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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.
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“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]
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“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]
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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
Flagged first, then by citations
Research works printed but not linked: 1
- Basun, 1991, J. Neural Transm. Park. Dis. Dement. Sect., 3, 231
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Sorted by citations
Items 201–300 of 769
Free Superoxide is an Intermediate in the Production of H 2 O 2 by Copper(I)‐Aβ Peptide and O 2
Reybier, K., Ayala, S., Aliès, B., Rodrigues, J. V., Rodriguez, S. B., Penna, G. L., Collin, F., Gomes, C. M., Hureau, C., & Faller, P. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508597 · Cited by 122
Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2008) · Biochemistry · doi:10.1021/bi8011093 · Cited by 119
Karr, J. W., & Szalai, V. A. (2008) · Biochemistry · doi:10.1021/bi702423h · Cited by 119
Only amyloidogenic intermediates of transthyretin induce apoptosis
Andersson, K., Olofsson, A., Nielsen, E. H., Svehag, S., & Lundgren, E. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00465-5 · Cited by 116
Copper, Zinc, and the Metallobiology of Alzheimer Disease
Bush, A. I. (2003) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-200307000-00005 · Cited by 117
Self-citationChen, W.-T., Hong, C., Lin, Y.-T., Chang, W.-H., Huang, H.-T., Liao, J., Chang, Y.-J., Hsieh, Y.-F., Cheng, C.-Y., Liu, H.-C., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035807 · Cited by 119
Amyloid-β Production: Major Link Between Oxidative Stress and BACE1
Tamagno, E., Guglielmotto, M., Monteleone, D., & Tabaton, M. (2011) · Neurotoxicity Research · doi:10.1007/s12640-011-9283-6 · Cited by 117
Quintanilla, R. A., Muñoz, F. J., Metcalfe, M., Hitschfeld, M., Olivares, G. H., Godoy, J. A., & Inestrosa, N. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411936200 · Cited by 114
Tickler, A. K., Smith, D. G., Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414178200 · Cited by 115
Self-citationRana, M., & Sharma, A. K. (2018) · Metallomics · doi:10.1039/c8mt00203g · Cited by 116
Habib, L. K., Lee, M. T. C., & Yang, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132860 · Cited by 114
Copper and Alzheimer’s Disease
Mathys, Z. K., & White, A. R. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-60189-2_10 · Cited by 115
Redox Processes of Methionine Relevant to β-Amyloid Oxidation and Alzheimer's Disease
Schöneich, C. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2621 · Cited by 112
De Simone, A., Tumiatti, V., Andrisano, V., & Milelli, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00931 · Cited by 110
Mayes, J., Tinker, C. L., Kolosov, O., Zhang, H., Tabner, B. J., & Allsop, D. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.525212 · Cited by 110
Chen, T., Wang, X., He, Y., Zhang, C., Wu, Z., Liao, K., Wang, J., & Guo, Z. (2009) · Inorganic Chemistry · doi:10.1021/ic900025x · Cited by 110
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
Jiang, D., Li, X., Williams, R. S., Patel, S., Men, L., Wang, Y., & Zhou, F. (2009) · Biochemistry · doi:10.1021/bi900907a · Cited by 109
Delineating the Mechanism of Alzheimer’s Disease Aβ Peptide Neurotoxicity
Cappai, R., & Barnham, K. J. (2008) · Neurochemical Research · doi:10.1007/s11064-007-9469-8 · Cited by 108
Oxidative Stress in Alzheimer’s Disease: Should We Keep Trying Antioxidant Therapies?
