FcRn: the neonatal Fc receptor comes of age

The blood–brain barrier: an overview

Ballabh, P., Braun, A., & Nedergaard, M. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.12.016 · Cited by 2,276 · see citing works

Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution.

Deisenhofer, J. (1981) · Biochemistry · doi:10.1021/bi00512a001 · Cited by 1,539 · see citing works

Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution.

Deisenhofer, J. (1981) · PubMed · Cited by 1,422 · 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

Anti-inflammatory Activity of IVIG Mediated Through the Inhibitory Fc Receptor

Samuelsson, A., Towers, T. L., & Ravetch, J. V. (2001) · Science · doi:10.1126/science.291.5503.484 · Cited by 1,051 · see citing works

An Fc receptor structurally related to MHC class I antigens

Simister, N. E., & Mostov, K. E. (1989) · Nature · doi:10.1038/337184a0 · Cited by 729 · see citing works

Metabolism of Immunoglobulins

Waldmann, T. A., & Strober, W. (2015) · Chemical immunology/Fortschritte der Allergielehre/Progress in allergy/Chemical immunology and allergy · doi:10.1159/000385919 · Cited by 723 · see citing works

The protection receptor for IgG catabolism is the beta2-microglobulin-containing neonatal intestinal transport receptor.

Junghans, R. P., & Anderson, C. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.11.5512 · Cited by 685 · see citing works

Convergent Solutions to Binding at a Protein-Protein Interface

DeLano, W. L., Ultsch, M. H., de, A. M., Vos, & Wells, J. A. (2000) · Science · doi:10.1126/science.287.5456.1279 · Cited by 673 · 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

The Major Histocompatibility Complex–related Fc Receptor for IgG (FcRn) Binds Albumin and Prolongs Its Lifespan

Chaudhury, C., Mehnaz, S., Robinson, J. M., Hayton, W. L., Pearl, D. K., Roopenian, D. C., & Anderson, C. L. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021829 · Cited by 640 · see citing works

Differences in promiscuity for antibody–FcRn interactions across species: implications for therapeutic antibodies

Ober, R. J., Radu, C. G., Ghetie, V. F., & Ward, E. S. (2001) · International Immunology · doi:10.1093/intimm/13.12.1551 · Cited by 502 · see citing works

Multiple Roles for the Major Histocompatibility Complex Class I– Related Receptor FcRn

Ghetie, V. F., & Ward, E. S. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.739 · Cited by 474 · see citing works

Human Neonatal Fc Receptor Mediates Transport of IgG into Luminal Secretions for Delivery of Antigens to Mucosal Dendritic Cells

Yoshida, M., Claypool, S. M., Wagner, J. S., Mizoguchi, E., Mizoguchi, A., Roopenian, D. C., Lencer, W. I., & Blumberg, R. S. (2004) · Immunity · doi:10.1016/j.immuni.2004.05.007 · Cited by 472 · see citing works

Abnormally short serum half‐lives of IgG in β2‐microglobulin‐deficient mice

Ghetie, V. F., Hubbard, J. G., Kim, J., Tsen, M. F., Lee, Y., & Ward, E. S. (1996) · European Journal of Immunology · doi:10.1002/eji.1830260327 · Cited by 469 · see citing works

THE TRANSMISSION OF IMMUNITY FROM MOTHER TO YOUNG AND THE CATABOLISM OF IMMUNOGLOBULINS

Brambell, F. W. R. (1966) · The Lancet · doi:10.1016/s0140-6736(66)92190-8 · Cited by 463 · see citing works

The MHC Class I-Like IgG Receptor Controls Perinatal IgG Transport, IgG Homeostasis, and Fate of IgG-Fc-Coupled Drugs

Roopenian, D. C., Christianson, G. J., Sproule, T. J., Brown, A. C., Akilesh, S., Jung, N., Petkova, S. B., Avanessian, L., Choi, E. Y., Shaffer, D. J., et al. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.7.3528 · Cited by 454 · see citing works

A Theoretical Model of γ-Globulin Catabolism

Brambell, F. W. R., Hemmings, W. A., & MORRIS, I. G. (1964) · Nature · doi:10.1038/2031352a0 · Cited by 451 · see citing works

Bidirectional FcRn-dependent IgG transport in a polarized human intestinal epithelial cell line

Dickinson, B. L., Badizadegan, K., Wu, Z., Ahouse, J. C., Zhu, X., Simister, N. E., Blumberg, R. S., & Lencer, W. I. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6968 · Cited by 433 · see citing works

Crystal structure of the complex of rat neonatal Fc receptor with Fc

Burmeister, W. P., Huber, A. H., & Björkman, P. J. (1994) · Nature · doi:10.1038/372379a0 · Cited by 432 · see citing works

Mechanism of Intravenous Immune Globulin Therapy in Antibody-Mediated Autoimmune Diseases

Yu, Z., & Lennon, V. A. (1999) · New England Journal of Medicine · doi:10.1056/nejm199901213400311 · Cited by 431 · see citing works

Mapping of the C1q Binding Site on Rituxan, a Chimeric Antibody with a Human IgG1 Fc

Idusogie, E. E., Presta, L. G., Gazzano, H., Tótpál, K., Wong, P. Y., Ultsch, M. H., Meng, Y. G., & Mulkerrin, M. G. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.8.4178 · Cited by 424 · 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

