Oxidative protein folding in eukaryotes
Open accessAbstract
The endoplasmic reticulum (ER) provides an environment that is highly optimized for oxidative protein folding. Rather than relying on small molecule oxidants like glutathione, it is now clear that disulfide formation is driven by a protein relay involving Ero1, a novel conserved FAD-dependent enzyme, and protein disulfide isomerase (PDI); Ero1 is oxidized by molecular oxygen and in turn acts as a specific oxidant of PDI, which then directly oxidizes disulfide bonds in folding proteins. While providing a robust driving force for disulfide formation, the use of molecular oxygen as the terminal electron acceptor can lead to oxidative stress through the production of reactive oxygen species and oxidized glutathione. How Ero1p distinguishes between the many different PDI-related proteins and how the cell minimizes the effects of oxidative damage from Ero1 remain important open questions.
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?
Reaction of cysteine with another cysteine under non-enzymatic and enzyme-mediated conditions leads to cystine, which stabilizes protein structures via intra- and intermolecular disulfide bridges.
“Reaction of cysteine with another cysteine under non-enzymatic as well as enzyme mediated conditions leads to cystine. Cystine is a vitally important modification, because it stabilizes protein structures via intra- and intermolecular disulfide bridges.”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [17]
The Abstract (page not provided) says disulfide bonds involving cysteine residues are often crucial to protein stability and describes both spontaneous formation in vitro and assisted formation in vivo. The section on oxidative folding machinery also describes enzyme-catalyzed disulfide formation. Our copy does not explicitly identify the product as cystine or establish the claim’s distinction between intra- and intermolecular bridges. (LLM, conf=0.85)
Experimental — accuracy not yet measured
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
Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968 · see citing works
Flagged first, then by citations
Research works printed but not linked: 43
- Anelli, T., M. Alessio, A. Mezghrani, T. Simmen, F. Talamo, A. Bachi, and R. Sitia. 2002. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 21: 835–844. 11847130 PMC125352
- Anfinsen, C.B., E. Haber, M. Sela, and F.H. White. 1961. The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc. Natl. Acad. Sci. USA. 47: 1309–1314. 13683522 PMC223141
- Bader, M., W. Muse, D.P. Ballou, C. Gassner, and J.C. Bardwell. 1999. Oxidative protein folding is driven by the electron transport system. Cell. 98: 217–227. 10428033
- Bader, M.W., T. Xie, C.A. Yu, and J.C. Bardwell. 2000. Disulfide bonds are generated by quinone reduction. J. Biol. Chem. 275: 26082–26088. 10854438
- Bader, M.W., A. Hiniker, J. Regeimbal, D. Goldstone, P.W. Haebel, J. Riemer, P. Metcalf, and J.C. Bardwell. 2001. Turning a disulfide isomerase into an oxidase: DsbC mutants that imitate DsbA. EMBO J. 20: 1555–1562. 11285220 PMC145499
- Bardwell, J.C., K. McGovern, and J. Beckwith. 1991. Identification of a protein required for disulfide bond formation in vivo. Cell. 67: 581–589. 1934062
- Bardwell, J.C., J.O. Lee, G. Jander, N. Martin, D. Belin, and J. Beckwith. 1993. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. USA. 90: 1038–1042. 8430071 PMC45806
- Cabibbo, A., M. Pagani, M. Fabbri, M. Rocchi, M.R. Farmery, N.J. Bulleid, and R. Sitia. 2000. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275: 4827–4833. 10671517
- Carelli, S., A. Ceriotti, A. Cabibbo, G. Fassina, M. Ruvo, and R. Sitia. 1997. Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER. Science 277:1681–1684. (published erratum appears in Science. 1998. 279:1288–1289) 9287224
- Cuozzo, J.W., and C.A. Kaiser. 1999. Competition between glutathione and protein thiols for disulphide-bond formation. Nat. Cell Biol. 1: 130–135. 10559898
- Frand, A.R., and C.A. Kaiser. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell. 1: 161–170. 9659913
- Frand, A.R., and C.A. Kaiser. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell. 4: 469–477. 10549279
