The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Brusatol enhances the efficacy of chemotherapy by inhibiting the Nrf2-mediated defense mechanism
Open accessAbstract
The major obstacle in cancer treatment is the resistance of cancer cells to therapies. Nrf2 is a transcription factor that regulates a cellular defense response and is ubiquitously expressed at low basal levels in normal tissues due to Keap1-dependent ubiquitination and proteasomal degradation. Recently, Nrf2 has emerged as an important contributor to chemoresistance. High constitutive expression of Nrf2 was found in many types of cancers, creating an environment conducive for cancer cell survival. Here, we report the identification of brusatol as a unique inhibitor of the Nrf2 pathway that sensitizes a broad spectrum of cancer cells and A549 xenografts to cisplatin and other chemotherapeutic drugs. Mechanistically, brusatol selectively reduces the protein level of Nrf2 through enhanced ubiquitination and degradation of Nrf2. Consequently, expression of Nrf2-downstream genes is reduced and the Nrf2-dependent protective response is suppressed. In A549 xenografts, brusatol and cisplatin cotreatment induced apoptosis, reduced cell proliferation, and inhibited tumor growth more substantially when compared with cisplatin treatment alone. Additionally, A549-K xenografts, in which Nrf2 is expressed at very low levels due to ectopic expression of Keap1, do not respond to brusatol treatment, demonstrating that brusatol-mediated sensitization to cisplatin is Nrf2 dependent. Moreover, a decrease in drug detoxification and impairment in drug removal may be the primary mechanisms by which brusatol enhances the efficacy of chemotherapeutic drugs. Taken together, these results clearly demonstrate the effectiveness of using brusatol to combat chemoresistance and suggest that brusatol can be developed into an adjuvant chemotherapeutic drug.
Overview
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
Verification
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?
In the citing paper
“brusatol has been shown to enhance the efficacy of chemotherapy by inhibiting Nrf2 [229,230].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [229]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway
Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630
Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224
Dinkova-Kostova, A. T., Holtzclaw, W. D., Cole, R. N., Itoh, K., Wakabayashi, N., Katoh, Y., Yamamoto, M., & Talalay, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172398899 · Cited by 1,947
Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex
Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,284
Self-citationMechanistic Studies of the Nrf2-Keap1 Signaling Pathway
Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,105
Self-citationRamos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102
Dysfunctional KEAP1–NRF2 Interaction in Non-Small-Cell Lung Cancer
Singh, A., Misra, V., Thimmulappa, R. K., Lee, H., Ames, S., Hoque, M. O., Herman, J. G., Baylin, S. B., Sidransky, D., Gabrielson, E., et al. (2006) · PLoS Medicine · doi:10.1371/journal.pmed.0030420 · Cited by 1,060
Cullinan, S. B., Gordan, J. D., Jin, J., Harper, J. W., & Diehl, J. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8477-8486.2004 · Cited by 986
NRF2 and KEAP1 mutations: permanent activation of an adaptive response in cancer
