Rubicon: LC 3‐associated phagocytosis and beyond
Open accessAbstract
Rubicon (Rubcn) was initially identified as a component of the Class III PI3K complex and a negative regulator of canonical autophagy and endosomal trafficking. However, Rubicon has attracted the most notoriety because of its critical role in LC3-associated phagocytosis (LAP), a form of noncanonical autophagy that utilizes some components of the autophagy machinery to process extracellular cargo. Additionally, Rubicon has been identified as a key modulator of the inflammatory response and viral replication. In this review, we discuss the known functions of Rubicon in LAP and other signaling pathways and examine the disease pathologies associated with Rubicon dysfunction in animal models and humans.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Rubicon appears to function in balancing classical autophagy and LAP, by committing a cell to LAP while inhibiting classical autophagy.
“Thus, Rubicon appears to function in balancing classical autophagy and LAP, by committing a cell to LAP while inhibiting classical autophagy (Wong et al., 2018).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Wong et al., 2018
Rubicon-deficient macrophages undergo normal levels of phagocytic uptake yet fail to recruit LC3B-II to phagosomes.
“Rubicon-deficient macrophages undergo normal levels of phagocytic uptake yet fail to recruit LC3B-II to phagosomes (Kim et al., 2013; Martinez et al., 2015; Wong et al., 2018).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Wong et al., 2018
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
3 retracted
Martinez, J., Malireddi, R. K. S., Lu, Q., Cunha, L. D., Pelletier, S., Gingras, S., Orchard, R., Guan, J.-L., Tan, H., Peng, J., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3192 · Cited by 758 · see citing works
Self-citationRetractedMartinez, J., Almendinger, J., Oberst, A., Ness, R., Dillon, C. P., Fitzgerald, P., Hengartner, M. O., & Green, D. R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1113421108 · Cited by 655 · see citing works
Self-citationRetractedMartinez, J., Cunha, L. D., Park, S., Yang, M., Lu, Q., Orchard, R., Li, Q.-Z., Yan, M., Janke, L., Guy, C., et al. (2016) · Nature · doi:10.1038/nature17950 · Cited by 381 · see citing works
Self-citationRetractedAutophagy and Viruses: Adversaries or Allies?
Dong, X., & Levine, B. (2013) · Journal of Innate Immunity · doi:10.1159/000346388 · Cited by 4,441 · see citing works
Induction of autophagy and inhibition of tumorigenesis by beclin 1
Liang, X. H., Jackson, S., Seaman, M., Brown, K., Kempkes, B., Hibshoosh, H., & Levine, B. (1999) · Nature · doi:10.1038/45257 · Cited by 3,347 · see citing works
Autophagy in immunity and inflammation
Levine, B., Mizushima, N., & Virgin, H. W. (2011) · Nature · doi:10.1038/nature09782 · Cited by 3,289 · see citing works
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Lazarou, M., Sliter, D. A., Kane, L. A., Sarraf, S. A., Wang, C., Burman, J. L., Sideris, D. P., Fogel, A. I., & Youle, R. J. (2015) · Nature · doi:10.1038/nature14893 · Cited by 2,774 · see citing works
Rioux, J. D., Xavier, R. J., Taylor, K. D., Silverberg, M. S., Goyette, P., Huett, A., Green, T., Kuballa, P., Barmada, M. M., Datta, L. W., et al. (2007) · Nature Genetics · doi:10.1038/ng2032 · Cited by 1,769 · see citing works
Autophagy: molecular machinery for self-eating
Yorimitsu, T., & Klionsky, D. J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401765 · Cited by 1,540 · see citing works
Matsunaga, K., Saitoh, T., Tabata, K., Omori, H., Satoh, T., Kurotori, N., Maejima, I., Shirahama-Noda, K., Ichimura, T., Isobe, T., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1846 · Cited by 1,235 · see citing works
