Proteomic Analyses Identify a Novel Role for EZH2 in the Initiation of Cancer Cell Drug Tolerance
Abstract
Acquisition of drug resistance remains a chief impediment to successful cancer therapy, and we previously described a transient drug-tolerant cancer cell population (DTPs) whose survival is in part dependent on the activities of the histone methyltransferases G9a/EHMT2 and EZH2, the latter being the catalytic component of the polycomb repressive complex 2 (PRC2). Here, we apply multiple proteomic techniques to better understand the role of these histone methyltransferases (HMTs) in the establishment of the DTP state. Proteome-wide comparisons of lysine methylation patterns reveal that DTPs display an increase in methylation on K116 of PRC member Jarid2, an event that helps stabilize and recruit PRC2 to chromatin. We also find that EZH2, in addition to methylating histone H3K27, also can methylate G9a at K185, and that methylated G9a better recruits repressive complexes to chromatin. These complexes are similar to complexes recruited by histone H3 methylated at K9. Finally, a detailed histone post-translational modification (PTM) analysis shows that EZH2, either directly or through its ability to methylate G9a, alters H3K9 methylation in the context of H3 serine 10 phosphorylation, primarily in a cancer cell subpopulation that serves as DTP precursors. We also show that combinations of histone PTMs recruit a different set of complexes to chromatin, shedding light on the temporal mechanisms that contribute to drug tolerance.
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In lung and breast cancer, including EGFR-mutant NSCLC cells treated with EGFR inhibitors, drug-tolerant persisters show an increase in methylation on K116 of PRC member Jarid2, which helps stabilize and recruit PRC2 to chromatin.
“In lung and breast cancer, including EGFR-mutant NSCLC cells treated with EGFR inhibitors, drug-tolerant persisters show an increase in methylation on K116 of PRC member Jarid2, which helps stabilize and recruit PRC2 to chromatin, according to proteome-wide comparisons of lysine methylation patterns [86].”
From Emerging Insights into Targeted Therapy-Tolerant Persister Cells in Cancer (2021) · cites this paper as [86]
EZH2 is emerging as a key player driving the epigenetic changes driving drug tolerance.
“Other master regulators of core developmental programs, such as enhancer of zeste homologue 2 (EZH2), which is the catalytic subunit of the Polycomb repressive complex 2 (PRC2), are emerging as key players driving the epigenetic changes driving drug tolerance.”
From Emerging Insights into Targeted Therapy-Tolerant Persister Cells in Cancer (2021) · cites this paper as [86]
Cites
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262 · see citing works
A Chromatin-Mediated Reversible Drug-Tolerant State in Cancer Cell Subpopulations
Sharma, S. V., Lee, D. Y., Li, B., Quinlan, M. P., Takahashi, F., Maheswaran, S., McDermott, U., Azizian, N., Zou, L., Fischbach, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.02.027 · Cited by 2,770 · see citing works
Self-citationRappsilber, J., Ishihama, Y., & Mann, M. (2002) · Analytical Chemistry · doi:10.1021/ac026117i · Cited by 2,589 · see citing works
Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313 · see citing works
Roesch, A., Fukunaga‐Kalabis, M., Schmidt, E. C., Zabierowski, S. E., Brafford, P. A., Vultur, A., Basu, D., Gimotty, P. A., VOGT, T. M., & Herlyn, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.020 · Cited by 1,162 · see citing works
Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
Rush, A. J., Moritz, A., Lee, K. A., Guo, A., Goss, V. L., Spek, E. J., Zhang, H., Zha, X., Polakiewicz, R. D., & Comb, M. J. (2004) · Nature Biotechnology · doi:10.1038/nbt1046 · Cited by 1,126 · see citing works
