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Volumn 287, Issue 29, 2012, Pages 24313-24319

Significant impact of single N-glycan residues on the biological activity of Fc-based antibody-like fragments

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY-DEPENDENT CELLULAR CYTOTOXICITIES; ANTIGEN-BINDING SITES; CORE OLIGOSACCHARIDE; EXPRESSION SYSTEM; GLYCOFORMS; HUMAN CELLS; HUMAN TUMOR CELLS; IMMUNE RESPONSE; N-GLYCAN; N-GLYCANS; PRESENCE/ABSENCE; RECEPTOR BINDING; SIGNIFICANT IMPACTS; THERAPEUTIC APPLICATION; WILD TYPES;

EID: 84863806221     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.360701     Document Type: Article
Times cited : (27)

References (30)
  • 1
    • 60849128549 scopus 로고    scopus 로고
    • Monoclonal antibodies as innovative therapeutics
    • Reichert, J. M. (2008) Monoclonal antibodies as innovative therapeutics. Curr. Pharm. Biotechnol. 9, 423-430
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 423-430
    • Reichert, J.M.1
  • 2
    • 77957361348 scopus 로고    scopus 로고
    • Development trends for human monoclonal antibody therapeutics
    • Nelson, A. L., Dhimolea, E., and Reichert, J. M. (2010) Development trends for human monoclonal antibody therapeutics. Nat. Rev. Drug Discov. 9, 767-774
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 767-774
    • Nelson, A.L.1    Dhimolea, E.2    Reichert, J.M.3
  • 3
    • 60849102193 scopus 로고    scopus 로고
    • Development of novel protein scaffolds as alternatives to whole antibodies for imaging and therapy. Status on discovery research and clinical validation
    • Wurch, T., Lowe, P., Caussanel, V., Bes, C., Beck, A., and Corvaia, N. (2008) Development of novel protein scaffolds as alternatives to whole antibodies for imaging and therapy. Status on discovery research and clinical validation. Curr. Pharm. Biotechnol. 9, 502-509
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 502-509
    • Wurch, T.1    Lowe, P.2    Caussanel, V.3    Bes, C.4    Beck, A.5    Corvaia, N.6
  • 4
    • 64349107630 scopus 로고    scopus 로고
    • Development trends for therapeutic antibody fragments
    • Nelson, A. L., and Reichert, J. M. (2009) Development trends for therapeutic antibody fragments. Nat. Biotechnol. 27, 331-337
    • (2009) Nat. Biotechnol. , vol.27 , pp. 331-337
    • Nelson, A.L.1    Reichert, J.M.2
  • 6
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis, R. (2009) Glycosylation as a strategy to improve antibody-based therapeutics. Nat. Rev. Drug Discov. 8, 226-234
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 10
    • 79953718390 scopus 로고    scopus 로고
    • Emerging antibody products and Nicotiana manufacturing
    • Whaley, K. J., Hiatt, A., and Zeitlin, L. (2011) Emerging antibody products and Nicotiana manufacturing. Human Vaccines 7, 349-356
    • (2011) Human Vaccines , vol.7 , pp. 349-356
    • Whaley, K.J.1    Hiatt, A.2    Zeitlin, L.3
  • 12
    • 24944498904 scopus 로고    scopus 로고
    • Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants
    • DOI 10.1038/nbt1094
    • Marillonnet, S., Thoeringer, C., Kandzia, R., Klimyuk, V., and Gleba, Y. (2005) Systemic Agrobacterium tumefaciens-mediated transfection of viral replicons for efficient transient expression in plants. Nat. Biotechnol. 23, 718-723 (Pubitemid 41716362)
    • (2005) Nature Biotechnology , vol.23 , Issue.6 , pp. 718-723
    • Marillonnet, S.1    Thoeringer, C.2    Kandzia, R.3    Klimyuk, V.4    Gleba, Y.5
  • 16
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher, Y., Perret, S., and Kamen, A. (2002) High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 30, E9
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 17
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • Stadlmann, J., Pabst, M., Kolarich, D., Kunert, R., and Altmann, F. (2008) Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics 8, 2858-2871
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 18
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcgamma receptor in complex with Fc
    • Radaev, S., Motyka, S., Fridman, W. H., Sautes-Fridman, C., and Sun, P. D. (2001) The structure of a human type III Fcgamma receptor in complex with Fc. J. Biol. Chem. 276, 16469-16477
    • (2001) J. Biol. Chem. , vol.276 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 19
    • 41749105290 scopus 로고    scopus 로고
    • Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure
    • DOI 10.1111/j.1467-7652.2008.00330.x
    • Strasser, R., Stadlmann, J., Schähs, M., Stiegler, G., Quendler, H., Mach, L., Glössl, J., Weterings, K., Pabst, M., and Steinkellner, H. (2008) Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure. Plant Biotechnol. J. 6, 392-402 (Pubitemid 351490228)
    • (2008) Plant Biotechnology Journal , vol.6 , Issue.4 , pp. 392-402
    • Strasser, R.1    Stadlmann, J.2    Schahs, M.3    Stiegler, G.4    Quendler, H.5    Mach, L.6    Glossl, J.7    Weterings, K.8    Pabst, M.9    Steinkellner, H.10
  • 20
    • 78650656127 scopus 로고    scopus 로고
    • Fc-glycosylation influences Fcγ receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12
    • Forthal, D. N., Gach, J. S., Landucci, G., Jez, J., Strasser, R., Kunert, R., and Steinkellner, H. (2010) Fc-glycosylation influences Fcγ receptor binding and cell-mediated anti-HIV activity of monoclonal antibody 2G12. J. Immunol. 185, 6876-6882
    • (2010) J. Immunol. , vol.185 , pp. 6876-6882
    • Forthal, D.N.1    Gach, J.S.2    Landucci, G.3    Jez, J.4    Strasser, R.5    Kunert, R.6    Steinkellner, H.7
  • 21
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses
    • Bruhns, P., Iannascoli, B., England, P., Mancardi, D. A., Fernandez, N., Jorieux, S., and Daëron, M. (2009) Specificity and affinity of human Fcγ receptors and their polymorphic variants for human IgG subclasses. Blood 113, 3716-3725
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6    Daëron, M.7
  • 22
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162: An element required for high affinity binding to non-fucosylated IgG glycoforms
    • DOI 10.1074/jbc.M510171200
    • Ferrara, C., Stuart, F., Sondermann, P., Brünker, P., and Umaña, P. (2006) The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J. Biol. Chem. 281, 5032-5036 (Pubitemid 43847767)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.8 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brunker, P.4    Umana, P.5
  • 23
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • DOI 10.1074/jbc.M202069200
    • Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H., and Presta, L. G. (2002) Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcγ RIII and antibody- dependent cellular toxicity. J. Biol. Chem. 277, 26733-26740 (Pubitemid 34951677)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Gloria, M.Y.6    Weikert, S.H.A.7    Presta, L.G.8
  • 25
    • 84855857695 scopus 로고    scopus 로고
    • Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds
    • Wozniak-Knopp, G., Stadlmann, J., and Rüker, F. (2012) Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds. PLoS One 7, e30083
    • (2012) PLoS One , vol.7
    • Wozniak-Knopp, G.1    Stadlmann, J.2    Rüker, F.3
  • 29
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-FcgammaRIII complex
    • DOI 10.1038/35018508
    • Sondermann, P., Huber, R., Oosthuizen, V., and Jacob, U. (2000) The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 406, 267-273 (Pubitemid 30604397)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthulzen, V.3    Jacob, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.