The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity
Open accessAbstract
Oxidative stress markers as well as high concentrations of copper are found in the vicinity of Abeta amyloid deposits in Alzheimer's disease. The neurotoxicity of Abeta in cell culture has been linked to H(2)O(2) generation by an unknown mechanism. We now report that Cu(II) markedly potentiates the neurotoxicity exhibited by Abeta in cell culture. The potentiation of toxicity is greatest for Abeta1-42 > Abeta1-40 >> mouse/rat Abeta1-40, corresponding to their relative capacities to reduce Cu(II) to Cu(I), form H(2)O(2) in cell-free assays and to exhibit amyloid pathology. The copper complex of Abeta1-42 has a highly positive formal reduction potential ( approximately +500-550 mV versus Ag/AgCl) characteristic of strongly reducing cuproproteins. These findings suggest that certain redox active metal ions may be important in exacerbating and perhaps facilitating Abeta-mediated oxidative damage in Alzheimer's disease.
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 cited source says what the claim attributes to it.
In the citing paper
“Since metal-Aβ species have been shown to be neurotoxic,25,51,92”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [92]
The cited source says what the claim attributes to it.
In the citing paper
“Because Cu2+–Aβ species have been shown to be neurotoxic,20,21,31,51,52”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [52]
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
Oxygen toxicity, oxygen radicals, transition metals and disease
Halliwell, B., & Gutteridge, J. M. C. (1984) · Biochemical Journal · doi:10.1042/bj2190001 · Cited by 5,330
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Self-citationScheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Self-citationCopper, 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
Rae, T., Schmidt, P. J., Pufahl, R. A., Culotta, V., & O’Halloran, T. V. (1999) · Science · doi:10.1126/science.284.5415.805 · Cited by 1,640
Increased amyloid-β42(43) in brains of mice expressing mutant presenilin 1
Duff, K., Eckman, C., Zehr, C., Yu, X., Prada, C.-M., Pérez‐Tur, J., Hutton, M., Buée, L., Harigaya, Y., Yager, D., et al. (1996) · Nature · doi:10.1038/383710a0 · Cited by 1,486
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
The cellular prion protein binds copper in vivo
Brown, D. R., Qin, K., Herms, J., Madlung, A., Manson, J., Strome, R., Fraser, P., Kruck, T., von Bohlen, A., Schulz-Schaeffer, W., et al. (1997) · Nature · doi:10.1038/37783 · Cited by 1,300
The biological chemistry of the elements
(1993) · The Science of The Total Environment · doi:10.1016/0048-9697(93)90224-t · Cited by 1,173
Research works printed but not linked: 1
- Basun, 1991, J. Neural Transm. Park. Dis. Dement. Sect., 3, 231
Cited by
Sorted by citations
Items 601–700 of 769
Magrì, A., Tabbì, G., Giuffrida, A., Pappalardo, G., Satriano, C., Naletova, I., Nicoletti, V. G., & Attanasio, F. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.08.013 · Cited by 9
Gómez-Castro, C. Z., Quintanar, L., & Vela, A. (2024) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-024-02061-1 · Cited by 9
Zimmeter, K., Vileno, B., Platas‐Iglesias, C., Vinjamuri, B., Sour, A., & Faller, P. (2023) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c00480 · Cited by 9
Behof, W. J., Whitmore, C. A., Haynes, J. R., Rosenberg, A. J., Tantawy, M. N., Peterson, T. E., Harrison, F. E., Beelman, R. B., Wijesinghe, P., Matsubara, J. A., et al. (2022) · FEBS Letters · doi:10.1002/1873-3468.14303 · Cited by 9
Song, T., Lam, C. N. W., Ng, D. C. M., Orlova, G., Laskin, J., Fang, D., & Chu, I. K. (2009) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2009.01.007 · Cited by 9
McDaid, D., Kim, E.-M., Reid, R. E., Leslie, J. C., Cleary, J. P., & O‘Hare, E. (2005) · Behavioural Pharmacology · doi:10.1097/01.fbp.0000166465.75809.85 · Cited by 9
