The DOI matches its Crossref record; 69 of the 71 references it cites were found in a registry or an index.
Oligomeric and Fibrillar Species of Amyloid-β Peptides Differentially Affect Neuronal Viability
Open accessAbstract
Genetic evidence predicts a causative role for amyloid-beta (A beta) in Alzheimer's disease. Recent debate has focused on whether fibrils (amyloid) or soluble oligomers of A beta are the active species that contribute to neurodegeneration and dementia. We developed two aggregation protocols for the consistent production of stable oligomeric or fibrillar preparations of A beta-(1-42). Here we report that oligomers inhibit neuronal viability 10-fold more than fibrils and approximately 40-fold more than unaggregated peptide, with oligomeric A beta-(1-42)-induced inhibition significant at 10 nm. Under A beta-(1-42) oligomer- and fibril-forming conditions, A beta-(1-40) remains predominantly as unassembled monomer and had significantly less effect on neuronal viability than preparations of A beta-(1-42). We applied the aggregation protocols developed for wild type A beta-(1-42) to A beta-(1-42) with the Dutch (E22Q) or Arctic (E22G) mutations. Oligomeric preparations of the mutations exhibited extensive protofibril and fibril formation, respectively, but were not consistently different from wild type A beta-(1-42) in terms of inhibition of neuronal viability. However, fibrillar preparations of the mutants appeared larger and induced significantly more inhibition of neuronal viability than wild type A beta-(1-42) fibril preparations. These data demonstrate that protocols developed to produce oligomeric and fibrillar A beta-(1-42) are useful in distinguishing the structural and functional differences between A beta-(1-42) and A beta-(1-40) and genetic mutations of A beta-(1-42).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“In addition, the MOAB-2-based oA42 ELISA detects oligomeric but not monomeric A42 using synthetic preparations characterized previously by our laboratory (data not shown) (47,48).”
From APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease (2012) · cites this paper as [47]
In the citing paper
“The 48 h total incubation leads to mature Aβ42 fibrils, as observed by TEM (Figure 10, panel a) while the Western blot shows the presence of higher order Aβ42 oligomers (Figure 10, lane a), likely due to an assembly-disassembly equilibrium that is established for mature Aβ fibrils.89–91”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [90]
In the citing paper
“However, this approach may not be optimal for the Aβ42 peptide, given the increased toxicity observed for the soluble Aβ42 oligomers.90”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [90]
In the citing paper
“Finally, in neurons, PCSK9 overexpression led to a worsening of neurotoxicity induced by different aggregation forms of Aβ, which have previously been demonstrated to have toxic effects in these cells [31,52].”
From PCSK9 affects astrocyte cholesterol metabolism and reduces neuron cholesterol supplying in vitro: potential implications in Alzheimer’s disease (2022) · cites this paper as [52]
In the citing paper
“All A preparations used were similar to those characterized previously (24) in that they contain monomers and oligomers of A but do not contain fibrils (see supplemental Fig. 1, A and B).”
From Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E (2007) · cites this paper as [24]
Citations
Cites
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
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
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Self-citationNeurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
Saudou, F., Finkbeiner, S. M., Devys, D., & Greenberg, M. E. (1998) · Cell · doi:10.1016/s0092-8674(00)81782-1 · Cited by 1,598
Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530
Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399
Holcomb, L., Gordon, M. N., McGowan, E., Yu, X., Benkovic, S., Jantzen, P., Wright, K., Saad, I., Mueller, R., Morgan, D., et al. (1998) · Nature Medicine · doi:10.1038/nm0198-097 · Cited by 1,386
Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.
Lorenzo, A., & Yankner, B. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.25.12243 · Cited by 1,324
Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline
Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,156
Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?
Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989
Ataxin-1 Nuclear Localization and Aggregation
Klement, I. A., Skinner, P. J., Kaytor, M. D., Yi, H. L., Hersch, S. M., Clark, H. B., Zoghbi, H. Y., & Orr, H. T. (1998) · Cell · doi:10.1016/s0092-8674(00)81781-x · Cited by 956
Tauopathy in Drosophila : Neurodegeneration Without Neurofibrillary Tangles
Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939
In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity
Pike, C. J., Walencewicz, A. J., Glabe, C. G., & Cotman, C. W. (1991) · Brain Research · doi:10.1016/0006-8993(91)91553-d · Cited by 841
Hartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & Selkoe, D. J. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 817
Alzheimer's Disease: A Central Role for Amyloid
Selkoe, D. J. (1994) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199409000-00003 · Cited by 752
Hendriks, L., van Duijn, C. M., Cras, P. P., Cruts, M., Hul, W. V., van Harskamp, F., Warren, A., McInnis, M. G., Antonarakis, S. E., Martin, J., et al. (1992) · Nature Genetics · doi:10.1038/ng0692-218 · Cited by 741
Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 699
Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 690
Moechars, D., Dewachter, I., Lorent, K., Reversé, D., Baekelandt, V., Naidu, A., Tesseur, I., Spittaels, K., Haute, C. V. D., Checler, F., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6483 · Cited by 668
Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains
Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618
Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease
Lansbury, P. T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3342 · Cited by 557
Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527
Grabowski, T. J., Cho, H. S., Vonsattel, J. P. G., Rebeck, G. W., & Greenberg, S. M. (2001) · Annals of Neurology · doi:10.1002/ana.1009 · Cited by 523
Roher, A. E., Chaney, M. O., Kuo, Y., Webster, S. D., Stine, W. B., Haverkamp, L. J., Woods, A. S., Cotter, R. J., Tuohy, J. M., Krafft, G. A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20631 · Cited by 494
Amyloid β Protein Precursor Gene and Hereditary Cerebral Hemorrhage with Amyloidosis (Dutch)
Broeckhoven, C. V., Haan, J., Bakker, E., Hardy, J., Hul, W. V., Wehnert, A., der Vlis, M. V.-V., & Roos, R. A. C. (1990) · Science · doi:10.1126/science.1971458 · Cited by 475
Amyloid β Protein Enhances the Survival of Hippocampal Neurons in Vitro
Whitson, J. S., Selkoe, D. J., & Cotman, C. W. (1989) · Science · doi:10.1126/science.2928783 · Cited by 469
Chui, D.-H., Tanahashi, H., Ozawa, K., Ikeda, S., Checler, F., Ueda, O., Suzuki, H., Araki, W., Inoue, H., Shirotani, K., et al. (1999) · Nature Medicine · doi:10.1038/8438 · Cited by 364
Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352
Self-citationVaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349
Self-citationGenetic Classification of Primary Neurodegenerative Disease
Hardy, J., & Gwinn, K. A. (1998) · Science · doi:10.1126/science.282.5391.1075 · Cited by 343
Haass, C., Hung, A. Y., Selkoe, D. J., & Teplow, D. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32503-6 · Cited by 319
Cummings, B. J., Pike, C. J., Shankle, R., & Cotman, C. W. (1996) · Neurobiology of Aging · doi:10.1016/s0197-4580(96)00170-4 · Cited by 305
Pathogenic Effects of D23N Iowa Mutant Amyloid β-Protein
Nostrand, W. E. V., Melchor, J. P., Cho, H. S., Greenberg, S. M., & Rebeck, G. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104135200 · Cited by 249
Wısnıewskı, T., Ghiso, J. A., & Frangione, B. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91706-i · Cited by 248
Miravalle, L., Tokuda, T., Chiarle, R., Giaccone, G., Bugiani, O., Tagliavini, F., Frangione, B., & Ghiso, J. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003154200 · Cited by 237
Kienlen-Campard, P., Miolet, S., Tasiaux, B., & Octave, J.-N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200887200 · Cited by 187
Contribution of somal Lewy bodies to neuronal death
Tompkins, M. M., & Hill, W. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00874-3 · Cited by 185
Podlisny, M. B., Walsh, D. M., Amarante, P., Ostaszewski, B. L., Stimson, E. R., Maggio, J. E., Teplow, D. B., & Selkoe, D. J. (1998) · Biochemistry · doi:10.1021/bi972029u · Cited by 185
β-Amyloid protein promotes neuritic branching in hippocampal cultures
Whitson, J. S., Glabe, C. G., Shintani, E., Abcar, A. C., & Cotman, C. W. (1990) · Neuroscience Letters · doi:10.1016/0304-3940(90)90867-9 · Cited by 185
Enhanced pathologic properties of Dutch-type mutant amyloid beta-protein.
