메뉴 건너뛰기




Volumn 9, Issue 2, 2014, Pages

Controllability analysis of protein glycosylation in Cho cells

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN;

EID: 84894639207     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0087973     Document Type: Article
Times cited : (42)

References (33)
  • 1
    • 79961191745 scopus 로고    scopus 로고
    • The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line
    • Xu X, Nagarajan H, Lewis NE, Pan S, Cai Z, et al. (2011) The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line. Nature Biotechnology 29: 735-U131.
    • (2011) Nature Biotechnology , vol.29
    • Xu, X.1    Nagarajan, H.2    Lewis, N.E.3    Pan, S.4    Cai, Z.5
  • 2
    • 68749110765 scopus 로고    scopus 로고
    • Optimal and consistent protein glycosylation in mammalian cell culture
    • Hossler P, Khattak SF, Li ZJ (2009) Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology 19: 936-949.
    • (2009) Glycobiology , vol.19 , pp. 936-949
    • Hossler, P.1    Khattak, S.F.2    Li, Z.J.3
  • 3
    • 0025840338 scopus 로고
    • The Oligosaccharides of Glycoproteins - Bioprocess Factors Affecting Oligosaccharide Structure and their Effect on Glycoprotein Properties
    • Goochee CF, Gramer MJ, Andersen DC, Bahr JB, Rasmussen JR (1991) The Oligosaccharides of Glycoproteins - Bioprocess Factors Affecting Oligosaccharide Structure and their Effect on Glycoprotein Properties. Bio-Technology 9: 1347-1355.
    • (1991) Bio-Technology , vol.9 , pp. 1347-1355
    • Goochee, C.F.1    Gramer, M.J.2    Andersen, D.C.3    Bahr, J.B.4    Rasmussen, J.R.5
  • 4
    • 33747362656 scopus 로고    scopus 로고
    • Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems
    • Butler M (2006) Optimisation of the cellular metabolism of glycosylation for recombinant proteins produced by mammalian cell systems. Cytotechnology 50: 57-76.
    • (2006) Cytotechnology , vol.50 , pp. 57-76
    • Butler, M.1
  • 5
    • 33845417633 scopus 로고    scopus 로고
    • Strategies for analysis of glycoprotein glycosylation
    • DOI 10.1016/j.bbapap.2006.10.007, PII S1570963906003487, Posttranslational Modifications in Proteomics
    • Geyer H, Geyer R (2006) Strategies for analysis of glycoprotein glycosylation. Biochimica Et Biophysica Acta-Proteins and Proteomics 1764: 1853-1869. (Pubitemid 44895032)
    • (2006) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1764 , Issue.12 , pp. 1853-1869
    • Geyer, H.1    Geyer, R.2
  • 7
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju TS (2008) Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Current Opinion in Immunology 20: 471-478.
    • (2008) Current Opinion in Immunology , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 8
    • 79952708279 scopus 로고    scopus 로고
    • FDA Revision 1. CDER C, editor. Rockiville, MD
    • FDA (2009) Q8(R1) Pharmaceutical Development Revision 1. In: CDER C, editor. Rockiville, MD.
    • (2009) Q8(R1) Pharmaceutical Development
  • 10
    • 0020945375 scopus 로고
    • Design of Resilient Processing Plants. 3. A General Framework for the Assessment of Dynamic Resilience
    • Morari M (1983) Design of Resilient Processing Plants. 3. A General Framework for the Assessment of Dynamic Resilience. Chemical Engineering Science 38: 1881-1891.
    • (1983) Chemical Engineering Science , vol.38 , pp. 1881-1891
    • Morari, M.1
  • 11
    • 0031095895 scopus 로고    scopus 로고
