The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
α-Synuclein-positive structures in cases with sporadic Alzheimer’s disease: morphology and its relationship to tau aggregation
Abstract
Alzheimer's disease (AD) and Parkinson's disease share common clinical and pathological features. In this study, we examined the relationship between AD pathology and alpha-synuclein aggregation. The frequency and distribution of alpha-synuclein-positive structures were systematically investigated in 27 cases with sporadic AD by alpha-synuclein immuno-histochemistry. Thirteen (48.2%) of 27 cases had various alpha-synuclein-positive structures as well as Lewy bodies. The frequency and density of senile plaques and neurofibrillary tangles were not significantly different between cases with alpha-synuclein structures and those without. alpha-Synuclein-positive structures were found most frequently in the amygdala. The alpha-synuclein-positive inclusions that are different from Lewy bodies were observed at the highest rate in the hippocampus. The discovery of alpha-synuclein as the constituent of Lewy bodies facilitated the detection of Lewy-related structures even in AD cases with widespread and numerous neurofibrillary tangles. alpha-Synuclein-positive inclusions except for Lewy bodies are exposed, and the distribution of them indicates that Lewy body formation may be influenced by the degree of tau aggregation. This study also supports the suggestion that cases with AD pathology can be classified into two groups according to the existence or absence of alpha-synuclein aggregation.
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
“co-morbid αSyn pathology has been reported in more than half of all autopsy-confirmed AD cases [22–24]”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [24]
In the citing paper
“co-morbid αSyn pathology has been reported in more than half of all autopsy-confirmed AD cases [22–24]”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [24]
Citations
Cites
McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123
Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mirra, S. S., Heyman, A., McKeel, D., Sumi, S. M., Crain, B. J., Brownlee, L. M., Vogel, F. S., Hughes, J. P., Belle, G. V., Berg, L., et al. (1991) · Neurology · doi:10.1212/wnl.41.4.479 · Cited by 4,961
McKeith, I. G., Galasko, D., Kosaka, K., Perry, E. K., Dickson, D. W., Hansen, L. A., Salmon, D. P., Lowe, J., Mirra, S. S., Byrne, E. J., et al. (1996) · Neurology · doi:10.1212/wnl.47.5.1113 · Cited by 3,960
(1998) · Europe PMC (PubMed Central) · Cited by 1,594
HYMAN, B. T., & TROJANOWSKI, J. Q. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199710000-00002 · Cited by 1,542
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,520
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,502
(1964) · The Medical Journal of Australia · doi:10.5694/j.1326-5377.1964.tb115841.x · Cited by 1,411
Cited by
Sorted by citations
Items 101–173 of 173
Pathological substrate of dementia in Parkinson's disease—its relation to DLB and DLBD
Mori, H. (2005) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2005.02.012 · Cited by 24
Vital, A., Canron, M., Gil, R., Hauw, J., & Vital, C. (2007) · Neuropathology · doi:10.1111/j.1440-1789.2007.00755.x · Cited by 23
Novel strategies in Parkinson’s disease treatment: a review
Mitchell, C. L., & Kurouski, D. (2024) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2024.1431079 · Cited by 27
Involvement of the Spinal Cord in Parkinson's Disease