Davis, J., & Nostrand, W. E. V. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2996 · Cited by 182
Ji, Z.-S., Miranda, R. D., Newhouse, Y. M., Weisgraber, K. H., Huang, Y., & Mahley, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112109200 · Cited by 177
Ward, R. V., JENNINGS, K. H., Jepras, R., Neville, W. A., OWEN, D. E., HAWKINS, J., Christie, G., Davis, J. B., George, A. R., Karran, E. H., et al. (2000) · Biochemical Journal · doi:10.1042/bj3480137 · Cited by 153
Jonghe, C. D., Zehr, C., Yager, D., Prada, C.-M., Younkin, S. G., Hendriks, L., Broeckhoven, C. V., & Eckman, C. B. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0202 · Cited by 151
Charge Alterations of E22 Enhance the Pathogenic Properties of the Amyloid β‐Protein
Melchor, J. P., McVoy, L., & Nostrand, W. E. V. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0742209.x · Cited by 125
Protofibrils, the unifying toxic molecule of neurodegenerative disorders?
Haass, C., & Steiner, H. (2001) · Nature Neuroscience · doi:10.1038/nn0901-859 · Cited by 98
Oligomerization and fibril assembly of the amyloid-β protein
Roher, A. E., Baudry, J. Y., Chaney, M. O., Kuo, Y., Stine, W. B., & Emmerling, M. R. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00030-2 · Cited by 89
Clements, A., Walsh, D. M., Williams, C. H., & Allsop, D. (1993) · Neuroscience Letters · doi:10.1016/0304-3940(93)90129-9 · Cited by 83
Oligomerization of β-amyloid of the Alzheimer’s and the Dutch-cerebral-haemorrhage types
SIAN, A. K., Frears, E. R., El‐Agnaf, O. M. A., PATEL, B. P., Manca, M. F., Siligardi, G., Hussain, R., & Austen, B. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3490299 · Cited by 61
Sajithlal, G. B., Huttunen, H. J., Rauvala, H., & Münch, G. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107627200 · Cited by 56
Mbebi, C., Sée, V., Mercken, L., Pradier, L., Müller, U., & Loeffler, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107948200 · Cited by 53
Connections, Cognition and Alzheimerʼs Disease
Hyman, B. T., Duyckaerts, C. J., Christen, Y., & Geula, C. (1998) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-199809000-00020 · Cited by 39
Aksenova, M. V., Aksenov, M. Y., Butterfield, D. A., & Carney, J. M. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(96)12717-8 · Cited by 39
Demeester, N., Mertens, C., Caster, H., Goethals, M., Vandekerckhove, J. S., Rosseneu, M., & Labeur, C. (2001) · European Journal of Neuroscience · doi:10.1046/j.0953-816x.2001.01579.x · Cited by 38
Forloni, G., Lucca, E., Angeretti, N., Torre, P. D., & Salmona, M. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69052048.x · Cited by 35
El‐Agnaf, O. M. A., Guthrie, D. J. S., Walsh, D. M., & Irvine, G. B. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2560560.x · Cited by 31
An honorable compromise regarding amyloid in Alzheimer disease
Terry, R. D. (2001) · Annals of Neurology · doi:10.1002/ana.1042 · Cited by 26
Monji, A., Tashiro, K., Yoshida, I., Kaname, H., Hayashi, Y., Matsuda, K., & Tashiro, N. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00273-6 · Cited by 23
Reduced Neuronal Activity is One of the Major Hallmarks of Alzheimer’s Disease
Swaab, D. F., Lucassen, P. J., van de Nes, J. A. P., Ravid, R., & Salehi, A. (1997) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-642-60680-9_7 · Cited by 4
Flagged first, then by citations
2 of the 71 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Aβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways
Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,316
Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168
Demuro, A., Mina, E. W., Kayed, R., Milton, S. C. F., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,057
Metadata
- Authors
- Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J.
- Affiliations
- Northwestern University (US)
- Corresponding author
- LaDu, Mary Jo
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-08
- Volume
- 277
- Issue
- 35
- Pages
- 32046-32053
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2168025729
- Cited by
- 1,452
- References
- 71
- Citations by year
- 2026: 25 · 2025: 33 · 2024: 40 · 2023: 46 · 2022: 45 · 2021: 47 · 2020: 49 · 2019: 55 · 2018: 65 · 2017: 58 · 2016: 61 · 2015: 70 · 2014: 78 · 2013: 86 · 2012: 86
- FWCI
- 22.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- amyloid-beta, amyloid-beta oligomers, amyloid fibrils, Alzheimer's disease, neuronal viability, peptide aggregation, protofibrils, neurotoxicity
- MeSH terms
- Alzheimer Disease, Cell Survival, Humans, Neuroblastoma, Neurons, Peptide Fragments, Tumor Cells, Cultured, Amyloid beta-Peptides, Microscopy, Atomic Force
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