Molecular Determinants of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2007) · Future Neurology · doi:10.2217/14796708.2.4.397 · Cited by 9
Melatonin Supplementation in Alzheimer’s disease: The Potential Role in Neurogenesis
Ebrahimi, R., Faramarzi, A., Salarvandian, S., Zarei, R., Heidari, M., Salehian, F., & Esmaeilpour, K. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05095-x · Cited by 8
Howells, C., Saar, K., Eaton, E. D., Ray, S., Palumaa, P., Shabala, L., Adlard, P. A., Bennett, W. R., West, A. K., Guillemin, G. J., et al. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.002 · Cited by 8
Revisiting Cu(II) Bound Amyloid-β40 and Amyloid-β42 Peptides: Varying Coordination Chemistries
Coskuner‐Weber, O. (2018) · Journal of the Turkish Chemical Society Section A Chemistry · doi:10.18596/jotcsa.424144 · Cited by 8
Potential of Fluorescent Nanoprobe in Diagnosis and Treatment of Alzheimer’s Disease
Lin, J., Li, H., Guo, J., Xu, Y., Li, H., Yan, J., Wang, Y., Chen, H., & Yuan, Z. (2022) · Nanomedicine · doi:10.2217/nnm-2022-0022 · Cited by 8
Yamanaka, Y., Yoshida, S., & Doi, H. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.12.008 · Cited by 8
Ginotra, Y. P., Ramteke, S., Walke, G. R., Rapole, S., & Kulkarni, P. P. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1133907 · Cited by 8
Potential role of serotonin as a biological reductant associated with copper transportation
Saito, K., Watanabe, K., Yanaoka, R., Kageyama, L., & Miura, T. (2019) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2019.110770 · Cited by 8
Neurobiological Mechanisms Involved in the Pathogenesis of Alzheimer’s Disease
Mir, F. A., & Rizvi, Z. A. (2019) · Springer eBooks · doi:10.1007/978-981-13-9636-6_13 · Cited by 8
Evidence for early identification of Alzheimer's diseasePreprint
Alexiou, A. T., & Vlamos, P. (2012) · arXiv (Cornell University) · doi:10.48550/arxiv.1209.4223 · Cited by 9
Disturbances of Copper Homeostasis and Brain Function
Rotilio, G., Ciriolo, M. R., Carrı̀, M. T., & Rossi, L. C. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-288-3_16 · Cited by 7
Kshirsagar, S., Alvir, R. V., Pradeepkiran, J. A., Reddy, A. P., & Reddy, P. H. (2025) · Mitochondrion · doi:10.1016/j.mito.2025.102036 · Cited by 7
Castro, A., Coria-Lucero, C. D., Anzulovich, A. C., & Navigatore-Fonzo, L. (2019) · Pathophysiology · doi:10.1016/j.pathophys.2019.07.003 · Cited by 7
Møller, L. B., & Aaseth, J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822946-0.00009-x · Cited by 8
Metal Ions and Alzheimer's Disease
Adlard, P. A., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/978-0-387-70830-0_15 · Cited by 6
Self-citationApplications of electron paramagnetic resonance to studies of neurological disease
Boas, J. F., Drew, S. C., & Curtain, C. C. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0261-8 · Cited by 7
Pitts, A. L., & Hall, M. B. (2013) · Inorganic Chemistry · doi:10.1021/ic401106z · Cited by 7
Regulation of Neuroactive Metals by the Choroid Plexus
Li, G. J., & Zheng, W. (2005) · CRC Press eBooks · doi:10.1201/9781420023404.ch9 · Cited by 7
Markert, C., Morré, D. M., & Morré, D. J. (2004) · BioFactors · doi:10.1002/biof.5520200405 · Cited by 7
Solioz, M. (2020) · Experimental Biology and Medicine · doi:10.1177/1535370219899898 · Cited by 7
Ekanayake, R. S. K., Streltsov, V. A., Best, S. P., & Chantler, C. T. (2024) · IUCrJ · doi:10.1107/s2052252524001830 · Cited by 6
Superoxide Reduction by Cu‐Amyloid Beta Peptide Complexes: A Density Functional Theory Study
Arrigoni, F., Carlo, C. D., Rovetta, A., GIOIA, L. D., Zampella, G., & Bertini, L. (2022) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202200245 · Cited by 7
Zhao, Q., Ma, L., Chen, S., Huang, L., She, G., Sun, Y., Shi, W., & Mu, L. (2024) · Talanta · doi:10.1016/j.talanta.2024.125716 · Cited by 6
Effects of oxidation on redox and cytotoxic properties of copper complex of Aβ1–16 peptide
Ramteke, S., Walke, G. R., Joshi, B. N., Rapole, S., & Kulkarni, P. P. (2014) · Free Radical Research · doi:10.3109/10715762.2014.960412 · Cited by 6