Raudino, F., & Leva, S. (2011) · International Journal of Neuroscience · doi:10.3109/00207454.2011.613551 · Cited by 22
Molecular Therapeutics in Development to Treat Alzheimer’s Disease
Tartaglia, M. C., & Ingelsson, M. (2024) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-024-00738-6 · Cited by 23
Kotarba, S., Kozłowska, M., Scios, M., Saramowicz, K., Barczuk, J., Granek, Z., Siwecka, N., Wiese, W., Golberg, M., Galita, G., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910797 · Cited by 24
Interaction between α-synuclein and tau in Parkinson's disease
Jellinger, K. A. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.10.006 · Cited by 22
Jellinger, K. A. (2007) · Springer eBooks · doi:10.1007/978-0-387-30377-2_15 · Cited by 22
Yamazaki, M., Hasegawa, M., Mori, O., Murayama, S., Tsuchiya, K., Ikeda, K., Chen, K.-M., Katayama, Y., & Oyanagi, K. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000182977.79483.89 · Cited by 21
Self-citationNakagawa, Y., & Yamada, S. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01234-3 · Cited by 20
The role of α-synuclein in neurodegeneration — An update
Jellinger, K. A. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0013-1 · Cited by 19
Park, J., Suh, S. W., Kim, G. E., Lee, S., Kim, J. S., Kim, H. S., Byun, S., Bae, J. B., Kim, J. H., Kim, S. E., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00725-z · Cited by 19
Intrinsic Disorder in Proteins Associated with Neurodegenerative Diseases
Uversky, V. N. (2008) · Focus on structural biology · doi:10.1007/978-1-4020-9434-7_2 · Cited by 20
Jellinger, K. A. (2011) · Neuropathology · doi:10.1111/j.1440-1789.2011.01246.x · Cited by 19
Mattsson, N., Insel, P. S., Tosun, D., Zhang, J., Jack, C. R., Galasko, D. R., Weiner, M. W., & Initiative, A. D. N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0085443 · Cited by 18
Hishikawa, N., Hashizume, Y., Ujihira, N., Okada, Y., Yoshida, M., & Sobue, G. (2003) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2003.00470.x · Cited by 18
Gawor, K., Tomé, S. O., Vandenberghe, R. R., Damme, P. V., Vandenbulcke, M., Otto, M., Arnim, C. A. F. V., Ghebremedhin, E., Ronisz, A., Ospitalieri, S., et al. (2024) · Brain Communications · doi:10.1093/braincomms/fcae442 · Cited by 22
Amyloid-β modulates the phase separation and aggregation of α-synuclein
Röntgen, A., Toprakcioglu, Z., Morris, O. M., & Vendruscolo, M. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2501987122 · Cited by 20
Lau, V. Z., Awogbindin, I. O., Frenkel, D., Whitehead, S. N., & Tremblay, M. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70363 · Cited by 16
Neubauer, A., Weissenbrunner, D., Pekrun, S., Roeber, S., Ruf, V. C., Feyen, P. L. C., Strübing, F., & Herms, J. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02952-w · Cited by 17
Hepta-Histidine Inhibits Tau Aggregation
Kondo, K., Ikura, T., Tanaka, H., Fujita, K., Takayama, S., Yoshioka, Y., Tagawa, K., Homma, H., Liu, S., Kawasaki, R., et al. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00164 · Cited by 12
Structural and Conformational Prerequisites of Amyloidogenesis
Uversky, V. N., Fernández, A., & Fink, A. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_1 · Cited by 12
Manabe, T., Katayama, T., Sato, N., Kudo, T., Matsuzaki, S., Imaizumi, K., & Tohyama, M. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00370-1 · Cited by 12
Tau expression and phosphorylation in enteroendocrine cells
