Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

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 · see citing works

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 · see citing works

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

Scheuner, 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 · see citing works

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 · see citing works

Hydrogen peroxide mediates amyloid β protein toxicity

Behl, C. (1994) · Cell · doi:10.1016/0092-8674(94)90131-7 · Cited by 2,074 · see citing works

Undetectable Intracellular Free Copper: The Requirement of a Copper Chaperone for Superoxide Dismutase

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 1,631 · see citing works

An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp ₇₁₇ ) Mutants

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 · see citing works

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 1,465 · see citing works

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 · see citing works

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 · see citing works

The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction

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 1,107 · see citing works

A model for beta-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease.

Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3270 · Cited by 1,086 · see citing works

Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009 · see citing works

Oxidative damage in Alzheimer's

Smith, M. A., Perry, G. L., Richey, P. L., Sayrec, L. M., Anderson, V. E., Beal, M. F., & Kowall, N. W. (1996) · Nature · doi:10.1038/382120b0 · Cited by 897 · see citing works

Metal-catalyzed oxidation of proteins. Physiological consequences

Stadtman, E. R., & Oliver, C. N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52199-2 · Cited by 862 · see citing works

Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Inactivation of the enzyme

Hodgson, E. K., & Fridovich, I. (1975) · Biochemistry · doi:10.1021/bi00695a010 · Cited by 785 · see citing works

A Role for 4‐Hydroxynonenal, an Aldehydic Product of Lipid Peroxidation, in Disruption of Ion Homeostasis and Neuronal Death Induced by Amyloid β‐Peptide

Mark, R. J., Lovell, M. A., Markesbery, W. R., Uchida, K., & Mattson, M. P. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68010255.x · Cited by 781 · see citing works

Brain Regional Correspondence Between Alzheimer's Disease Histopathology and Biomarkers of Protein Oxidation

Hensley, K., Hall, N., Subramaniam, R., Cole, P., Harris, M., Aksenov, M., Aksenova, M., Gabbita, S. P., Wu, J. F., Carney, J. M., et al. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65052146.x · Cited by 779 · see citing works

Novel thioether bond revealed by a 1.7 Å crystal structure of galactose oxidase

Ito, N., Phillips, S. E. V., Stevens, C., Ogel, Z. B., McPherson, M. J., Keen, J. N., Yadav, K. D. S., & Knowles, P. F. (1991) · Nature · doi:10.1038/350087a0 · Cited by 763 · see citing works

The biological chemistry of the elements

Exley, C. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90327-6 · Cited by 721 · see citing works

Amyloid‐β Deposition in Alzheimer Transgenic Mice Is Associated with Oxidative Stress

Smith, M. A., Hirai, K., Hsiao, K., Pappolla, M. A., Harris, P. L. R., Siedlak, S. L., Tabaton, M., & Perry, G. L. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70052212.x · Cited by 547 · see citing works

Copper, iron, and zinc imbalances in severely degenerated brain regions in Alzheimer’s disease: possible relation to oxidative stress.

Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (1996) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(96)00203-1 · Cited by 540 · see citing works

Solution Structures of β Peptide and Its Constituent Fragments: Relation to Amyloid Deposition

Barrow, C. J., & Zagorski, M. G. (1991) · Science · doi:10.1126/science.1853202 · Cited by 538 · see citing works

Aqueous Dissolution of Alzheimer's Disease Aβ Amyloid Deposits by Biometal Depletion

Cherny, R. A., Legg, J. T., McLean, C. A., Fairlie, D. P., Huang, X., Atwood, C. S., Beyreuther, K., Tanzi, R. E., Masters, C. L., & Bush, A. I. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23223 · Cited by 482 · see citing works

Alzheimer's disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact.

