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Volumn 34, Issue 11, 2016, Pages 895-908

The Highly Evolvable Antibody Fc Domain

Author keywords

antibody engineering; antibody Fc; effector functions; serum half life

Indexed keywords

ANTIGENS; BINS; BODY FLUIDS; DIAGNOSIS;

EID: 84965102123     PISSN: 01677799     EISSN: 18793096     Source Type: Journal    
DOI: 10.1016/j.tibtech.2016.04.005     Document Type: Review
Times cited : (39)

References (71)
  • 1
    • 84920502297 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2014
    • 1 Walsh, G., Biopharmaceutical benchmarks 2014. Nat. Biotech. 32 (2014), 992–1000.
    • (2014) Nat. Biotech. , vol.32 , pp. 992-1000
    • Walsh, G.1
  • 2
    • 84889806552 scopus 로고    scopus 로고
    • In-depth qualitative and quantitative analysis of composite glycosylation profiles and other micro-heterogeneity on intact monoclonal antibodies by high-resolution native mass spectrometry using a modified Orbitrap
    • 2 Rosati, S., et al. In-depth qualitative and quantitative analysis of composite glycosylation profiles and other micro-heterogeneity on intact monoclonal antibodies by high-resolution native mass spectrometry using a modified Orbitrap. mAbs 5 (2013), 917–924.
    • (2013) mAbs , vol.5 , pp. 917-924
    • Rosati, S.1
  • 3
    • 84947032537 scopus 로고    scopus 로고
    • The structural role of antibody N-glycosylation in receptor interactions
    • 3 Subedi, G.P., Barb, A.W., The structural role of antibody N-glycosylation in receptor interactions. Structure 23 (2015), 1573–1583.
    • (2015) Structure , vol.23 , pp. 1573-1583
    • Subedi, G.P.1    Barb, A.W.2
  • 4
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • 4 Jefferis, R., Glycosylation as a strategy to improve antibody-based therapeutics. Nat. Rev. Drug Discov. 8 (2009), 226–234.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 5
    • 84922807192 scopus 로고    scopus 로고
    • The current status and prospects of antibody engineering for therapeutic use: focus on glycoengineering technology
    • 5 Niwa, R., Satoh, M., The current status and prospects of antibody engineering for therapeutic use: focus on glycoengineering technology. J. Pharm. Sci. 104 (2015), 930–941.
    • (2015) J. Pharm. Sci. , vol.104 , pp. 930-941
    • Niwa, R.1    Satoh, M.2
  • 6
    • 84863470971 scopus 로고    scopus 로고
    • Marketing approval of mogamulizumab: a triumph for glyco-engineering
    • 6 Beck, A., Reichert, J.M., Marketing approval of mogamulizumab: a triumph for glyco-engineering. mAbs 4 (2012), 419–425.
    • (2012) mAbs , vol.4 , pp. 419-425
    • Beck, A.1    Reichert, J.M.2
  • 7
    • 84923031045 scopus 로고    scopus 로고
    • Clinical role of obinutuzumab in the treatment of naive patients with chronic lymphocytic leukemia
    • 7 Cerquozzi, S., Owen, C., Clinical role of obinutuzumab in the treatment of naive patients with chronic lymphocytic leukemia. Biologics: Targets Ther. 9 (2015), 13–22.
    • (2015) Biologics: Targets Ther. , vol.9 , pp. 13-22
    • Cerquozzi, S.1    Owen, C.2
  • 8
    • 0029946383 scopus 로고    scopus 로고
    • ‘Knobs-into-holes’ engineering of antibody CH3 domains for heavy chain heterodimerization
    • 8 Ridgway, J.B.B., et al. ‘Knobs-into-holes’ engineering of antibody CH3 domains for heavy chain heterodimerization. Protein Eng. 9 (1996), 617–621.
