메뉴 건너뛰기




Volumn 13, Issue 7, 2012, Pages 8398-8429

Function and 3D structure of the N-glycans on glycoproteins

Author keywords

Glycoform; Glycoprotein; N glycan; Protein crystallography

Indexed keywords

ARYLPHORIN; BETA DALACTOSIDASE; CELL SURFACE RECEPTOR; FC RECEPTOR; GLYCAN; GLYCOPEPTIDE; IMMUNOGLOBULIN FC FRAGMENT; MANNOSE; UNCLASSIFIED DRUG; VIRUS SIALIDASE; GLYCOPROTEIN; POLYSACCHARIDE;

EID: 84864365553     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms13078398     Document Type: Review
Times cited : (102)

References (112)
  • 1
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius, A.; Aebi, M. Intracellular functions of N-linked glycans. Science 2001, 291, 2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 2
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler, R.; Hermjakob, H.; Sharon, N. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1999, 1473, 4-8.
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 3
    • 0026705382 scopus 로고
    • Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine:β-D-mannoside β-1,4-N-acetylglucosaminyltransferase III from rat kidney
    • Nishikawa, A.; Ihara, Y.; Hatakeyama, M.; Kangawa, K.; Taniguchi, N. Purification, cDNA cloning, and expression of UDP-N-acetylglucosamine:β-D-mannoside β-1,4-N-acetylglucosaminyltransferase III from rat kidney. J. Biol. Chem. 1992, 267, 18199-18204.
    • (1992) J. Biol. Chem , vol.267 , pp. 18199-18204
    • Nishikawa, A.1    Ihara, Y.2    Hatakeyama, M.3    Kangawa, K.4    Taniguchi, N.5
  • 4
    • 0020356007 scopus 로고
    • A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc:α-D-mannoside-β-1,6-N-acetylglucosaminyltransferase
    • Cummings, R.D.; Trowbridge, I.S.; Kornfeld, S. A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc:α-D-mannoside-β-1,6-N-acetylglucosaminyltransferase. J. Biol. Chem. 1982, 257, 13421-13427.
    • (1982) J. Biol. Chem , vol.257 , pp. 13421-13427
    • Cummings, R.D.1    Trowbridge, I.S.2    Kornfeld, S.3
  • 6
    • 0030220095 scopus 로고    scopus 로고
    • The structural role of sugars in glycoproteins
    • Wyss, D.F.; Wagner, G. The structural role of sugars in glycoproteins. Curr. Opin. Biotechnol. 1996, 7, 409-416.
    • (1996) Curr. Opin. Biotechnol , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner, G.2
  • 7
    • 0033548254 scopus 로고    scopus 로고
    • Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1)
    • Kwong, P.D.; Wyatt, R.; Desjardins, E.; Robinson, J.; Culp, J.S.; Hellmig, B.D.; Sweet, R.W.; Sodroski, J.; Hendrickson, W.A. Probability analysis of variational crystallization and its application to gp120, the exterior envelope glycoprotein of type 1 human immunodeficiency virus (HIV-1). J. Biol. Chem. 1999, 274, 4115-4123.
    • (1999) J. Biol. Chem , vol.274 , pp. 4115-4123
    • Kwong, P.D.1    Wyatt, R.2    Desjardins, E.3    Robinson, J.4    Culp, J.S.5    Hellmig, B.D.6    Sweet, R.W.7    Sodroski, J.8    Hendrickson, W.A.9
  • 9
    • 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
  • 10
    • 0024559003 scopus 로고
    • Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity
    • Stanley, P. Chinese hamster ovary cell mutants with multiple glycosylation defects for production of glycoproteins with minimal carbohydrate heterogeneity. Mol. Cell. Biol. 1989, 9, 377-383.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 377-383
    • Stanley, P.1
  • 11
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves, P.J.; Callewaert, N.; Contreras, R.; Khorana, H.G. Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc. Natl. Acad. Sci. USA 2002, 99, 13419-13424.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 13
    • 0032937844 scopus 로고    scopus 로고
    • A statistical analysis of Nand O-glycan linkage conformations from crystallographic data
    • Petrescu, A.J.; Petrescu, S.M.; Dwek, R.A.; Wormald, M.R. A statistical analysis of Nand O-glycan linkage conformations from crystallographic data. Glycobiology 1999, 9, 343-352.
