The class I major histocompatibility complex related Fc receptor shows pH-dependent stability differences correlating with immunoglobulin binding and release

Structure of the human class I histocompatibility antigen, HLA-A2

Björkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., & Wiley, D. C. (1987) · Nature · doi:10.1038/329506a0 · Cited by 3,470 · see citing works

Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules

Falk, K., Rötzschke, O., Stevanovié, S., Jung, G., & Rammensee, H. (1991) · Nature · doi:10.1038/351290a0 · Cited by 2,412 · see citing works

The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens

Bjorkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., & Wiley, D. C. (1987) · Nature · doi:10.1038/329512a0 · Cited by 2,377 · see citing works

Antigen Recognition By Class-I Restricted T Lymphocyte

Townsend, A., & Bodmer, H. C. (1989) · Annual Review of Immunology · doi:10.1146/annurev.iy.07.040189.003125 · Cited by 1,192 · see citing works

Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolution

Saper, M. A., Björkman, P. J., & Wiley, D. C. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90567-p · Cited by 1,077 · see citing works

Association of class I major histocompatibility heavy and light chains induced by viral peptides

Townsend, A., Öhlén, C., Bastin, J. M., Ljunggren, H., Foster, L., & Kärre, K. (1989) · Nature · doi:10.1038/340443a0 · Cited by 985 · see citing works

Empty MHC class I molecules come out in the cold

Ljunggren, H., Stam, N. J., Öhlén, C., Neefjes, J., Höglund, P., Heemels, M.-T., Bastin, J. M., Schumacher, T. N., Townsend, A., Kärre, K., et al. (1990) · Nature · doi:10.1038/346476a0 · Cited by 921 · see citing works

Crystal Structures of Two Viral Peptides in Complex with Murine MHC Class I H-2K b

Fremont, D. H., Matsumura, M., Stura, E. A., Peterson, P. A., & Wilson, L. A. (1992) · Science · doi:10.1126/science.1323877 · Cited by 861 · see citing works

Identification of self peptides bound to purified HLA-B27

Jardetzky, T. S., Lane, W. S., Robinson, R. A., Madden, D. R., & Wiley, D. C. (1991) · Nature · doi:10.1038/353326a0 · Cited by 823 · see citing works

Isolation and analysis of naturally processed viral peptides as recognized by cytotoxic T cells

Rötzschke, O., Falk, K., Deres, K., Schild, H., Norda, M., Metzger, J. W., Jung, G., & Rammensee, H. (1990) · Nature · doi:10.1038/348252a0 · Cited by 771 · see citing works

Emerging Principles for the Recognition of Peptide Antigens by MHC Class I Molecules

Matsumura, M., Fremont, D. H., Peterson, P. A., & Wilson, L. A. (1992) · Science · doi:10.1126/science.1323878 · Cited by 731 · 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

The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation

Madden, D. R., Gorga, J. C., Strominger, J. L., & Wiley, D. C. (1991) · Nature · doi:10.1038/353321a0 · Cited by 679 · see citing works

Isolation of an endogenously processed immunodominant viral peptide from the class I H–2Kb molecule

van Bleek, G. M., & Nathenson, S. G. (1990) · Nature · doi:10.1038/348213a0 · Cited by 675 · see citing works

Specificity pockets for the side chains of peptide antigens in HLA-Aw68

Garrett, T., Saper, M. A., Björkman, P. J., Strominger, J. L., & Wiley, D. C. (1989) · Nature · doi:10.1038/342692a0 · Cited by 653 · see citing works

Cellular peptide composition governed by major histocompatibility complex class I molecules

Falk, K., Rötzschke, O., & Rammensee, H. (1990) · Nature · doi:10.1038/348248a0 · Cited by 436 · see citing works

Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro

Schumacher, T. N., Heemels, M.-T., Neefjes, J., Kast, W. M., Melief, C. J. M., & Ploegh, H. L. (1990) · Cell · doi:10.1016/0092-8674(90)90020-f · Cited by 410 · 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

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

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

Atomic structure of a human MHC molecule presenting an influenza virus peptide

Silver, M. L., Guo, H., Strominger, J. L., & Wiley, D. C. (1992) · Nature · doi:10.1038/360367a0 · Cited by 251 · see citing works