Shivers, B. D., Hilbich, C., Multhaup, G., Salbaum, M., Beyreuther, K. T., & SEEBURG, P. H. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02952.x · Cited by 442 · see citing works

Insulin-like growth factor I protects and rescues hippocampal neurons against β-amyloid- and human amylin-induced toxicity

Doré, S., Kar, S., & Quirion, R. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4772 · Cited by 325 · see citing works

Selective increase in lipid peroxidation in the inferior temporal cortex in Alzheimer's disease

Palmer, A. M., & Burns, M. A. (1994) · Brain Research · doi:10.1016/0006-8993(94)91670-5 · Cited by 168 · see citing works

The Role of Iron in Beta Amyloid Toxicity

Schubert, D. A., & Chevion, M. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2678 · Cited by 159 · see citing works

Promotion of transition metal-induced reactive oxygen species formation by β-amyloid

Bondy, S. C., Guo‐Ross, S. X., & Truong, A. T. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00461-2 · Cited by 139 · see citing works

Brain tissue accumulates 67copper by two ligand-dependent saturable processes. A high affinity, low capacity and a low affinity, high capacity process.

Hartter, D. E., & Barnea, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)35425-0 · Cited by 125 · see citing works

Aβ25–35 induces rapid lysis of red blood cells: contrast with Aβ1–42 and examination of underlying mechanisms

Mattson, M. P., Begley, J. G., Mark, R. J., & Furukawa, K. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00824-x · Cited by 125 · see citing works

Cerebrospinal fluid trace element content in dementia

Hershey, C. O., Hershey, L. A., Varnes, A. W., Vibhakar, S. D., Lavin, P., & Strain, W. H. (1983) · Neurology · doi:10.1212/wnl.33.10.1350 · Cited by 121 · see citing works

Determination of Serum Copper and Iron in a Single Small Sample

Landers, J. W., & Zak, B. (1958) · American Journal of Clinical Pathology · doi:10.1093/ajcp/29.6_ts.590 · Cited by 121 · see citing works

A New Method for Simulating Randomly Oriented Powder Spectra in Magnetic Resonance: TheSydneyOperaHouse(SOPHE) Method

Wang, D., & Hanson, G. R. (1995) · Journal of Magnetic Resonance Series A · doi:10.1006/jmra.1995.9978 · Cited by 114 · see citing works

Amyloid β Peptides Do Not Form Peptide-derived Free Radicals Spontaneously, but Can Enhance Metal-catalyzed Oxidation of Hydroxylamines to Nitroxides

Dikalov, S., Vitek, M. P., Maples, K. R., & Mason, R. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9392 · Cited by 95 · see citing works

Exacerbation of Copper Toxicity in Primary Neuronal Cultures Depleted of Cellular Glutathione

White, A. R., Bush, A. I., Beyreuther, K. T., Masters, C. L., & Cappai, R. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722092.x · Cited by 89 · see citing works

[11] Electron paramagnetic resonance

Pilbrow, J. R., & Hanson, G. R. (1993) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(93)27013-7 · Cited by 86 · see citing works

The Structure of Neuritic Plaques in the Cerebral Cortex of Aged Rats

Vaughan, D. W., & Peters, A. (1981) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-198107000-00009 · Cited by 78 · see citing works

Alzheimer's Precursor Protein and the Use of Bathocuproine for Determining Reduction of Copper(II)

Sayre, L. M., & Multhaup, G. (1996) · Science · doi:10.1126/science.274.5294.1933 · Cited by 34 · see citing works

Quantitation of Hydrogen Peroxide Using Tris(2-carboxyethyl)phosphine

Han, J. C., Yen, S. F., Han, G., & Han, P. F. (1996) · Analytical Biochemistry · doi:10.1006/abio.1996.0059 · Cited by 22 · see citing works

Free radicals and antioxidants in normal physiological functions and human disease

Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269 · see citing works

Neurodegenerative diseases and oxidative stress

Barnham, K. J., Masters, C. L., & Bush, A. I. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1330 · Cited by 3,683 · see citing works

Reactive Oxygen Species (ROS)-Based Nanomedicine

Yang, B., Chen, Y., & Shi, J. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00626 · Cited by 2,453 · see citing works

