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Volumn 24, Issue 1, 2010, Pages 9-21

Glycosylation of therapeutic proteins: An effective strategy to optimize efficacy

Author keywords

[No Author keywords available]

Indexed keywords

AGALSIDASE ALFA; AGALSIDASE BETA; ALGLUCERASE; ALPHA 1 ANTITRYPSIN; ALPHAN3 INTERFERON; ALTEPLASE; BETA1A INTERFERON; COMPLEMENT COMPONENT C1S INHIBITOR; DORNASE ALFA; DROTRECOGIN; FOLLISTIM AQ; GALSULFASE; HAEMOCOMPLETTAN; HYALURONIDASE; HYLENEX; IDURONATE 2 SULFATASE; IMIGLUCERASE; LARONIDASE; NOVEL ERYTHROPOIESIS STIMULATING PROTEIN; PLASMINOGEN ACTIVATOR; PROTEIN; RECOMBINANT ANTITHROMBIN III; RECOMBINANT BLOOD CLOTTING FACTOR 7A; RECOMBINANT BLOOD CLOTTING FACTOR 9; RECOMBINANT CHORIONIC GONADOTROPIN; RECOMBINANT FOLLITROPIN; RECOMBINANT GLUCAN 1,4 ALPHA GLUCOSIDASE; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; RECOMBINANT GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; RECOMBINANT LUTEINIZING HORMONE; RECOMBINANT THYROTROPIN; TENECTEPLASE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 75149183678     PISSN: 11738804     EISSN: 1179190X     Source Type: Journal    
DOI: 10.2165/11530550-000000000-00000     Document Type: Review
Times cited : (384)

References (234)
  • 1
    • 0036535753 scopus 로고    scopus 로고
    • Recombinant protein expression for therapeutic applications
    • Andersen DC, Krummen L. Recombinant protein expression for therapeutic applications. Curr Opin Biotechnol 2002; 13 (2): 117-123
    • (2002) Curr Opin Biotechnol , vol.13 , Issue.2 , pp. 117-123
    • Andersen, D.C.1    Krummen, L.2
  • 3
    • 34347395337 scopus 로고    scopus 로고
    • Formulation development for hydrophobic therapeutic proteins
    • Hawe A, Friess W. Formulation development for hydrophobic therapeutic proteins. Pharm Dev Technol 2007; 12 (3): 223-237
    • (2007) Pharm Dev Technol , vol.12 , Issue.3 , pp. 223-237
    • Hawe, A.1    Friess, W.2
  • 4
    • 0032782071 scopus 로고    scopus 로고
    • Instability, stabilization, and formulation of liquid protein pharmaceuticals
    • Wang W. Instability, stabilization, and formulation of liquid protein pharmaceuticals. Int J Pharm 1999; 185 (2): 129-188
    • (1999) Int J Pharm , vol.185 , Issue.2 , pp. 129-188
    • Wang, W.1
  • 5
    • 18244365849 scopus 로고    scopus 로고
    • Protein drug stability: A formulation challenge
    • Frokjaer S, Otzen DE. Protein drug stability: a formulation challenge. Nature Rev Drug Discov 2005; 4 (4): 298-306
    • (2005) Nature Rev Drug Discov , vol.4 , Issue.4 , pp. 298-306
    • Frokjaer, S.1    Otzen, D.E.2
  • 6
    • 0024806396 scopus 로고
    • Stability of protein pharmaceuticals
    • Manning MC, Patel K, Borchardt RT. Stability of protein pharmaceuticals. Pharm Res 1989; 6 (11): 903-918
    • (1989) Pharm Res , vol.6 , Issue.11 , pp. 903-918
    • Manning, M.C.1    Patel, K.2    Borchardt, R.T.3
  • 7
    • 0027525683 scopus 로고
    • Protein stability: Impact upon protein pharmaceuticals [letter]
    • Davis GC. Protein stability: impact upon protein pharmaceuticals [letter]. Biologicals 1993; 21 (2): 105
    • (1993) Biologicals , vol.21 , Issue.2 , pp. 105
    • Davis, G.C.1
  • 8
    • 0036890693 scopus 로고    scopus 로고
    • The stability factor: Importance in formulation development
    • Krishnamurthy R, Manning MC. The stability factor: importance in formulation development. Curr Pharm Biotechnol 2002; 3 (4): 361-371
    • (2002) Curr Pharm Biotechnol , vol.3 , Issue.4 , pp. 361-371
    • Krishnamurthy, R.1    Manning, M.C.2
  • 9
    • 0035287319 scopus 로고    scopus 로고
    • Factors affecting short-term and long-termstabilities of proteins
    • Arakawa T, Prestrelski SJ, Kenney WC, et al. Factors affecting short-term and long-termstabilities of proteins.AdvDrugDelivRev 2001; 46 (1-3): 307-326
    • (2001) Adv Drug Deliv Rev , vol.46 , Issue.1-3 , pp. 307-326
    • Arakawa, T.1    Prestrelski, S.J.2    Kenney, W.C.3
  • 10
    • 0033962569 scopus 로고    scopus 로고
    • Biopharmaceutical formulation
    • Lee JC. Biopharmaceutical formulation. Curr Opin Biotechnol 2000; 11 (1): 81-84
    • (2000) Curr Opin Biotechnol , vol.11 , Issue.1 , pp. 81-84
    • Lee, J.C.1
  • 11
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W. Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 2005; 289 (1-2): 1-30
    • (2005) Int J Pharm , vol.289 , Issue.1-2 , pp. 1-30
    • Wang, W.1
  • 13
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Solá RJ, Griebenow K. Effects of glycosylation on the stability of protein pharmaceuticals. J Pharm Sci 2009; 98 (4): 1223-1245
    • (2009) J Pharm Sci , vol.98 , Issue.4 , pp. 1223-1245
    • Solá, R.J.1    Griebenow, K.2
  • 14
    • 12344281758 scopus 로고    scopus 로고
    • Commercial challenges of protein drug delivery
    • Brown LR. Commercial challenges of protein drug delivery. Expert Opin Drug Deliv 2005; 2 (1): 29-42
    • (2005) Expert Opin Drug Deliv , vol.2 , Issue.1 , pp. 29-42
    • Brown, L.R.1
  • 15
    • 18644361997 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic considerations in the development of therapeutic proteins
    • Mahmood I, Green MD. Pharmacokinetic and pharmacodynamic considerations in the development of therapeutic proteins. Clin Pharmacokinet 2005; 44 (4): 331-347
    • (2005) Clin Pharmacokinet , vol.44 , Issue.4 , pp. 331-347
    • Mahmood, I.1    Green, M.D.2
  • 16
    • 4344634877 scopus 로고    scopus 로고
    • Pharmacokinetic aspects of biotechnology products
    • Tang L, Persky AM, Hochhaus G, et al. Pharmacokinetic aspects of biotechnology products. J Pharm Sci 2004; 93 (9): 2184-2204
    • (2004) J Pharm Sci , vol.93 , Issue.9 , pp. 2184-2204
    • Tang, L.1    Persky, A.M.2    Hochhaus, G.3
  • 17
  • 18
    • 0037338175 scopus 로고    scopus 로고
    • Rational design and engineering of therapeutic proteins
    • Marshall SA, Lazar GA, Chirino AJ, et al. Rational design and engineering of therapeutic proteins. Drug Discov Today 2003; 8 (5): 212-221
    • (2003) Drug Discov Today , vol.8 , Issue.5 , pp. 212-221
    • Marshall, S.A.1    Lazar, G.A.2    Chirino, A.J.3
  • 19
    • 0042430531 scopus 로고    scopus 로고
    • Designing proteins for therapeutic applications
    • Lazar GA, Marshall SA, Plecs JJ, et al. Designing proteins for therapeutic applications. Curr Opin Struct Biol 2003; 13 (4): 513-518
    • (2003) Curr Opin Struct Biol , vol.13 , Issue.4 , pp. 513-518
    • Lazar, G.A.1    Marshall, S.A.2    Plecs, J.J.3
  • 20
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 2005; 21 (1): 11-16
    • (2005) Biotechnol Prog , vol.21 , Issue.1 , pp. 11-16
    • Jefferis, R.1
  • 21
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov 2009; 8 (3): 226-234
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.3 , pp. 226-234
    • Jefferis, R.1
  • 22
    • 60549114878 scopus 로고    scopus 로고
    • Glycosylation of antibody therapeutics: Optimization for purpose
    • Jefferis R. Glycosylation of antibody therapeutics: optimization for purpose. Methods Mol Biol 2009; 483: 223-238
    • (2009) Methods Mol Biol , vol.483 , pp. 223-238
    • Jefferis, R.1
  • 23
    • 33947545682 scopus 로고    scopus 로고
    • Sialic acids: Carbohydrate moieties that influence the biological and physical properties of biopharmaceutical proteins and living cells
    • Byrne B, Donohoe GG, O'Kennedy R. Sialic acids: carbohydrate moieties that influence the biological and physical properties of biopharmaceutical proteins and living cells. Drug Discov Today 2007; 12 (7-8): 319
    • (2007) Drug Discov Today , vol.12 , Issue.7-8 , pp. 319
    • Byrne, B.1    Donohoe, G.G.2    O'Kennedy, R.3
  • 24
    • 25444435396 scopus 로고    scopus 로고
    • Glycoengineering: The effect of glycosylation on the properties of therapeutic proteins
    • Sinclair AM, Elliott S. Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J Pharm Sci 2005; 94 (8): 1626-1635
    • (2005) J Pharm Sci , vol.94 , Issue.8 , pp. 1626-1635
    • Sinclair, A.M.1    Elliott, S.2
  • 25
    • 12244272391 scopus 로고    scopus 로고
    • Enhancement of therapeutic protein in vivo activities through glycoengineering
    • Elliott S, Lorenzini T, Asher S, et al. Enhancement of therapeutic protein in vivo activities through glycoengineering. Nat Biotechnol 2003; 21 (4): 414-421
    • (2003) Nat Biotechnol , vol.21 , Issue.4 , pp. 414-421
    • Elliott, S.1    Lorenzini, T.2    Asher, S.3
  • 26
    • 39149098790 scopus 로고    scopus 로고
    • Novel long-lasting interferon alpha derivatives designed by glycoengineering
    • Ceaglio N, Etcheverrigaray M, Kratje R, et al. Novel long-lasting interferon alpha derivatives designed by glycoengineering. Biochimie 2008; 90 (3): 437-449
    • (2008) Biochimie , vol.90 , Issue.3 , pp. 437-449
    • Ceaglio, N.1    Etcheverrigaray, M.2    Kratje, R.3
  • 27
    • 0142248500 scopus 로고    scopus 로고
    • Sugar coating extends half-lives and improves effectiveness of cytokine hormones
    • Koury MJ. Sugar coating extends half-lives and improves effectiveness of cytokine hormones. Trends Biotechnol 2003; 21 (11): 462-464
    • (2003) Trends Biotechnol , vol.21 , Issue.11 , pp. 462-464
    • Koury, M.J.1
  • 28
    • 0035979377 scopus 로고    scopus 로고
    • Glycoengineering of therapeutic glycoproteins: In vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues
    • Raju TS, Briggs JB, Chamow SM, et al. Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues. Biochemistry 2001; 40 (30): 8868-8876
    • (2001) Biochemistry , vol.40 , Issue.30 , pp. 8868-8876
    • Raju, T.S.1    Briggs, J.B.2    Chamow, S.M.3
  • 29
    • 60849113728 scopus 로고    scopus 로고
    • Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and Fc-fusion proteins
    • Beck A, Wagner-Rousset E, Bussat MC, et al. Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and Fc-fusion proteins. Curr Pharm Biotechnol 2008; 9 (6): 482-501
    • (2008) Curr Pharm Biotechnol , vol.9 , Issue.6 , pp. 482-501
    • Beck, A.1    Wagner-Rousset, E.2    Bussat, M.C.3
  • 30
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W. Lyophilization and development of solid protein pharmaceuticals. Int J Pharm 2000; 203 (1-2): 1-60
    • (2000) Int J Pharm , vol.203 , Issue.1-2 , pp. 1-60
    • Wang, W.1
  • 31
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • Wang W, Singh S, Zeng DL, et al. Antibody structure, instability, and formulation. J Pharm Sci 2007; 96 (1): 1-26
    • (2007) J Pharm Sci , vol.96 , Issue.1 , pp. 1-26
    • Wang, W.1    Singh, S.2    Zeng, D.L.3
  • 32
    • 0031241608 scopus 로고    scopus 로고
    • Degradative covalent reactions important to protein stability
    • Volkin DB, Mach H, Middaugh CR. Degradative covalent reactions important to protein stability. Mol Biotechnol 1997; 8 (2): 105-122
    • (1997) Mol Biotechnol , vol.8 , Issue.2 , pp. 105-122
    • Volkin, D.B.1    MacH, H.2    Middaugh, C.R.3
  • 33
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace CN. Conformational stability of globular proteins. Trends Biochem Sci 1990; 15 (1): 14-17
    • (1990) Trends Biochem Sci , vol.15 , Issue.1 , pp. 14-17
    • Pace, C.N.1
  • 34
    • 0032904703 scopus 로고    scopus 로고
    • Secondary structure and protein deamidation
    • XieM, Schowen RL. Secondary structure and protein deamidation. J Pharm Sci 1999; 88 (1): 8-13
    • (1999) J Pharm Sci , vol.88 , Issue.1 , pp. 8-13
    • Xie, M.1    Schowen, R.L.2
  • 35
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • Pace CN. Measuring and increasing protein stability. Trends Biotechnol 1990; 8 (4): 93-98