β2-Microglobulin from serum associates with MHC class I antigens on the surface of cultured cells

Bernabéu, C., van de Rijn, M., Lerch, P. G., & Terhorst, C. (1984) · Nature · doi:10.1038/308642a0 · Cited by 148 · see citing works

Thermal Stability Comparison of Purified Empty and Peptide-Filled Forms of a Class I MHC Molecule

Fahnestock, M. L., Tamir, I., Narhi, L. O., & Björkman, P. J. (1992) · Science · doi:10.1126/science.1360705 · Cited by 128 · see citing works

Excess β2 microglobulin promoting functional peptide association with purified soluble class I MHC molecules

Kozlowski, S., Takeshita, T., Boehncke, W., Takahashi, H., Boyd, L. F., Germain, R. N., Berzofsky, J. A., & Margulies, D. H. (1991) · Nature · doi:10.1038/349074a0 · Cited by 121 · see citing works

The β2-microglobulin dissociation rate is an accurate measure of the stability of MHC class I heterotrimers and depends on which peptide is bound

Parker, K. C., DiBrino, M., Hull, L. K., & Coligan, J. E. (1992) · The Journal of Immunology · doi:10.4049/jimmunol.149.6.1896 · Cited by 110 · see citing works

Expression and crystallization of a soluble and functional form of an Fc receptor related to class I histocompatibility molecules.

Gastinel, L. N., Simister, N. E., & Björkman, P. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.2.638 · Cited by 98 · 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

Dissociation and exchange of the beta 2-microglobulin subunit of HLA-A and HLA-B antigens.

Hyafil, F., & Strominger, J. L. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.11.5834 · Cited by 79 · see citing works

Cloning and Expression of the Neonatal Rat Intestinal Fc Receptor, a Major Histocompatibility Complex Class I Antigen HomologPreprint

Simister, N. E., & Mostov, K. E. (1989) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1989.054.01.068 · Cited by 64 · see citing works

Cytotoxic T lymphocytes from HLA-A2 transgenic mice specific for HLA-A2 expressed on human cells.

Bernhard, E. J., Le, A. X., Barbosa, J. A., Lacy, E., & Engelhard, V. H. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.168.3.1157 · Cited by 36 · see citing works

Binding of subclasses of rat immunoglobulin G to detergent-isolated Fc receptor from neonatal rat intestine.

Hobbs, S., Jackson, L. E., & Peppard, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47523-0 · Cited by 25 · see citing works

Subunit interactions of class I histocompatibility antigens

Parker, K. C., & Strominger, J. L. (1985) · Biochemistry · doi:10.1021/bi00341a039 · Cited by 20 · see citing works

Cold dark matter makes an exit

Lindley, D. (1991) · Nature · doi:10.1038/349014a0 · Cited by 12 · see citing works

MHC meets mother's milk

Parham, P. (1989) · Nature · doi:10.1038/337118a0 · Cited by 8 · see citing works

Molecular Basis of Fc Receptor Function

Hulett, M. D., & Hogarth, P. M. (1994) · Advances in immunology · doi:10.1016/s0065-2776(08)60671-9 · Cited by 496 · 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

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

The Neonatal Fc Receptor (FcRn): A Misnomer?

Pyzik, M., Sand, K. M. K., Hubbard, J. J., Andersen, J. T., Sandlie, I., & Blumberg, R. S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01540 · Cited by 432 · see citing works

Transepithelial Transport of Fc-Targeted Nanoparticles by the Neonatal Fc Receptor for Oral Delivery

Pridgen, E. M., Alexis, F., Kuo, T. T., Levy‐Nissenbaum, E., Karnik, R., Blumberg, R. S., Langer, R., & Farokhzad, O. C. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007049 · Cited by 408 · 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

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

Fc RECEPTORS AND THEIR INTERACTIONS WITH IMMUNOGLOBULINS

Raghavan, M., & Björkman, P. J. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.181 · Cited by 312 · see citing works

The therapeutic age of the neonatal Fc receptor

Pyzik, M., Kozicky, L. K., Gandhi, A. K., & Blumberg, R. S. (2023) · Nature Reviews Immunology · doi:10.1038/s41577-022-00821-1 · Cited by 288 · see citing works

