The DOI matches its Crossref record; 83 of the 83 references it cites were found in a registry or an index.
Aβ-mediated ROS production by Cu ions: Structural insights, mechanisms and relevance to Alzheimer's disease
Abstract
Metal ions are involved in Alzheimer's disease (AD) via their ability to induce aggregation of amyloidogenic peptide and production of Reactive Oxygen Species (ROS), two key events in the development of the pathology. Here, we review very recent results concerning the coordination of Cu(I) and Cu(II) ion to the amyloid-beta peptide, the one encountered in AD. Implications of these structural data for the redox chemistry of the Cu(I/II)-Abeta couple are discussed. The different pathways for the ROS generation by the Cu(I/II)-Abeta species are described. In the more relevant one, reduction of dioxygen is realized by a two-electron process involving two Cu(I) in close vicinity, while the production of the hydroxyl radical from hydrogen peroxide is less constrained. A brief summary of how the Abeta peptide is oxidised during the ROS production is also given. Lastly, the pro- vs. anti-oxidant properties of Abeta are commented on.
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
“For example, it was shown that that metal ions promote Aβ aggregation,16,17 as well as formation of reactive oxygen species (ROS) and lead to oxidative stress.18–20”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [18]
In the citing paper
“as well as lead to formation of reactive oxygen species (ROS) and oxidative stress.3,26–31,33–36”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [35]
In the citing paper
“These metal ions have been shown to affect Aβ aggregation, as well as lead to the formation of reactive oxygen species (ROS).12−16”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [14]
Citations
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
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
Handbook of Chemistry and Physics
(1937) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/20.1.142a · Cited by 4,759
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Copper, iron and zinc in Alzheimer's disease senile plaques
Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120
Hydrogen peroxide mediates amyloid β protein toxicity
Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074
Oxidative Damage Is the Earliest Event in Alzheimer Disease
Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885
Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729
Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357
The metallobiology of Alzheimer's disease
Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315
Huang, X., Atwood, C., Hartshorn, M. A., Multhaup, G., Goldstein, L. E., Scarpa, R. C., Cuajungco, M. P., Gray, D. N., Lim, J. T., Moir, R. D., et al. (1999) · Biochemistry · doi:10.1021/bi990438f · Cited by 1,117
Methionine residues as endogenous antioxidants in proteins
Levine, R. L., Mosoni, L., Berlett, B. S., & Stadtman, E. R. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15036 · Cited by 1,041
Ascorbate regulation and its neuroprotective role in the brain
Rice, M. E. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01543-x · Cited by 835
Allan Butterfield, D. (2002) · Free Radical Research · doi:10.1080/1071576021000049890 · Cited by 786
Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity
Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762
The redox chemistry of the Alzheimer's disease amyloid β peptide
Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608
Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid
Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 587
Butterfield, D. A., Reed, T., Newman, S. F., & Sultana, R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.037 · Cited by 564
Dong, J., Atwood, C., Anderson, V. E., Siedlak, S. L., Smith, M. A., Perry, G. L., & CAREY, P. R. (2003) · Biochemistry · doi:10.1021/bi0272151 · Cited by 560
Hou, L., Shao, H., Zhang, Y., Li, H. L., Menon, N. K., Neuhaus, E. B., Brewer, J. M., Byeon, I. L., Ray, D. G., Vitek, M. P., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja036813f · Cited by 525
Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 494
Suh, Y.-H., & Checler, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.469 · Cited by 476
Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468
Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease
Syme, C. D., Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313572200 · Cited by 459
Isolation of Low‐Molecular‐Weight Proteins from Amyloid Plaque Fibers in Alzheimer's Disease
Selkoe, D. J., Abraham, C. R., Podlisny, M. B., & Duffy, L. K. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb08501.x · Cited by 452
Physiological production of the β-amyloid protein and the mechanism of Alzheimer's disease
Selkoe, D. J. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90008-a · Cited by 423
Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., & Kurt Wüthrich, A. (1998) · Pure and Applied Chemistry · doi:10.1351/pac199870010117 · Cited by 402