Beclin 1 Forms Two Distinct Phosphatidylinositol 3-Kinase Complexes with Mammalian Atg14 and UVRAG
Itakura, E., Kishi, C., Inoue, K., & Mizushima, N. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-01-0080 · Cited by 1,176 · see citing works
Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
Liang, C., Feng, P., Ku, B., Dotan, I., Canaani, D., Oh, B., & Jung, J. U. (2006) · Nature Cell Biology · doi:10.1038/ncb1426 · Cited by 1,025 · see citing works
Zhong, Y., Wang, Q. J., Li, X., Yan, Y., Backer, J. M., Chait, B. T., Heintz, N., & Yue, Z. (2009) · Nature Cell Biology · doi:10.1038/ncb1854 · Cited by 1,005 · see citing works
Han, J., Zheng, H., Cui, Y., Sun, L., Ye, D., Hu, Z. Q., Xu, J., Cai, Z., Huang, W., Zhao, G., et al. (2009) · Nature Genetics · doi:10.1038/ng.472 · Cited by 938 · see citing works
Liang, C., Lee, J.-S., Inn, K.-S., Gack, M. U., Li, Q., Roberts, E. A., Vergne, I., Deretic, V., Feng, P., Akazawa, C., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1740 · Cited by 792 · see citing works
Gene-microbiota interactions contribute to the pathogenesis of inflammatory bowel disease
Chu, H., Khosravi, A., Kusumawardhani, I. P., Kwon, A. H. K., Vasconcelos, A. C., Cunha, L. D., Mayer, A. E., Shen, Y., Wu, W.-L., Kambal, A., et al. (2016) · Science · doi:10.1126/science.aad9948 · Cited by 647 · see citing works
Type I Interferon in the Pathogenesis of Lupus
Crow, M. K. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1002795 · Cited by 565 · see citing works
Activation of antibacterial autophagy by NADPH oxidases
Huang, J., Canadien, V., Lam, G. Y., Steinberg, B. E., Dinauer, M. C., Magalhaes, M. A. O., Glogauer, M., Grinstein, S., & Brumell, J. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811045106 · Cited by 556 · see citing works
Regulation of lipid stores and metabolism by lipophagy
Liu, K., & Czaja, M. J. (2013) · Cell Death & Differentiation · doi:10.1038/cdd.2012.63 · Cited by 542 · see citing works
Aggrephagy: Selective Disposal of Protein Aggregates by Macroautophagy
Lamark, T., & Johansen, T. (2012) · International Journal of Cell Biology · doi:10.1155/2012/736905 · Cited by 490 · see citing works
Florey, O., Kim, S. E., Sandoval, C. P., Haynes, C. M., & Overholtzer, M. (2011) · Nature Cell Biology · doi:10.1038/ncb2363 · Cited by 459 · see citing works
Regulation of membrane traffic by phosphoinositide 3-kinases
Lindmo, K., & Stenmark, H. (2006) · Journal of Cell Science · doi:10.1242/jcs.02855 · Cited by 425 · see citing works
The adaptor protein CARD9 is required for innate immune responses to intracellular pathogens
Hsu, Y.-M. S., Zhang, Y., You, Y., Wang, D., Li, H., Duramad, O., Qin, F. X.-F., Dong, C., & Lin, X. (2006) · Nature Immunology · doi:10.1038/ni1426 · Cited by 420 · see citing works
Tanaka, S., Hikita, H., Tatsumi, T., Sakamori, R., Nozaki, Y., Sakane, S., Shiode, Y., Nakabori, T., Saito, Y., Hiramatsu, N., et al. (2016) · Hepatology · doi:10.1002/hep.28820 · Cited by 376 · see citing works
Liang, Q., Seo, G. J., Choi, Y. J., Kwak, M., Ge, J., Rodgers, M. A., Shi, M., Leslie, B. J., Hopfner, K., Ha, T., et al. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.01.009 · Cited by 351 · see citing works
Genetic variants at CD28, PRDM1 and CD2/CD58 are associated with rheumatoid arthritis risk
Raychaudhuri, S., Thomson, B. P., Remmers, E. F., Eyre, S., Hinks, A., Guiducci, C., Catanese, J. J., ., G. X., Stahl, E. A., Chen, R., et al. (2009) · Nature Genetics · doi:10.1038/ng.479 · Cited by 351 · see citing works
Henault, J., Martinez, J., Riggs, J. M., Tian, J., Mehta, P., Clarke, L., Sasai, M., Latz, E., Brinkmann, M. M., Iwasaki, A., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.09.014 · Cited by 348 · see citing works
