Effects of altered FcγR binding on antibody pharmacokinetics in cynomolgus monkeys

Fcγ receptors as regulators of immune responses

Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947 · see citing works

Humanization of an anti-p185HER2 antibody for human cancer therapy.

Carter, P., Presta, L., Gorman, C., Ridgway, J., Henner, D., Wong, W., Rowland, A., Kotts, C., Carver, M. E., & Shepard, H. (1992) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.89.10.4285 · Cited by 1,958 · see citing works

Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-dependent Cellular Toxicity

Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835 · see citing works

The Absence of Fucose but Not the Presence of Galactose or Bisecting N-Acetylglucosamine of Human IgG1 Complex-type Oligosaccharides Shows the Critical Role of Enhancing Antibody-dependent Cellular Cytotoxicity

Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413 · see citing works

The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins

Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., & Dwek, R. A. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141702 · Cited by 1,308 · see citing works

High Resolution Mapping of the Binding Site on Human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and Design of IgG1 Variants with Improved Binding to the FcγR

Shields, R. L., Namenuk, A. K., Hong, K., Meng, Y. G., Rae, J., Briggs, J. B., Xie, D., Lai, J., Stadlen, A., Li, B., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009483200 · Cited by 1,164 · see citing works

THE COVALENT STRUCTURE OF AN ENTIRE γG IMMUNOGLOBULIN MOLECULE

Edelman, G. M., Cunningham, B. A., Gall, W. E., Gottlieb, P. D., Rutishauser, U. S., & Waxdal, M. J. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.1.78 · Cited by 903 · see citing works

Fc receptor but not complement binding is important in antibody protection against HIV

Hessell, A. J., Hangartner, L., Hunter, M., Havenith, C. E. G., Beurskens, F. J. M., Bakker, J. M., Lanigan, C. M. S., Landucci, G., Forthal, D. N., Parren, P. W. H. I., et al. (2007) · Nature · doi:10.1038/nature06106 · Cited by 899 · see citing works

Glycosylation as a strategy to improve antibody-based therapeutics

Jefferis, R. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2804 · Cited by 829 · cited 2× · see citing works

Properties of Human IgG1s Engineered for Enhanced Binding to the Neonatal Fc Receptor (FcRn)

Dall’Acqua, W. F., Kiener, P. A., & Wu, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604292200 · Cited by 648 · see citing works

Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types

Kanda, Y., Yamada, T., Mori, K., Okazaki, A., Inoue, M., Kitajima-Miyama, K., Kuni-Kamochi, R., Nakano, R., Yano, K., Kakita, S., et al. (2007) · Glycobiology · doi:10.1093/glycob/cwl057 · Cited by 372 · see citing works

Marketed therapeutic antibodies compendium

Reichert, J. M. (2012) · mAbs · doi:10.4161/mabs.19931 · Cited by 368 · see citing works

Effector Function Activities of a Panel of Mutants of a Broadly Neutralizing Antibody against Human Immunodeficiency Virus Type 1

Hezareh, M., Hessell, A. J., Jensen, R. C., van de Winkel, J. G. J., & Parren, P. W. H. I. (2001) · Journal of Virology · doi:10.1128/jvi.75.24.12161-12168.2001 · Cited by 294 · see citing works

Expression of full-length immunoglobulins in Escherichia coli: rapid and efficient production of aglycosylated antibodies

Simmons, L. C., Reilly, D. E., Klimowski, L., Raju, T. S., Meng, G., Sims, P. W., Hong, K., Shields, R. L., Damico, L. A., Rancatore, P., et al. (2002) · Journal of Immunological Methods · doi:10.1016/s0022-1759(02)00036-4 · Cited by 282 · see citing works

Industrial Purification of Pharmaceutical Antibodies: Development, Operation, and Validation of Chromatography Processes

Fahrner, R. L., Knudsen, H. L., Basey, C. D., et al. (2001) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2001.10648017 · Cited by 261 · see citing works

A strategy for risk mitigation of antibodies with fast clearance

Hötzel, I., Theil, F.-P., Bernstein, L. J., Prabhu, S., Deng, R., Quintana, L., Lutman, J., Sibia, R., Chan, P., Bumbaca, D., et al. (2012) · mAbs · doi:10.4161/mabs.22189 · Cited by 245 · see citing works

A humanized anti-IL-6 antibody (ALD518) in non-small cell lung cancer

Bayliss, T. J., Smith, J. T., Schuster, M., Dragnev, K., & Rigas, J. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.627850 · Cited by 237 · see citing works

Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1.