    • (1999) Glycobiology , vol.9 , pp. 343-352
    • Petrescu, A.J.1    Petrescu, S.M.2    Dwek, R.A.3    Wormald, M.R.4
  • 14
    • 0036462598 scopus 로고    scopus 로고
    • Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling
    • Wormald, M.R.; Petrescu, A.J.; Pao, Y.L.; Glithero, A.; Elliott, T.; Dwek, R.A. Conformational studies of oligosaccharides and glycopeptides: Complementarity of NMR, X-ray crystallography, and molecular modelling. Chem. Rev. 2002, 102, 371-386.
    • (2002) Chem. Rev , vol.102 , pp. 371-386
    • Wormald, M.R.1    Petrescu, A.J.2    Pao, Y.L.3    Glithero, A.4    Elliott, T.5    Dwek, R.A.6
  • 16
    • 38549146892 scopus 로고    scopus 로고
    • Glycoconjugate Data Bank: Structures-An annotated glycan structure database and N-glycan primary structure verification service
    • Nakahara, T.; Hashimoto, R.; Nakagawa, H.; Monde, K.; Miura, N.; Nishimura, S. Glycoconjugate Data Bank: Structures-An annotated glycan structure database and N-glycan primary structure verification service. Nucleic Acids Res. 2008, 36, D368-371.
    • (2008) Nucleic Acids Res , vol.36
    • Nakahara, T.1    Hashimoto, R.2    Nakagawa, H.3    Monde, K.4    Miura, N.5    Nishimura, S.6
  • 17
    • 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
  • 18
    • 0035012654 scopus 로고    scopus 로고
    • Crystal structure at 2.8 Å of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding
    • Martin, W.L.; West, A.P., Jr.; Gan, L.; Bjorkman, P.J. Crystal structure at 2.8 Å of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding. Mol. Cell 2001, 7, 867-877.
    • (2001) Mol. Cell , vol.7 , pp. 867-877
    • Martin, W.L.1    West Jr., A.P.2    Gan, L.3    Bjorkman, P.J.4
  • 19
    • 0031017896 scopus 로고    scopus 로고
    • Refined structure of an intact IgG2a monoclonal antibody
    • Harris, L.J.; Larson, S.B.; Hasel, K.W.; McPherson, A. Refined structure of an intact IgG2a monoclonal antibody. Biochemistry 1997, 36, 1581-1597.
    • (1997) Biochemistry , vol.36 , pp. 1581-1597
    • Harris, L.J.1    Larson, S.B.2    Hasel, K.W.3    McPherson, A.4
  • 21
    • 0028829350 scopus 로고
    • Glycobiology: The function of sugar in the IgG molecule
    • Dwek, R.A.; Lellouch, A.C.; Wormald, M.R. Glycobiology: "The function of sugar in the IgG molecule". J. Anat. 1995, 187 (Pt 2), 279-292.
    • (1995) J. Anat , vol.187 , Issue.Pt 2 , pp. 279-292
    • Dwek, R.A.1    Lellouch, A.C.2    Wormald, M.R.3
  • 22
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcγ RIII and antibody-dependent cellular toxicity
    • Shields, R.L.; Lai, J.; Keck, R.; O'Connell, L.Y.; Hong, K.; Meng, Y.G.; Weikert, S.H.; Presta, L.G. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcγ RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 2002, 277, 26733-26740.
    • (2002) J. Biol. Chem , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7    Presta, L.G.8
  • 23
    • 28544449847 scopus 로고    scopus 로고
    • Divergent immunoglobulin G subclass activity through selective Fc receptor binding
    • Nimmerjahn, F.; Ravetch, J.V. Divergent immunoglobulin G subclass activity through selective Fc receptor binding. Science 2005, 310, 1510-1512.
