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Volumn 6, Issue 16, 2014, Pages 1829-1846

PEGylation and its impact on the design of new protein-based medicines

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINASE MACROGOL; CERTOLIZUMAB PEGOL; CONTINUOUS ERYTHROPOIESIS RECEPTOR ACTIVATOR; PEGADEMASE; PEGAPTANIB; PEGINTERFERON ALPHA2A; PEGINTERFERON ALPHA2B; PEGLOTICASE; PEGVISOMANT; RECOMBINANT GRANULOCYTE COLONY STIMULATING FACTOR; MACROGOL DERIVATIVE; PROTEIN;

EID: 84911920558     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.14.125     Document Type: Review
Times cited : (76)

References (179)
  • 1
    • 79955666020 scopus 로고    scopus 로고
    • Introduction to current and future protein therapeutics: A protein engineering perspective
    • Carter PJ. Introduction to current and future protein therapeutics: a protein engineering perspective. Exp. Cell Res. 317(9), 1261-1269 (2011
    • (2011) Exp. Cell Res , vol.317 , Issue.9 , pp. 1261-1269
    • Carter, P.J.1
  • 2
    • 37749004225 scopus 로고    scopus 로고
    • Protein therapeutics: A summary and pharmacological classification
    • Leader B, Baca QJ, Golan DE. Protein therapeutics: a summary and pharmacological classification. Nat. Rev. Drug Discov. 7(1), 21-39 (2008
    • (2008) Nat. Rev. Drug Discov , vol.7 , Issue.1 , pp. 21-39
    • Leader, B.1    Baca, Q.J.2    Golan, D.E.3
  • 3
    • 79955038892 scopus 로고    scopus 로고
    • Strategies to prolong the plasma residence time of peptide drugs
    • Pollaro L, Heinis C. Strategies to prolong the plasma residence time of peptide drugs. MedChemComm 1(5), 319 (2010
    • (2010) MedChemComm , vol.1 , Issue.5 , pp. 319
    • Pollaro, L.1    Heinis, C.2
  • 4
    • 64749101544 scopus 로고    scopus 로고
    • PEG-modified biopharmaceuticals
    • Bailon P, Won C. PEG-modified biopharmaceuticals. Expert Opin. Drug Deliv. 6(1), 1-16 (2009
    • (2009) Expert Opin. Drug Deliv , vol.6 , Issue.1 , pp. 1-16
    • Bailon, P.1    Won, C.2
  • 7
    • 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. 97(10), 4167-4183 (2008
    • (2008) J. Pharm. Sci , vol.97 , Issue.10 , pp. 4167-4183
    • Fishburn, C.S.1
  • 8
    • 56749098212 scopus 로고    scopus 로고
    • Designing PEGylated therapeutic molecules: Advantages in ADMET properties
    • Hamidi M, Rafiei P, Azadi A. Designing PEGylated therapeutic molecules: advantages in ADMET properties. Expert Opin. Drug Discov. 3(11), 1293-1307 (2008
    • (2008) Expert Opin. Drug Discov , vol.3 , Issue.11 , pp. 1293-1307
    • Hamidi, M.1    Rafiei, P.2    Azadi, A.3
  • 9
    • 0035284411 scopus 로고    scopus 로고
    • Peptide and protein PEGylation a review of problems and solutions
    • Veronese F. Peptide and protein PEGylation a review of problems and solutions. Biomaterials 22(5), 405-417 (2001
    • (2001) Biomaterials , vol.22 , Issue.5 , pp. 405-417
    • Veronese, F.1
  • 11
    • 80052908831 scopus 로고    scopus 로고
    • Product development issues for PEGylated proteins
    • Payne RW, Murphy BM, Manning MC. Product development issues for PEGylated proteins. Pharm. Dev. Technol. 16(5), 423-440 (2010
    • (2010) Pharm. Dev. Technol , vol.16 , Issue.5 , pp. 423-440
    • Payne, R.W.1    Murphy, B.M.2    Manning, M.C.3
  • 13
    • 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. 21(4), 414-421 (2003
    • (2003) Nat. Biotechnol , vol.21 , Issue.4 , pp. 414-421
    • Elliott, S.1    Lorenzini, T.2    Asher, S.3
  • 14
    • 75149183678 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins an effective strategy to optimize efficacy
    • Sola RJ, Grievenow K. Glycosylation of therapeutic proteins an effective strategy to optimize efficacy. Biodrugs 24(1), 9-21 (2010
    • (2010) Biodrugs , vol.24 , Issue.1 , pp. 9-21
    • Sola, R.J.1    Grievenow, K.2
  • 15
    • 70449732650 scopus 로고    scopus 로고
    • Pharmacological significance of glycosylation in therapeutic proteins
    • Li H, d'Anjou M. Pharmacological significance of glycosylation in therapeutic proteins. Curr. Opin. Biotech. 20(6), 678-684 (2009
    • (2009) Curr. Opin. Biotech , vol.20 , Issue.6 , pp. 678-684
    • Li, H.1    D'anjou, M.2
  • 16
    • 80052569742 scopus 로고    scopus 로고
    • Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies
    • Beck A, Reichert JM. Therapeutic Fc-fusion proteins and peptides as successful alternatives to antibodies. MAbs 3(5), 415-416 (2011
    • (2011) MAbs , vol.3 , Issue.5 , pp. 415-416
    • Beck, A.1    Reichert, J.M.2
  • 17
    • 84885370061 scopus 로고    scopus 로고
    • Albumin as a versatile platform for drug half-life extension
    • Sleep D, Cameron J, Evans LR. Albumin as a versatile platform for drug half-life extension. Biochim. Biophys. Acta 1830(12), 5526-5534 (2013
    • (2013) Biochim. Biophys. Acta , vol.1830 , Issue.12 , pp. 5526-5534
    • Sleep, D.1    Cameron, J.2    Evans, L.R.3
  • 18
    • 70350438004 scopus 로고    scopus 로고
    • The versatile MHC class I-related FcRn protects IgG and albumin from degradation: Implications for development of new diagnostics and therapeutics
    • Andersen J, Sandlie I. The versatile MHC class I-related FcRn protects IgG and albumin from degradation: implications for development of new diagnostics and therapeutics. Drug Metabol. Pharmacokinet. 24(4), 318-332 (2009
    • (2009) Drug Metabol. Pharmacokinet , vol.24 , Issue.4 , pp. 318-332
    • Andersen, J.1    Sandlie, I.2
  • 19
    • 77649253359 scopus 로고    scopus 로고
    • FcRn receptor-mediated pharmacokinetics of therapeutic IgG in the eye
    • Kim H, Robinson S, Csaky K. FcRn receptor-mediated pharmacokinetics of therapeutic IgG in the eye. Mol. Vis. 15, 2803-2812 (2009
    • (2009) Mol. Vis , vol.15 , pp. 2803-2812
    • Kim, H.1    Robinson, S.2    Csaky, K.3
  • 20
    • 65249134948 scopus 로고    scopus 로고
    • Pharmaceutically important pre-And posttranslational modifications on human serum albumin
    • Otagiri M, Chuang V. Pharmaceutically important pre-And posttranslational modifications on human serum albumin. Bio. Pharm. Bull. 32(4), 527-534 (2009
    • (2009) Bio. Pharm. Bull , vol.32 , Issue.4 , pp. 527-534
    • Otagiri, M.1    Chuang, V.2
  • 21
    • 70350018276 scopus 로고    scopus 로고
    • Biodistribution of a bispecific single-chain diabody and its half-life extended derivatives
    • Stork R, Campigna E, Robert B, Muller D, Kontermann RE. Biodistribution of a bispecific single-chain diabody and its half-life extended derivatives. J. Biol. Chem. 284(38), 25612-25619 (2009
    • (2009) J. Biol. Chem , vol.284 , Issue.38 , pp. 25612-25619
    • Stork, R.1    Campigna, E.2    Robert, B.3    Muller, D.4    Kontermann, R.E.5
  • 22
    • 0036001387 scopus 로고    scopus 로고
    • Pharmaceutical strategies utilizing recombinant human serum albumin
    • Tuan Giam Chuang V, Kragh-Hansen U, Otagiri M. Pharmaceutical strategies utilizing recombinant human serum albumin. Pharm. Res. 19(5), 569-577 (2002
    • (2002) Pharm. Res , vol.19 , Issue.5 , pp. 569-577
    • Tuan Giam Chuang, V.1    Kragh-Hansen, U.2    Otagiri, M.3
  • 23
    • 0037144397 scopus 로고    scopus 로고
    • Albumin binding as a general strategy for improving the pharmacokinetics of proteins
    • Dennis M, Zhang M, Meng Y, et al. Albumin binding as a general strategy for improving the pharmacokinetics of proteins. J. Biol. Chem. 277(38), 35035-35043 (2002
    • (2002) J. Biol. Chem , vol.277 , Issue.38 , pp. 35035-35043
    • Dennis, M.1    Zhang, M.2    Meng, Y.3
  • 24
    • 0037225719 scopus 로고    scopus 로고
    • An IFN-β-Albumin fusion protein that displays improved pharmacokinetic and pharmacodynamic properties in nonhuman primates
    • Sung C, Nardelli B, LaFleur D, et al. An IFN-β-Albumin fusion protein that displays improved pharmacokinetic and pharmacodynamic properties in nonhuman primates. J. Interferon Cytokine Res. 23(1), 25-36 (2003
    • (2003) J. Interferon Cytokine Res , vol.23 , Issue.1 , pp. 25-36
    • Sung, C.1    Nardelli, B.2    Lafleur, D.3
  • 25
    • 0036826998 scopus 로고    scopus 로고
    • Albugranin TM, a recombinant human granulocyte colony stimulating factor (G-CSF) genetically fused to recombinant human albumin induces prolonged myelopoietic effects in mice and monkeys
