Widespread Backtracking by RNA Pol II Is a Major Effector of Gene Activation, 5′ Pause Release, Termination, and Transcription Elongation Rate
Open accessAbstract
In addition to phosphodiester bond formation, RNA polymerase II has an RNA endonuclease activity, stimulated by TFIIS, which rescues complexes that have arrested and backtracked. How TFIIS affects transcription under normal conditions is poorly understood. We identified backtracking sites in human cells using a dominant-negative TFIIS (TFIIS DN) that inhibits RNA cleavage and stabilizes backtracked complexes. Backtracking is most frequent within 2 kb of start sites, consistent with slow elongation early in transcription, and in 3' flanking regions where termination is enhanced by TFIIS DN, suggesting that backtracked pol II is a favorable substrate for termination. Rescue from backtracking by RNA cleavage also promotes escape from 5' pause sites, prevents premature termination of long transcripts, and enhances activation of stress-inducible genes. TFIIS DN slowed elongation rates genome-wide by half, suggesting that rescue of backtracked pol II by TFIIS is a major stimulus of elongation under normal conditions.
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?
Slowing down transcription using mutants of the elongation factor TFIIS shifts termination upstream.
“Consistent with the results obtained with slow RNA Pol II mutants, slowing‐down transcription using mutants of the elongation factor TFIIS also shifts termination upstream (Sheridan et al, 2019; Zatreanu et al, 2019).”
From RNA polymerase II speed: a key player in controlling and adapting transcriptome composition (2021) · cites this paper as Sheridan et al, 2019
TFIIS increases RNA Pol II speed in human cells.
“Accordingly, TFIIS increases RNA Pol II speed in human cells (Sheridan et al, 2019; Zatreanu et al, 2019), while its deletion had no effect on RNA Pol II velocity in budding yeast (Mason & Struhl, 2005).”
From RNA polymerase II speed: a key player in controlling and adapting transcriptome composition (2021) · cites this paper as Sheridan et al, 2019
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
Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2
Love, M. I., Huber, W., & Anders, S. (2014) · Genome Biology · doi:10.1186/s13059-014-0550-8 · Cited by 95,106 · see citing works
The Sequence Alignment/Map format and SAMtools
Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041 · see citing works
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400 · see citing works
Gratzner, H. G. (1982) · Science · doi:10.1126/science.7123245 · Cited by 2,653 · see citing works
Nascent RNA Sequencing Reveals Widespread Pausing and Divergent Initiation at Human Promoters
Core, L. J., Waterfall, J. J., & Lis, J. T. (2008) · Science · doi:10.1126/science.1162228 · Cited by 1,986 · see citing works
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247 · see citing works
Human breast cancer cells generated by oncogenic transformation of primary mammary epithelial cells
Elenbaas, B., Spirio, L., Koerner, F., Fleming, M. D., Zimonjic, D. B., Donaher, J. L., Popescu, N. C., Hahn, W. C., & Weinberg, R. A. (2001) · Genes & Development · doi:10.1101/gad.828901 · Cited by 878 · see citing works
Getting up to speed with transcription elongation by RNA polymerase II
Jonkers, I., & Lis, J. T. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3953 · Cited by 876 · see citing works
Coupling mRNA processing with transcription in time and space
Bentley, D. L. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3662 · Cited by 828 · see citing works
Self-citationNascent transcript sequencing visualizes transcription at nucleotide resolution
Churchman, L. S., & Weissman, J. S. (2011) · Nature · doi:10.1038/nature09652 · Cited by 823 · see citing works
Progression through the RNA Polymerase II CTD Cycle
Buratowski, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.019 · Cited by 777 · see citing works
Jonkers, I., Kwak, H., & Lis, J. T. (2014) · eLife · doi:10.7554/elife.02407 · Cited by 581 · see citing works
Hypoxic Regulation of Lactate Dehydrogenase A
Firth, J. D., Ebert, B. L., & Ratcliffe, P. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21021 · Cited by 576 · see citing works
Mammalian NET-Seq Reveals Genome-wide Nascent Transcription Coupled to RNA Processing
Nojima, T., Gomes, T., Grosso, A. R. F., Kimura, H., Dye, M. J., Dhir, S., Carmo-Fonseca, M., & Proudfoot, N. J. (2015) · Cell · doi:10.1016/j.cell.2015.03.027 · Cited by 562 · see citing works
The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II
Kim, M., Krogan, N. J., Vasiljeva, L., Rando, O. J., Nedea, E. C., Greenblatt, J., & Buratowski, S. (2004) · Nature · doi:10.1038/nature03041 · Cited by 557 · see citing works
TT-seq maps the human transient transcriptome
Schwalb, B., Michel, M., Zacher, B., Frühauf, K., Demel, C., Tresch, A., Gagneur, J., & Cramer, P. (2016) · Science · doi:10.1126/science.aad9841 · Cited by 548 · see citing works