    • Comparison of Various Control Configurations for Continuous Bioreactors
    • Zhao Y, Skogestad S (1997) Comparison of various control configurations for continuous bioreactors. Industrial & Engineering Chemistry Research 36: 697-705. (Pubitemid 127493383)
    • (1997) Industrial and Engineering Chemistry Research , vol.36 , Issue.3 , pp. 697-705
    • Zhao, Y.1    Skogestad, S.2
  • 12
    • 0029700793 scopus 로고    scopus 로고
    • Controllability analysis of an industrial polymerization reactor
    • Lewin DR, Bogle D (1996) Controllability analysis of an industrial polymerization reactor. Computers & Chemical Engineering 20: S871-S876. (Pubitemid 126653505)
    • (1996) Computers and Chemical Engineering , vol.20 , Issue.SUPPL.2
    • Lewin, D.R.1    Bogle, D.2
  • 13
    • 42949177422 scopus 로고    scopus 로고
    • Quantitative comparison of dynamic controllability between a reactive distillation column and a conventional multi-unit process
    • DOI 10.1016/j.compchemeng.2007.06.022, PII S0098135407001743
    • Kaymak DB, Luyben WL (2008) Quantitative comparison of dynamic controllability between a reactive distillation column and a conventional multi-unit process. Computers & Chemical Engineering 32: 1456-1470. (Pubitemid 351608418)
    • (2008) Computers and Chemical Engineering , vol.32 , Issue.7 , pp. 1456-1470
    • Kaymak, D.B.1    Luyben, W.L.2
  • 15
    • 0343581263 scopus 로고    scopus 로고
    • A mathematical model of N-linked glycoform biosynthesis
    • DOI 10.1002/(SICI)1097-0290(19970920)55:6<890::AID
    • Umana P, Bailey JE (1997) A mathematical model of N-linked glycoform biosynthesis. Biotechnology and Bioengineering 55: 890-908. (Pubitemid 27360509)
    • (1997) Biotechnology and Bioengineering , vol.55 , Issue.6 , pp. 890-908
    • Umana, P.1    Bailey, J.E.2
  • 16
    • 28844473175 scopus 로고    scopus 로고
    • A mathematical model of N-linked glycosylation
    • DOI 10.1002/bit.20645
    • Krambeck FJ, Betenbaugh MJ (2005) A mathematical model of N-linked glycosylation. Biotechnology and Bioengineering 92: 711-728. (Pubitemid 41772467)
    • (2005) Biotechnology and Bioengineering , vol.92 , Issue.6 , pp. 711-728
    • Krambeck, F.J.1    Betenbaugh, M.J.2
  • 18
    • 40249093192 scopus 로고    scopus 로고
    • Systems Analysis of N-Glycan Processing in Mammalian Cells
    • Hossler P, Mulukutla BC, Hu WS (2007) Systems Analysis of N-Glycan Processing in Mammalian Cells. Plos One 2.
    • (2007) Plos One , vol.2
    • Hossler, P.1    Mulukutla, B.C.2    Hu, W.S.3
  • 19
    • 82955237386 scopus 로고    scopus 로고
    • A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus
    • del Val IJ, Nagy JM, Kontoravdi C (2011) A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus. Biotechnology Progress 27: 1730-1743.
    • (2011) Biotechnology Progress , vol.27 , pp. 1730-1743
    • Del Val, I.J.1    Nagy, J.M.2    Kontoravdi, C.3
  • 20
    • 0033900506 scopus 로고    scopus 로고
    • New measure of process output controllability
    • DOI 10.1016/S0959-1524(99)00045-1
    • Vinson DR, Georgakis C (2000) A new measure of process output controllability. Journal of Process Control 10: 185-194. (Pubitemid 30556716)
    • (2000) Journal of Process Control , vol.10 , Issue.2 , pp. 185-194
    • Vinson, D.R.1    Georgakis, C.2
  • 23
    • 0003493786 scopus 로고    scopus 로고
    • 3rd ed. Rockville, MD: Pearson Addison Wesley