    • (1996) Protein Eng. , vol.9 , pp. 617-621
    • Ridgway, J.B.B.1
  • 9
    • 84929454314 scopus 로고    scopus 로고
    • Engineering antibodies for dual specificity and enhanced potency
    • 9 Ko, S., Jung, S., Engineering antibodies for dual specificity and enhanced potency. Biotechnol. Bioproc. E. 20 (2015), 201–210.
    • (2015) Biotechnol. Bioproc. E. , vol.20 , pp. 201-210
    • Ko, S.1    Jung, S.2
  • 10
    • 84889850198 scopus 로고    scopus 로고
    • Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity
    • 10 Shatz, W., et al. Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity. mAbs 5 (2013), 872–881.
    • (2013) mAbs , vol.5 , pp. 872-881
    • Shatz, W.1
  • 11
    • 84904627207 scopus 로고    scopus 로고
    • Type I and type II Fc receptors regulate innate and adaptive immunity
    • 11 Pincetic, A., et al. Type I and type II Fc receptors regulate innate and adaptive immunity. Nat. Immunol. 15 (2014), 707–716.
    • (2014) Nat. Immunol. , vol.15 , pp. 707-716
    • Pincetic, A.1
  • 12
    • 84942919876 scopus 로고    scopus 로고
    • In vitro glycoengineering of IgG1 and Its effect on Fc receptor binding and ADCC activity
    • 12 Thomann, M., et al. In vitro glycoengineering of IgG1 and Its effect on Fc receptor binding and ADCC activity. PLoS ONE, 10, 2015, e0134949.
    • (2015) PLoS ONE , vol.10 , pp. e0134949
    • Thomann, M.1
  • 13
    • 84964411843 scopus 로고    scopus 로고
    • Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion
    • 13 Liu, R., et al. Evaluation of a glycoengineered monoclonal antibody via LC-MS analysis in combination with multiple enzymatic digestion. mAbs 8 (2016), 340–346.
    • (2016) mAbs , vol.8 , pp. 340-346
    • Liu, R.1
  • 14
    • 33645218704 scopus 로고    scopus 로고
    • Engineered antibody Fc variants with enhanced effector function
    • 14 Lazar, G.A., et al. Engineered antibody Fc variants with enhanced effector function. Proc. Natl. Acad. Sci. U.S.A. 103 (2006), 4005–4010.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4005-4010
    • Lazar, G.A.1
  • 15
    • 76249100176 scopus 로고    scopus 로고
    • Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells
    • 15 Jung, S.T., et al. Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells. Proc. Natl. Acad. Sci. U.S.A. 107 (2010), 604–609.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 604-609
    • Jung, S.T.1
  • 16
    • 84874101229 scopus 로고    scopus 로고
    • Effective phagocytosis of low Her2 tumor cell lines with engineered, aglycosylated IgG displaying high Fc gamma RIIa affinity and selectivity
    • 16 Jung, S.T., et al. Effective phagocytosis of low Her2 tumor cell lines with engineered, aglycosylated IgG displaying high Fc gamma RIIa affinity and selectivity. ACS Chem. Biol. 8 (2013), 368–375.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 368-375
    • Jung, S.T.1
  • 17
    • 58149510052 scopus 로고    scopus 로고
    • Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors
    • 17 Sazinsky, S.L., et al. Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors. Proc. Natl. Acad. Sci. U.S.A. 105 (2008), 20167–20172.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 20167-20172
    • Sazinsky, S.L.1
  • 18
    • 34548770705 scopus 로고    scopus 로고
    • Fc Optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion In vivo via low-affinity activating Fc gamma receptors
    • 18 Stavenhagen, J.B., et al. Fc Optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion In vivo via low-affinity activating Fc gamma receptors. Cancer Res. 67 (2007), 8882–8890.