Receptor-mediated Immunoglobulin G Transport Across Mucosal Barriers in Adult Life

Spiekermann, G. M., Finn, P. W., Ward, E. S., Dumont, J., Dickinson, B. L., Blumberg, R. S., & Lencer, W. I. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020400 · Cited by 403 · see citing works

Cell Surface Recycling of Internalized Antigen Permits Dendritic Cell Priming of B Cells

Bergtold, A., Desai, D. D., Gavhane, A., & Clynes, R. (2005) · Immunity · doi:10.1016/j.immuni.2005.09.013 · Cited by 401 · see citing works

Crystal Structure at 2.8 Å of an FcRn/Heterodimeric Fc Complex

Martin, W. L., West, A. P., Gan, L., & Bjorkman, P. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00230-1 · Cited by 391 · see citing works

Crystal structure of the complex of rat neonatal Fc receptor with Fc

(1995) · Trends in Genetics · doi:10.1016/0168-9525(95)90005-5 · Cited by 382 · see citing works

Increasing the Affinity of a Human IgG1 for the Neonatal Fc Receptor: Biological Consequences

Acqua, W. F. D., Woods, R. M., Ward, E. S., Palaszynski, S., Patel, N., Brewah, Y. A., Wu, H., Kiener, P. A., & Langermann, S. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.9.5171 · Cited by 368 · see citing works

Isolation from human placenta of the IgG transporter, FcRn, and localization to the syncytiotrophoblast: implications for maternal-fetal antibody transport

Leach, J. L., Sedmak, D. D., Osborne, J. M., Rahill, B., Lairmore, M. D., & Anderson, C. L. (1996) · The Journal of Immunology · doi:10.4049/jimmunol.157.8.3317 · Cited by 348 · see citing works

Isolation and characterization of an Fc receptor from neonatal rat small intestine

Simister, N. E., & Rees, A. R. (1985) · European Journal of Immunology · doi:10.1002/eji.1830150718 · Cited by 341 · see citing works

Crystal structure at 2.2 Å resolution of the MHC-related neonatal Fc receptor

Burmeister, W. P., Gastinel, L. N., Simister, N. E., Blum, M. L., & Björkman, P. J. (1994) · Nature · doi:10.1038/372336a0 · Cited by 336 · see citing works

An IgG‐transporting Fc receptor expressed in the syncytiotrophoblast of human placenta

Simister, N. E., Story, C. M., Chen, H., & Hunt, J. S. (1996) · European Journal of Immunology · doi:10.1002/eji.1830260718 · Cited by 332 · see citing works

The MHC class I-related receptor, FcRn, plays an essential role in the maternofetal transfer of γ-globulin in humans

Firan, M., Bawdon, R., Radu, C., Ober, R. J., Eaken, D., Antohe, F., Ghetie, V., & Ward, E. S. (2001) · International Immunology · doi:10.1093/intimm/13.8.993 · Cited by 330 · see citing works

Expression of the neonatal Fc receptor, FcRn, on human intestinal epithelial cells

Israel, E. J., TAYLOR, S., WU, Z., Mizoguchi, E., Blumberg, R. S., Bhan, A. K., & Simister, N. E. (1997) · Immunology · doi:10.1046/j.1365-2567.1997.00326.x · Cited by 328 · see citing works

MHC Class I-Related Neonatal Fc Receptor for IgG Is Functionally Expressed in Monocytes, Intestinal Macrophages, and Dendritic Cells

Zhu, X., Meng, G., Dickinson, B. L., Li, X., Mizoguchi, E., Miao, L., Wang, Y., Robert, C., Wu, B., Smith, P. D., et al. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.5.3266 · Cited by 322 · see citing works

Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants

Raghavan, M., Bonagura, V. R., Morrison, S. L., & Bjorkman, P. J. (1995) · Biochemistry · doi:10.1021/bi00045a005 · Cited by 317 · see citing works

Enhanced half-life of genetically engineered human IgG1 antibodies in a humanized FcRn mouse model: potential application in humorally mediated autoimmune disease

Petkova, S. B., Akilesh, S., Sproule, T. J., Christianson, G. J., Khabbaz, H. J. A., Brown, A. C., Presta, L. G., Meng, Y. G., & Roopenian, D. C. (2006) · International Immunology · doi:10.1093/intimm/dxl110 · Cited by 315 · see citing works

Visualizing the site and dynamics of IgG salvage by the MHC class I-related receptor, FcRn

Ober, R. J., Martinez, C., Vaccaro, C., Zhou, J., & Ward, E. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.4.2021 · Cited by 314 · see citing works

An Engineered Human IgG1 Antibody with Longer Serum Half-Life

Hinton, P. R., Xiong, J. M., Johlfs, M. G., Tang, M. T., Keller, S., & Tsurushita, N. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.1.346 · Cited by 282 · see citing works

The mechanism of intestinal uptake and transcellular transport of IgG in the neonatal rat

Jones, E. A., & Waldmann, T. A. (1972) · Journal of Clinical Investigation · doi:10.1172/jci107116 · Cited by 279 · see citing works

Engineered Human IgG Antibodies with Longer Serum Half-lives in Primates

Hinton, P. R., Johlfs, M. G., Xiong, J. M., Hanestad, K., Ong, K. C., Bullock, C., Keller, S., Tang, M. T., Tso, J. Y., Vásquez, M., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300470200 · Cited by 274 · see citing works

Mediated efflux of IgG molecules from brain to blood across the blood–brain barrier

Zhang, Y., & Pardridge, W. M. (2001) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(01)00242-9 · Cited by 272 · see citing works

Expression of the neonatal Fc receptor (FcRn) at the blood–brain barrier

Schlachetzki, F., Zhu, C., & Pardridge, W. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00840.x · Cited by 268 · see citing works

pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat.

