Structural analysis of the EGFR/HER3 heterodimer reveals the molecular basis for activating HER3 mutations
Open accessAbstract
Cancer-associated mutations in the catalytically inactive receptor HER3 enhance its ability to activate other members of the human epidermal growth factor receptor family.
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?
HER3 features very low catalytic activity but engages in oncogenic signaling by acting as a scaffold to enable receptor heterodimerization.
“HER3 features very low catalytic activity but engages in oncogenic signaling by acting as a scaffold to enable receptor heterodimerization.8−10”
From Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence (2023) · cites this paper as [10]
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
Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works
PD-1 and PD-L1 Immune Checkpoint Blockade to Treat Breast Cancer
Hartkopf, A. D., Taran, F., Wallwiener, M., Walter, C. B., Krämer, B., Grischke, E., & Brucker, S. Y. (2016) · Breast Care · doi:10.1159/000453569 · Cited by 30,989 · see citing works
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
<i>PHENIX</i> : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716 · see citing works
Canonical dynamics: Equilibrium phase-space distributions
Hoover, W. G. (1985) · Physical Review A · doi:10.1103/physreva.31.1695 · Cited by 23,453 · see citing works
<i>Phaser</i> crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works
Nishimura, R., Osako, T., Nishiyama, Y., Tashima, R., Nakano, M., Fujisue, M., Toyozumi, Y., & Arima, N. (2013) · Oncology · doi:10.1159/000353099 · Cited by 13,239 · see citing works
Comprehensive molecular portraits of human breast tumours
The Cancer Genome Atlas Network (2012) · Nature · doi:10.1038/nature11412 · Cited by 12,129 · see citing works
Comprehensive molecular characterization of human colon and rectal cancer
The Cancer Genome Atlas Network (2012) · Nature · doi:10.1038/nature11252 · Cited by 8,499 · see citing works
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334 · see citing works
Untangling the ErbB signalling network
Yarden, Y., & Sliwkowski, M. X. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052073 · Cited by 6,974 · see citing works
Comparison of multiple Amber force fields and development of improved protein backbone parameters
Horn̆ák, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A. E., & Simmerling, C. L. (2006) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21123 · Cited by 6,903 · see citing works
Improved side-chain torsion potentials for the Amber ff99SB protein force field
Lindorff-Larsen, K., Piana, S., Palmo, K., Maragakis, P., Klepeis, J., Dror, R., & Shaw, D. (2010) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.22711 · Cited by 6,037 · see citing works
Self-citationConstant pressure molecular dynamics algorithms
Martyna, G. J., Tobias, D. J., & Klein, M. L. (1994) · The Journal of Chemical Physics · doi:10.1063/1.467468 · Cited by 5,845 · see citing works
Joung, I., & Cheatham, T. (2008) · Journal of Physical Chemistry B · doi:10.1021/jp8001614 · Cited by 3,326 · see citing works
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
Zhang, X., Gureasko, J., Shen, K., Cole, P. A., & Kuriyan, J. (2006) · Cell · doi:10.1016/j.cell.2006.05.013 · Cited by 1,650 · see citing works
Kr�utler, V., A, W. F. V. G., & Hünenberger, P. H. (2001) · Journal of Computational Chemistry · doi:10.1002/1096-987x(20010415)22:5 · Cited by 1,444 · see citing works
Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains
Ogiso, H., Ishitani, R., Nureki, O., Fukai, S., Yamanaka, M., Kim, J.-H., Saito, K., Sakamoto, A., Inoue, M., Shirouzu, M., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00963-7 · Cited by 1,227 · see citing works
Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.017 · Cited by 1,192 · see citing works
Novel anticancer targets: revisiting ERBB2 and discovering ERBB3
Baselga, J. M., & Swain, S. M. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2656 · Cited by 1,144 · see citing works
Tzahar, E., Waterman, H., Chen, X., Levkowitz, G., Karunagaran, D., Lavi, S., Ratzkin, B. J., & Yarden, Y. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.10.5276 · Cited by 1,039 · see citing works