    • (1990) Trends Biotechnol , vol.8 , Issue.4 , pp. 93-98
    • Pace, C.N.1
  • 36
    • 31344474356 scopus 로고    scopus 로고
    • Colloidal behavior of proteins: Effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution
    • Valente JJ, Payne RW, Manning MC, et al. Colloidal behavior of proteins: effects of the second virial coefficient on solubility, crystallization and aggregation of proteins in aqueous solution. Curr Pharm Biotechnol 2005; 6 (6): 427-436
    • (2005) Curr Pharm Biotechnol , vol.6 , Issue.6 , pp. 427-436
    • Valente, J.J.1    Payne, R.W.2    Manning, M.C.3
  • 37
    • 0242515822 scopus 로고    scopus 로고
    • Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor
    • Chi EY, Krishnan S, Kendrick BS, et al. Roles of conformational stability and colloidal stability in the aggregation of recombinant human granulocyte colony-stimulating factor. Protein Sci 2003; 12 (5): 903-913
    • (2003) Protein Sci , vol.12 , Issue.5 , pp. 903-913
    • Chi, E.Y.1    Krishnan, S.2    Kendrick, B.S.3
  • 38
    • 48549086114 scopus 로고    scopus 로고
    • Effects of solution conditions, processing parameters, and container materials on aggregation of a monoclonal antibody during freeze-thawing
    • Kueltzo LA, Wang W, Randolph TW, et al. Effects of solution conditions, processing parameters, and container materials on aggregation of a monoclonal antibody during freeze-thawing. J Pharm Sci 2008; 97 (5): 1801-1812
    • (2008) J Pharm Sci , vol.97 , Issue.5 , pp. 1801-1812
    • Kueltzo, L.A.1    Wang, W.2    Randolph, T.W.3
  • 39
    • 33749057744 scopus 로고    scopus 로고
    • Protein aggregation and bioprocessing
    • Cromwell ME, Hilario E, Jacobson F. Protein aggregation and bioprocessing. AAPS J 2006; 8 (3): E572-9
    • (2006) AAPS J , vol.8 , Issue.3
    • Cromwell, M.E.1    Hilario, E.2    Jacobson, F.3
  • 40
    • 36749040335 scopus 로고    scopus 로고
    • Non-native protein aggregation kinetics
    • Roberts CJ. Non-native protein aggregation kinetics. Biotechnol Bioeng 2007; 98 (5): 927-938
    • (2007) Biotechnol Bioeng , vol.98 , Issue.5 , pp. 927-938
    • Roberts, C.J.1
  • 41
    • 0016222589 scopus 로고
    • The role of the kidney in the metabolism of plasma proteins
    • Strober W, Waldmann TA. The role of the kidney in the metabolism of plasma proteins. Nephron 1974; 13 (1): 35-66
    • (1974) Nephron , vol.13 , Issue.1 , pp. 35-66
    • Strober, W.1    Waldmann, T.A.2
  • 42
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly (ethylene glycol)-protein conjugates
    • Caliceti P, Veronese FM. Pharmacokinetic and biodistribution properties of poly (ethylene glycol)-protein conjugates. Adv Drug Deliv Rev 2003; 55 (10): 1261-1277
    • (2003) Adv Drug Deliv Rev , vol.55 , Issue.10 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.M.2
  • 43
    • 0030660505 scopus 로고    scopus 로고
    • Distribution of glycosaminoglycans in rat renal tubular epithelium
    • Weinstein T, Gafter U, Chagnac A, et al. Distribution of glycosaminoglycans in rat renal tubular epithelium. J Am Soc Nephrol 1997; 8 (4): 586-595
    • (1997) J Am Soc Nephrol , vol.8 , Issue.4 , pp. 586-595
    • Weinstein, T.1    Gafter, U.2    Chagnac, A.3
  • 44
    • 35148864458 scopus 로고    scopus 로고
    • Renal clearance of quantum dots
    • Choi HS, Liu W, Misra P, et al. Renal clearance of quantum dots. Nat Biotechnol 2007; 25 (10): 1165-1170
    • (2007) Nat Biotechnol , vol.25 , Issue.10 , pp. 1165-1170
    • Choi, H.S.1    Liu, W.2    Misra, P.3
  • 45
    • 0027658023 scopus 로고
    • Mechanism of receptor regulation during repeated administration of drugs
    • Montastruc JL, Galitzky J, Berlan M, et al. Mechanism of receptor regulation during repeated administration of drugs. Therapie 1993; 48 (5): 421-426
    • (1993) Therapie , vol.48 , Issue.5 , pp. 421-426
    • Montastruc, J.L.1    Galitzky, J.2    Berlan, M.3
  • 46
    • 0028032075 scopus 로고
    • From receptor internalization to nuclear translocation: New targets for long-term pharmacology
    • Laduron PM. From receptor internalization to nuclear translocation: new targets for long-term pharmacology. Biochem Pharmacol 1994; 47 (1): 3-13
    • (1994) Biochem Pharmacol , vol.47 , Issue.1 , pp. 3-13
    • Laduron, P.M.1
  • 47
    • 3843142857 scopus 로고    scopus 로고
    • Second-generation biopharmaceuticals
    • Walsh G. Second-generation biopharmaceuticals. Eur J Pharm Biopharm 2004; 58 (2): 185-196
    • (2004) Eur J Pharm Biopharm , vol.58 , Issue.2 , pp. 185-196
    • Walsh, G.1
  • 48
    • 0032848329 scopus 로고    scopus 로고
    • Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells
    • Grabenhorst E, Schlenke P, Pohl S, et al. Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells. Glycoconj J 1999; 16 (2): 81-97
    • (1999) Glycoconj J , vol.16 , Issue.2 , pp. 81-97
    • Grabenhorst, E.1    Schlenke, P.2    Pohl, S.3
  • 49
    • 35248882544 scopus 로고    scopus 로고
    • Modulation of protein biophysical properties by chemical glycosylation: Biochemical insights and biomedical implications
    • Solá RJ, Rodriguez-Martinez JA, Griebenow K. Modulation of protein biophysical properties by chemical glycosylation: biochemical insights and biomedical implications. Cell Mol Life Sci 2007; 64 (16): 2133-2152
    • (2007) Cell Mol Life Sci , vol.64 , Issue.16 , pp. 2133-2152
    • Solá, R.J.1    Rodriguez-Martinez, J.A.2    Griebenow, K.3
  • 50
    • 0026848764 scopus 로고
    • Glycoprotein pharmaceuticals: Scientific and regulatory considerations, and the US Orphan Drug Act
    • Liu DT. Glycoprotein pharmaceuticals: scientific and regulatory considerations, and the US Orphan Drug Act. Trends Biotechnol 1992; 10 (4): 114-120
    • (1992) Trends Biotechnol , vol.10 , Issue.4 , pp. 114-120
    • Liu, D.T.1
  • 51
    • 33646892873 scopus 로고    scopus 로고
    • Asparagine-linked protein glycosylation: From eukaryotic to prokaryotic systems
    • Weerapana E, Imperiali B. Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems. Glycobiology 2006; 16 (6): 91-101R
    • (2006) Glycobiology , vol.16 , Issue.6
    • Weerapana, E.1    Imperiali, B.2
  • 52
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M, Jensen ON. Proteomic analysis of post-translational modifications. Nature Biotechnol 2003; 21 (3): 255-261
    • (2003) Nature Biotechnol , vol.21 , Issue.3 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 53
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • Walsh CT, Garneau-Tsodikova S, Gatto GJ. Protein posttranslational modifications: the chemistry of proteome diversifications. Angewandte Chemie Int Ed 2005; 44 (45): 7342-7372
    • (2005) Angewandte Chemie Int Ed , vol.44 , Issue.45 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto, G.J.3
  • 54
    • 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 (1): 4-8
    • (1999) Biochim Biophys Acta , vol.1473 , Issue.1 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 55
    • 0031971883 scopus 로고    scopus 로고
    • Enzyme action in glycoprotein synthesis
    • Sears P, Wong CH. Enzyme action in glycoprotein synthesis. Cell Mol Life Sci 1998; 54 (3): 223-252
    • (1998) Cell Mol Life Sci , vol.54 , Issue.3 , pp. 223-252
    • Sears, P.1    Wong, C.H.2
  • 56
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: A model organism helps elucidate congenital human diseases
    • Lehle L, Strahl S, Tanner W. Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew Chem Int Ed Engl 2006; 45 (41): 6802-6818
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.41 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 57
    • 30544454698 scopus 로고    scopus 로고
    • Characterization of protein N-glycosylation
    • Medzihradszky KF. Characterization of protein N-glycosylation. Methods Enzymol 2005; 405: 116-138
    • (2005) Methods Enzymol , vol.405 , pp. 116-138
    • Medzihradszky, K.F.1
  • 58
    • 30544433136 scopus 로고    scopus 로고
    • Methods in enzymology: O-glycosylation of proteins
    • Peter-Katalinic J. Methods in enzymology: O-glycosylation of proteins. Methods Enzymol 2005; 405: 139-171
    • (2005) Methods Enzymol , vol.405 , pp. 139-171
    • Peter-Katalinic, J.1
  • 59
    • 40249093192 scopus 로고    scopus 로고
    • Systems analysis of N-glycan processing in mammalian cells
    • Hossler P, Mulukutla BC, Hu WS. Systems analysis of N-glycan processing in mammalian cells. PLoS One 2007; 2 (1): e713
    • (2007) PLoS One , vol.2 , Issue.1
    • Hossler, P.1    Mulukutla, B.C.2    Hu, W.S.3
  • 60
    • 33746750608 scopus 로고    scopus 로고
    • Challenges in therapeutic glycoprotein production
    • Sethuraman N, Stadheim TA. Challenges in therapeutic glycoprotein production. Curr Opin Biotechnol 2006; 17 (4): 341-346
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.4 , pp. 341-346
    • Sethuraman, N.1    Stadheim, T.A.2
  • 61
    • 4644341836 scopus 로고    scopus 로고
    • Tailor-made glycoproteins
    • Hsieh-Wilson LC. Tailor-made glycoproteins. Trends Biotechnol 2004; 22 (10): 489-491
    • (2004) Trends Biotechnol , vol.22 , Issue.10 , pp. 489-491
    • Hsieh-Wilson, L.C.1
  • 62
    • 62649171202 scopus 로고    scopus 로고
    • Emerging methods for the production of homogeneous human glycoproteins
    • Rich JR,Withers SG. Emerging methods for the production of homogeneous human glycoproteins. Nat Chem Biol 2009; 5 (4): 206-215
    • (2009) Nat Chem Biol , vol.5 , Issue.4 , pp. 206-215
    • Rich, J.R.1    Withers, S.G.2
  • 63
    • 40749160803 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation and its potential use in drug and vaccine development
    • Tarp MA, Clausen H. Mucin-type O-glycosylation and its potential use in drug and vaccine development. Biochim Biophys Acta 2008; 1780 (3): 546-563
    • (2008) Biochim Biophys Acta , vol.1780 , Issue.3 , pp. 546-563
    • Tarp, M.A.1    Clausen, H.2
  • 64
    • 33751422228 scopus 로고    scopus 로고
    • Strategies for the preparation of homogenous glycoproteins
    • Brik A, Ficht S, Wong CH. Strategies for the preparation of homogenous glycoproteins. Curr Opin Chem Biol 2006; 10 (6): 638-644
    • (2006) Curr Opin Chem Biol , vol.10 , Issue.6 , pp. 638-644
    • Brik, A.1    Ficht, S.2    Wong, C.H.3
  • 65
    • 0035997381 scopus 로고    scopus 로고
    • Homogeneous glycopeptides and glycoproteins for biological investigation
    • Grogan MJ, Pratt MR, Marcaurelle LA, et al. Homogeneous glycopeptides and glycoproteins for biological investigation. Annu Rev Biochem 2002; 71: 593-634
    • (2002) Annu Rev Biochem , vol.71 , pp. 593-634
    • Grogan, M.J.1    Pratt, M.R.2    Marcaurelle, L.A.3
  • 66
    • 59649120676 scopus 로고    scopus 로고
    • Glycoprotein synthesis: An update
    • Gamblin DP, Scanlan EM, Davis BG. Glycoprotein synthesis: an update. Chem Rev 2009; 109 (1): 131-163
    • (2009) Chem Rev , vol.109 , Issue.1 , pp. 131-163
    • Gamblin, D.P.1    Scanlan, E.M.2    Davis, B.G.3
  • 67
    • 39149101471 scopus 로고    scopus 로고
    • Site-selective glycosylation of proteins: Creating synthetic glycoproteins
    • van Kasteren SI, Kramer HB, Gamblin DP, et al. Site-selective glycosylation of proteins: creating synthetic glycoproteins.Nat Protoc 2007; 2 (12): 3185-3194
    • (2007) Nat Protoc , vol.2 , Issue.12 , pp. 3185-3194
    • Van Kasteren, S.I.1    Kramer, H.B.2    Gamblin, D.P.3
  • 68
    • 37049029216 scopus 로고    scopus 로고
    • Site-directed conjugation of 'clicked' glycopolymers to form glycoprotein mimics: Binding to mammalian lectin and induction of immunological function