Rodewald, R. (1976) · The Journal of Cell Biology · doi:10.1083/jcb.71.2.666 · Cited by 266 · see citing works

Complete FcRn dependence for intravenous Ig therapy in autoimmune skin blistering diseases

Li, N. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24394 · Cited by 263 · see citing works

Exocytosis of IgG as mediated by the receptor, FcRn: An analysis at the single-molecule level

Ober, R. J., Martinez, C., Lai, X., Zhou, J., & Ward, E. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402970101 · Cited by 258 · see citing works

Crystal Structure and Immunoglobulin G Binding Properties of the Human Major Histocompatibility Complex-Related Fc Receptor ,

West, A. P., & Björkman, P. J. (2000) · Biochemistry · doi:10.1021/bi000749m · Cited by 256 · see citing works

Functional expression of the MHC class I-related receptor, FcRn, in endothelial cells of mice

Borvák, J. (1998) · International Immunology · doi:10.1093/intimm/10.9.1289 · Cited by 254 · see citing works

Neonatal Fc receptor for IgG regulates mucosal immune responses to luminal bacteria

Yoshida, M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci27821 · Cited by 237 · see citing works

Overview of monoclonal antibodies in cancer therapy: present and promise

Stern, M., & Herrmann, R. (2005) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2004.10.011 · Cited by 235 · see citing works

Pulmonary delivery of an erythropoietin Fc fusion protein in non-human primates through an immunoglobulin transport pathway

Bitonti, A. J., Dumont, J. A., Low, S. C., Peters, R., Kropp, K. E., Palombella, V. J., Stattel, J. M., Lu, Y., Tan, C. A., Song, J. J., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403235101 · Cited by 234 · see citing works

IgG-Assisted Age-Dependent Clearance of Alzheimer's Amyloid β Peptide by the Blood–Brain Barrier Neonatal Fc Receptor

Deane, R., Sagare, A. P., Hamm, K., Parisi, M., LaRue, B., Guo, H., Wu, Z., Holtzman, D. M., & Zloković, B. V. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3697-05.2005 · Cited by 233 · see citing works

Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody—antigen interaction

Corper, A. L., Sohi, M. K., Bonagura, V. R., Steinitz, M. O., Jefferis, R., Feinstein, A., Beale, D., Taussig, M., & Sutton, B. J. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0597-374 · Cited by 224 · see citing works

Evidence to support the cellular mechanism involved in serum IgG homeostasis in humans

Ward, E. S. (2003) · International Immunology · doi:10.1093/intimm/dxg018 · Cited by 216 · see citing works

Perspective – FcRn transports albumin: relevance to immunology and medicine

Anderson, C. L., Chaudhury, C., Kim, J., Bronson, C. L., Wani, M. A., & Mohanty, S. (2006) · Trends in Immunology · doi:10.1016/j.it.2006.05.004 · Cited by 209 · see citing works

Tailoring the Pharmacokinetics and Positron Emission Tomography Imaging Properties of Anti–Carcinoembryonic Antigen Single-Chain Fv-Fc Antibody Fragments

Kenanova, V. E., Olafsen, T., Crow, D. M., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.622.65.2 · Cited by 207 · see citing works

The MHC class I-like Fc receptor promotes humorally mediated autoimmune disease

Akilesh, S., Petkova, S. B., Sproule, T. J., Shaffer, D. J., Christianson, G. J., & Roopenian, D. C. (2004) · Journal of Clinical Investigation · doi:10.1172/jci18838 · Cited by 197 · see citing works

Requirement for a beta 2-microglobulin-associated Fc receptor for acquisition of maternal IgG by fetal and neonatal mice.

Israel, E. J., Patel, V., Taylor, S. F., Marshak‐Rothstein, A., & Simister, N. E. (1995) · The Journal of Immunology · doi:10.4049/jimmunol.154.12.6246 · Cited by 192 · see citing works

Crystal structure of a streptococcal protein G domain bound to an Fab fragment

Derrick, J. P., & Wigley, D. B. (1992) · Nature · doi:10.1038/359752a0 · Cited by 187 · see citing works

Characterization and Localization of the Neonatal Fc Receptor in Adult Human Kidney

Haymann, J., Levraud, J., BOUET, S., Kappès, V., Hagège, J., Nguyen, G., Xu, Y., Rondeau, É., & Sraer, J. (2000) · Journal of the American Society of Nephrology · doi:10.1681/asn.v114632 · Cited by 176 · see citing works

Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1

Medesan, C., Matesoi, D., Radu, C., Ghetie, V, & Ward, E. S. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.5.2211 · Cited by 175 · see citing works

Expression of functionally active FcRn and the differentiated bidirectional transport of IgG in human placental endothelial cells

Antohe, F., Rădulescu, L., Gafencu, A., Gheţie, V., & Simionescu, M. (2001) · Human Immunology · doi:10.1016/s0198-8859(00)00244-5 · Cited by 175 · see citing works