    • (2005) Science , vol.310 , pp. 1510-1512
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 25
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • Samuelsson, A.; Towers, T.L.; Ravetch, J.V. Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor. Science 2001, 291, 484-486.
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 26
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umaña, P.; Jean-Mairet, J.; Moudry, R.; Amstutz, H.; Bailey, J.E. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat. Biotechnol. 1999, 17, 176-180.
    • (1999) Nat. Biotechnol , vol.17 , pp. 176-180
    • Umaña, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 27
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa, T.; Nakamura, K.; Yamane, N.; Shoji-Hosaka, E.; Kanda, Y.; Sakurada, M.; Uchida, K.; Anazawa, H.; Satoh, M.; Yamasaki, M.; et al. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. 2003, 278, 3466-3473.
    • (2003) J. Biol. Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10
  • 28
    • 0020738965 scopus 로고
    • The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G
    • Sutton, B.J.; Phillips, D.C. The three-dimensional structure of the carbohydrate within the Fc fragment of immunoglobulin G. Biochem. Soc. Trans. 1983, 11, 130-132.
    • (1983) Biochem. Soc. Trans , vol.11 , pp. 130-132
    • Sutton, B.J.1    Phillips, D.C.2
  • 30
  • 31
    • 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
  • 33
    • 64149121224 scopus 로고    scopus 로고
    • Structural characterization of a human Fc fragment engineered for extended serum half-life
    • Oganesyan, V.; Damschroder, M.M.; Woods, R.M.; Cook, K.E.; Wu, H.; Dall'Acqua, W.F. Structural characterization of a human Fc fragment engineered for extended serum half-life. Mol. Immunol. 2009, 46, 1750-1755.
    • (2009) Mol. Immunol , vol.46 , pp. 1750-1755
    • Oganesyan, V.1    Damschroder, M.M.2    Woods, R.M.3    Cook, K.E.4    Wu, H.5    Dall'Acqua, W.F.6
  • 35
    • 39149106011 scopus 로고    scopus 로고
    • Structural characterization of a mutated, ADCC-enhanced human Fc fragment
    • Oganesyan, V.; Damschroder, M.M.; Leach, W.; Wu, H.; Dall'Acqua, W.F. Structural characterization of a mutated, ADCC-enhanced human Fc fragment. Mol. Immunol. 2008, 45, 1872-1882.
    • (2008) Mol. Immunol , vol.45 , pp. 1872-1882
    • Oganesyan, V.1    Damschroder, M.M.2    Leach, W.3    Wu, H.4    Dall'Acqua, W.F.5
  • 36
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W.L.; Ultsch, M.H.; de Vos, A.M.; Wells, J.A. Convergent solutions to binding at a protein-protein interface. Science 2000, 287, 1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 38
    • 84864336665 scopus 로고    scopus 로고
    • Department of Natural Sciences, Bowie State University, Bowie, MD, USA., Unpublished Work
    • Branden, B.C. Department of Natural Sciences, Bowie State University, Bowie, MD, USA. Unpublished Work, 2009.
    • (2009)
    • Branden, B.C.1
  • 41
    • 59449104345 scopus 로고    scopus 로고
    • New insights into intra- and intermolecular interactions of immunoglobulins: Crystal structure of mouse IgG2b-Fc at 2.1-Å resolution
    • Kolenko, P.; Dohnálek, J.; Dušková, J.; Skálová, T.; Collard, R.; Hašek, J. New insights into intra- and intermolecular interactions of immunoglobulins: Crystal structure of mouse IgG2b-Fc at 2.1-Å resolution. Immunology 2009, 126, 378-385.
    • (2009) Immunology , vol.126 , pp. 378-385
    • Kolenko, P.1    Dohnálek, J.2    Dušková, J.3    Skálová, T.4    Collard, R.5    Hašek, J.6
  • 44
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcγ receptor in complex with Fc
    • Radaev, S.; Motyka, S.; Fridman, W.H.; Sautes-Fridman, C.; Sun, P.D. The structure of a human type III Fcγ receptor in complex with Fc. J. Biol. Chem. 2001, 276, 16469-16477.