    • Halpern W, Riccobene T, Agostini H, et al. Albugranin TM, a recombinant human granulocyte colony stimulating factor (G-CSF) genetically fused to recombinant human albumin induces prolonged myelopoietic effects in mice and monkeys. Pharm. Res. 19(11), 1720-1729 (2002
    • (2002) Pharm. Res , vol.19 , Issue.11 , pp. 1720-1729
    • Halpern, W.1    Riccobene, T.2    Agostini, H.3
  • 27
    • 72449130972 scopus 로고    scopus 로고
    • New strategy for the extension of the serum half-life of antibody fragments
    • Trussel S, Dumelin C, Frey K, Villa A, Buller F, Neri D. New strategy for the extension of the serum half-life of antibody fragments. Bioconjug. Chem. 20, 2286-2292 (2009
    • (2009) Bioconjug. Chem , vol.20 , pp. 2286-2292
    • Trussel, S.1    Dumelin, C.2    Frey, K.3    Villa, A.4    Buller, F.5    Neri, D.6
  • 28
    • 0017701219 scopus 로고
    • Alteration of immunlogical properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • Abuchowski A, Es T, Palczuk N, Davis F. Alteration of immunlogical properties of bovine serum albumin by covalent attachment of polyethylene glycol. J. Biol. Chem. 252(11), 3578-3581 (1977
    • (1977) J. Biol. Chem , vol.252 , Issue.11 , pp. 3578-3581
    • Abuchowski, A.1    Es, T.2    Palczuk, N.3    Davis, F.4
  • 29
    • 0037124546 scopus 로고    scopus 로고
    • The orgin of pegnology
    • Davis F. The orgin of pegnology. Adv. Drug Deliv. Rev. 54, 457-458 (2002
    • (2002) Adv. Drug Deliv. Rev , vol.54 , pp. 457-458
    • Davis, F.1
  • 30
    • 0029360545 scopus 로고
    • Chemistry of poly(ethylene glycol) conjugates with biologically active molecules
    • Zalipsky S. Chemistry of poly(ethylene glycol) conjugates with biologically active molecules. Adv. Drug Deliv. Rev. 16, 157-182 (1995
    • (1995) Adv. Drug Deliv. Rev , vol.16 , pp. 157-182
    • Zalipsky, S.1
  • 33
    • 0037362655 scopus 로고    scopus 로고
    • Effect of PEGylation on pharmaceuticals
    • Harris J, Chess R. Effect of PEGylation on pharmaceuticals. Nat. Rev. Drug Dis. 2(3), 214-221 (2003
    • (2003) Nat. Rev. Drug Dis , vol.2 , Issue.3 , pp. 214-221
    • Harris, J.1    Chess, R.2
  • 34
    • 3042722268 scopus 로고    scopus 로고
    • Protein, peptide and nonpeptide drug PEGylation for therapeutic application
    • Pasut G, Guiotto A, Veronese F. Protein, peptide and nonpeptide drug PEGylation for therapeutic application. Expert Opin. Ther. Pat. 14(5), 1-36 (2004
    • (2004) Expert Opin. Ther. Pat , vol.14 , Issue.5 , pp. 1-36
    • Pasut, G.1    Guiotto, A.2    Veronese, F.3
  • 35
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese F, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov. Today 10(21), 1451-1458 (2005
    • (2005) Drug Discov. Today , vol.10 , Issue.21 , pp. 1451-1458
    • Veronese, F.1    Pasut, G.2
  • 36
    • 34547607522 scopus 로고    scopus 로고
    • Polymer-drug conjugation, recent achievements and general strategies
    • Pasut G, Veronese F. Polymer-drug conjugation, recent achievements and general strategies. Prog. Polym. Sci. 32, 933-961 (2007
    • (2007) Prog. Polym. Sci , vol.32 , pp. 933-961
    • Pasut, G.1    Veronese, F.2
  • 37
    • 27744530542 scopus 로고    scopus 로고
    • Site-specific polymer modification of therapeutic proteins
    • Kochendoerfer G. Site-specific polymer modification of therapeutic proteins. Curr. Opin. Chem. Biol. 9, 555-560 (2005
    • (2005) Curr. Opin. Chem. Biol , vol.9 , pp. 555-560
    • Kochendoerfer, G.1
  • 38
    • 44849088699 scopus 로고    scopus 로고
    • Peptide/protein-polymer conjugates: Synthetic strategies and design concepts
    • Gauthier M, Klok H. Peptide/protein-polymer conjugates: synthetic strategies and design concepts. Chem. Comm. (Camb.) 23, 2591-2611 (2008
    • (2008) Chem. Comm. (Camb , vol.23 , pp. 2591-2611
    • Gauthier, M.1    Klok, H.2
  • 39
    • 37249018985 scopus 로고    scopus 로고
    • Modern trends in polymer bioconjugates design
    • Lutz J, Borner H. Modern trends in polymer bioconjugates design. Prog. Polym. Sci. 33, 1-39 (2008
    • (2008) Prog. Polym. Sci , vol.33 , pp. 1-39
    • Lutz, J.1    Borner, H.2
  • 40
    • 33845544743 scopus 로고    scopus 로고
    • Synthesis of protein-polymer conjugates
    • Heredia K, Maynard M. Synthesis of protein-polymer conjugates. Org. Biomol. Chem. 5(1), 45-53 (2007
    • (2007) Org. Biomol. Chem , vol.5 , Issue.1 , pp. 45-53
    • Heredia, K.1    Maynard, M.2
  • 41
    • 33845938292 scopus 로고    scopus 로고
    • PEGylated proteins: Evaluation of their safety in the absence of definitive metabolism studies
    • Webster R, Didier E, Harris P, et al. PEGylated proteins: evaluation of their safety in the absence of definitive metabolism studies. Drug Metabol. Dispos. 35(1), 9-16 (2007
    • (2007) Drug Metabol. Dispos , vol.35 , Issue.1 , pp. 9-16
    • Webster, R.1    Didier, E.2    Harris, P.3
  • 42
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly (ethylene glycol)-protein conjugates
    • Caliceti P, Veronese F. Pharmacokinetic and biodistribution properties of poly (ethylene glycol)-protein conjugates. Adv. Drug Deliv. Rev. 55(10), 1261-1277 (2003
    • (2003) Adv. Drug Deliv. Rev , vol.55 , Issue.10 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.2
  • 43
    • 35648954720 scopus 로고    scopus 로고
    • Size comparison between proteins PEGylated with branched and linear poly (ethylene glycol) molecules
    • Fee C. Size comparison between proteins PEGylated with branched and linear poly (ethylene glycol) molecules. Biotechnol. Bioeng. 98(4), 725-731 (2007
    • (2007) Biotechnol. Bioeng , vol.98 , Issue.4 , pp. 725-731
    • Fee, C.1
  • 44
    • 84875614235 scopus 로고    scopus 로고
    • The site-specific TGase-mediated PEGylation of proteins occurs at flexible sites
    • Veronese FM (Ed. Birkhauser, Basel, Switzerland, 89-112
    • Fontana A Spolaore B Mero A, et al The site-specific TGase-mediated PEGylation of proteins occurs at flexible sites. In: PEGylated Protein Drugs: Basic Science and Clinical Applications. Veronese FM (Ed.). Birkhauser, Basel, Switzerland, 89-112 (2009
    • (2009) PEGylated Protein Drugs: Basic Science and Clinical Applications
    • Fontana, A.1    Spolaore, B.2    Mero, A.3
  • 45
    • 75749146715 scopus 로고    scopus 로고
    • Pegylated interferons for the treatment of chronic hepatitis C: Pharmacological and clinical differences between peginterferon-2a and peginterferon-2b
    • Foster GR Pegylated Interferons for the Treatment of Chronic Hepatitis C: Pharmacological and Clinical Differences between peginterferon-2a and peginterferon-2b. Drugs 70(2), 147-165 (2010
    • (2010) Drugs , vol.70 , Issue.2 , pp. 147-165
    • Foster, G.R.1
  • 46
    • 0037179698 scopus 로고    scopus 로고
    • Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection
    • Fried M, Shiffman M, Reddy K, et al. Peginterferon alfa-2a plus ribavirin for chronic hepatitis C virus infection. N. Engl. J. Med. 34, 975-982 (2002
    • (2002) N. Engl. J. Med , vol.34 , pp. 975-982
    • Fried, M.1    Shiffman, M.2    Reddy, K.3
  • 47
  • 48
    • 77958614232 scopus 로고    scopus 로고
    • Hepatitis C treatment: Current and future perspectives
    • Munir S, Saleem S, Idrees M, et al. Hepatitis C treatment: current and future perspectives. Virol. J. 7(1), 296-301 (2010
    • (2010) Virol. J. , vol.7 , Issue.1 , pp. 296-301
    • Munir, S.1    Saleem, S.2    Idrees, M.3
  • 49
    • 79851470805 scopus 로고    scopus 로고
    • Interferon in the treatment of chronic hepatitis C: A drug caught between past and future
    • Vezali E, Aghemo A, Colombo M. Interferon in the treatment of chronic hepatitis C: a drug caught between past and future. Expert Opin. Biol. Ther. 11 (3), 301-313 (2011
    • (2011) Expert Opin. Biol. Ther , vol.11 , Issue.3 , pp. 301-313
    • Vezali, E.1    Aghemo, A.2    Colombo, M.3
  • 50
    • 78650805298 scopus 로고    scopus 로고
    • Optimal therapy in hepatitis C virus genotypes 2 and 3 patients
    • Petta S, Craxi A. Optimal therapy in hepatitis C virus genotypes 2 and 3 patients. Liver Int. 31, 36-44 (2011
    • (2011) Liver Int , vol.31 , pp. 36-44
    • Petta, S.1    Craxi, A.2
  • 51
    • 33646154457 scopus 로고    scopus 로고
    • Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study
    • Rajan RS, Li T, Aras M, et al. Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study. Protein Sci. 15(5), 1063-1075 (2006