West, S., Gromak, N., & Proudfoot, N. J. (2004) · Nature · doi:10.1038/nature03035 · Cited by 506 · see citing works
Rates of in situ transcription and splicing in large human genes
Singh, J., & Padgett, R. A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1666 · Cited by 487 · see citing works
Complete RNA Polymerase II Elongation Complex Structure and Its Interactions with NTP and TFIIS
Kettenberger, H., Armache, K., & Cramer, P. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.040 · Cited by 437 · see citing works
Regulation of Alternative Splicing Through Coupling with Transcription and Chromatin Structure
Naftelberg, S., Schor, I. E., Ast, G., & Kornblihtt, A. R. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034242 · Cited by 437 · see citing works
Nechaev, S., Fargo, D. C., dos Santos, G., Liu, L., Gao, Y., & Adelman, K. (2010) · Science · doi:10.1126/science.1181421 · Cited by 424 · see citing works
Yamada, T., Yamaguchi, Y., Inukai, N., Okamoto, S., Mura, T., & Handa, H. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2005.11.024 · Cited by 421 · see citing works
Transcriptional termination in mammals: Stopping the RNA polymerase II juggernaut
Proudfoot, N. J. (2016) · Science · doi:10.1126/science.aad9926 · Cited by 413 · see citing works
Dynamic association of capping enzymes with transcribing RNA polymerase IIPreprint
Schroeder, S. C., Schwer, B., Shuman, S., & Bentley, D. L. (2000) · Genes & Development · doi:10.1101/gad.836300 · Cited by 387 · see citing works
Self-citationNucleosomes Are Context-Specific, H2A.Z-Modulated Barriers to RNA Polymerase
Weber, C. M., Ramachandran, S., & Henikoff, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.014 · Cited by 386 · see citing works
Structure of paused transcription complex Pol II–DSIF–NELF
Vos, S. M., Farnung, L., Urlaub, H., & Cramer, P. (2018) · Nature · doi:10.1038/s41586-018-0442-2 · Cited by 378 · see citing works
Connelly, S., & Manley, J. L. (1988) · Genes & Development · doi:10.1101/gad.2.4.440 · Cited by 377 · see citing works
Structural basis of RNA polymerase II backtracking, arrest and reactivation
Cheung, A. C. M., & Cramer, P. (2011) · Nature · doi:10.1038/nature09785 · Cited by 373 · see citing works
Architecture of the RNA Polymerase II-TFIIS Complex and Implications for mRNA Cleavage
Kettenberger, H., Armache, K., & Cramer, P. (2003) · Cell · doi:10.1016/s0092-8674(03)00598-1 · Cited by 355 · see citing works
RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes
Glover-Cutter, K. M., Kim, S., Espinosa, J. M., & Bentley, D. L. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1352 · Cited by 343 · see citing works
Self-citationRegulation of Metabolism by Hypoxia-Inducible Factor 1
Semenza, G. L. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.010678 · Cited by 342 · see citing works
Danko, C. G., Hah, N., Luo, X., Martins, A. L., Core, L., Lis, J. T., Siepel, A., & Kraus, W. L. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.02.015 · Cited by 333 · see citing works
Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
Heidemann, M., Hintermair, C., Voß, K., & Eick, D. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.013 · Cited by 300 · see citing works
Izban, M. G., & Luse, D. S. (1992) · Genes & Development · doi:10.1101/gad.6.7.1342 · Cited by 299 · see citing works
Veloso, A., Kirkconnell, K. S., Magnuson, B., Biewen, B., Paulsen, M. T., Wilson, T. E., & Ljungman, M. (2014) · Genome Research · doi:10.1101/gr.171405.113 · Cited by 281 · see citing works
Nucleosomes Can Form a Polar Barrier to Transcript Elongation by RNA Polymerase II
Bondarenko, V. A., Steele, L. M., Újvári, A., Gaykalova, D. A., Kulaeva, O. I., Polikanov, Y. S., Luse, D. S., & Studitsky, V. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.09.009 · Cited by 272 · see citing works
Nechaev, S., & Adelman, K. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.11.001 · Cited by 266 · see citing works
6-Azauracil inhibition of GTP biosynthesis in Saccharomyces cerevisiae
Exinger, F., & Lacroute, F. (1992) · Current Genetics · doi:10.1007/bf00351735 · Cited by 252 · see citing works
Transcriptional Fidelity and Proofreading by RNA Polymerase II
Thomas, M. J., Platas, A. A., & Hawley, D. K. (1998) · Cell · doi:10.1016/s0092-8674(00)81191-5 · Cited by 252 · see citing works
Fong, N., Brannan, K., Erickson, B., Kim, H., Cortazar, M. A., Sheridan, R. M., Nguyen, T., Karp, S., & Bentley, D. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.026 · Cited by 217 · see citing works
Self-citationFuchs, G., Voichek, Y., Benjamin, S., Gilad, S., Amit, I., & Oren, M. (2014) · Genome Biology · doi:10.1186/gb-2014-15-5-r69 · Cited by 203 · see citing works
Steurer, B., Janssens, R. C., Geverts, B., Geijer, M. E., Wienholz, F., Theil, A., Chang, J., Dealy, S. C., Pothof, J., van Cappellen, W. V., et al. (2018) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1717920115 · Cited by 203 · see citing works
Elongation factor-dependent transcript shortening by template-engaged RNA polymerase II.