Self-citationp62 and NDP52 Proteins Target Intracytosolic Shigella and Listeria to Different Autophagy Pathways
Mostowy, S., Sancho-Shimizu, V., Hamon, M. A., Simeone, R., Brosch, R., Johansen, T., & Cossart, P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.223610 · Cited by 294 · see citing works
Jayadev, S., & Bird, T. D. (2013) · Genetics in Medicine · doi:10.1038/gim.2013.28 · Cited by 273 · see citing works
mTORC1 Phosphorylates UVRAG to Negatively Regulate Autophagosome and Endosome Maturation
Kim, Y. M., Jung, C. H., Seo, M., Kim, E. K., Park, J.-M., Bae, S. S., & Kim, D. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.013 · Cited by 272 · see citing works
Rubicon controls endosome maturation as a Rab7 effector
Sun, Q., Westphal, W., Wong, K. N., Tan, I., & Zhong, Q. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010554107 · Cited by 251 · see citing works
The LC3 interactome at a glance
Wild, P. S., McEwan, D. G., & Đikić, I. (2013) · Journal of Cell Science · doi:10.1242/jcs.140426 · Cited by 250 · see citing works
Kuma, A., & Mizushima, N. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.002 · Cited by 237 · see citing works
Regulation of autophagy by phosphatidylinositol 3‐phosphate
Burman, C., & Ktistakis, N. T. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.011 · Cited by 234 · see citing works
Autophagy Limits Listeria monocytogenes Intracellular Growth in the Early Phase of Primary Infection
Py, B., Lipinski, M. M., & Yuan, J. (2007) · Autophagy · doi:10.4161/auto.3618 · Cited by 227 · see citing works
Differential Use of CARD9 by Dectin-1 in Macrophages and Dendritic Cells
Goodridge, H. S., Shimada, T., Wolf, A. J., Hsu, Y.-M. S., Becker, C. A., Lin, X., & Underhill, D. M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.182.2.1146 · Cited by 202 · see citing works
Gong, L., Cullinane, M., Treerat, P., Ramm, G., Prescott, M., Adler, B., Boyce, J. D., & Devenish, R. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017852 · Cited by 175 · see citing works
Yang, C., Lee, J., Rodgers, M. A., Min, C., Lee, J., Kim, H. J., Lee, K.-H., Kim, C., Oh, B., Zandi, E., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.018 · Cited by 163 · see citing works
Sun, Q., Zhang, J., Fan, W., Wong, K. N., Ding, X., Chen, S., & Zhong, Q. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126425 · Cited by 153 · see citing works
Metabolic Connections during Apoptotic Cell Engulfment
Han, C. Z., & Ravichandran, K. S. (2011) · Cell · doi:10.1016/j.cell.2011.12.006 · Cited by 144 · see citing works
Joachim, J., Jefferies, H. B. J., Razi, M., Frith, D., Snijders, A. P., Chakravarty, P., Judith, D., & Tooze, S. A. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.11.018 · Cited by 141 · see citing works
Toll-like receptor signaling in the lysosomal pathways
Sanjuan, M. A., Milasta, S., & Green, D. R. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00732.x · Cited by 137 · see citing works
The PI3K, Metabolic, and Autophagy Networks: Interactive Partners in Cellular Health and Disease
Shanware, N. P., Bray, K., & Abraham, R. T. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134717 · Cited by 130 · see citing works
Rab cascades and tethering factors in the endomembrane system
Markgraf, D. F., Peplowska, K., & Ungermann, C. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.01.090 · Cited by 120 · see citing works
Wang, L., Tian, Y., & Ou, J. J. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004764 · Cited by 119 · see citing works
Macrophage Autophagy in Immunity to Cryptococcus neoformans and Candida albicans
Nicola, A. M., Albuquerque, P., Martinez, L. R., Dal-Rosso, R. A., Saylor, C., Jesus, M. D., Nosanchuk, J. D., & Casadevall, A. (2012) · Infection and Immunity · doi:10.1128/iai.00358-12 · Cited by 114 · see citing works