    • (2007) Cancer Res. , vol.67 , pp. 8882-8890
    • Stavenhagen, J.B.1
  • 19
    • 77958167235 scopus 로고    scopus 로고
    • Fc-engineered anti-CD40 antibody enhances multiple effector functions and exhibits potent in vitro and in vivo antitumor activity against hematologic malignancies
    • 19 Horton, H.M., et al. Fc-engineered anti-CD40 antibody enhances multiple effector functions and exhibits potent in vitro and in vivo antitumor activity against hematologic malignancies. Blood 116 (2010), 3004–3012.
    • (2010) Blood , vol.116 , pp. 3004-3012
    • Horton, H.M.1
  • 20
    • 54249100952 scopus 로고    scopus 로고
    • Potent in vitro and in vivo activity of an Fc-engineered anti-CD19 monoclonal antibody against lymphoma and leukemia
    • 20 Horton, H.M., et al. Potent in vitro and in vivo activity of an Fc-engineered anti-CD19 monoclonal antibody against lymphoma and leukemia. Cancer Res. 68 (2008), 8049–8057.
    • (2008) Cancer Res. , vol.68 , pp. 8049-8057
    • Horton, H.M.1
  • 21
    • 84864561123 scopus 로고    scopus 로고
    • Enhanced ADCC activity of affinity maturated and Fc-engineered mini-antibodies directed against the AML stem cell antigen CD96
    • 21 Mohseni Nodehi, S., et al. Enhanced ADCC activity of affinity maturated and Fc-engineered mini-antibodies directed against the AML stem cell antigen CD96. PLoS ONE, 7, 2012, e42426.
    • (2012) PLoS ONE , vol.7 , pp. e42426
    • Mohseni Nodehi, S.1
  • 22
    • 53349120501 scopus 로고    scopus 로고
    • Optimization of antibody binding to Fc gamma RIIa enhances macrophage phagocytosis of tumor cells
    • 22 Richards, J.O., et al. Optimization of antibody binding to Fc gamma RIIa enhances macrophage phagocytosis of tumor cells. Mol. Cancer Ther. 7 (2008), 2517–2527.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2517-2527
    • Richards, J.O.1
  • 23
    • 82255167636 scopus 로고    scopus 로고
    • Anti-tumor activity and toxicokinetics analysis of MGAH22, an anti-HER2 monoclonal antibody with enhanced Fc gamma receptor binding properties
    • 23 Nordstrom, J., et al. Anti-tumor activity and toxicokinetics analysis of MGAH22, an anti-HER2 monoclonal antibody with enhanced Fc gamma receptor binding properties. Breast Cancer Res., 13, 2011, R123.
    • (2011) Breast Cancer Res. , vol.13 , pp. R123
    • Nordstrom, J.1
  • 24
    • 84863928141 scopus 로고    scopus 로고
    • Development of an Fc-enhanced anti-B7-H3 monoclonal antibody with potent antitumor activity
    • 24 Loo, D., et al. Development of an Fc-enhanced anti-B7-H3 monoclonal antibody with potent antitumor activity. Clin. Cancer Res. 18 (2012), 3834–3845.
    • (2012) Clin. Cancer Res. , vol.18 , pp. 3834-3845
    • Loo, D.1
  • 25
    • 84945289818 scopus 로고    scopus 로고
    • Structural analysis of Fc/Fc gamma R complexes: a blueprint for antibody design
    • 25 Caaveiro, J.M.M., et al. Structural analysis of Fc/Fc gamma R complexes: a blueprint for antibody design. Immunol. Rev. 268 (2015), 201–221.
    • (2015) Immunol. Rev. , vol.268 , pp. 201-221
    • Caaveiro, J.M.M.1
  • 26
    • 84896718811 scopus 로고    scopus 로고
    • Asymmetrical Fc engineering greatly enhances antibody-dependent cellular cytotoxicity (ADCC) effector function and stability of the modified antibodies
    • 26 Liu, Z., et al. Asymmetrical Fc engineering greatly enhances antibody-dependent cellular cytotoxicity (ADCC) effector function and stability of the modified antibodies. J. Biol. Chem. 289 (2014), 3571–3590.