Wright, A. M., & Morrison, S. L. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.3.1087 · Cited by 192 · see citing works

Monoclonal antibodies: what are the pharmacokinetic and pharmacodynamic considerations for drug development?

Deng, R., Jin, F., Prabhu, S., & Iyer, S. (2012) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2012.643868 · Cited by 126 · see citing works

The effect of Fc glycan forms on human IgG2 antibody clearance in humans

Chen, X., Liu, D., & Flynn, G. C. (2008) · Glycobiology · doi:10.1093/glycob/cwn120 · Cited by 115 · see citing works

In vivo trafficking and catabolism of IgG1 antibodies with Fc associated carbohydrates of differing structure

Wright, A. M., Sato, Y., Okada, T., Chang, K. H., Endo, T., & Morrison, S. L. (2000) · Glycobiology · doi:10.1093/glycob/10.12.1347 · Cited by 111 · see citing works

Pharmacokinetics/Pharmacodynamics of Nondepleting Anti-CD4 Monoclonal Antibody (TRX1) in Healthy Human Volunteers

Ng, C. M., Stefanich, E. G., Anand, B. S., Fielder, P. J., & Vaickus, L. (2005) · Pharmaceutical Research · doi:10.1007/s11095-005-8814-3 · Cited by 109 · see citing works

Effect of constant and variable domain glycosylation on pharmacokinetics of therapeutic antibodies in mice

Millward, T. A., Heitzmann, M., Bill, K., Längle, U., Schumacher, P., & Forrer, K. (2007) · Biologicals · doi:10.1016/j.biologicals.2007.05.003 · Cited by 91 · see citing works

Phase I Pharmacokinetic and Pharmacodynamic Dose-Escalation Study of RG7160 (GA201), the First Glycoengineered Monoclonal Antibody Against the Epidermal Growth Factor Receptor, in Patients With Advanced Solid Tumors

Paz-Ares, L. G., Gomez‐Roca, C., Delord, J., Cervantes, A. M. R., Markman, B., Corral, J., Soria, J., Bergé, Y., Roda, D., Russell-Yarde, F., et al. (2011) · Journal of Clinical Oncology · doi:10.1200/jco.2011.34.8888 · Cited by 80 · see citing works

With or Without Sugar? (A)glycosylation of Therapeutic Antibodies

Hristodorov, D., Fischer, R., & Lindén, L. (2012) · Molecular Biotechnology · doi:10.1007/s12033-012-9612-x · Cited by 75 · see citing works

Differential clearance of glycoforms of IgG in normal and autoimmune-prone mice

Newkirk, M. M., Novick, J., Stevenson, M. M., et al. (1996) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.1996.d01-847.x · Cited by 61 · see citing works

Enhancement of DNA uptake in FUT8‐deleted CHO cells for transient production of afucosylated antibodies

Wong, A. W., Baginski, T. K., & Reilly, D. E. (2010) · Biotechnology and Bioengineering · doi:10.1002/bit.22749 · Cited by 46 · see citing works

Molecular and Functional Characterization of Cynomolgus Monkey IgG Subclasses

Jacobsen, F. W., Padaki, R., Morris, A. E., Aldrich, T. L., Armitage, R. J., Allen, M. J., Lavallee, J. C., & Arora, T. K. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1001685 · Cited by 41 · see citing works

Onartuzumab (MetMAb): Using Nonclinical Pharmacokinetic and Concentration–Effect Data to Support Clinical Development

Xiang, H., Bender, B. C., Reyes, A. E., Merchant, M. A., Jumbe, N. L. ‘., Romero, M., Davancaze, T., Nijem, I., Mai, E., Young, J. C., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0260 · Cited by 35 · see citing works

Phase I study of obinutuzumab ( GA 101) in J apanese patients with relapsed or refractory B ‐cell non‐ H odgkin lymphoma

Ogura, M., Tobinai, K., Hatake, K., et al. (2012) · Cancer Science · doi:10.1111/cas.12040 · Cited by 34 · see citing works

Identification of IgG1 variants with increased affinity to FcγRIIIa and unaltered affinity to FcγRI and FcRn: Comparison of soluble receptor-based and cell-based binding assays

Lu, Y., Vernes, J.-M., Chiang, N., Ou, Q., Ding, J., Adams, C. W., Hong, K., Truong, B.-T., Ng, D., Shen, A. Y., et al. (2010) · Journal of Immunological Methods · doi:10.1016/j.jim.2010.12.014 · Cited by 29 · see citing works

Quantitative determination of humanized monoclonal antibody rhuMAb2H7 in cynomolgus monkey serum using a Generic Immunoglobulin Pharmacokinetic (GRIP) assay

