Cell surface dynamics and cellular distribution of endogenous FcRn
Open accessAbstract
A major role for FcRn is the salvage of pinocytosed IgG and albumin from a degradative fate in lysosomes. FcRn achieves this by binding IgG in a pH-dependent manner in acidic endosomes and recycling it to the plasma membrane to be released at neutral pH. This is important in maintaining high serum IgG and albumin levels and has the potential to be exploited to modulate the pharmacokinetics of antibody-based therapeutics. Although FcRn is responsible for the recycling of IgG, the dynamic behaviour of endogenous FcRn is not well understood. Our data shows that the majority of endogenous receptor is distributed throughout the endosomal system and is present only at a low percentage on the plasma membrane at steady state. A significant fraction of FcRn at the cell surface appears to be endocytosis resistant while the remainder can undergo rapid endocytosis. To maintain surface levels of the receptor, endocytosed FcRn is replaced with FcRn from the internal pool. This unexpected complexity in FcRn cell surface dynamics has led us to propose a model for FcRn trafficking that should be taken into account when targeting FcRn at the cell surface for therapeutic purposes.
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FcRn expression is dynamically regulated and broadly distributed throughout the uptake/endosomal pathway, although most evidence demonstrates that only a small fraction sits at the cell surface at any one point in time.
“our understanding is that FcRn expression is dynamically regulated and broadly distributed throughout the uptake/endosomal pathway, although most evidence demonstrates that only a small fraction sits at the cell surface at any one point in time [13–16].”
From The uptake, intracellular trafficking and recycling of FcRn-blocking therapeutics in human endothelial cells in vitro (2026) · cites this paper as [13]
The Discussion reports that endogenous FcRn is distributed throughout the endosomal system in HepG2 cells and that approximately 4–7% is at the cell surface. It also describes dynamic trafficking between surface and internal pools, but does not establish that FcRn expression itself is dynamically regulated; the authors say that a signal mobilising intracellular FcRn has yet to be identified. (LLM, conf=0.85)
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Cites
A guided tour into subcellular colocalization analysis in light microscopy
Bolte, S., & Cordelières, F. P. (2006) · Journal of Microscopy · doi:10.1111/j.1365-2818.2006.01706.x · Cited by 5,286 · see citing works
A practical guide to evaluating colocalization in biological microscopy
Dunn, K. W., Kamocka, M. M., & McDonald, J. H. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00462.2010 · Cited by 2,012 · see citing works
Maxfield, F. R., & McGraw, T. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1315 · Cited by 1,701 · see citing works
Mannose 6-phosphate receptors: new twists in the tale
Ghosh, P., Dahms, N. M., & Kornfeld, S. A. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1050 · Cited by 1,083 · see citing works
EEA1, an Early Endosome-Associated Protein.
Mu, F., Callaghan, J. M., Steele‐Mortimer, O., Stenmark, H., Parton, R. G., Campbell, P. L., McCluskey, J., Yeo, J.-P., Tock, E. P. C., & Toh, B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13503 · Cited by 704 · see citing works
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
Ciechanover, A. J., Schwartz, A. L., Dautry‐Varsat, A., & Lodish, H. F. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44551-0 · Cited by 559 · see citing works
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
Endocytosis of Receptor Tyrosine KinasesPreprint
Goh, L. K., & Sorkin, A. D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a017459 · Cited by 449 · see citing works
Regulated Migration of Epidermal Growth Factor Receptor from Caveolae
Mineo, C., Gill, G. N., & Anderson, R. G. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30636 · Cited by 321 · see citing works
Raghavan, M., Bonagura, V. R., Morrison, S. L., & Bjorkman, P. J. (1995) · Biochemistry · doi:10.1021/bi00045a005 · Cited by 317 · 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
Albumin Binding to FcRn: Distinct from the FcRn−IgG Interaction
Chaudhury, C., Brooks, C. L., Carter, D. C., Robinson, J. M., & Anderson, C. L. (2006) · Biochemistry · doi:10.1021/bi052628y · Cited by 290 · see citing works
Dependence of antibody-mediated presentation of antigen on FcRn
Qiao, S., Kobayashi, K., Johansen, F., Sollid, L. M., Andersen, J. T., Milford, E. L., Roopenian, D. C., Lencer, W. I., & Blumberg, R. S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801717105 · Cited by 283 · 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 263 · 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
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
Association with Membrane Protrusions Makes ErbB2 an Internalization-resistant Receptor
Hommelgaard, A. M., Lerdrup, M., & van Deurs, B. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-08-0596 · Cited by 210 · see citing works
Ward, E. S., Martinez, C., Vaccaro, C., Zhou, J., Tang, Q., & Ober, R. J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-08-0735 · Cited by 193 · see citing works
Internalization and subcellular localization of transferrin and transferrin receptors in HeLa cells.