    • (2014) J. Biol. Chem. , vol.289 , pp. 3571-3590
    • Liu, Z.1
  • 27
    • 49449109842 scopus 로고    scopus 로고
    • Inhibition of B cell receptor-mediated activation of primary human B cells by coengagement of CD19 and Fc gamma RIIb with Fc-engineered antibodies
    • 27 Chu, S.Y., et al. Inhibition of B cell receptor-mediated activation of primary human B cells by coengagement of CD19 and Fc gamma RIIb with Fc-engineered antibodies. Mol. Immunol. 45 (2008), 3926–3933.
    • (2008) Mol. Immunol. , vol.45 , pp. 3926-3933
    • Chu, S.Y.1
  • 28
    • 84885007880 scopus 로고    scopus 로고
    • Engineered antibody Fc variant with selectively enhanced Fc gamma RIIb binding over both Fc gamma RIIa(R131) and Fc gamma RIIa(H131)
    • 28 Mimoto, F., et al. Engineered antibody Fc variant with selectively enhanced Fc gamma RIIb binding over both Fc gamma RIIa(R131) and Fc gamma RIIa(H131). Protein Eng. Des. Sel. 26 (2013), 589–598.
    • (2013) Protein Eng. Des. Sel. , vol.26 , pp. 589-598
    • Mimoto, F.1
  • 29
    • 84919949974 scopus 로고    scopus 로고
    • IgGA: a ‘cross-isotype’ engineered human Fc antibody domain that displays both IgG-like and IgA-like effector functions
    • 29 Kelton, W., et al. IgGA: a ‘cross-isotype’ engineered human Fc antibody domain that displays both IgG-like and IgA-like effector functions. Chem. Biol. 21 (2014), 1603–1609.
    • (2014) Chem. Biol. , vol.21 , pp. 1603-1609
    • Kelton, W.1
  • 30
    • 84872496673 scopus 로고    scopus 로고
    • Generation and comparative characterization of glycosylated and aglycosylated human IgG1 antibodies
    • 30 Hristodorov, D., et al. Generation and comparative characterization of glycosylated and aglycosylated human IgG1 antibodies. Mol. Biotechnol. 53 (2013), 326–335.
    • (2013) Mol. Biotechnol. , vol.53 , pp. 326-335
    • Hristodorov, D.1
  • 31
    • 84904344421 scopus 로고    scopus 로고
    • Aglycosylated full-length IgG antibodies: steps toward next-generation immunotherapeutics
    • 31 Ju, M-S., Jung, S.T., Aglycosylated full-length IgG antibodies: steps toward next-generation immunotherapeutics. Curr. Opin. Biotech. 30 (2014), 128–139.
    • (2014) Curr. Opin. Biotech. , vol.30 , pp. 128-139
    • Ju, M.-S.1    Jung, S.T.2
  • 32
    • 84904364868 scopus 로고    scopus 로고
    • Engineering an aglycosylated Fc variant for enhanced Fc gamma RI engagement and pH-dependent human FcRn binding
    • 32 Jung, S., Kang, T.H., Engineering an aglycosylated Fc variant for enhanced Fc gamma RI engagement and pH-dependent human FcRn binding. Biotechnol. Bioproc. E. 19 (2014), 780–789.
    • (2014) Biotechnol. Bioproc. E. , vol.19 , pp. 780-789
    • Jung, S.1    Kang, T.H.2
  • 33
    • 84867836578 scopus 로고    scopus 로고
    • Revisiting the role of glycosylation in the structure of human IgG Fc
    • 33 Borrok, M.J., et al. Revisiting the role of glycosylation in the structure of human IgG Fc. ACS Chem. Biol. 7 (2012), 1596–1602.