    • (2001) J. Biol. Chem , vol.276 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 45
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex
    • Sondermann, P.; Huber, R.; Oosthuizen, V.; Jacob, U. The 3.2-Å crystal structure of the human IgG1 Fc fragment-FcγRIII complex. Nature 2000, 406, 267-273.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 48
    • 58849162321 scopus 로고    scopus 로고
    • Analysis and validation of carbohydrate three-dimensional structures
    • Lütteke, 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
    • Lütteke, T.1
  • 49
    • 0031028909 scopus 로고    scopus 로고
    • Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides
    • Wormald, M.R.; Rudd, P.M.; Harvey, D.J.; Chang, S.C.; Scragg, I.G.; Dwek, R.A. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 1997, 36, 1370-1380.
    • (1997) Biochemistry , vol.36 , pp. 1370-1380
    • Wormald, M.R.1    Rudd, P.M.2    Harvey, D.J.3    Chang, S.C.4    Scragg, I.G.5    Dwek, R.A.6
  • 50
    • 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 13C 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 13C 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
  • 51
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • Barb, A.W.; Prestegard, J.H. NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. Nat. Chem. Biol. 2011, 7, 147-153.
    • (2011) Nat. Chem. Biol , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 54
    • 33646105366 scopus 로고    scopus 로고
    • Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy
    • Yamaguchi, Y.; Nishimura, M.; Nagano, M.; Yagi, H.; Sasakawa, H.; Uchida, K.; Shitara, K.; Kato, K. Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy. Biochim. Biophys. Acta 2006, 1760, 693-700.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 693-700
    • Yamaguchi, Y.1    Nishimura, M.2    Nagano, M.3    Yagi, H.4    Sasakawa, H.5    Uchida, K.6    Shitara, K.7    Kato, K.8
  • 55
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types
    • Kanda, Y.; Yamada, T.; Mori, K.; Okazaki, A.; Inoue, M.; Kitajima-Miyama, K.; Kuni-Kamochi, R.; Nakano, R.; Yano, K.; Kakita, S.; et al. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types. Glycobiology 2007, 17, 104-118.
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10
  • 56
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E.; Henrick, K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr 2004, 60, 2256-2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 57
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister, W.P.; Huber, A.H.; Bjorkman, P.J. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 1994, 372, 379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 58
    • 0033613146 scopus 로고    scopus 로고
    • Characterization of the 2:1 complex between the class I MHC-related Fc receptor and its Fc ligand in solution
    • Martin, W.L.; Bjorkman, P.J. Characterization of the 2:1 complex between the class I MHC-related Fc receptor and its Fc ligand in solution. Biochemistry 1999, 38, 12639-12647.
    • (1999) Biochemistry , vol.38 , pp. 12639-12647
    • Martin, W.L.1    Bjorkman, P.J.2
  • 59
    • 0039643451 scopus 로고    scopus 로고
    • Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand
    • Sánchez, L.M.; Penny, D.M.; Bjorkman, P.J. Stoichiometry of the interaction between the major histocompatibility complex-related Fc receptor and its Fc ligand. Biochemistry 1999, 38, 9471-9476.
    • (1999) Biochemistry , vol.38 , pp. 9471-9476
    • Sánchez, L.M.1    Penny, D.M.2    Bjorkman, P.J.3
  • 60
    • 0034076307 scopus 로고    scopus 로고
    • Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets
    • Clynes, R.A.; Towers, T.L.; Presta, L.G.; Ravetch, J.V. Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets. Nat. Med. 2000, 6, 443-446.
    • (2000) Nat. Med , vol.6 , pp. 443-446
    • Clynes, R.A.1    Towers, T.L.2    Presta, L.G.3    Ravetch, J.V.4
  • 61
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene
    • Cartron, G.; Dacheux, L.; Salles, G.; Solal-Celigny, P.; Bardos, P.; Colombat, P.; Watier, H. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene. Blood 2002, 99, 754-758.
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6    Watier, H.7
  • 62
    • 0028813628 scopus 로고
    • Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding
    • Liu, C.; Eichelberger, M.C.; Compans, R.W.; Air, G.M. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 1995, 69, 1099-1106.