Wang, Q., Werstiuk, N. H., Kramer, J. R., & Bell, R. A. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp200260e · Cited by 6
Burden, C. M. (2016) · Cited by 6
Kumar, A., Sharma, P., Prasad, R., & Pal, A. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.04.001 · Cited by 6
Brain cholesterol homeostasis in Wilson disease
Cacciatore, S., & Tenori, L. (2013) · Medical Hypotheses · doi:10.1016/j.mehy.2013.10.018 · Cited by 6
Jin, H., Kim, M., Young-Min, S. U. H., Choi, S. J., Nam Shik, M. U. N., Kim, H. K., Kim, E. K., & Shin, D. H. (2005) · Journal of Food Science · doi:10.1111/j.1365-2621.2005.tb07122.x · Cited by 6
Volatile oil of Acori tatarinowii rhizoma: potential candidate drugs for mitigating dementia
Bu, Y., Li, S., Ye, T., Wang, Y., Song, M., & Chen, J. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1552801 · Cited by 6
Deuterium trafficking, mitochondrial dysfunction, copper homeostasis, and neurodegenerative disease
Seneff, S., & Kyriakopoulos, A. M. (2025) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2025.1639327 · Cited by 5
Guantieri, V., Venzo, A., Marco, V. D., Acampora, M., & Biondi, B. (2007) · Inorganica Chimica Acta · doi:10.1016/j.ica.2007.05.026 · Cited by 5
Nanoparticle-mediated delivery of AChE inhibitors for the treatment of Alzheimer’s disease
Namdeo, P., Mathew, J., & Garg, A. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85544-0.00004-6 · Cited by 5
Hæffner, F., Barnham, K. J., Bush, A. I., & Brinck, T. (2009) · Journal of Molecular Modeling · doi:10.1007/s00894-009-0619-6 · Cited by 5
Self-citationN’Go, P. K., Ahami, O. T. A., Hessni, A. E., Azzaoui, F.-Z., Aboussaleh, Y., & Tako, A. N. (2021) · Translational Neuroscience · doi:10.1515/tnsci-2020-0183 · Cited by 5
Folarin, O. R., Olopade, F. E., & Olopade, J. O. (2021) · Nigerian Journal of Physiological Sciences · doi:10.54548/njps.v36i2.1 · Cited by 5
The Function of the Amyloid Precursor Protein Family
Cappai, R., Needham, B. E., & Ciccotosto, G. D. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_3 · Cited by 5
Toxic Levels of Amyloid Beta Peptide Do Not Induce VEGF Synthesis
Park, S.-Y., & Chae, C. (2007) · Molecules and Cells · doi:10.1016/s1016-8478(23)10757-6 · Cited by 5
Copper in Brain and Neurodegeneration
Liddell, J. R., Bush, A. I., & White, A. R. (2004) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2143 · Cited by 5
Self-citationKumar, G., Srivastava, A., Kumar, P., Srikrishna, S., & Singh, V. P. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e24074 · Cited by 4
Ratner, M. H., & Rutchik, J. S. (2024) · Frontiers in Toxicology · doi:10.3389/ftox.2024.1451235 · Cited by 4
Chen, W., Hong, C., Lin, Y.-T., Chang, W., Huang, H.-T., Liao, J., Chang, Y., Hsieh, Y.-F., Cheng, C., Liu, H.-C., et al. (2012) · Cited by 4
Amyloid β-Peptide(1-42), Oxidative Stress, and Alzheimer’s Disease
Butterfield, D. A. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_5 · Cited by 4
The Aβcentric Pathway of Alzheimer’s Disease
Villemagne, V. L., Cappai, R., Barnham, K. J., Cherny, R. A., Opazo, C., Novakovic, K. E., Rowe, C. C., & Masters, C. L. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_2 · Cited by 4
Self-citationIron is increased in the brains of ageing mice lacking the neurofilament light gene
Vickers, J. C., King, A. E., McCormack, G. H., Bindoff, A. D., & Adlard, P. A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0224169 · Cited by 4
Free Radicals, Metal Ions, and Aβ Aggregation and Neurotoxicity
Barnham, K. J., Curtain, C. C., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/978-0-387-36534-3_2 · Cited by 4
Self-citationModelling Copper Binding to the Amyloid-ß Peptide in Alzheimer’s Disease
Epa, V. C., Streltsov, V. A., & Varghese, J. N. (2010) · Australian Journal of Chemistry · doi:10.1071/ch09454 · Cited by 4
Alzheimer's Pathogenesis, Metal-Mediated Redox Stress, and Potential Nanotheranostics.