Hayes, J. D., & McMahon, M. J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.12.008 · Cited by 870
Nrf2 enhances resistance of cancer cells to chemotherapeutic drugs, the dark side of Nrf2
Wang, X.-J., Sun, Z., Villeneuve, N. F., Zhang, S., Zhao, F., Li, Y., Chen, W., Yi, X., Zheng, W., Wondrak, G. T., et al. (2008) · Carcinogenesis · doi:10.1093/carcin/bgn095 · Cited by 839
Self-citation
Cited by
Sorted by citations
Items 601–681 of 681
Targeting Nrf2 in inflammation and cancer
Cowan, J. (2014) · UEA Digital Repository (University of East Anglia) · Cited by 1
Gounder, S. S., Kannan, S., Devadoss, D., Miller, C. J., Whitehead, K. S., Odelberg, S. J., Firpo, M. A., Paine, R., Hoidal, J. R., Abel, E. D., et al. (2013) · PLoS ONE · doi:10.1371/annotation/684807c2-1777-4008-9eda-c6036553b082 · Cited by 1
Dean, Z. (2015) · UA Campus Repository (The University of Arizona)
Resistance to chemotherapy in non-small cell lung cancer with Keap1 gene mutation
Yamadori, T., Ishii, Y., Homma, S., Kurishima, K., Minami, Y., Noguchi, M., & Hizawa, N. (2012) · International Cancer Conference Journal · doi:10.1007/s13691-011-0011-0
The Role of the Nrf2-Keap1 Pathway in Autophagy and How it Contributes to Arsenic Carcinogenicity
Lau, A. (2012) · UA Campus Repository (The University of Arizona)
Self-citationAngefertigt mit Genehmigung der Mathematisch-Naturwissenschaftlichen Fakultät der
Bonn, R. F.-W.-U. (2012)
REGULATION OF THE OXIDATIVE STRESS RESPONSE BY ARID1A
Kwan, S. Y. (2015) · Digital Commons-TMC (Texas Medical Center)
The role of mitochondria in innate immunity and inflammation
Widdrington, J. D. (2016)
Molecular and Chemical Modulation of NRF2 for Disease Intervention
Harder, B. G. (2017) · UA Campus Repository (The University of Arizona)
Sapiro, J. M. (2017) · UA Campus Repository (The University of Arizona)
Xu, Y., Xu, M., Zhang, L., Zhu, Z., Guo, S., Su, S., Guo, J., Che, C., Lin, Z., Zhao, M., et al. (2019) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2019.03.052
Increasing Chemosensitivity in Colorectal Cancer
Agro, L. A. (2019) · TSpace (University of Toronto)
FAIR and bias-free network modules for mechanism-based disease redefinitions
Hassan, A. (2021) · Research Publications (Maastricht University) · doi:10.26481/dis.20210707ah
Targeting Oxidative Stress Specific NRF2 In Pancreatic Cancer Stem Cells
Sagar, S., Rajesh, C., & Radhakrishnan, P. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-1247-3_95-1
Implications of NRF2 in Cancer Progression and Therapeutics
Agrawal, M., & Agrawal, S. K. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-1247-3_79-1
Erratum to: The 2014 Beatson international cancer conference: powering the cancer machine
Kamphorst, J. J., & Murphy, D. J. (2014) · Cancer & Metabolism · doi:10.1186/s40170-014-0127-8
Target Selection vs. Response Selection
McPeek, R. M. (2015) · Encyclopedia of Computational Neuroscience · doi:10.1007/978-1-4614-6675-8_320
Target Selection vs. Response Selection
McPeek, R. M. (2022) · Encyclopedia of Computational Neuroscience · doi:10.1007/978-1-0716-1006-0_320
Rewiring of Drug Metabolism and Its Cross‐talk with Metabolic Reprogramming in Cancer
Majumder, S., & Manna, S. K. (2022) · Wiley eBooks · doi:10.1002/9781119851042.ch27
Implications of NRF2 in Cancer Progression and Therapeutics
Agrawal, M., & Agrawal, S. K. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-5422-0_79
Targeting Oxidative Stress Specific NRF2 in Pancreatic Cancer Stem Cells