    • (2006) Protein Sci , vol.15 , Issue.5 , pp. 1063-1075
    • Rajan, R.S.1    Li, T.2    Aras, M.3
  • 52
    • 1542378867 scopus 로고    scopus 로고
    • Peginterferon-Alpha2a and ribavirin combination therapy in chronic hepatitis C: A randomized study of treatment duration and ribavirin dose
    • Hadziyannis S. Peginterferon-Alpha2a and ribavirin combination therapy in chronic hepatitis C: a randomized study of treatment duration and ribavirin dose. Ann. Intern. Med. 140, 346-355 (2004
    • (2004) Ann. Intern. Med , vol.140 , pp. 346-355
    • Hadziyannis, S.1
  • 53
    • 33646558624 scopus 로고    scopus 로고
    • Pharmacodynamics of PEG-IFN alpha differentiate HIV/HCV coinfected sustained virological responders from nonresponders
    • Talal AH, Ribeiro RM, Powers KA, et al. Pharmacodynamics of PEG-IFN alpha differentiate HIV/HCV coinfected sustained virological responders from nonresponders. Hepatology 43, 943-953 (2006
    • (2006) Hepatology , vol.43 , pp. 943-953
    • Talal, A.H.1    Ribeiro, R.M.2    Powers, K.A.3
  • 54
    • 70349242026 scopus 로고    scopus 로고
    • Peginterferon alpha-2a (40 kDa) and ribavirin: Comparable rates of sustained virological response in subsets of older and younger HCV genotype 1 patients
    • Reddy KR, Messinger D, Popescu M, Hadziyannis SJ. Peginterferon alpha-2a (40 kDa) and ribavirin: comparable rates of sustained virological response in subsets of older and younger HCV genotype 1 patients. J. Viral Hepat. 16(10), 724-731 (2009
    • (2009) J. Viral Hepat , vol.16 , Issue.10 , pp. 724-731
    • Reddy, K.R.1    Messinger, D.2    Popescu, M.3    Hadziyannis, S.J.4
  • 55
    • 18244377180 scopus 로고    scopus 로고
    • Structural and biologic characterization of pegylated recombinant ifn-Alpha2b
    • Grace M, Youngster S, Gitlin G, et al. Structural and biologic characterization of pegylated recombinant IFN-Alpha2b. J. Interferon Cytokine Res. 21(12), 1103-1115 (2001
    • (2001) J Interferon Cytokine Res , vol.21 , Issue.12 , pp. 1103-1115
    • Grace, M.1    Youngster, S.2    Gitlin, G.3
  • 56
    • 0033055121 scopus 로고    scopus 로고
    • Isolation, characterization, and stability of positional isomers of mono-PEGylated salmon calcitonins
    • Lee K, Moon S, Park M, et al. Isolation, characterization, and stability of positional isomers of mono-PEGylated salmon calcitonins. Pharm. Res. 16(6), 813-818 (1999
    • (1999) Pharm. Res , vol.16 , Issue.6 , pp. 813-818
    • Lee, K.1    Moon, S.2    Park, M.3
  • 57
    • 84875948110 scopus 로고    scopus 로고
    • PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion assembly, and fibronectin fibrillogenesis
    • Zhang C, Hekmatfar S, Ramanathan A, Karuri NW. PEGylated human plasma fibronectin is proteolytically stable, supports cell adhesion, cell migration, focal adhesion assembly, and fibronectin fibrillogenesis. Biotechnol. Prog. 29(2), 493-504 (2013
    • (2013) Biotechnol. Prog , vol.29 , Issue.2 , pp. 493-504
    • Zhang, C.1    Hekmatfar, S.2    Ramanathan, A.3    Karuri, N.W.4
  • 58
    • 0025784230 scopus 로고
    • Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol
    • Hershfield MS, Chaffee S, Koro-Johnson L, Mary A, Smith AA, Short SA. Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc. Natl Acad. Sci. USA 88(16), 7185-7189 (1991
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.16 , pp. 7185-7189
    • Hershfield, M.S.1    Chaffee, S.2    Koro-Johnson, L.3    Mary, A.4    Smith, A.A.5    Short, S.A.6
  • 59
    • 77953542643 scopus 로고    scopus 로고
    • Infliximab-related hepatitis: Discussion of a case and review of the literature
    • Mancini S, Amorotti E, Vecchio S, Ponz De Leon M, Roncucci L. Infliximab-related hepatitis: discussion of a case and review of the literature. Intern Emerg. Med. 5(3), 193-200 (2010
    • (2010) Intern Emerg. Med , vol.5 , Issue.3 , pp. 193-200
    • Mancini, S.1    Amorotti, E.2    Vecchio, S.3    Ponz De Leon, M.4    Roncucci, L.5
  • 60
    • 54349091558 scopus 로고    scopus 로고
    • Safety-related regulatory actions for biologicals approved in the united states and the european union
    • Giezen T, Mantel-Teeuwisse A, Straus S, Schellekens H, Leufkens H, Egberts A. Safety-related regulatory actions for biologicals approved in the United States and the European Union. JAMA 300(16), 1887-1896 (2008
    • (2008) JAMA , vol.300 , Issue.16 , pp. 1887-1896
    • Giezen, T.1    Mantel-Teeuwisse, A.2    Straus, S.3    Schellekens, H.4    Leufkens, H.5    Egberts, A.6
  • 61
    • 78650543555 scopus 로고    scopus 로고
    • Impact of product-related factors on immunogenicity of biotherapeutics
    • Singh SK. Impact of product-related factors on immunogenicity of biotherapeutics. J. Pharm. Sci. 100(2), 354-387 (2011
    • (2011) J. Pharm. Sci , vol.100 , Issue.2 , pp. 354-387
    • Singh, S.K.1
  • 62
    • 0025019752 scopus 로고
    • The clinical efficacy of poly(ethylene glycol) modified proteins
    • Fuertges F, Abuchowski A. The clinical efficacy of poly(ethylene glycol) modified proteins. J. Cont. Rel. 11, 139-148 (1990
    • (1990) J. Cont. Rel , vol.11 , pp. 139-148
    • Fuertges, F.1    Abuchowski, A.2
  • 63
    • 0037124398 scopus 로고    scopus 로고
    • Structural and biological characterization of pegylated recombinant interferon alpha-2b and its therapeutic implications
    • Wang Y, Youngster S, Grace M, Bausch J, Wyss DF. Structural and biological characterization of pegylated recombinant interferon alpha-2b and its therapeutic implications. Adv. Drug Deliv. Rev. 54, 547-570 (2002
    • (2002) Adv. Drug Deliv. Rev , vol.54 , pp. 547-570
    • Wang, Y.1    Youngster, S.2    Grace, M.3    Bausch, J.4    Wyss, D.F.5
  • 64
    • 36549004553 scopus 로고    scopus 로고
    • Anti-cancer peg-enzymes 30 years old, but still a current approach
    • Pasut G, Sergi M, Veronese F. Anti-cancer PEG-enzymes: 30 years old, but still a current approach. Adv. Drug Deliv. Rev. 60, 69-78 (2008
    • (2008) Adv. Drug Deliv. Rev , vol.60 , pp. 69-78
    • Pasut, G.1    Sergi, M.2    Veronese, F.3
  • 65
    • 36549084078 scopus 로고    scopus 로고
    • Formulation of neulasta (pegfilgrastim
    • Piedmonte D, Treuheit M. Formulation of Neulasta (pegfilgrastim). Adv. Drug Deliv. Rev. 60, 50-58 (2008
    • (2008) Adv. Drug Deliv. Rev , vol.60 , pp. 50-58
    • Piedmonte, D.1    Treuheit, M.2
  • 66
    • 36549089052 scopus 로고    scopus 로고
    • PEG-uricase in the management of treatment-resistant gout and hyperuricemia
    • Sherman M, Saifer M, Ruiz F. PEG-uricase in the management of treatment-resistant gout and hyperuricemia. Adv. Drug Deliv. Rev. 60, 59-68 (2008
    • (2008) Adv. Drug Deliv. Rev , vol.60 , pp. 59-68
    • Sherman, M.1    Saifer, M.2    Ruiz, F.3
  • 67
    • 34249317587 scopus 로고    scopus 로고
    • Toxicity and hemodynamic effects after single dose administration of MalPEG-hemoglobin (MP4) in rhesus monkeys
    • Young M, Malavalli A, Winslow N, Candegriff K, Winslow R. Toxicity and hemodynamic effects after single dose administration of MalPEG-hemoglobin (MP4) in rhesus monkeys. Transl. Res. 149(6), 333-342 (2007
    • (2007) Transl. Res , vol.149 , Issue.6 , pp. 333-342
    • Young, M.1    Malavalli, A.2    Winslow, N.3    Candegriff, K.4    Winslow, R.5
  • 68
    • 0031946518 scopus 로고    scopus 로고
    • Short communication: Renal tubular vacuolation in animals treated with polyethylene-glycol-conjugated proteins
    • Bendele A, Seely J, Richey C, Sennello G, Shopp G. Short communication: renal tubular vacuolation in animals treated with polyethylene-glycol-conjugated proteins. Toxicol. Sci. 42(2), 152-157 (1998
    • (1998) Toxicol. Sci , vol.42 , Issue.2 , pp. 152-157
    • Bendele, A.1    Seely, J.2    Richey, C.3    Sennello, G.4    Shopp, G.5
  • 69
    • 34447523749 scopus 로고    scopus 로고
    • Certolizumab Pegol for the treatment of Crohn's disease
    • Sandborn W, Feagan B, Stoinov S, et al. Certolizumab Pegol for the treatment of Crohn's disease. N. Engl. J. Med. 357(3), 228-238 (2007
    • (2007) N. Engl. J. Med , vol.357 , Issue.3 , pp. 228-238
    • Sandborn, W.1    Feagan, B.2    Stoinov, S.3
  • 70
    • 84911913550 scopus 로고    scopus 로고
    • CimziaR, package insertLondon, UK
    • CimziaR, package insert. UCB, London, UK (2008
    • (2008) UCB
  • 71
  • 72
    • 33847392443 scopus 로고    scopus 로고