Oxidative stress hypothesis in Alzheimer’s disease

Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383 · see citing works

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 · see citing works

The neurobiology of zinc in health and disease

Frederickson, C. J., Koh, J., & Bush, A. I. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1671 · Cited by 1,841 · see citing works

Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)

Gaggelli, E., Kozlowski, H., Valensin, D., & Valensin, G. (2006) · Chemical Reviews · doi:10.1021/cr040410w · Cited by 1,729 · see citing works

Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology

Matés, J. M. (2000) · Toxicology · doi:10.1016/s0300-483x(00)00306-1 · Cited by 1,510 · see citing works

Role of Free Radicals in the Neurodegenerative Diseases: Therapeutic Implications for Antioxidant Treatment

Halliwell, B. (2001) · Drugs & Aging · doi:10.2165/00002512-200118090-00004 · Cited by 1,502 · see citing works

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447 · see citing works

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 · see citing works

Role of Catalase in Oxidative Stress- and Age-Associated Degenerative Diseases

Nandi, A., Yan, L.-J., Jana, C. K., & Das, N. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9613090 · Cited by 1,185 · see citing works

Metals, oxidative stress and neurodegenerative disorders

Jomová, K., Vondráková, D., Lawson, M. K., & Valko, M. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0563-x · Cited by 1,053 · see citing works

Selective neuronal vulnerability to oxidative stress in the brain

Wang, X. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00012 · Cited by 1,008 · see citing works

Antioxidant Activity/Capacity Measurement. 1. Classification, Physicochemical Principles, Mechanisms, and Electron Transfer (ET)-Based Assays

Apak, R., Özyürek, M., Güçlü, K., & Çapanoğlu, E. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b04739 · Cited by 988 · see citing works

Early-onset Amyloid Deposition and Cognitive Deficits in Transgenic Mice Expressing a Double Mutant Form of Amyloid Precursor Protein 695

Chishti, M. A., Yang, D.-S., Janus, C., Phinney, A. L., Horne, P., Pearson, J., Strome, R., Zuker, N., Loukides, J., French, J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100710200 · Cited by 955 · see citing works

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 881 · see citing works

Oxidative Stress and Neurotoxicity

Sayre, L. M., Perry, G. L., & Smith, M. A. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700210j · Cited by 868 · see citing works

Oxidative Stress and the Pathogenesis of Alzheimer's Disease

Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855 · see citing works

Oxidative stress in Alzheimer’s disease

Chen, Z., & Zhong, C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1423-y · Cited by 797 · see citing works

Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?

Ischiropoulos, H., & Beckman, J. S. (2003) · Journal of Clinical Investigation · doi:10.1172/jci200317638 · Cited by 748 · see citing works

Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity

Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735 · see citing works

Metals and neuroscience

Bush, A. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00073-3 · Cited by 731 · see citing works

Rapid Restoration of Cognition in Alzheimer's Transgenic Mice with 8-Hydroxy Quinoline Analogs Is Associated with Decreased Interstitial Aβ

Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672 · see citing works

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 653 · see citing works

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641 · see citing works

Alzheimer's Disease: From Pathology to Therapeutic Approaches

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626 · see citing works

Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo

Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620 · see citing works

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 · see citing works

Iron neurochemistry in Alzheimer's disease and Parkinson's disease: targets for therapeutics

Belaidi, A. A., & Bush, A. I. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13425 · Cited by 580 · see citing works

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 580 · see citing works

Therapeutics for Alzheimer's Disease Based on the Metal Hypothesis

Bush, A. I., & Tanzi, R. E. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.001 · Cited by 566 · see citing works

Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases

Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works

Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide

Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530 · see citing works

Copper in disorders with neurological symptoms: Alzheimer’s, Menkes, and Wilson diseases

Strausak, D., Mercer, J. F. B., Dieter, H. H., Stremmel, W., & Multhaup, G. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00454-3 · Cited by 508 · see citing works

Copper in the brain and Alzheimer’s disease

Hung, Y. H., Bush, A. I., & Cherny, R. A. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 496 · see citing works