Polymeric nanoparticle drug delivery technologies for oral delivery applications

Pridgen, E. M., Alexis, F., & Farokhzad, O. C. (2015) · Expert Opinion on Drug Delivery · doi:10.1517/17425247.2015.1018175 · Cited by 270 · see citing works

Neonatal Fc Receptor: From Immunity to Therapeutics

Kuo, T. T., Baker, K., Yoshida, M., Qiao, S., Aveson, V. G., Lencer, W. I., & Blumberg, R. S. (2010) · Journal of Clinical Immunology · doi:10.1007/s10875-010-9468-4 · Cited by 248 · see citing works

Neonatal Fc receptor and IgG-based therapeutics

Kuo, T. T., & Aveson, V. G. (2011) · mAbs · doi:10.4161/mabs.3.5.16983 · Cited by 236 · see citing works

FcRn: the MHC class I-related receptor that is more than an IgG transporter

Ghetie, V. F., & Ward, E. S. (1997) · Immunology Today · doi:10.1016/s0167-5699(97)01172-9 · Cited by 215 · see citing works

Finally! the Brambell receptor (FcRB)

Junghans, R. P. (1997) · Immunologic Research · doi:10.1007/bf02786322 · Cited by 205 · see citing works

Factors Affecting the FcRn-Mediated Transplacental Transfer of Antibodies and Implications for Vaccination in Pregnancy

Wilcox, C. R., Holder, B., & Jones, C. E. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01294 · Cited by 200 · 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 recycling and transcytotic pathways for IgG transport by FcRn are distinct and display an inherent polarity

Tzaban, S., Massol, R. H., Yen, E., Hamman, W., Frank, S. R., Lapierre, L. A., Hansen, S. H., Goldenring, J. R., Blumberg, R. S., & Lencer, W. I. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200809122 · Cited by 169 · see citing works

Polymeric Nanoparticle Technologies for Oral Drug Delivery

Pridgen, E. M., Alexis, F., & Farokhzad, O. C. (2014) · Clinical Gastroenterology and Hepatology · doi:10.1016/j.cgh.2014.06.018 · Cited by 168 · see citing works

The Immunologic Functions of the Neonatal Fc Receptor for IgG

Räth, T., Kuo, T. T., Baker, K., Qiao, S., Kobayashi, K., Yoshida, M., Roopenian, D. C., Fiebiger, E., Lencer, W. I., & Blumberg, R. S. (2012) · Journal of Clinical Immunology · doi:10.1007/s10875-012-9768-y · Cited by 159 · 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

Boosting therapeutic potency of antibodies by taming Fc domain functions

Kang, T. H., & Jung, S. T. (2019) · Experimental & Molecular Medicine · doi:10.1038/s12276-019-0345-9 · Cited by 142 · 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

The MHC class I homolog encoded by human cytomegalovirus binds endogenous peptides

Fahnestock, M. L., Johnson, J. L., Feldman, R. M. R., Neveu, J. M., Lane, W. S., & Björkman, P. J. (1995) · Immunity · doi:10.1016/1074-7613(95)90129-9 · Cited by 141 · see citing works

Immune and non-immune functions of the (not so) neonatal Fc receptor, FcRn

Baker, K., Qiao, S., Kuo, T. T., Kobayashi, K., Yoshida, M., Lencer, W. I., & Blumberg, R. S. (2009) · Seminars in Immunopathology · doi:10.1007/s00281-009-0160-9 · Cited by 131 · see citing works

The Versatile MHC Class I-related FcRn Protects IgG and Albumin from Degradation: Implications for Development of New Diagnostics and Therapeutics

Andersen, J. T., & Sandlie, I. (2009) · Drug Metabolism and Pharmacokinetics · doi:10.2133/dmpk.24.318 · Cited by 123 · see citing works

The Role of FcRn in Antigen Presentation

Baker, K., Räth, T., Pyzik, M., & Blumberg, R. S. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00408 · Cited by 123 · see citing works

Engineering therapeutic monoclonal antibodies

Liu, X., Pop, L. M., & Vitetta, E. S. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00601.x · Cited by 108 · see citing works