Lamb, J. E., Ray, F., Ward, J. H., Kushner, J. P., & Kaplan, J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32120-3 · Cited by 175 · see citing works
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
Wani, M. A., Haynes, L. D., Kim, J., Bronson, C. L., Chaudhury, C., Mohanty, S., Waldmann, T. A., Robinson, J. M., & Anderson, C. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600548103 · Cited by 147 · see citing works
Claypool, S. M., Dickinson, B. L., Wagner, J. S., Johansen, F.-E., Venu, N., Borawski, J. A., Lencer, W. I., & Blumberg, R. S. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-11-0832 · Cited by 139 · see citing works
Engineered Monoclonal Antibody with Novel Antigen-Sweeping Activity In Vivo
Igawa, T., Maeda, A., Haraya, K., Tachibana, T., Iwayanagi, Y., Mimoto, F., Higuchi, Y., Ishii, S., Tamba, S., Hironiwa, N., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063236 · Cited by 106 · see citing works
Multivalent immune complexes divert FcRn to lysosomes by exclusion from recycling sorting tubules
Weflen, A. W., Baier, N., Tang, Q.-J., Van den Hof, M., Blumberg, R. S., Lencer, W. I., & Massol, R. H. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-04-0174 · Cited by 101 · see citing works
Waldmann, T. A., & Terry, W. D. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114947 · Cited by 101 · see citing works
Igawa, T., Haraya, K., & Hattori, K. (2016) · Immunological Reviews · doi:10.1111/imr.12392 · Cited by 99 · see citing works
The transmission of immune globulins from the mother to the foetal and newborn young
Brambell, F. W. R. (1969) · Proceedings of The Nutrition Society · doi:10.1079/pns19690007 · Cited by 97 · see citing works
Targeting FcRn for the modulation of antibody dynamics
Ward, E. S., Devanaboyina, S. C., & Ober, R. J. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.02.007 · Cited by 89 · see citing works
Tesar, D. B., Tiangco, N. E., & Björkman, P. J. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00457.x · Cited by 87 · see citing works
Quantitative cumulative biodistribution of antibodies in mice
Yip, V., Palma, E., Tesar, D. B., Mundo, E. E., Bumbaca, D., Torres, E. K., Reyes, N. A., Shen, B., Fielder, P. J., Prabhu, S., et al. (2014) · mAbs · doi:10.4161/mabs.28254 · Cited by 87 · see citing works
Gabriel, L. R., Wu, S., Kearney, P. J., Bellve, K. D., Standley, C., Fogarty, K. E., & Melikian, H. E. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3284-13.2013 · Cited by 78 · see citing works
Dukes, J. D., Fish, L. P., Richardson, J. D., Blaikley, E., Burns, S., Caunt, C. J., Chalmers, A. D., & Whitley, P. R. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-04-0343 · Cited by 65 · see citing works
Self-citationNeonatal 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 64 · see citing works
Dukes, J. D., Whitley, P. R., & Chalmers, A. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028659 · Cited by 57 · see citing works
Self-citationBerryman, M. A., & Rodewald, R. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.6.2347 · Cited by 51 · see citing works
New functions of the MHC class I-related Fc receptor, FcRn
Simister, N. E., Israel, E. J., Ahouse, J. C., & Story, C. M. (1997) · Biochemical Society Transactions · doi:10.1042/bst0250481 · Cited by 48 · see citing works
Ellinger, I., Praetor, A., & Hunziker, W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8998 · Cited by 44 · see citing works
Using multifocal plane microscopy to reveal novel trafficking processes in the recycling pathway
Gan, Z., Ram, S., Ober, R. J., & Ward, E. S. (2013) · Journal of Cell Science · doi:10.1242/jcs.116327 · Cited by 38 · see citing works
Cell-Surface Biotinylation to Study Endocytosis and Recycling of Occludin
Nishimura, N., & Sasaki, T. (2008) · Methods in molecular biology · doi:10.1007/978-1-59745-178-9_7 · Cited by 30 · see citing works
Targeting FcRn for therapy: From live cell imaging to in vivo studies in mice