Structural basis of pH-dependent antibody binding by the neonatal Fc receptor

Vaughn, D. E., & Björkman, P. J. (1998) · Structure · doi:10.1016/s0969-2126(98)00008-2 · Cited by 171 · see citing works

The Chicken Yolk Sac IgY Receptor, a Functional Equivalent of the Mammalian MHC-Related Fc Receptor, Is a Phospholipase A2 Receptor Homolog

West, A. P., Herr, A. B., & Björkman, P. J. (2004) · Immunity · doi:10.1016/s1074-7613(04)00113-x · Cited by 170 · see citing works

Intravenous Immunoglobulin Mediates an Increase in Anti-Platelet Antibody Clearance via the FcRn Receptor

Hansen, R. J., & Balthasar, J. P. (2002) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1613331 · Cited by 165 · see citing works

Ueber Immunität durch Vererbung und Säugung

Ehrlich, P. (1892) · Medical Microbiology and Immunology · doi:10.1007/bf02284236 · Cited by 161 · see citing works

Beta 2-microglobulin-, CD8+ T-cell-deficient mice survive inoculation with high doses of vaccinia virus and exhibit altered IgG responses.

Spriggs, M. K., Koller, B. H., Sato, T., et al. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.6070 · Cited by 157 · see citing works

Mouse MHC class I-like Fc receptor encoded outside the MHC.

Ahouse, J. J., Hagerman, C. L., Mittal, P., Gilbert, D. J., Copeland, N. G., Jenkins, N. A., & Simister, N. E. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.151.11.6076 · Cited by 151 · see citing works

Investigation of the interaction between the class I MHC-related Fc receptor and its immunoglobulin G ligand

Raghavan, M., Chen, M. Y., Gastinel, L. N., & Björkman, P. J. (1994) · Immunity · doi:10.1016/1074-7613(94)90082-5 · Cited by 144 · see citing works

Localization of the site of the murine IgG1 molecule that is involved in binding to the murine intestinal Fc receptor

Kim, J., Tsen, M. F., Ghetie, V. F., & Ward, E. S. (1994) · European Journal of Immunology · doi:10.1002/eji.1830241025 · Cited by 142 · see citing works

Monomeric Fc Fusions

Dumont, J. A., Low, S. C., Peters, R., & Bitonti, A. J. (2006) · BioDrugs · doi:10.2165/00063030-200620030-00002 · Cited by 130 · see citing works

Delivery of an Erythropoietin-Fc Fusion Protein by Inhalation in Humans through an Immunoglobulin Transport Pathway

Dumont, J. A., Bitonti, A. J., Clark, D., et al. (2005) · Journal of Aerosol Medicine · doi:10.1089/jam.2005.18.294 · Cited by 129 · see citing works

FcRn-mediated transcytosis of immunoglobulin G in human renal proximal tubular epithelial cells

Kobayashi, N., Suzuki, Y., Tsuge, T., Okumura, K., Ra, C., & Tomino, Y. (2002) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.0164.2001 · Cited by 126 · see citing works

Effects of intravenous immunoglobulin on platelet count and antiplatelet antibody disposition in a rat model of immune thrombocytopenia

Hansen, R. J., & Balthasar, J. P. (2002) · Blood · doi:10.1182/blood.v100.6.2087 · Cited by 125 · see citing works

Amelioration of Experimental Autoimmune Myasthenia Gravis in Rats by Neonatal FcR Blockade

Liu, L., Garcia, A. M., Santoro, H., Zhang, Y., McDonnell, K. A., Dumont, J., & Bitonti, A. J. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.8.5390 · Cited by 122 · see citing works

The stoichiometry and affinity of the interaction of murine Fc fragments with the MHC class I-related receptor, FcRn

Popov, S., Hubbard, J. G., Kim, J.-K., Ober, B. T., Ghetie, V. F., & Ward, E. S. (1996) · Molecular Immunology · doi:10.1016/0161-5890(96)00004-1 · Cited by 120 · see citing works

Distribution of the IgG Fc Receptor, FcRn, in the Human Fetal Intestine

Shah, U. S., Dickinson, B. L., Blumberg, R. S., Simister, N. E., Lencer, W. I., & Walker, W. A. (2003) · Pediatric Research · doi:10.1203/01.pdr.0000047663.81816.e3 · Cited by 120 · see citing works

Oral and pulmonary delivery of FSH–Fc fusion proteins via neonatal Fc receptor-mediated transcytosis

Low, S. C., Nunes, S. L., Bitonti, A. J., et al. (2005) · Human Reproduction · doi:10.1093/humrep/deh896 · Cited by 117 · see citing works

Divergent activities of an engineered antibody in murine and human systems have implications for therapeutic antibodies

Vaccaro, C., Bawdon, R. E., Wanjie, S., Ober, R. J., & Ward, E. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606304103 · Cited by 114 · see citing works

Crystallization and Stoichiometry of Binding of a Complex between a Rat Intestinal Fc Receptor and Fc

Huber, A. H., Kelley, R. F., Gastinel, L. N., & Björkman, P. J. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1220 · Cited by 90 · see citing works

Identification of critical IgG binding epitopes on the neonatal Fc receptor

Vaughn, D. E., Milburn, C. M., Penny, D. M., Martin, W. L., Johnson, J. L., & Björkman, P. J. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1388 · Cited by 89 · see citing works