    • Geng J, Mantovani G, Tao L, et al. Site-directed conjugation of 'clicked' glycopolymers to form glycoprotein mimics: binding to mammalian lectin and induction of immunological function. J Am Chem Soc 2007; 129 (49): 15156-15163
    • (2007) J Am Chem Soc , vol.129 , Issue.49 , pp. 15156-15163
    • Geng, J.1    Mantovani, G.2    Tao, L.3
  • 69
    • 33748359131 scopus 로고    scopus 로고
    • Biotinylated glycopolymers synthesized by atom transfer radical polymerization
    • Vazquez-Dorbatt V, Maynard HD. Biotinylated glycopolymers synthesized by atom transfer radical polymerization. Biomacromolecules 2006; 7 (8): 2297-2302
    • (2006) Biomacromolecules , vol.7 , Issue.8 , pp. 2297-2302
    • Vazquez-Dorbatt, V.1    Maynard, H.D.2
  • 70
    • 68849112932 scopus 로고    scopus 로고
    • Synthesis of a pyridyl disulfide end-functionalized glycopolymer for conjugation to biomolecules and patterning on gold surfaces
    • Vazquez-Dorbatt V, Tolstyka ZP, Chang CW, et al. Synthesis of a pyridyl disulfide end-functionalized glycopolymer for conjugation to biomolecules and patterning on gold surfaces. Biomacromolecules 2009; 10 (8): 2207-2212
    • (2009) Biomacromolecules , vol.10 , Issue.8 , pp. 2207-2212
    • Vazquez-Dorbatt, V.1    Tolstyka, Z.P.2    Chang, C.W.3
  • 71
    • 0038753800 scopus 로고    scopus 로고
    • Use of combinatorial genetic libraries to humanize N-linked glycosylation in the yeast Pichia pastoris
    • Choi BK, Bobrowicz P, Davidson RC, et al. Use of combinatorial genetic libraries to humanize N-linked glycosylation in the yeast Pichia pastoris. Proc Natl Acad Sci U S A 2003; 100 (9): 5022-5027
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.9 , pp. 5022-5027
    • Choi, B.K.1    Bobrowicz, P.2    Davidson, R.C.3
  • 72
    • 32344449790 scopus 로고    scopus 로고
    • Optimization of humanized IgGs in glycoengineered Pichia pastoris
    • Li H, Sethuraman N, Stadheim TA, et al. Optimization of humanized IgGs in glycoengineered Pichia pastoris. Nat Biotechnol 2006; 24 (2): 210-215
    • (2006) Nat Biotechnol , vol.24 , Issue.2 , pp. 210-215
    • Li, H.1    Sethuraman, N.2    Stadheim, T.A.3
  • 73
    • 0042322600 scopus 로고    scopus 로고
    • Production of complex human glycoproteins in yeast
    • Hamilton SR, Bobrowicz P, Bobrowicz B, et al. Production of complex human glycoproteins in yeast. Science 2003; 301 (5637): 1244-1246
    • (2003) Science , vol.301 , Issue.5637 , pp. 1244-1246
    • Hamilton, S.R.1    Bobrowicz, P.2    Bobrowicz, B.3
  • 74
    • 33748483846 scopus 로고    scopus 로고
    • Humanization of yeast to produce complex terminally sialylated glycoproteins
    • Hamilton SR, Davidson RC, Sethuraman N, et al. Humanization of yeast to produce complex terminally sialylated glycoproteins. Science 2006; 313 (5792): 1441-1443
    • (2006) Science , vol.313 , Issue.5792 , pp. 1441-1443
    • Hamilton, S.R.1    Davidson, R.C.2    Sethuraman, N.3
  • 75
    • 60849113986 scopus 로고    scopus 로고
    • Production of monoclonal antibodies by glycoengineered Pichia pastoris
    • Potgieter TI, Cukan M, Drummond JE, et al. Production of monoclonal antibodies by glycoengineered Pichia pastoris. J Biotechnol 2009; 139 (4): 318-325
    • (2009) J Biotechnol , vol.139 , Issue.4 , pp. 318-325
    • Potgieter, T.I.1    Cukan, M.2    Drummond, J.E.3
  • 76
    • 36549015182 scopus 로고    scopus 로고
    • Production of humanized glycoproteins in bacteria and yeasts
    • Chiba Y, Jigami Y. Production of humanized glycoproteins in bacteria and yeasts. Curr Opin Chem Biol 2007; 11 (6): 670-676
    • (2007) Curr Opin Chem Biol , vol.11 , Issue.6 , pp. 670-676
    • Chiba, Y.1    Jigami, Y.2
  • 77
    • 70349765520 scopus 로고    scopus 로고
    • The production of biopharmaceuticals in plant systems
    • Karg SR, Kallio PT. The production of biopharmaceuticals in plant systems. Biotechnol Adv 2009; 27 (6): 879-894
    • (2009) Biotechnol Adv , vol.27 , Issue.6 , pp. 879-894
    • Karg, S.R.1    Kallio, P.T.2
  • 78
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler P, Khattak SF, Li ZJ. Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 2009; 19 (9): 936-949
    • (2009) Glycobiology , vol.19 , Issue.9 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 79
    • 66749161478 scopus 로고    scopus 로고
    • Glycan engineering and production of 'humanized' glycoprotein in yeast cells
    • Chiba Y, Akeboshi H. Glycan engineering and production of 'humanized' glycoprotein in yeast cells. Biol Pharm Bull 2009; 32 (5): 786-795
    • (2009) Biol Pharm Bull , vol.32 , Issue.5 , pp. 786-795
    • Chiba, Y.1    Akeboshi, H.2
  • 80
    • 2442648926 scopus 로고    scopus 로고
    • Production of therapeutic proteins in fungal hosts
    • Ballew N, Gerngross T. Production of therapeutic proteins in fungal hosts. Expert Opin Biol Ther 2004; 4 (5): 623-626
    • (2004) Expert Opin Biol Ther , vol.4 , Issue.5 , pp. 623-626
    • Ballew, N.1    Gerngross, T.2
  • 81
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • Gerngross TU. Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat Biotechnol 2004; 22 (11): 1409-1414
    • (2004) Nat Biotechnol , vol.22 , Issue.11 , pp. 1409-1414
    • Gerngross, T.U.1
  • 82
    • 68149118066 scopus 로고    scopus 로고
    • Increasing the sialylation of therapeutic glycoproteins: The potential of the sialic acid biosynthetic pathway
    • Bork K, Horstkorte R, Weidemann W. Increasing the sialylation of therapeutic glycoproteins: the potential of the sialic acid biosynthetic pathway. J Pharm Sci 2009; 98 (10): 3499-3508
    • (2009) J Pharm Sci , vol.98 , Issue.10 , pp. 3499-3508
    • Bork, K.1    Horstkorte, R.2    Weidemann, W.3
  • 83
    • 33947611087 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins in different production systems
    • Werner RG, Kopp K, Schlueter M. Glycosylation of therapeutic proteins in different production systems. Acta Paediatr Suppl 2007; 96 (455): 17-22
    • (2007) Acta Paediatr Suppl , vol.96 , Issue.455 , pp. 17-22
    • Werner, R.G.1    Kopp, K.2    Schlueter, M.3
  • 84
    • 66949119639 scopus 로고    scopus 로고
    • N-linked glycosylation in bacteria: An unexpected application
    • Langdon RH, Cuccui J, Wren BW. N-linked glycosylation in bacteria: an unexpected application. Future Microbiol 2009; 4 (4): 401-412
    • (2009) Future Microbiol , vol.4 , Issue.4 , pp. 401-412
    • Langdon, R.H.1    Cuccui, J.2    Wren, B.W.3
  • 85
    • 56049113736 scopus 로고    scopus 로고
    • Glyco-engineering of biotherapeutic proteins in plants
    • Ko K, Ahn MH, Song M, et al. Glyco-engineering of biotherapeutic proteins in plants. Mol Cells 2008; 25 (4): 494-503
    • (2008) Mol Cells , vol.25 , Issue.4 , pp. 494-503
    • Ko, K.1    Ahn, M.H.2    Song, M.3
  • 86
    • 44949158950 scopus 로고    scopus 로고
    • Assessment of cell engineering strategies for improved therapeutic protein production in CHO cells
    • Mohan C, Kim YG, Koo J, et al. Assessment of cell engineering strategies for improved therapeutic protein production in CHO cells. Biotechnol J 2008; 3 (5): 624-630
    • (2008) Biotechnol J , vol.3 , Issue.5 , pp. 624-630
    • Mohan, C.1    Kim, Y.G.2    Koo, J.3
  • 87
    • 35348927443 scopus 로고    scopus 로고
    • Protein N-glycosylation in the baculovirus-insect cell system
    • Shi X, Jarvis DL. Protein N-glycosylation in the baculovirus-insect cell system. Curr Drug Targets 2007; 8 (10): 1116-1125
    • (2007) Curr Drug Targets , vol.8 , Issue.10 , pp. 1116-1125
    • Shi, X.1    Jarvis, D.L.2
  • 88
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: The advent of fully humanized yeast
    • Hamilton SR, Gerngross TU. Glycosylation engineering in yeast: the advent of fully humanized yeast. Curr Opin Biotechnol 2007; 18 (5): 387-392
    • (2007) Curr Opin Biotechnol , vol.18 , Issue.5 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 89
    • 0032526093 scopus 로고    scopus 로고
    • Human alpha-galactosidase A: Glycosylation site 3 is essential for enzyme solubility
    • Ioannou YA, Zeidner KM, Grace ME, et al. Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility. Biochem J 1998; 332 (Pt 3): 789-797
    • (1998) Biochem J , vol.332 , Issue.PART 3 , pp. 789-797
    • Ioannou, Y.A.1    Zeidner, K.M.2    Grace, M.E.3
  • 90
    • 2942674460 scopus 로고    scopus 로고
    • Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley alpha-glucosidase
    • Clark SE, Muslin EH, Henson CA. Effect of adding and removing N-glycosylation recognition sites on the thermostability of barley alpha-glucosidase. Protein Eng Des Sel 2004; 17 (3): 245-249
    • (2004) Protein Eng des Sel , vol.17 , Issue.3 , pp. 245-249
    • Clark, S.E.1    Muslin, E.H.2    Henson, C.A.3
  • 91
    • 0031008063 scopus 로고    scopus 로고
    • Effect of glycosylation on the stability of alpha1-antitrypsin toward urea denaturation and thermal deactivation
    • Kwon KS, Yu MH. Effect of glycosylation on the stability of alpha1-antitrypsin toward urea denaturation and thermal deactivation. Biochim Biophys Acta 1997; 1335 (3): 265-272
    • (1997) Biochim Biophys Acta , vol.1335 , Issue.3 , pp. 265-272
    • Kwon, K.S.1    Yu, M.H.2
  • 92
    • 0031842383 scopus 로고    scopus 로고
    • Retardation of thermal and urea induced inactivation of alpha-chymotrypsin by modification with carbohydrate polymers
    • Sundaram PV, Venkatesh R. Retardation of thermal and urea induced inactivation of alpha-chymotrypsin by modification with carbohydrate polymers. Protein Eng 1998; 11 (8): 699-705
    • (1998) Protein Eng , vol.11 , Issue.8 , pp. 699-705
    • Sundaram, P.V.1    Venkatesh, R.2
  • 93
    • 33747126829 scopus 로고    scopus 로고
    • Engineering of protein thermodynamic, kinetic, and colloidal stability: Chemical glycosylation with monofunctionally activated glycans
    • Solá RJ,Al-Azzam W, Griebenow K. Engineering of protein thermodynamic, kinetic, and colloidal stability: chemical glycosylation with monofunctionally activated glycans. Biotechnol Bioeng 2006; 94 (6): 1072-1079
    • (2006) Biotechnol Bioeng , vol.94 , Issue.6 , pp. 1072-1079
    • Solá, R.J.1    Al-Azzam, W.2    Griebenow, K.3
  • 94
    • 0032539529 scopus 로고    scopus 로고
    • Mobilities of the inner three core residues and the Man (alpha 1-6) branch of the glycan at Asn78 of the alpha-subunit of human chorionic gonadotropin are restricted by the protein
    • van Zuylen CW, de Beer T, Leeflang BR, et al. Mobilities of the inner three core residues and the Man (alpha 1-6) branch of the glycan at Asn78 of the alpha-subunit of human chorionic gonadotropin are restricted by the protein. Biochemistry 1998; 37 (7): 1933-1940
    • (1998) Biochemistry , vol.37 , Issue.7 , pp. 1933-1940
    • Van Zuylen, C.W.1    De Beer, T.2    Leeflang, B.R.3
  • 95
    • 0030699055 scopus 로고    scopus 로고
    • Effect of active oxygen radicals on protein and carbohydrate moieties of recombinant human erythropoietin
    • Uchida E, Morimoto K, Kawasaki N, et al. Effect of active oxygen radicals on protein and carbohydrate moieties of recombinant human erythropoietin. Free Radic Res 1997; 27 (3): 311-323
    • (1997) Free Radic Res , vol.27 , Issue.3 , pp. 311-323
    • Uchida, E.1    Morimoto, K.2    Kawasaki, N.3
  • 96
    • 0026317615 scopus 로고
    • The effect of carbohydrate on the structure and stability of erythropoietin
    • Narhi LO, Arakawa T, Aoki KH, et al. The effect of carbohydrate on the structure and stability of erythropoietin. J Biol Chem 1991; 266 (34): 23022-23026