Ferreira, M. E. S., de Vasconcelos, A. S., Vilhena, T. D. C., da Silva, T. L., Barbosa, A. D. S., Gomes, A. R. Q., Dolabela, M. F., & Percário, S. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0157-y · Cited by 111
Squitti, R., Ghidoni, R., Siotto, M., Ventriglia, M., Benussi, L., Paterlini, A., Magri, M., Binetti, G. G., Cassetta, E., Caprara, D., et al. (2014) · Annals of Neurology · doi:10.1002/ana.24136 · Cited by 108
Cu2+ Affects Amyloid-β (1–42) Aggregation by Increasing Peptide-Peptide Binding Forces
Hane, F. T., Tran, G., Attwood, S. J., & Leonenko, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059005 · Cited by 111
Klug, G. M., Lošić, D., Supundi, Subasinghe, S., Aguilar, M., Martin, L. L., & Small, D. H. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03815.x · Cited by 109
Promotion of Oxidative Lipid Membrane Damage by Amyloid β Proteins
Murray, I. V. J., Sindoni, M. E., & Axelsen, P. H. (2005) · Biochemistry · doi:10.1021/bi050926p · Cited by 107
Cahill, C. M., Lahiri, D. K., Huang, X., & Rogers, J. T. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.12.001 · Cited by 108
Self-citationNeuronal and Vascular Oxidative Stress in Alzheimers Disease
Massaad, C. A. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376244 · Cited by 102
Chao, X., He, X., Yang, Y., Zhou, X., Jin, M., Liu, S., Cheng, Z., Liu, P., Wang, Y., Yu, J., et al. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.08.036 · Cited by 103
Cellular Senescence and Iron Dyshomeostasis in Alzheimer’s Disease
Masaldan, S., Belaidi, A. A., Ayton, S., & Bush, A. I. (2019) · Pharmaceuticals · doi:10.3390/ph12020093 · Cited by 106
Self-citationHands, S. L., Sajjad, M. U., Newton, M. J., & Wyttenbach, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.307587 · Cited by 106
Alzheimer’s Disease: Mechanism and Approach to Cell Therapy
Amemori, T., Jendelová, P., Růžička, J., Urdzíková, L. M., & Syková, E. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125961 · Cited by 110
Altered microglial copper homeostasis in a mouse model of Alzheimer’s disease
Zheng, Z., White, C., Lee, J., Peterson, T. S., Bush, A. I., Sun, G. Y., Weisman, G. A., & Petris, M. J. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06888.x · Cited by 103
Self-citationOxidative stress in Alzheimer’s Disease: Implications for Prevention and Therapy
Behl, C. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_3 · Cited by 100
Ciccotosto, G. D., Tew, D. J., Curtain, C. C., Smith, D., Carrington, D., Masters, C. L., Bush, A. I., Cherny, R. A., Cappai, R., & Barnham, K. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406465200 · Cited by 101
Self-citationBellingham, S. A., Ciccotosto, G. D., Needham, B. E., Fodero, L. R., White, A. R., Masters, C. L., Cappai, R., & Camakaris, J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02731.x · Cited by 100
Self-citationZindo, F. T., Joubert, J., & Malan, S. F. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.12 · Cited by 99
Iliyasu, M. O., Musa, S. A., Oladele, S. B., & Iliya, A. I. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1081938 · Cited by 106
Phosphorylation of p66Shc and forkhead proteins mediates Aβ toxicity
Smith, W. W., Norton, D. D., Gorospe, M., Jiang, H., Nemoto, S., Holbrook, N. J., Finkel, T., & Kusiak, J. W. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200410041 · Cited by 100
Baruch-Suchodolsky, R., & Fischer, B. (2009) · Biochemistry · doi:10.1021/bi802361k · Cited by 98
Delineating common molecular mechanisms in Alzheimer's and prion diseases
Barnham, K. J., Cappai, R., Beyreuther, K. T., Masters, C. L., & Hill, A. F. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.06.006 · Cited by 97
Self-citationAhmed, S. S. S. J., & Santosh, W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011252 · Cited by 103
Natural Antioxidants for Neurodegenerative Diseases
Zhao, B. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:283 · Cited by 98
Neurodegeneration and oxidative stress: prion disease results from loss of antioxidant defence.