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1596-1602
    • Borrok, M.J.1
  • 34
    • 80052622662 scopus 로고    scopus 로고
    • Bypassing glycosylation: engineering aglycosylated full-length IgG antibodies for human therapy
    • 34 Jung, S.T., et al. Bypassing glycosylation: engineering aglycosylated full-length IgG antibodies for human therapy. Curr. Opin. Biotech. 22 (2011), 858–867.
    • (2011) Curr. Opin. Biotech. , vol.22 , pp. 858-867
    • Jung, S.T.1
  • 35
    • 84940959004 scopus 로고    scopus 로고
    • Structural consequences of aglycosylated IgG Fc variants evolved for Fc gamma RI binding
    • 35 Ju, M-S., et al. Structural consequences of aglycosylated IgG Fc variants evolved for Fc gamma RI binding. Mol. Immunol. 67 (2015), 350–356.
    • (2015) Mol. Immunol. , vol.67 , pp. 350-356
    • Ju, M.-S.1
  • 36
    • 0034655265 scopus 로고    scopus 로고
    • Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc
    • 36 Idusogie, E.E., et al. Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc. J. Immunol. 164 (2000), 4178–4184.
    • (2000) J. Immunol. , vol.164 , pp. 4178-4184
    • Idusogie, E.E.1
  • 37
    • 0035194285 scopus 로고    scopus 로고
    • Effector function activities of a panel of mutants of a broadly neutralizing antibody against human immunodeficiency virus type 1
    • 37 Hezareh, M., et al. Effector function activities of a panel of mutants of a broadly neutralizing antibody against human immunodeficiency virus type 1. J. Virol. 75 (2001), 12161–12168.
    • (2001) J. Virol. , vol.75 , pp. 12161-12168
    • Hezareh, M.1
  • 38
    • 0035865063 scopus 로고    scopus 로고
    • Engineered antibodies with increased activity to recruit complement
    • 38 Idusogie, E.E., et al. Engineered antibodies with increased activity to recruit complement. J. Immunol. 166 (2001), 2571–2575.
    • (2001) J. Immunol. , vol.166 , pp. 2571-2575
    • Idusogie, E.E.1
  • 39
    • 45549090117 scopus 로고    scopus 로고
    • Engineered antibodies of IgG1/IgG3 mixed isotype with enhanced cytotoxic activities
    • 39 Natsume, A., et al. Engineered antibodies of IgG1/IgG3 mixed isotype with enhanced cytotoxic activities. Cancer Res. 68 (2008), 3863–3872.
    • (2008) Cancer Res. , vol.68 , pp. 3863-3872
    • Natsume, A.1
  • 40
    • 77953659426 scopus 로고    scopus 로고
    • Engineered Fc variant antibodies with enhanced ability to recruit complement and mediate effector functions
    • 40 Moore, G.L., et al. Engineered Fc variant antibodies with enhanced ability to recruit complement and mediate effector functions. mAbs 2 (2010), 181–189.
    • (2010) mAbs , vol.2 , pp. 181-189
    • Moore, G.L.1
  • 41
    • 84929649892 scopus 로고    scopus 로고
    • Fc engineering of human IgG1 for altered binding to the neonatal Fc receptor affects Fc effector functions
    • 41 Grevys, A., et al. Fc engineering of human IgG1 for altered binding to the neonatal Fc receptor affects Fc effector functions. J. Immunol. 194 (2015), 5497–5508.
    • (2015) J. Immunol. , vol.194 , pp. 5497-5508
    • Grevys, A.1
  • 42
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • 42 Shields, R.L., et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J. Biol. Chem. 276 (2001), 6591–6604.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1
  • 43
    • 29644434678 scopus 로고    scopus 로고
    • An engineered human IgG1 antibody with longer serum half-Life
    • 43 Hinton, P.R., et al. An engineered human IgG1 antibody with longer serum half-Life. J. Immunol. 176 (2006), 346–356.