    • (1995) J. Virol , vol.69 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 63
    • 0019119577 scopus 로고
    • A revision of the system of nomenclature for influenza viruses: A WHO memorandum
    • A revision of the system of nomenclature for influenza viruses: A WHO memorandum. Bull. World Health Organ. 1980, 58, 585-591.
    • (1980) Bull. World Health Organ , vol.58 , pp. 585-591
  • 65
    • 0020059828 scopus 로고
    • Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane
    • Blok, J.; Air, G.M.; Laver, W.G.; Ward, C.W.; Lilley, G.G.; Woods, E.F.; Roxburgh, C.M.; Inglis, A.S. Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane. Virology 1982, 119, 109-121.
    • (1982) Virology , vol.119 , pp. 109-121
    • Blok, J.1    Air, G.M.2    Laver, W.G.3    Ward, C.W.4    Lilley, G.G.5    Woods, E.F.6    Roxburgh, C.M.7    Inglis, A.S.8
  • 66
    • 0024827395 scopus 로고
    • The neuraminidase of influenza virus
    • Air, G.M.; Laver, W.G. The neuraminidase of influenza virus. Proteins 1989, 6, 341-356.
    • (1989) Proteins , vol.6 , pp. 341-356
    • Air, G.M.1    Laver, W.G.2
  • 67
    • 0022643192 scopus 로고
    • Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy
    • Murti, K.G.; Webster, R.G. Distribution of hemagglutinin and neuraminidase on influenza virions as revealed by immunoelectron microscopy. Virology 1986, 149, 36-43.
    • (1986) Virology , vol.149 , pp. 36-43
    • Murti, K.G.1    Webster, R.G.2
  • 69
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim, C.U.; Lew, W.; Williams, M.A.; Liu, H.; Zhang, L.; Swaminathan, S.; Bischofberger, N.; Chen, M.S.; Mendel, D.B.; Tai, C.Y.; et al. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc. 1997, 119, 681-690.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.4    Zhang, L.5    Swaminathan, S.6    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10
  • 70
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese, J.N.; Laver, W.G.; Colman, P.M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 1983, 303, 35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 71
    • 0023475950 scopus 로고
    • Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus
    • Baker, A.T.; Varghese, J.N.; Laver, W.G.; Air, G.M.; Colman, P.M. Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins 1987, 2, 111-117.
    • (1987) Proteins , vol.2 , pp. 111-117
    • Baker, A.T.1    Varghese, J.N.2    Laver, W.G.3    Air, G.M.4    Colman, P.M.5
  • 72
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B.; Richards, F.M. The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol. 1971, 55, 379-400.
    • (1971) J. Mol. Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 73
    • 0026508847 scopus 로고
    • The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid
    • Burmeister, W.P.; Ruigrok, R.W.; Cusack, S. The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J. 1992, 11, 49-56.
    • (1992) EMBO J , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 74
    • 0025895628 scopus 로고
    • Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution
    • Varghese, J.N.; Colman, P.M. Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution. J. Mol. Biol. 1991, 221, 473-486.
    • (1991) J. Mol. Biol , vol.221 , pp. 473-486
    • Varghese, J.N.1    Colman, P.M.2
  • 75
    • 0028925854 scopus 로고
    • A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies
    • White, C.L.; Janakiraman, M.N.; Laver, W.G.; Philippon, C.; Vasella, A.; Air, G.M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995, 245, 623-634.
    • (1995) J. Mol. Biol , vol.245 , pp. 623-634
    • White, C.L.1    Janakiraman, M.N.2    Laver, W.G.3    Philippon, C.4    Vasella, A.5    Air, G.M.6    Luo, M.7
  • 76
    • 84864352730 scopus 로고    scopus 로고
    • Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK. Unpublished Work
    • Rudino-Pinera, E.; Tunnah, P.; Crennell, S.J.; Webster, R.G.; Laver, W.G.; Garman, E.F. Department of Biochemistry, University of Oxford, South Parks Road, Oxford, UK. Unpublished Work, 2006.