    • (1991) J Biol Chem , vol.266 , Issue.34 , pp. 23022-23026
    • Narhi, L.O.1    Arakawa, T.2    Aoki, K.H.3
  • 97
    • 0025214337 scopus 로고
    • The role of carbohydrate in recombinant human erythropoietin
    • Tsuda E, Kawanishi G, Ueda M, et al. The role of carbohydrate in recombinant human erythropoietin. Eur J Biochem 1990; 188 (2): 405-411
    • (1990) Eur J Biochem , vol.188 , Issue.2 , pp. 405-411
    • Tsuda, E.1    Kawanishi, G.2    Ueda, M.3
  • 98
    • 14444271579 scopus 로고    scopus 로고
    • Structural and functional differences between glycosylated and non-glycosylated forms of human interferon-beta (IFN-beta)
    • Runkel L, Meier W, Pepinsky RB, et al. Structural and functional differences between glycosylated and non-glycosylated forms of human interferon-beta (IFN-beta). Pharm Res 1998; 15 (4): 641-649
    • (1998) Pharm Res , vol.15 , Issue.4 , pp. 641-649
    • Runkel, L.1    Meier, W.2    Pepinsky, R.B.3
  • 99
    • 0031766727 scopus 로고    scopus 로고
    • The structure of human interferonbeta: Implications for activity
    • Karpusas M, Whitty A, Runkel L, et al. The structure of human interferonbeta: implications for activity. Cell Mol Life Sci 1998; 54 (11): 1203-1216
    • (1998) Cell Mol Life Sci , vol.54 , Issue.11 , pp. 1203-1216
    • Karpusas, M.1    Whitty, A.2    Runkel, L.3
  • 100
    • 0023629280 scopus 로고
    • Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line
    • Conradt HS, Egge H, Peter-Katalinic J, et al. Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line. J Biol Chem 1987; 262 (30): 14600-14605
    • (1987) J Biol Chem , vol.262 , Issue.30 , pp. 14600-14605
    • Conradt, H.S.1    Egge, H.2    Peter-Katalinic, J.3
  • 101
    • 0027957966 scopus 로고
    • Glycoforms modify the dynamic stability and functional activity of an enzyme
    • Rudd PM, Joao HC, Coghill E, et al. Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 1994; 33 (1): 17-22
    • (1994) Biochemistry , vol.33 , Issue.1 , pp. 17-22
    • Rudd, P.M.1    Joao, H.C.2    Coghill, E.3
  • 102
    • 1342281681 scopus 로고    scopus 로고
    • Glycosylation of onconase increases its conformational stability and toxicity for cancer cells
    • Kim BM, Kim H, Raines RT, et al. Glycosylation of onconase increases its conformational stability and toxicity for cancer cells. Biochem Biophys Res Commun 2004; 315 (4): 976-983
    • (2004) Biochem Biophys Res Commun , vol.315 , Issue.4 , pp. 976-983
    • Kim, B.M.1    Kim, H.2    Raines, R.T.3
  • 103
    • 0027944915 scopus 로고
    • Glycosylation of recombinant human granulocyte colony stimulating factor: Implications for stability and potency
    • Nissen C. Glycosylation of recombinant human granulocyte colony stimulating factor: implications for stability and potency. Eur J Cancer 1994; 30A Suppl. 3: S12-4
    • (1994) Eur J Cancer , vol.30 A , Issue.SUPPL. 3
    • Nissen, C.1
  • 104
    • 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, et al. 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 1990; 265 (20): 11432-11435
    • (1990) J Biol Chem , vol.265 , Issue.20 , pp. 11432-11435
    • Oh-Eda, M.1    Hasegawa, M.2    Hattori, K.3
  • 105
    • 0028113365 scopus 로고
    • Physicochemical and biochemical characteristics of glycosylated recombinant human granulocyte colony stimulating factor (lenograstim)
    • Ono M. Physicochemical and biochemical characteristics of glycosylated recombinant human granulocyte colony stimulating factor (lenograstim). Eur J Cancer 1994; 30A Suppl. 3: S7-11
    • (1994) Eur J Cancer , vol.30 A , Issue.SUPPL. 3
    • Ono, M.1
  • 106
    • 0020744376 scopus 로고
    • Glycosylation of thyroid-stimulating hormone in pituitary tumor cells: Influence of high mannose oligosaccharide units on subunit aggregation, combination, and intracellular degradation
    • Weintraub BD, Stannard BS,Meyers L. Glycosylation of thyroid-stimulating hormone in pituitary tumor cells: influence of high mannose oligosaccharide units on subunit aggregation, combination, and intracellular degradation. Endocrinology 1983; 112 (4): 1331-1345
    • (1983) Endocrinology , vol.112 , Issue.4 , pp. 1331-1345
    • Weintraub, B.D.1    Stannard, B.S.2    Meyers, L.3
  • 107
    • 33745792134 scopus 로고    scopus 로고
    • Effect of glycosylation at Asn302 of pro-urokinase on its stability in culture supernatant
    • Yang B, Li TD. Effect of glycosylation at Asn302 of pro-urokinase on its stability in culture supernatant. Chin Med Sci J 2006; 21 (2): 128-130
    • (2006) Chin Med Sci J , vol.21 , Issue.2 , pp. 128-130
    • Yang, B.1    Li, T.D.2
  • 108
    • 0029610548 scopus 로고
    • Physical stabilization of insulin by glycosylation
    • Baudys M, Uchio T, Mix D, et al. Physical stabilization of insulin by glycosylation. J Pharm Sci 1995; 84 (1): 28-33
    • (1995) J Pharm Sci , vol.84 , Issue.1 , pp. 28-33
    • Baudys, M.1    Uchio, T.2    Mix, D.3
  • 109
    • 33747099227 scopus 로고    scopus 로고
    • Effect of posttranslational modifications on the thermal stability of a recombinant monoclonal antibody
    • Liu H, Bulseco GG, Sun J. Effect of posttranslational modifications on the thermal stability of a recombinant monoclonal antibody. Immunol Lett 2006; 106 (2): 144-153
    • (2006) Immunol Lett , vol.106 , Issue.2 , pp. 144-153
    • Liu, H.1    Bulseco, G.G.2    Sun, J.3
  • 110
    • 0033519426 scopus 로고    scopus 로고
    • Glycosylation of human IgG-Fc: Influences on structure revealed by differential scanning micro-calorimetry
    • Ghirlando R, Lund J, Goodall M, et al. Glycosylation of human IgG-Fc: influences on structure revealed by differential scanning micro-calorimetry. Immunol Lett 1999; 68 (1): 47-52
    • (1999) Immunol Lett , vol.68 , Issue.1 , pp. 47-52
    • Ghirlando, R.1    Lund, J.2    Goodall, M.3
  • 111
    • 0027519943 scopus 로고
    • Protein glycosylation. Structural and functional aspects
    • Lis H, Sharon N. Protein glycosylation. Structural and functional aspects. Eur J Biochem 1993; 218 (1): 1-27
    • (1993) Eur J Biochem , vol.218 , Issue.1 , pp. 1-27
    • Lis, H.1    Sharon, N.2
  • 112
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993; 3 (2): 97-130
    • (1993) Glycobiology , vol.3 , Issue.2 , pp. 97-130
    • Varki, A.1
  • 113
    • 0016666851 scopus 로고
    • The resistance of glycoproteins to proteolytic inactivation
    • Vegarud G, Christensen TB. The resistance of glycoproteins to proteolytic inactivation. Acta Chem Scand B 1975; 29 (8): 887-888
    • (1975) Acta Chem Scand B , vol.29 , Issue.8 , pp. 887-888
    • Vegarud, G.1    Christensen, T.B.2
  • 114
    • 0016830344 scopus 로고
    • Glycosylation of proteins: A new method of enzyme stabilization
    • Vegarud G, Christnsen TB. Glycosylation of proteins: a new method of enzyme stabilization. Biotechnol Bioeng 1975; 17 (9): 1391-1397
    • (1975) Biotechnol Bioeng , vol.17 , Issue.9 , pp. 1391-1397
    • Vegarud, G.1    Christnsen, T.B.2
  • 115
    • 70149100403 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of glycosylated glucagon-like peptide 1: Effect of glycosylation on proteolytic resistance and in vivo blood glucose-lowering activity
    • Ueda T, Tomita K, Notsu Y, et al. Chemoenzymatic synthesis of glycosylated glucagon-like peptide 1: effect of glycosylation on proteolytic resistance and in vivo blood glucose-lowering activity. JAmChemSoc 2009; 131 (17): 6237-6245
    • (2009) J Am Chem Soc , vol.131 , Issue.17 , pp. 6237-6245
    • Ueda, T.1    Tomita, K.2    Notsu, Y.3
  • 116
    • 1542513235 scopus 로고    scopus 로고
    • Human serum inactivates non-glycosylated but not glycosylated granulocyte colony stimulating factor by a protease dependent mechanism: Significance of carbohydrates on the glycosylated molecule
    • Carter CR, Keeble JR, Thorpe R. Human serum inactivates non-glycosylated but not glycosylated granulocyte colony stimulating factor by a protease dependent mechanism: significance of carbohydrates on the glycosylated molecule. Biologicals 2004; 32 (1): 37-47
    • (2004) Biologicals , vol.32 , Issue.1 , pp. 37-47
    • Carter, C.R.1    Keeble, J.R.2    Thorpe, R.3
  • 117
    • 0033564008 scopus 로고    scopus 로고
    • Site-directed removal of N-glycosylation sites in human gastric lipase
    • Wicker-Planquart C, Canaan S, Riviere M, et al. Site-directed removal of N-glycosylation sites in human gastric lipase. Eur J Biochem 1999; 262 (3): 644-651
    • (1999) Eur J Biochem , vol.262 , Issue.3 , pp. 644-651
    • Wicker-Planquart, C.1    Canaan, S.2    Riviere, M.3
  • 118
    • 0025883206 scopus 로고
    • Glycosylation of human protein C affects its secretion, processing, functional activities, and activation by thrombin
    • Grinnell BW, Walls JD, Gerlitz B. Glycosylation of human protein C affects its secretion, processing, functional activities, and activation by thrombin. J Biol Chem 1991; 266 (15): 9778-9785
    • (1991) J Biol Chem , vol.266 , Issue.15 , pp. 9778-9785
    • Grinnell, B.W.1    Walls, J.D.2    Gerlitz, B.3
  • 119
    • 0033777689 scopus 로고    scopus 로고
    • Glycosylation of prourokinase produced by Pichia pastoris impairs enzymatic activity but not secretion
    • Wang P, Zhang J, Sun Z, et al. Glycosylation of prourokinase produced by Pichia pastoris impairs enzymatic activity but not secretion. Protein Expr Purif 2000; 20 (2): 179-185
    • (2000) Protein Expr Purif , vol.20 , Issue.2 , pp. 179-185
    • Wang, P.1    Zhang, J.2    Sun, Z.3
  • 120
    • 0027500857 scopus 로고
    • Effect of carbohydrates on the pharmacokinetics of human interferon-gamma
    • Sareneva T, Cantell K, Pyhala L, et al. Effect of carbohydrates on the pharmacokinetics of human interferon-gamma. J Interferon Res 1993; 13 (4): 267-269
    • (1993) J Interferon Res , vol.13 , Issue.4 , pp. 267-269
    • Sareneva, T.1    Cantell, K.2    Pyhala, L.3
  • 121
    • 34547909649 scopus 로고    scopus 로고
    • Fc glycans terminated with N-acetylglucosamine residues increase antibody resistance to papain
    • Raju TS, Scallon B. Fc glycans terminated with N-acetylglucosamine residues increase antibody resistance to papain. Biotechnol Prog 2007; 23 (4): 964-971
    • (2007) Biotechnol Prog , vol.23 , Issue.4 , pp. 964-971
    • Raju, T.S.1    Scallon, B.2
  • 122
    • 35648982031 scopus 로고    scopus 로고
    • Site determination of protein glycosylation based on digestion with immobilized nonspecific proteases and Fourier transform ion cyclotron resonance mass spectrometry
    • Clowers BH, Dodds ED, Seipert RR, et al. Site determination of protein glycosylation based on digestion with immobilized nonspecific proteases and Fourier transform ion cyclotron resonance mass spectrometry. J Proteome Res 2007; 6 (10): 4032-4040
    • (2007) J Proteome Res , vol.6 , Issue.10 , pp. 4032-4040
    • Clowers, B.H.1    Dodds, E.D.2    Seipert, R.R.3
  • 123
    • 0016307685 scopus 로고
    • The dual role of sialic acid in the hepatic recognition and catabolism of serum glycoproteins
    • Ashwell G, Morell A. The dual role of sialic acid in the hepatic recognition and catabolism of serum glycoproteins. Biochem Soc Symp 1974; (40): 117-124
    • (1974) Biochem Soc Symp , Issue.40 , pp. 117-124
    • Ashwell, G.1    Morell, A.2
  • 124
    • 0016322758 scopus 로고
    • The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins
    • Ashwell G, Morell AG. The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv Enzymol Relat Areas Mol Biol 1974; 41 (0): 99-128