- Frand, A.R., and C.A. Kaiser. 2000. Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum. Mol. Biol. Cell. 11: 2833–2843. 10982384 PMC14959
- Frand, A.R., J.W. Cuozzo, and C.A. Kaiser. 2000. Pathways for protein disulphide bond formation. Trends Cell Biol. 10: 203–210. 10754564
- Freedman, R.B. 1989. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell. 57: 1069–1072. 2544299
- Gerber, J., U. Muhlenhoff, G. Hofhaus, R. Lill, and T. Lisowsky. 2001. Yeast ERV2p is the first microsomal FAD-linked sulfhydryl oxidase of the Erv1p/Alrp protein family. J. Biol. Chem. 276: 23486–23491. 11313344
- Gess, B., K.H. Hofbauer, R.H. Wenger, C. Lohaus, H.E. Meyer, and A. Kurtz. 2003. The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur. J. Biochem. 270: 2228–2235. 12752442
- Gilbert, H.F. 1990. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63: 69–172. 2407068
- Gliszczynska, A., and A. Koziolowa. 1998. Chromatographic determination of flavin derivatives in baker's yeast. J. Chromatogr. A. 822: 59–66. 9810711
- Goldberger, R.F., C.J. Epstein, and C.B. Anfinsen. 1963. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 238: 628–635. 13948694
- Gross, E., C.S. Sevier, A. Vala, C.A. Kaiser, and D. Fass. 2002. A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat. Struct. Biol. 9: 61–67. 11740506
- Harding, H.P., Y. Zhang, and D. Ron. 1999. Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase. Nature. 397: 271–274. 9930704
- Harding, H.P., Y. Zhang, H. Zeng, I. Novoa, P.D. Lu, M. Calfon, N. Sadri, C. Yun, B. Popko, R. Paules, et al. 2003. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell. 11: 619–633. 12667446
- Holst, B., C. Tachibana, and J.R. Winther. 1997. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J. Cell Biol. 138: 1229–1238. 9298979 PMC2132551
- Laboissiere, M.C., S.L. Sturley, and R.T. Raines. 1995. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270: 28006–28009. 7499282
- Lange, H., T. Lisowsky, J. Gerber, U. Muhlenhoff, G. Kispal, and R. Lill. 2001. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2: 715–720. 11493598 PMC1083998
- Lee, J., G. Hofhaus, and T. Lisowsky. 2000. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 477: 62–66. 10899311
- Lisowsky, T. 1994. ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae. Curr. Genet. 26: 15–20. 7954891
- Mezghrani, A., A. Fassio, A. Benham, T. Simmen, I. Braakman, and R. Sitia. 2001. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20: 6288–6296. 11707400 PMC125306
- Missiakas, D., C. Georgopoulos, and S. Raina. 1993. Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo. Proc. Natl. Acad. Sci. USA. 90: 7084–7088. 7688471 PMC47080
- Molinari, M., and A. Helenius. 1999. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature. 402: 90–93. 10573423
- Pagani, M., M. Fabbri, C. Benedetti, A. Fassio, S. Pilati, N.J. Bulleid, A. Cabibbo, and R. Sitia. 2000. Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275: 23685–23692. 10818100
- Pagani, M., S. Pilati, G. Bertoli, B. Valsasina, and R. Sitia. 2001. The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function. FEBS Lett. 508: 117–120. 11707280
- Pollard, M.G., K.J. Travers, and J.S. Weissman. 1998. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 1: 171–182. 9659914
- Princiotta, M.F., D. Finzi, S.B. Qian, J. Gibbs, S. Schuchmann, F. Buttgereit, J.R. Bennink, and J.W. Yewdell. 2003. Quantitating protein synthesis, degradation, and endogenous antigen processing. Immunity. 18: 343–354. 12648452
- Rietsch, A., P. Bessette, G. Georgiou, and J. Beckwith. 1997. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179: 6602–6608. 9352906 PMC179585
- Senkevich, T.G., C.L. White, E.V. Koonin, and B. Moss. 2000. A viral member of the ERV1/ALR protein family participates in a cytoplasmic pathway of disulfide bond formation. Proc. Natl. Acad. Sci. USA. 97: 12068–12073. 11035794 PMC17295
- Sevier, C.S., J.W. Cuozzo, A. Vala, F. Aslund, and C.A. Kaiser. 2001. A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation. Nat. Cell Biol. 3: 874–882. 11584268
- Thorpe, C., K.L. Hoober, S. Raje, N.M. Glynn, J. Burnside, G.K. Turi, and D.L. Coppock. 2002. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Arch. Biochem. Biophys. 405: 1–12. 12176051
