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
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–262 of 262
Interactions of pyridinecarboxylic acid chelators with brain metal ions: Cu(II), Zn(II), and Al(III)
Sija, É., Dean, A., Jakusch, T., Marco, V. D., Venzo, A., & Kiss, T. (2011) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-011-0482-x · Cited by 8
Vafaeezadeh, M., Hashemi, M. M., & Ghavidel, N. (2016) · RSC Advances · doi:10.1039/c5ra20179a · Cited by 8
The Hair Cycle and Its Relation to Nutrition
Trüeb, R. M. (2020) · Springer eBooks · doi:10.1007/978-3-030-59920-1_4 · Cited by 7
Lee, S., Dagar, A., Cho, I., Kim, K., Park, I. W., Yoon, S., Cha, M., Shin, J., Kim, H. Y., Kim, I., et al. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.2c00788 · Cited by 7
Bin, Y., Jiang, Z., & Xiang, J. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1512-7 · Cited by 7
He, K., Li, X., Ye, X., Yuan, L., Li, X., Chen, X., & Deng, Y. (2012) · Food Research International · doi:10.1016/j.foodres.2012.04.010 · Cited by 7
Hu, R., Xiao, Z., Qiao, M., Liu, C., Wu, G., Wang, Y., Huang, Z., & Dong, M. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13318 · Cited by 6
Lesiów, M. K., & Krupa, K. (2021) · New Journal of Chemistry · doi:10.1039/d1nj00617g · Cited by 4
Behar, A. E., Sabater, L., Baskin, M., Hureau, C., & Maayan, G. (2021) · Angewandte Chemie · doi:10.1002/ange.202109758 · Cited by 4
Self-citationKim, D., Bang, J. K., & Kim, S. H. (2014) · Angewandte Chemie · doi:10.1002/ange.201410389 · Cited by 4
Kim, D., Kim, N. H., & Kim, S. H. (2012) · Angewandte Chemie · doi:10.1002/ange.201208108 · Cited by 4
Redox Status and Aging Link in Neurodegenerative Diseases 2015
de la Cruz, V. P., Sathyasaikumar, K. V., & Pedraza‐Chaverrí, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/494316 · Cited by 5
Tomasello, M. F., Di Rosa, M. C., Naletova, I., Sciacca, M. F. M., Giuffrida, A., Maccarrone, G., & Attanasio, F. (2025) · Bioinorganic Chemistry and Applications · doi:10.1155/bca/4226220 · Cited by 3
Zonzin, M., Chianese, M., Squarcina, A., Dereje, D. M., Campofelice, A., Fermo, A. D., Belluti, F., Marino, N., Dębicki, F., Kotynia, A., et al. (2025) · Molecules · doi:10.3390/molecules30163419 · Cited by 3
Antioxidant promotion of tyrosine nitration in the presence of copper(ii)
Qiao, L., Liu, B., & Girault, H. H. (2013) · Metallomics · doi:10.1039/c3mt00048f · Cited by 3
Green, K. N., Johnston, H. M., Burnett, M. E., & Brewer, S. M. (2016) · Comments on Inorganic Chemistry · doi:10.1080/02603594.2016.1241616 · Cited by 3
Recent Advances in the Quest for Treatment and Management of Alzheimer and Other Dementia
Tanwir, S. E., & Kumar, A. (2019) · Open Journal of Medicinal Chemistry · doi:10.4236/ojmc.2019.91001 · Cited by 3
Copper Complexation by Peptides Implicated in Neurodegenerative Diseases
Dorlet, P., & Hureau, C. (2020) · Springer eBooks · doi:10.1007/978-3-030-39668-8_4 · Cited by 3
Self-citationSun, B., & Jiang, H. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112636 · Cited by 2
Fusobacterium nucleatum’s Copper-FomA Proteins: Driving Cancer Forward
Lesiów, M. K., Kwiatkowski, B., Pietrzyk, P., Kyzioł, A., Rolka, K., & Komarnicka, U. K. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c01747 · Cited by 2
Metal ions and beta amyloid: conformational modifications and biological aspects
Granzotto, A., & Zatta, P. F. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_7 · Cited by 2
Proteome analyses of human macrophages exposed to low cytotoxic IC90 copper (2+) ions
Taira, M., Shimoyama, Y., Kagiya, T., Sasaki, M., Nezu, T., Harada, H., & Kimura, S. (2011) · Dental Materials Journal · doi:10.4012/dmj.2010-088 · Cited by 2
Zhao, J., Ma, B., & Nussinov, R. (2016) · Israel Journal of Chemistry · doi:10.1002/ijch.201600093 · Cited by 2
Joo, J. O., Kim, I. H., & Oh, B. (2014) · KSBB Journal · doi:10.7841/ksbbj.2014.29.3.139 · Cited by 2
Mathenge, S. G. (2014) · Cited by 2
Sources of ROS Species an Its Harmful and Benefical Effects on Human HealthPreprint
Munir, S. (2021) · Preprints.org · doi:10.20944/preprints202101.0606.v1 · Cited by 2
Design of non-aggregating variants of Aβ peptide
Caine, J. M., Churches, Q. I., Waddington, L. J., Nigro, J., Breheney, K., Masters, C. L., Nuttall, S. D., & Streltsov, V. A. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.09.102 · Cited by 1
Essential trace metals in health and disease
Makević, V., Luka, S. R. D., & Ilić, A. Ž. (2023) · Medicinski podmladak · doi:10.5937/mp74-43573 · Cited by 1
Li, H., Yin, Z., Cui, F., Wang, W., & Zhang, D. (2025) · Frontiers in Nutrition · doi:10.3389/fnut.2025.1461852 · Cited by 1
Small Molecule Inhibitors for Amyloid Aggregation
Thomas, A., Kaur, G., Ali, R., & Verma, S. K. (2021) · doi:10.1002/9783527811014.ch6 · Cited by 1
Cytochrome c as a distinct modulator of amyloid-beta amyloidogenesis in a peroxide-dependent mannerPreprint
Du, Z., Nam, E., Lin, Y., Hong, M., Molnár, T., Kondo, I., Ishimori, K., Baik, M., Lee, Y., & Lim, M. H. (2022) · ChemRxiv · doi:10.26434/chemrxiv-2022-3h55t · Cited by 1
The role of cyclophilin D in mitochondrial calcium homeostasis in adult neurons.