    • (2006) J. Immunol. , vol.176 , pp. 346-356
    • Hinton, P.R.1
  • 44
    • 84455208902 scopus 로고    scopus 로고
    • Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential
    • 44 Stapleton, N.M., et al. Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential. Nat. Commun., 2, 2011, 599.
    • (2011) Nat. Commun. , vol.2 , pp. 599
    • Stapleton, N.M.1
  • 45
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • 45 Dall'Acqua, W.F., et al. Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn). J. Biol. Chem. 281 (2006), 23514–23524.
    • (2006) J. Biol. Chem. , vol.281 , pp. 23514-23524
    • Dall'Acqua, W.F.1
  • 46
    • 84887418713 scopus 로고    scopus 로고
    • A novel investigational Fc-modified humanized monoclonal antibody, Motavizumab-YTE, has an extended half-life in healthy adults
    • 46 Robbie, G.J., et al. A novel investigational Fc-modified humanized monoclonal antibody, Motavizumab-YTE, has an extended half-life in healthy adults. Antimicrob. Agents Chemother 57 (2013), 6147–6153.
    • (2013) Antimicrob. Agents Chemother , vol.57 , pp. 6147-6153
    • Robbie, G.J.1
  • 47
    • 67649207267 scopus 로고    scopus 로고
    • Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates
    • 47 Yeung, Y.A., et al. Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates. J. Immunol. 182 (2009), 7663–7671.
    • (2009) J. Immunol. , vol.182 , pp. 7663-7671
    • Yeung, Y.A.1
  • 48
    • 84922780197 scopus 로고    scopus 로고
    • pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling
    • 48 Borrok, M.J., et al. pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling. J. Biol. Chem. 290 (2015), 4282–4290.
    • (2015) J. Biol. Chem. , vol.290 , pp. 4282-4290
    • Borrok, M.J.1
  • 49
    • 76349123565 scopus 로고    scopus 로고
    • Enhanced antibody half-life improves in vivo activity
    • 49 Zalevsky, J., et al. Enhanced antibody half-life improves in vivo activity. Nat. Biotech. 28 (2010), 157–159.
    • (2010) Nat. Biotech. , vol.28 , pp. 157-159
    • Zalevsky, J.1
  • 50
    • 77954638589 scopus 로고    scopus 로고
    • Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties
    • 50 Wozniak-Knopp, G., et al. Introducing antigen-binding sites in structural loops of immunoglobulin constant domains: Fc fragments with engineered HER2/neu-binding sites and antibody properties. Protein Eng. Des. Sel. 23 (2010), 289–297.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 289-297
    • Wozniak-Knopp, G.1
  • 51
    • 84857263421 scopus 로고    scopus 로고
    • Directed evolution of stabilized IgG1-Fc scaffolds by application of strong heat shock to libraries displayed on yeast
    • 51 Traxlmayr, M.W., et al. Directed evolution of stabilized IgG1-Fc scaffolds by application of strong heat shock to libraries displayed on yeast. B.B.A. Proteins Proteom. 1824 (2012), 542–549.
    • (2012) B.B.A. Proteins Proteom. , vol.1824 , pp. 542-549
    • Traxlmayr, M.W.1
  • 52
    • 84855857695 scopus 로고    scopus 로고
    • Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds
    • 52 Wozniak-Knopp, G., et al. Stabilisation of the Fc fragment of human IgG1 by engineered intradomain disulfide bonds. PLoS ONE, 7, 2012, e30083.
    • (2012) PLoS ONE , vol.7 , pp. e30083
    • Wozniak-Knopp, G.1
  • 53
    • 84920475389 scopus 로고    scopus 로고
    • Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometry
    • 53 Jensen, P.F., et al. Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometry. Mol. Cell. Proteomics 14 (2015), 148–161.
    • (2015) Mol. Cell. Proteomics , vol.14 , pp. 148-161
    • Jensen, P.F.1
  • 54
    • 84930081913 scopus 로고    scopus 로고
    • Differential Fc-receptor engagement drives an anti-tumor vaccinal effect
    • 54 DiLillo, et al. Differential Fc-receptor engagement drives an anti-tumor vaccinal effect. Cell 161 (2015), 1035–1045.