Brown, D. R. (2005) · PubMed · Cited by 97
The Relevance of Metals in the Pathophysiology of Neurodegeneration, Pathological Considerations
Jellinger, K. A. (2013) · International review of neurobiology · doi:10.1016/b978-0-12-410502-7.00002-8 · Cited by 101
Signal Transduction Cascades Associated with Oxidative Stress in Alzheimer's Disease
Petersen, R. B., Nunomura, A., Lee, H., Casadesús, G., Perry, G. L., Smith, M. A., & Zhu, X. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11202 · Cited by 101
The amyloid‐β peptide and its role in Alzheimer's disease
Clippingdale, A. B., Wade, J. D., & Barrow, C. J. (2001) · Journal of Peptide Science · doi:10.1002/psc.324 · Cited by 103
Mechanisms by which metals promote events connected to neurodegenerative diseases
Campbell, A., Smith, M. A., Sayre, L. M., Bondy, S. C., & Perry, G. L. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00455-5 · Cited by 96
Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Ohashi, R., Takegoshi, K., Nagao, M., Shimizu, T., & Shirasawa, T. (2005) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.99.437 · Cited by 104
Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation
Bhak, G., Choe, Y., & Paik, S.-R. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.9.541 · Cited by 99
Molecular changes in fetal Down syndrome brain
Engidawork, E., & Lübec, G. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01614.x · Cited by 96
Zinc in Alzheimer’s Disease: A Meta-Analysis of Serum, Plasma, and Cerebrospinal Fluid Studies
Ventriglia, M., Brewer, G. J., Simonelli, I., Mariani, S., Siotto, M., Bucossi, S., & Squitti, R. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141296 · Cited by 94
Sang, Z., Qiang, X., Li, Y., Yuan, W., Liu, Q., Shi, Y., Ang, W., Luo, Y., Tan, Z., & Deng, Y. (2015) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2015.02.063 · Cited by 93
The Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's Disease
Drew, S. C. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00317 · Cited by 93
Metal complexes that bind to the amyloid-β peptide of relevance to Alzheimer’s disease
Gomes, L. M., Bataglioli, J. C., & Storr, T. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213255 · Cited by 94
Nanotechnology for Alzheimer’s disease detection and treatment
Nazem, A., & Mansoori, G. A. (2011) · Insciences Journal · doi:10.5640/insc.0104169 · Cited by 96
Kański, J., Aksenova, M. V., Schöneich, C., & Butterfield, D. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00821-3 · Cited by 93
Quiroz‐Baez, R., Rojas, E., & Arias, C. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.06.012 · Cited by 93
Brain Activation of SIRT1: Role in Neuropathology
Paraíso, A. F., Mendes, K. L., & Santos, S. H. S. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8459-x · Cited by 91
Copper imbalance in Alzheimer’s disease: Convergence of the chemistry and the clinic
Kepp, K. P., & Squitti, R. (2019) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2019.06.018 · Cited by 93
Ma, Q., Hu, J. N., Wu, W., Liu, H., Du, J., Fu, Y., Wu, Y., Lei, P., Zhao, Y., & Li, Y. (2006) · Biopolymers · doi:10.1002/bip.20523 · Cited by 91
Perrone, L., Mothes-Martin, E., Vignes, M., Mockel, A., Figueroa, C. M., Miquel, M., Maddelein, M., & Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900474 · Cited by 93
Hsu, H.-W., Bondy, S. C., & Kitazawa, M. (2018) · Toxicological Sciences · doi:10.1093/toxsci/kfy025 · Cited by 88
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
Self-citationThe missing link in the amyloid cascade of Alzheimer’s disease – Metal ions
Tiiman, A., Palumaa, P., & Tõugu, V. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.023 · Cited by 92
