메뉴 건너뛰기




Volumn 131, Issue 1, 2013, Pages 78-88

Characterisation of the post-translational modifications of a novel, human cell line-derived recombinant human factor VIII

Author keywords

factor VIII inhibitors; Haemophilia A; HEK 293 F cell line; human cl rhFVIII; post translational modifications

Indexed keywords

EPITOPE; GALACTOSE; GLYCAN; MANNOSE; N GLYCOLOYLNEURAMINIC ACID; RECOMBINANT BLOOD CLOTTING FACTOR 8; RECOMBINANT HUMAN BLOOD CLOTTING FACTOR 8; UNCLASSIFIED DRUG;

EID: 84871660904     PISSN: 00493848     EISSN: 18792472     Source Type: Journal    
DOI: 10.1016/j.thromres.2012.09.011     Document Type: Article
Times cited : (109)

References (70)
  • 1
    • 77954506432 scopus 로고    scopus 로고
    • Rate of inhibitor development in previously-untreated hemophilia a patients treated with plasma-derived or recombinant factor VIII concentrates. A systematic review
    • A. Iorio, S. Halimeh, S. Holzhauer, N. Goldenberg, E. Marchesini, and M. Marcucci Rate of inhibitor development in previously-untreated hemophilia a patients treated with plasma-derived or recombinant factor VIII concentrates. A systematic review J Thromb Haemost 8 2010 1256 1265
    • (2010) J Thromb Haemost , vol.8 , pp. 1256-1265
    • Iorio, A.1    Halimeh, S.2    Holzhauer, S.3    Goldenberg, N.4    Marchesini, E.5    Marcucci, M.6
  • 2
    • 84871654769 scopus 로고    scopus 로고
    • C. Brower, A.R. Thompson, and A. Hemophilia accessed 30 Apr. 2010
    • C. Brower, A.R. Thompson, and A. Hemophilia http://www.ncbi.nlm.nih.gov/ bookshelf/br.fcgi?book=gene&part=hemo-a accessed 30 Apr. 2010
  • 3
    • 0141832940 scopus 로고    scopus 로고
    • Hemophilia: Treatment options in the twenty-first century
    • P.M. Mannucci Hemophilia: treatment options in the twenty-first century J Thromb Haemost 1 2003 1349 1355
    • (2003) J Thromb Haemost , vol.1 , pp. 1349-1355
    • Mannucci, P.M.1
  • 5
    • 0036588662 scopus 로고    scopus 로고
    • Progress in haemophilic care: Ethical issues
    • DOI 10.1046/j.1365-2516.2002.00615.x
    • E. Berntorp Progress in haemophilic care: ethical issues Haemophilia 8 2002 435 438 (Pubitemid 35277170)
    • (2002) Haemophilia , vol.8 , Issue.3 , pp. 435-438
    • Berntorp, E.1
  • 6
    • 78650360430 scopus 로고    scopus 로고
    • From human to humans - Introducing the first recombinant human FVIII product produced from a human line cell. A special symposium at the International Society on Thrombosis and Haemostasis (ISTH) Congress 2009
    • [loose insert]
    • E.G. Tuddenham, C. Kannicht, C. Agerkvist, H. Sandberg, S. Knaub, and N. Zozulya From human to humans - Introducing the first recombinant human FVIII product produced from a human line cell. A special symposium at the International Society on Thrombosis and Haemostasis (ISTH) Congress 2009 Thromb Haemost 103 2010 [loose insert]
    • (2010) Thromb Haemost , vol.103
    • Tuddenham, E.G.1    Kannicht, C.2    Agerkvist, C.3    Sandberg, H.4    Knaub, S.5    Zozulya, N.6
  • 8
    • 33745526819 scopus 로고    scopus 로고
    • Protein glycosylation in diverse cell systems: Implications for modification and analysis of recombinant proteins
    • DOI 10.1586/14789450.3.3.345