Sagar, S., Rajesh, C., & Radhakrishnan, P. (2022) · Handbook of Oxidative Stress in Cancer: Therapeutic Aspects · doi:10.1007/978-981-16-5422-0_95
Vyas, A. R., Harbison, R. A., Faden, D. L., Kubik, M. W., Palmer, D., Zhang, Q. H., Osmanbeyoglu, H. U., Kiselyov, K. I., Méndez, E., & Duvvuri, U. (2023) · doi:10.1158/1078-0432.c.6530409
Vyas, A. R., Harbison, R. A., Faden, D. L., Kubik, M. W., Palmer, D., Zhang, Q. H., Osmanbeyoglu, H. U., Kiselyov, K. I., Méndez, E., & Duvvuri, U. (2023) · doi:10.1158/1078-0432.c.6530409.v1
Data from The Impact of miRNA-Based Molecular Diagnostics and Treatment of NRF2-Stabilized Tumors
Yamamoto, S., Inoue, J., Kawano, T., Kozaki, K., Omura, K., & Inazawa, J. (2023) · doi:10.1158/1541-7786.c.6539530
Wu, Z., Zhu, Z., Cao, J., Wu, W., Deng, C., Xie, Q., & Hu, S. (2023) · Medicine · doi:10.1097/md.0000000000036771
NRF2'nin İkili Doğası: Kanser Gelişiminde Koruyucu ve Teşvik Edici Rolü
Kaleler, İ., & Yaylım, İ. (2024) · Haliç Üniversitesi Fen Bilimleri Dergisi · doi:10.46373/hafebid.1442953
Xia, R. M., Tang, H., Shen, J., Xu, S., Liang, Y., Zhang, Y., Gong, X., Yue, M., Zhang, D., Tao, C., et al. (2021) · Figshare · doi:10.6084/m9.figshare.14168644
Self-citationGong, M., Li, Y., Ye, X., Zhang, L., Wang, Z., Xu, X., Shen, Y., & Zheng, C. (2020) · Figshare · doi:10.6084/m9.figshare.12552329
Liao, H., Zhu, D., Bai, M., Chen, H., Yan, S., Yu, J., Zhu, H., Zheng, W., & Fan, G. (2020) · Figshare · doi:10.6084/m9.figshare.13059035
Dewangan, N. R., Agrawal, P. P., Sahu, P., Sahu, D., Yadav, M., Gupta, P., & Ahirwar, B. (2024) · The Natural Products Journal · doi:10.2174/0122103155293700240408043538 · Cited by 1
Comparative pharmacognostic exploration of medicinal plants and their adulterants
Patil-Patankar, V. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15383-9.00031-7
Fan, Z., Tian, Y., Liu, B., Ning, M., Wei, J. J., Zeng, L., Zhao, Y., & Zhang, M. (2024) · Research Square · doi:10.21203/rs.3.rs-4856576/v1
A diffusion model conditioned on compound bioactivity profiles for predicting high-content imagesPreprint
Cook, S., Chyba, J., Gresoro, L., Quackenbush, D., Qiu, M., Kutchukian, P. S., Martin, É., Skewes-Cox, P., & Godinez, W. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.10.616543
Mateos, R. N., Winardi, W., Chiba, K., Okada, A., Suzuki, A., Mitsuishi, Y., & Shiraishi, Y. (2024) · npj Systems Biology and Applications · doi:10.1038/s41540-024-00475-w
Sonakar, A. K., Kumar, A. V., Kalita, B. C., Garg, V. K., Buttar, H. S., Kashyap, D., & Wilson, D. W. (2024) · Advances in biochemistry in health and disease · doi:10.1007/978-3-031-75686-3_15
Exploring the Anti-Tumor Effects of Brusatol in Aggressive B-Cell LymphomasPreprint
Szmyra, M., Haingartner, S., Jantscher, S., Bernhart, E. M., Kovács-Hajdu, P., Bošková, V., Krall, N., Zupo, A., Pircher, T., Pansy, K., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.16.649058
Amjad, E., & Sokouti, B. (2025) · Egyptian Journal of Medical Human Genetics · doi:10.1186/s43042-025-00742-3
Wang, W., Deng, K., Chen, W., Du, L., & Chen, J. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112153
Rearrangement of signaling pathways and adaptation of tumor cells to hypoxia
Andreeva, O. E., Mikhaevich, E. I., & Ma, K. (2025) · Advances in molecular oncology · doi:10.17650/2313-805x-2025-12-4-8-23
Regulatory impact of phytochemicals on metabolic diseases by targeting Nrf2-ARE signaling mechanism
