The DOI matches its Crossref record; 59 of the 60 references it cites were found in a registry or an index, and 1 are not checked yet.
Alzheimer’s-Causing Mutations Shift Aβ Length by Destabilizing γ-Secretase-Aβn Interactions
Open accessAbstract
Alzheimer's disease (AD)-linked mutations in Presenilins (PSEN) and the amyloid precursor protein (APP) lead to production of longer amyloidogenic Aβ peptides. The shift in Aβ length is fundamental to the disease; however, the underlying mechanism remains elusive. Here, we show that substrate shortening progressively destabilizes the consecutive enzyme-substrate (E-S) complexes that characterize the sequential γ-secretase processing of APP. Remarkably, pathogenic PSEN or APP mutations further destabilize labile E-S complexes and thereby promote generation of longer Aβ peptides. Similarly, destabilization of wild-type E-S complexes by temperature, compounds, or detergent promotes release of amyloidogenic Aβ. In contrast, E-Aβ n stabilizers increase γ-secretase processivity. Our work presents a unifying model for how PSEN or APP mutations enhance amyloidogenic Aβ production, suggests that environmental factors may increase AD risk, and provides the theoretical basis for the development of γ-secretase/substrate stabilizing compounds for the prevention of AD.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Thus, GDE2 loss leads to an increase in Aβ peptides, in particular, the longer Aβ42 peptide associated with pathogenic Aβ species (31).”
From GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein (2021) · cites this paper as [31]
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.
Citations
Cites
Yung-Chi, C., & Prusoff, W. H. (1973) · Biochemical Pharmacology · doi:10.1016/0006-2952(73)90196-2 · Cited by 12,922
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
A presenilin-1-dependent γ-secretase-like protease mediates release of Notch intracellular domain
De Strooper, B., Annaert, W., Cupers, P., Saftig, P., Craessaerts, K., Mumm, J. S., Schroeter, E. H., Schrijvers, V., Wolfe, M. S., Ray, W. J., et al. (1999) · Nature · doi:10.1038/19083 · Cited by 2,100
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962
Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,959
Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
De Strooper, B., Saftig, P., Craessaerts, K., Vanderstichele, H., Guhde, G., Annaert, W., Von Figura, K., & Van Leuven, F. (1998) · Nature · doi:10.1038/34910 · Cited by 1,818
A century of trends in adult human height
NCD Risk Factor Collaboration (NCD-RisC) (2016) · eLife · doi:10.7554/elife.13410 · Cited by 1,558
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Weggen, S., Eriksen, J. L., Das, P., Sagi, S. A., Wang, R., Pietrzik, C. U., Findlay, K. A., Smith, T. E., Murphy, M. P., Bulter, T., et al. (2001) · Nature · doi:10.1038/35102591 · Cited by 1,388
Single App knock-in mouse models of Alzheimer’s disease
Saito, T., Matsuba, Y., Mihira, N., Takano, J., Nilsson, P., Itohara, S., Iwata, N., & Saido, T. C. (2014) · Nature Neuroscience · doi:10.1038/nn.3697 · Cited by 1,366
Self-citationSampling the conformational space of the catalytic subunit of human γ-secretase
Bai, X., Rajendra, E., Yang, G., Shi, Y., & Scheres, S. H. W. (2015) · eLife · doi:10.7554/elife.11182 · Cited by 548
An atomic structure of human γ-secretase
Bai, X., Yan, C., Yang, G., Lu, P., Ma, D., Sun, L., Zhou, R., Scheres, S. H. W., & Shi, Y. (2015) · Nature · doi:10.1038/nature14892 · Cited by 512