Reines, D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50596-8 · Cited by 198 · see citing works
Unified two‐metal mechanism of RNA synthesis and degradation by RNA polymerase
Sosunov, V. V., Sosunova, E., Mustaev, A., Bass, I., Nikiforov, V., & Goldfarb, A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg193 · Cited by 198 · see citing works
Use of Bru-Seq and BruChase-Seq for genome-wide assessment of the synthesis and stability of RNA
Paulsen, M. T., Veloso, A., Prasad, J., Bedi, K., Ljungman, E. A., Magnuson, B., Wilson, T. E., & Ljungman, M. E. (2013) · Methods · doi:10.1016/j.ymeth.2013.08.015 · Cited by 194 · see citing works
Efficient Release from Promoter-Proximal Stall Sites Requires Transcript Cleavage Factor TFIIS
Adelman, K., Marr, M. T., Werner, J. K., Saunders, A., Ni, Z., Andrulis, E. D., & Lis, J. T. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.028 · Cited by 168 · see citing works
Thompson, N. E., Aronson, D. B., & Burgess, R. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39260-9 · Cited by 166 · see citing works
Sigurðsson, S., Dirac-Svejstrup, A. B., & Svejstrup, J. Q. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.026 · Cited by 141 · see citing works
Zhang, J.-W., Palangat, M., & Landick, R. (2009) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.1732 · Cited by 137 · see citing works
Kinetic Competition between RNA Polymerase II and Sen1-Dependent Transcription Termination
Hazelbaker, D. Z., Marquardt, S., Wlotzka, W., & Buratowski, S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.014 · Cited by 128 · see citing works
Donation of catalytic residues to RNA polymerase active center by transcription factor Gre
Sosunova, E., Sosunov, V. V., Kozlov, M. V., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2536698100 · Cited by 126 · see citing works
Pause & go: from the discovery of RNA polymerase pausing to its functional implications
Mayer, A., Landry, H. M., & Churchman, L. S. (2017) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2017.03.002 · Cited by 125 · see citing works
Shaw, R. J., & Reines, D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.20.7427-7437.2000 · Cited by 124 · see citing works
Bourgeois, C. F., Kim, Y. K., Churcher, M. J., West, M. J., & Karn, J. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1079-1093.2002 · Cited by 118 · see citing works
Mammalian NET-seq analysis defines nascent RNA profiles and associated RNA processing genome-wide
Nojima, T., Gomes, T., Carmo‐Fonseca, M., & Proudfoot, N. J. (2016) · Nature Protocols · doi:10.1038/nprot.2016.012 · Cited by 111 · see citing works
Izban, M. G., & Luse, D. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31468-6 · Cited by 107 · cited 1× · see citing works
“TFIIS-stimulated endonucleolytic cleavage releases RNA fragments 2 – 14 bases long (Izban and Luse, 1993).”