The Autophagy Regulator Rubicon Is a Feedback Inhibitor of CARD9-Mediated Host Innate Immunity
Yang, C., Rodgers, M. A., Min, C.-K., Lee, J., Kingeter, L. M., Lee, J., Jong, A., Kramnik, I., Lin, X., & Jung, J. U. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.01.019 · Cited by 104 · see citing works
Liang, Q., Chang, B., Brulois, K., Castro, K., Min, C., Rodgers, M. A., Shi, M., Ge, J., Feng, P., Oh, B., et al. (2013) · Journal of Virology · doi:10.1128/jvi.01898-13 · Cited by 84 · see citing works
Herpes simplex virus interferes with amyloid precursor protein processing
Shipley, S. J., Parkin, E. T., Itzhaki, R. F., & Dobson, C. B. (2005) · BMC Microbiology · doi:10.1186/1471-2180-5-48 · Cited by 68 · see citing works
Roles of autophagy in HIV infection
Dinkins, C., Pilli, M., & Kehrl, J. H. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.88 · Cited by 67 · see citing works
Okazaki, N. (2003) · DNA Research · doi:10.1093/dnares/10.1.35 · Cited by 63 · see citing works
Xenophagy in herpes simplex virus replication and pathogenesis
Alexander, D., & Leib, D. A. (2008) · Autophagy · doi:10.4161/auto.5222 · Cited by 57 · see citing works
Assoum, M., Salih, M. A. M., Drouot, N., Hmida, D., Lagier‐Tourenne, C., AlDrees, A., Elmalik, S. A., Ahmed, T. S., Seidahmed, M. Z., Kabiraj, M. M., et al. (2010) · Brain · doi:10.1093/brain/awq181 · Cited by 54 · see citing works
Endosomal membrane traffic: convergence point targeted by Mycobacterium tuberculosis and HIV
Deretic, V. P., Vergne, I., Chua, J., Master, S. S., Singh, S., Fazio, J. A., & Kyei, G. B. (2004) · Cellular Microbiology · doi:10.1111/j.1462-5822.2004.00449.x · Cited by 54 · see citing works
Ueyama, T., Nakakita, J., Nakamura, T., Kobayashi, T., Kobayashi, T., Son, J., Sakuma, M., Sakaguchi, H., Leto, T. L., & Saito, N. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237289 · Cited by 44 · see citing works
Inducible Rubicon facilitates viral replication by antagonizing interferon production
Wan, Y., Cao, W., Han, T., Ren, S., Feng, J. J., Chen, T.-L., Wang, J., Broering, R., Lu, M., & Zhu, Y. (2017) · Cellular and Molecular Immunology · doi:10.1038/cmi.2017.1 · Cited by 44 · see citing works
Essential role for UVRAG in autophagy and maintenance of cardiac function
Song, Z., An, L. K., Ye, Y., Wu, J., Zou, Y., He, L., & Zhu, H. (2013) · Cardiovascular Research · doi:10.1093/cvr/cvt223 · Cited by 37 · see citing works
Zi, Z., Song, Z., Zhang, S., Ye, Y., Li, C., Xu, M., Zou, Y., He, L., & Zhu, H. (2014) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000000188 · Cited by 36 · see citing works
Kim, J., Kim, T., Lee, H., Nikapitiya, C., Uddin, M. B., Park, M.-E., Pathinayake, P. S., Lee, E. S., Chathuranga, K., Herath, T. U. B., et al. (2017) · Journal of Virology · doi:10.1128/jvi.00248-17 · Cited by 34 · see citing works
The Salih Ataxia Mutation Impairs Rubicon Endosomal Localization
Assoum, M., Salih, M. A. M., Drouot, N., Hnia, K., Martelli, A., & Koenig, M. (2013) · The Cerebellum · doi:10.1007/s12311-013-0489-4 · Cited by 29 · see citing works
Perspectives on HCV: Current Therapeutic Regimens and Drug–Drug Interactions
Chan, J., & Chung, R. T. (2017) · Clinical Pharmacology in Drug Development · doi:10.1002/cpdd.338 · Cited by 11 · see citing works
Chapter 22 Streptococcus‐, Shigella‐, and Listeria‐Induced Autophagy
Ogawa, M., Nakagawa, I., Yoshikawa, Y., Hain, T., Chakraborty, T., & Sasakawa, C. (2009) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(08)03622-7 · Cited by 9 · see citing works
Flagged first, then by citations
Research works printed but not linked: 4