    • (2006)
    • Rudino-Pinera, E.1    Tunnah, P.2    Crennell, S.J.3    Webster, R.G.4    Laver, W.G.5    Garman, E.F.6
  • 78
    • 0032546756 scopus 로고    scopus 로고
    • Three-dimensional structures of single-chain Fv-neuraminidase complexes
    • Malby, R.L.; McCoy, A.J.; Kortt, A.A.; Hudson, P.J.; Colman, P.M. Three-dimensional structures of single-chain Fv-neuraminidase complexes. J. Mol. Biol. 1998, 279, 901-910.
    • (1998) J. Mol. Biol , vol.279 , pp. 901-910
    • Malby, R.L.1    McCoy, A.J.2    Kortt, A.A.3    Hudson, P.J.4    Colman, P.M.5
  • 81
    • 67650287954 scopus 로고    scopus 로고
    • The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin
    • Ryu, K.S.; Lee, J.O.; Kwon, T.H.; Choi, H.H.; Park, H.S.; Hwang, S.K.; Lee, Z.W.; Lee, K.B.; Han, Y.H.; Choi, Y.S.; et al. The presence of monoglucosylated N196-glycan is important for the structural stability of storage protein, arylphorin. Biochem. J. 2009, 421, 87-96.
    • (2009) Biochem. J , vol.421 , pp. 87-96
    • Ryu, K.S.1    Lee, J.O.2    Kwon, T.H.3    Choi, H.H.4    Park, H.S.5    Hwang, S.K.6    Lee, Z.W.7    Lee, K.B.8    Han, Y.H.9    Choi, Y.S.10
  • 82
    • 0030056713 scopus 로고    scopus 로고
    • Common origin of arthropod tyrosinase, arthropod hemocyanin, insect hexamerin, and dipteran arylphorin receptor
    • Burmester, T.; Scheller, K. Common origin of arthropod tyrosinase, arthropod hemocyanin, insect hexamerin, and dipteran arylphorin receptor. J. Mol. Evol. 1996, 42, 713-728.
    • (1996) J. Mol. Evol , vol.42 , pp. 713-728
    • Burmester, T.1    Scheller, K.2
  • 83
    • 0026054117 scopus 로고
    • The function and evolution of insect storage hexamers
    • Telfer, W.H.; Kunkel, J.G. The function and evolution of insect storage hexamers. Annu. Rev. Entomol. 1991, 36, 205-228.
    • (1991) Annu. Rev. Entomol , vol.36 , pp. 205-228
    • Telfer, W.H.1    Kunkel, J.G.2
  • 84
    • 17444429974 scopus 로고    scopus 로고
    • Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins
    • Jung, H.I.; Kim, Y.H.; Kim, S. Structural basis for the presence of a monoglucosylated oligosaccharide in mature glycoproteins. Biochem. Biophys. Res. Commun. 2005, 331, 100-106.
    • (2005) Biochem. Biophys. Res. Commun , vol.331 , pp. 100-106
    • Jung, H.I.1    Kim, Y.H.2    Kim, S.3
  • 87
    • 33947205049 scopus 로고    scopus 로고
    • Characterization of the bga1-encoded glycoside hydrolase family 35 β-galactosidase of Hypocrea jecorina with galacto-β-D-galactanase activity
    • Gamauf, C.; Marchetti, M.; Kallio, J.; Puranen, T.; Vehmaanperä, J.; Allmaier, G.; Kubicek, C.P.; Seiboth, B. Characterization of the bga1-encoded glycoside hydrolase family 35 β-galactosidase of Hypocrea jecorina with galacto-β-D-galactanase activity. FEBS J. 2007, 274, 1691-1700.
    • (2007) FEBS J , vol.274 , pp. 1691-1700
    • Gamauf, C.1    Marchetti, M.2    Kallio, J.3    Puranen, T.4    Vehmaanperä, J.5    Allmaier, G.6    Kubicek, C.P.7    Seiboth, B.8
  • 88
    • 79952445041 scopus 로고    scopus 로고
    • Crystal structures of Trichoderma reesei β-galactosidase reveal conformational changes in the active site
    • Maksimainen, M.; Hakulinen, N.; Kallio, J.M.; Timoharju, T.; Turunen, O.; Rouvinen, J. Crystal structures of Trichoderma reesei β-galactosidase reveal conformational changes in the active site. J. Struct. Biol. 2011, 174, 156-163.