Schöneich, C. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.009 · Cited by 372
Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β
Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371
Different Mechanisms of Oxidative Stress and Neurotoxicity for Alzheimer‘s Aβ(1−42) and Aβ(25−35)
Varadarajan, S., Kanski, J., Aksenova, M., Lauderback, C., & Butterfield, D. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010452r · Cited by 346
Causes of oxidative stress in Alzheimer disease
Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336
Metals and Alzheimer's disease
Adlard, P. A., & Bush, A. I. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-102-303 · Cited by 324
Zou, K., Gong, J.-S., Yanagisawa, K., & Michikawa, M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04833.2002 · Cited by 305
Atwood, C., Obrenovich, M. E., Liu, T., Chan, H., Perry, G. L., Smith, M. A., & Martins, R. N. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(03)00174-7 · Cited by 297
Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P. (2007) · ChemBioChem · doi:10.1002/cbic.200700111 · Cited by 273
Self-citationKuo, Y., Kokjohn, T. A., Beach, T. G., Sue, L. I., Brune, D. C., Lopez, J. C., Kalback, W. M., Abramowski, D., Sturchler, C., Staufenbiel, M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007859200 · Cited by 247
Pleomorphic Copper Coordination by Alzheimer’s Disease Amyloid-β Peptide
Drew, S. C., Noble, C. J., Masters, C. L., Hanson, G. R., & Barnham, K. J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja808073b · Cited by 246
Tabner, B. J., El‐Agnaf, O. M. A., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J., & Allsop, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500238200 · Cited by 243
Hou, L., Kang, I., Marchant, R. E., & Zagorski, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200338200 · Cited by 218
Bruce, A. J., Malfroy, B., & Baudry, M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.6.2312 · Cited by 216
Metals ions and neurodegeneration
Molina‐Holgado, F., Hider, R. C., Gaeta, A., Williams, R., & Francis, P. T. (2007) · BioMetals · doi:10.1007/s10534-006-9033-z · Cited by 206
Jiang, D., Men, L., Wang, J., Zhang, Y., Chickenyen, S., Wang, Y., & Zhou, F. (2007) · Biochemistry · doi:10.1021/bi700508n · Cited by 204
Smith, D. P., Ciccotosto, G. D., Tew, D. J., Fodero‐Tavoletti, M. T., Johanssen, T., Masters, C. L., Barnham, K. J., & Cappai, R. (2007) · Biochemistry · doi:10.1021/bi0620961 · Cited by 193
Shearer, J., & Szalai, V. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805940m · Cited by 191
Barnham, K. J., Ciccotosto, G. D., Tickler, A. K., Ali, F. E. A., Smith, D. G., Williamson, N. A., Lam, Y.-H., Carrington, D., Tew, D. J., Kocak, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305494200 · Cited by 191
Oxidation of Cholesterol by Amyloid Precursor Protein and β-Amyloid Peptide
Nelson, T. J., & Alkon, D. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409071200 · Cited by 185
Three Histidine Residues of Amyloid-β Peptide Control the Redox Activity of Copper and Iron
Nakamura, M., Shishido, N., Nunomura, A., Smith, M. A., Perry, G. L., Hayashi, Y., Nakayama, K., & Hayashi, T. (2007) · Biochemistry · doi:10.1021/bi701079z · Cited by 184
NMR Reveals Anomalous Copper(II) Binding to the Amyloid Aβ Peptide of Alzheimer's Disease
Hou, L., & Zagorski, M. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja046032u · Cited by 169
A Molecular Switch in Amyloid Assembly: Met35and Amyloid β-Protein Oligomerization
Bitan, G., Tarus, B., Vollers, S. S., Lashuel, H. A., Condron, M. M., Straub, J. E., & Teplow, D. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0349296 · Cited by 158
Himes, R. A., Park, G. Y., Siluvai, G. S., Blackburn, N. J., & Karlin, K. D. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200803908 · Cited by 148
Why is the amyloid beta peptide of Alzheimer’s disease neurotoxic?
Rauk, A. (2008) · Dalton Transactions · doi:10.1039/b718601k · Cited by 139
Copper, β-amyloid, and Alzheimer's disease: Tapping a sensitive connection
Bush, A. I., Masters, C. L., & Tanzi, R. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2135061100 · Cited by 128
Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2008) · Biochemistry · doi:10.1021/bi8011093 · Cited by 119
Protein aggregation, metals and oxidative stress in neurodegenerative diseases
Tabner, B. J., El-Agnaf, O. M. A., German, M. J., Fullwood, N. J., & Allsop, D. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051082 · Cited by 118
Dikalov, S., Vitek, M. P., & Mason, R. P. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.11.004 · Cited by 110
Schöneich, C., & Williams, T. D. (2002) · Chemical Research in Toxicology · doi:10.1021/tx025504k · Cited by 107
Himes, R. A., Park, G. Y., Barry, A. N., Blackburn, N. J., & Karlin, K. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja0708013 · Cited by 104
The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease.