Wang, W. T., Tailor, B. A., Cohen, D. S., & Huang, X. (2019) · PubMed · Cited by 4
Self-citationEthiology and pathogenesis of amyloidoses: the molecular and genetic basis
Schavlovsky, M. M. (2010) · Medical academic journal · doi:10.17816/maj10463-81 · Cited by 4
Designing Novel Peptidic Inhibitors of Beta Amyloid Oligomerization
Roy, S. S. (2010) · Libraries and Cultural Resources (University of Calgary) · doi:10.5072/prism/17548 · Cited by 4
Engineering Synthetic Electron Transfer Chains from Metallopeptide Membranes
Sementilli, A., Rengifo, R. F., Li, W., Stewart, A. M., Stewart, K. L., Twahir, U. T., Kim, Y., Yue, J., Mehta, A. K., Shearer, J., et al. (2023) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c02861 · Cited by 3
Investigating Cu(I) binding to model peptides of N-terminal Aβ isoforms
Hjelmstad, A. S., Pushie, M. J., Ruth, K., Escobedo, M., Kuter, K. E., & Haas, K. L. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112480 · Cited by 3
Thick conducting polymer films for ultra-low frequency stimulation
Snr, Y. O. A., & Proctor, C. M. (2025) · APL Electronic Devices · doi:10.1063/5.0272441 · Cited by 3
Formation of Methionine Sulfoxide of Amyloid β‐Peptide (1‐40) by Cu(bdpe)/H2O2 System
Kishita, A., Nishino, S., Togashi, T., & Nishida, Y. (2005) · Synthesis and Reactivity in Inorganic Metal-Organic and Nano-Metal Chemistry · doi:10.1080/15533170500301820 · Cited by 3
Mocanu, C. S., Darie‐Ion, L., Petre, B. A., Grădinaru, V. R., & Drochioiu, G. (2022) · Journal of King Saud University - Science · doi:10.1016/j.jksus.2022.102184 · Cited by 3
Eslami, M., Hashemianzadeh, S. M., Moghaddam, K. G., Khorsandi, L., & Sajadi, S. A. S. (2015) · RSC Advances · doi:10.1039/c5ra11346f · Cited by 3
Balamurugan, G., & Muralidharan, P. (2010) · Bangladesh Journal of Pharmacology · doi:10.3329/bjp.v5i1.5644 · Cited by 3
Metales de transición y enfermedad de Alzheimer
Opazo, C. (2005) · Revista Española de Geriatría y Gerontología · doi:10.1016/s0211-139x(05)74885-x · Cited by 3
The Role of Hydrogen Peroxide as a Signaling Molecule
Czubryt, M. P., & Pierce, G. N. (2003) · Progress in experimental cardiology · doi:10.1007/978-1-4615-0347-7_19 · Cited by 3
Mozziconacci, O., Bhagavathy, G. V., Yamamoto, T., Wilson, G. S., Glass, R. S., & Schöneich, C. (2016) · Tetrahedron · doi:10.1016/j.tet.2016.08.075 · Cited by 3
Ferrari, E., Cravello, L., Bonacina, M., Salmoiraghi, F., & Magri, F. (2005) · Techniques in the behavioral and neural sciences · doi:10.1016/s0921-0709(05)80064-1 · Cited by 3
Neuroinflammatory Environments Promote Amyloid-ß Deposition and Posttranslational Modification
Atwood, C., Smith, M. A., Martins, R. N., Tanzi, R. E., Roher, A. E., Bush, A. I., & Perry, G. L. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-297-5_12 · Cited by 3
Self-citationMulthaup, G., Dieter, H. H., Beyreuther, K. T., & Bayer, T. A. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-288-3_17 · Cited by 4
Self-citationThe Design of Metal Complexes to Target the Amyloid‐β Peptide in Alzheimer's Disease
Webb, M. I. (2023) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2846 · Cited by 3
Amyloid Beta Oligomers as Early Triggers of Neuronal Cytoskeleton Dysfunction in Alzheimer’s Disease
Gasca-Martínez, Y., Ontiveros‐Torres, M. Á., López-Gallegos, I., & Jarero-Basulto, J. J. (2026) · Pathophysiology · doi:10.3390/pathophysiology33010014 · Cited by 2