Extraction, purification and analysis of histones
Shechter, D., Dormann, H. L., Allis, C. D., & Hake, S. B. (2007) · Nature Protocols · doi:10.1038/nprot.2007.202 · Cited by 1,054 · see citing works
Méndez, J., & Stillman, B. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8602-8612.2000 · Cited by 913 · see citing works
Lewis, P., Elsaesser, S. J., Noh, K., Stadler, S., & Allis, C. (2010) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1008850107 · Cited by 830 · see citing works
Vermeulen, M., Eberl, H. C., Matarese, F., Marks, H., Denissov, S., Butter, F., Lee, K. K., Olsen, J. V., Hyman, A. A., Stunnenberg, H. G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.020 · Cited by 806 · see citing works
Target-Decoy Search Strategy for Mass Spectrometry-Based Proteomics
Elias, J. E., & Gygi, S. P. (2010) · Methods in Molecular Biology · doi:10.1007/978-1-60761-444-9_5 · Cited by 644 · see citing works
Lo, W., Trievel, R. C., Rojas, J. R., Duggan, L. J., Hsu, J.-Y., Allis, C. D., Marmorstein, R., & Berger, S. L. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80257-9 · Cited by 573 · see citing works
Peng, J. C., Valouev, A., Swigut, T., Zhang, J., Zhao, Y., Sidow, A., & Wysocka, J. (2009) · Cell · doi:10.1016/j.cell.2009.12.002 · Cited by 548 · see citing works
A chemical probe selectively inhibits G9a and GLP methyltransferase activity in cells
Vedadi, M., Baršytė-Lovejoy, D., Liu, F., Rival‐Gervier, S., Allali‐Hassani, A., Labrie, V., Wigle, T. J., DiMaggio, P. A., Wasney, G. A., Siarheyeva, A., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.599 · Cited by 547 · see citing works
Knutson, S. K., Kawano, S., Minoshima, Y., Warholic, N. M., Huang, K., Xiao, Y., Kadowaki, T., Uesugi, M., Kuznetsov, G., Kumar, N., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0773 · Cited by 529 · see citing works
Immunoaffinity Enrichment and Mass Spectrometry Analysis of Protein Methylation
Guo, A., Gu, H., Zhou, J., Mulhern, D., Wang, Y., Lee, K. A., Yang, V., Aguiar, M., Kornhauser, J. M., Jia, X., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.027870 · Cited by 473 · see citing works
Chemical derivatization of histones for facilitated analysis by mass spectrometry
Garcia, B. A., Mollah, S., Ueberheide, B. M., Busby, S. A., Muratore‐Schroeder, T. L., Shabanowitz, J., & Hunt, D. F. (2007) · Nature Protocols · doi:10.1038/nprot.2007.106 · Cited by 389 · see citing works
Quantitative Proteomic Analysis of Histone Modifications
Huang, H., Lin, S., Garcia, B. A., & Zhao, Y. (2015) · Chemical Reviews · doi:10.1021/cr500491u · Cited by 383 · see citing works
Epigenetic silencing by the HUSH complex mediates position-effect variegation in human cells
Tchasovnikarova, I. A., Timms, R. T., Matheson, N. J., Wals, K., Antrobus, R., Göttgens, B., Dougan, G., Dawson, M. A., & Lehner, P. J. (2015) · Science · doi:10.1126/science.aaa7227 · Cited by 360 · see citing works
An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells
Vinogradova, M. V., Gehling, V. S., Gustafson, A. E., Arora, S., Tindell, C., WILSON, C. A., Williamson, K. E., Guler, G. D., Gangurde, P., Manieri, W., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2085 · Cited by 358 · see citing works
Self-citationProtein lysine methyltransferase G9a acts on non-histone targets
Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347 · see citing works
Raha, D., Wilson, T. R., Peng, J., Peterson, D., Yue, P., Evangelista, M., Wilson, C., Merchant, M., & Settleman, J. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3456 · Cited by 307 · see citing works
Self-citationJarid2 Methylation via the PRC2 Complex Regulates H3K27me3 Deposition during Cell Differentiation