Escape from HER-family tyrosine kinase inhibitor therapy by the kinase-inactive HER3
Sergina, N. V., Rausch, M., Wang, D., Blair, J. A., Hann, B. C., Shokat, K. M., & Moasser, M. M. (2007) · Nature · doi:10.1038/nature05474 · Cited by 993 · see citing works
Crystal Structures of c-Src Reveal Features of Its Autoinhibitory Mechanism
Xu, W., Doshi, A. H., Lei, M., Eck, M. J., & Harrison, S. C. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80356-1 · Cited by 871 · see citing works
Optimized Molecular Dynamics Force Fields Applied to the Helix−Coil Transition of Polypeptides
Best, R. B., & Hummer, G. (2009) · The Journal of Physical Chemistry B · doi:10.1021/jp901540t · Cited by 836 · see citing works
EGF Activates Its Receptor by Removing Interactions that Autoinhibit Ectodomain Dimerization
Ferguson, K. M., Berger, M. B., Mendrola, J. M., Cho, H., Leahy, D. J., & Lemmon, M. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00047-9 · Cited by 801 · see citing works
Garrett, T., McKern, N. M., Lou, M., ELLEMAN, T. C., Adams, T. E., Lovrecz, G. O., Zhu, H., Walker, F., Frenkel, M. J., Hoyne, P. A., et al. (2002) · Cell · doi:10.1016/s0092-8674(02)00940-6 · Cited by 783 · see citing works
Processing diffraction data with mosflm
Leslie, A. G. W., & Powell, H. R. (2007) · NATO science series. Series II, Mathematics, physics and chemistry · doi:10.1007/978-1-4020-6316-9_4 · Cited by 617 · see citing works
Garrett, T., McKern, N. M., Lou, M., ELLEMAN, T. C., Adams, T. E., Lovrecz, G. O., Kofler, M., Jorissen, R. N., Nice, E. C., Burgess, A. W., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00048-0 · Cited by 614 · see citing works
Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment
Jura, N., Endres, N., Engel, K., Deindl, S., Das, R., Lamers, M. H., Wemmer, D. E., Zhang, X., & Kuriyan, J. (2009) · Cell · doi:10.1016/j.cell.2009.04.025 · Cited by 609 · see citing works
Self-citationArchitecture and Membrane Interactions of the EGF Receptor
Arkhipov, A. S., Shan, Y., Das, R., Endres, N., Eastwood, M. P., Wemmer, D. E., Kuriyan, J., & Shaw, D. E. (2013) · Cell · doi:10.1016/j.cell.2012.12.030 · Cited by 507 · see citing works
Self-citationEngelman, J. A., Janne, P. A., Mermel, C. H., Pearlberg, J., Mukohara, T., Fleet, C., Cichowski, K. M., Johnson, B. E., & Cantley, L. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409773102 · Cited by 494 · see citing works
Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor
Endres, N., Das, R., Smith, A. W., Arkhipov, A. S., Kovács, E., Huang, Y., Pelton, J. G., Shan, Y., Shaw, D. E., Wemmer, D. E., et al. (2013) · Cell · doi:10.1016/j.cell.2012.12.032 · Cited by 493 · see citing works
Self-citationGarrett, J. T., Olivares, M. G., Rinehart, C., Granja-Ingram, N. D. M., Sanchez, V. M., Chakrabarty, A., Dave, B., Cook, R. S., Pao, W. J., McKinely, E., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016140108 · Cited by 469 · see citing works
ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze autophosphorylation
Shi, F., Telesco, S., Liu, Y., Radhakrishnan, R., & Lemmon, M. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002753107 · Cited by 469 · see citing works
The structural basis of calcium transport by the calcium pump
Olesen, C., Picard, M., Winther, A.-M. L., Gyrup, C., Morth, J. P., Oxvig, C., MØLLER, J. V., & Nissen, P. (2007) · Nature · doi:10.1038/nature06418 · Cited by 468 · see citing works
Erickson, S. L., O’Shea, K. S., Ghaboosi, N., Loverro, L., Frantz, G. D., Bauer, M., Lu, L. H., & Moore, M. W. (1997) · Development · doi:10.1242/dev.124.24.4999 · Cited by 467 · see citing works
Aertgeerts, K., Skene, R. J., Yano, J. K., Sang, B., Zou, H., Snell, G., Jennings, A. J., Iwamoto, K., Habuka, N., Hirokawa, A., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.206193 · Cited by 448 · see citing works
Crystal Structure of Hck in Complex with a Src Family–Selective Tyrosine Kinase Inhibitor
Schindler, T. H., Sicheri, F., Pico, A. R., Gazit, A., Levitzki, A., & Kuriyan, J. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80357-3 · Cited by 429 · see citing works
Heregulin‐dependent regulation of HER2/neu oncogenic signaling by heterodimerization with HER3.