Takami, M., Nagashima, Y., Sano, Y., Ishihara, S., Morishima-Kawashima, M., Funamoto, S., & Ihara, Y. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.2362-09.2009 · Cited by 498
The mechanism of γ‐Secretase dysfunction in familial Alzheimer disease
Chávez‐Gutiérrez, L., Bammens, L., Benilova, I., Vandersteen, A., Benurwar, M., Borgers, M., Lismont, S., Zhou, L., Van Cleynenbreugel, S., Esselmann, H., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.79 · Cited by 495
Self-citationThe amyloid precursor protein has a flexible transmembrane domain and binds cholesterol
Barrett, P. J., Song, Y., Van Horn, W. D., Hustedt, E. J., Schafer, J. M., Hadziselimovic, A., Beel, A. J., & Sanders, C. R. (2012) · Science · doi:10.1126/science.1219988 · Cited by 467
Cholesterol-Dependent γ-Secretase Activity in Buoyant Cholesterol-Rich Membrane Microdomains
Wahrle, S., Das, P., Nyborg, A. C., McLendon, C., Shoji, M., Kawarabayashi, T., Younkin, L. H., Younkin, S. G., & Golde, T. E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0470 · Cited by 356
Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production
Kukar, T. L., Murphy, M. P., Eriksen, J. L., Sagi, S. A., Weggen, S., Smith, T. E., Ladd, T. B., Khan, M. A., Kache, R., Beard, J. D., et al. (2005) · Nature Medicine · doi:10.1038/nm1235 · Cited by 290
Potent amyloidogenicity and pathogenicity of Aβ43
Saito, T., Suemoto, T., Brouwers, N., Sleegers, K., Funamoto, S., Mihira, N., Matsuba, Y., Yamada, K., Nilsson, P., Takano, J., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2858 · Cited by 282
Self-citationWiltfang, J., Esselmann, H., Bibl, M., Av, S., Otto, M., Paul, S., Schmidt, B., Klafki, H., Maler, M., Dyrks, T., et al. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00818.x · Cited by 274
Direct and Potent Regulation of γ-Secretase by Its Lipid Microenvironment
Osenkowski, P., Ye, W., Wang, R., Wolfe, M. S., & Selkoe, D. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801925200 · Cited by 271
Increased in Vivo Amyloid-β42 Production, Exchange, and Loss in Presenilin Mutation Carriers
Potter, R., Patterson, B. W., Elbert, D. L., Ovod, V., Kasten, T., Sigurdson, W., Mawuenyega, K., Blazey, T., Goate, A., Chott, R., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3005615 · Cited by 236
Nonsteroidal anti-inflammatory drugs lower Aβ42 and change presenilin 1 conformation
Lleó, A., Berezovska, O., Herl, L. D., Raju, S., Deng, A., Bacskai, B. J., Frosch, M. P., Irizarry, M. C., & Hyman, B. T. (2004) · Nature Medicine · doi:10.1038/nm1112 · Cited by 198
Biophysical Properties of Camelid VHH Domains Compared to Those of Human VH3 Domains
Ewert, S., Cambillau, C., Conrath, K., & Plückthun, A. (2002) · Biochemistry · doi:10.1021/bi011239a · Cited by 184
Freire, E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10118 · Cited by 177
Qualitative changes in human γ-secretase underlie familial Alzheimer’s disease
Szaruga, M., Veugelen, S., Benurwar, M., Lismont, S., Sepulveda-Falla, D., Lleo, A., Ryan, N. S., Lashley, T., Fox, N. C., Murayama, S., et al. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150892 · Cited by 155
Self-citationSato, T., Dohmae, N., Qi, Y. A., Kakuda, N., Misonou, H., Mitsumori, R., Maruyama, H., Koo, E. H., Haass, C., Takio, K., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211161200 · Cited by 150
The amyloid-beta forming tripeptide cleavage mechanism of γ-secretase