    • (2011) J. Struct. Biol , vol.174 , pp. 156-163
    • Maksimainen, M.1    Hakulinen, N.2    Kallio, J.M.3    Timoharju, T.4    Turunen, O.5    Rouvinen, J.6
  • 90
    • 0036677372 scopus 로고    scopus 로고
    • Glycosylation defining cancer malignancy: New wine in an old bottle
    • Hakomori, S. Glycosylation defining cancer malignancy: New wine in an old bottle. Proc. Natl. Acad. Sci. USA 2002, 99, 10231-10233.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10231-10233
    • Hakomori, S.1
  • 93
    • 0346157290 scopus 로고    scopus 로고
    • Innate immunity: An overview
    • Beutler, B. Innate immunity: An overview. Mol. Immunol. 2004, 40, 845-859.
    • (2004) Mol. Immunol , vol.40 , pp. 845-859
    • Beutler, B.1
  • 94
    • 12444341944 scopus 로고    scopus 로고
    • Toll-like receptors in innate immunity
    • Takeda, K.; Akira, S. Toll-like receptors in innate immunity. Int. Immunol. 2005, 17, 1-14.
    • (2005) Int. Immunol , vol.17 , pp. 1-14
    • Takeda, K.1    Akira, S.2
  • 95
    • 23044445303 scopus 로고    scopus 로고
    • Crystal structure of human Toll-like receptor 3 (TLR3) ectodomain
    • Choe, J.; Kelker, M.S.; Wilson, I.A. Crystal structure of human Toll-like receptor 3 (TLR3) ectodomain. Science 2005, 309, 581-585.
    • (2005) Science , vol.309 , pp. 581-585
    • Choe, J.1    Kelker, M.S.2    Wilson, I.A.3
  • 96
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • Liu, L.; Botos, I.; Wang, Y.; Leonard, J.N.; Shiloach, J.; Segal, D.M.; Davies, D.R. Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science 2008, 320, 379-381.
    • (2008) Science , vol.320 , pp. 379-381
    • Liu, L.1    Botos, I.2    Wang, Y.3    Leonard, J.N.4    Shiloach, J.5    Segal, D.M.6    Davies, D.R.7
  • 98
    • 0028774038 scopus 로고
    • Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution
    • Bodian, D.L.; Jones, E.Y.; Harlos, K.; Stuart, D.I.; Davis, S.J. Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 Å resolution. Structure 1994, 2, 755-766.
    • (1994) Structure , vol.2 , pp. 755-766
    • Bodian, D.L.1    Jones, E.Y.2    Harlos, K.3    Stuart, D.I.4    Davis, S.J.5
  • 100
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R.O. Integrins: Bidirectional, allosteric signaling machines. Cell 2002, 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 101
    • 84860273145 scopus 로고    scopus 로고
    • Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor
    • Nagae, M.; Re, S.; Mihara, E.; Nogi, T.; Sugita, Y.; Takagi, J. Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor. J. Cell. Biol. 2012, 197, 131-140.
    • (2012) J. Cell. Biol , vol.197 , pp. 131-140
    • Nagae, M.1    Re, S.2    Mihara, E.3    Nogi, T.4    Sugita, Y.5    Takagi, J.6
  • 102
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D.J.; Aukhil, I.; Erickson, H.P. 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996, 84, 155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 103
    • 84893482610 scopus 로고
    • Solution for Best Rotation to Relate 2 Sets of Vectors
    • Kabsch, W. Solution for Best Rotation to Relate 2 Sets of Vectors. Acta Crystallogr. Sect. A 1976, 32, 922-923.