Chapelet, G., Béguin, N., Castellano, B., Grit, I., de Coppet, P., Oullier, T., Neunlist, M., Blottière, H. M., Rolli‐Derkinderen, M., Dréan, G. L., et al. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1166848 · Cited by 13
Impact of α-Synuclein Pathology on Aging
Parkkinen, L. (2005) · Cited by 11
Cong, C., Zhang, W., Qian, X., Qiu, W., & Ma, C. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201548 · Cited by 10
Mak, E., Przybelski, S. A., Wiste, H. J., Fought, A. J., Schwarz, C. G., Senjem, M. L., Jack, C. R., Lowe, V. J., Petersen, R. C., Boeve, B. F., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.14571 · Cited by 9
Yilmaz, S. N., Steiner, K., Marksteiner, J., Faserl, K., Villunger, M., Sarg, B., & Humpel, C. (2024) · Biomolecules · doi:10.3390/biom14101326 · Cited by 9
Insoluble α-synuclein in alzheimer’s disease without lewy body formation
Broe, M., Shepherd, C. E., Mann, D. M. A., Milward, E. A., Gai, W. P., Thiel, E., & Halliday, G. M. (2005) · Neurotoxicity Research · doi:10.1007/bf03033777 · Cited by 9
Pande, R., Huang, Y., Teeple, E. A., Joshi, P. K., Flores‐Morales, A., Latta‐Mahieu, M., Sardi, S. P., Cedazo-Mı́nguez, Á., Klinger, K. W., Madden, S. L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.06.442950 · Cited by 9
Readman, M. R., Wan, F., Fairman, I., Linkenauger, S. A., Crawford, T. J., & Plack, C. J. (2023) · Brain Sciences · doi:10.3390/brainsci13081196 · Cited by 8
Ding, Y., Wang, L., Liu, J., Deng, Y., Jiao, Y., & Zhao, A. (2025) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2024.100040 · Cited by 8
Beyond amyloid plaque, targeting α-synuclein in Alzheimer disease: The battle continues
Al-Kuraishy, H. M., Sulaiman, G. M., Mohammed, H. A., Al-Gareeb, A. I., Albuhadily, A. K., Ali, A. A., & Abu-Alghayth, M. H. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102684 · Cited by 10
Identification of Multicolor Fluorescent Probes for Heterogeneous Aβ Deposits in Alzheimer’s Disease
Mukherjee, A., Al‐Lahham, R., Corkins, M. E., Samanta, S., Schmeichel, A. M., Singer, W., Low, P. A., Govindaraju, T., & Soto, C. A. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.802614 · Cited by 8
Winkel, I., Ermann, N., Żelwetro, A., Sambor, B., Mroczko, B., Kornhuber, J., Paradowski, B., & Lewczuk, P. (2021) · Journal of Neural Transmission · doi:10.1007/s00702-021-02351-x · Cited by 7
A glimpse into the structural properties of α‐synuclein oligomers
Santos, J., Pallarès, I., & Ventura, S. (2023) · BioFactors · doi:10.1002/biof.2021 · Cited by 7
Mroczek, K. H., Fernando, S., Fisher, P. R., & Annesley, S. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.741662 · Cited by 8
Démences : où sont les corps de Lewy ?
Lebouvier, T., Delrieu, J., Evain, S., Pallardy, A., Sauvaget, A., Letournel, F., Chevrier, R., Lepetit, M., Vercelletto, M., Boutoleau‐Bretonnière, C., et al. (2013) · Revue Neurologique · doi:10.1016/j.neurol.2013.05.004 · Cited by 7
Holec, S. A. M., Lee, J., Khedmatgozar, C. R., Wojewska, M. J., Oehler, A., Halliday, G. M., Gentleman, S., & Woerman, A. L. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02093-x · Cited by 6
Wu, J., Geng, C., Liu, L., & Tang, Y. (2025) · Medicine Plus · doi:10.1016/j.medp.2025.100112 · Cited by 8
Alpha‐Synuclein Demonstrates Varying Binding Affinities With Different Tau Isoforms
Fischer, A., Schmitz, M., Thom, T., Zafar, S., Younas, N., Correia, S., Correia, A. D. S., Canaslan, S., & Zerr, I. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70053 · Cited by 6