Bolduc, D. M., Montagna, D. R., Seghers, M., Wolfe, M. S., & Selkoe, D. J. (2016) · eLife · doi:10.7554/elife.17578 · Cited by 145
Fernandez, M. A., Klutkowski, J. A., Freret, T., & Wolfe, M. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.581165 · Cited by 136
Proteolysis inside the Membrane Is a Rate-Governed Reaction Not Driven by Substrate Affinity
Dickey, S. W., Baker, R. P., Cho, S., & Urban, S. (2013) · Cell · doi:10.1016/j.cell.2013.10.053 · Cited by 124
Okochi, M., Tagami, S., Yanagida, K., Takami, M., Kodama, T. S., Mori, K., Nakayama, T., Ihara, Y., & Takeda, M. (2013) · Cell Reports · doi:10.1016/j.celrep.2012.11.028 · Cited by 123
Effects of Membrane Lipids on the Activity and Processivity of Purified γ-Secretase
Holmes, O. W., Paturi, S., Ye, W., Wolfe, M. S., & Selkoe, D. J. (2012) · Biochemistry · doi:10.1021/bi300303g · Cited by 121
Learning by Failing: Ideas and Concepts to Tackle γ-Secretases in Alzheimer's Disease and Beyond
De Strooper, B., & Chávez Gutiérrez, L. (2015) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124309 · Cited by 119
Familial Alzheimer’s Disease Mutations in Presenilin Generate Amyloidogenic Aβ Peptide Seeds
Veugelen, S., Saito, T., Saido, T. C., Chávez‐Gutiérrez, L., & Strooper, B. D. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.010 · Cited by 107
Self-citationγ-Secretase Associated with Lipid Rafts
Matsumura, N., Takami, M., Okochi, M., Wada‐Kakuda, S., Fujiwara, H., Tagami, S., Funamoto, S., Ihara, Y., & Morishima‐Kawashima, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.510131 · Cited by 103
Winkler, E., Kamp, F., Scheuring, J., Ebke, A., Fukumori, A., & Steiner, H. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.356659 · Cited by 102
Secretion of the Notch-1 Aβ-like Peptide during Notch Signaling
Okochi, M., Fukumori, A., Jiang, J., Itoh, N., Kimura, R., Steiner, H., Haass, C., Tagami, S., & Takeda, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513250200 · Cited by 100
Architectural and thermodynamic principles underlying intramembrane protease function
Baker, R. P., & Urban, S. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1021 · Cited by 98
Moin, S. M., & Urban, S. (2012) · eLife · doi:10.7554/elife.00173 · Cited by 98
Dimitrov, M. I., Alattia, J., Lemmin, T., Lehal, R., Fligier, A., Houacine, J., Hussain, I., Radtke, F., Peraro, M. D., Beher, D., et al. (2013) · Nature Communications · doi:10.1038/ncomms3246 · Cited by 92
Jiang, Q., DeTolla, L. J., Singh, I. S., Gatdula, L., Fitzgerald, B., van Rooijen, N., Cross, A. S., & Hasday, J. D. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.276.6.r1653 · Cited by 83
Olichon, A., Schweizer, D., Muyldermans, S., & de Marco, A. (2007) · BMC Biotechnology · doi:10.1186/1472-6750-7-7 · Cited by 81
Signature Amyloid β Profiles Are Produced by Different γ-Secretase Complexes
Acx, H., Chávez‐Gutiérrez, L., Serneels, L., Lismont, S., Benurwar, M., Elad, N., & Strooper, B. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.530907 · Cited by 79
Self-citationAllosteric Modulation of PS1/γ-Secretase Conformation Correlates with Amyloid β42/40 Ratio
Uemura, K., Lill, C. M., Li, X., Peters, J. A., Ivanov, A., Fan, Z., Strooper, B. D., Bacskai, B. J., Hyman, B. T., & Berezovska, O. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007893 · Cited by 75
Allosteric regulation of γ-secretase activity by a phenylimidazole-type γ-secretase modulator