The Neonatal Fc Receptor (FcRn) Enhances Human Immunodeficiency Virus Type 1 (HIV-1) Transcytosis across Epithelial Cells

Gupta, S., Gach, J. S., Becerra, J. C., Phan, T. B., Pudney, J. A., Moldoveanu, Z., Joseph, S., Landucci, G., Supnet, M., Ping, L., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003776 · Cited by 102 · see citing works

A comprehensive review of the neonatal Fc receptor and its application in drug delivery

Martins, J. P., Kennedy, P. J., Santos, H. A., Barrias, C. C., & Sarmento, B. F. C. C. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.03.007 · Cited by 102 · see citing works

The Recognition of the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule, T10, by the γδ T Cell, G8

Crowley, M. P., Reich, Z., Mavaddat, N., Altman, J. D., & Chien, Y. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.7.1223 · Cited by 96 · see citing works

Non‐classical MHC class I molecules on intestinal epithelial cells: mediators of mucosal crosstalk

Shao, L., Kamalu, O., & Mayer, L. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00295.x · Cited by 93 · see citing works

Human FcRn Transgenic Mice for Pharmacokinetic Evaluation of Therapeutic Antibodies

Roopenian, D. C., Christianson, G. J., & Sproule, T. J. (2006) · Methods in molecular biology · doi:10.1007/978-1-60761-058-8_6 · Cited by 89 · see citing works

Glucose-responsive oral insulin delivery for postprandial glycemic regulation

Yu, J., Zhang, Y., Wang, J., Wen, D., Kahkoska, A. R., Buse, J. B., & Gu, Z. (2018) · Nano Research · doi:10.1007/s12274-018-2264-9 · Cited by 88 · see citing works

FcRn: From Molecular Interactions to Regulation of IgG Pharmacokinetics and Functions

Challa, D. K., Velmurugan, R., Ober, R. J., & Ward, E. S. (2014) · Current topics in microbiology and immunology · doi:10.1007/978-3-319-07911-0_12 · Cited by 84 · see citing works

Characterization of the porcine neonatal Fc receptor—potential use for trans‐epithelial protein delivery

Stirling, C. M. A., Charleston, B., Takamatsu, H., Claypool, S. M., Lencer, W. I., Blumberg, R. S., & Wileman, T. E. (2005) · Immunology · doi:10.1111/j.1365-2567.2004.02121.x · Cited by 82 · see citing works

Neonatal Fc receptor expression in macrophages is indispensable for IgG homeostasis

Challa, D. K., Wang, X., Montoyo, H. P., Velmurugan, R., Ober, R. J., & Ward, E. S. (2019) · mAbs · doi:10.1080/19420862.2019.1602459 · Cited by 74 · see citing works

Orally Administrable Therapeutic Synthetic Nanoparticle for Zika Virus

Surnar, B., Kamran, M. Z., Shah, A. S., Basu, U., Kolishetti, N., Deo, S. K., Jayaweera, D. T., Daunert, S., & Dhar, S. (2019) · ACS Nano · doi:10.1021/acsnano.9b02807 · 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

Characterization of a Murine Cytomegalovirus Class I Major Histocompatibility Complex (MHC) Homolog: Comparison to MHC Molecules and to the Human Cytomegalovirus MHC Homolog

Chapman, T. L., & Björkman, P. J. (1998) · Journal of Virology · doi:10.1128/jvi.72.1.460-466.1998 · Cited by 68 · see citing works

IgG regulation through FcRn blocking: A novel mechanism for the treatment of myasthenia gravis

Wolfe, G. I., Ward, E. S., de Haard, H., Ulrichts, P., Mozaffar, T., Pasnoor, M., & Vidarsson, G. (2021) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2021.118074 · Cited by 66 · see citing works

Neonatal Fc receptor (FcRn): a novel target for therapeutic antibodies and antibody engineering

Wang, Y., Tian, Z., Diraviyam, T., & Zhang, X. (2014) · Journal of drug targeting · doi:10.3109/1061186x.2013.875030 · Cited by 62 · see citing works