Zhiyan, C., Min, Z., Yida, D., He, C., Hu, X., Yutong, L., Huan, W., & Sun, L. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1424803 · Cited by 5
Tau and its interactions with other proteins in neurodegenerative diseases
Mroczek, K. H., Annesley, S. J., & Fisher, P. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815950-7.00028-x · Cited by 5
Stehouwer, J. S., Huang, G., Guarino, D. S., Debnath, M. L., Polu, A., Geib, S. J., Lopresti, B. J., Ikonomović, M. D., Mason, N. S., Mach, R. H., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02988 · Cited by 4
Uchida, K., Morikawa, K., Muguruma, Y., Hosokawa, M., Tsutsumiuchi, K., Kaneda, D., Hashizume, Y., Akatsu, H., & Inoue, K. (2021) · Journal of Chromatography B · doi:10.1016/j.jchromb.2021.122885 · Cited by 4
Nazeen, S., Wang, X., Zielinski, D., Lam, I., Hallacli, E., Xu, P., Ethier, E., Strom, R., Zanella, C. A., Nithianandam, V., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.03.583145 · Cited by 5
Mesentier-Louro, L. A., Goldman, C., Gaese, S., Buonfiglioli, A., Kyriakis, D., Harlock, A., Ndayisaba, A., Sartori, E. R., Uchitelev, A., Fullard, J. F., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.09.637107 · Cited by 4
Lin, X., Guo, Y., Dong, R., Wang, B., & Bi, Y. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.935869 · Cited by 3
Aggregation and properties of α‒synuclein and related proteins
El‐Agnaf, O. M. A., & Irvine, G. B. (2001) · Journal of Spectroscopy · doi:10.1155/2001/939274 · Cited by 3
Jellinger, K. A., & Krismer, F. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0687-7_4 · Cited by 3
Rierola, M., Trushina, N. I., Monteiro-Abreu, N., Conze, C., Holtmannspötter, M., Kurre, R., Holzer, M., Arendt, T., Heinisch, J. J., Brandt, R., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.09.495530 · Cited by 4
PolyGR-containing aggregates link with pathology and clinical features of Alzheimer’s disease
Phuong, H. T., Tomas, R. F., Akmese, C., Mijares, A. M. P., Gerstin, I. M., Guo, S., Bell, L. R., Ellwood, R., Yegorova, S., Ng, S. K., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02954-8 · Cited by 2
Mak, E., Przybelski, S. A., Reid, R. I., Wiste, H. J., Fought, A. J., Schwarz, C. G., Senjem, M. L., Vemuri, P., Jack, C. R., Lowe, V. J., et al. (2026) · Alzheimer s Research & Therapy · doi:10.1186/s13195-026-01995-9 · Cited by 3
Wang, Q.-Q., Sun, Q.-Q., Guo, Y.-S., Yin, S., & Zhou, J. (2026) · Translational Neurodegeneration · doi:10.1186/s40035-026-00571-3 · Cited by 2
Cholesterol dysregulation in APOE4 astrocytes promotes α-synuclein pathology in miBrains
Mesentier-Louro, L. A., Goldman, C., Gaese, S., Buonfiglioli, A., Kyriakis, D., Harlock, A., Ndayisaba, A., Sartori, E. R., Uchitelev, A., Fullard, J. F., et al. (2026) · Cell stem cell · doi:10.1016/j.stem.2026.08.001 · Cited by 6
Gawor, K., Tomé, S. O., Vandenberghe, R. R., Damme, P. V., Vandenbulcke, M., Otto, M., Arnim, C. A. F. V., Ghebremedhin, E., Ronisz, A., Ospitalieri, S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.21.599515 · Cited by 2
Silva‐Lucero, M., Rivera‐Osorio, J., Gomez‐Virgilio, L., López-Toledo, G., Luna‐Muñoz, J., Montiel-Sosa, J. F., Soto-Rojas, L. O., Pacheco‐Herrero, M., & Cárdenas‐Aguayo, M. D. C. (2022) · Diagnostics · doi:10.3390/diagnostics12051165 · Cited by 1
Differential risk of Alzheimer's disease in MCI subjects with elevated Abeta
Zhou, B., & Fukushima, M. (2024) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2024.123319 · Cited by 1