Sanulli, S., Justin, N., Teissandier, A., Ancelin, K., Portoso, M., Caron, M. J., Michaud, A., Lombard, B., da Rocha, S. T., Offer, J., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.020 · Cited by 285 · see citing works
Guler, G. D., Tindell, C. A., Pitti, R., Wilson, C., Nichols, K., KaiWai Cheung, T., Kim, H.-J., Wongchenko, M., Yan, Y., Haley, B., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.07.002 · Cited by 277 · see citing works
Self-citationIwase, S., Xiang, B., Ghosh, S., Ren, T., Lewis, P. W., Cochrane, J. C., Allis, C. D., Picketts, D. J., Patel, D. J., Li, H., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2062 · Cited by 272 · see citing works
Sampath, S. C., Marazzi, I., Yap, K. L., Sampath, S. C., Krutchinsky, A. N., Mecklenbräuker, I., Viale, A. J., Rudensky, E., Zhou, M., Chait, B. T., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.026 · Cited by 246 · see citing works
Eberl, H. C., Spruijt, C. G., Kelstrup, C. D., Vermeulen, M., & Mann, M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.10.026 · Cited by 189 · see citing works
Maksakova, I. A., Thompson, P. J., Goyal, P., Jones, S. J. M., Singh, P. B., Karimi, M. M., & Lorincz, M. C. (2013) · Epigenetics & Chromatin · doi:10.1186/1756-8935-6-15 · Cited by 185 · see citing works
Svinkina, T., Gu, H., Silva, J. C., Mertins, P., Qiao, J., Fereshetian, S., Jaffe, J. D., Kuhn, E. W., Udeshi, N. D., & Carr, S. A. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.047555 · Cited by 179 · see citing works
Atrx promotes heterochromatin formation at retrotransposons
Sadic, D., Schmidt, K. M., Groh, S., Kondofersky, I., Ellwart, J. W., Fuchs, C., Theis, F. J., & Schotta, G. (2015) · EMBO Reports · doi:10.15252/embr.201439937 · Cited by 174 · see citing works
AKT methylation by SETDB1 promotes AKT kinase activity and oncogenic functions
Guo, J., Dai, X., Laurent, B., Zheng, N., Gan, W., Zhang, J., Guo, A., Yuan, M., Liu, P., Asara, J. M., et al. (2019) · Nature Cell Biology · doi:10.1038/s41556-018-0261-6 · Cited by 153 · see citing works
Zinc Finger Protein Wiz Links G9a/GLP Histone Methyltransferases to the Co-repressor Molecule CtBP
Ueda, J., Tachibana, M., Ikura, T., & Shinkai, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603087200 · Cited by 137 · see citing works
Bakalarski, C. E., Elias, J. E., Villén, J., Haas, W., Gerber, S. A., Everley, P. A., & Gygi, S. P. (2008) · Journal of Proteome Research · doi:10.1021/pr800333e · Cited by 127 · see citing works
Maile, T. M., Izrael-Tomasevic, A., Cheung, T. K., Guler, G. D., Tindell, C., Masselot, A., Liang, J., Zhao, F., Trojer, P., Classon, M., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.046573 · Cited by 118 · see citing works
Self-citationH3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1
Jurkowska, R. Z., Su, Q., Kungulovski, G., Tempel, W., Liu, Y., Bashtrykov, P., Stiefelmaier, J., Jurkowski, T. P., Kudithipudi, S., Weirich, S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02259-9 · Cited by 116 · see citing works
Identifying novel proteins recognizing histone modifications using peptide pull-down assay
Wysocka, J. (2006) · Methods · doi:10.1016/j.ymeth.2006.05.028 · Cited by 88 · see citing works
Trimethylation of histone H3 lysine 4 impairs methylation of histone H3 lysine 9
Binda, O., LeRoy, G., Bua, D. J., Garcia, B. A., Gozani, O., & Richard, S. (2010) · Epigenetics · doi:10.4161/epi.5.8.13278 · Cited by 77 · see citing works
Cdyl, a New Partner of the Inactive X Chromosome and Potential Reader of H3K27me3 and H3K9me2
Escamilla-Del-Arenal, M., da Rocha, S. T., Spruijt, C. G., Masui, O., Renaud, O., Smits, A. H., Margueron, R., Vermeulen, M., & Heard, É. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00866-13 · Cited by 74 · see citing works