    • (1976) Acta Crystallogr. Sect. A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 104
    • 0030916713 scopus 로고    scopus 로고
    • Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface
    • Casasnovas, J.M.; Springer, T.A.; Liu, J.H.; Harrison, S.C.; Wang, J.H. Crystal structure of ICAM-2 reveals a distinctive integrin recognition surface. Nature 1997, 387, 312-315.
    • (1997) Nature , vol.387 , pp. 312-315
    • Casasnovas, J.M.1    Springer, T.A.2    Liu, J.H.3    Harrison, S.C.4    Wang, J.H.5
  • 105
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: Glycan presentation and protein-fold stability
    • Wormald, M.R.; Dwek, R.A. Glycoproteins: Glycan presentation and protein-fold stability. Structure 1999, 7, R155-160.
    • (1999) Structure , vol.7
    • Wormald, M.R.1    Dwek, R.A.2
  • 106
    • 0026624745 scopus 로고
    • Effects of glycosylation on protein conformation and amide proton exchange rates in RNase B
    • Joao, H.C.; Scragg, I.G.; Dwek, R.A. Effects of glycosylation on protein conformation and amide proton exchange rates in RNase B. FEBS Lett. 1992, 307, 343-346.
    • (1992) FEBS Lett , vol.307 , pp. 343-346
    • Joao, H.C.1    Scragg, I.G.2    Dwek, R.A.3
  • 108
    • 33846204799 scopus 로고    scopus 로고
    • A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins
    • Mikami, S.; Kobayashi, T.; Yokoyama, S.; Imataka, H. A hybridoma-based in vitro translation system that efficiently synthesizes glycoproteins. J. Biotechnol. 2006, 127, 65-78.
    • (2006) J. Biotechnol , vol.127 , pp. 65-78
    • Mikami, S.1    Kobayashi, T.2    Yokoyama, S.3    Imataka, H.4
  • 109
    • 84856241064 scopus 로고    scopus 로고
    • Glycosylation of skeletal calsequestrin: Implications for its function
    • Sanchez, E.J.; Lewis, K.M.; Munske, G.R.; Nissen, M.S.; Kang, C. Glycosylation of skeletal calsequestrin: Implications for its function. J. Biol. Chem. 2012, 287, 3042-3050.
    • (2012) J. Biol. Chem , vol.287 , pp. 3042-3050
    • Sanchez, E.J.1    Lewis, K.M.2    Munske, G.R.3    Nissen, M.S.4    Kang, C.5
  • 110
    • 83055166012 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor
    • Zou, G.; Ochiai, H.; Huang, W.; Yang, Q.; Li, C.; Wang, L.X. Chemoenzymatic synthesis and Fcγ receptor binding of homogeneous glycoforms of antibody Fc domain. Presence of a bisecting sugar moiety enhances the affinity of Fc to FcγIIIa receptor. J. Am. Chem. Soc. 2011, 133, 18975-18991.
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 18975-18991
    • Zou, G.1    Ochiai, H.2    Huang, W.3    Yang, Q.4    Li, C.5    Wang, L.X.6
  • 111
    • 84859524073 scopus 로고    scopus 로고
    • Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide
    • Murakami, M.; Okamoto, R.; Izumi, M.; Kajihara, Y. Chemical synthesis of an erythropoietin glycoform containing a complex-type disialyloligosaccharide. Angew. Chem. Int. Ed. Engl. 2012, 51, 3567-3572.
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 3567-3572
    • Murakami, M.1    Okamoto, R.2    Izumi, M.3    Kajihara, Y.4
  • 112
    • 84857383999 scopus 로고    scopus 로고
    • Total synthesis of the α-subunit of human glycoprotein hormones: Toward fully synthetic homogeneous human follicle-stimulating hormone
    • Aussedat, B.; Fasching, B.; Johnston, E.; Sane, N.; Nagorny, P.; Danishefsky, S.J. Total synthesis of the α-subunit of human glycoprotein hormones: Toward fully synthetic homogeneous human follicle-stimulating hormone. J. Am. Chem. Soc. 2012, 134, 3532-3541.
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 3532-3541
    • Aussedat, B.1    Fasching, B.2    Johnston, E.3    Sane, N.4    Nagorny, P.5    Danishefsky, S.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.