Barsukova, A. G. (2009) · doi:10.6083/m4fq9tk2
Coordination of Metal Ions to β-Amyloid Peptide: Impact on Alzheimer’s Disease
Faller, P., Penna, G. L., Hureau, C., & Furlan, S. (2013) · Modecular medicine and medicinal · doi:10.1142/9781848167551_0004
Self-citationSzereszewski, K. E. (2019) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2019-13837
BIOSORPTION OF Ag+, Cu2+ AND Fe3+ BY GELLAN GUM
Othman, S. E., El-Saadany, S. S., Labieb, S., & Hefnawy, T. H. (2017) · Zagazig Journal of Agricultural Research · doi:10.21608/zjar.2017.52255
Nam, G., Yi, Y., Lee, H. J., Lee, J., Kang, J., & Lim, M. H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14902-9
Interactions of pyridinecarboxylic acid chelators with brain metal ions: Cu(II), Zn(II), and Al(III)
Sija, É., Dean, A., Jakusch, T., Marco, V. D., Venzo, A., & Kiss, T. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_17
Delsuc, N., Hammouda, Y. B. H., Coulibaly, K., Bathily, A., Han, M. T. S., & Policar, C. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4139609
Santis, E. D., Alleva, S., Minicozzi, V., Morante, S., & Stellato, F. (2024) · ChemPlusChem · doi:10.1002/cplu.202300712 · Cited by 2
Jawad, M. J., Uthirapathy, S., Altalbawy, F. M. A., Oghenemaro, E. F., Rizaev, J. A., Lal, M., Eldesoqui, M. B., Sharma, N., Pramanik, A., & AL-Hamairy, A. K. (2024) · Inflammopharmacology · doi:10.1007/s10787-024-01622-9
Vijayalakshmi, K. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5153733
Der Haarzyklus und seine Beziehung zur Ernährung
Trüeb, R. M. (2025) · Springer eBooks · doi:10.1007/978-3-031-72154-0_4
Pandey, R., Roy, A. N., Sarkar, S., Rohman, R., Chakraborty, K., Bargakshatriya, R., Pandey, S., Pruthwiraj, Bhattacharya, D., Kumar, S., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.30.673002
Ryu, W., Lee, D., Hong, S., Kim, J., Lee, J., Bang, J. K., Jung, Y., Kim, H.-J., & Kim, S. H. (2025) · Inorganic Chemistry Frontiers · doi:10.1039/d5qi02016f
Wadioni, A., Adebayo, O. G., Masanwoola, A. V., & Chimezie, J. (2025) · Journal of Trace Elements and Minerals · doi:10.1016/j.jtemin.2025.100274
Oxidation of the amyloid-beta peptide and consequences on the etiology of Alzheimer's disease
Cheignon, C. (2016) · theses.fr (ABES) · doi:10.70675/27d2850fzde9ez4784zab4ezbc50e483dc63
Effects of zinc and copper ions in the amyloid cascade linked to Alzheimer's disease
Borghesani, V. (2018) · theses.fr (ABES) · doi:10.70675/d82c3f9az0deaz45e9z9097zeb1f4fd0a45b
Singh, K., Priyadarshi, N., Goyal, B., Singhal, N. K., & Goyal, D. (2026) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.5c00649
Pradhan, T., Sarkar, R., Leonhard‐Preu, J., Schnell, A. F., Schwierz, N., & Reif, B. (2026) · ChemBioChem · doi:10.1002/cbic.70460
Ku, Y., Wang, Y., Lee, M. N., & Wang, Y. (2026) · Journal of the Chinese Chemical Society · doi:10.1002/jccs.70250
Alzheimer’s disease diagnosis based on gene selection and cross-tissue validation
Zhang, X., Tang, X., Bo, Q., Ma, Y., Fang, S., & Hou, H. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2026.1890236
Cerlati, O., Putaux, J., Marty, J., Mingotaud, A., Vicendo, P., Pimienta, V., & Collin, F. (2026) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2026.141831
Malpani, P., Bhatt, S., Mehta, A., Bhuvanesh, N. S. P., Joshi, H., & Sharma, A. K. (2026) · Inorganica Chimica Acta · doi:10.1016/j.ica.2026.123496
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