Wallasch, C., Weiss, F. U., Niederfellner, G., Jallal, B., Issing, W., & Ullrich, A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00101.x · Cited by 406 · see citing works
Millisecond-scale molecular dynamics simulations on Anton
Shaw, D. E., Dror, R. O., Salmon, J. K., Grossman, J. P., Mackenzie, K. M., Bank, J. A., Young, C., Deneroff, M. M., Batson, B., Bowers, K. J., et al. (2009) · Proceedings of the Conference on High Performance Computing Networking, Storage and Analysis · doi:10.1145/1654059.1654099 · Cited by 382 · see citing works
Self-citationOncogenic ERBB3 mutations in human cancers.
Jaiswal, B. S., Kljavin, N. M., Stawiski, E. W., Chan, E., Parikh, C., Durinck, S., Chaudhuri, S., Pujara, K., Guillory, J., Edgar, K. A., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.04.012 · Cited by 350 · see citing works
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
Jura, N., Shan, Y., Cao, X., Shaw, D. E., & Kuriyan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912101106 · Cited by 338 · see citing works
Self-citationThe Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain
Brewer, M. R., Choi, S. H., Alvarado, D., Moravcevic, K., Pozzi, A., Lemmon, M. A., & Carpenter, G. F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.034 · Cited by 314 · see citing works
Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms
Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works
Self-citationField, M. J., Albe, M., Bret, C., Martin, F. P.-D., & Thomas, A. M. (2000) · Journal of Computational Chemistry · doi:10.1002/1096-987x(200009)21:12 · Cited by 303 · see citing works
Millisecond-scale molecular dynamics simulations on Anton
Shaw, D. E., Dror, R. O., Salmon, J. K., Grossman, J. P., MacKenzie, K., Bank, J. A., Young, C., Deneroff, M. M., Batson, B., Bowers, K. J., et al. (2009) · International Conference for High Performance Computing, Networking, Storage and Analysis (SC) · doi:10.1145/1654059.1654126 · Cited by 294 · see citing works
Self-citationThe influence of heregulins on human Schwann cell proliferation
Levi, A., Bunge, R. P., Lofgren, J. A., et al. (1995) · Journal of Neuroscience · doi:10.1523/jneurosci.15-02-01329.1995 · Cited by 251 · see citing works
Adams, J. A. (2002) · Biochemistry · doi:10.1021/bi020617o · Cited by 233 · see citing works
The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand
Bouyain, S., Longo, P. A., Li, S., Ferguson, K. M., & Leahy, D. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507591102 · Cited by 191 · see citing works
Mechanism of Activation and Inhibition of the HER4/ErbB4 Kinase
Qiu, C., Tarrant, M. K., Choi, S. H., Sathyamurthy, A., Bose, R., Banjade, S., Pal, A., Bornmann, W. G., Lemmon, M. A., Cole, P. A., et al. (2008) · Structure · doi:10.1016/j.str.2007.12.016 · Cited by 187 · see citing works
Campbell, M. R., Amin, D. N., & Moasser, M. M. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-09-1218 · Cited by 187 · see citing works
Structural Basis for Negative Cooperativity in Growth Factor Binding to an EGF Receptor
Alvarado, D., Klein, D. E., & Lemmon, M. A. (2010) · Cell · doi:10.1016/j.cell.2010.07.015 · Cited by 181 · see citing works
ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface
Berger, M. B., Mendrola, J. M., & Lemmon, M. A. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.06.014 · Cited by 150 · see citing works
Mi, L.-Z., Lu, C., Li, Z., Nishida, N., Walz, T., & Springer, T. A. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2092 · Cited by 145 · see citing works
Amin, D. N., Campbell, M. R., & Moasser, M. M. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.08.007 · Cited by 143 · see citing works
Cutoff Size Need Not Strongly Influence Molecular Dynamics Results for Solvated Polypeptides
Beck, D. A. C., Armen, R. S., & Daggett, V. (2004) · Biochemistry · doi:10.1021/bi0486381 · Cited by 133 · see citing works
Structural basis of CX-4945 binding to human protein kinase CK2
Ferguson, A. D., Sheth, P. R., Basso, A. D., Paliwal, S., Gray, K., Fischmann, T. O., & Le, H. V. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.11.019 · Cited by 121 · see citing works
A common, avoidable source of error in molecular dynamics integrators