Biochemical characterization and crystalization of human Zn-α 2 -glycoprotein, a soluble class I major histocompatibility complex homolog

Sánchez, L. M., López-Otı́n, C., & Björkman, P. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4626 · Cited by 57 · see citing works

Biomimetic and bioinspired strategies for oral drug delivery

Hu, X., Yang, G., Chen, S., Luo, S., & Zhang, J. (2019) · Biomaterials Science · doi:10.1039/c9bm01378d · Cited by 53 · see citing works

An engineered affibody molecule with pH-dependent binding to FcRn mediates extended circulatory half-life of a fusion protein

Seijsing, J., Lindborg, M., Höidén‐Guthenberg, I., Bönisch, H., Gunneriusson, E., Frejd, F. Y., Abrahmsén, L., Ekblad, C., Löfblom, J., Uhlén, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417717111 · Cited by 52 · see citing works

Are endosomal trafficking parameters better targets for improving mAb pharmacokinetics than FcRn binding affinity?

Gurbaxani, B. M., Dostálek, M., & Gardner, I. B. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.05.008 · Cited by 50 · see citing works

Ca²⁺-dependent Calmodulin Binding to FcRn Affects Immunoglobulin G Transport in the Transcytotic Pathway

Dickinson, B. L., Claypool, S. M., D'Angelo, J. A., Aiken, M. L., Venu, N., Yen, E. H., Wagner, J. S., Borawski, J. A., Pierce, A. T., Hershberg, R., et al. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-07-0658 · Cited by 50 · see citing works

The effect of fatty diacid acylation of human PYY3-36 on Y2 receptor potency and half-life in minipigs

Østergaard, S., Paulsson, J. F., Kofoed, J., Zosel, F., Olsen, J., Jeppesen, C. B., Spetzler, J. C., Ynddal, L., Schleiss, L. G., Christoffersen, B. Ø., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-00654-3 · Cited by 49 · see citing works

Monoclonal Antibody Engineering and Design to Modulate FcRn Activities: A Comprehensive Review

Ramdani, Y., Lamamy, J., Watier, H., & Gouilleux‐Gruart, V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179604 · Cited by 46 · see citing works

Expression of FcRn, the MHC Class I-Related Receptor for IgG, in Human Keratinocytes

Cauza, K., Hinterhuber, G., Dingelmaier‐Hovorka, R., Brugger, K., Klosner, G., Horvat, R., Wolff, K. S., & Foedinger, D. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.23542.x · Cited by 46 · see citing works

Structure of a Pheromone Receptor-Associated MHC Molecule with an Open and Empty Groove

Olson, R., Huey‐Tubman, K. E., Dulac, C. G., & Björkman, P. J. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030257 · Cited by 45 · see citing works

The structure and evolution of FcRn

Simister, N. E., & Ahouse, J. C. (1996) · Research in Immunology · doi:10.1016/0923-2494(96)89647-7 · Cited by 43 · see citing works

Human cytomegalovirus evades antibody-mediated immunity through endoplasmic reticulum-associated degradation of the FcRn receptor

Liu, X., Palaniyandi, S., Zhu, I., Tang, J., Li, W., Wu, X., Ochsner, S. P., Pauza, C. D., Cohen, J. I., & Zhu, X. (2019) · Nature Communications · doi:10.1038/s41467-019-10865-y · Cited by 42 · see citing works

Evidence for a common mucosal immune system in the pig

Wilson, H. L., & Obradovic, M. R. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.09.004 · Cited by 42 · see citing works

Insulin Delivery Using Dynamic Covalent Boronic Acid/Ester‐Controlled Release

Banach, Ł., Williams, G. T., & Fossey, J. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202100118 · Cited by 41 · see citing works

Effects of Peptide Length and Composition on Binding to an Empty Class I MHC Heterodimer

Fahnestock, M. L., Johnson, J. L., Feldman, R. M. R., Tsomides, T. J., Mayer, J. P., Narhi, L. O., & Björkman, P. J. (1994) · Biochemistry · doi:10.1021/bi00192a020 · Cited by 41 · see citing works

Building the design, translation and development principles of polymeric nanomedicines using the case of clinically advanced poly(lactide(glycolide))–poly(ethylene glycol) nanotechnology as a model: An industrial viewpoint