    • S.A. Brooks Protein glycosylation in diverse cell systems: implications for modification and analysis of recombinant proteins Expert Rev Proteomics 3 2006 345 359 (Pubitemid 43979408)
    • (2006) Expert Review of Proteomics , vol.3 , Issue.3 , pp. 345-359
    • Brooks, S.A.1
  • 9
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • DOI 10.1038/nbt1252, PII NBT1252
    • G. Walsh, and R. Jefferis Post-translational modifications in the context of therapeutic proteins Nat Biotechnol 24 2006 1241 1252 (Pubitemid 44564769)
    • (2006) Nature Biotechnology , vol.24 , Issue.10 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 10
    • 79951789201 scopus 로고    scopus 로고
    • A commentary on the differences in pharmacokinetics between recombinant and plasma-derived factor IX and their implications for dosing
    • S. Bjorkman A commentary on the differences in pharmacokinetics between recombinant and plasma-derived factor IX and their implications for dosing Haemophilia 17 2011 179 184
    • (2011) Haemophilia , vol.17 , pp. 179-184
    • Bjorkman, S.1
  • 12
    • 44249093256 scopus 로고    scopus 로고
    • Back to the future: A recent history of haemophilia treatment
    • DOI 10.1111/j.1365-2516.2008.01708.x, State of the Art.XXVIII International Congress of the World Federation of Hemophilia
    • P.M. Mannucci Back to the future: a recent history of haemophilia treatment Haemophilia 14 Suppl. 3 2008 10 18 (Pubitemid 351722377)
    • (2008) Haemophilia , vol.14 , Issue.SUPPL. 3 , pp. 10-18
    • Mannucci, P.M.1
  • 13
    • 79951806675 scopus 로고    scopus 로고
    • Patient and parent preferences for haemophilia A treatments
    • A.F. Mohamed, J.D. Epstein, and J.M. Li-McLeod Patient and parent preferences for haemophilia A treatments Haemophilia 17 1-3-2011 209 214
    • (2011) Haemophilia , vol.17 , pp. 209-214
    • Mohamed, A.F.1    Epstein, J.D.2    Li-Mcleod, J.M.3
  • 14
    • 43149125439 scopus 로고    scopus 로고
    • Physicians' preferences towards coagulation factor concentrates in the treatment of haemophilia with inhibitors: A discrete choice experiment
    • DOI 10.1111/j.1365-2516.2008.01656.x
    • W.C. Lee, A.V. Joshi, S. Woolford, M. Sumner, M. Brown, and N. Hadker Physicians' preferences towards coagulation factor concentrates in the treatment of Haemophilia with inhibitors: a discrete choice experiment Haemophilia 14 2008 454 465 (Pubitemid 351638731)
    • (2008) Haemophilia , vol.14 , Issue.3 , pp. 454-465
    • Lee, W.C.1    Joshi, A.V.2    Woolford, S.3    Sumner, M.4    Brown, M.5    Hadker, N.6    Pashos, C.L.7
  • 15
    • 33751010515 scopus 로고    scopus 로고
    • Recombinant vs. plasma-derived products, especially those with intact VWF, regarding inhibitor development
    • DOI 10.1111/j.1365-2516.2006.01373.x
    • C.E. Ettingshausen, and W. Kreuz Recombinant vs. plasma-derived products, especially those with intact VWF, regarding inhibitor development Haemophilia 12 Suppl. 6 2006 102 106 (Pubitemid 44741510)
    • (2006) Haemophilia , vol.12 , Issue.SUPPL. 6 , pp. 102-106
    • Ettingshausen, C.E.1    Kreuz, W.2
  • 16
    • 0030056318 scopus 로고    scopus 로고
    • Immune tolerance for the treatment of factor VIII inhibitors - Twenty years' 'Bonn protocol'