Zheng, H., Amit, T., Bar‐Am, O., Fridkin, M., Mandel, S. A., & Youdim, M. B. H. (2022) · Springer eBooks · doi:10.1007/978-3-030-62059-2_234 · Cited by 2
Linking copper and neurotoxic activities to the CNS
Santos, G., Ávila-Rodriguez, M., Rubio, É. P., Galembeck, E., & Borges, J. M. P. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-89835-5.00035-1 · Cited by 2
Alzheimer's disease – a metallic problem
Dorrell, S. (2001) · Drug Discovery Today · doi:10.1016/s1359-6446(00)01638-x · Cited by 2
Monomeric Aβ and metals reduce their cytotoxicities to each other
Matsuzaki, S., Yasuda, Y., Kobayashi, S., Koyama, Y., Kawamoto, K., Katayama, T., & Tohyama, M. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.161 · Cited by 2
Reactive oxygen and nitrogen species: Weapons of neuronal destruction
Mazzulli, J., Lind, S., & Ischiropoulos, H. (2005) · Cited by 2
The Amyloid _-Protein and Alzheimer's Disease
Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2
Targeting Transition Metals for Neuroprotection in Alzheimer’s Disease
Ayton, S., Belaidi, A. A., Lei, P., & Bush, A. I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803690-7.00010-7 · Cited by 2
Self-citationKumari, Y., Raj, K., & Singh, P. K. (2023) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9789815136142123010011 · Cited by 2
Metal Complexing Agents for the Treatment of Alzheimer's Disease
White, A. R., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/7355_2007_011 · Cited by 2
Self-citationZheng, H., Amit, T., Bar‐Am, O., Fridkin, M., Mandel, S. A., & Youdim, M. B. H. (2020) · Springer eBooks · doi:10.1007/978-3-319-56015-1_234-1 · Cited by 2
Leong, S. L., Barnham, K. J., Multhaup, G., & Cappai, R. (2004) · Handbook of Metalloproteins · doi:10.1002/0470028637.met206 · Cited by 2
Self-citationRole of Metals in Alzheimer Disease
Roberts, B. R., & Bush, A. I. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch24 · Cited by 2
Self-citationCu2+ Affects Amyloid-\b{eta} (1-42) Aggregation by Increasing Peptide-Peptide Binding ForcesPreprint
Hane, F. T., Tran, G., Attwood, S. J., & Leonenko, Z. (2017) · arXiv (Cornell University) · doi:10.48550/arxiv.1704.08317 · Cited by 2
Leong, S. L., Barnham, K. J., Multhaup, G., & Cappai, R. (2004) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0633 · Cited by 2
Self-citationLiu, Z., Hu, B., Tang, J., Liu, X., Cheng, B., Jia, C., & Zhang, L. (2024) · Journal of Alzheimer s Disease · doi:10.1177/13872877241289381 · Cited by 2
Suseela, Y. V., Mandal, S. K., Jacquemin, D., Govindaraju, T., & Faller, P. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202502598 · Cited by 1
Chronobiology and Neurodegeneration: The Role of Melatonin in Alzheimer's Disease
Vaja, R., Vohra, M., Ramachandran, A. V., & Baxi, D. B. (2025) · Nutritional Psychiatry · doi:10.1016/j.nupsyc.2025.100001 · Cited by 1
Kawon, K. K., Setkowicz, Z., Czyżycki, M., Rauk, Z., Wilk, A., Sławek, A., Cieślak, J., Aquilanti, G., Carlomagno, I., Dróźdż, A., et al. (2026) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2026.127816 · Cited by 1
Oxidative stress and inflammation in neurodegenerative disorders
Jomová, K., Alomar, S. Y., Valko, R., Nepovimová, E., Kuča, K., & Valko, M. (2026) · Archives of Toxicology · doi:10.1007/s00204-026-04518-5 · Cited by 1