Takeo, K., Tanimura, S., Shinoda, T., Osawa, S., Zahariev, I. K., Takegami, N., Ishizuka‐Katsura, Y., Shinya, N., Takagi‐Niidome, S., Tominaga, A., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402171111 · Cited by 74
Presenilin-1 adopts pathogenic conformation in normal aging and in sporadic Alzheimer’s disease
Wahlster, L., Arimon, M., Nasser‐Ghodsi, N., Post, K. L., Serrano‐Pozo, A., Uemura, K., & Berezovska, O. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1065-6 · Cited by 72
Li, Y., Lu, S. H.-J., Tsai, C., Böhm, C., Qamar, S., Dodd, R. B., Meadows, W., Jeon, A. H. W., McLeod, A., Chen, F., et al. (2013) · Structure · doi:10.1016/j.str.2013.09.018 · Cited by 63
Substrate ectodomain is critical for substrate preference and inhibition of γ-secretase
Funamoto, S., Sasaki, T., Ishihara, S., Nobuhara, M., Nakano, M., Watanabe‐Takahashi, M., Saito, T., Kakuda, N., Miyasaka, T., Nishikawa, K., et al. (2013) · Nature Communications · doi:10.1038/ncomms3529 · Cited by 60
Self-citationAltered γ‐secretase activity in mild cognitive impairment and Alzheimer's disease
Kakuda, N., Shoji, M., Arai, H., Furukawa, K., Ikeuchi, T., Akazawa, K., Takami, M., Hatsuta, H., Murayama, S., Hashimoto, Y., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200214 · Cited by 58
The dynamic conformational landscape of γ-secretase
Elad, N., Strooper, B. D., Lismont, S., Hagen, W. J. H., Veugelen, S., Arimon, M., Horré, K., Berezovska, O., Sachse, C., & Chávez‐Gutiérrez, L. (2014) · Journal of Cell Science · doi:10.1242/jcs.164384 · Cited by 57
Self-citationAdvances in MALDI and Laser-Induced Soft Ionization Mass Spectrometry
Cramer, R. (2015) · Springer eBooks · doi:10.1007/978-3-319-04819-2 · Cited by 52
Substrate docking to γ-secretase allows access of γ-secretase modulators to an allosteric site
Uemura, K., Farner, K. C., Hashimoto, T., Nasser‐Ghodsi, N., Wolfe, M. S., Koo, E. H., Hyman, B. T., & Berezovska, O. (2010) · Nature Communications · doi:10.1038/ncomms1129 · Cited by 49
Liu, C. Y., Ohki, Y., Tomita, T., Osawa, S., Reed, B., Jagust, W. J., Berlo, V. V., Jin, L., Chui, H. C., Coppola, G., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161203 · Cited by 23
Binding of longer Aβ to transmembrane domain 1 of presenilin 1 impacts on Aβ42 generation
Ohki, Y., Shimada, N., Tominaga, A., Osawa, S., Higo, T., Yokoshima, S., Fukuyama, T., Tomita, T., & Iwatsubo, T. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-7 · Cited by 22
Cholestenoic acid, an endogenous cholesterol metabolite, is a potent γ-secretase modulator
Jung, J. I., Price, A. R., Ladd, T. B., Ran, Y., Park, H.-J., Ceballos‐Diaz, C., Smithson, L. A., Hochhaus, G., Tang, Y., Akula, R., et al. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0021-z · Cited by 21
Svedružić, Ž. M., Popović, K., Smoljan, I., & Jengić, V. Š. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032293 · Cited by 18
Alzheimer’s-causing mutations shift Aβ length by destabilizing γ-secretase-Aβn interactions
Szaruga, M., Munteanu, B., Lismont, S., Veugelen, S., Horré, K., Mercken, M. H., Saido, T. C., Ryan, N. S., Vos, T. D., Savvides, S. N., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.058 · Cited by 15
Self-citationArra, M., Emanuele, E., Martinelli, V. C., Minoretti, P., Bertona, M., & Geroldi, D. (2006) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000096743 · Cited by 10
Whole/Intact Cell MALDI MS Biotyping in Mammalian Cell Analysis