Gambhir, L., Pokhriyal, A., Kapoor, N., & Kandwal, P. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-31698-2.00012-6
Role of Brusatol in Preventing Gastrointestinal Cancer: Recent Trends and Future Perspectives
Thakral, F., Sehgal, R., Singh, G., Kaur, G., Haque, S., Chauhan, R., Gupta, M., & Tuli, H. S. (2026) · Archiv der Pharmazie · doi:10.1002/ardp.70191
Pharmacokinetics and nephrotoxicity of cisplatin modulated by combination therapy with brusatol
Guo, N., Zhang, Y., Yuan, G., Zhang, X., Zhang, W., & Wen, Q. I. N. G. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1708101
Wu, Y., Feng, H., Wang, Y., Tian, L., Han, C., Yan, L., Song, J., & Shen, D. (2026) · Phytotherapy Research · doi:10.1002/ptr.70243
Deng, J., Xun, Z., Chen, H., Cen, Y., Luo, Y., Liu, W., Chen, W., Chen, J., Ye, J., Gao, X., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.20.706928
Brusatol inhibits metastasis of triple-negative breast cancer through metabolic reprogramming
Yu, X., Diao, X., Fan, X., Wu, C., Wang, S., Liu, M., Cheung, E. C. W., & Chen, L. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1708878
Zhong, P., Zhuge, S., Tu, Y., Li, J., Xu, Y., Meffo, T. M., Ke, Y., Liu, J., Xu, L., Gao, F., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111388
Self-citationPoisson, C. (2013) · theses.fr (ABES) · doi:10.70675/11ddda7ezed4cz4c93z9a10z6bd0bb5ec1a3
de Bourayne, M. (2015) · theses.fr (ABES) · doi:10.70675/fed3e8c8z64c2z4e1ez81a9z054e2d240b5f
Camus, M. (2017) · theses.fr (ABES) · doi:10.70675/4def68c4zdc9ez422eza783z692c3f1ea21e
唐, 骏. (2026) · Advances in Clinical Medicine · doi:10.12677/acm.2026.1641340
Jin, X., Yang, S., Pan, D., Jin, B., Zhang, Y., & Yang, C. (2026) · Scientific Reports · doi:10.1038/s41598-026-45960-w
Ciblage thérapeutique de la réponse au stress cellulaire dans l'ostéosarcome
Moukengué, B. (2019) · theses.fr (ABES) · doi:10.70675/26cb2736z4fbdz42d2zabcbzca5db0a782e1
A diffusion model conditioned on compound bioactivity profiles for generating high-content images
Cook, S., Chyba, J., Gresoro, L., Quackenbush, D., Qiu, M., Kutchukian, P. S., Martin, E. J., Skewes-Cox, P., & Godinez, W. J. (2026) · Scientific Reports · doi:10.1038/s41598-026-44976-6
Polyphyllin B induces ferroptosis in triple-negative breast cancer by inactivating NRF2
Deng, P., Zhu, S., Wu, Y., Fang, Z., Zhang, A., 张栋益, 胡孝渠, & Zhou, X. Y. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1803145
Zhu, Y. U. N. L. O. N., Liu, M., Kwok, H. F., & Chen, L. (2026) · Molecular Therapy Oncology · doi:10.1016/j.omton.2026.201225
Kawaguchi, S., Sato, K., Izawa, J., Takayama, N., Hayakawa, H., Suzaki, K., Goyama, S., Kato, C., Sakashita, E., Tominaga, K., et al. (2026) · Cancer Science · doi:10.1111/cas.70423
Rosindol: A fluorogen for the quantitative measurement of reactive oxygen species in living cellsPreprint
Monnone, A., Nicknish, M., Montezco, J. J. J., Sanganoo, C., Aggarwal, N., Luong, A., Schaus, S. E., & Grinstaff, M. W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.04.730197
Xue, D., Li, W., Yu, F., Jiang, Q., Yu, H., Li, X., Qiu, J., & Niu, G. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112770
Pawar, C. S., & Prasad, N. R. (2026) · Drug Development Research · doi:10.1002/ddr.70358
Lipid peroxidation in cancer: a double-edged sword shaping progression and therapy
Allowitz, K. V. (2026) · Medical Oncology · doi:10.1007/s12032-026-03351-1