    • (1974) Adv Enzymol Relat Areas Mol Biol , vol.41 , Issue.0 , pp. 99-128
    • Ashwell, G.1    Morell, A.G.2
  • 125
    • 0026302399 scopus 로고
    • Structural characteristics and regulation of the asialoglycoprotein receptor
    • Stockert RJ, Morell AG, Ashwell G. Structural characteristics and regulation of the asialoglycoprotein receptor. Targeted Diagn Ther 1991; 4: 41-64
    • (1991) Targeted Diagn Ther , vol.4 , pp. 41-64
    • Stockert, R.J.1    Morell, A.G.2    Ashwell, G.3
  • 126
    • 0016143294 scopus 로고
    • A membrane receptor protein for asialoglycoproteins
    • Pricer Jr WE, Hudgin RL, Ashwell G, et al. A membrane receptor protein for asialoglycoproteins. Methods Enzymol 1974; 34: 688-691
    • (1974) Methods Enzymol , vol.34 , pp. 688-691
    • Pricer Jr., W.E.1    Hudgin, R.L.2    Ashwell, G.3
  • 127
    • 0014408285 scopus 로고
    • Physical and chemical studies on ceruloplasmin, V: Metabolic studies on sialic acid-free ceruloplasmin in vivo
    • Morell AG, Irvine RA, Sternlieb I, et al. Physical and chemical studies on ceruloplasmin, V: metabolic studies on sialic acid-free ceruloplasmin in vivo. J Biol Chem 1968; 243 (1): 155-159
    • (1968) J Biol Chem , vol.243 , Issue.1 , pp. 155-159
    • Morell, A.G.1    Irvine, R.A.2    Sternlieb, I.3
  • 128
    • 0024276082 scopus 로고
    • Involvement of various organs in the initial plasma clearance of differently glycosylated rat liver secretory proteins
    • Gross V,Heinrich PC, vom Berg D, et al. Involvement of various organs in the initial plasma clearance of differently glycosylated rat liver secretory proteins. Eur J Biochem 1988; 173 (3): 653-659
    • (1988) Eur J Biochem , vol.173 , Issue.3 , pp. 653-659
    • Gross, V.1    Heinrich, P.C.2    Vom Berg, D.3
  • 129
    • 0015217323 scopus 로고
    • The role of sialic acid in determining the survival of glycoproteins in the circulation
    • Morell AG, Gregoriadis G, Scheinberg IH, et al. The role of sialic acid in determining the survival of glycoproteins in the circulation. J Biol Chem 1971; 246 (5): 1461-1467
    • (1971) J Biol Chem , vol.246 , Issue.5 , pp. 1461-1467
    • Morell, A.G.1    Gregoriadis, G.2    Scheinberg, I.H.3
  • 130
    • 0017088202 scopus 로고
    • Effect of glycosylation on the in vivo circulating half-life of ribonuclease
    • Baynes JW, Wold F. Effect of glycosylation on the in vivo circulating half-life of ribonuclease. J Biol Chem 1976; 251 (19): 6016-6024
    • (1976) J Biol Chem , vol.251 , Issue.19 , pp. 6016-6024
    • Baynes, J.W.1    Wold, F.2
  • 131
    • 0022340897 scopus 로고
    • Receptor-mediated endocytosis
    • Wileman T, Harding C, Stahl P. Receptor-mediated endocytosis. Biochem J 1985; 232 (1): 1-14
    • (1985) Biochem J , vol.232 , Issue.1 , pp. 1-14
    • Wileman, T.1    Harding, C.2    Stahl, P.3
  • 132
    • 0018069858 scopus 로고
    • Plasma clearance of glycoproteins with terminal mannose and N-acetylglucosamine by liver nonparenchymal cells: Studies with beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, ribonuclease B and agalacto-orosomucoid
    • Schlesinger PH, Doebber TW, Mandell BF, et al. Plasma clearance of glycoproteins with terminal mannose and N-acetylglucosamine by liver nonparenchymal cells: studies with beta-glucuronidase, N-acetyl-beta-D- glucosaminidase, ribonuclease B and agalacto-orosomucoid. Biochem J 1978; 176 (1): 103-109
    • (1978) Biochem J , vol.176 , Issue.1 , pp. 103-109
    • Schlesinger, P.H.1    Doebber, T.W.2    Mandell, B.F.3
  • 133
    • 0019214256 scopus 로고
    • The role of extra-hepatic tissues in the receptor-mediated plasma clearance of glycoproteins terminated by mannose or N-acetylglucosamine
    • Schlesinger PH, Rodman JS, Doebber TW, et al. The role of extra-hepatic tissues in the receptor-mediated plasma clearance of glycoproteins terminated by mannose or N-acetylglucosamine. Biochem J 1980; 192 (2): 597-606
    • (1980) Biochem J , vol.192 , Issue.2 , pp. 597-606
    • Schlesinger, P.H.1    Rodman, J.S.2    Doebber, T.W.3
  • 134
    • 0019463053 scopus 로고
    • Isolation and characterization of a mannose/N-acetylglucosamine/ fucose-binding protein from rat liver
    • Townsend R, Stahl P. Isolation and characterization of a mannose/N-acetylglucosamine/ fucose-binding protein from rat liver. Biochem J 1981; 194 (1): 209-214
    • (1981) Biochem J , vol.194 , Issue.1 , pp. 209-214
    • Townsend, R.1    Stahl, P.2
  • 135
    • 0018170526 scopus 로고
    • Human beta-glucuronidase: In vivo clearance and in vitro uptake by a glycoprotein recognition system on reticuloendothelial cells
    • Achord DT, Brot FE, Bell CE, et al. Human beta-glucuronidase: in vivo clearance and in vitro uptake by a glycoprotein recognition system on reticuloendothelial cells. Cell 1978; 15 (1): 269-278
    • (1978) Cell , vol.15 , Issue.1 , pp. 269-278
    • Achord, D.T.1    Brot, F.E.2    Bell, C.E.3
  • 136
    • 0037136420 scopus 로고    scopus 로고
    • Glycans as endocytosis signals: The cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors
    • Weigel PH, Yik JH. Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors. Biochim Biophys Acta 2002; 1572 (2-3): 341-363
    • (2002) Biochim Biophys Acta , vol.1572 , Issue.2-3 , pp. 341-363
    • Weigel, P.H.1    Yik, J.H.2
  • 137
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action
    • Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol Sci 2009; 30 (7): 356-362
    • (2009) Trends Pharmacol Sci , vol.30 , Issue.7 , pp. 356-362
    • Jefferis, R.1
  • 138
    • 0034693398 scopus 로고    scopus 로고
    • Improved bioavailability to the brain of glycosylatedMet-enkephalin analogs
    • Egleton RD, Mitchell SA, Huber JD, et al. Improved bioavailability to the brain of glycosylatedMet-enkephalin analogs. Brain Res 2000; 881 (1): 37-46
    • (2000) Brain Res , vol.881 , Issue.1 , pp. 37-46
    • Egleton, R.D.1    Mitchell, S.A.2    Huber, J.D.3
  • 139
    • 0035200718 scopus 로고    scopus 로고
    • Improved blood-brain barrier penetration and enhanced analgesia of an opioid peptide by glycosylation
    • Egleton RD, Mitchell SA, Huber JD, et al. Improved blood-brain barrier penetration and enhanced analgesia of an opioid peptide by glycosylation. J Pharmacol Exp Ther 2001; 299 (3): 967-972
    • (2001) J Pharmacol Exp Ther , vol.299 , Issue.3 , pp. 967-972
    • Egleton, R.D.1    Mitchell, S.A.2    Huber, J.D.3
  • 140
    • 0029063811 scopus 로고
    • Glycosylated peptide hormones: Pharmacological properties and conformational studies of analogues of [1-desamino, 8-D-arginine] vasopressin
    • Kihlberg J, Ahman J, Walse B, et al. Glycosylated peptide hormones: pharmacological properties and conformational studies of analogues of [1-desamino, 8-D-arginine]vasopressin. J Med Chem 1995; 38 (1): 161-169
    • (1995) J Med Chem , vol.38 , Issue.1 , pp. 161-169
    • Kihlberg, J.1    Ahman, J.2    Walse, B.3
  • 141
    • 0035122334 scopus 로고    scopus 로고
    • Glycosylated RGD-containing peptides: Tracer for tumor targeting and angiogenesis imaging with improved biokinetics
    • Haubner R, Wester HJ, Burkhart F, et al. Glycosylated RGD-containing peptides: tracer for tumor targeting and angiogenesis imaging with improved biokinetics. J Nucl Med 2001; 42 (2): 326-336
    • (2001) J Nucl Med , vol.42 , Issue.2 , pp. 326-336
    • Haubner, R.1    Wester, H.J.2    Burkhart, F.3
  • 142
    • 0027310350 scopus 로고
    • SDZ CO 611: A highly potent glycated analog of somatostatin with improved oral activity
    • Albert R, Marbach P, Bauer W, et al. SDZ CO 611: a highly potent glycated analog of somatostatin with improved oral activity.Life Sci 1993; 53 (6): 517-525
    • (1993) Life Sci , vol.53 , Issue.6 , pp. 517-525
    • Albert, R.1    Marbach, P.2    Bauer, W.3
  • 143
    • 0026355305 scopus 로고
    • Comparative pharmacokinetics and pharmacodynamics of epoetin alfa and epoetin beta
    • Halstenson CE, Macres M, Katz SA, et al. Comparative pharmacokinetics and pharmacodynamics of epoetin alfa and epoetin beta. Clin Pharmacol Ther 1991; 50 (6): 702-712
    • (1991) Clin Pharmacol Ther , vol.50 , Issue.6 , pp. 702-712
    • Halstenson, C.E.1    MacRes, M.2    Katz, S.A.3
  • 144
    • 0034463325 scopus 로고    scopus 로고
    • Glycosylated human interleukin-1alpha neoglyco IL-1alpha coupled with N-acetylneuraminic acid exhibits selective activities in vivo and altered tissue distribution
    • Sasayama S,MoriyaK, Chiba T, et al.Glycosylated human interleukin-1alpha, neoglyco IL-1alpha, coupled with N-acetylneuraminic acid exhibits selective activities in vivo and altered tissue distribution.Glycoconj J 2000; 17 (6): 353-359
    • (2000) Glycoconj J , vol.17 , Issue.6 , pp. 353-359
    • Sasayama, S.1    Moriya, K.2    Chiba, T.3
  • 145
    • 61649120342 scopus 로고    scopus 로고
    • Altered chain-length and glycosylation modify the pharmacokinetics of human serum albumin
    • Iwao Y, Hiraike M, Kragh-Hansen U, et al. Altered chain-length and glycosylation modify the pharmacokinetics of human serum albumin. Biochim Biophys Acta 2009; 1794 (4): 634-641
    • (2009) Biochim Biophys Acta , vol.1794 , Issue.4 , pp. 634-641
    • Iwao, Y.1    Hiraike, M.2    Kragh-Hansen, U.3
  • 146
    • 38349123331 scopus 로고    scopus 로고
    • Effect of constant and variable domain glycosylation on pharmacokinetics of therapeutic antibodies in mice
    • Millward TA, Heitzmann M, Bill K, et al. Effect of constant and variable domain glycosylation on pharmacokinetics of therapeutic antibodies in mice. Biologicals 2008; 36 (1): 41-47
    • (2008) Biologicals , vol.36 , Issue.1 , pp. 41-47
    • Millward, T.A.1    Heitzmann, M.2    Bill, K.3
  • 147
    • 0034666718 scopus 로고    scopus 로고
    • Modulation of clearance of recombinant serum albumin by either glycosylation or truncation
    • Sheffield WP, Marques JA, Bhakta V, et al. Modulation of clearance of recombinant serum albumin by either glycosylation or truncation. Thromb Res 2000; 99 (6): 613-621
    • (2000) Thromb Res , vol.99 , Issue.6 , pp. 613-621
    • Sheffield, W.P.1    Marques, J.A.2    Bhakta, V.3
  • 148
    • 0344286025 scopus 로고    scopus 로고
    • Influence of glycosylation on the clearance of recombinant human sex hormone-binding globulin from rabbit blood
    • Cousin P, Dechaud H, Grenot C, et al. Influence of glycosylation on the clearance of recombinant human sex hormone-binding globulin from rabbit blood. J Steroid Biochem Mol Biol 1999; 70 (4-6): 115-121
    • (1999) J Steroid Biochem Mol Biol , vol.70 , Issue.4-6 , pp. 115-121
    • Cousin, P.1    Dechaud, H.2    Grenot, C.3
  • 149
    • 0029828126 scopus 로고    scopus 로고
    • In vivo bioactivities and clearance patterns of highly purified human luteinizing hormone isoforms
    • Burgon PG, Stanton PG, Robertson DM. In vivo bioactivities and clearance patterns of highly purified human luteinizing hormone isoforms. Endocrinology 1996; 137 (11): 4827-4836
    • (1996) Endocrinology , vol.137 , Issue.11 , pp. 4827-4836
    • Burgon, P.G.1    Stanton, P.G.2    Robertson, D.M.3
  • 150
    • 0026567278 scopus 로고
    • Blood clearance in the rat of a recombinant mouse monoclonal antibody lacking the N-linked oligosaccharide side chains of the CH2 domains
    • Wawrzynczak EJ, Cumber AJ, Parnell GD, et al. Blood clearance in the rat of a recombinant mouse monoclonal antibody lacking the N-linked oligosaccharide side chains of the CH2 domains. Mol Immunol 1992; 29 (2): 213-220