    • H.H. Brackmann, J. Oldenburg, and R. Schwaab Immune tolerance for the treatment of factor VIII inhibitors-twenty years' 'bonn protocol' Vox Sang 70 Suppl. 1 1996 30 35 (Pubitemid 26055992)
    • (1996) Vox Sanguinis , vol.70 , Issue.SUPPL. 1 , pp. 30-35
    • Brackmann, H.H.1    Oldenburg, J.2    Schwaab, R.3
  • 17
    • 34248220822 scopus 로고    scopus 로고
    • Current European practice in immune tolerance induction therapy in patients with haemophilia and inhibitors
    • J. Astermark, M. Morado, A. Rocino, H.M. van den Berg, D.M. Von, and A. Gringeri Current European practice in immune tolerance induction therapy in patients with haemophilia and inhibitors Haemophilia 12 2006 363 371
    • (2006) Haemophilia , vol.12 , pp. 363-371
    • Astermark, J.1    Morado, M.2    Rocino, A.3    Van Den Berg, H.M.4    Von, D.M.5    Gringeri, A.6
  • 19
    • 73349085222 scopus 로고    scopus 로고
    • Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII
    • M.P. Kosloski, R.D. Miclea, and S.V. Balu-Iyer Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII AAPS J 11 2009 424 431
    • (2009) AAPS J , vol.11 , pp. 424-431
    • Kosloski, M.P.1    Miclea, R.D.2    Balu-Iyer, S.V.3
  • 21
    • 75149183678 scopus 로고    scopus 로고
    • Glycosylation of therapeutic proteins: An effective strategy to optimize efficacy
    • R.J. Sola, and K. Griebenow Glycosylation of therapeutic proteins: an effective strategy to optimize efficacy BioDrugs 24 2010 9 21
    • (2010) BioDrugs , vol.24 , pp. 9-21
    • Sola, R.J.1    Griebenow, K.2
  • 22
    • 21644462706 scopus 로고    scopus 로고
    • Appropriate glycosylation of recombinant proteins for human use: Implications of choice of expression system
    • S.A. Brooks Appropriate glycosylation of recombinant proteins for human use: implications of choice of expression system Mol Biotechnol 28 2004 241 255
    • (2004) Mol Biotechnol , vol.28 , pp. 241-255
    • Brooks, S.A.1
  • 24
    • 84862883478 scopus 로고    scopus 로고
    • Prevention and prediction of inhibitor risk
    • J. Astermark Prevention and prediction of inhibitor risk Haemophilia 18 Suppl. 4 2012 38 42
    • (2012) Haemophilia , vol.18 , Issue.SUPPL. 4 , pp. 38-42
    • Astermark, J.1
  • 25
    • 84859408575 scopus 로고    scopus 로고
    • Current controversies in the formation and treatment of alloantibodies to factor VIII in congenital hemophilia A
    • R. Kruse-Jarres Current controversies in the formation and treatment of alloantibodies to factor VIII in congenital hemophilia A Hematology Am Soc Hematol Educ Program 2011 2011 407 412
    • (2011) Hematology Am Soc Hematol Educ Program , vol.2011 , pp. 407-412
    • Kruse-Jarres, R.1
  • 27
    • 80055114308 scopus 로고    scopus 로고
    • Can B-domain deletion alter the immunogenicity of recombinant factor VIII? A meta-analysis of prospective clinical studies
    • L.M. Aledort, R.J. Navickis, and M.M. Wilkes Can B-domain deletion alter the immunogenicity of recombinant factor VIII? A meta-analysis of prospective clinical studies J Thromb Haemost 9 2011 2180 2192
    • (2011) J Thromb Haemost , vol.9 , pp. 2180-2192
    • Aledort, L.M.1    Navickis, R.J.2    Wilkes, M.M.3
  • 28
    • 80055116249 scopus 로고    scopus 로고
    • Concentrate-related inhibitor risk: Is a difference always real?