    • Clinical pharmacodynamic effects of the growth hormone receptor antagonish Pegvisomant: Implications for cancer therapy
    • Yin D, Vreeland F, Schaaf L, Millham R, Duncan B, Sharma A. Clinical pharmacodynamic effects of the growth hormone receptor antagonish Pegvisomant: implications for cancer therapy. Clin. Cancer Res. 13(3), 1000-1009 (2007
    • (2007) Clin. Cancer Res , vol.13 , Issue.3 , pp. 1000-1009
    • Yin, D.1    Vreeland, F.2    Schaaf, L.3    Millham, R.4    Duncan, B.5    Sharma, A.6
  • 73
    • 27544496736 scopus 로고    scopus 로고
    • Protein PEGylation decreases observed target association rates via a dual blocking mechanism
    • Kubetzko S, Sarkar C, Pluckthun A. Protein PEGylation decreases observed target association rates via a dual blocking mechanism. Mol. Pharmacol. 68, 1439-1454 (2005
    • (2005) Mol. Pharmacol , vol.68 , pp. 1439-1454
    • Kubetzko, S.1    Sarkar, C.2    Pluckthun, A.3
  • 74
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • Veronese F, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov. Today 10(21), 1451-1458 (2005
    • (2005) Drug Discov. Today , vol.10 , Issue.21 , pp. 1451-1458
    • Veronese, F.1    Pasut, G.2
  • 75
    • 3042722268 scopus 로고    scopus 로고
    • Protein, peptide and nonpeptide drug PEGylation for therapeutic application
    • Pasut G, Guiotto A, Veronese F. Protein, peptide and nonpeptide drug PEGylation for therapeutic application. Expert Opin. Ther. Pat. 14(5), 1-36 (2004
    • (2004) Expert Opin. Ther. Pat , vol.14 , Issue.5 , pp. 1-36
    • Pasut, G.1    Guiotto, A.2    Veronese, F.3
  • 76
    • 0025701741 scopus 로고
    • Proton NMR characterization of poly(ethylene glycols) and derivatives
    • Dust JM, Fang ZH, Harris JM. Proton NMR characterization of poly(ethylene glycols) and derivatives. Macromolecules 23(16), 3742-3746 (1990
    • (1990) Macromolecules , vol.23 , Issue.16 , pp. 3742-3746
    • Dust, J.M.1    Fang, Z.H.2    Harris, J.M.3
  • 77
    • 54349121309 scopus 로고    scopus 로고
    • Size of pegylated protein conjugates studied by various methods
    • Kusterle M, Jevševar S, Porekar VG. Size of pegylated protein conjugates studied by various methods. Acta Chem. Slov. 55, 594-601 (2008
    • (2008) Acta Chem. Slov , vol.55 , pp. 594-601
    • Kusterle, M.1    Jevševar, S.2    Porekar, V.G.3
  • 78
    • 0031193807 scopus 로고    scopus 로고
    • Branched and linear Poly(ethylene glycol): Influence of the polymer structure on enzymological, pharmacokinetic, and immunological properties of protein conjugates
    • Veronese FM, Caliceti P, Schiavon O. Branched and linear Poly(ethylene glycol): influence of the polymer structure on enzymological, pharmacokinetic, and immunological properties of protein conjugates. J. Bioact. Compat. Polym. 12, 196-207 (1997
    • (1997) J. Bioact. Compat. Polym , vol.12 , pp. 196-207
    • Veronese, F.M.1    Caliceti, P.2    Schiavon, O.3
  • 80
    • 9244221679 scopus 로고    scopus 로고
    • Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins
    • Fee CJ, Van Alstine JM. Prediction of the viscosity radius and the size exclusion chromatography behavior of PEGylated proteins. Bioconjug. Chem. 15(6), 1304-1313 (2004
    • (2004) Bioconjug. Chem , vol.15 , Issue.6 , pp. 1304-1313
    • Fee, C.J.1    Van Alstine, J.M.2
  • 81
    • 75749146715 scopus 로고    scopus 로고
    • Pegylated interferons for the treatment of chronic hepatitis C: Pharmacological and clinical differences between peginterferon-2a and peginterferon-2b
    • Foster GR Pegylated Interferons for the Treatment of Chronic Hepatitis C: Pharmacological and Clinical Differences between peginterferon-2a and peginterferon-2b. Drugs 70(2), 147-165 (2010
    • (2010) Drugs , vol.70 , Issue.2 , pp. 147-165
    • Foster, G.R.1
  • 84
    • 38949169818 scopus 로고    scopus 로고
    • Enhanced circulating half-life and antitumor activity of a site-specific pegylated interferon-α protein therapeutic
    • Bell S, Fam C, Chlipala E, et al. Enhanced circulating half-life and antitumor activity of a site-specific pegylated interferon-α protein therapeutic. Bioconjug. Chem. 19(1), 299-305 (2008
    • (2008) Bioconjug. Chem , vol.19 , Issue.1 , pp. 299-305
    • Bell, S.1    Fam, C.2    Chlipala, E.3
  • 85
    • 79952450902 scopus 로고    scopus 로고
    • Kinetic and stoichiometric analysis of the modification process for N-Terminal PEGylation of staphylokinase
    • Wang J, Hu T, Liu Y, Zhang G, Ma G, Su Z. Kinetic and stoichiometric analysis of the modification process for N-Terminal PEGylation of staphylokinase. Anal. Biochem. 412(1), 114-116 (2011
    • (2011) Anal. Biochem , vol.412 , Issue.1 , pp. 114-116
    • Wang, J.1    Hu, T.2    Liu, Y.3    Zhang, G.4    Ma, G.5    Su, Z.6
  • 86
    • 0242584999 scopus 로고    scopus 로고
    • N-Terminal site-specific mono-PEGylation of epidermal growth factor
    • Lee H, Jang IH, Ryu SH, Park TG. N-Terminal site-specific mono-PEGylation of epidermal growth factor. Pharm. Res. 20(5), 818-825 (2003
    • (2003) Pharm. Res , vol.20 , Issue.5 , pp. 818-825
    • Lee, H.1    Jang, I.H.2    Ryu, S.H.3    Park, T.G.4
  • 87
    • 77549088667 scopus 로고    scopus 로고
    • Characterization of a monoPEG20000-Endostar
    • Tong Y, Zhong K, Tian H, et al. Characterization of a monoPEG20000-Endostar. Int. J. Biol. Macromol. 46(3), 331-336 (2010
    • (2010) Int. J. Biol. Macromol , vol.46 , Issue.3 , pp. 331-336
    • Tong, Y.1    Zhong, K.2    Tian, H.3
  • 88
    • 20044390237 scopus 로고    scopus 로고
    • PEGylation of octreotide: II Effect of N-Terminal mono-PEGylation on biological activity and pharmacokinetics
    • Na DH, Lee KC, Deluca PP. PEGylation of octreotide: II. Effect of N-Terminal mono-PEGylation on biological activity and pharmacokinetics. Pharm. Res. 22(5), 743-749 (2005
    • (2005) Pharm. Res , vol.22 , Issue.5 , pp. 743-749
    • Na, D.H.1    Lee, K.C.2    Deluca, P.P.3
  • 89
    • 34250006003 scopus 로고    scopus 로고
    • Structural characterization of PEGylated rHuG-CSF and location of PEG attachment sites
    • Cindric M, Cepo T, Galic N, et al. Structural characterization of PEGylated rHuG-CSF and location of PEG attachment sites. J. Pharmaceut. Biomed. 44(2), 388-395 (2007
    • (2007) J. Pharmaceut. Biomed , vol.44 , Issue.2 , pp. 388-395
    • Cindric, M.1    Cepo, T.2    Galic, N.3
  • 90
    • 33746705584 scopus 로고    scopus 로고
    • Preparation and stability of N-Terminal mono-PEGylated recombinant human endostatin
    • Nie Y, Zhang X, Wang X, Chen J. Preparation and stability of N-Terminal mono-PEGylated recombinant human endostatin. Bioconjug. Chem. 17(4), 995-999 (2006
    • (2006) Bioconjug. Chem , vol.17 , Issue.4 , pp. 995-999
    • Nie, Y.1    Zhang, X.2    Wang, X.3    Chen, J.4
  • 91
    • 67650064606 scopus 로고    scopus 로고
    • Enhanced circulation half-life of site-specific PEGylated rhG-CSF: Optimization of PEG molecular weight
    • Zhai Y, Zhao Y, Lei J, Su Z, Ma G. Enhanced circulation half-life of site-specific PEGylated rhG-CSF: optimization of PEG molecular weight. J. Biotechnol. 14, 259-266 (2009
    • (2009) J. Biotechnol , vol.14 , pp. 259-266
    • Zhai, Y.1    Zhao, Y.2    Lei, J.3    Su, Z.4    Ma, G.5
  • 92
    • 0025784230 scopus 로고
    • Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol
    • Hershfield M, Chaffee S. Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol. Proc. Natl Acad. Sci. USA. 88(16), 7185-7189 (1991
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.16 , pp. 7185-7189
    • Hershfield, M.1    Chaffee, S.2
  • 93
    • 12444305299 scopus 로고    scopus 로고
    • Site-specific PEGylation of a lysine-deficient TNF-Alpha with full bioactivity
    • Yamamoto Y, Tsutsumi Y, Yoshioka Y, et al. Site-specific PEGylation of a lysine-deficient TNF-Alpha with full bioactivity. Nat. Biotechnol. 21, 546-552 (2003
    • (2003) Nat. Biotechnol , vol.21 , pp. 546-552
    • Yamamoto, Y.1    Tsutsumi, Y.2    Yoshioka, Y.3
  • 94
    • 84911870957 scopus 로고    scopus 로고
    • EMEA
    • EMEA. Cimzia 'assesment report'. www.ema.europa.eu/docs/en-GB/document-library/EPAR-Public-Assessment-report/human/001037/WC500069735.pdf
    • Cimzia Assesment Report
  • 95
    • 33746273552 scopus 로고    scopus 로고
    • Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis
    • Gadgil HS, Bondarenko PV, Pipes GD, et al. Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis. Anal. Biochem. 355(2), 165-174 (2006
    • (2006) Anal. Biochem , vol.355 , Issue.2 , pp. 165-174
    • Gadgil, H.S.1    Bondarenko, P.V.2    Pipes, G.D.3
  • 96
    • 84861749627 scopus 로고    scopus 로고
    • State of the art in PEGylation: The great versatility achieved after forty years of research
    • Pasut G, Veronese FM. State of the art in PEGylation: the great versatility achieved after forty years of research. J. Control. Release 161(2), 461-472 (2012
    • (2012) J. Control. Release , vol.161 , Issue.2 , pp. 461-472
    • Pasut, G.1    Veronese, F.M.2
  • 97
    • 70349314669 scopus 로고    scopus 로고
    • FN3: A new protein scaffold reaches the clinic
    • Bloom L, Calabro V. FN3: a new protein scaffold reaches the clinic. Drug Discov. Today 14, 949-955 (2009
    • (2009) Drug Discov. Today , vol.14 , pp. 949-955
    • Bloom, L.1    Calabro, V.2
  • 98
    • 78650468405 scopus 로고    scopus 로고
    • Adnectins: Engineered target-binding protein therapeutics
    • Lipovsek D. Adnectins: engineered target-binding protein therapeutics. Protein Eng. Des. Sel. 24(1-2), 3-9 (2011
    • (2011) Protein Eng. Des. Sel , vol.24 , Issue.1-2 , pp. 3-9
    • Lipovsek, D.1
  • 100
    • 41149160183 scopus 로고    scopus 로고
    • Contribution of linker stability to the activities of anticancer immunoconjugates
    • Alley S, Benjamin D, Jeffrey S, et al. Contribution of linker stability to the activities of anticancer immunoconjugates. Bioconjug. Chem. 19, 759-765 (2008
    • (2008) Bioconjug. Chem , vol.19 , pp. 759-765
    • Alley, S.1    Benjamin, D.2    Jeffrey, S.3
  • 101
    • 80054828086 scopus 로고    scopus 로고
    • Tunable degradation of maleimide-Thiol adducts in reducing environments
    • Baldwin AD, Kiick KL. Tunable degradation of maleimide-Thiol adducts in reducing environments. Bioconjug. Chem. 22(10), 1946-1953 (2011
    • (2011) Bioconjug. Chem , vol.22 , Issue.10 , pp. 1946-1953
    • Baldwin, A.D.1    Kiick, K.L.2
  • 102
    • 84875789991 scopus 로고    scopus 로고
    • Reversible maleimide-Thiol adducts yield glutathione-sensitive poly(ethylene glycol)-heparin hydrogels
    • Baldwin AD, Kiick KL. Reversible maleimide-Thiol adducts yield glutathione-sensitive poly(ethylene glycol)-heparin hydrogels. Polym. Chem. 4(1), 133 (2012
    • (2012) Polym. Chem , vol.4 , Issue.1 , pp. 133
    • Baldwin, A.D.1    Kiick, K.L.2
  • 103
    • 84863012529 scopus 로고    scopus 로고
    • Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates
    • Shen BQ, Xu K, Liu L, et al. Conjugation site modulates the in vivo stability and therapeutic activity of antibody-drug conjugates. Nat. Biotechnol. 30(2), 184-189 (2012
    • (2012) Nat. Biotechnol , vol.30 , Issue.2 , pp. 184-189
    • Shen, B.Q.1    Xu, K.2    Liu, L.3
  • 104
    • 84887976957 scopus 로고    scopus 로고
    • Rapid, stable, chemoselective labeling of thiols with Julia-Kocienski-like reagents: A serumstable alternative to maleimide-based protein conjugation
    • Toda N, Asano S, Barbas CF 3rd. Rapid, stable, chemoselective labeling of thiols with Julia-Kocienski-like reagents: a serumstable alternative to maleimide-based protein conjugation. Angew Chem. Int. Ed. Engl. 52(48), 12592-12596 (2013
    • (2013) Angew Chem. Int. Ed. Engl , vol.52 , Issue.48 , pp. 12592-12596
    • Toda, N.1    Asano, S.2    Barbas, C.F.3
  • 106
    • 84896513331 scopus 로고    scopus 로고
    • A new reagent for stable thiol-specific conjugation
    • Badescu G, Bryant P, Swierkosz J, et al. A new reagent for stable thiol-specific conjugation. Bioconjug. Chem. 25(3), 460-469 (2013
    • (2013) Bioconjug. Chem , vol.25 , Issue.3 , pp. 460-469
    • Badescu, G.1    Bryant, P.2    Swierkosz, J.3
  • 107
    • 33846406038 scopus 로고    scopus 로고
    • Site-specific PEGylation of protein disulfide bonds using a three-carbon bridge
    • Balan S, Choi J, Godwin A, et al. Site-specific PEGylation of protein disulfide bonds using a three-carbon bridge. Bioconjug. Chem. 18(1), 61-76 (2007
    • (2007) Bioconjug. Chem , vol.18 , Issue.1 , pp. 61-76
    • Balan, S.1    Choi, J.2    Godwin, A.3
  • 108
    • 33646863688 scopus 로고    scopus 로고
    • Site-specific PEGylation of native disulfide bonds in therapeutic proteins
    • Shaunak S, Godwin A, Choi J, et al. Site-specific PEGylation of native disulfide bonds in therapeutic proteins. Nat. Chem. Bio. 2 (6), 312-313 (2006
    • (2006) Nat. Chem. Bio , vol.2 , Issue.6 , pp. 312-313
    • Shaunak, S.1    Godwin, A.2    Choi, J.3
  • 109
    • 79951709244 scopus 로고    scopus 로고
    • In situ maleimide bridging of disulfides and a new approach to protein PEGylation
    • Schumacher FF, Nobles M, Ryan CP, et al. In situ maleimide bridging of disulfides and a new approach to protein PEGylation. Bioconjug. Chem. 1-5 (2011
    • (2011) Bioconjug. Chem , pp. 1-5
    • Schumacher, F.F.1    Nobles, M.2    Ryan, C.P.3
  • 112
    • 3543050105 scopus 로고    scopus 로고
    • His tag effect on solubility of human proteins produced in Escherichia coli: A comparison between four expression vectors
    • Woestenenk E, Hammarstrom M, van den Berg S, Hard T, Berglund H. His tag effect on solubility of human proteins produced in Escherichia coli: a comparison between four expression vectors. J. Struct. Func. Genomics 5(3), 217-229 (2004
    • (2004) J. Struct. Func. Genomics , vol.5 , Issue.3 , pp. 217-229
    • Woestenenk, E.1    Hammarstrom, M.2    Van Den Berg, S.3    Hard, T.4    Berglund, H.5
  • 113
    • 33847162720 scopus 로고    scopus 로고
    • On-column refolding purification and characterization of recombinant human interferon-?1 produced in Escherichia coli
    • Li M, Huang D. On-column refolding purification and characterization of recombinant human interferon-?1 produced in Escherichia coli. Protein Expr. Purif. 53(1), 119-123 (2007
    • (2007) Protein Expr. Purif , vol.53 , Issue.1 , pp. 119-123
    • Li, M.1    Huang, D.2
  • 114
    • 28144464877 scopus 로고    scopus 로고
    • Potential for using histidine tags in purification of proteins at large scale
    • Gaberc-Porekar V, Menart V. Potential for using histidine tags in purification of proteins at large scale. Chem. Eng. Technol. 28(11), 1306-1314 (2005
    • (2005) Chem. Eng. Technol , vol.28 , Issue.11 , pp. 1306-1314
    • Gaberc-Porekar, V.1    Menart, V.2
  • 115
    • 33751259946 scopus 로고    scopus 로고
    • A Phase i study of single administration of antibody-directed enzyme prodrug therapy with the recombinant anti-carcinoembryonic antigen antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug
    • Mayer A, Francis RJ, Sharma SK, et al. A Phase I study of single administration of antibody-directed enzyme prodrug therapy with the recombinant anti-carcinoembryonic antigen antibody-enzyme fusion protein MFECP1 and a bis-iodo phenol mustard prodrug. Clin. Cancer Res. 12(21), 6509-6516 (2006
    • (2006) Clin. Cancer Res , vol.12 , Issue.21 , pp. 6509-6516
    • Mayer, A.1    Francis, R.J.2    Sharma, S.K.3
  • 116
    • 36048994993 scopus 로고    scopus 로고
    • From laboratory to Phase I/II cancer trials with recombinant biotherapeutics
    • Tolner B, Smith L, Hillyer T, et al. From laboratory to Phase I/II cancer trials with recombinant biotherapeutics. Eur. J. Cancer 43(17), 2515-2522 (2007
    • (2007) Eur. J. Cancer , vol.43 , Issue.17 , pp. 2515-2522
    • Tolner, B.1    Smith, L.2    Hillyer, T.3
  • 117
    • 20244384857 scopus 로고    scopus 로고
    • Recombinant NY-ESO-1 cancer antigen: Production and purification under cGMP conditions
    • Murphy R, Green S, Ritter G, et al. Recombinant NY-ESO-1 cancer antigen: production and purification under cGMP conditions. Prep. Biochem. Biotech. 35(2), 119-134 (2005
    • (2005) Prep. Biochem. Biotech , vol.35 , Issue.2 , pp. 119-134
    • Murphy, R.1    Green, S.2    Ritter, G.3
  • 118
    • 14744292328 scopus 로고
    • Production, purification and immunogenicity of a malaria transmission-blocking vaccine candidate: TBV25H expressed in yeast and purified using nickel-NTA agarose
    • Kaslow D, Shiloach J. Production, purification and immunogenicity of a malaria transmission-blocking vaccine candidate: TBV25H expressed in yeast and purified using nickel-NTA agarose. Nat. Biotechnol. 12(5), 494-499 (1994