Grimes, M. L., Hall, B. S., Foltz, L., Levy, T. M., Rikova, K., Gaiser, J., Cook, W. J. J., Smirnova, E., Wheeler, T. J., Clark, N. R., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aaq1087 · Cited by 64 · see citing works
Gu, H., Ren, J. M., Jia, X., Levy, T. M., Rikova, K., Yang, V., Lee, K. A., Stokes, M. P., & Silva, J. C. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.052266 · Cited by 63 · see citing works
Noh, K., Maze, I. S., Zhao, D. Y., Xiang, B., Wenderski, W., Lewis, P. W., Shen, L., Li, H., & Allis, C. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1411258112 · Cited by 57 · see citing works
Chang, Y., Horton, J. R., Bedford, M. T., Zhang, X., & Cheng, X. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.03.018 · Cited by 52 · see citing works
Chen, C. C. L., Goyal, P., Karimi, M. M., Abildgaard, M. H., Kimurâ, H., & Lorincz, M. C. (2017) · Genome Research · doi:10.1101/gr.224717.117 · Cited by 51 · see citing works
Giri, S., Aggarwal, V., Pontis, J., Shen, Z., Chakraborty, A., Khan, A. A., Mizzen, C. A., Prasanth, K. V., Ait‐Si‐Ali, S., Ha, T., et al. (2015) · eLife · doi:10.7554/elife.06496 · Cited by 50 · see citing works
Erratum: A stress-induced early innate response causes multidrug tolerance in melanoma
Menon, D. R., Das, S. K., Krepler, C., Vultur, A., Rinner, B., Schauer, S., Kashofer, K., Wagner, K., Zhang, G.-Z., Rad, E. B., et al. (2015) · Oncogene · doi:10.1038/onc.2014.432 · Cited by 48 · see citing works
Maier, V., Feeney, C. M., Taylor, J. E., Creech, A. L., Qiao, J., Szántó, A., Das, P. P., Chevrier, N., Cifuentes‐Rojas, C., Orkin, S. H., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.044586 · Cited by 47 · see citing works
Chromodomain protein CDYL is required for transmission/restoration of repressive histone marks
Liu, Y., Liu, S., Yuan, S., Yu, H., Zhang, Y., Yang, X., Xie, G., Chen, Z., Li, W., Xu, B., et al. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx013 · Cited by 47 · see citing works
Global Proteomics Analysis of Protein Lysine Methylation
Cao, X., & Garcia, B. A. (2016) · Current Protocols in Protein Science · doi:10.1002/cpps.16 · Cited by 44 · see citing works
Simon, J. M., Parker, J. S., Liu, F., Rothbart, S. B., Ait‐Si‐Ali, S., Strahl, B. D., Jin, J. J., Davis, I. J., Mosley, A. L., & Pattenden, S. G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.654459 · Cited by 40 · see citing works
Kunowska, N., Rotival, M., Yu, L., Choudhary, J. S., & Dillon, N. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1350 · Cited by 38 · see citing works
Hinohara, K., Wu, H., Vigneau, S., McDonald, T. O., Igarashi, K. J., Yamamoto, K. N., Madsen, T., Fassl, A., Egri, S. B., Papanastasiou, M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.01.012 · Cited by 38 · see citing works
Analysis of the human HP1 interactome reveals novel binding partners
Rosnoblet, C., Vandamme, J., Völkel, P., & Angrand, P. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.08.059 · Cited by 37 · see citing works
Doll, S., Urisman, A., Osés-Prieto, J. A., Arnott, D. P., & Burlingame, A. L. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.063883 · Cited by 37 · see citing works
Self-citationAnania, V. G., Pham, V. C., Huang, X., Masselot, A., Lill, J. R., & Kirkpatrick, D. S. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031062 · Cited by 29 · see citing works
Self-citationWang, C., Cai, W., Li, Y., Deng, H., Bao, X., Girton, J. R., Johansen, J., & Johansen, K. M. (2011) · Journal of Cell Science · doi:10.1242/jcs.092585 · Cited by 26 · see citing works
Giri, S., & Prasanth, S. G. (2015) · Nucleus · doi:10.1080/19491034.2015.1102814 · Cited by 16 · see citing works