Exploring the Structural Details of Cu(I) Binding to α-Synuclein by NMR Spectroscopy
Binolfi, A., Valiente‐Gabioud, A. A., Durán, R., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2010) · Journal of the American Chemical Society · doi:10.1021/ja107842f · Cited by 86
A Prochelator Activated by Hydrogen Peroxide Prevents Metal‐Induced Amyloid β Aggregation
Dickens, M. G., & Franz, K. J. (2009) · ChemBioChem · doi:10.1002/cbic.200900597 · Cited by 86
A review of genome mutation and Alzheimer's disease
Thomas, P., & Fenech, M. F. (2006) · Mutagenesis · doi:10.1093/mutage/gel055 · Cited by 88
Vestergaard, M. C. M., Kerman, K., & Tamiya, E. (2005) · Analytica Chimica Acta · doi:10.1016/j.aca.2005.01.067 · Cited by 85
Pogocki, D., Ruman, T., Danilczuk, M., Danilczuk, M., Celuch, M., & Wałajtys-Rode, E. (2007) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2007.02.038 · Cited by 84
Cherny, R. A., Barnham, K. J., Lynch, T., Volitakis, I., Li, Q.-X., McLean, C., Multhaup, G., Beyreuther, K. T., Tanzi, R. E., Masters, C. L., et al. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4285 · Cited by 85
Self-citationLipid peroxidation and 4-hydroxy-2-nonenal formation by copper ion bound to amyloid-β peptide
Hayashi, T., Shishido, N., Nakayama, K., Nunomura, A., Smith, M. A., Perry, G. L., & Nakamura, M. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.013 · Cited by 84
Rimola, A., Rodrı́guez-Santiago, L., & Sodupe, M. (2006) · The Journal of Physical Chemistry B · doi:10.1021/jp064957l · Cited by 84
Modulation of tau phosphorylation by environmental copper
Voss, K., Harris, C., Ralle, M., Duffy, M., Murchison, C., & Quinn, J. F. (2014) · Translational Neurodegeneration · doi:10.1186/2047-9158-3-24 · Cited by 83
Brimson, J. M., Brimson, S. J., Brimson, C. A., Rakkhitawatthana, V., & Tencomnao, T. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13045074 · Cited by 83
Direct Evidence That All Three Histidine Residues Coordinate to Cu(II) in Amyloid-β1−16
Shin, B., & Saxena, S. (2008) · Biochemistry · doi:10.1021/bi801014x · Cited by 83
Jiang, D., Li, X., Liu, L., Yagnik, G. B., & Zhou, F. (2010) · The Journal of Physical Chemistry B · doi:10.1021/jp9095375 · Cited by 83
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
Pal, A., Badyal, R. K., Vasishta, R. K., Attri, S. V., Thapa, B. R., & Prasad, R. (2013) · Biological Trace Element Research · doi:10.1007/s12011-013-9665-0 · Cited by 82
Ferrer, I., Lizcano, J. M., Hernández‐Guillamón, M., & Unzeta, M. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02465-x · Cited by 81
Choi, H., Park, H., Koh, S., Choi, N.-Y., Yu, H., Park, J., Lee, Y. J., & Lee, K. (2011) · NeuroToxicology · doi:10.1016/j.neuro.2011.12.005 · Cited by 82
White, A. R., Multhaup, G., Galatis, D., McKinstry, W. J., Parker, M. W., Pipkorn, R., Beyreuther, K. T., Masters, C. L., & Cappai, R. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-02-00365.2002 · Cited by 82
Self-citationAlzheimer’s Disease: Pathogenesis and Therapeutic Interventions
Ogbodo, J. O., Agbo, C. P., Njoku, U. O., Ogugofor, M. O., Egba, S. I., Ihim, S. A., Echezona, A. C., Brendan, K. C., Upaganlawar, A. B., & Upasani, C. D. (2021) · Current Aging Science · doi:10.2174/1874609814666210302085232 · Cited by 86
Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
Opazo, C., Barría, M. I., Ruiz, F. H., & Inestrosa, N. C. (2003) · BioMetals · doi:10.1023/a:1020795422185 · Cited by 83
Guglielmotto, M., Tamagno, E., & Danni, O. (2009) · The Scientific World JOURNAL · doi:10.1100/tsw.2009.93 · Cited by 82
The state versus amyloid-β: the trial of the most wanted criminal in Alzheimer disease