Ward, E. S., Velmurugan, R., & Ober, R. J. (2014) · Immunology Letters · doi:10.1016/j.imlet.2014.02.008 · Cited by 13 · see citing works
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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 445 · see citing works
Molitoris, B. A., Sandoval, R. M., Yadav, S. P. S., & Wagner, M. C. (2022) · Physiological Reviews · doi:10.1152/physrev.00014.2021 · Cited by 146 · 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
Lee, C., Kang, T. H., Godon, O., Watanabe, M., Delidakis, G., Gillis, C. M., Sterlin, D., Hardy, D., Cogné, M., Macdonald, L. E., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13108-2 · Cited by 86 · see citing works
Novel myostatin-specific antibody enhances muscle strength in muscle disease models
Muramatsu, H., Kuramochi, T., Katada, H., Ueyama, A., Ruike, Y., Ohmine, K., Shida-Kawazoe, M., Miyano-Nishizawa, R., Shimizu, Y., Okuda, M., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-81669-8 · Cited by 62 · see citing works
In Translation: FcRn across the Therapeutic Spectrum
Qi, T., & Cao, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063048 · Cited by 59 · see citing works
Antibody variable sequences have a pronounced effect on cellular transport and plasma half-life
Grevys, A., Frick, R., Mester, S., Flem-Karlsen, K., Nilsen, J., Foss, S., Sand, K. M. K., Emrich, T., Fischer, J. A. A., Greiff, V., et al. (2022) · iScience · doi:10.1016/j.isci.2022.103746 · Cited by 51 · see citing works
Martins, J. P., Figueiredo, P., Wang, S., Espo, E., Celi, E., Martins, B., Kemell, M., Moslova, K., Mäkilä, E. M., Salonen, J., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.08.007 · Cited by 50 · see citing works
Therapeutic antibodies – natural and pathological barriers and strategies to overcome them
Ojaimi, Y. A., Blin, T., Lamamy, J., Gracia, M., Pitiot, A., Denevault‐Sabourin, C., Joubert, N., Pouget, J., Gouilleux‐Gruart, V., Heuzé‐Vourc'h, N., et al. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108022 · Cited by 41 · see citing works
Brennan, F. R., Polli, J. R., Sathish, J. G., Ramones, M., Wolf, B., Schlothauer, T., Peters, S. J., Maier, C. C., Ji, C., Wensel, D. L., et al. (2025) · mAbs · doi:10.1080/19420862.2025.2505092 · Cited by 40 · 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
Sepp, A., Meno‐Tetang, G. M. L., Weber, A. D., Sanderson, A., Schön, O., & Berges, A. (2019) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-019-09640-9 · Cited by 35 · see citing works
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Li, T. R., & Balthasar, J. P. (2018) · Biomolecules · doi:10.3390/biom8040115 · Cited by 30 · see citing works
Liu, A., He, M., Liu, C., Ye, Z., Tan, C. P., Liu, Y., Gong, J., Lei, J., He, Y., Zhu, S., et al. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c08697 · Cited by 22 · see citing works
Fonseca, M. H. G., Furtado, G. P., Bezerra, M. R. L., Pontes, L. Q., & Fernandes, C. F. C. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.07.141 · Cited by 21 · see citing works
Ko, S., Jo, M., Kyung, M., Lee, W., Ko, W. H., Na, J., Chun, Y. S., Ko, B. J., & Jung, S. T. (2025) · Journal of Biological Engineering · doi:10.1186/s13036-025-00506-y · Cited by 19 · see citing works
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Sihombing, M. A. E. M., Safitri, M., Zhou, T. G., Wang, L., McGinty, S., Zhang, H., Yin, Y., Peng, Q., Qiu, J., & Wang, G. (2021) · DNA and Cell Biology · doi:10.1089/dna.2020.5647 · Cited by 19 · see citing works
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Kougentakis, C. M., Shurtleff, M. J., Lieser, R. M., Chen, T., Collins, C. B., Johnson, I. E., Gu, S., Akama, K. T., Doran, K. H., Fung, C. K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.12.632472 · Cited by 17 · see citing works
Liu, S., Li, Y., Li, Z., Wu, S., Harrold, J. M., & Shah, D. K. (2024) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-024-09922-x · Cited by 16 · see citing works