    • A. Iorio, M. Marcucci, and M. Makris Concentrate-related inhibitor risk: is a difference always real? J Thromb Haemost 9 2011 2176 2179
    • (2011) J Thromb Haemost , vol.9 , pp. 2176-2179
    • Iorio, A.1    Marcucci, M.2    Makris, M.3
  • 30
    • 37149041623 scopus 로고    scopus 로고
    • Inhibitor development in haemophilia A: The role of von Willebrand factor/factor VIII concentrates
    • DOI 10.1111/j.1365-2516.2007.01507.x
    • J. Goudemand Inhibitor development in haemophilia A: the role of von Willebrand factor/factor VIII concentrates Haemophilia 13 Suppl. 5 2007 47 51 (Pubitemid 350253404)
    • (2007) Haemophilia , vol.13 , Issue.SUPPL. 5 , pp. 47-51
    • Goudemand, J.1
  • 31
    • 44649136183 scopus 로고    scopus 로고
    • The role of VWF for the success of immune tolerance induction
    • W. Kreuz The role of VWF for the success of immune tolerance induction Thromb Res 122 Suppl. 2 2008 S7 S12
    • (2008) Thromb Res , vol.122 , Issue.SUPPL. 2
    • Kreuz, W.1
  • 34
    • 4844227035 scopus 로고    scopus 로고
    • Relationships between factor VIII:Ag and factor VIII in recombinant and plasma-derived factor VIII concentrates
    • DOI 10.1111/j.1365-2516.2004.00957.x
    • Y. Lin, X. Yang, M.C. Chevrier, S. Craven, T.W. Barrowcliffe, and R. Lemieux Relationships between factor VIII:Ag and factor VIII in recombinant and plasma-derived factor VIII concentrates Haemophilia 10 2004 459 469 (Pubitemid 39317754)
    • (2004) Haemophilia , vol.10 , Issue.5 , pp. 459-469
    • Lin, Y.1    Yang, X.2    Chevrier, M.-C.3    Craven, S.4    Barrowcliffe, T.W.5    Lemieux, R.6    Ofoso, F.A.7
  • 35
    • 79955147317 scopus 로고    scopus 로고
    • Low incidence of factor VIII inhibitors in previously untreated patients during prophylaxis, on-demand treatment and surgical procedures, with Octanate®: Interim report from an ongoing prospective clinical study
    • A. Klukowska, V. Komrska, M. Jansen, and P. Laguna Low incidence of factor VIII inhibitors in previously untreated patients during prophylaxis, on-demand treatment and surgical procedures, with Octanate®: interim report from an ongoing prospective clinical study Haemophilia 17 1-12-2010 399 406
    • (2010) Haemophilia , vol.17 , pp. 399-406
    • Klukowska, A.1    Komrska, V.2    Jansen, M.3    Laguna, P.4
  • 36
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • DOI 10.1023/A:1026488408951
    • F. Altmann, E. Staudacher, I.B.H. Wilson, and L. März Insect cells as hosts for the expression of recombinant glycoproteins Glycoconj J 16 1999 109 123 (Pubitemid 29472137)
    • (1999) Glycoconjugate Journal , vol.16 , Issue.2 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.H.3    Marz, L.4
  • 37
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression systems in the pharmaceutical industry
    • DOI 10.1007/s00253-004-1656-9
    • F.R. Schmidt Recombinant expression systems in the pharmaceutical industry Appl Microbiol Biotechnol 65 2004 363 372 (Pubitemid 39281088)
    • (2004) Applied Microbiology and Biotechnology , vol.65 , Issue.4 , pp. 363-372
    • Schmidt, F.R.1
  • 38
    • 28244484911 scopus 로고    scopus 로고
    • The promise and challenges of bioengineered recombinant clotting factors
    • DOI 10.1111/j.1538-7836.2005.01367.x
    • S.W. Pipe The promise and challenges of bioengineered recombinant clotting factors J Thromb Haemost 3 2005 1692 1701 (Pubitemid 41716555)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.8 , pp. 1692-1701
    • Pipe, S.W.1
  • 40
    • 4444383627 scopus 로고    scopus 로고
    • Charge analysis of N-Glycans from human recombinant coagulation factor VIII and human FVIII standards [2]
    • W.F. Schilow, E. Schoerner-Burkhardt, and R. Seitz Charge analysis of N-glycans from human recombinant coagulation factor VIII and human FVIII standards Thromb Haemost 92 2004 427 428 (Pubitemid 39172325)