Reddy, L. H., & Bazile, D. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2016.08.012 · Cited by 38 · see citing works

FcRn expression in cancer: Mechanistic basis and therapeutic opportunities

Rudnik‐Jansen, I., & Howard, K. A. (2021) · Journal of Controlled Release · doi:10.1016/j.jconrel.2021.07.007 · Cited by 38 · see citing works

Reduced FcRn-mediated transcytosis of IgG2 due to a missing Glycine in its lower hinge

Stapleton, N. M., Brinkhaus, M., Armour, K. L., Bentlage, A. E. H., de Taeye, S. W., Temming, A. R., Mok, J. Y., Brasser, G., Maas, M. J., van Esch, W. J. E., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40731-2 · Cited by 36 · see citing works

Claudin‐4 Undergoes Age‐Dependent Change in Cellular Localization on Pig Jejunal Villous Epithelial Cells, Independent of Bacterial Colonization

Pasternak, J. A., Kent-Dennis, C., Kessel, A. G. V., & Wilson, H. L. (2015) · Mediators of Inflammation · doi:10.1155/2015/263629 · Cited by 34 · see citing works

Hybrid IgA2/IgG1 Antibodies with Tailor-Made Effector Functions

Chintalacharuvu, K. R., Vuong, L.-U. C., Loi, L. A., Larrick, J. W., & Morrison, S. L. (2001) · Clinical Immunology · doi:10.1006/clim.2001.5083 · Cited by 31 · see citing works

MHC homologs in the nervous system — they haven’t lost their groove

Olson, R., Dulac, C. G., & Björkman, P. J. (2006) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2006.05.007 · Cited by 29 · see citing works

Fc Receptors in Immune Responses

Mancardi, D. A., & Daëron, M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.00119-7 · Cited by 29 · see citing works

Relevance of the Materno-Fetal Interface for the Induction of Antigen-Specific Immune Tolerance

Mimoun, A., Delignat, S., Peyron, I., Daventure, V., Lecerf, M., Dimitrov, J. D., Kaveri, S. V., Bayry, J., & Lacroix‐Desmazes, S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00810 · Cited by 28 · see citing works

Peptide-Independent Folding and CD8αα Binding by the Nonclassical Class I Molecule, Thymic Leukemia Antigen

Weber, D. A., Attinger, A., Kemball, C. C., Wigal, J. L., Pohl, J., Xiong, Y., Reinherz, E. L., Cheroutre, H., Kronenberg, M., & Jensen, P. E. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.10.5708 · Cited by 28 · see citing works

Human FcRn Transgenic Mice for Pharmacokinetic Evaluation of Therapeutic Antibodies

Roopenian, D. C., Christianson, G. J., Proetzel, G., & Sproule, T. J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3661-8_6 · Cited by 27 · see citing works

Structure and Function of Immunoglobulins

Späth, P. (1999) · Sepsis · doi:10.1023/a:1009899803032 · Cited by 27 · see citing works

Design, expression and characterization of a soluble single-chain functional human neonatal Fc receptor

Feng, Y., Gong, R., & Dimitrov, D. S. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.03.012 · Cited by 25 · see citing works

Genetically Engineered Humanized Mouse Models for Preclinical Antibody Studies

Proetzel, G., Wiles, M. V., & Roopenian, D. C. (2013) · BioDrugs · doi:10.1007/s40259-013-0071-0 · Cited by 22 · see citing works

Computational determination of the structure of rat fc bound to the neonatal fc receptor

Weng, Z., Gulukota, K., Vaughn, D. E., Björkman, P. J., & DeLisi, C. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2020 · Cited by 20 · see citing works

The Protective Properties of Milk and Colostrum in Non-Human Species

Tizard, I. R. (2010) · Springer eBooks · doi:10.1007/978-1-4615-0661-4_7 · Cited by 20 · see citing works

Novel molecules related to MHC antigens

Stroynowski, I., & Forman, J. (1995) · Current Opinion in Immunology · doi:10.1016/0952-7915(95)80034-4 · Cited by 20 · see citing works