The RNA exosome promotes transcription termination of backtracked RNA polymerase II
Lemay, J., Larochelle, M., Marguerat, S., Atkinson, S. R., Bähler, J., & Bachand, F. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2893 · Cited by 91 · see citing works
Sekine, S., Murayama, Y., Svetlov, V. V., Nudler, E., & Yokoyama, S. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.014 · Cited by 90 · see citing works
Dynamic turnover of paused Pol II complexes at human promotersPreprint
Erickson, B., Sheridan, R. M., Cortázar, M. A., & Bentley, D. L. (2018) · Genes & Development · doi:10.1101/gad.316810.118 · Cited by 90 · see citing works
Self-citationJeon, C., Yoon, H. S., & Agarwal, K. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.9106 · Cited by 77 · see citing works
Carrière, L., Graziani, S., Alibert, O., Ghavi-Helm, Y., Boussouar, F., Humbertclaude, H., Jounier, S., Aude, J.-C., Keime, C., Murvai, J., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr737 · Cited by 75 · see citing works
Palangat, M., Renner, D. B., Price, D. H., & Landick, R. C. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409405102 · Cited by 70 · see citing works
Ccr4-Not and TFIIS Function Cooperatively To Rescue Arrested RNA Polymerase II
Dutta, A., Babbarwal, V., Fu, J., Brunke-Reese, D., Libert, D. M., Willis, J., & Reese, J. C. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00044-15 · Cited by 61 · see citing works
Ishibashi, T., Dangkulwanich, M., Coello, Y., Lionberger, T. A., Lubkowska, L., Ponticelli, A. S., Kashlev, M., & Bustamante, C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401611111 · Cited by 55 · see citing works
Zhang, C., & Burton, Z. F. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.070 · Cited by 54 · see citing works
Anamika, K., Gyenis, Á., Poidevin, L., Poch, O., & Tora, L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038769 · Cited by 54 · see citing works
Gómez-Herreros, F., de Miguel-Jiménez, L., Morillo‐Huesca, M., Delgado-Ramos, L., Muñoz-Centeno, M. C., & Chávez, S. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks340 · Cited by 42 · see citing works
Misincorporation by RNA polymerase is a major source of transcription pausing in vivo
James, K., Gamba, P., Cockell, S., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw969 · Cited by 39 · see citing works
Wide-ranging and unexpected consequences of altered Pol II catalytic activity in vivo
Malik, I., Qiu, C., Snavely, T. C., & Kaplan, C. D. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx037 · Cited by 31 · see citing works
Ishibashi, T., Dangkulwanich, M., Coello, Y., et al. (2014) · Cited by 13 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Cortazar, M. A., Sheridan, R. M., Erickson, B., Fong, N., Glover-Cutter, K., Brannan, K., & Bentley, D. L. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.031 · Cited by 227 · see citing works
Self-citationRNA polymerase II speed: a key player in controlling and adapting transcriptome composition
Muniz, L., Nicolas, E., & Trouche, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020105740 · Cited by 203 · see citing works
“Accordingly, TFIIS increases RNA Pol II speed in human cells (Sheridan et al , 2019; Zatreanu et al , 2019), while its deletion had no effect on RNA Pol II velocity in budding yeast (Mason & Struhl, 2005).”
Co-transcriptional splicing regulates 3′ end cleavage during mammalian erythropoiesis
Reimer, K. A., Mimoso, C. A., Adelman, K., & Neugebauer, K. M. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.018 · Cited by 180 · see citing works
Zatreanu, D., Han, Z., Mitter, R., Tumini, E., Williams, H., Gregersen, L., Dirac-Svejstrup, A. B., Roma, S., Stewart, A., Aguilera, A., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.037 · Cited by 124 · see citing works
Nascent Transcript Folding Plays a Major Role in Determining RNA Polymerase Elongation Rates
Turowski, T. W., Petfalski, E., Goddard, B. D., French, S. L., Helwak, A., & Tollervey, D. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.002 · Cited by 75 · see citing works
Organismal benefits of transcription speed control at gene boundaries
Leng, X., Ivanov, M., Kindgren, P., Malik, I., Thieffry, A., Brodersen, P., Sandelin, A., Kaplan, C. D., & Marquardt, S. (2020) · The EMBO Reports · doi:10.15252/embr.201949315 · Cited by 40 · see citing works
- Authors
- Sheridan, R. M., Fong, N., D’Alessandro, A., & Bentley, D. L.
- Affiliations
- University of Colorado Anschutz (US)
- Corresponding author
- Bentley, David L.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2019-01
- Volume
- 73
- Issue
- 1
- Pages
- 107-118.e4
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC6320282
- OpenAlex
- W2902183734
- Cited by
- 123
- References
- 70
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 22 · 2023: 13 · 2022: 12 · 2021: 27 · 2020: 16 · 2019: 12
- FWCI
- 4.89
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 367 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R35GM118051)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- TFIIS, transcription termination, gene activation, stress-inducible genes, 3' flanking region, RNA cleavage
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Kinetics, Mutation, RNA, RNA Polymerase II, Transcriptional Activation, 3' Flanking Region, Transcriptional Elongation Factors, Mice, HEK293 Cells, RNA Cleavage, Transcription Elongation, Genetic, Transcription Termination, Genetic
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