    • (2004) Thrombosis and Haemostasis , vol.92 , Issue.2 , pp. 427-428
    • Schilow, W.F.1    Schoerner-Burkhardt, E.2    Seitz, R.3
  • 41
    • 33746750608 scopus 로고    scopus 로고
    • Challenges in therapeutic glycoprotein production
    • DOI 10.1016/j.copbio.2006.06.010, PII S0958166906000942
    • N. Sethuraman, and T.A. Stadheim Challenges in therapeutic glycoprotein production Curr Opin Biotechnol 17 2006 341 346 (Pubitemid 44163459)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 341-346
    • Sethuraman, N.1    Stadheim, T.A.2
  • 42
    • 84863847365 scopus 로고    scopus 로고
    • The first recombinant human coagulation factor VIII of human origin: Human cell line and manufacturing characteristics
    • E. Casademunt, K. Martinelle, M. Jernberg, S. Winge, M. Tiemeyer, and L. Biesert The first recombinant human coagulation factor VIII of human origin: human cell line and manufacturing characteristics Eur J Haematol 89 2012 165 176
    • (2012) Eur J Haematol , vol.89 , pp. 165-176
    • Casademunt, E.1    Martinelle, K.2    Jernberg, M.3    Winge, S.4    Tiemeyer, M.5    Biesert, L.6
  • 44
    • 84862908041 scopus 로고    scopus 로고
    • Recombinant factor IX-Fc fusion protein (rFIXFc) demonstrates safety and prolonged activity in a phase 1/2a study in hemophilia B patients
    • A.D. Shapiro, M.V. Ragni, L.A. Valentino, N.S. Key, N.C. Josephson, and J.S. Powell Recombinant factor IX-Fc fusion protein (rFIXFc) demonstrates safety and prolonged activity in a phase 1/2a study in hemophilia B patients Blood 119 2012 666 672
    • (2012) Blood , vol.119 , pp. 666-672
    • Shapiro, A.D.1    Ragni, M.V.2    Valentino, L.A.3    Key, N.S.4    Josephson, N.C.5    Powell, J.S.6
  • 47
    • 84255201559 scopus 로고    scopus 로고
    • Characterization of gamma-carboxylated tryptic peptides by collision-induced dissociation and electron transfer dissociation mass spectrometry
    • M. Ramstrom, and H. Sandberg Characterization of gamma-carboxylated tryptic peptides by collision-induced dissociation and electron transfer dissociation mass spectrometry Eur J Mass Spectrom 17 2011 497 506
    • (2011) Eur J Mass Spectrom , vol.17 , pp. 497-506
    • Ramstrom, M.1    Sandberg, H.2
  • 48
    • 84871659373 scopus 로고    scopus 로고
    • Mass Spectrometry-Based Strategies for Characterization of N-glycosylation Sites of Human Coagulation Factor VIII Functional Domains
    • Bremen, Germany
    • M. Ramström, U. Eriksson, H. Sandberg. Mass Spectrometry-Based Strategies for Characterization of N-glycosylation Sites of Human Coagulation Factor VIII Functional Domains. 18th International Mass Spectrometry Conference 2009, Bremen, Germany.
    • (2009) 18th International Mass Spectrometry Conference
    • Ramström, M.1    Eriksson, U.2    Sandberg, H.3
  • 49
    • 0034568463 scopus 로고    scopus 로고
    • Carbohydrate analysis by high-performance anion-exchange chromatography with pulsed amperometric detection: The potential is still growing
    • T.R. Cataldi, C. Campa, and G.E. De Benedetto Carbohydrate analysis by high-performance anion-exchange chromatography with pulsed amperometric detection: the potential is still growing Fresenius J Anal Chem 368 2000 739 758
    • (2000) Fresenius J Anal Chem , vol.368 , pp. 739-758
    • Cataldi, T.R.1    Campa, C.2    De Benedetto, G.E.3
  • 50
    • 0026733430 scopus 로고
    • Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells
    • T. Hironaka, K. Furukawa, P.C. Esmon, M.A. Fournel, S. Sawada, and M. Kato Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells J Biol Chem 267 1992 8012 8020
    • (1992) J Biol Chem , vol.267 , pp. 8012-8020
    • Hironaka, T.1    Furukawa, K.2    Esmon, P.C.3    Fournel, M.A.4    Sawada, S.5    Kato, M.6
  • 53