Ezerioha, C. E., Uahomo, P. O., Chidi-Ezerioha, P. A., Akpan, G. W., & Chukundah, S. (2026) · Frontiers in Pharmacology · doi:10.3389/fphar.2026.1907919
Recent advancements in NRF2-regulated ferroptosis modulation for targeted cancer therapy
Ülker, Ö. C., Capozzi, A., Sari-Goktas, N. N., Sorice, M., Saso, L., & Buttari, B. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12705-x
CHAC1-linked NRF2 protein expression participates in pancreatic islet protection by dextrorphan
Weippert, C., Kirschner, P., Bartosinska, B., Köster, A., Eberhard, D., & Lammert, E. (2026) · iScience · doi:10.1016/j.isci.2026.117474
Tadayonfar, R., Bahrami, M., Sobhani, E., Raisi, A., Dezfoulian, O., Davoodi, F., Kamalpour, M., & Kheradmand, A. (2026) · The FASEB Journal · doi:10.1096/fj.202600831r
Choi, H. Y., Kwon, H., & Hah, Y. (2026) · Antioxidants · doi:10.3390/antiox15101223
Oria, R. S., Umeano, V. A., CHUKWU, V. O., Inyang, H. O., & Usin, S. G. (2026) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-026-02185-y
Ferrer, B., Tinkov, A. A., Santamaria, A., Rocha, J. B., Skalny, A. V., Bowman, A. B., & Aschner, M. (2026) · Neurochemical Research · doi:10.1007/s11064-026-04898-1
Gómez-Galán, M., Gil‐Martínez, J., de Juan, V. G., Bizkarguenaga, M., León-Barberena, J., Navarro‐Corcuera, A., Embade, N., Fernández‐Ramos, D., Lopitz‐Otsoa, F., lu, S., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-10150900/v1
BindingDB Entry 50006254: Non-electrophilic modulators of the canonical Keap1/Nrf2 pathway.
BindingDB (2020) · UC San Diego · doi:10.7270/q20v8gsc
BindingDB Entry 50019686: Stapled Peptides as Direct Inhibitors of Nrf2-sMAF Transcription Factors.
BindingDB (2024) · UC San Diego · doi:10.7270/q2qj7np4
BindingDB Entry 50022224: NRF2 inhibitors: Recent progress, future design and therapeutic potential.
BindingDB (2025) · UC San Diego · doi:10.7270/q27h1q92
Yang, Y., Li, Y., Hao, X., Yan, W., & Ma, X. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1985224
Metadata
- Authors
- Ren, D., Villeneuve, N. F., Jiang, T., Wu, T., Lau, A., Toppin, H. A., & Zhang, D. D.
- Affiliations
- Department of Pharmacology and Toxicology, University of Arizona, Tucson, AZ 85721;
- University of Arizona (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-01-04
- Volume
- 108
- Issue
- 4
- Pages
- 1433-1438
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3029730
- OpenAlex
- W2077950988
- Cited by
- 673
- References
- 47
- Citations by year
- 2026: 41 · 2025: 43 · 2024: 42 · 2023: 48 · 2022: 59 · 2021: 47 · 2020: 65 · 2019: 48 · 2018: 44 · 2017: 52 · 2016: 48 · 2015: 38 · 2014: 36 · 2013: 34 · 2012: 21
- FWCI
- 12.45
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (ES006694)
- National Institute of Environmental Health Sciences (ES-006694, R01ES015010, P30ES006694)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- brusatol, Nrf2, chemoresistance, cisplatin, Keap1, ubiquitination, proteasomal degradation, apoptosis, A549 xenograft, drug detoxification, adjuvant chemotherapy, lung cancer
- MeSH terms
- Animals, Antineoplastic Agents, Antineoplastic Combined Chemotherapy Protocols, Cisplatin, Drug Synergism, Glutathione, HeLa Cells, Humans, Lung Neoplasms, Mice, Nude, Immunoblotting, Molecular Structure, Signal Transduction, Apoptosis, Xenograft Model Antitumor Assays, Quassins, Intracellular Space, Cell Line, Tumor, Cell Proliferation, NF-E2-Related Factor 2, Mice, Ubiquitination
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