Characterization of the 2:1 Complex between the Class I MHC-Related Fc Receptor and Its Fc Ligand in Solution

Martin, W. L., & Björkman, P. J. (1999) · Biochemistry · doi:10.1021/bi9913505 · Cited by 88 · see citing works

Pulmonary administration of therapeutic proteins using an immunoglobulin transport pathway

Bitonti, A. J., & Dumont, J. A. (2006) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2006.07.015 · Cited by 87 · see citing works

Ligand Valency Affects Transcytosis, Recycling and Intracellular Trafficking Mediated by the Neonatal Fc Receptor

Tesar, D. B., Tiangco, N. E., & Björkman, P. J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00457.x · Cited by 86 · see citing works

IgG transport across mucosal barriers by neonatal Fc receptor for IgG and mucosal immunity

Yoshida, M., Masuda, A., Kuo, T. T., Kobayashi, K., Claypool, S. M., Takagawa, T., Kutsumi, H., Azuma, T., Lencer, W. I., & Blumberg, R. S. (2006) · Springer Seminars in Immunopathology · doi:10.1007/s00281-006-0054-z · Cited by 80 · see citing works

Net absorption of IgG via FcRn-mediated transcytosis across rat alveolar epithelial cell monolayers

Kim, K., Fandy, T. E., Lee, V. H. L., Ann, D. K., Borok, Z., & Crandall, E. D. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00121.2004 · Cited by 70 · see citing works

Stoichiometry of the Interaction between the Major Histocompatibility Complex-Related Fc Receptor and Its Fc Ligand

Sánchez, L. M., Penny, D. M., & Björkman, P. J. (1999) · Biochemistry · doi:10.1021/bi9907330 · Cited by 70 · see citing works

Catabolism of the Murine IgGl Molecule: Evidence that Both CH2‐CH3 Domain Interfaces are Required for Persistence of IgGl in the Circulation of Mice

Kim, J., Tsen, M. F., Ghetie, V. F., & Ward, E. S. (1994) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.1994.tb03488.x · Cited by 69 · see citing works

Expression and Transport Functionality of FcRn within Rat Alveolar Epithelium: A Study in Primary Cell Culture and in the Isolated Perfused Lung

Sakagami, M., Omidi, Y., Campbell, L., Kandalaft, L. E., Morris, C. J., Barar, J., & Gumbleton, M. (2005) · Pharmaceutical Research · doi:10.1007/s11095-005-9226-0 · Cited by 68 · see citing works

Maturation of the Maternofoetal Transport System for Human γ-Globulin in the Mouse

Morphis, L., & Gitlin, D. (1970) · Nature · doi:10.1038/228573a0 · Cited by 66 · see citing works

Prevention of systemic lupus erythematosus in MRL/lpr mice by administration of an immunoglobulin-binding peptide

Marino, M., Ruvo, M., Falco, S. D., et al. (2000) · Nature Biotechnology · doi:10.1038/77296 · Cited by 65 · see citing works

FcRn mediates elongated serum half-life of human IgG in cattle

Kacskovıcs, I., Kis, Z., Mayer, B., West, A. P., Tiangco, N. E., Tilahun, M. E., Cervenak, L., Björkman, P. J., Goldsby, R. A., Szenci, O., et al. (2006) · International Immunology · doi:10.1093/intimm/dxh393 · Cited by 57 · see citing works

Human placental Fcγ‐binding proteins in the maternofetal transfer of IgG

Kristoffersen, E. K. (1996) · Apmis · doi:10.1111/j.1600-0463.1996.tb05583.x · Cited by 54 · see citing works

Pharmacokinetic Effects of 4C9, An Anti-FcRn Antibody, in Rats: Implications for the Use of FcRn Inhibitors for the Treatment of Humoral Autoimmune and Alloimmune Conditions

Getman, K. E., & Balthasar, J. P. (2005) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.20297 · Cited by 54 · see citing works

THE METABOLISM OF NORMAL PLASMA PROTEINS AND GAMMA-MYELOMA PROTEIN IN MICE BEARING PLASMA-CELL TUMORS

Humphrey, J., & Fahey, J. L. (1961) · Journal of Clinical Investigation · doi:10.1172/jci104392 · Cited by 49 · see citing works

The neonatal Fc receptor (FcRn) is expressed in the bovine lung

Mayer, B. (2004) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2003.10.010 · Cited by 31 · see citing works

Quantitative methods for developing Fc mutants with extended half‐lives

Kamei, D. T., Lao, B. J., Speed, M. A., Deshpande, R. R., Xu, H., Tidor, B., & Lauffenburger, D. A. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20624 · Cited by 27 · see citing works

IgG binding and expression of its receptor in rat intestine during postnatal development.