- Travers, K.J., C.K. Patil, L. Wodicka, D.J. Lockhart, J.S. Weissman, and P. Walter. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell. 101: 249–258. 10847680
- Tsai, B., and T.A. Rapoport. 2002. Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J. Cell Biol. 159: 207–216. 12403808 PMC2173060
- Tu, B.P., and J.S. Weissman. 2002. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 10: 983–994. 12453408
- Tu, B.P., S. Ho-Schleyer, K.J. Travers, and J.S. Weissman. 2000. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science. 290: 1571–1574. 11090354
Cited by
Sorted by citations
Activation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731 · see citing works
From endoplasmic-reticulum stress to the inflammatory response
Zhang, K., & Kaufman, R. J. (2008) · Nature · doi:10.1038/nature07203 · Cited by 2,010 · see citing works
Calcium and ROS: A mutual interplay
Görlach, A., Bertram, K., Hudecova, S., & Krizanova, O. (2015) · Redox Biology · doi:10.1016/j.redox.2015.08.010 · Cited by 1,546 · see citing works
Endoplasmic reticulum stress signalling-from basic mechanisms to clinical applications
Almanza, A., Carlesso, A., Chintha, C., Creedican, S., Doultsinos, D., Leuzzi, B., Luís, A., McCarthy, N., Montibeller, L., More, S., et al. (2019) · The FEBS Journal · doi:10.1111/febs.14608 · Cited by 1,034 · see citing works
ROS Generation and Antioxidant Defense Systems in Normal and Malignant Cells
Snezhkina, A. V., Kudryavtseva, A. V., Kardymon, O. L., Savvateeva, M. V., Melnikova, N. V., Krasnov, G. S., & Dmitriev, A. A. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6175804 · Cited by 934 · see citing works
Schuldiner, M., Collins, S. R., Thompson, N. J., Denic, V., Bhamidipati, A., Punna, T., Ihmels, J., Andrews, B., Boone, C., Greenblatt, J. F., et al. (2005) · Cell · doi:10.1016/j.cell.2005.08.031 · Cited by 870 · see citing works
Self-citationReactive oxygen species in health and disease
Alfadda, A. A., & Sallam, R. M. (2012) · Journal of Biomedicine and Biotechnology · doi:10.1155/2012/936486 · Cited by 824 · see citing works
Jones, D. P., & Sies, H. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2015.6247 · Cited by 647 · see citing works
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600 · see citing works
Peroxiredoxin functions as a peroxidase and a regulator and sensor of local peroxides
Rhee, S. G., Woo, H. A., Kil, I. S., & Bae, S. H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.283432 · Cited by 603 · see citing works
Gregor, M. F., & Hotamisligil, G. S. (2007) · Journal of Lipid Research · doi:10.1194/jlr.r700007-jlr200 · Cited by 586 · see citing works
Santos, C. X. C., Tanaka, L. Y., Wosniak, J., & Laurindo, F. R. M. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2625 · Cited by 572 · see citing works
Positive and Negative Regulation of Insulin Signaling by Reactive Oxygen and Nitrogen Species
Bashan, N., Kovsan, J., Kachko, I., Ovadia, H., & Rudich, A. (2009) · Physiological Reviews · doi:10.1152/physrev.00014.2008 · Cited by 542 · see citing works
Burton, G. J., Yung, H.-W., Cindrova-Davies, T., & Charnock-Jones, D. S. (2009) · Placenta · doi:10.1016/j.placenta.2008.11.003 · Cited by 502 · see citing works
Mitochondrial dysfunction in neurodegenerative disorders
Klemmensen, M. M., Borrowman, S. H., Pearce, C., Pyles, B., & Chandra, B. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2023.10.002 · Cited by 396 · see citing works
Endoplasmic reticulum stress and pancreatic β-cell death
Fonseca, S. G., Gromada, J., & Urano, F. (2011) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2011.02.008 · Cited by 384 · see citing works
Oxidative stress and calcium dysregulation by palmitate in type 2 diabetes
Ly, L. D., Xu, S., Choi, S.-K., Ha, C.-M., Thoudam, T., Cha, S.-K., Wiederkehr, A., Wollheim, C. B., Lee, I.-K., & Park, K.-S. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.157 · Cited by 378 · see citing works
Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“Formation and cleavage of disulfide bonds is a reversible process, which is controlled by several enzymes in vivo [17].”