    • (2015) Cell , vol.161 , pp. 1035-1045
    • DiLillo1
  • 55
    • 84890028543 scopus 로고    scopus 로고
    • Transepithelial transport of Fc -targeted nanoparticles by the neonatal Fc receptor for oral delivery
    • 213ra167-213
    • 55 Pridgen, E.M., et al. Transepithelial transport of Fc -targeted nanoparticles by the neonatal Fc receptor for oral delivery. Sci. Transl. Med., 5, 2013 213ra167-213.
    • (2013) Sci. Transl. Med. , vol.5
    • Pridgen, E.M.1
  • 56
    • 84952361181 scopus 로고    scopus 로고
    • Enhanced FcRn-dependent transepithelial delivery of IgG by Fc engineering and polymerization
    • 56 Foss, S., et al. Enhanced FcRn-dependent transepithelial delivery of IgG by Fc engineering and polymerization. J. Control Release 223 (2016), 42–52.
    • (2016) J. Control Release , vol.223 , pp. 42-52
    • Foss, S.1
  • 57
    • 84918774655 scopus 로고    scopus 로고
    • Fc fusion as a platform technology: potential for modulating immunogenicity
    • 57 Levin, D., et al. Fc fusion as a platform technology: potential for modulating immunogenicity. Trends Biotechnol. 33 (2015), 27–34.
    • (2015) Trends Biotechnol. , vol.33 , pp. 27-34
    • Levin, D.1
  • 58
    • 84893657950 scopus 로고    scopus 로고
    • The function of Fc gamma receptors in dendritic cells and macrophages
    • 58 Guilliams, M., et al. The function of Fc gamma receptors in dendritic cells and macrophages. Nat. Rev. Immunol. 14 (2014), 94–108.
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 94-108
    • Guilliams, M.1
  • 59
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fc gamma receptors and their polymorphic variants for human IgG subclasses
    • 59 Bruhns, P., et al. Specificity and affinity of human Fc gamma receptors and their polymorphic variants for human IgG subclasses. Blood 113 (2009), 3716–3725.
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1
  • 60
    • 84905568602 scopus 로고    scopus 로고
    • Contribution of human Fc gamma Rs to disease with evidence from human polymorphisms and transgenic animal studies
    • 60 Gillis, C.M., et al. Contribution of human Fc gamma Rs to disease with evidence from human polymorphisms and transgenic animal studies. Front. Immunol., 5, 2014, 234.
    • (2014) Front. Immunol. , vol.5 , pp. 234
    • Gillis, C.M.1
  • 61
    • 0033629719 scopus 로고    scopus 로고
    • Association between Fc gamma RIIa-R131 allotype and bacteremic Pneumococcal pneumonia
    • 61 Yee, A.M.F., et al. Association between Fc gamma RIIa-R131 allotype and bacteremic Pneumococcal pneumonia. Clin. Infect. Dis. 30 (2000), 25–28.
    • (2000) Clin. Infect. Dis. , vol.30 , pp. 25-28
    • Yee, A.M.F.1
  • 62
    • 76249090327 scopus 로고    scopus 로고
    • Dynamics of the interaction of human IgG subtype immune complexes with cells expressing R and H allelic forms of a low-affinity Fc gamma receptor CD32A
    • 62 Shashidharamurthy, R., et al. Dynamics of the interaction of human IgG subtype immune complexes with cells expressing R and H allelic forms of a low-affinity Fc gamma receptor CD32A. J. Immunol. 183 (2009), 8216–8224.