Monteiro, J., Fernandes, A., Tato, D. G., Moreira, E., Ribeiro, R. J. T., Reguengo, H., Gonçalves, J., & Fresco, P. (2025) · Cancers · doi:10.3390/cancers17193262 · Cited by 15 · see citing works
Reusch, J., Andersen, J. T., Rant, U., & Schlothauer, T. (2024) · mAbs · doi:10.1080/19420862.2024.2361585 · Cited by 13 · see citing works
Smulders, L., Altman, R., Briseno, C., Saatchi, A., Wallace, L., AlSebaye, M., Stahelin, R. V., & Nikolaidis, N. (2022) · Biomolecules · doi:10.3390/biom12060856 · Cited by 13 · see citing works
Lv, W., & Champion, J. A. (2020) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2020.102315 · Cited by 11 · see citing works
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Mono-amino acid linkers enable highly potent small molecule-drug conjugates by conditional release
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Pedreño-López, N., Rosen, B. C., Flores, W. J., Gorman, M. J., Voigt, T. B., Ricciardi, M. J., Crosno, K., Weisgrau, K. L., Parks, C. L., Lifson, J. D., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.657424 · Cited by 6 · see citing works
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Deissler, H. L., Lang, G. K., & Lang, G. E. (2018) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-018-4166-7 · Cited by 6 · see citing works
Peng, F., Zhang, H., He, X., & Song, Z. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1136513 · Cited by 5 · see citing works
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Okamoto, M., Furukawa, K., Mizushima, S., & Murai, A. (2025) · Poultry Science · doi:10.1016/j.psj.2025.105946 · Cited by 4 · see citing works
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Esawi, E., Mahmoud, I. S., Abdullah, M. S., Abuarqoub, D. A., Ahram, M. A., & Alshaer, W. (2023) · ACS Omega · doi:10.1021/acsomega.3c01678 · Cited by 4 · see citing works
Qiu, X. I., & Wang, M. Z. (2020) · Drug Metabolism and Disposition · doi:10.1124/dmd.120.000075 · Cited by 4 · see citing works
Sun, Y., Xu, X., Wu, T., Fukuda, T., Isaji, T., Morii, S., Nakano, M., & Gu, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107558 · Cited by 4 · see citing works
Antibodies as drugs—a Keystone Symposia report
Cable, J., Saphire, E. O., Hayday, A., Wiltshire, T. D., Mousa, J. J., Humphreys, D. P., Breij, E. C. W., Bruhns, P., Broketa, M., Furuya, G., et al. (2022) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14915 · Cited by 3 · see citing works
He, M., Li, L., Jiang, G., Tao, Z., Tang, Y., Zhang, Y., Jin, S., Kesse, S., Yang, H., Zhang, S., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.147252 · Cited by 1 · see citing works
Sirina, J., D'Hooghe, L. E., Singhvi-Hanns, L. A., Cole, S. L., Shock, A., Holliday, N. D., & Stoddart, L. A. (2026) · Cellular Immunology · doi:10.1016/j.cellimm.2026.105128
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- Authors
- D’Hooghe, L., Chalmers, A. D., Heywood, S., & Whitley, P.
- Affiliations
- UCB Pharma (United Kingdom) (GB)
- University of Bath (GB)
- Corresponding author
- Heywood, Sam
- Whitley, Paul
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2017-08-17
- Volume
- 12
- Issue
- 8
- Pages
- e0182695
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC5560688
- OpenAlex
- W2745739499
- Cited by
- 42
- References
- 41
- Citations by year
- 2025: 9 · 2024: 5 · 2023: 4 · 2022: 6 · 2021: 9 · 2020: 2 · 2019: 4 · 2018: 3
- FWCI
- 1.89
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- University of Bath
- UCB Pharma
- Topics
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- neonatal Fc receptor, cell surface dynamics, receptor trafficking, endocytosis, IgG recycling, endosomal system, plasma membrane, antibody pharmacokinetics
- MeSH terms
- Cell Membrane, Endocytosis, Humans, Receptors, Fc, Histocompatibility Antigens Class I, Protein Transport, Hep G2 Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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