    • (1992) Mol Immunol , vol.29 , Issue.2 , pp. 213-220
    • Wawrzynczak, E.J.1    Cumber, A.J.2    Parnell, G.D.3
  • 151
    • 0025918501 scopus 로고
    • High sialic acid content slows prourokinase turnover in rabbits
    • Henkin J, Dudlak D, Beebe DP, et al. High sialic acid content slows prourokinase turnover in rabbits. Thromb Res 1991; 63 (2): 215-225
    • (1991) Thromb Res , vol.63 , Issue.2 , pp. 215-225
    • Henkin, J.1    Dudlak, D.2    Beebe, D.P.3
  • 152
    • 0025059456 scopus 로고
    • The pharmacokinetic pattern of glycosylated human recombinant lymphotoxin (LT) in rats after intravenous administration
    • Kawatsu M, Takeo K, Kajikawa T, et al. The pharmacokinetic pattern of glycosylated human recombinant lymphotoxin (LT) in rats after intravenous administration. J Pharmacobiodyn 1990; 13 (9): 549-557
    • (1990) J Pharmacobiodyn , vol.13 , Issue.9 , pp. 549-557
    • Kawatsu, M.1    Takeo, K.2    Kajikawa, T.3
  • 153
    • 0023111790 scopus 로고
    • The role of N-glycosylation for the plasma clearance of rat liver secretory glycoproteins
    • Gross V, Steube K, Tran-Thi T, et al. The role of N-glycosylation for the plasma clearance of rat liver secretory glycoproteins. Eur J Biochem 1987; 162 (1): 83-88
    • (1987) Eur J Biochem , vol.162 , Issue.1 , pp. 83-88
    • Gross, V.1    Steube, K.2    Tran-Thi, T.3
  • 154
    • 38849095658 scopus 로고    scopus 로고
    • The glycosylation and in vivo stability of human granulocyte-macrophage colony-stimulating factor produced in rice cells
    • Kim HJ, Lee DH, Kim DK, et al. The glycosylation and in vivo stability of human granulocyte-macrophage colony-stimulating factor produced in rice cells. Biol Pharm Bull 2008; 31 (2): 290-294
    • (2008) Biol Pharm Bull , vol.31 , Issue.2 , pp. 290-294
    • Kim, H.J.1    Lee, D.H.2    Kim, D.K.3
  • 156
    • 43949141204 scopus 로고    scopus 로고
    • Survival of von Willebrand factor released following DDAVP in a type 1 von Willebrand disease cohort: Influence of glycosylation, proteolysis and gene mutations
    • Millar CM, Riddell AF, Brown SA, et al. Survival of von Willebrand factor released following DDAVP in a type 1 von Willebrand disease cohort: influence of glycosylation, proteolysis and gene mutations. Thromb Haemost 2008; 99 (5): 916-924
    • (2008) Thromb Haemost , vol.99 , Issue.5 , pp. 916-924
    • Millar, C.M.1    Riddell, A.F.2    Brown, S.A.3
  • 157
    • 34548355197 scopus 로고    scopus 로고
    • Pharmacokinetics and pharmacodynamics of epoetin delta in two studies in healthy volunteers and two studies in patients with chronic kidney disease
    • Smith WB, Dowell JA, Pratt RD. Pharmacokinetics and pharmacodynamics of epoetin delta in two studies in healthy volunteers and two studies in patients with chronic kidney disease. Clin Ther 2007; 29 (7): 1368-1380
    • (2007) Clin Ther , vol.29 , Issue.7 , pp. 1368-1380
    • Smith, W.B.1    Dowell, J.A.2    Pratt, R.D.3
  • 158
    • 34447296997 scopus 로고    scopus 로고
    • Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys
    • Jones AJ, Papac DI, Chin EH, et al. Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys. Glycobiology 2007; 17 (5): 529-540
    • (2007) Glycobiology , vol.17 , Issue.5 , pp. 529-540
    • Jones, A.J.1    Papac, D.I.2    Chin, E.H.3
  • 159
    • 0037622799 scopus 로고    scopus 로고
    • Glycosylation of an Nterminal extension prolongs the half-life and increases the in vivo activity of follicle stimulating hormone
    • Perlman S, van den Hazel B, Christiansen J, et al. Glycosylation of an Nterminal extension prolongs the half-life and increases the in vivo activity of follicle stimulating hormone. J Clin Endocrinol Metab 2003; 88 (7): 3227-3235
    • (2003) J Clin Endocrinol Metab , vol.88 , Issue.7 , pp. 3227-3235
    • Perlman, S.1    Van Den Hazel, B.2    Christiansen, J.3
  • 160
    • 0037168912 scopus 로고    scopus 로고
    • Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones
    • Barrios-De-Tomasi J, Timossi C, MerchantH, et al. Assessment of the in vitro and in vivo biological activities of the human follicle-stimulating isohormones. Mol Cell Endocrinol 2002; 186 (2): 189-198
    • (2002) Mol Cell Endocrinol , vol.186 , Issue.2 , pp. 189-198
    • Barrios-De-Tomasi, J.1    Timossi, C.2    Merchant, H.3
  • 161
    • 0036316443 scopus 로고    scopus 로고
    • Optimizing the use of erythropoietic agents: Pharmacokinetic and pharmacodynamic considerations
    • Macdougall IC.Optimizing the use of erythropoietic agents: pharmacokinetic and pharmacodynamic considerations. Nephrol Dial Transplant 2002; 17 Suppl. 5: 66-70
    • (2002) Nephrol Dial Transplant , vol.17 , Issue.SUPPL. 5 , pp. 66-70
    • MacDougall, I.C.1
  • 162
    • 0034663089 scopus 로고    scopus 로고
    • Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin
    • Ni H, Blajchman MA, Ananthanarayanan VS, et al. Mutation of any site of N-linked glycosylation accelerates the in vivo clearance of recombinant rabbit antithrombin. Thromb Res 2000; 99 (4): 407-415
    • (2000) Thromb Res , vol.99 , Issue.4 , pp. 407-415
    • Ni, H.1    Blajchman, M.A.2    Ananthanarayanan, V.S.3
  • 163
    • 0034038611 scopus 로고    scopus 로고
    • O-glycosylation delays the clearance of human IGF-binding protein-6 from the circulation
    • Marinaro JA, Casley DJ, Bach LA. O-glycosylation delays the clearance of human IGF-binding protein-6 from the circulation. Eur J Endocrinol 2000; 142 (5): 512-516
    • (2000) Eur J Endocrinol , vol.142 , Issue.5 , pp. 512-516
    • Marinaro, J.A.1    Casley, D.J.2    Bach, L.A.3
  • 164
    • 0032534987 scopus 로고    scopus 로고
    • Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels
    • Chitlaru T, Kronman C, Zeevi M, et al. Modulation of circulatory residence of recombinant acetylcholinesterase through biochemical or genetic manipulation of sialylation levels. Biochem J 1998; 336 (Pt 3): 647-658
    • (1998) Biochem J , vol.336 , Issue.PART 3 , pp. 647-658
    • Chitlaru, T.1    Kronman, C.2    Zeevi, M.3
  • 165
    • 0030948899 scopus 로고    scopus 로고
    • Structure of glycan moieties responsible for the extended circulatory life time of fetal bovine serum acetylcholinesterase and equine serum butyrylcholinesterase
    • Saxena A, Raveh L, Ashani Y, et al. Structure of glycan moieties responsible for the extended circulatory life time of fetal bovine serum acetylcholinesterase and equine serum butyrylcholinesterase. Biochemistry 1997; 36 (24): 7481-7489
    • (1997) Biochemistry , vol.36 , Issue.24 , pp. 7481-7489
    • Saxena, A.1    Raveh, L.2    Ashani, Y.3
  • 166
    • 0028041190 scopus 로고
    • Structure-function studies of oligosaccharides of recombinant human thyrotrophin by sequential deglycosylation and resialylation
    • Thotakura NR, Szkudlinski MW, Weintraub BD. Structure-function studies of oligosaccharides of recombinant human thyrotrophin by sequential deglycosylation and resialylation. Glycobiology 1994; 4 (4): 525-533
    • (1994) Glycobiology , vol.4 , Issue.4 , pp. 525-533
    • Thotakura, N.R.1    Szkudlinski, M.W.2    Weintraub, B.D.3
  • 167
    • 0027104509 scopus 로고
    • Mechanisms of tissue-type plasminogen activator (tPA) clearance by the liver
    • OtterM, Kuiper J, van Berkel TJ, et al. Mechanisms of tissue-type plasminogen activator (tPA) clearance by the liver. Ann N Y Acad Sci 1992; 667: 431-442
    • (1992) Ann N y Acad Sci , vol.667 , pp. 431-442
    • Otter, M.1    Kuiper, J.2    Van Berkel, T.J.3
  • 168
    • 0025893335 scopus 로고
    • The importance of N- and O-linked oligosaccharides for the biosynthesis and in vitro and in vivo biologic activities of erythropoietin
    • Wasley LC, Timony G, Murtha P, et al. The importance of N- and O-linked oligosaccharides for the biosynthesis and in vitro and in vivo biologic activities of erythropoietin. Blood 1991; 77 (12): 2624-2632
    • (1991) Blood , vol.77 , Issue.12 , pp. 2624-2632
    • Wasley, L.C.1    Timony, G.2    Murtha, P.3
  • 169
    • 0025291299 scopus 로고
    • In vitro and in vivo bioactivity of recombinant human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines
    • Galway AB, Hsueh AJ, Keene JL, et al. In vitro and in vivo bioactivity of recombinant human follicle-stimulating hormone and partially deglycosylated variants secreted by transfected eukaryotic cell lines. Endocrinology 1990; 127 (1): 93-100
    • (1990) Endocrinology , vol.127 , Issue.1 , pp. 93-100
    • Galway, A.B.1    Hsueh, A.J.2    Keene, J.L.3
  • 170
    • 0023906725 scopus 로고
    • Biochemical determinants of clearance of tissue-type plasminogen activator from the circulation
    • Lucore CL, Fry ET, Nachowiak DA, et al. Biochemical determinants of clearance of tissue-type plasminogen activator from the circulation. Circulation 1988; 77 (4): 906-914
    • (1988) Circulation , vol.77 , Issue.4 , pp. 906-914
    • Lucore, C.L.1    Fry, E.T.2    Nachowiak, D.A.3
  • 171
    • 0023595330 scopus 로고
    • Glycosylation of human fibrinogen and fibrin in vitro: Its consequences on the properties of fibrin (ogen)
    • Mirshahi M, Soria J, Soria C, et al. Glycosylation of human fibrinogen and fibrin in vitro: its consequences on the properties of fibrin (ogen). Thromb Res 1987; 48 (3): 279-289
    • (1987) Thromb Res , vol.48 , Issue.3 , pp. 279-289
    • Mirshahi, M.1    Soria, J.2    Soria, C.3
  • 172
    • 10044237889 scopus 로고    scopus 로고
    • Control of rHuEPO biological activity: The role of carbohydrate
    • Elliott S, Egrie J, Browne J, et al. Control of rHuEPO biological activity: the role of carbohydrate. Exp Hematol 2004; 32 (12): 1146-1155
    • (2004) Exp Hematol , vol.32 , Issue.12 , pp. 1146-1155
    • Elliott, S.1    Egrie, J.2    Browne, J.3
  • 173
    • 0030309183 scopus 로고    scopus 로고
    • Opioid receptor affinity and analgesic activity of O- and C-glycosylated opioid peptides
    • Negri L, Melchiorri P, Rocchi R, et al. Opioid receptor affinity and analgesic activity of O- and C-glycosylated opioid peptides. Acta Physiol Hung 1996; 84 (4): 441-443
    • (1996) Acta Physiol Hung , vol.84 , Issue.4 , pp. 441-443
    • Negri, L.1    Melchiorri, P.2    Rocchi, R.3
  • 174
    • 55749111387 scopus 로고    scopus 로고
    • The pharmacology of PEGylation: Balancing PD with PK to generate novel therapeutics
    • Fishburn CS. The pharmacology of PEGylation: balancing PD with PK to generate novel therapeutics. J Pharm Sci 2008; 97 (10): 4167-4183
    • (2008) J Pharm Sci , vol.97 , Issue.10 , pp. 4167-4183
    • Fishburn, C.S.1
  • 175
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju TS. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr Opin Immunol 2008; 20 (4): 471-478
    • (2008) Curr Opin Immunol , vol.20 , Issue.4 , pp. 471-478
    • Raju, T.S.1
  • 176
    • 63449138097 scopus 로고    scopus 로고
    • Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions
    • Crispin M, Bowden TA, Coles CH, et al. Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions. J Mol Biol 2009; 387 (5): 1061-1066
    • (2009) J Mol Biol , vol.387 , Issue.5 , pp. 1061-1066
    • Crispin, M.1    Bowden, T.A.2    Coles, C.H.3
  • 178
    • 66149092757 scopus 로고    scopus 로고
    • Agalsidase alfa for the treatment of Fabry disease: New data on clinical efficacy and safety
    • Beck M. Agalsidase alfa for the treatment of Fabry disease: new data on clinical efficacy and safety. Expert Opin Biol Ther 2009; 9 (2): 255-261
    • (2009) Expert Opin Biol Ther , vol.9 , Issue.2 , pp. 255-261
    • Beck, M.1
  • 179