Gill, R. K., Mahmood, S., Sodhi, C. P., et al. (1999) · PubMed · Cited by 26 · see citing works

Functional analysis of the mouse Fcgrt 5′ proximal promoter

Tiwari, B., & Junghans, R. P. (2004) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/j.bbaexp.2004.10.002 · Cited by 25 · see citing works

Analysis of the promoter region of the human FcRn gene

Mikulska, J., & Simister, N. E. (2000) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(00)00068-3 · Cited by 23 · see citing works

Membrane-anchored Human FcRn can Oligomerize in the Absence of IgG

Praetor, A., Jones, R. M., Wong, W. L., & Hunziker, W. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00626-5 · Cited by 15 · see citing works

Untitled work

(1999) · doi:10.1002/(sici)1521-4141(199909)29:09

mRNA vaccines for infectious diseases: principles, delivery and clinical translation

Chaudhary, N., Weissman, D., & Whitehead, K. A. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00283-5 · Cited by 1,555 · see citing works

Therapeutic antibodies: successes, limitations and hopes for the future

Chames, P., Van Regenmortel, M., Weiss, E., & Baty, D. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00190.x · Cited by 1,382 · see citing works

The Genome Sequence of Taurine Cattle: A Window to Ruminant Biology and Evolution

The Bovine Genome Sequencing and Analysis Consortium, Elsik, C. G., Tellam, R. L., Worley, K. C., Gibbs, R. A., Muzny, D. M., Weinstock, G. M., Adelson, D. L., Eichler, E. E., Elnitski, L., et al. (2009) · Science · doi:10.1126/science.1169588 · Cited by 1,287 · see citing works

IgG placental transfer in healthy and pathological pregnancies

Palmeira, P., Quinello, C., Silveira-Lessa, A. L., Zago, C. A., & Carneiro-Sampaio, M. (2012) · Clinical and Developmental Immunology · doi:10.1155/2012/985646 · Cited by 1,037 · 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 · see citing works

Alternative molecular formats and therapeutic applications for bispecific antibodies

Spiess, C., Zhai, Q., & Carter, P. J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.01.003 · Cited by 607 · see citing works

Population Pharmacokinetics of Therapeutic Monoclonal Antibodies

Dirks, N. L., & Meibohm, B. (2010) · Clinical Pharmacokinetics · doi:10.2165/11535960-000000000-00000 · Cited by 500 · see citing works

High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans

Goetze, A. M., Liu, Y. D., Zhang, Z., Shah, B., Lee, E., Bondarenko, P. V., & Flynn, G. C. (2011) · Glycobiology · doi:10.1093/glycob/cwr027 · Cited by 467 · see citing works

Antibody Glycosylation and Its Impact on the Pharmacokinetics and Pharmacodynamics of Monoclonal Antibodies and Fc-Fusion Proteins

Liu, L. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24444 · Cited by 428 · see citing works

Effects of Charge on Antibody Tissue Distribution and Pharmacokinetics

Boswell, C. A., Tesar, D. B., Mukhyala, K., Theil, F.-P., Fielder, P. J., & Khawli, L. A. (2010) · Bioconjugate Chemistry · doi:10.1021/bc100261d · Cited by 398 · see citing works

The renaissance of complement therapeutics

Ricklin, D., Mastellos, D. C., Reis, E. S., & Lambris, J. D. (2018) · Nature Reviews Nephrology · doi:10.1038/nrneph.2017.156 · Cited by 379 · see citing works

A Novel Investigational Fc-Modified Humanized Monoclonal Antibody, Motavizumab-YTE, Has an Extended Half-Life in Healthy Adults

Robbie, G. J., Criste, R., Dall'Acqua, W. F., Jensen, K., Patel, N. K., Losonsky, G. A., & Griffin, M. P. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01285-13 · Cited by 366 · 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

Bispecific antibodies for cancer therapy: The light at the end of the tunnel?

Chames, P., & Baty, D. (2009) · mAbs · doi:10.4161/mabs.1.6.10015 · Cited by 336 · see citing works

Maternal IgG and IgA Antibodies Dampen Mucosal T Helper Cell Responses in Early Life

Koch, M. A., Reiner, G. L., Lugo, K. A., Kreuk, L. S. M., Stanbery, A. G., Ansaldo, E., Seher, T. D., Ludington, W. B., & Barton, G. M. (2016) · Cell · doi:10.1016/j.cell.2016.04.055 · Cited by 315 · 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

Safety and immunotoxicity assessment of immunomodulatory monoclonal antibodies

Brennan, F. R., Morton, L. D., Spindeldreher, S., Kiessling, A., Allenspach, R., Hey, A., Müller, P., Frings, W., & Sims, J. (2010) · mAbs · doi:10.4161/mabs.2.3.11782 · Cited by 250 · see citing works

Losing your nerves? Maybe it's the antibodies

Diamond, B., Huerta, P. T., Mina-Osorio, P., Kowal, C., & Volpe, B. T. (2009) · Nature Reviews Immunology · doi:10.1038/nri2529 · Cited by 247 · see citing works

Developability Assessment During the Selection of Novel Therapeutic Antibodies

Jarasch, A., Koll, H., Regula, J. T., Bader, M., Papadimitriou, A., & Kettenberger, H. (2015) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.24430 · Cited by 242 · see citing works

Charge-mediated influence of the antibody variable domain on FcRn-dependent pharmacokinetics

Schoch, A., Kettenberger, H., Mundigl, O., Winter, G., Engert, J., Heinrich, J., & Emrich, T. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1408766112 · Cited by 202 · see citing works

Influence of N-glycosylation on effector functions and thermal stability of glycoengineered IgG1 monoclonal antibody with homogeneous glycoforms

Wada, R., Matsui, M., & Kawasaki, N. (2019) · mAbs · doi:10.1080/19420862.2018.1551044 · Cited by 186 · see citing works