Yang, J., Ng, C., Lowman, H. B., et al. (2008) · Journal of Immunological Methods · doi:10.1016/j.jim.2008.01.016 · Cited by 26 · see citing works

A novel homogeneous Biotin–digoxigenin based assay for the detection of human anti-therapeutic antibodies in autoimmune serum

Qiu, Z. J., Ying, Y., Fox, M., et al. (2010) · Journal of Immunological Methods · doi:10.1016/j.jim.2010.09.013 · Cited by 24 · see citing works

Technology comparisons for anti-therapeutic antibody and neutralizing antibody assays in the context of an anti-TNF pharmacokinetic study

Loyet, K. M., Deng, R., Liang, W., et al. (2009) · Journal of Immunological Methods · doi:10.1016/j.jim.2009.03.012 · Cited by 22 · see citing works

Clinical immunogenicity specificity assessments: A platform evaluation

Peng, K., Siradze, K., Quarmby, V. E., et al. (2010) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2010.09.035 · Cited by 17 · see citing works

Novel human IgG1 and IgG4 Fc-engineered antibodies with completely abolished immune effector functions

Schlothauer, T., Herter, S., Koller, C. F., Grau-Richards, S., Steinhart, V., Spick, C., Kubbies, M., Klein, C., Umaña, P., & Mössner, E. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw040 · Cited by 425 · see citing works

IgG Fc engineering to modulate antibody effector functions

Wang, X., Mathieu, M., & Brezski, R. J. (2018) · Protein & Cell · doi:10.1007/s13238-017-0473-8 · Cited by 356 · see citing works

Tutorial on monoclonal antibody pharmacokinetics and its considerations in early development

Ovacik, M., & Lin, K. (2018) · Clinical and Translational Science · doi:10.1111/cts.12567 · Cited by 299 · see citing works

Antibody-Mediated Targeting of Tau In Vivo Does Not Require Effector Function and Microglial Engagement

Lee, S.-H., Le Pichon, C. E., Adolfsson, O., Gafner, V., Pihlgren, M., Lin, H., Solanoy, H., Brendza, R., Ngu, H., Foreman, O., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.06.099 · Cited by 125 · see citing works

Multi-angle effector function analysis of human monoclonal IgG glycovariants

Dashivets, T., Thomann, M., Rueger, P., Knaupp, A., Buchner, J., & Schlothauer, T. (2015) · PLOS ONE · doi:10.1371/journal.pone.0143520 · Cited by 101 · see citing works

Assessments of antibody biodistribution

Glassman, P. M., Abuqayyas, L., & Balthasar, J. P. (2015) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.365 · Cited by 42 · see citing works

Increased in vivo effector function of human IgG4 isotype antibodies through afucosylation

Gong, Q., Hazen, M., Marshall, B., Crowell, S. R., Ou, Q., Wong, A. W., Phung, W., Vernes, J.-M., Meng, Y. G., Tejada, M., et al. (2016) · mAbs · doi:10.1080/19420862.2016.1189049 · Cited by 26 · see citing works

Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels

Vaccaro, C., Zhou, J., Ober, R. J., & Ward, E. S. (2005) · Nature Biotechnology · doi:10.1038/nbt1143 · Cited by 407 · see citing works

FcRn, but not FcγRs, drives maternal-fetal transplacental transport of human IgG antibodies

Borghi, S., Bournazos, S., Thulin, N. K., Li, C., Gajewski, A., Sherwood, R., Zhang, S., Harris, E., Jagannathan, P., Wang, L., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2004325117 · Cited by 95 · see citing works

FcRn, but not FcγRs, drives maternal-fetal transplacental transport of human IgG antibodiesPreprint

Borghi, S., Bournazos, S., Thulin, N. K., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.22.999243 · Cited by 4 · see citing works

The Dual Targeting of FcRn and FcγRs via Monomeric Fc Fragments Results in Strong Inhibition of IgG-Dependent Autoimmune Pathologies

Monnet, C., Jacque, É., de Romeuf, C., Fontayne, A., Abache, T., Fournier, N., Dupont, G., Derache, D., Engrand, A., Bauduin, A., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.728322 · Cited by 18 · see citing works

Qualification of a homogeneous cell-based neonatal Fc receptor (FcRn) binding assay and its application to studies on Fc functionality of IgG-based therapeutics

Mathur, A., Arora, T., Liu, L., Crouse-Zeineddini, J., & Mukku, V. R. (2013) · Journal of Immunological Methods · doi:10.1016/j.jim.2013.01.011 · Cited by 21 · see citing works