    • (1994) Nat. Biotechnol , vol.12 , Issue.5 , pp. 494-499
    • Kaslow, D.1    Shiloach, J.2
  • 119
    • 79951634978 scopus 로고    scopus 로고
    • Arginine-specific modification of proteins with polyethylene glycol
    • Gauthier MA, Klok HA. Arginine-specific modification of proteins with polyethylene glycol. Biomacromolecules 12, 482-493 (2010
    • (2010) Biomacromolecules , vol.12 , pp. 482-493
    • Gauthier, M.A.1    Klok, H.A.2
  • 120
    • 0037124507 scopus 로고    scopus 로고
    • Enzymatic procedure for site-specific pegylation of proteins
    • Sato H. Enzymatic procedure for site-specific pegylation of proteins. Adv. Drug Deliv. Rev. 54, 487-504 (2002
    • (2002) Adv. Drug Deliv. Rev , vol.54 , pp. 487-504
    • Sato, H.1
  • 121
    • 70350439266 scopus 로고    scopus 로고
    • Site-directed enzymatic PEGylation of the human granulocyte colonystimulating factor
    • Maullu C, Raimondo D, Caboi F, et al. Site-directed enzymatic PEGylation of the human granulocyte colonystimulating factor. FEBS J. 276(22), 6741-6750 (2009
    • (2009) FEBS J. , vol.276 , Issue.22 , pp. 6741-6750
    • Maullu, C.1    Raimondo, D.2    Caboi, F.3
  • 122
    • 78649810925 scopus 로고    scopus 로고
    • Chemoenzymatic methods for site-specific protein modification
    • Rabuka D. Chemoenzymatic methods for site-specific protein modification. Curr. Opin. Chem. Biol. 14, 790-796 (2010
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 790-796
    • Rabuka, D.1
  • 123
    • 33748689917 scopus 로고    scopus 로고
    • GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli
    • Defrees S, Wang ZG, Xing R, et al. GlycoPEGylation of recombinant therapeutic proteins produced in Escherichia coli. Glycobiology 16(9), 833-843 (2006
    • (2006) Glycobiology , vol.16 , Issue.9 , pp. 833-843
    • Defrees, S.1    Wang, Z.G.2    Xing, R.3
  • 124
    • 79951580612 scopus 로고    scopus 로고
    • Biophysical characterisation of GlycoPEGylated recombinant human factor VIIa
    • Plesner B, Westh P, Nielsen A. Biophysical characterisation of GlycoPEGylated recombinant human factor VIIa. Int. J. Pharm. 406, 62-68 (2011
    • (2011) Int. J. Pharm , vol.406 , pp. 62-68
    • Plesner, B.1    Westh, P.2    Nielsen, A.3
  • 125
    • 84863129027 scopus 로고    scopus 로고
    • Generation and biochemical characterization of glycoPEGylated factor VIIa derivatives
    • Stennicke HR, Ostergaard H, Bayer RJ, et al. Generation and biochemical characterization of glycoPEGylated factor VIIa derivatives. Tierärztliche Praxis Grobtiere 36(3), 163-169 (2008
    • (2008) Tierärztliche Praxis Grobtiere , vol.36 , Issue.3 , pp. 163-169
    • Stennicke, H.R.1    Ostergaard, H.2    Bayer, R.J.3
  • 126
    • 80053001348 scopus 로고    scopus 로고
    • Site-specific modification of recombinant proteins: A novel platform for modifying glycoproteins expressed in e
    • Henderson GE, Isett KD, Gerngross TU. Site-specific modification of recombinant proteins: a novel platform for modifying glycoproteins expressed in E. coli. Bioconjug. Chem. 22(5), 903-912 (2011
    • (2011) Coli. Bioconjug. Chem , vol.22 , Issue.5 , pp. 903-912
    • Henderson, G.E.1    Isett, K.D.2    Gerngross, T.U.3
  • 127
    • 84860827170 scopus 로고    scopus 로고
    • Direct peptide bioconjugation/PEGylation at tyrosine with linear and branched polymeric diazonium salts
    • Jones MW, Mantovani G, Blindauer CA, et al. Direct peptide bioconjugation/PEGylation at tyrosine with linear and branched polymeric diazonium salts. J. Am. Chem. Soc. 134(17), 7406-7413 (2012
    • (2012) J. Am. Chem. Soc , vol.134 , Issue.17 , pp. 7406-7413
    • Jones, M.W.1    Mantovani, G.2    Blindauer, C.A.3
  • 128
    • 15744396333 scopus 로고    scopus 로고
    • Dual-surface modification of the tobacco mosaic virus
    • Schlick TL, Ding Z, Kovacs EW, Francis MB. Dual-surface modification of the tobacco mosaic virus. J. Am. Chem. Soc. 127(11), 3718-3723 (2005
    • (2005) J. Am. Chem. Soc , vol.127 , Issue.11 , pp. 3718-3723
    • Schlick, T.L.1    Ding, Z.2    Kovacs, E.W.3    Francis, M.B.4
  • 129
    • 44249085588 scopus 로고    scopus 로고
    • C-Terminal mini-PEGylation of glucose-dependent insulinotropic polypeptide exhibits metabolic stability and improved glucose homeostasis in dietary-induced diabetes
    • Gault VA, Kerr BD, Irwin N, Flatt PR. C-Terminal mini-PEGylation of glucose-dependent insulinotropic polypeptide exhibits metabolic stability and improved glucose homeostasis in dietary-induced diabetes. Biochem. Pharmacol. 75(12), 2325-2333 (2008
    • (2008) Biochem. Pharmacol , vol.75 , Issue.12 , pp. 2325-2333
    • Gault, V.A.1    Kerr, B.D.2    Irwin, N.3    Flatt, P.R.4
  • 130
    • 33646154457 scopus 로고    scopus 로고
    • Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study
    • Rajan RS, Li T, Aras M, et al. Modulation of protein aggregation by polyethylene glycol conjugation: GCSF as a case study. Protein Sci. 15(5), 1063-1075 (2006
    • (2006) Protein Sci , vol.15 , Issue.5 , pp. 1063-1075
    • Rajan, R.S.1    Li, T.2    Aras, M.3
  • 131
    • 33646909899 scopus 로고    scopus 로고
    • Structure-function engineering of interferon-β-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-PEGylation
    • Basu A, Yang K, Wang M, et al. Structure-function engineering of interferon-β-1b for improving stability, solubility, potency, immunogenicity, and pharmacokinetic properties by site-selective mono-PEGylation. Bioconjug. Chem. 17(3), 618-630 (2006
    • (2006) Bioconjug. Chem , vol.17 , Issue.3 , pp. 618-630
    • Basu, A.1    Yang, K.2    Wang, M.3
  • 132
    • 0030059104 scopus 로고    scopus 로고
    • Site-specific attachment of functionalized poly (ethylene glycol) to the amino terminus of proteins
    • Gaertner HF, Offord RE. Site-specific attachment of functionalized poly (ethylene glycol) to the amino terminus of proteins. Bioconjug. Chem. 7(1), 38-44 (1996
    • (1996) Bioconjug. Chem , vol.7 , Issue.1 , pp. 38-44
    • Gaertner, H.F.1    Offord, R.E.2
  • 134
    • 36849064395 scopus 로고    scopus 로고
    • Solid-phase PEGylation of recombinant interferon α-2a for site-specific modification: Process performance, characterization, and in vitro bioactivity
    • Lee B, Kwon J, Kim H, Yamamoto S. Solid-phase PEGylation of recombinant interferon α-2a for site-specific modification: process performance, characterization, and in vitro bioactivity. Bioconjug. Chem. 18(6), 1728-1734 (2007
    • (2007) Bioconjug. Chem , vol.18 , Issue.6 , pp. 1728-1734
    • Lee, B.1    Kwon, J.2    Kim, H.3    Yamamoto, S.4
  • 135
    • 79959192999 scopus 로고    scopus 로고
    • Recombinant protein hydrazides: Application to site-specific protein PEGylation
    • Thom J, Anderson D, McGregor J, Cotton G. Recombinant protein hydrazides: application to site-specific protein PEGylation. Bioconjug. Chem. 22(6), 1017-1020 (2011
    • (2011) Bioconjug. Chem , vol.22 , Issue.6 , pp. 1017-1020
    • Thom, J.1    Anderson, D.2    McGregor, J.3    Cotton, G.4
  • 136
    • 84887976957 scopus 로고    scopus 로고
    • Rapid, stable, chemoselective labeling of thiols with julia-kocienski-like reagents: A serumstable alternative to maleimide-based protein conjugation
    • Toda N, Asano S, Barbas CF. Rapid, stable, chemoselective labeling of thiols with julia-kocienski-like reagents: a serumstable alternative to maleimide-based protein conjugation. Angew. Chem. Int. Ed. Engl. 52(48), 12592-12596 (2013
    • (2013) Angew. Chem. Int. Ed. Engl , vol.52 , Issue.48 , pp. 12592-12596
    • Toda, N.1    Asano, S.2    Barbas, C.F.3
  • 138
    • 33846406038 scopus 로고    scopus 로고
    • Site-specific PEGylation of protein disulfide bonds using a three-carbon bridge
    • Balan S, Choi JW, Godwin A, et al. Site-specific PEGylation of protein disulfide bonds using a three-carbon bridge. Bioconjug. Chem. 18(1), 61-76 (2007
    • (2007) Bioconjug. Chem , vol.18 , Issue.1 , pp. 61-76
    • Balan, S.1    Choi, J.W.2    Godwin, A.3
  • 140
    • 84856278455 scopus 로고    scopus 로고
    • Polymeric dibromomaleimides as extremely efficient disulfide bridging bioconjugation and pegylation agents
    • Jones MW, Strickland RA, Schumacher FF, et al. Polymeric dibromomaleimides as extremely efficient disulfide bridging bioconjugation and pegylation agents. J. Am. Chem. Soc. 134(3), 1847-1852 (2011