    • 0013192938 scopus 로고    scopus 로고
    • A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease
    • LeeK, Jin X, ZhangK, et al.A biochemical and pharmacological comparison of enzyme replacement therapies for the glycolipid storage disorder Fabry disease. Glycobiology 2003; 13 (4): 305-313
    • (2003) Glycobiology , vol.13 , Issue.4 , pp. 305-313
    • Lee, K.1    Jin, X.2    Zhang, K.3
  • 180
    • 34547097519 scopus 로고    scopus 로고
    • Spotlight on agalsidase beta in Fabry disease
    • Keating GM, Simpson D. Spotlight on agalsidase beta in Fabry disease. Biodrugs 2007; 21 (4): 269-271
    • (2007) Biodrugs , vol.21 , Issue.4 , pp. 269-271
    • Keating, G.M.1    Simpson, D.2
  • 181
    • 33947316741 scopus 로고    scopus 로고
    • Agalsidase beta: A review of its use in the management of Fabry disease
    • DOI 10.2165/00003495-200767030-00007
    • Keating GM, Simpson D. Agalsidase beta: a review of its use in the management of Fabry disease. Drugs 2007; 67 (3): 435-455 (Pubitemid 46437099)
    • (2007) Drugs , vol.67 , Issue.3 , pp. 435-455
    • Keating, G.M.1    Simpson, D.2
  • 183
    • 0025918707 scopus 로고
    • Structures and functional roles of the sugar chains of human erythropoietins
    • Takeuchi M, Kobata A. Structures and functional roles of the sugar chains of human erythropoietins. Glycobiology 1991; 1 (4): 337-346
    • (1991) Glycobiology , vol.1 , Issue.4 , pp. 337-346
    • Takeuchi, M.1    Kobata, A.2
  • 184
    • 6344240488 scopus 로고    scopus 로고
    • Long-acting follicle-stimulating hormone analogs containing N-linked glycosylation exhibited increased bioactivity compared with o-linked analogs in female rats
    • Weenen C, Pena JE, Pollak SV, et al. Long-acting follicle-stimulating hormone analogs containing N-linked glycosylation exhibited increased bioactivity compared with o-linked analogs in female rats. J Clin Endocrinol Metab 2004; 89 (10): 5204-5212
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.10 , pp. 5204-5212
    • Weenen, C.1    Pena, J.E.2    Pollak, S.V.3
  • 185
    • 0035961977 scopus 로고    scopus 로고
    • Human FSH isoforms: Carbohydrate complexity as determinant of in-vitro bioactivity
    • Creus S, Chaia Z, Pellizzari EH, et al. Human FSH isoforms: carbohydrate complexity as determinant of in-vitro bioactivity. Mol Cell Endocrinol 2001; 174 (1-2): 41-49
    • (2001) Mol Cell Endocrinol , vol.174 , Issue.1-2 , pp. 41-49
    • Creus, S.1    Chaia, Z.2    Pellizzari, E.H.3
  • 186
    • 0031931057 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic interactions between recombinant human luteinizing hormone and recombinant human follicle-stimulating hormone
    • DOI 10.1016/S0015-0282(97)00503-7, PII S0015028297005037
    • le Cotonnec JY, Loumaye E, Porchet HC, et al. Pharmacokinetic and pharmacodynamic interactions between recombinant human luteinizing hormone and recombinant human follicle-stimulating hormone. Fertil Steril 1998; 69 (2): 201-209 (Pubitemid 28117094)
    • (1998) Fertility and Sterility , vol.69 , Issue.2 , pp. 201-209
    • Le Cotonnec, J.-Y.1    Loumaye, E.2    Porchet, H.C.3    Beltrami, V.4    Munafo, A.5
  • 187
    • 0031907479 scopus 로고    scopus 로고
    • Clinical pharmacology of recombinant human luteinizing hormone, part II: Bioavailability of recombinant human luteinizing hormone assessed with an immunoassay and an in vitro bioassay
    • le Cotonnec JY, Porchet HC, Beltrami V, et al. Clinical pharmacology of recombinant human luteinizing hormone, part II: bioavailability of recombinant human luteinizing hormone assessed with an immunoassay and an in vitro bioassay. Fertil Steril 1998; 69 (2): 195-200
    • (1998) Fertil Steril , vol.69 , Issue.2 , pp. 195-200
    • Le Cotonnec, J.Y.1    Porchet, H.C.2    Beltrami, V.3
  • 188
    • 0031906425 scopus 로고    scopus 로고
    • Clinical pharmacology of recombinant human luteinizing hormone, part I: Pharmacokinetics after intravenous administration to healthy female volunteers and comparison with urinary human luteinizing hormone
    • le Cotonnec JY, Porchet HC, Beltrami V, et al. Clinical pharmacology of recombinant human luteinizing hormone, part I: pharmacokinetics after intravenous administration to healthy female volunteers and comparison with urinary human luteinizing hormone. Fertil Steril 1998; 69 (2): 189-194
    • (1998) Fertil Steril , vol.69 , Issue.2 , pp. 189-194
    • Le Cotonnec, J.Y.1    Porchet, H.C.2    Beltrami, V.3
  • 189
    • 4344574965 scopus 로고    scopus 로고
    • Fast renal trapping of porcine luteinizing hormone (pLH) shown by 123I-scintigraphic imaging in rats explains its short circulatory half-life
    • Klett D, Bernard S, Lecompte F, et al. Fast renal trapping of porcine luteinizing hormone (pLH) shown by 123I-scintigraphic imaging in rats explains its short circulatory half-life. Reprod Biol Endocrinol 2003; 1: 64
    • (2003) Reprod Biol Endocrinol , vol.1 , pp. 64
    • Klett, D.1    Bernard, S.2    Lecompte, F.3
  • 190
    • 47349088932 scopus 로고    scopus 로고
    • Lutropin alfa
    • Dhillon S, Keating GM. Lutropin alfa. Drugs 2008; 68 (11): 1529-1540
    • (2008) Drugs , vol.68 , Issue.11 , pp. 1529-1540
    • Dhillon, S.1    Keating, G.M.2
  • 191
    • 0026585325 scopus 로고
    • Circulatory half-life but not interaction with the lutropin/chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharides
    • Baenziger JU, Kumar S, Brodbeck RM, et al. Circulatory half-life but not interaction with the lutropin/chorionic gonadotropin receptor is modulated by sulfation of bovine lutropin oligosaccharides. Proc Natl Acad Sci U S A 1992; 89 (1): 334-338
    • (1992) Proc Natl Acad Sci U S A , vol.89 , Issue.1 , pp. 334-338
    • Baenziger, J.U.1    Kumar, S.2    Brodbeck, R.M.3
  • 192
    • 0025632985 scopus 로고
    • Recombinant latent transforming growth factor beta 1 has a longer plasma half-life in rats than active transforming growth factor beta 1, and a different tissue distribution
    • Wakefield LM, Winokur TS, Hollands RS, et al. Recombinant latent transforming growth factor beta 1 has a longer plasma half-life in rats than active transforming growth factor beta 1, and a different tissue distribution. J Clin Invest 1990; 86 (6): 1976-1984
    • (1990) J Clin Invest , vol.86 , Issue.6 , pp. 1976-1984
    • Wakefield, L.M.1    Winokur, T.S.2    Hollands, R.S.3
  • 193
    • 0032465272 scopus 로고    scopus 로고
    • Glycosylated and non-glycosylated recombinant human granulocyte colony-stimulating factor (rhG-CSF): What is the difference?
    • Hoglund M. Glycosylated and non-glycosylated recombinant human granulocyte colony-stimulating factor (rhG-CSF): what is the difference? Med Oncol 1998; 15 (4): 229-233
    • (1998) Med Oncol , vol.15 , Issue.4 , pp. 229-233
    • Hoglund, M.1
  • 194
    • 0027398663 scopus 로고
    • Comparative pharmacokinetics of single-dose administration of mammalian and bacterially-derived recombinant human granulocyte-macrophage colony-stimulating factor
    • Hovgaard D, Mortensen BT, Schifter S, et al. Comparative pharmacokinetics of single-dose administration of mammalian and bacterially-derived recombinant human granulocyte-macrophage colony-stimulating factor. Eur J Haematol 1993; 50 (1): 32-36
    • (1993) Eur J Haematol , vol.50 , Issue.1 , pp. 32-36
    • Hovgaard, D.1    Mortensen, B.T.2    Schifter, S.3
  • 195
    • 0036534028 scopus 로고    scopus 로고
    • Clinical applications of colony-stimulating factors: A historical perspective
    • Sylvester RK. Clinical applications of colony-stimulating factors: a historical perspective. Am J Health Syst Pharm 2002; 59 (7 Suppl. 2): S6-12
    • (2002) Am J Health Syst Pharm , vol.59 , Issue.7 SUPPL. 2
    • Sylvester, R.K.1
  • 196
    • 0027942320 scopus 로고
    • Carbohydrate does not modulate the in vivo effects of injected interleukin-3
    • Ziltener HJ, Clark-Lewis I, Jones AT, et al. Carbohydrate does not modulate the in vivo effects of injected interleukin-3. Exp Hematol 1994; 22 (11): 1070-1075
    • (1994) Exp Hematol , vol.22 , Issue.11 , pp. 1070-1075
    • Ziltener, H.J.1    Clark-Lewis, I.2    Jones, A.T.3
  • 197
    • 0027181195 scopus 로고
    • N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: The functional role of carbohydrate as to its lectin-like character and clearance velocity
    • Fukushima K, Watanabe H, Takeo K, et al. N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity. Arch Biochem Biophys 1993; 304 (1): 144-153
    • (1993) Arch Biochem Biophys , vol.304 , Issue.1 , pp. 144-153
    • Fukushima, K.1    Watanabe, H.2    Takeo, K.3
  • 198
    • 0019364614 scopus 로고
    • The role of sialic acid in the functional activity and the hepatic clearance of C1-INH
    • Minta JO. The role of sialic acid in the functional activity and the hepatic clearance of C1-INH. J Immunol 1981; 126 (1): 245-249
    • (1981) J Immunol , vol.126 , Issue.1 , pp. 245-249
    • Minta, J.O.1
  • 199
    • 40049100471 scopus 로고    scopus 로고
    • Rhucin, a recombinant C1 inhibitor for the treatment of hereditary angioedema and cerebral ischemia
    • Longhurst H. Rhucin, a recombinant C1 inhibitor for the treatment of hereditary angioedema and cerebral ischemia. Curr Opin Investig Drugs 2008; 9 (3): 310-323
    • (2008) Curr Opin Investig Drugs , vol.9 , Issue.3 , pp. 310-323
    • Longhurst, H.1
  • 200
    • 25844432828 scopus 로고    scopus 로고
    • A phase i study of recombinant human C1 inhibitor in asymptomatic patients with hereditary angioedema
    • van Doorn MB, Burggraaf J, van Dam T, et al. A phase I study of recombinant human C1 inhibitor in asymptomatic patients with hereditary angioedema. J Allergy Clin Immunol 2005; 116 (4): 876-883
    • (2005) J Allergy Clin Immunol , vol.116 , Issue.4 , pp. 876-883
    • Van Doorn, M.B.1    Burggraaf, J.2    Van Dam, T.3
  • 201
    • 31744447070 scopus 로고    scopus 로고
    • Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain
    • Raju TS, Scallon BJ. Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain. Biochem Biophys Res Commun 2006; 341 (3): 797-803
    • (2006) Biochem Biophys Res Commun , vol.341 , Issue.3 , pp. 797-803
    • Raju, T.S.1    Scallon, B.J.2
  • 202
    • 45749158577 scopus 로고    scopus 로고
    • The function of the human interferon-beta 1a glycan determined in vivo
    • Dissing-Olesen L, Thaysen-Andersen M, Meldgaard M, et al. The function of the human interferon-beta 1a glycan determined in vivo. J Pharmacol Exp Ther 2008; 326 (1): 338-347
    • (2008) J Pharmacol Exp Ther , vol.326 , Issue.1 , pp. 338-347
    • Dissing-Olesen, L.1    Thaysen-Andersen, M.2    Meldgaard, M.3
  • 203
    • 0020630652 scopus 로고
    • Renal metabolism of homologous serum interferon
    • Bocci V, Di Francesco P, Pacini A, et al. Renal metabolism of homologous serum interferon. Antiviral Res 1983; 3 (1): 53-58
    • (1983) Antiviral Res , vol.3 , Issue.1 , pp. 53-58
    • Bocci, V.1    Di Francesco, P.2    Pacini, A.3
  • 204
    • 0032522258 scopus 로고    scopus 로고
    • Functional consequences of mutations in Ser-52 and Ser-60 in human blood coagulation factor VII
    • IinoM, Foster DC, Kisiel W. Functional consequences of mutations in Ser-52 and Ser-60 in human blood coagulation factor VII. Arch Biochem Biophys 1998; 352 (2): 182-192
    • (1998) Arch Biochem Biophys , vol.352 , Issue.2 , pp. 182-192
    • Iino, M.1    Foster, D.C.2    Kisiel, W.3
  • 205
    • 53549092514 scopus 로고    scopus 로고
    • Extending half-life in coagulation factors: Where do we stand?