Biological metals and metal-targeting compounds in major neurodegenerative diseases

Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497 · see citing works

Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease

Karuppagounder, S. S., Pinto, J. T., Xu, H., Chen, H., Beal, M. F., & Gibson, G. E. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.10.008 · Cited by 488 · see citing works

Striking while the iron is hot: Iron metabolism and ferroptosis in neurodegeneration

Masaldan, S., Bush, A. I., Devos, D., Rolland, A., & Moreau, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.033 · Cited by 485 · see citing works

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 · see citing works

Metal dyshomeostasis and oxidative stress in Alzheimer’s disease

Greenough, M. A., Camakaris, J., & Bush, A. I. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.08.014 · Cited by 439 · see citing works

Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)

Kozłowski, H., Łuczkowski, M., Remelli, M., & Valensin, D. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.013 · Cited by 438 · see citing works

Redox‐Active Metals, Oxidative Stress, and Alzheimer's Disease Pathology

HUANG, X., MOIR, R. D., TANZI, R. E., BUSH, A. I., & ROGERS, J. T. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.012 · Cited by 425 · see citing works

The chemistry of Alzheimer’s disease

Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417 · see citing works

Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease

Rasia, R. M., Bertoncini, C. W., Marsh, D., Hoyer, W., Cherny, D., Zweckstetter, M., Griesinger, C., Jovin, T. M., & Fernández, C. O. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407881102 · Cited by 407 · see citing works

Targeted nanoparticles for drug delivery through the blood–brain barrier for Alzheimer's disease

Roney, C. A., Kulkarni, P. V., Arora, V., Antich, P. P., Bonte, F. J., Wu, A., Mallikarjuana, N. N., Manohar, S. K., Liang, H., Kulkarni, A. R., et al. (2005) · Journal of Controlled Release · doi:10.1016/j.jconrel.2005.07.024 · Cited by 408 · see citing works

Oxidative Stress, Amyloid-β Peptide, and Altered Key Molecular Pathways in the Pathogenesis and Progression of Alzheimer’s Disease

Butterfield, D. A., & Boyd-Kimball, D. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170543 · Cited by 403 · see citing works

Evidence that the β-Amyloid Plaques of Alzheimer's Disease Represent the Redox-silencing and Entombment of Aβ by Zinc

Cuajungco, M. P., Goldstein, L. E., Nunomura, A., Smith, M. A., Lim, J. T., Atwood, C., Huang, X., Farrag, Y. W., Perry, G. L., & Bush, A. I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000165200 · Cited by 392 · see citing works

Oxidative stress signalling in Alzheimer's disease

Zhu, X., Raina, A. K., Lee, H., Casadesús, G., Smith, M. A., & Perry, G. L. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.012 · Cited by 390 · see citing works

Clusterin in Alzheimer’s Disease: Mechanisms, Genetics, and Lessons From Other Pathologies

Foster, E. M., Dangla-Valls, A., Lovestone, S., Ribe, E. M., & Buckley, N. J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00164 · Cited by 381 · see citing works

Redox-active iron mediates amyloid-β toxicity

Rottkamp, C. A., Raina, A. K., Zhu, X., Gaier, E., Bush, A. I., Atwood, C., Chevion, M., Perry, G. L., & Smith, M. A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00494-9 · Cited by 376 · see citing works

Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease

Schöneich, C. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.009 · Cited by 372 · see citing works

The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer’s disease

Miranda, S., Opazo, C., Larrondo, L. F., Muñoz, F. J., Ruiz, F., Leighton, F., & Inestrosa, N. C. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00015-0 · Cited by 369 · see citing works

Synaptically released zinc: Physiological functions and pathological effects

Frederickson, C. J., & Bush, A. I. (2001) · BioMetals · doi:10.1023/a:1012934207456 · Cited by 360 · see citing works

Metallostasis in Alzheimer's disease

Ayton, S., Lei, P., & Bush, A. I. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.558 · Cited by 354 · see citing works

