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Volumn 9, Issue 5, 2014, Pages

Glycoengineering of Interferon-β 1a improves its biophysical and pharmacokinetic properties

Author keywords

[No Author keywords available]

Indexed keywords

BETA1A INTERFERON; MUTANT PROTEIN; R27T; UNCLASSIFIED DRUG; BETA INTERFERON; LIGAND; MONOSACCHARIDE; N ACETYLNEURAMINIC ACID;

EID: 84901414491     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0096967     Document Type: Article
Times cited : (32)

References (43)
  • 2
    • 78549294190 scopus 로고    scopus 로고
    • Chronic progressive multiple sclerosis - Pathogenesis of neurodegeneration and therapeutic strategies
    • Fitzner D, Simons M (2010) Chronic progressive multiple sclerosis - pathogenesis of neurodegeneration and therapeutic strategies. Curr Neuropharmacol 8: 305-315.
    • (2010) Curr Neuropharmacol , vol.8 , pp. 305-315
    • Fitzner, D.1    Simons, M.2
  • 3
    • 84870659860 scopus 로고    scopus 로고
    • Multiple sclerosis: The role of cytokines in pathogenesis and in therapies
    • Amedei A, Prisco D, D'Elios MM (2012) Multiple sclerosis: the role of cytokines in pathogenesis and in therapies. Int J Mol Sci 13: 13438-13460.
    • (2012) Int J Mol Sci , vol.13 , pp. 13438-13460
    • Amedei, A.1    Prisco, D.2    D'Elios, M.M.3
  • 4
    • 84878828527 scopus 로고    scopus 로고
    • Patient perceptions of multiple sclerosis and its treatment
    • de Seze J, Borgel F, Brudon F (2012) Patient perceptions of multiple sclerosis and its treatment. Patient Prefer Adherence 6: 263-273.
    • (2012) Patient Prefer Adherence , vol.6 , pp. 263-273
    • De Seze, J.1    Borgel, F.2    Brudon, F.3
  • 6
    • 84555191747 scopus 로고    scopus 로고
    • Emerging oral drugs for relapsing-remitting multiple sclerosis
    • Gasperini C, Ruggieri S (2011) Emerging oral drugs for relapsing-remitting multiple sclerosis. Expert Opin Emerg Drugs 16: 697-712.
    • (2011) Expert Opin Emerg Drugs , vol.16 , pp. 697-712
    • Gasperini, C.1    Ruggieri, S.2
  • 8
    • 17844380498 scopus 로고    scopus 로고
    • Pegylation: A novel process for modifying pharmacokinetics
    • Harris JM, Martin NE, Modi M (2001) Pegylation: a novel process for modifying pharmacokinetics. Clin Pharmacokinet 40: 539-551. (Pubitemid 32738660)
    • (2001) Clinical Pharmacokinetics , vol.40 , Issue.7 , pp. 539-551
    • Milton, H.J.1    Martin, N.E.2    Modi, M.3
  • 9
    • 0141565183 scopus 로고    scopus 로고
    • Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function
    • DOI 10.1016/j.chembiol.2003.08.006
    • Watt GM, Lund J, Levens M, Kolli VS, Jefferis R, et al. (2003) Site-specific glycosylation of an aglycosylated human IgG1-Fc antibody protein generates neoglycoproteins with enhanced function. Chem Biol 10: 807-814. (Pubitemid 37171899)
    • (2003) Chemistry and Biology , vol.10 , Issue.9 , pp. 807-814
    • Watt, G.M.1    Lund, J.2    Levens, M.3    Kolli, V.S.K.4    Jefferis, R.5    Boons, G.-J.6
  • 10
    • 0027253357 scopus 로고
    • The Conjugation of Proteins with Polyethylene-Glycol and Other Polymers - Altering Properties of Proteins to Enhance Their Therapeutic Potential
    • Katre NV (1993) The Conjugation of Proteins with Polyethylene-Glycol and Other Polymers - Altering Properties of Proteins to Enhance Their Therapeutic Potential. Advanced Drug Delivery Reviews 10: 91-114.
    • (1993) Advanced Drug Delivery Reviews , vol.10 , pp. 91-114
    • Katre, N.V.1
  • 11
    • 84856894168 scopus 로고    scopus 로고
    • PEGylation of interferon-beta-1a: A promising strategy in multiple sclerosis
    • Kieseier BC, Calabresi PA (2012) PEGylation of interferon-beta-1a: a promising strategy in multiple sclerosis. CNS Drugs 26: 205-214.
    • (2012) CNS Drugs , vol.26 , pp. 205-214
    • Kieseier, B.C.1    Calabresi, P.A.2
  • 12
    • 0031766727 scopus 로고    scopus 로고
    • The structure of human interferon-beta: Implications for activity
    • DOI 10.1007/s000180050248
    • Karpusas M, Whitty A, Runkel L, Hochman P (1998) The structure of human interferon-beta: implications for activity. Cell Mol Life Sci 54: 1203-1216. (Pubitemid 28529112)
    • (1998) Cellular and Molecular Life Sciences , vol.54 , Issue.11 , pp. 1203-1216
    • Karpusas, M.1    Whitty, A.2    Runkel, L.3    Hochman, P.4
  • 14