    • Lay DC (2006) Linear Algebra and its Applications. 3rd ed. Rockville, MD: Pearson Addison Wesley. pp. 471-481.
    • (2006) Linear Algebra and Its Applications , pp. 471-481
    • Lay, D.C.1
  • 27
    • 33646070900 scopus 로고    scopus 로고
    • Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous beta 1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II
    • Ferrara C, Brunker P, Suter T, Moser S, Puntener U, et al. (2006) Modulation of therapeutic antibody effector functions by glycosylation engineering: Influence of Golgi enzyme localization domain and co-expression of heterologous beta 1,4-N-acetylglucosaminyltransferase III and Golgi alpha-mannosidase II. Biotechnology and Bioengineering 93: 851-861.
    • (2006) Biotechnology and Bioengineering , vol.93 , pp. 851-861
    • Ferrara, C.1    Brunker, P.2    Suter, T.3    Moser, S.4    Puntener, U.5
  • 28
    • 0032032778 scopus 로고    scopus 로고
    • Synthesis of bisected glycoforms of recombinant IFN-beta by overexpression of beta-l,4-N-acetylglucosaminyltransferase III in Chinese hamster ovary cells
    • DOI 10.1021/bp970118s
    • Sburlati AR, Umana P, Prati EGP, Bailey JE (1998) Synthesis of bisected glycoforms of recombinant IFN-beta by overexpression of beta-1,4-N-acetylglu- cosaminyltransferase III in Chinese hamster ovary cells. Biotechnology Progress 14: 189-192. (Pubitemid 28202601)
    • (1998) Biotechnology Progress , vol.14 , Issue.2 , pp. 189-192
    • Sburlati, A.R.1    Umana, P.2    Prati, E.G.P.3    Bailey, J.E.4
  • 29
    • 0033527910 scopus 로고    scopus 로고
    • Tetracycline-regulated overexpression of glycosyltransferases in Chinese hamster ovary cells
    • DOI 10.1002/(SICI)1097-0290(19991205)65:5<542::AID
    • Umana P, Jean-Mairet J, Bailey JE (1999) Tetracycline-regulated overexpression of glycosyltransferases in Chinese hamster ovary cells. Biotechnology and Bioengineering 65: 542-549. (Pubitemid 29513646)
    • (1999) Biotechnology and Bioengineering , vol.65 , Issue.5 , pp. 542-549
    • Umana, P.1    Jean-Mairet, J.2    Bailey, J.E.3
  • 30
    • 33750835115 scopus 로고    scopus 로고
    • Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies
    • DOI 10.1517/14712598.6.11.1161
    • Satoh M, Iida S, Shitara K (2006) Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies. Expert Opinion on Biological Therapy 6: 1161-1173. (Pubitemid 44714143)
    • (2006) Expert Opinion on Biological Therapy , vol.6 , Issue.11 , pp. 1161-1173
    • Satoh, M.1    Iida, S.2    Shitara, K.3
  • 31
    • 33644825884 scopus 로고    scopus 로고
    • Effects of elevated ammonium on glycosylation gene expression in CHO cells
    • Chen PF, Harcum SW (2006) Effects of elevated ammonium on glycosylation gene expression in CHO cells. Metabolic Engineering 8: 123-132.
    • (2006) Metabolic Engineering , vol.8 , pp. 123-132
    • Chen, P.F.1    Harcum, S.W.2
  • 33
    • 78149250500 scopus 로고    scopus 로고
    • An Investigation of Intracellular Glycosylation Activities in CHO Cells: Effects of Nucleotide Sugar Precursor Feeding
    • Wong NSC, Wati L, Nissom PM, Feng HT, Lee MM, et al. (2010) An Investigation of Intracellular Glycosylation Activities in CHO Cells: Effects of Nucleotide Sugar Precursor Feeding. Biotechnology and Bioengineering 107: 321-336.
    • (2010) Biotechnology and Bioengineering , vol.107 , pp. 321-336
    • Wong, N.S.C.1    Wati, L.2    Nissom, P.M.3    Feng, H.T.4    Lee, M.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.