Prenatal correction of x-linked hypohidrotic ectodermal dysplasia

Schneider, H., Faschingbauer, F., Schuepbach-Mallepell, S., Körber, I., Wohlfart, S., Dick, A., Wahlbuhl, M., Kowalczyk-Quintas, C., Vigolo, M., Kirby, N., et al. (2018) · New England Journal of Medicine · doi:10.1056/nejmoa1714322 · Cited by 183 · see citing works

Minipig as a potential translatable model for monoclonal antibody pharmacokinetics after intravenous and subcutaneous administration

Zheng, Y., Tesar, D. B., Benincosa, L., Birnböck, H., Boswell, C. A., Bumbaca, D., Cowan, K. J., Danilenko, D. M., Daugherty, A. L., Fielder, P. J., et al. (2012) · mAbs · doi:10.4161/mabs.4.2.19387 · Cited by 149 · see citing works

Lessons for the clinic from rituximab pharmacokinetics and pharmacodynamics

Golay, J., Semenzato, G., Rambaldi, A., Foà, R., Gaidano, G., Gamba, E., Pane, F., Pinto, A., Specchia, G., Zaja, F., et al. (2013) · mAbs · doi:10.4161/mabs.26008 · Cited by 148 · see citing works

Glycodelete engineering of mammalian cells simplifies N-glycosylation of recombinant proteins

Meuris, L., Santens, F., Elson, G., Festjens, N., Boone, M., Dos Santos, A., Devos, S., Rousseau, F., Plets, E., Houthuys, E., et al. (2014) · Nature Biotechnology · doi:10.1038/nbt.2885 · Cited by 141 · see citing works

IVIg Use Associated with Ten-Fold Reduction of Serious Infections in Multiple Myeloma Patients Treated with Anti-BCMA Bispecific Antibodies

Lancman, G., Parsa, K., Kotlarz, K., Avery, L., Lurie, A., Lieberman-Cribbin, A., Cho, H. J., Parekh, S. S., Richard, S., Richter, J., et al. (2023) · Blood Cancer Discovery · doi:10.1158/2643-3230.bcd-23-0049 · Cited by 140 · see citing works

Rescuing AAV gene transfer from neutralizing antibodies with an IgG-degrading enzyme

Elmore, Z. C., Oh, D. K., Simon, K. E., Fanous, M. M., & Asokan, A. (2020) · JCI Insight · doi:10.1172/jci.insight.139881 · Cited by 137 · 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

Physiochemical and Biochemical Factors Influencing the Pharmacokinetics of Antibody Therapeutics

Bumbaca, D., Boswell, C. A., Fielder, P. J., & Khawli, L. A. (2012) · The AAPS Journal · doi:10.1208/s12248-012-9369-y · Cited by 119 · see citing works

Glycosylation and Fc Receptors

Hayes, J. M., Cosgrave, E. F. J., Struwe, W. B., Wormald, M., Davey, G. P., Jefferis, R., & Rudd, P. M. (2014) · Current Topics in Microbiology and Immunology · doi:10.1007/978-3-319-07911-0_8 · Cited by 110 · see citing works

Monoclonal antibodies for prophylactic and therapeutic use against viral infections

Both, L., Banyard, A. C., van Dolleweerd, C., Wright, E., Ma, J. K.-C., & Fooks, A. R. (2013) · Vaccine · doi:10.1016/j.vaccine.2013.01.025 · Cited by 107 · see citing works

Sex-hormone-driven innate antibodies protect females and infants against EPEC infection

Zeng, Z., Surewaard, B. G. J., Wong, C. H. Y., Guettler, C., Petri, B., Burkhard, R., Wyss, M., Le Moual, H., Devinney, R., Thompson, G. C., et al. (2018) · Nature Immunology · doi:10.1038/s41590-018-0211-2 · Cited by 96 · 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

The relationship between amyloid-beta and brain capillary endothelial cells in Alzheimer’s disease

Su, Q., Guo, J.-H., Zhang, Y.-L., Wang, J., & Zhang, Z.-N. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.335829 · Cited by 91 · see citing works

Polymeric human Fc-fusion proteins with modified effector functions

Mekhaiel, D. N. A., Czajkowsky, D. M., Andersen, J. T., Shi, J., El-Faham, M., Doenhoff, M., McIntosh, R. S., Sandlie, I., He, J., Hu, J., et al. (2011) · Scientific Reports · doi:10.1038/srep00124 · Cited by 85 · see citing works

Improved Therapeutic Results by Pretargeted Radioimmunotherapy of Non–Hodgkin's Lymphoma with a New Recombinant, Trivalent, Anti-CD20, Bispecific Antibody

Sharkey, R. M., Karacay, H., Litwin, S., Rossi, E. A., McBride, W. J., Chang, C.-H., & Goldenberg, D. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0037 · Cited by 75 · see citing works

Probiotics, mechanisms of action, and clinical perspectives for diarrhea management in children

do Carmo, M. S., Santos, C. I. D., Araújo, M. C., Girón, J. A., Fernandes, E. S., & Monteiro-Neto, V. (2018) · Food & Function · doi:10.1039/c8fo00376a · Cited by 75 · see citing works

Maternal autism-associated IgG antibodies delay development and produce anxiety in a mouse gestational transfer model

Braunschweig, D., Golub, M. S., Koenig, C. M., Qi, L., Pessah, I. N., Van de Water, J., & Berman, R. F. (2012) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2012.08.002 · Cited by 71 · see citing works