    • (2011) J. Am. Chem. Soc , vol.134 , Issue.3 , pp. 1847-1852
    • Jones, M.W.1    Strickland, R.A.2    Schumacher, F.F.3
  • 141
    • 62549119508 scopus 로고    scopus 로고
    • Transglutaminase-mediated PEGylation of proteins: Direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG
    • Mero A, Spolaore B, Veronese FM, Fontana A. Transglutaminase-mediated PEGylation of proteins: direct identification of the sites of protein modification by mass spectrometry using a novel monodisperse PEG. Bioconjug. Chem. 20(2), 384-389 (2009
    • (2009) Bioconjug. Chem , vol.20 , Issue.2 , pp. 384-389
    • Mero, A.1    Spolaore, B.2    Veronese, F.M.3    Fontana, A.4
  • 142
    • 84863155417 scopus 로고    scopus 로고
    • Site-specific PEGylation at histidine tags
    • Cong Y, Pawlisz E, Bryant P, et al. Site-specific PEGylation at histidine tags. Bioconjug. Chem. 23(2), 248-263 (2012
    • (2012) Bioconjug. Chem , vol.23 , Issue.2 , pp. 248-263
    • Cong, Y.1    Pawlisz, E.2    Bryant, P.3
  • 144
    • 45749151511 scopus 로고    scopus 로고
    • Chemoselective modification of proteins: Hitting the target
    • Carrico IS. Chemoselective modification of proteins: hitting the target. Chem. Soc. Rev. 37(7), 1423-1431 (2008
    • (2008) Chem. Soc. Rev , vol.37 , Issue.7 , pp. 1423-1431
    • Carrico, I.S.1
  • 145
    • 79751479008 scopus 로고    scopus 로고
    • Emerging synthetic approaches for protein-polymer conjugations
    • Broyer RM, Grover GN, Maynard HD. Emerging synthetic approaches for protein-polymer conjugations. Chem. Comm. 47, 2212-2226 (2011
    • (2011) Chem. Comm , vol.47 , pp. 2212-2226
    • Broyer, R.M.1    Grover, G.N.2    Maynard, H.D.3
  • 146
    • 76149123221 scopus 로고    scopus 로고
    • Tyrosine bioconjugation through aqueous ene-Type reactions: A click-like reaction for tyrosine
    • Ban H, Gavrilyuk J, Barbas III CF. Tyrosine bioconjugation through aqueous ene-Type reactions: a click-like reaction for tyrosine. J. Am. Chem. Soc. 132(5), 1523-1525 (2010
    • (2010) J. Am. Chem. Soc , vol.132 , Issue.5 , pp. 1523-1525
    • Ban, H.1    Gavrilyuk, J.2    Barbas, C.F.3
  • 147
    • 78751614082 scopus 로고    scopus 로고
    • Site-specific protein cross-linking by peroxidase-catalyzed activation of a tyrosine-containing peptide tag
    • Minamihata K, Goto M, Kamiya N. Site-specific protein cross-linking by peroxidase-catalyzed activation of a tyrosine-containing peptide tag. Bioconjug. Chem. 22, 74-81 (2011
    • (2011) Bioconjug. Chem , vol.22 , pp. 74-81
    • Minamihata, K.1    Goto, M.2    Kamiya, N.3
  • 148
    • 76949103845 scopus 로고    scopus 로고
    • PEGylated polymers for medicine: From conjugation to self-Assembled systems
    • Joralemon MJ, McRae S, Emrick T. PEGylated polymers for medicine: from conjugation to self-Assembled systems. Chem. Commun. (Camb.) 46(9), 1377 (2010
    • (2010) Chem. Commun. (Camb , vol.46 , Issue.9 , pp. 1377
    • Joralemon, M.J.1    McRae, S.2    Emrick, T.3
  • 149
    • 78649829465 scopus 로고    scopus 로고
    • Residuespecific incorporation of non-canonical amino acids into proteins: Recent developments and applications
    • Johnson JA, Lu YY, Van Deventer JA, Tirrell DA. Residuespecific incorporation of non-canonical amino acids into proteins: recent developments and applications. Curr. Opin. Chem. Biol. 14, 774-780 (2010
    • (2010) Curr. Opin. Chem. Biol , vol.14 , pp. 774-780
    • Johnson, J.A.1    Lu, Y.Y.2    Van Deventer, J.A.3    Tirrell, D.A.4
  • 150
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu CC, Schultz PG. Adding new chemistries to the genetic code. Ann. Rev. Biochem. 79, 413-444 (2010
    • (2010) Ann. Rev. Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 151
    • 72949090352 scopus 로고    scopus 로고
    • Incorporation of unnatural amino acids for synthetic biology
    • Voloshchuk N, Montclare JK. Incorporation of unnatural amino acids for synthetic biology. Mol. Biosyst. 6(1), 65-80 (2009
    • (2009) Mol. Biosyst , vol.6 , Issue.1 , pp. 65-80
    • Voloshchuk, N.1    Montclare, J.K.2
  • 152
    • 33847035549 scopus 로고    scopus 로고
    • Non-canonical amino acids in protein polymer design
    • Connor RE, Tirrell DA. Non-canonical amino acids in protein polymer design. Polym. Rev. 47(1), 9-28 (2007
    • (2007) Polym. Rev , vol.47 , Issue.1 , pp. 9-28
    • Connor, R.E.1    Tirrell, D.A.2
  • 153
    • 38849132058 scopus 로고    scopus 로고
    • Processing of N-Terminal unnatural amino acids in recombinant human interferon-β in Escherichia coli
    • Wang A, Winblade Nairn N, Johnson RS, Tirrell DA, Grabstein K. Processing of N-Terminal unnatural amino acids in recombinant human interferon-β in Escherichia coli. Chembiochem 9(2), 324-330 (2008
    • (2008) Chembiochem , vol.9 , Issue.2 , pp. 324-330
    • Wang, A.1    Winblade Nairn, N.2    Johnson, R.S.3    Tirrell, D.A.4    Grabstein, K.5
  • 154
    • 33847139762 scopus 로고    scopus 로고
    • Protein and cellular engineering with unnatural amino acids
    • Liao J. Protein and cellular engineering with unnatural amino acids. Biotechnol. Prog. 23(1), 28-31 (2007
    • (2007) Biotechnol. Prog , vol.23 , Issue.1 , pp. 28-31
    • Liao, J.1
  • 155
    • 33847050891 scopus 로고    scopus 로고
    • Biosynthetic-synthetic polymer conjugates
    • Van Hest J. Biosynthetic-synthetic polymer conjugates. Polym. Rev. 47(1), 63-92 (2007
    • (2007) Polym. Rev , vol.47 , Issue.1 , pp. 63-92
    • Van Hest, J.1
  • 156
    • 10744227326 scopus 로고    scopus 로고
    • Tailoring structure-function and pharmacokinetic properties of single-chain Fv proteins by site-specific PEGylation
    • Yang K, Basu A, Wang M, et al. Tailoring structure-function and pharmacokinetic properties of single-chain Fv proteins by site-specific PEGylation. Protein Eng. 16(10), 761-770 (2003
    • (2003) Protein Eng , vol.16 , Issue.10 , pp. 761-770
    • Yang, K.1    Basu, A.2    Wang, M.3
  • 157
    • 12344260516 scopus 로고    scopus 로고
    • A long-Acting, highly potent interferon a-2 conjugate created using site-specific PEGylation
    • Rosendahl M, Doherty D, Smith S, Carlson S, Chlipala E, Cox G. A long-Acting, highly potent interferon a-2 conjugate created using site-specific PEGylation. Bioconjug. Chem. 16, 200-207 (2005
    • (2005) Bioconjug. Chem , vol.16 , pp. 200-207
    • Rosendahl, M.1    Doherty, D.2    Smith, S.3    Carlson, S.4    Chlipala, E.5    Cox, G.6
  • 158
    • 77955492929 scopus 로고    scopus 로고
    • Rational design of a fully active, long-Acting PEGylated factor VIII for hemophilia A treatment
    • Mei B, Pan C, Jiang H, et al. Rational design of a fully active, long-Acting PEGylated factor VIII for hemophilia A treatment. Blood 116(2), 270-279 (2010
    • (2010) Blood , vol.116 , Issue.2 , pp. 270-279
    • Mei, B.1    Pan, C.2    Jiang, H.3
  • 159
    • 25444439806 scopus 로고    scopus 로고
    • Site-specific PEGylation of engineered cysteine analogues of recombinant human granulocyte-macrophage colony-stimulating factor
    • Doherty DH, Rosendahl MS, Smith DJ, Hughes JM, Chlipala EA, Cox GN. Site-specific PEGylation of engineered cysteine analogues of recombinant human granulocyte-macrophage colony-stimulating factor. Bioconjug. Chem. 16(5), 1291-1298 (2005
    • (2005) Bioconjug. Chem , vol.16 , Issue.5 , pp. 1291-1298
    • Doherty, D.H.1    Rosendahl, M.S.2    Smith, D.J.3    Hughes, J.M.4    Chlipala, E.A.5    Cox, G.N.6
  • 160
    • 38949097057 scopus 로고    scopus 로고
    • Building a parallel metabolism within the cell
    • Filipovska A, Rackham O. Building a parallel metabolism within the cell. ACS Chem. Biol. 3(1), 51-63 (2008
    • (2008) ACS Chem. Biol , vol.3 , Issue.1 , pp. 51-63
    • Filipovska, A.1    Rackham, O.2
  • 161
    • 80052167452 scopus 로고    scopus 로고
    • Prolonged half-life and preserved enzymatic properties of factor IX selectively PEGylated on native N-glycans in the activation peptide
    • Ostergaard H, Bjelke JR, Hansen L, et al. Prolonged half-life and preserved enzymatic properties of factor IX selectively PEGylated on native N-glycans in the activation peptide. Blood 118(8), 2333-2341 (2011
    • (2011) Blood , vol.118 , Issue.8 , pp. 2333-2341
    • Ostergaard, H.1    Bjelke, J.R.2    Hansen, L.3
  • 162
    • 0028337034 scopus 로고