Rottkamp, C. A., Atwood, C., Joseph, J. A., Nunomura, A., Perry, G. L., & Smith, M. A. (2002) · Peptides · doi:10.1016/s0196-9781(02)00069-4 · Cited by 81
Self-citationAlzheimer's Aβ fused to green fluorescent protein induces growth stress and a heat shock response
Caine, J., Sankovich, S. E., Antony, H., Waddington, L. J., Macreadie, P. I., Varghese, J. N., & Macreadie, I. G. (2007) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2007.00285.x · Cited by 85
Metals in alzheimer's disease: a systemic perspective
Squitti, R. (2011) · Frontiers in bioscience · doi:10.2741/3938 · Cited by 80
A doença de Alzheimer: aspectos fisiopatológicos e farmacológicos
Sereniki, A., & Vital, M. A. B. F. (2008) · Revista de Psiquiatria do Rio Grande do Sul · doi:10.1590/s0101-81082008000200002 · Cited by 121
Sabbagh, J. J., Kinney, J. W., & Cummings, J. L. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.027 · Cited by 80
Imaging hydrogen peroxide in Alzheimer’s disease via cascade signal amplification
Yang, J., Yang, J., Liang, S. H., Xu, Y., Moore, A. V., & Ran, C. (2016) · Scientific Reports · doi:10.1038/srep35613 · Cited by 78
Mechanisms of action of amyloid-beta and its precursor protein in neuronal cell death
Leong, Y. Q., Ng, K. Y., Chye, S. M., Ling, A. P. K., & Koh, R. Y. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-019-00516-y · Cited by 80
Chung, R. S., Howells, C., Eaton, E. D., Shabala, L., Zovo, K., Palumaa, P., Sillard, R., Woodhouse, A., Bennett, W. R., Ray, S., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012030 · Cited by 84
Prion protein does not redox-silence Cu2+, but is a sacrificial quencher of hydroxyl radicals
Nadal, R. C., Abdelraheim, S. R., Brazier, M. W., Rigby, S. E. J., Brown, D. R., & Viles, J. H. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.09.019 · Cited by 77
Hydrogen peroxide can be generated by tau in the presence of Cu(II)
Su, X., Wu, W., Huang, Z., Hu, J. N., Lei, P., Yu, C., Zhao, Y., & Li, Y. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.191 · Cited by 77
Müller, T., Langner, C., Fuchsbichler, A., Heinz‐Erian, P., Ellemunter, H., Schlenck, B., Bavdekar, A., Pradhan, A. M., Pandit, A., Müller‐Höcker, J., et al. (2004) · Hepatology · doi:10.1002/hep.20108 · Cited by 77
Multhaup, G., Strausak, D., Bissig, K.-D., & Solioz, M. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5757 · Cited by 75
Self-citationPal, A., Siotto, M., Prasad, R., & Squitti, R. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-141194 · Cited by 76
Radioiodinated clioquinol as a biomarker for β‐amyloid: Zn2+ complexes in Alzheimer's disease
Opazo, C., Luza, S., Villemagne, V. L., Volitakis, I., Rowe, C. C., Barnham, K. J., Altschul, D., Masters, C. L., Cherny, R. A., & Bush, A. I. (2006) · Aging Cell · doi:10.1111/j.1474-9726.2006.00196.x · Cited by 76
Self-citationSolid-State63Cu and65Cu NMR Spectroscopy of Inorganic and Organometallic Copper(I) Complexes
Tang, J. A., Ellis, B. D., Warren, T. H., Hanna, J. V., Macdonald, C. L. B., & Schurko, R. W. (2007) · Journal of the American Chemical Society · doi:10.1021/ja073238x · Cited by 76
Pedersen, J. T., Teilum, K., Heegaard, N. H. H., Østergaard, J., Adolph, H., & Hemmingsen, L. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201006335 · Cited by 75
Clark, I. A., Atwood, C., Bowen, R. L., Paz-Filho, G., & Vissel, B. (2012) · Pharmacological Reviews · doi:10.1124/pr.112.005850 · Cited by 76
Self-citation
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
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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.
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