Placental antibody transfer efficiency and maternal levels: specific for measles, coxsackievirus A16, enterovirus 71, poliomyelitis I-III and HIV-1 antibodies

Fu, C., Lu, L., Wu, H., Shaman, J., Cao, Y., Fang, F., Yang, Q., He, Q., Yang, Z., & Wang, M. (2016) · Scientific Reports · doi:10.1038/srep38874 · Cited by 71 · see citing works

Projecting human pharmacokinetics of monoclonal antibodies from nonclinical data: comparative evaluation of prediction approaches in early drug development

Wang, J., Iyer, S., Fielder, P. J., Davis, J. D., & Deng, R. (2016) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.1952 · Cited by 69 · see citing works

Increased Muscle Force Production and Bone Mineral Density in ActRIIB-Fc-Treated Mature Rodents

Chiu, C.-S., Peekhaus, N., Weber, H., Adamski, S., Murray, E. M., Zhang, H. Z., Zhao, J. Z., Ernst, R., Lineberger, J., Huang, L., et al. (2013) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glt030 · Cited by 68 · see citing works

Expression of Neonatal Fc Receptor in the Eye

Powner, M. B., McKenzie, J. A. G., Christianson, G. J., Roopenian, D. C., & Fruttiger, M. (2014) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.13-12574 · Cited by 62 · see citing works

Physiologically based pharmacokinetic models of small molecules and therapeutic antibodies: a mini‐review on fundamental concepts and applications

Ferl, G. Z., Theil, F., & Wong, H. (2016) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.1994 · Cited by 54 · see citing works

Influence of improved FcRn binding on the subcutaneous bioavailability of monoclonal antibodies in cynomolgus monkeys

Datta-Mannan, A., Witcher, D. R., Lu, J., & Wroblewski, V. J. (2012) · mAbs · doi:10.4161/mabs.4.2.19364 · Cited by 53 · see citing works

Tumor Cell Targeting by Iron Oxide Nanoparticles Is Dominated by Different Factors In Vitro versus In Vivo

NDong, C., Tate, J. A., Kett, W. C., Batra, J., Demidenko, E., Lewis, L. D., Hoopes, P. J., Gerngross, T. U., & Griswold, K. E. (2015) · PLOS ONE · doi:10.1371/journal.pone.0115636 · Cited by 50 · see citing works

A new method for pharmaceutical compounding and storage of anti-VEGF biologics for intravitreal use in silicone oil-free prefilled plastic syringes

Lode, H. E., Gjølberg, T. T., Foss, S., Sivertsen, M. S., Brustugun, J., Andersson, Y., Jørstad, Ø. K., Moe, M. C., & Andersen, J. T. (2019) · Scientific Reports · doi:10.1038/s41598-019-54226-7 · Cited by 40 · see citing works

Farewell to Animal Testing: Innovations on Human Intestinal Microphysiological Systems

Kang, T., & Kim, H. (2016) · Micromachines · doi:10.3390/mi7070107 · Cited by 40 · see citing works

Importance and Considerations of Antibody Engineering in Antibody-Drug Conjugates Development from a Clinical Pharmacologist’s Perspective

Lucas, A. T., Moody, A., Schorzman, A. N., & Zamboni, W. C. (2021) · Antibodies · doi:10.3390/antib10030030 · Cited by 40 · see citing works

Hematopoietic cells as site of first-pass catabolism after subcutaneous dosing and contributors to systemic clearance of a monoclonal antibody in mice

Richter, W. F., Christianson, G. J., Frances, N., Grimm, H. P., Proetzel, G., & Roopenian, D. C. (2018) · mAbs · doi:10.1080/19420862.2018.1458808 · Cited by 39 · see citing works

Developing the IVIG biomimetic, Hexa-Fc, for drug and vaccine applications

Czajkowsky, D. M., Andersen, J. T., Fuchs, A., Wilson, T. J., Mekhaiel, D., Colonna, M., He, J., Shao, Z., Mitchell, D. A., Wu, G., et al. (2015) · Scientific Reports · doi:10.1038/srep09526 · Cited by 38 · see citing works

Biological sex differences in pharmacokinetics and adverse drug reactions

Aljohmani, A., & Yildiz, D. (2026) · Naunyn-Schmiedeberg's Archives of Pharmacology · doi:10.1007/s00210-025-04721-8 · Cited by 35 · 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

Pharmacokinetic‐pharmacodynamic modelling of the anti‐FcRn monoclonal antibody rozanolixizumab: Translation from preclinical stages to the clinic

Lledo‐Garcia, R., Dixon, K., Shock, A., & Oliver, R. (2022) · CPT: Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12739 · Cited by 18 · see citing works

Transplacental transfer of total immunoglobulin G and antibodies to Plasmodium falciparum antigens between the 24th week of gestation and term

Kayatani, A. K. K., Leke, R. G. F., Leke, R. I. J., Fogako, J., & Taylor, D. W. (2022) · Scientific Reports · doi:10.1038/s41598-022-21908-8 · Cited by 10 · 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 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

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

In vivo depletion of serum IgG by an affibody molecule binding the neonatal Fc receptor

Seijsing, J., Yu, S., Frejd, F. Y., Höidén‐Guthenberg, I., & Gräslund, T. (2018) · Scientific Reports · doi:10.1038/s41598-018-23481-5 · Cited by 49 · 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