Lippert, R. A., Bowers, K. J., Dror, R. O., et al. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2431176 · Cited by 114 · see citing works
Wood, E. R., Shewchuk, L. M., Ellis, B., Brignola, P. S., Brashear, R. L., Caferro, T. R., Dickerson, S. H., Dickson, H. D., Donaldson, K. H., Gaul, M. D., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708281105 · Cited by 113 · see citing works
Frolov, A., Schuller, K., Tzeng, C.-W. D., Cannon, E. E., Ku, B. C., Howard, J. H., Vickers, S. M., Heslin, M. J., Buchsbaum, D. J., & Arnoletti, J. P. (2007) · Cancer Biology & Therapy · doi:10.4161/cbt.6.4.3849 · Cited by 89 · see citing works
The upgraded role of HER3 and HER4 receptors in breast cancer
Koutras, A. K., Fountzilas, G., Kalogeras, K. T., Starakis, I., Iconomou, G., & Kalofonos, H. P. (2009) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2009.04.011 · Cited by 86 · see citing works
ErbB signaling in cardiac development and disease
Sanchez-Soria, P., & Camenisch, T. D. (2010) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2010.09.011 · Cited by 83 · see citing works
Yu, Z., Boggon, T. J., Kobayashi, S. S., Jin, C., Ma, P. C., Dowlati, A., Kern, J. A., Tenen, D. G., & Halmos, B. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1248 · Cited by 71 · see citing works
Her4 and Her2/neu Tyrosine Kinase Domains Dimerize and Activate in a Reconstituted in Vitro System
Monsey, J. D., Shen, W., Schlesinger, P. H., & Bose, R. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096032 · Cited by 65 · see citing works
ErbB3 expression promotes tumorigenesis in pancreatic adenocarcinoma
Liles, J. S., Arnoletti, J. P., Tzeng, C.-W. D., Howard, J. H., Kossenkov, A. V., Kulesza, P., Heslin, M. J., & Frolov, A. (2010) · Cancer Biology & Therapy · doi:10.4161/cbt.10.6.12532 · Cited by 63 · see citing works
Chausovsky, A., Waterman, H., Elbaum, M., Yarden, Y., Geiger, B., & Bershadsky, A. D. (2000) · Oncogene · doi:10.1038/sj.onc.1203410 · Cited by 42 · see citing works
Collier, T. S., Diraviyam, K., Monsey, J. D., Shen, W., Sept, D., & Bose, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.474882 · Cited by 35 · see citing works
Neuregulin-1/ErbB signaling: a druggable target for treating heart failure
Xu, Y., Li, X., & Zhou, M. (2008) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2008.11.004 · Cited by 34 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence
Duran-Frigola, M., Cigler, M., & Winter, G. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11098 · Cited by 50 · see citing works
Computed cancer interactome explains the effects of somatic mutations in cancers
Zhang, J., Pei, J., Durham, J., Bos, T., & Cong, Q. (2022) · Protein Science · doi:10.1002/pro.4479 · Cited by 31 · see citing works
HER3 Alterations in Cancer and Potential Clinical Implications
Kilroy, M. K., Park, S., Feroz, W., Patel, H., Mishra, R., Alanazi, S., & Garrett, J. T. (2022) · Cancers · doi:10.3390/cancers14246174 · Cited by 21 · see citing works
- Authors
- Littlefield, P., Liu, L., Mysore, V., Shan, Y., Shaw, D. E., & Jura, N.
- Affiliations
- University of California, San Francisco (US)
- D. E. Shaw Research (US)
- Corresponding author
- Jura, Natalia
- Venue
- Science Signaling
- Published
- 2014-12-02
- Volume
- 7
- Issue
- 354
- Pages
- ra114-ra114
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC4492339
- OpenAlex
- W2157884341
- Cited by
- 126
- References
- 69
- Citations by year
- 2026: 7 · 2025: 7 · 2024: 6 · 2023: 12 · 2022: 12 · 2021: 15 · 2020: 13 · 2019: 14 · 2018: 13 · 2017: 10 · 2016: 9 · 2015: 6 · 2014: 2
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Update notices
- correction (2015-09-01)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- U.S. Public Health Service (R01 RGM109176A)
- National Institute of General Medical Sciences (R01GM109176)
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- HER3, EGFR, heterodimerization, allosteric activation, kinase domain crystal structure, cancer-associated mutations, dimer interface, HER2, receptor tyrosine kinase signaling
- MeSH terms
- Cloning, Molecular, Crystallization, Humans, Models, Molecular, Mutation, Signal Transduction, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Dimerization, Receptor, ErbB-3, Molecular Dynamics Simulation, ErbB Receptors
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