Enhanced In Vitro Transcytosis of Simian Immunodeficiency Virus Mediated by Vaccine-Induced Antibody Predicts Transmitted/Founder Strain Number After Rectal Challenge

Gupta, S., Pegu, P., Venzon, D. J., Gach, J. S., Ma, Z.-M., Landucci, G., Miller, C. J., Franchini, G., & Forthal, D. N. (2014) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiu300 · Cited by 17 · see citing works

The Role of Antigen Presentation in Tumor-Associated Macrophages

Stopforth, R. J., & Ward, E. S. (2020) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.2020034910 · Cited by 16 · see citing works

Investigation of FcRn‐Mediated Transepithelial Mechanisms for Oral Nanoparticle Delivery Systems

Yu, Y., Wu, Z., Wu, J., Shen, X., Wu, R., Zhou, M., Li, L., & Huang, Y. (2021) · Advanced Therapeutics · doi:10.1002/adtp.202100145 · Cited by 15 · see citing works

Characteristic of the components and the metabolism mechanism of goat colostrum: a review

Zhou, A., Liu, G., & Jiang, X. (2023) · Animal Biotechnology · doi:10.1080/10495398.2023.2199500 · Cited by 14 · see citing works

The role of immunoglobulin transport receptor, neonatal Fc receptor in mucosal infection and immunity and therapeutic intervention

Qian, S., Zhang, D., Yang, Z., Li, R., Zhang, X., Gao, F., & Yu, L. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112583 · Cited by 12 · see citing works

Single chain antibody fragments with pH dependent binding to FcRn enabled prolonged circulation of therapeutic peptide in vivo

Qiu, Y., Lv, W., Xu, M., & Xu, Y. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.03.017 · Cited by 12 · see citing works

Crystal structure of the MHC class Ib molecule H2-M3

Wang, C.-R., Lindahl, K. F., & Deisenhofer, J. (1996) · Research in Immunology · doi:10.1016/0923-2494(96)89644-1 · Cited by 12 · see citing works

Origin of the apical transcytic membrane system in jejunal absorptive cells of neonates

Kumagai, N., Baba, R., Sakuma, Y., Arita, K., Shinohara, M., Kourogi, M., Fujimoto, S., & Fujita, M. (2011) · Medical Molecular Morphology · doi:10.1007/s00795-010-0506-3 · Cited by 11 · see citing works

Advances in polymeric nanoparticles for oral drug delivery: mechanisms, challenges, emerging trends, and preclinical to clinical perspectives

Zehravi, M., Khan, S. L., Gupta, J. K., Jahnavi, P., Babu, R. H., Vidiyala, N., Averineni, A., Dharmamoorthy, G., Dantinapalli, V. L. S., Elumalai, S., et al. (2025) · 3 Biotech · doi:10.1007/s13205-025-04659-x · Cited by 10 · see citing works

Mannose 6-phosphate receptor-targeting antibodies preserve Fc receptor-mediated recycling

Gauthier, C., Mariot, J., Daurat, M., Dhommée, C., Cheikh, K. E., Morère, E., Depaepe, G., Gary‐Bobo, M., Morère, A., Garcia, M., et al. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.05.011 · Cited by 10 · see citing works

Robust Expression of the Human Neonatal Fc Receptor in a Truncated Soluble Form and as a Full-Length Membrane-Bound Protein in Fusion with eGFP

Seijsing, J., Lindborg, M., Löfblom, J., Uhlén, M., & Gräslund, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081350 · Cited by 10 · see citing works

Rapid detection of procalcitonin using dual-color carbon quantum dots as fluorescent probes in FRET assay

Tian, Y., Du, Y., Chen, Z., Li, L., Yan, R., Li, X., & Yue, J. (2025) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2025.126207 · Cited by 9 · see citing works

Sialylation-dependent pharmacokinetics and differential complement pathway inhibition are hallmarks of CR1 activityin vivo

Wymann, S., Mischnik, M., Leong, D., Ghosh, S., Tan, X., Cao, H., Kuehnemuth, B., Powers, G. A., Halder, P., de Souza, M. J., et al. (2022) · Biochemical Journal · doi:10.1042/bcj20220054 · Cited by 8 · see citing works