    • 70449570719 scopus 로고    scopus 로고
    • Functional roles of the factor VIII B domain
    • S.W. Pipe Functional roles of the factor VIII B domain Haemophilia 15 2009 1187 1196
    • (2009) Haemophilia , vol.15 , pp. 1187-1196
    • Pipe, S.W.1
  • 55
    • 0029436859 scopus 로고
    • Characterization of a recombinant antihaemophilia-A factor (Factor VIII-deltaII) by matrix-assisted laser desorption/ionization mass spectrometry
    • N. Bihoreau, J.F. Veillon, C. Ramon, J.M. Scohyers, and J.M. Schmitter Characterization of a recombinant antihaemophilia-A factor (Factor VIII-deltaII) by matrix-assisted laser desorption/ionization mass spectrometry Rapid Commun Mass Spectrom 9 1995 1584 1588
    • (1995) Rapid Commun Mass Spectrom , vol.9 , pp. 1584-1588
    • Bihoreau, N.1    Veillon, J.F.2    Ramon, C.3    Scohyers, J.M.4    Schmitter, J.M.5
  • 56
    • 0023677854 scopus 로고
    • Association of the factor VIII light chain with von Willebrand factor
    • P. Lollar, D.C. Hill-Eubanks, and C.G. Parker Association of the factor VIII light chain with von Willebrand factor J Biol Chem 263 1988 10451 10455
    • (1988) J Biol Chem , vol.263 , pp. 10451-10455
    • Lollar, P.1    Hill-Eubanks, D.C.2    Parker, C.G.3
  • 57
    • 0025853365 scopus 로고
    • Heterogeneity in the tyrosine sulfation of Chinese hamster ovary cell produced recombinant FVIII
    • J. Mikkelsen, J. Thomsen, and M. Ezban Heterogeneity in the tyrosine sulfation of Chinese hamster ovary cell produced recombinant FVIII Biochemistry 30 1991 1533 1537
    • (1991) Biochemistry , vol.30 , pp. 1533-1537
    • Mikkelsen, J.1    Thomsen, J.2    Ezban, M.3
  • 59
    • 0026040327 scopus 로고
    • Insight into the structure, function, and biosynthesis of factor VIII through recombinant DNA technology
    • R.J. Kaufman Insight into the structure, function, and biosynthesis of factor VIII through recombinant DNA technology Ann Hematol 63 1991 155 165
    • (1991) Ann Hematol , vol.63 , pp. 155-165
    • Kaufman, R.J.1
  • 60
    • 0026619051 scopus 로고
    • Human urokinase contains GalNAcβ(1-4)[Fucα(1-3)] GlcNAcβ(1-2) as a novel terminal element in N-linked carbohydrate chains
    • DOI 10.1016/0014-5793(92)81512-K
    • A.A. Bergwerff, and J.E. Thomas-Oates van OJ, Kamerling JP, Vliegenthart JF. Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains FEBS Lett 314 1992 389 394 (Pubitemid 23005696)
    • (1992) FEBS Letters , vol.314 , Issue.3 , pp. 389-394
    • Bergwerff, A.A.1    Thomas Oates, J.E.2    Van Oostrum, J.3    Kamerling, J.P.4    Vliegenthart, J.F.G.5
  • 61
    • 0028885690 scopus 로고
    • Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities
    • A. Dell, H.R. Morris, R.L. Easton, M. Panico, M. Patankar, and S. Oehniger Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities J Biol Chem 270 1995 24116 24126
    • (1995) J Biol Chem , vol.270 , pp. 24116-24126
    • Dell, A.1    Morris, H.R.2    Easton, R.L.3    Panico, M.4    Patankar, M.5    Oehniger, S.6
  • 62
    • 0027718176 scopus 로고
    • Novel Asn-linked oligosaccharides terminating in GalNAcβ(1 → 4)[Fucα(1 → 3)]GlcNAcβ(1 → ·) are present in recombinant human Protein C expressed in human kidney 293 cells
    • S.B. Yan, and Y.B. Chao van HH. Novel Asn-linked oligosaccharides terminating in GalNAc beta (1->4)[Fuc alpha (1->3)]GlcNAc beta (1->.) are present in recombinant human protein C expressed in human kidney 293 cells Glycobiology 3 1993 597 608 (Pubitemid 24028867)
    • (1993) Glycobiology , vol.3 , Issue.6 , pp. 597-608
    • Yan, S.B.1    Chao, Y.B.2    Van Halbeek, H.3
  • 63
    • 0028299926 scopus 로고
    • Human protein C inhibits selectin-mediated cell adhesion: Role of unique fucosylated oligosaccharide