    • (2009) J. Immunol. , vol.183 , pp. 8216-8224
    • Shashidharamurthy, R.1
  • 63
    • 82255186670 scopus 로고    scopus 로고
    • Genome-wide association study identifies FCGR2A as a susceptibility locus for Kawasaki disease
    • 63 Khor, C.C., et al. Genome-wide association study identifies FCGR2A as a susceptibility locus for Kawasaki disease. Nat. Genet. 43 (2011), 1241–1246.
    • (2011) Nat. Genet. , vol.43 , pp. 1241-1246
    • Khor, C.C.1
  • 64
    • 79957874790 scopus 로고    scopus 로고
    • FcγR2A and 3A polymorphisms predict clinical outcome of trastuzumab in both neoadjuvant and metastatic settings in patients with HER2-positive breast cancer
    • 64 Tamura, K., et al. FcγR2A and 3A polymorphisms predict clinical outcome of trastuzumab in both neoadjuvant and metastatic settings in patients with HER2-positive breast cancer. Ann. Oncol. 22 (2011), 1302–1307.
    • (2011) Ann. Oncol. , vol.22 , pp. 1302-1307
    • Tamura, K.1
  • 65
    • 84864307083 scopus 로고    scopus 로고
    • Platelet-associated antibodies, cellular immunity and FCGR3a genotype influence the response to rituximab in immune thrombocytopenia
    • 65 Cooper, N., et al. Platelet-associated antibodies, cellular immunity and FCGR3a genotype influence the response to rituximab in immune thrombocytopenia. Brit. J. Haematol. 158 (2012), 539–547.
    • (2012) Brit. J. Haematol. , vol.158 , pp. 539-547
    • Cooper, N.1
  • 66
    • 84876502612 scopus 로고    scopus 로고
    • FCGR3A-158 polymorphism influences the biological response to infliximab in Crohn's disease through affecting the ADCC activity
    • 66 Moroi, R., et al. FCGR3A-158 polymorphism influences the biological response to infliximab in Crohn's disease through affecting the ADCC activity. Immunogenetics 65 (2013), 265–271.
    • (2013) Immunogenetics , vol.65 , pp. 265-271
    • Moroi, R.1
  • 67
    • 84896055730 scopus 로고    scopus 로고
    • Complement is activated by IgG hexamers assembled at the cell surface
    • 67 Diebolder, C.A., et al. Complement is activated by IgG hexamers assembled at the cell surface. Science 343 (2014), 1260–1263.
    • (2014) Science , vol.343 , pp. 1260-1263
    • Diebolder, C.A.1
  • 68
    • 84956951205 scopus 로고    scopus 로고
    • Structural basis of complement membrane attack complex formation
    • 68 Marina, S., et al. Structural basis of complement membrane attack complex formation. Nat. Commun., 7, 2016, 10587.
    • (2016) Nat. Commun. , vol.7 , pp. 10587
    • Marina, S.1
  • 69
    • 4344600286 scopus 로고    scopus 로고
    • C5a initiates the inflammatory cascade in immune complex peritonitis
    • 69 Godau, J., et al. C5a initiates the inflammatory cascade in immune complex peritonitis. J. Immunol. 173 (2004), 3437–3445.
    • (2004) J. Immunol. , vol.173 , pp. 3437-3445
    • Godau, J.1
  • 70
    • 18344372376 scopus 로고    scopus 로고
    • Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies
    • 70 Simmons, L.C., et al. Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies. J. Immunol. Methods 263 (2002), 133–147.
    • (2002) J. Immunol. Methods , vol.263 , pp. 133-147
    • Simmons, L.C.1
  • 71
    • 84940955731 scopus 로고    scopus 로고
    • The neonatal Fc receptor, FcRn, as a target for drug delivery and therapy
    • 71 Sockolosky, J.T., et al. The neonatal Fc receptor, FcRn, as a target for drug delivery and therapy. Adv. Drug Deliv. Rev. 91 (2015), 109–124.
    • (2015) Adv. Drug Deliv. Rev. , vol.91 , pp. 109-124
    • Sockolosky, J.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.