    • 0019306804 scopus 로고
    • Expression of human fibroblast interferon gene in Escherichia coli
    • DOI 10.1038/287193a0
    • Derynck R, Remaut E, Saman E, Stanssens P, De Clercq E, et al. (1980) Expression of human fibroblast interferon gene in Escherichia coli. Nature 287: 193-197. (Pubitemid 10019764)
    • (1980) Nature , vol.287 , Issue.5779 , pp. 193-197
    • Derynck, R.1    Remaut, E.2    Saman, E.3
  • 16
    • 0024207853 scopus 로고
    • Comparative study of the asparagine-linked sugar chains of natural human interferon-beta1 and recombinant human interferon-beta1 produced by three different mammalian cells
    • Kagawa Y, Takasaki S, Utsumi J, Hosoi K, Shimizu H, et al. (1988) Comparative study of the asparagine-linked sugar chains of natural human interferon-beta 1 and recombinant human interferon-beta 1 produced by three different mammalian cells. J Biol Chem 263: 17508-17515. (Pubitemid 19029332)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.33 , pp. 17508-17515
    • Kagawa, Y.1    Takasaki, S.2    Utsumi, J.3    Hosoi, K.4    Shimizu, H.5    Kochibe, N.6    Kobata, A.7
  • 17
    • 67449119292 scopus 로고    scopus 로고
    • Effects of glycosylation on the stability of protein pharmaceuticals
    • Sola RJ, Griebenow K (2009) Effects of glycosylation on the stability of protein pharmaceuticals. J Pharm Sci 98: 1223-1245.
    • (2009) J Pharm Sci , vol.98 , pp. 1223-1245
    • Sola, R.J.1    Griebenow, K.2
  • 18
    • 11844291300 scopus 로고    scopus 로고
    • Protein aggregation and its inhibition in biopharmaceutics
    • Wang W (2005) Protein aggregation and its inhibition in biopharmaceutics. Int J Pharm 289: 1-30.
    • (2005) Int J Pharm , vol.289 , pp. 1-30
    • Wang, W.1
  • 19
    • 78649443723 scopus 로고    scopus 로고
    • High productivity of human recombinant beta-interferon from a lowtemperature perfusion culture
    • Rodriguez J, Spearman M, Tharmalingam T, Sunley K, Lodewyks C, et al. (2010) High productivity of human recombinant beta-interferon from a lowtemperature perfusion culture. J Biotechnol 150: 509-518.
    • (2010) J Biotechnol , vol.150 , pp. 509-518
    • Rodriguez, J.1    Spearman, M.2    Tharmalingam, T.3    Sunley, K.4    Lodewyks, C.5
  • 20
    • 13544255561 scopus 로고    scopus 로고
    • Enhanced production of monomeric interferon-beta by CHO cells through the control of culture conditions
    • DOI 10.1021/bp049807b
    • Rodriguez J, Spearman M, Huzel N, Butler M (2005) Enhanced production of monomeric interferon-beta by CHO cells through the control of culture conditions. Biotechnol Prog 21: 22-30. (Pubitemid 40218468)
    • (2005) Biotechnology Progress , vol.21 , Issue.1 , pp. 22-30
    • Rodriguez, J.1    Spearman, M.2    Huzel, N.3    Butler, M.4
  • 23
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner MF, Olson AJ, Spehner JC (1996) Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38: 305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Olson, A.J.2    Spehner, J.C.3
  • 24
    • 0035953960 scopus 로고    scopus 로고
    • Quantum mechanical study of the nonbonded forces in water-methanol complexes
    • Kirschner KN, Woods RJ (2001) Quantum mechanical study of the nonbonded forces in water-methanol complexes. J Phys Chem A 105: 4150-4155.
    • (2001) J Phys Chem A , vol.105 , pp. 4150-4155
    • Kirschner, K.N.1    Woods, R.J.2
  • 27
    • 33751080784 scopus 로고    scopus 로고
    • Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex
    • DOI 10.1110/ps.062283006
    • Quadt-Akabayov SR, Chill JH, Levy R, Kessler N, Anglister J (2006) Determination of the human type I interferon receptor binding site on human interferon-alpha2 by cross saturation and an NMR-based model of the complex. Protein Sci 15: 2656-2668. (Pubitemid 44771702)
    • (2006) Protein Science , vol.15 , Issue.11 , pp. 2656-2668
    • Quadt-Akabayov, S.R.1    Chill, J.H.2    Levy, R.3    Kessler, N.4    Anglister, J.5
  • 29
    • 84867154277 scopus 로고    scopus 로고
    • Saturable sinusoidal uptake is rate-determining process in hepatic elimination of docetaxel in rats
    • Yoon I, Han S, Choi YH, Kang HE, Cho HJ, et al. (2012) Saturable sinusoidal uptake is rate-determining process in hepatic elimination of docetaxel in rats. Xenobiotica 42: 1110-1119.
    • (2012) Xenobiotica , vol.42 , pp. 1110-1119