Kim, H., Lee, H. J., Shin, D.-J., Lee, Y., Noh, Y., & Park, K. H. (2019) · Journal of Sleep Medicine · doi:10.13078/jsm.190046 · Cited by 1
Genetics of Atypical Parkinsonism
Gasser, T. (2005) · Humana Press eBooks · doi:10.1385/1-59259-834-x:139 · Cited by 1
Biomarkers and Surrogate Markers in Drug Development
Cutler, N. R., Sramek, J. J., Murphy, M. F., Riordan, H., Bieck, P. R., & Carta, A. (2010) · Wiley eBooks · doi:10.1002/9781444318579.ch4
Anti-Aging Medicine LiteratureWatch
Pawelec, G. (1998) · Rejuvenation Research · doi:10.1089/rej.1.1998.1.275
Joppe, K. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8016
Mitsuyama, Y. (2019) · Kyushu Neuropsychiatry · doi:10.11642/kyushuneurop.65.3_4_113
Anti-Aging Medicine LiteratureWatch
(2001) · Rejuvenation Research · doi:10.1089/10945450152466215
Brain cross-omics integration in Alzheimer’s diseasePreprint
Eteleeb, A. M., Novotny, B. C., Soriano‐Tárraga, C., Sohn, C., Dhungel, E., Brase, L., Nallapu, A., Buss, J., Farias, F., Bergmann, K., et al. (2022) · medRxiv · doi:10.1101/2022.12.10.22283295
Synaptotoxic forms of amyloid-β and α-synuclein act through a common pathwayPreprint
Ribé, E. M., Ghosh, A., Pasławski, W., Savory, K., Ballard, C. G., Morin, P., Cash, D., Hirth, F., Williams, G. H., Svenningsson, P., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.13.638131
Martínez-Valbuena, I., Valenti‐Azcarate, R., Villegas, I. A., Marcilla, I., Marti-Andres, G., Caballero, M.-C., Riverol, M., Tuñon, M.-T., Fraser, P. E., & Luquin, M.-R. (2021) · Figshare · doi:10.6084/m9.figshare.14391481
Thornton, J. M., & Stevenson, J. L. (2026) · Journal of Alzheimer s Disease · doi:10.1177/13872877251412923
Carvalho, F., Maximiano, P., Hashemi, M., & Simões, P. N. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.29.702600
Alpha‐synuclein co‐pathology in a real‐world early Alzheimer's disease cohort
Shiner, T., Nathan, T., Levy, M. H., David, A. B., Omer, N., Awad, A. A., Ash, E. L., Gana‐Weisz, M., Goldstein, O., Alcalay, Y., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71240
Étude de la propagation prion-like de l'alpha-synucléine dans des réseaux de neurones reconstruits
Courte, J. (2019) · theses.fr (ABES) · doi:10.70675/95ccfbd6zedb2z4a1bz8024zb46a3ec60ebf
When Pathologies Collide: The Intersection of Tau and Alpha-Synuclein in Neurodegenerative Diseases
Hunt, J. N., & Kortagere, S. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-06163-6
Metadata
- Authors
- Arai, Y., Yamazaki, M., Mori, O., Muramatsu, H., Asano, G., & Katayama, Y.
- Affiliations
- Nippon Medical School (JP)
- Corresponding author
- Yamazaki, Mineo
- Venue
- Brain Research
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 888
- Issue
- 2
- Pages
- 287-296
- ISSN
- 0006-8993 (ISSN-L)
- OpenAlex
- W2072878433
- Cited by
- 173
- References
- 35
- Citations by year
- 2026: 7 · 2025: 16 · 2024: 11 · 2023: 8 · 2022: 13 · 2021: 13 · 2020: 7 · 2019: 8 · 2018: 2 · 2016: 4 · 2014: 6 · 2013: 5 · 2012: 2
- FWCI
- 5.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- alpha-synuclein, sporadic Alzheimer's disease, Lewy bodies, tau aggregation, neurofibrillary tangles, amyloid plaques, amygdala, hippocampus, Alzheimer's disease classification
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Brain, Inclusion Bodies, Female, Humans, Immunohistochemistry, Male, Middle Aged, Nerve Tissue Proteins, Neurites, Neurofibrillary Tangles, tau Proteins, Microscopy, Confocal, Synucleins, alpha-Synuclein, Plaque, Amyloid
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