Bellver‐Sanchís, A., Ralchev, N., Romanska, P. R., Dyakova, N. K., Ivanova, K. I., Griñán‐Ferré, C., & Marchev, A. S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177833 · Cited by 1
Redox Chemistry of Sulfur, Selenium and Tellurium Compounds
Glass, R. S. (2011) · Springer eBooks · doi:10.1007/978-3-642-20699-3_3 · Cited by 1
Metals Involvement in Alzheimer’s Disease Pathogenesis
Squitti, R., & Salustri, C. (2011) · InTech eBooks · doi:10.5772/16880 · Cited by 1
Neurotoxicity of the Alzheimer’s β-Amyloid Peptide
Howlett, D. R. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-888-5_6 · Cited by 1
Aβ-Like Peptide Displayed on Bacteriophage T7 Catalyzes Chromate and Uranyl Reduction
Jin, H., Lin, C., Shang, J., Wilkins, M. J., Liu, Y., Gong, W., Xu, W., Squier, T. C., & Long, P. E. (2013) · Journal of Environmental Protection · doi:10.4236/jep.2013.48100 · Cited by 1
Oxidative Stress and Alzheimer Disease: Mechanisms and Therapeutic Opportunities
Mondragón‐Rodríguez, S., García‐Sierra, F., Casadesús, G., Lee, H., Petersen, R. B., Perry, G. L., Zhu, X., & Smith, M. A. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_18 · Cited by 1
Lanning, J. D., & Meredith, S. C. (2011) · Springer eBooks · doi:10.1007/978-94-007-2774-8_14 · Cited by 1
Scanning Probe Microscopy Methods of Imaging Amyloid Peptides During the Aggregation Process
Tinker, C. L. (2016) · Springer theses · doi:10.1007/978-3-319-39534-0_6 · Cited by 1
Sharma, P., Senthilkumar, R., Brahmachari, V., Sundaramoorthy, E., Mahajan, A., Sharma, A., & Sengupta, S. (2015) · Cited by 1
Xiu, F., Xu, S., Zhang, C., & Wang, L. (2021) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162021020266 · Cited by 1
Metadata
- Authors
- 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., Scarpa, R. C., Saunders, A. J., Lim, J., Moir, R. D., Glabe, C., Bowden, E. F., Masters, C. L., Fairlie, D. P., Tanzi, R. E., & Bush, A. I.
- Affiliations
- Harvard University (US)
- The University of Queensland (AU)
- North Carolina State University (US)
- Heidelberg University (DE)
- University of California, Irvine (US)
- Mental Health Research Institute (AU)
- Corresponding author
- Bush, Ashley I.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-12
- Volume
- 274
- Issue
- 52
- Pages
- 37111-37116
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2131633241
- Cited by
- 762
- References
- 40
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 13 · 2023: 14 · 2022: 14 · 2021: 10 · 2020: 15 · 2019: 30 · 2018: 16 · 2017: 19 · 2016: 26 · 2015: 27 · 2014: 33 · 2013: 28 · 2012: 42
- FWCI
- 14.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Massachusetts General Hospital
- Commonwealth of Massachusetts
- National Institutes of Health
- Medical Research Council
- Australian Research Council
- National Health and Medical Research Council
- National Institute on Aging
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid-beta, copper(II), neurotoxicity, oxidative stress, hydrogen peroxide production, amyloid-beta 42, Aβ40, copper proteins, metal ions, redox-active metals, oxidative damage
- MeSH terms
- Animals, Brain, Cells, Cultured, Computer Simulation, Copper, Electron Spin Resonance Spectroscopy, Hydrogen Peroxide, Oxidation-Reduction, Amyloid beta-Peptides, Rats
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