- [7]Matsunaga K, Saitoh T, Tabata K, Omori H, Satoh T, Kurotori N, Maejima I, Shirahama-Noda K, Ichimura T, Isobe T, Akira S, Noda T & Yoshimori T (2009) Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages, Nature cell biology. 11, 385– 96. 19270696
- [23]Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, Heintz N & Yue Z (2009) Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex, Nature cell biology. 11, 468– 76. 19270693 PMC2664389
- [51]Bird TD (1993) Hereditary Ataxia Overview in GeneReviews(R) (Pagon RA, Adam MP, Ardinger HH, Wallace SE, Amemiya A, Bean LJH, Bird TD, Ledbetter N, Mefford HC, Smith RJH & Stephens K, eds), Seattle (WA). 20301317
- [60]Martinez JM, R. K.; Lu Q; Cunha LD; Pelletier S; Gingras S; Orchard R; Guan JL; Tan H; Peng J; Kanneganti TD; Virgin HW, and Green DR (2015) Molecular characterization of LC3-associated phagocytosis (LAP) reveals distinct roles for Rubicon, NOX2, and autophagy proteins., Nature cell biology. PMC4612372 26098576
Cited by
Sorted by citations
The cell biology of the retinal pigment epithelium
Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422 · see citing works
Microglial autophagy–associated phagocytosis is essential for recovery from neuroinflammation
Berglund, R., Guerreiro-Cacais, A. O., Adzemovic, M. Z., Zeitelhofer, M., Lund, H., Ewing, E., Ruhrmann, S., Nutma, E., Parsa, R., Thessen-Hedreul, M., et al. (2020) · Science Immunology · doi:10.1126/sciimmunol.abb5077 · Cited by 149 · see citing works
Lc3-associated phagocytosis—The highway to hell for phagocytosed microbes
Herb, M., Gluschko, A., & Schramm, M. (2020) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2019.04.016 · Cited by 103 · see citing works
Age-dependent loss of adipose Rubicon promotes metabolic disorders via excess autophagy
Yamamuro, T., Kawabata, T., Fukuhara, A., Saita, S., Nakamura, S., Takeshita, H., Fujiwara, M., Enokidani, Y., Yoshida, G., Tabata, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17985-w · Cited by 97 · see citing works
Asare, P. F., Roscioli, E., Hurtado, P. R., Tran, H. B., Mah, C. Y., & Hodge, S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01298 · Cited by 50 · see citing works
VPS34 in Autophagy, Cancer and Cancer Therapy
Bartolini, E., Janji, B., & Gao, R. (2026) · doi:10.20944/preprints202603.0323.v1 · Cited by 1 · see citing works
- Authors
- Wong, S., Sil, P., & Martinez, J.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- National Institutes of Health (US)
- Corresponding author
- Wong, Sing‐Wai
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2017-12-29
- Volume
- 285
- Issue
- 8
- Pages
- 1379-1388
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- PMC
- PMC6779045
- OpenAlex
- W2773257251
- Cited by
- 101
- References
- 64
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 10 · 2023: 12 · 2022: 13 · 2021: 14 · 2020: 16 · 2019: 11 · 2018: 5
- FWCI
- 1.16
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- public-domain
- onlinelibrary.wiley.com/termsAndConditions#vor (vor)
- Locations
- FEBS Journal (publishedVersion, public-domain)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (Z99-ES999999)
- National Institute of Environmental Health Sciences (ZIAES103286)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Rubicon, LC3-associated phagocytosis, non-canonical autophagy, class III PI3K, autophagy regulation, endosomal trafficking, inflammation, viral replication, disease pathology
- MeSH terms
- Autophagy-Related Proteins, Animals, Autophagy, Humans, Microtubule-Associated Proteins, Models, Biological, Phagocytosis, Phagosomes, Endosomes, Signal Transduction, Intracellular Signaling Peptides and Proteins
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 ›
Are you an author, or do you see a problem with this page? Request a review