Exploiting the neonatal crystallizable fragment receptor to treat kidney disease

Dylewski, J. F., Haddad, G., & Blaine, J. T. (2023) · Kidney International · doi:10.1016/j.kint.2023.09.024 · Cited by 6 · see citing works

Fc Receptors and Fc Receptor-Like Molecules within the Immunoreceptor Family

Daëron, M. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.02017-8 · Cited by 5 · see citing works

Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility

Kajikawa, M., Ose, T., Fukunaga, Y., Okabe, Y., Matsumoto, N., Yonezawa, K., Shimizu, N., Kollnberger, S., Kasahara, M., & Maenaka, K. (2018) · Nature Communications · doi:10.1038/s41467-018-06797-8 · Cited by 4 · see citing works

Monomeric Fc Fusion Molecules

Dumont, J. A., Low, S. C., Peters, R., & Bitonti, A. J. (2009) · Wiley eBooks · doi:10.1002/9780470485408.ch33 · Cited by 4 · see citing works

A POSSIBLE APPROACH FOR ORAL DRUG DELIVERY OF NANOPARTICLES

Minhat, R. A., & Hagen, T. (2014) · COSMOS · doi:10.1142/s0219607714400035 · Cited by 3 · see citing works

FcRn antagonists in ITP

Newland, A. C., & McDonald, V. (2020) · Annals of Blood · doi:10.21037/aob-20-55 · Cited by 3 · see citing works

New and emerging treatments of Guillain–Barré syndrome

Lehmann, H. C., Zhang, G., & Sheikh, K. A. (2014) · Expert Opinion on Orphan Drugs · doi:10.1517/21678707.2014.925393 · Cited by 2 · see citing works

Regulation of Immunological Responses by the Neonatal Fc Receptor for IgG, FcRn

Baker, K., Räth, T., & Blumberg, R. S. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7107-3_8 · Cited by 1 · see citing works

ADVANCES IN TRANSLATIONAL SCIENCE

Sellin, J. H., Murthy, S. K., Goetz, M., Hoffman, A. W., & Kießlich, R. (2012) · Cited by 1 · see citing works

Monomeric Fc Fusion Technology: An Approach to Create Long‐Lasting Clotting Factors

Dumont, J. A., Jin, X., Peters, R., Luk, A. Y., Pierce, G. F., & Bitonti, A. J. (2012) · Wiley eBooks · doi:10.1002/9783527644827.ch10 · Cited by 1 · see citing works

Overview Of Antibody- Based Therapeutics Present And Future Promise

Grewal, I. S. (2009) · CRC Press eBooks · doi:10.1201/9781420063219-6 · Cited by 1 · see citing works

Commentary The polymeric immunoglobulin receptor and the Brambell receptor: non-haematopoietic FcRs, with much to compare

Junghans, R. P. (1998) · Springer eBooks · doi:10.1007/978-94-011-5018-7_7

Antibodies and B Lymphocytes

Cushley, W., & Borland, G. (2010) · Wiley eBooks · doi:10.1002/9780470688618.taw0097

Characterization and Engineering of Human Proteins as Therapeutic Candidates

Kim, K. (2018) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2018.354

Investigating the role of kidney mononuclear phagocytes in immune complex-induced inflammation.

Richoz, N. (2019) · Apollo (University of Cambridge) · doi:10.17863/cam.50696

FcRn Expression in Endometrial Cancer and Its Association with Clinicopathologic Features

Song, D. H., Yang, J., Kim, C. H., Kim, M. H., Jo, J. Y., & Baek, J. C. (2023) · Diagnostics · doi:10.3390/diagnostics13243660

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

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

Molecular mechanism of pH dependent antibody binding: Structure/function studies on the neonatal Fc receptor

Vaughn, D. E. (2012) · CaltechTHESIS (California Institute of Technology) · doi:10.7907/bzyh-hn75

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

Conformational Destabilization of Immunoglobulin G Increases the Low pH Binding Affinity with the Neonatal Fc Receptor

Walters, B. T., Jensen, P. F., Larraillet, V., Lin, K., Patapoff, T. W., Schlothauer, T., Rand, K. D., & Zhang, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691568 · Cited by 42 · see citing works