    • Lillicrap D. Extending half-life in coagulation factors: where do we stand? Thromb Res 2008; 122 Suppl. 4: S2-8
    • (2008) Thromb Res , vol.122 , Issue.SUPPL. 4
    • Lillicrap, D.1
  • 206
    • 0037757532 scopus 로고    scopus 로고
    • Polysialylated insulin: Synthesis, characterization and biological activity in vivo
    • Jain S, Hreczuk-Hirst DH, McCormack B, et al. Polysialylated insulin: synthesis, characterization and biological activity in vivo. Biochim Biophys Acta 2003; 1622 (1): 42-49
    • (2003) Biochim Biophys Acta , vol.1622 , Issue.1 , pp. 42-49
    • Jain, S.1    Hreczuk-Hirst, D.H.2    McCormack, B.3
  • 208
    • 0034490003 scopus 로고    scopus 로고
    • Polysialic acids: Potential in improving the stability and pharmacokinetics of proteins and other therapeutics
    • Gregoriadis G, Fernandes A, Mital M, et al. Polysialic acids: potential in improving the stability and pharmacokinetics of proteins and other therapeutics. Cell Mol Life Sci 2000; 57 (13-14): 1964-1969
    • (2000) Cell Mol Life Sci , vol.57 , Issue.13-14 , pp. 1964-1969
    • Gregoriadis, G.1    Fernandes, A.2    Mital, M.3
  • 209
    • 43149096504 scopus 로고    scopus 로고
    • N-glycosylation as novel strategy to improve pharmacokinetic properties of bispecific single-chain diabodies
    • Stork R, Zettlitz KA, Muller D, et al. N-glycosylation as novel strategy to improve pharmacokinetic properties of bispecific single-chain diabodies. J Biol Chem 2008; 283 (12): 7804-7812
    • (2008) J Biol Chem , vol.283 , Issue.12 , pp. 7804-7812
    • Stork, R.1    Zettlitz, K.A.2    Muller, D.3
  • 210
    • 0030835335 scopus 로고    scopus 로고
    • Polysialylated asparaginase: Preparation, activity and pharmacokinetics
    • Fernandes AI, Gregoriadis G. Polysialylated asparaginase: preparation, activity and pharmacokinetics. Biochim Biophys Acta 1997; 1341 (1): 26-34
    • (1997) Biochim Biophys Acta , vol.1341 , Issue.1 , pp. 26-34
    • Fernandes, A.I.1    Gregoriadis, G.2
  • 211
    • 0035901757 scopus 로고    scopus 로고
    • The effect of polysialylation on the immunogenicity and antigenicity of asparaginase: Implication in its pharmacokinetics
    • Fernandes AI, Gregoriadis G. The effect of polysialylation on the immunogenicity and antigenicity of asparaginase: implication in its pharmacokinetics. Int J Pharm 2001; 217 (1-2): 215-224
    • (2001) Int J Pharm , vol.217 , Issue.1-2 , pp. 215-224
    • Fernandes, A.I.1    Gregoriadis, G.2
  • 212
    • 0036865723 scopus 로고    scopus 로고
    • The enigma of the metabolic fate of circulating erythropoietin (Epo) in view of the pharmacokinetics of the recombinant drugs rhEpo and NESP
    • Jelkmann W. The enigma of the metabolic fate of circulating erythropoietin (Epo) in view of the pharmacokinetics of the recombinant drugs rhEpo and NESP. Eur J Haematol 2002; 69 (5-6): 265-274
    • (2002) Eur J Haematol , vol.69 , Issue.5-6 , pp. 265-274
    • Jelkmann, W.1
  • 213
    • 0037384789 scopus 로고    scopus 로고
    • Darbepoetin alfa has a longer circulating half-life and greater in vivo potency than recombinant human erythropoietin
    • Egrie JC, Dwyer E, Browne JK, et al. Darbepoetin alfa has a longer circulating half-life and greater in vivo potency than recombinant human erythropoietin. Exp Hematol 2003; 31 (4): 290-299
    • (2003) Exp Hematol , vol.31 , Issue.4 , pp. 290-299
    • Egrie, J.C.1    Dwyer, E.2    Browne, J.K.3
  • 214
    • 33644867127 scopus 로고    scopus 로고
    • Cellular trafficking and degradation of erythropoietin and novel erythropoiesis stimulating protein (NESP)
    • Gross AW, Lodish HF. Cellular trafficking and degradation of erythropoietin and novel erythropoiesis stimulating protein (NESP). J Biol Chem 2006; 281 (4): 2024-2032
    • (2006) J Biol Chem , vol.281 , Issue.4 , pp. 2024-2032
    • Gross, A.W.1    Lodish, H.F.2
  • 215
    • 0037111558 scopus 로고    scopus 로고
    • Recombinant human thrombopoietin: Basic biology and evaluation of clinical studies
    • Kuter DJ, Begley CG. Recombinant human thrombopoietin: basic biology and evaluation of clinical studies. Blood 2002; 100 (10): 3457-3469
    • (2002) Blood , vol.100 , Issue.10 , pp. 3457-3469
    • Kuter, D.J.1    Begley, C.G.2
  • 216
    • 17444385555 scopus 로고    scopus 로고
    • Effects of long-acting recombinant human follicle-stimulating hormone analogs containing N-linked glycosylation on murine folliculogenesis
    • Ruman JI, Pollak S, Trousdale RK, et al. Effects of long-acting recombinant human follicle-stimulating hormone analogs containing N-linked glycosylation on murine folliculogenesis. Fertil Steril 2005; 83 Suppl. 1: 1303-1309
    • (2005) Fertil Steril , vol.83 , Issue.SUPPL. 1 , pp. 1303-1309
    • Ruman, J.I.1    Pollak, S.2    Trousdale, R.K.3
  • 217
    • 57849140300 scopus 로고    scopus 로고
    • Efficacy of native and hyperglycosylated follicle-stimulating hormone analogs for promoting fertility in female mice
    • Trousdale RK, Yu B, Pollak SV, et al. Efficacy of native and hyperglycosylated follicle-stimulating hormone analogs for promoting fertility in female mice. Fertil Steril 2009; 91 (1): 265-270
    • (2009) Fertil Steril , vol.91 , Issue.1 , pp. 265-270
    • Trousdale, R.K.1    Yu, B.2    Pollak, S.V.3
  • 218
    • 64549108038 scopus 로고    scopus 로고
    • Advances in recombinant DNA technology: Corifollitropin alfa, a hybrid molecule with sustained folliclestimulating activity and reduced injection frequency
    • Fauser BC, Mannaerts BM, Devroey P, et al. Advances in recombinant DNA technology: corifollitropin alfa, a hybrid molecule with sustained folliclestimulating activity and reduced injection frequency. Hum Reprod Update 2009; 15 (3): 309-321
    • (2009) Hum Reprod Update , vol.15 , Issue.3 , pp. 309-321
    • Fauser, B.C.1    Mannaerts, B.M.2    Devroey, P.3
  • 219
    • 63849083548 scopus 로고    scopus 로고
    • Corifollitropin alfa, a long-acting follicle-stimulating hormone agonist for the treatment of infertility
    • Loutradis D, Drakakis P, Vlismas A, et al. Corifollitropin alfa, a long-acting follicle-stimulating hormone agonist for the treatment of infertility. Curr Opin Investig Drugs 2009; 10 (4): 372-380
    • (2009) Curr Opin Investig Drugs , vol.10 , Issue.4 , pp. 372-380
    • Loutradis, D.1    Drakakis, P.2    Vlismas, A.3
  • 220
    • 10344231983 scopus 로고    scopus 로고
    • Pharmacodynamics of a single low dose of long-acting recombinant follicle-stimulating hormone (FSH-carboxy terminal peptide, corifollitropin alfa) in women with World Health Organization group II anovulatory infertility
    • Balen AH, Mulders AG, Fauser BC, et al. Pharmacodynamics of a single low dose of long-acting recombinant follicle-stimulating hormone (FSH-carboxy terminal peptide, corifollitropin alfa) in women with World Health Organization group II anovulatory infertility. J Clin Endocrinol Metab 2004; 89 (12): 6297-6304
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.12 , pp. 6297-6304
    • Balen, A.H.1    Mulders, A.G.2    Fauser, B.C.3
  • 221
    • 2442425992 scopus 로고    scopus 로고
    • Induction of multiple follicular development by a single dose of long-acting recombinant follicle-stimulating hormone (FSH-CTP, corifollitropin alfa) for controlled ovarian stimulation before in vitro fertilization
    • Devroey P, Fauser BC, Platteau P, et al. Induction of multiple follicular development by a single dose of long-acting recombinant follicle-stimulating hormone (FSH-CTP, corifollitropin alfa) for controlled ovarian stimulation before in vitro fertilization. J Clin Endocrinol Metab 2004; 89 (5): 2062-2070
    • (2004) J Clin Endocrinol Metab , vol.89 , Issue.5 , pp. 2062-2070
    • Devroey, P.1    Fauser, B.C.2    Platteau, P.3
  • 222
    • 0035988486 scopus 로고    scopus 로고
    • Single dose pharmacokinetics and effects on follicular growth and serum hormones of a long-acting recombinant FSH preparation (FSH-CTP) in healthy pituitary-suppressed females
    • Duijkers IJ, Klipping C, Boerrigter PJ, et al. Single dose pharmacokinetics and effects on follicular growth and serum hormones of a long-acting recombinant FSH preparation (FSH-CTP) in healthy pituitary-suppressed females. Hum Reprod 2002; 17 (8): 1987-1993
    • (2002) Hum Reprod , vol.17 , Issue.8 , pp. 1987-1993
    • Duijkers, I.J.1    Klipping, C.2    Boerrigter, P.J.3
  • 223
    • 0036303882 scopus 로고    scopus 로고
    • Lysosomal disorders
    • Wraith JE. Lysosomal disorders. Semin Neonatol 2002; 7 (1): 75-83
    • (2002) Semin Neonatol , vol.7 , Issue.1 , pp. 75-83
    • Wraith, J.E.1
  • 224
    • 68149132035 scopus 로고    scopus 로고
    • Glycosylation- and phosphorylationdependent intracellular transport of lysosomal hydrolases
    • Pohl S, Marschner K, Storch S, et al. Glycosylation- and phosphorylationdependent intracellular transport of lysosomal hydrolases. Biol Chem 2009; 390 (7): 521-527
    • (2009) Biol Chem , vol.390 , Issue.7 , pp. 521-527
    • Pohl, S.1    Marschner, K.2    Storch, S.3
  • 225
    • 0025365591 scopus 로고
    • Lysosomal enzyme targeting
    • Kornfeld S. Lysosomal enzyme targeting. Biochem Soc Trans 1990; 18 (3): 367-374
    • (1990) Biochem Soc Trans , vol.18 , Issue.3 , pp. 367-374
    • Kornfeld, S.1
  • 226
    • 0242524418 scopus 로고    scopus 로고
    • Enzyme therapy for lysosomal storage disease: Principles, practice, and prospects
    • Grabowski GA, Hopkin RJ. Enzyme therapy for lysosomal storage disease: principles, practice, and prospects. Annu RevGenomicsHum Genet 2003; 4: 403-436
    • (2003) Annu Rev Genomics Hum Genet , vol.4 , pp. 403-436
    • Grabowski, G.A.1    Hopkin, R.J.2
  • 227
    • 0023491490 scopus 로고
    • Lectin-specific targeting of lysosomal enzymes to reticuloendothelial cells
    • Murray GJ. Lectin-specific targeting of lysosomal enzymes to reticuloendothelial cells. Methods Enzymol 1987; 149: 25-42
    • (1987) Methods Enzymol , vol.149 , pp. 25-42
    • Murray, G.J.1
  • 228
    • 0344094038 scopus 로고
    • Evidence for receptormediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages
    • Stahl PD, Rodman JS, Miller MJ, et al. Evidence for receptormediated binding of glycoproteins, glycoconjugates, and lysosomal glycosidases by alveolar macrophages. Proc Natl Acad Sci U S A 1978; 75 (3): 1399-1403
    • (1978) Proc Natl Acad Sci U S A , vol.75 , Issue.3 , pp. 1399-1403
    • Stahl, P.D.1    Rodman, J.S.2    Miller, M.J.3
  • 229
    • 0017872552 scopus 로고
    • The uptake of native and desialylated glucocerebrosidase by rat hepatocytes and Kupffer cells
    • Furbish FS, Steer CJ, Barranger JA, et al. The uptake of native and desialylated glucocerebrosidase by rat hepatocytes and Kupffer cells. Biochem Biophys Res Commun 1978; 81 (3): 1047-1053
    • (1978) Biochem Biophys Res Commun , vol.81 , Issue.3 , pp. 1047-1053
    • Furbish, F.S.1    Steer, C.J.2    Barranger, J.A.3
  • 230
    • 0019475525 scopus 로고
    • Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation
    • Furbish FS, Steer CJ, Krett NL, et al. Uptake and distribution of placental glucocerebrosidase in rat hepatic cells and effects of sequential deglycosylation. Biochim Biophys Acta 1981; 673 (4): 425-434
    • (1981) Biochim Biophys Acta , vol.673 , Issue.4 , pp. 425-434
    • Furbish, F.S.1    Steer, C.J.2    Krett, N.L.3
  • 231
    • 0018193103 scopus 로고
    • The uptake of agalactoglucocerebrosidase by rat hepatocytes and Kupffer cells
    • Steer CJ, Furbish FS, Barranger JA, et al. The uptake of agalactoglucocerebrosidase by rat hepatocytes and Kupffer cells. FEBS Lett 1978; 91 (2): 202-205
    • (1978) FEBS Lett , vol.91 , Issue.2 , pp. 202-205
    • Steer, C.J.1    Furbish, F.S.2    Barranger, J.A.3
  • 232
    • 46749139421 scopus 로고    scopus 로고
    • Biochemical and pharmacological characterization of different recombinant acid alpha-glucosidase preparations evaluated for the treatment of Pompe disease
    • McVie-Wylie AJ, Lee KL, Qiu H, et al. Biochemical and pharmacological characterization of different recombinant acid alpha-glucosidase preparations evaluated for the treatment of Pompe disease. Mol Genet Metab 2008; 94 (4): 448-455
    • (2008) Mol Genet Metab , vol.94 , Issue.4 , pp. 448-455
    • McVie-Wylie, A.J.1    Lee, K.L.2    Qiu, H.3
  • 234
    • 0034112722 scopus 로고    scopus 로고
    • Enzyme replacement therapy in mucopolysaccharidosis I: Altered distribution and targeting of alpha-Liduronidase in immunized rats
    • Turner CT, Hopwood JJ, Brooks DA. Enzyme replacement therapy in mucopolysaccharidosis I: altered distribution and targeting of alpha-Liduronidase in immunized rats. Mol Genet Metab 2000; 69 (4): 277-285
    • (2000) Mol Genet Metab , vol.69 , Issue.4 , pp. 277-285
    • Turner, C.T.1    Hopwood, J.J.2    Brooks, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.