Streltsov, V., Titmuss, S. J., Epa, V., Barnham, K., Masters, C. L., & Varghese, J. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.134429 · Cited by 103
Synthesis, structure, and reactivity of monomeric two-coordinate copper(I) complexes
Sorrell, T. N., & Jameson, D. L. (1983) · Journal of the American Chemical Society · doi:10.1021/ja00357a009 · Cited by 101
Chemistry and structural studies on the dioxygen-binding copper-1,2-dimethylimidazole system
Sanyal, I., Karlin, K. D., Strange, R. W., & Blackburn, N. J. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00077a027 · Cited by 98
Kowalik-Jankowska, T., Ruta, M., Wiśniewska, K., Łankiewicz, L., & Dyba, M. (2004) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2004.03.001 · Cited by 92
Methionine regulates copper/hydrogen peroxide oxidation products of Aβ
Ali, F. E. A., Separovic, F., Barrow, C. J., Cherny, R. A., Fraser, F. W., Bush, A. I., Masters, C. L., & Barnham, K. J. (2004) · Journal of Peptide Science · doi:10.1002/psc.626 · Cited by 87
Galeazzi, L., Ronchi, P., Franceschi, C., & Giunta, S. (1999) · Amyloid · doi:10.3109/13506129908993282 · Cited by 87
Allsop, D., Mayes, J., Moore, S., Masad, A. A., & Tabner, B. J. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361293 · Cited by 86
Kański, J., Varadarajan, S., Aksenova, M. V., & Butterfield, D. A. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(01)00097-7 · Cited by 83
M35 Oxidation Induces Aβ40-like Structural and Dynamical Changes in Aβ42
Yan, Y., McCallum, S. A., & Wang, C. (2008) · Journal of the American Chemical Society · doi:10.1021/ja711189c · Cited by 63
Toxicity mediated by soluble oligomers of β‐amyloid(1–42) on cholinergic SN56.B5.G4 cells
Heinitz, K., Beck, M., Schliebs, R., & Perez-Polo, J. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04015.x · Cited by 58
Turnbull, S., Tabner, B. J., El‐Agnaf, O. M. A., Twyman, L. J., & Allsop, D. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00510-x · Cited by 54
Attenuated amyloid-β aggregation and neurotoxicity owing to methionine oxidation
Johansson, A., Bergquist, J., Volbracht, C., Päiviö, A., Leist, M., Lannfelt, L., & Westlind‐Danielsson, A. (2007) · Neuroreport · doi:10.1097/wnr.0b013e3280b07c21 · Cited by 53
da Silva, G. F. Z., Tay, W. M., & Ming, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411533200 · Cited by 51
da Silva, G. F. Z., & Ming, L. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604421 · Cited by 50
Clainche, L. L., Giorgi, M., & Reinaud, O. M. (2000) · European Journal of Inorganic Chemistry · doi:10.1002/1099-0682(200009)2000:9 · Cited by 50
Tabner, B. J., Turnbull, S., Fullwood, N. J., German, M. J., & Allsop, D. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330548 · Cited by 47
Baruch-Suchodolsky, R., & Fischer, B. (2008) · Biochemistry · doi:10.1021/bi800114g · Cited by 44
Murakami, K., Hara, H., Masuda, Y., Ohigashi, H., & Irie, K. (2007) · ChemBioChem · doi:10.1002/cbic.200700240 · Cited by 40
Substrate mediated reduction of copper-amyloid-β complex in Alzheimer’s disease
Streltsov, V. A., & Varghese, J. N. (2008) · Chemical Communications · doi:10.1039/b803911a · Cited by 31
Maiti, N. C., Jiang, D., Wain, A. J., Patel, S., Dinh, K. L., & Zhou, F. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp802038p · Cited by 31
Metal Binding and Radical Generation of Proteins in Human Neurological Diseases and Aging
Multhaup, G., & Masters, C. L. (2018) · Routledge eBooks · doi:10.1201/9780203747605-11 · Cited by 29
Is Covalently Crosslinked Aβ Responsible for Synaptotoxicity in Alzheimers Disease?
Naylor, R., Hill, A. F., & Barnham, K. J. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898433 · Cited by 10
Flagged first, then by citations
Cited by
Sorted by citations
Oxidative stress and the amyloid beta peptide in Alzheimer’s disease
Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185
Self-citationCopper–Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity
Elwell, C. E., Gagnon, N. L., Neisen, B. D., Dhar, D., Spaeth, A. D., Yee, G. M., & Tolman, W. B. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00636 · Cited by 723
Bioinorganic Chemistry of Alzheimer’s Disease
Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683
Egorova, K. S., & Ananikov, V. P. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201603777 · Cited by 501
Viles, J. H. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.003 · Cited by 404
Metadata
- Authors
- Hureau, C., & Faller, P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Hureau, Christelle
- Venue
- Biochimie
- Publisher
- Elsevier BV
- Published
- 2009-10
- Volume
- 91
- Issue
- 10
- Pages
- 1212-1217
- ISSN
- 0037-9042 (ISSN-L)
- 0300-9084
- OpenAlex
- W2020526702
- Cited by
- 259
- References
- 83
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 11 · 2023: 7 · 2022: 7 · 2021: 12 · 2020: 13 · 2019: 15 · 2018: 17 · 2017: 23 · 2016: 19 · 2015: 10 · 2014: 17 · 2013: 16 · 2012: 31
- FWCI
- 16.57
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimie (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Keywords
- amyloid-beta, copper ions, reactive oxygen species, Alzheimer's disease, copper coordination, dioxygen reduction, hydroxyl radicals, hydrogen peroxide, metal-peptide interactions, antioxidant activity
- MeSH terms
- Alzheimer Disease, Animals, Copper, Humans, Models, Biological, Signal Transduction, Amyloid beta-Peptides, Reactive Oxygen Species
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