BackgroundMonitoring disulfide bond formation in the eukaryotic cytosol
Østergaard, H., Tachibana, C., & Winther, J. R. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200402120 · Cited by 333 · see citing works
Mori, T., Hayashi, T., Hayashi, E., & Su, T.-P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0076941 · Cited by 317 · see citing works
Pluquet, O., Pourtier, A., & Abbadie, C. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00334.2014 · Cited by 305 · see citing works
Regulation of protein function and signaling by reversible cysteine S-nitrosylation
Gould, N., Doulias, P.-T., Tenopoulou, M., Raju, K., & Ischiropoulos, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.r113.460261 · Cited by 274 · see citing works
The Oxidative Stress of Zinc Deficiency
Eide, D. J. (2011) · Metallomics · doi:10.1039/c1mt00064k · Cited by 214 · see citing works
Crosstalk between Hypoxia and ER Stress Response: a Key Regulator of Macrophage Polarization
Díaz-Bulnes, P., Saiz, M. L., López-Larrea, C., & Rodríguez, R. M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02951 · Cited by 175 · see citing works
May, D., Itin, A., Gal, O., Kalinski, H., Feinstein, E., & Keshet, E. (2005) · Oncogene · doi:10.1038/sj.onc.1208325 · Cited by 167 · see citing works
Driving the cell cycle through metabolism
Cai, L., & Tu, B. P. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154010 · Cited by 140 · see citing works
Self-citationAyer, A., Gourlay, C. W., & Dawes, I. W. (2014) · FEMS Yeast Research · doi:10.1111/1567-1364.12114 · Cited by 125 · see citing works
Policastro, L. L., Ibañez, I. L., Notcovich, C., Duran, H. A., & Podhajcer, O. L. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4367 · Cited by 120 · see citing works
Multiple Post-translational Modifications Affect Heterologous Protein Synthesis
Tokmakov, A. A., Kurotani, A., Takagi, T., Toyama, M., Shirouzu, M., Fukami, Y., & Yokoyama, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366351 · Cited by 88 · see citing works
The unfolded protein response and cancer: A brighter future unfolding?
Scriven, P., Brown, N. J., Pockley, A. G., & Wyld, L. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0150-5 · Cited by 67 · see citing works
Potential for cellular stress response to hepatic factor VIII expression from AAV vector
Zolotukhin, I., Markusic, D. M., Palaschak, B., Hoffman, B. E., Srikanthan, M. A., & Herzog, R. W. (2016) · Molecular Therapy - Methods & Clinical Development · doi:10.1038/mtm.2016.63 · Cited by 65 · see citing works
Endoplasmic Reticulum Stress and Reactive Oxygen Species in Plants
Cao, J., Wang, C., Hao, N., Fujiwara, T., & Wu, T. (2022) · Antioxidants · doi:10.3390/antiox11071240 · Cited by 58 · see citing works
Kritsiligkou, P., Rand, J. D., Weids, A. J., Wang, X., Kershaw, C. J., & Grant, C. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.001824 · Cited by 36 · see citing works
The ambiguous aspects of oxygen
Napolitano, G., Fasciolo, G., & Venditti, P. (2022) · Oxygen · doi:10.3390/oxygen2030027 · Cited by 30 · see citing works
- Authors
- Tu, B. P., & Weissman, J. S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-02-02
- Volume
- 164
- Issue
- 3
- Pages
- 341-346
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2172237
- OpenAlex
- W2059586921
- Cited by
- 1,041
- References
- 1
- Citations by year
- 2026: 27 · 2025: 27 · 2024: 44 · 2023: 43 · 2022: 44 · 2021: 52 · 2020: 52 · 2019: 41 · 2018: 44 · 2017: 39 · 2016: 54 · 2015: 43 · 2014: 55 · 2013: 55 · 2012: 61
- FWCI
- 3.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- oxidative protein folding, endoplasmic reticulum, disulfide bond formation, Ero1, protein disulfide isomerase, FAD-dependent oxidase, molecular oxygen as oxidant, reactive oxygen species, oxidative stress, glutathione disulfide
- MeSH terms
- Animals, Endoplasmic Reticulum, Eukaryotic Cells, Glycoproteins, Humans, Membrane Glycoproteins, Oxidation-Reduction, Oxidoreductases, Protein Folding, Protein Disulfide-Isomerases
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