    • Distribution and tissue uptake of poly(ethylene glycol) with different molecular weights after intravenous administration to mice
    • Yamaoka T, Tabata Y, Ikada Y. Distribution and tissue uptake of poly(ethylene glycol) with different molecular weights after intravenous administration to mice. J. Pharm. Sci. 83(4), 601-606 (1994
    • (1994) J. Pharm. Sci , vol.83 , Issue.4 , pp. 601-606
    • Yamaoka, T.1    Tabata, Y.2    Ikada, Y.3
  • 163
    • 84866896587 scopus 로고    scopus 로고
    • Immunogenicity of polyethylene glycol (PEG
    • Garay RP, Labaune JP. Immunogenicity of polyethylene glycol (PEG). Open Conf. Proc. J. 2, 104-107 (2011
    • (2011) Open Conf. Proc. J. , vol.2 , pp. 104-107
    • Garay, R.P.1    Labaune, J.P.2
  • 164
    • 34250800861 scopus 로고    scopus 로고
    • Antibody against poly(ethylene glycol) adversely affects PEGasparaginase therapy in acute lymphoblastic leukemia patients
    • Armstrong JK, Hempel G, Koling S, et al. Antibody against poly(ethylene glycol) adversely affects PEGasparaginase therapy in acute lymphoblastic leukemia patients. Cancer 110(1), 103-111 (2007
    • (2007) Cancer , vol.110 , Issue.1 , pp. 103-111
    • Armstrong, J.K.1    Hempel, G.2    Koling, S.3
  • 165
    • 33746995205 scopus 로고    scopus 로고
    • Control of hyperuricemia in subjects with refractory gout, and induction of antibody against poly(ethylene glycol) (PEG), in a Phase i trial of subcutaneous PEGylated urate oxidase
    • Ganson NJ, Kelly SJ, Scarlett E, Sundy JS, Hershfield MS. Control of hyperuricemia in subjects with refractory gout, and induction of antibody against poly(ethylene glycol) (PEG), in a Phase I trial of subcutaneous PEGylated urate oxidase. Arthritis Res. Ther. 8(1), R12 (2006
    • (2006) Arthritis Res. Ther , vol.8 , Issue.1 , pp. R12
    • Ganson, N.J.1    Kelly, S.J.2    Scarlett, E.3    Sundy, J.S.4    Hershfield, M.S.5
  • 166
    • 33846889329 scopus 로고    scopus 로고
    • Poly(amino acid)s: Promising enzymatically degradable stealth coatings for liposomes
    • Romberg B, Metselaar JM, Baranyi L, et al. Poly(amino acid)s: promising enzymatically degradable stealth coatings for liposomes. Int. J. Pharm. 331(2), 186-189 (2007
    • (2007) Int. J. Pharm , vol.331 , Issue.2 , pp. 186-189
    • Romberg, B.1    Metselaar, J.M.2    Baranyi, L.3
  • 167
    • 0037619168 scopus 로고    scopus 로고
    • Poly-l)-glutamic acid-paclitaxel (ct-2103) [xyotax], a biodegradable polymeric drug conjugate: Characterization, preclinical pharmacology, and preliminary clinical data
    • Singer JW, Baker B, De Vries P, et al. Poly-(L)-glutamic acid-paclitaxel (CT-2103) [XYOTAX], a biodegradable polymeric drug conjugate: characterization, preclinical pharmacology, and preliminary clinical data. Adv. Exp. Med. Biol. 519, 81-99 (2003
    • (2003) Adv. Exp. Med. Biol , vol.519 , pp. 81-99
    • Singer, J.W.1    Baker, B.2    De Vries, P.3
  • 168
    • 44649193032 scopus 로고    scopus 로고
    • Phase iii trial comparing paclitaxel poliglumex (ct-2103, ppx) in combination with carboplatin versus standard paclitaxel and carboplatin in the treatment of ps 2 patients with chemotherapy-naive advanced non-small cell lung cancer
    • Langer CJ, O'Byrne KJ, Socinski MA, et al. Phase III trial comparing paclitaxel poliglumex (CT-2103, PPX) in combination with carboplatin versus standard paclitaxel and carboplatin in the treatment of PS 2 patients with chemotherapy-naive advanced non-small cell lung cancer. J. Thorac. Oncol. 3(6), 623-630 (2008
    • (2008) J. Thorac. Oncol , vol.3 , Issue.6 , pp. 623-630
    • Langer, C.J.1    O'byrne, K.J.2    Socinski, M.A.3
  • 169
    • 27744553029 scopus 로고    scopus 로고
    • A Phase i and pharmacokinetic study of paclitaxel poliglumex (XYOTAX), investigating both 3-weekly and 2-weekly schedules
    • Boddy AV, Plummer ER, Todd R, et al. A Phase I and pharmacokinetic study of paclitaxel poliglumex (XYOTAX), investigating both 3-weekly and 2-weekly schedules. Clin. Cancer Res. 11(21), 7834-7840 (2005
    • (2005) Clin. Cancer Res , vol.11 , Issue.21 , pp. 7834-7840
    • Boddy, A.V.1    Plummer, E.R.2    Todd, R.3
  • 170
    • 35348868039 scopus 로고    scopus 로고
    • Phase i trial of poly-L-glutamate camptothecin (CT-2106) administered weekly in patients with advanced solid malignancies
    • Homsi J, Simon GR, Garrett CR, et al. Phase I trial of poly-L-glutamate camptothecin (CT-2106) administered weekly in patients with advanced solid malignancies. Clin. Cancer Res. 13(19), 5855-5861 (2007
    • (2007) Clin. Cancer Res , vol.13 , Issue.19 , pp. 5855-5861
    • Homsi, J.1    Simon, G.R.2    Garrett, C.R.3
  • 171
    • 66149174919 scopus 로고    scopus 로고
    • Site-specific polysialylation of an antitumor single-chain Fv fragment
    • Constantinou A, Epenetos AA, Hreczuk-Hirst D, et al. Site-specific polysialylation of an antitumor single-chain Fv fragment. Bioconjug. Chem. 20(5), 924-931 (2009
    • (2009) Bioconjug. Chem , vol.20 , Issue.5 , pp. 924-931
    • Constantinou, A.1    Epenetos, A.A.2    Hreczuk-Hirst, D.3
  • 172
    • 23444455640 scopus 로고    scopus 로고
    • Improving the therapeutic efficacy of peptides and proteins: A role for polysialic acids
    • Gregoriadis G, Jain S, Papaioannou I, Laing P. Improving the therapeutic efficacy of peptides and proteins: a role for polysialic acids. Int. J. Pharm. 300(1-2), 125-130 (2005
    • (2005) Int. J. Pharm , vol.300 , Issue.1-2 , pp. 125-130
    • Gregoriadis, G.1    Jain, S.2    Papaioannou, I.3    Laing, P.4
  • 173
    • 84860838557 scopus 로고    scopus 로고
    • Organosoluble enzyme conjugates with poly(2-oxazoline) s via pyromellitic acid dianhydride
    • Konieczny S, Fik CP, Averesch NJ, Tiller JC. Organosoluble enzyme conjugates with poly(2-oxazoline) s via pyromellitic acid dianhydride. J. Biotechnol. 159(3), 195-203 (2012
    • (2012) J. Biotechnol , vol.159 , Issue.3 , pp. 195-203
    • Konieczny, S.1    Fik, C.P.2    Averesch, N.J.3    Tiller, J.C.4
  • 174
    • 4344701890 scopus 로고    scopus 로고
    • The mechanism of protraction of insulin detemir, a long-Acting, acylated analog of human insulin
    • Havelund S, Plum A, Ribel U, et al. The mechanism of protraction of insulin detemir, a long-Acting, acylated analog of human insulin. Pharm. Res. 21(8), 1498-1504 (2004
    • (2004) Pharm. Res , vol.21 , Issue.8 , pp. 1498-1504
    • Havelund, S.1    Plum, A.2    Ribel, U.3
  • 176
    • 0026069645 scopus 로고
    • Synthetic polymers conjugated to monoclonal antibodies: Vehicles for tumour-Targeted drug delivery
    • Seymour LW, Flanagan PA, al-Shamkhani A, et al. Synthetic polymers conjugated to monoclonal antibodies: vehicles for tumour-Targeted drug delivery. Sel. Cancer Ther. 7(2), 59-73 (1991
    • (1991) Sel. Cancer Ther , vol.7 , Issue.2 , pp. 59-73
    • Seymour, L.W.1    Flanagan, P.A.2    Al-Shamkhani, A.3
  • 177
    • 75749144204 scopus 로고    scopus 로고
    • Structural and chemical aspects of HPMA copolymers as drug carriers
    • Ulbrich K, Subr V. Structural and chemical aspects of HPMA copolymers as drug carriers. Adv. Drug Deliv. Rev. 62(2), 150-166 (2010
    • (2010) Adv. Drug Deliv. Rev , vol.62 , Issue.2 , pp. 150-166
    • Ulbrich, K.1    Subr, V.2
  • 178
    • 34547735974 scopus 로고    scopus 로고
    • Fusion of a recombinant antibody fragment with a homo-Amino-Acid polymer: Effects on biophysical properties and prolonged plasma half-life
    • Schlapschy M, Theobald I, Mack H, Schottelius M, Wester H, Skerra A. Fusion of a recombinant antibody fragment with a homo-Amino-Acid polymer: effects on biophysical properties and prolonged plasma half-life. Protein Eng. Des. Sel. 20(6), 273 (2007
    • (2007) Protein Eng. Des. Sel , vol.20 , Issue.6 , pp. 273
    • Schlapschy, M.1    Theobald, I.2    MacK, H.3    Schottelius, M.4    Wester, H.5    Skerra, A.6
  • 179
    • 71849085755 scopus 로고    scopus 로고
    • A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner
    • Schellenberger V, Wang CW, Geething NC, et al. A recombinant polypeptide extends the in vivo half-life of peptides and proteins in a tunable manner. Nat. Biotechnol. 27(12), 1186-1190 (2009
    • (2009) Nat. Biotechnol , vol.27 , Issue.12 , pp. 1186-1190
    • Schellenberger, V.1    Wang, C.W.2    Geething, N.C.3


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