    • B.W. Grinnell, R.B. Hermann, and S.B. Yan Human protein C inhibits selectin-mediated cell adhesion: role of unique fucosylated oligosaccharide Glycobiology 4 1994 221 225 (Pubitemid 24147897)
    • (1994) Glycobiology , vol.4 , Issue.2 , pp. 221-225
    • Grinnell, B.W.1    Hermann, R.B.2    Yan, S.B.3
  • 64
    • 38749117878 scopus 로고    scopus 로고
    • The Galalpha1,3Galbeta1,4GlcNAc-R (alpha-Gal) epitope: A carbohydrate of unique evolution and clinical relevance
    • B.A. Macher, and U. Galili The Galalpha1,3Galbeta1,4GlcNAc-R (alpha-Gal) epitope: a carbohydrate of unique evolution and clinical relevance Biochim Biophys Acta 1780 2008 75 88
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 75-88
    • MacHer, B.A.1    Galili, U.2
  • 65
    • 58749102075 scopus 로고    scopus 로고
    • Sensitive and specific detection of the non-human sialic Acid N-glycolylneuraminic acid in human tissues and biotherapeutic products
    • S.L. Diaz, V. Padler-Karavani, D. Ghaderi, N. Hurtado-Ziola, H. Yu, and X. Chen Sensitive and specific detection of the non-human sialic Acid N-glycolylneuraminic acid in human tissues and biotherapeutic products PLoS One 4 2009 e4241
    • (2009) PLoS One , vol.4 , pp. 4241
    • Diaz, S.L.1    Padler-Karavani, V.2    Ghaderi, D.3    Hurtado-Ziola, N.4    Yu, H.5    Chen, X.6
  • 66
    • 33748467172 scopus 로고    scopus 로고
    • Xenotransplantation and ABO incompatible transplantation: The similarities they share
    • DOI 10.1016/j.transci.2006.05.007, PII S1473050206000905
    • U. Galili Xenotransplantation and ABO incompatible transplantation: the similarities they share Transfus Apher Sci 35 2006 45 58 (Pubitemid 44354321)
    • (2006) Transfusion and Apheresis Science , vol.35 , Issue.1 , pp. 45-58
    • Galili, U.1
  • 67
    • 0033565256 scopus 로고    scopus 로고
    • Increased immunogenicity of tumor vaccines complexed with anti-gal: Studies in knockout mice for α1,3galactosyltransferase
    • D.C. LaTemple, J.T. Abrams, S.Y. Zhang, and U. Galili Increased immunogenicity of tumor vaccines complexed with anti-Gal: studies in knockout mice for alpha1,3galactosyltransferase Cancer Res 59 1999 3417 3423 (Pubitemid 29334502)
    • (1999) Cancer Research , vol.59 , Issue.14 , pp. 3417-3423
    • LaTemple, D.C.1    Abrams, J.T.2    Zhang, S.Y.3    Galili, U.4
  • 68
    • 0021208290 scopus 로고
    • Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis
    • K. Yamashita, T. Ohkura, Y. Tachibana, S. Takasaki, and A. Kobata Comparative study of the oligosaccharides released from baby hamster kidney cells and their polyoma transformant by hydrazinolysis J Biol Chem 259 1984 10834 10840 (Pubitemid 14031211)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.17 , pp. 10834-10840
    • Yamashita, K.1    Ohkura, T.2    Tachibana, Y.3
  • 69
    • 0029823771 scopus 로고    scopus 로고
    • Elucidation of N-linked oligosaccharide structures of recombinant human Factor VIII using fluorophore-assisted carbohydrate electrophoresis
    • H.P. Kumar, C. Hague, T. Haley, C.M. Starr, M.J. Besman, and R.L. Lundblad Elucidation of N-linked oligosaccharide structures of recombinant human factor VIII using fluorophore-assisted carbohydrate electrophoresis Biotechnol Appl Biochem 24 Pt 3 1996 207 216 (Pubitemid 26414179)
    • (1996) Biotechnology and Applied Biochemistry , vol.24 , Issue.3 , pp. 207-216
    • Kumar, H.P.M.1    Hague, C.2    Haley, T.3    Starr, C.M.4    Besman, M.J.5    Lundblad, R.L.6    Baker, D.7
  • 70
    • 23144441143 scopus 로고    scopus 로고
    • GlyProt: In silico glycosylation of proteins
    • DOI 10.1093/nar/gki385
    • A. Bohne-Lang, and C.W. von der Lieth GlyProt: in silico glycosylation of proteins Nucleic Acids Res 33 2005 W214 W219 (Pubitemid 44529911)
    • (2005) Nucleic Acids Research , vol.33
    • Bohne-Lang, A.1    Von Der Lieth, C.-W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.