Munteanu, B., & Hopf, C. (2015) · Springer eBooks · doi:10.1007/978-3-319-04819-2_13 · Cited by 5
Self-citationThe dynamic conformational landscape of gamma-secretase
Elad, N., Strooper, B. D., Lismont, S., Hagen, W., Veugelen, S., Arimon, M., Horre, K., Berezovska, O., Sachse, C., & Chavez-Gutierrez, L. (2015) · UCL Discovery (University College London) · Cited by 3
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Scheltens, P., De Strooper, B., Kivipelto, M., Holstege, H., Chételat, G., Teunissen, C. E., Cummings, J., & van der Flier, W. M. (2021) · The Lancet · doi:10.1016/s0140-6736(20)32205-4 · Cited by 5,465
Microglia in Alzheimer’s disease
Hansen, D. V., Hanson, J. E., & Sheng, M. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201709069 · Cited by 1,935
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Domínguez, L., Shea, J., Dokholyan, N. V., Simone, A. D., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 680
Inflammatory Processes in Alzheimer’s Disease—Pathomechanism, Diagnosis and Treatment: A Review
Twarowski, B., & Herbet, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076518 · Cited by 489
Kwart, D., Gregg, A., Scheckel, C., Murphy, E. A., Paquet, D., Duffield, M. D., Fak, J. J., Olsen, O., Darnell, R. B., & Tessier‐Lavigne, M. (2019) · Neuron · doi:10.1016/j.neuron.2019.07.010 · Cited by 327
Metadata
- Authors
- Szaruga, M., Munteanu, B., Lismont, S., Veugelen, S., Horré, K., Mercken, M., Saido, T. C., Ryan, N. S., De Vos, T., Savvides, S. N., Gallardo, R., Schymkowitz, J., Rousseau, F., Fox, N. C., Hopf, C., De Strooper, B., & Chávez-Gutiérrez, L.
- Affiliations
- Technische Hochschule Mannheim (DE)
- VIB-KU Leuven Center for Brain & Disease Research (BE)
- Janssen (Belgium) (BE)
- RIKEN Center for Brain Science (JP)
- University College London (GB)
- Ghent University (BE)
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-07
- Volume
- 170
- Issue
- 3
- Pages
- 443-456.e14
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2742157915
- Cited by
- 248
- References
- 59
- Citations by year
- 2026: 12 · 2025: 15 · 2024: 35 · 2023: 29 · 2022: 27 · 2021: 30 · 2020: 44 · 2019: 32 · 2018: 20 · 2017: 4
- FWCI
- 20.51
- Type
- journal article
- Language
- en
- Update notices
- erratum (2021-04-15)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Ghent University Academic Bibliography (Ghent University) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Lirias (submittedVersion)
- Funders
- European Regional Development Fund
- Agentschap voor Innovatie door Wetenschap en Technologie
- KU Leuven (OT/12/092, METH/14/07)
- European Research Council
- Janssen Pharmaceuticals
- Ministerium für Wissenschaft, Forschung und Kunst Baden-Württemberg
- Herculesstichting (AUGE/11/029)
- Fonds Wetenschappelijk Onderzoek (G074115)
- Deutsche Forschungsgemeinschaft (1S16516N, INST 874/7-1 FUGG, SB/131289)
- Belgian Federal Science Policy Office (P7/16)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, gamma-secretase, presenilin mutations, amyloid precursor protein mutations, temperature dependence of enzyme activity, detergent effects on enzyme activity, Alzheimer's disease prevention
- MeSH terms
- Alzheimer Disease, Animals, Brain, Cell Line, Enzyme Stability, Female, Humans, Membrane Proteins, Models, Molecular, Mutation, Peptide Hydrolases, Endopeptidases, Amyloid beta-Protein Precursor, Mice, Presenilin-1, HEK293 Cells
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