    • Yoon, I.1    Han, S.2    Choi, Y.H.3    Kang, H.E.4    Cho, H.J.5
  • 30
    • 84878862760 scopus 로고    scopus 로고
    • The limited intestinal absorption via paracellular pathway is responsible for the low oral bioavailability of doxorubicin
    • Kim JE, Cho HJ, Kim JS, Shim CK, Chung SJ, et al. (2013) The limited intestinal absorption via paracellular pathway is responsible for the low oral bioavailability of doxorubicin. Xenobiotica 43: 579-591.
    • (2013) Xenobiotica , vol.43 , pp. 579-591
    • Kim, J.E.1    Cho, H.J.2    Kim, J.S.3    Shim, C.K.4    Chung, S.J.5
  • 31
    • 4143097166 scopus 로고    scopus 로고
    • A new approach for determining the stability of recombinant human epidermal growth factor by thermal Fourier transform infrared (FTIR) microspectroscopy
    • Yang CH, Wu PC, Huang YB, Tsai YH (2004) A new approach for determining the stability of recombinant human epidermal growth factor by thermal Fourier transform infrared (FTIR) microspectroscopy. J Biomol Struct Dyn 22: 101-110. (Pubitemid 39095287)
    • (2004) Journal of Biomolecular Structure and Dynamics , vol.22 , Issue.1 , pp. 101-110
    • Yang, C.-H.1    Wu, P.-C.2    Huang, Y.-B.3    Tsai, Y.-H.4
  • 32
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation
    • Dong A, Prestrelski SJ, Allison SD, Carpenter JF (1995) Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation. J Pharm Sci 84: 415-424.
    • (1995) J Pharm Sci , vol.84 , pp. 415-424
    • Dong, A.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 34
    • 0004014257 scopus 로고
    • Computer Program, Department of Biochemistry and Molecular Biology, University College London
    • Hubbard SJT (1993) NACCESS. Computer Program, Department of Biochemistry and Molecular Biology, University College London.
    • (1993) NACCESS
    • Hubbard, S.J.T.1
  • 37
    • 46149089907 scopus 로고    scopus 로고
    • Effect of glycosylation on protein folding: A close look at thermodynamic stabilization
    • Shental-Bechor D, Levy Y (2008) Effect of glycosylation on protein folding: a close look at thermodynamic stabilization. Proc Natl Acad Sci U S A 105: 8256- 8261.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8256-8261
    • Shental-Bechor, D.1    Levy, Y.2
  • 38
    • 84970049990 scopus 로고
    • The Carbohydrate Frontier
    • Knight P (1989) The Carbohydrate Frontier. Bio-Technology 7: 35-&.
    • (1989) Bio-Technology , vol.7 , pp. 35
    • Knight, P.1
  • 40
    • 33845337623 scopus 로고    scopus 로고
    • Effectiveness of darbepoietin alfa in anemic patients with chronic kidney disease (CKD) in predialysis period
    • Wanic-Kossowska M, Tykarski A, Kobelski M, Czekalski S (2006) [Effectiveness of darbepoietin alfa in anemic patients with chronic kidney disease (CKD) in predialysis period]. Pol Arch Med Wewn 116: 663-670.
    • (2006) Pol Arch Med Wewn , vol.116 , pp. 663-670
    • Wanic-Kossowska, M.1    Tykarski, A.2    Kobelski, M.3    Czekalski, S.4
  • 41
    • 67149105612 scopus 로고    scopus 로고
    • Subcutaneous administration of darbepoetin alfa effectively maintains hemoglobin concentrations at extended dose intervals in peritoneal dialysis patients
    • Fang YW, Chang CH (2009) Subcutaneous administration of darbepoetin alfa effectively maintains hemoglobin concentrations at extended dose intervals in peritoneal dialysis patients. Perit Dial Int 29: 199-203.
    • (2009) Perit Dial Int , vol.29 , pp. 199-203
    • Fang, Y.W.1    Chang, C.H.2
  • 42
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • DOI 10.1038/nbt1252, PII NBT1252
    • Walsh G, Jefferis R (2006) Post-translational modifications in the context of therapeutic proteins. Nat Biotechnol 24: 1241-1252. (Pubitemid 44564769)
    • (2006) Nature Biotechnology , vol.24 , Issue.10 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 43
    • 0026787654 scopus 로고
    • Role of glycosylation on the secretion and biological activity of erythropoietin
    • Delorme E, Lorenzini T, Giffin J, Martin F, Jacobsen F, et al. (1992) Role of glycosylation on the secretion and biological activity of erythropoietin. Biochemistry 31: 9871-9876.
    • (1992) Biochemistry , vol.31 , pp. 9871-9876
    • Delorme, E.1    Lorenzini, T.2    Giffin, J.3    Martin, F.4    Jacobsen, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.