Complementary Methods for the Identification of Substrates of Proteolysis
Pham, V. C., Anania, V. G., Phung, Q. T., & Lill, J. R. (2014) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/b978-0-12-417158-9.00014-5 · Cited by 14 · see citing works
Self-citationSbirkov, Y., Kwok, C., Bhamra, A., Thompson, A., Gil, V., Zelent, A., & Petrie, K. R. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071440 · Cited by 11 · see citing works
The Breast Cancer Oncogene EMSY Represses Transcription of Antimetastatic microRNA miR-31
Viré, E. A., Curtis, C. N., Dávalos, V., Git, A., Robson, S. C., Villanueva, A., Vidal, A., Barbieri, I., Aparicio, S. A. J. R., Esteller, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.041 · Cited by 7 · see citing works
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Proteomic characterization of post-translational modifications in drug discovery
Zhai, L., Chen, K., Hao, B., & Tan, M. (2022) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-01017-y · Cited by 50 · see citing works
Thinking Differently about Cancer Treatment Regimens
Settleman, J., Neto, J. M. F., & Bernards, R. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1187 · Cited by 50 · see citing works
Noberini, R., Robusti, G., & Bonaldi, T. (2021) · FEBS Journal · doi:10.1111/febs.15707 · Cited by 49 · see citing works
Elevated Methionine Flux Drives Pyroptosis Evasion in Persister Cancer Cells
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Casciello, F., Kelly, G., Ramarao-Milne, P., Kamal, N., Stewart, T. A., Mukhopadhyay, P., Kazakoff, S. H., Miranda, M. S., Kim, D., Davis, F. M., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-2218 · Cited by 26 · see citing works
Song, X.-H., Yang, L., Zheng, X., Zhu, Q., Liao, X.-L., Liu, K., Zhang, W., Peng, Q., Zhu, Y., Zhao, L.-Y., et al. (2023) · MedComm · doi:10.1002/mco2.342 · Cited by 26 · see citing works
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Kuchaříková, H., Dobrovolná, P., Lochmanová, G., & Zdráhal, Z. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100114 · Cited by 21 · see citing works
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Self-citationThe epigenome and the many facets of cancer drug tolerance
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Thiruvalluvan, M., Billet, S., Liu, Z., Lownik, J. C., Waissengrin, B., Kim, H., Villamejor, A. L., Milshteyn, L., Li, X., Gayhart, M. G., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101237 · Cited by 9 · see citing works
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- Authors
- Pham, V., Pitti, R., Tindell, C. A., Cheung, T. K., Masselot, A., Stephan, J.-P., Guler, G. D., Wilson, C., Lill, J., Arnott, D., & Classon, M.
- Affiliations
- Genentech (US)
- Corresponding author
- Arnott, David
- Classon, Marie
- ORCID
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2020-03-11
- Volume
- 19
- Issue
- 4
- Pages
- 1533-1547
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W3010902400
- Cited by
- 26
- References
- 59
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 1 · 2023: 6 · 2022: 5 · 2021: 7
- FWCI
- 1.46
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Health Sciences › Medicine › Oncology › Cancer Cells and Metastasis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- EZH2, drug tolerance, histone methyltransferase, polycomb repressive complex 2, JARID2, H3K27 methylation, H3K9 methylation, H3S10 phosphorylation, histone modifications, lysine methylation, chemoresistance
- MeSH terms
- Enhancer of Zeste Homolog 2 Protein, Drug Tolerance, Histones, Methylation, Neoplasms, Proteomics, Polycomb Repressive Complex 2
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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