H., Pasternack L., Machajewski T.D., Seitz O., Millar D.S., Dyson H.J., Wong C.H. Glycosylation of threonine of the repeating unit of RNA polymerase II with beta-linked N-acetylglucosame leads to a turnlike structure. J. Am. Chem. Soc. 1998, 120:11567-11575.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11567-11575
    • Simanek, E.E.1    Huang, D.H.2    Pasternack, L.3    Machajewski, T.D.4    Seitz, O.5    Millar, D.S.6    Dyson, H.J.7    Wong, C.H.8
  • 88
    • 61749095310 scopus 로고    scopus 로고
    • NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation
    • Slynko V., Schubert M., Numao S., Kowarik M., Aebi M., Allain F.H.T. NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation. J. Am. Chem. Soc. 2009, 131:1274-1281.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1274-1281
    • Slynko, V.1    Schubert, M.2    Numao, S.3    Kowarik, M.4    Aebi, M.5    Allain, F.H.T.6
  • 89
    • 0030848719 scopus 로고    scopus 로고
    • Immunoreactive T and Tn epitopes in cancer diagnosis, prognosis, and immunotherapy
    • Springer G.F. Immunoreactive T and Tn epitopes in cancer diagnosis, prognosis, and immunotherapy. J. Mol. Med. 1997, 75:594-602.
    • (1997) J. Mol. Med. , vol.75 , pp. 594-602
    • Springer, G.F.1
  • 91
    • 0028957151 scopus 로고
    • Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides
    • Takahashi N., Nakagawa H., Fujikawa K., Kawamura Y., Tomiya N. Three-dimensional elution mapping of pyridylaminated N-linked neutral and sialyl oligosaccharides. Anal. Biochem. 1995, 226:139-146.
    • (1995) Anal. Biochem. , vol.226 , pp. 139-146
    • Takahashi, N.1    Nakagawa, H.2    Fujikawa, K.3    Kawamura, Y.4    Tomiya, N.5
  • 92
    • 0036451590 scopus 로고    scopus 로고
    • O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines-distinct specificity of GalNAc-transferase isoforms
    • Takeuchi H., Kato K., Hassan H., Clausen H., Irimura T. O-GalNAc incorporation into a cluster acceptor site of three consecutive threonines-distinct specificity of GalNAc-transferase isoforms. Eur. J. Biochem. 2002, 269:6173-6183.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6173-6183
    • Takeuchi, H.1    Kato, K.2    Hassan, H.3    Clausen, H.4    Irimura, T.5
  • 94
    • 0037234565 scopus 로고    scopus 로고
    • All in the family: The UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases
    • Ten Hagen K.G., Fritz T.A., Tabak L.A. All in the family: The UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferases. Glycobiology 2003, 13:1R-16R.
    • (2003) Glycobiology , vol.13
    • Ten Hagen, K.G.1    Fritz, T.A.2    Tabak, L.A.3
  • 95
    • 0033671867 scopus 로고    scopus 로고
    • Stabilization of human recombinant erythropoietin through interactions with the highly branched N-glycans
    • Toyoda T., Itai T., Arakawa T., Aoki K.H., Yamaguchi H. Stabilization of human recombinant erythropoietin through interactions with the highly branched N-glycans. J. Biochem. 2000, 128:731-737.
    • (2000) J. Biochem. , vol.128 , pp. 731-737
    • Toyoda, T.1    Itai, T.2    Arakawa, T.3    Aoki, K.H.4    Yamaguchi, H.5
  • 96
    • 0036236811 scopus 로고    scopus 로고
    • N-glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface: Studies by surface plasmon resonance analysis
    • Toyoda T., Arakawa T., Yamaguchi H. N-glycans stabilize human erythropoietin through hydrophobic interactions with the hydrophobic protein surface: Studies by surface plasmon resonance analysis. J. Biochem. 2002, 131:511-515.
    • (2002) J. Biochem. , vol.131 , pp. 511-515
    • Toyoda, T.1    Arakawa, T.2    Yamaguchi, H.3
  • 97
    • 44049095632 scopus 로고    scopus 로고
    • Protein-glycan interactions in the control of innate and adaptive immune responses
    • van Kooyk Y., Rabinovich G.A. Protein-glycan interactions in the control of innate and adaptive immune responses. Nat. Immunol. 2008, 9:593-601.
    • (2008) Nat. Immunol. , vol.9 , pp. 593-601
    • van Kooyk, Y.1    Rabinovich, G.A.2
  • 99
    • 0343373375 scopus 로고
    • 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins
    • Vliegenthart J.F.G., Dorland L., Van Halbeek H. 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins. Adv. Carbohydr. Chem. Biochem. 1983, 41:209-374.
    • (1983) Adv. Carbohydr. Chem. Biochem. , vol.41 , pp. 209-374
    • Vliegenthart, J.F.G.1    Dorland, L.2    Van Halbeek, H.3
  • 100
    • 46549088526 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation
    • Wang L.X. Chemoenzymatic synthesis of glycopeptides and glycoproteins through endoglycosidase-catalyzed transglycosylation. Carbohydr. Res. 2008, 343:1509-1522.
    • (2008) Carbohydr. Res. , vol.343 , pp. 1509-1522
    • Wang, L.X.1
  • 102
    • 33751019949 scopus 로고    scopus 로고
    • Identification of O-GlcNAc sites on proteins
    • M. Fukuda (Ed.)
    • Whelan S.A., Hart G.W. Identification of O-GlcNAc sites on proteins. Methods in Enzymology 2006, Vol. 415, pp.113-133. M. Fukuda (Ed.).
    • (2006) Methods in Enzymology , vol.415 , pp. 113-133
    • Whelan, S.A.1    Hart, G.W.2
  • 104
    • 0032176417 scopus 로고    scopus 로고
    • Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective C-13 labeling of the glycans
    • Yamaguchi Y., Kato K., Shindo M., Aoki S., Furusho K., Koga K., Takahashi N., Arata Y., Shimada I. Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective C-13 labeling of the glycans. J. Biomol. NMR 1998, 12:385-394.
    • (1998) J. Biomol. NMR , vol.12 , pp. 385-394
    • Yamaguchi, Y.1    Kato, K.2    Shindo, M.3    Aoki, S.4    Furusho, K.5    Koga, K.6    Takahashi, N.7    Arata, Y.8    Shimada, I.9
  • 106
    • 40149092211 scopus 로고    scopus 로고
    • Chemical synthesis of a glycoprotein having an intact human complex-type sialyloligosaccharide under the Boc and Fmoc synthetic strategies
    • Yamamoto N., Tanabe Y., Okamoto R., Dawson P.E., Kajihara Y. Chemical synthesis of a glycoprotein having an intact human complex-type sialyloligosaccharide under the Boc and Fmoc synthetic strategies. J. Am. Chem. Soc. 2008, 130:501-510.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 501-510
    • Yamamoto, N.1    Tanabe, Y.2    Okamoto, R.3    Dawson, P.E.4    Kajihara, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.