Metals and amyloid‐β in Alzheimer's disease

Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., & Li, Q. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00434.x · Cited by 353 · see citing works

Overexpression of Alzheimer's Disease Amyloid-β Opposes the Age-dependent Elevations of Brain Copper and Iron

Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K. T., Masters, C. L., Bush, A. I., & Li, Q. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 352 · see citing works

Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

Brown, D. R., & Kozłowski, H. (2004) · Dalton Transactions · doi:10.1039/b401985g · Cited by 343 · see citing works

Oxidative stress in Alzheimer's disease

Chauhan, V. P. S., & Chauhan, A. (2006) · Pathophysiology · doi:10.1016/j.pathophys.2006.05.004 · Cited by 341 · see citing works

Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease

Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332 · see citing works

The essential elements of Alzheimer’s disease

Lei, P., Ayton, S., & Bush, A. I. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.008207 · Cited by 336 · see citing works

Copper-Dependent Inhibition of Human Cytochrome<i>c</i>Oxidase by a Dimeric Conformer of Amyloid-β_1-42

Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327 · see citing works

Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice

Bayer, T. A., Schäfer, S., Simons, A., Kemmling, A., Kamer, T., Tepest, R., Eckert, A., Schüssel, K., Eikenberg, O., Sturchler, C., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332818100 · Cited by 325 · see citing works

The Antioxidant Mechanisms Underlying the Aged Garlic Extract- and S-Allylcysteine-Induced Protection

Colín-González, A. L., Santana-Martínez, R. A., Silva‐Islas, C. A., Chánez‐Cárdenas, M. E., Santamarı́a, A., & Maldonado, P. D. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/907162 · Cited by 324 · see citing works

Metal complexing agents as therapies for Alzheimer’s disease

Bush, A. I. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00120-3 · Cited by 310 · see citing works

Dementia of Alzheimer’s disease and other neurodegenerative disorders—memantine, a new hope

Sonkusare, S. K., Kaul, C. L., & Ramarao, P. (2004) · Pharmacological Research · doi:10.1016/j.phrs.2004.05.005 · Cited by 306 · see citing works

Nanotechnology-based drug delivery systems for the treatment of Alzheimer’s disease

Fonseca‐Santos, B., Chorilli, M., & Gremião, M. P. D. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s87148 · Cited by 313 · see citing works

A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage

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 · see citing works

Management of oxidative stress and other pathologies in Alzheimer’s disease

Simunkova, M., Alwasel, S. H., Alhazza, I. M., Jomova, K., Kollar, V., Rusko, M., & Valko, M. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02538-y · Cited by 303 · see citing works

Antioxidant neuroprotection in Alzheimer’s disease as preventive and therapeutic approach2 2This article is part of a series of reviews on “Causes and Consequences of Oxidative Stress in Alzheimer’s Disease.” The full list of papers may be found on the homepage of the journal.

Behl, C., & Moosmann, B. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00883-3 · Cited by 301 · see citing works

Amyloid-β: a chameleon walking in two worlds: a review of the trophic and toxic properties of amyloid-β

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 292 · see citing works

Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease

Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 288 · see citing works

Aluminium in Alzheimer?s disease: are we still at a crossroad?

Gupta, V. B., Anitha, S., Hegde, M. L., Zecca, L., Garruto, R. M., Ravid, R., Shankar, S. K., Stein, R., Shanmugavelu, P., & Rao, K. S. J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4317-3 · Cited by 290 · see citing works

Copper and Zinc Binding to Amyloid‐β: Coordination, Dynamics, Aggregation, Reactivity and Metal‐Ion Transfer

Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285 · see citing works

Pyruvate Released by Astrocytes Protects Neurons from Copper-Catalyzed Cysteine Neurotoxicity

Wang, X. F., & Cynader, M. S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-10-03322.2001 · Cited by 285 · see citing works

Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics

Duce, J. A., & Bush, A. I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.003 · Cited by 281 · see citing works

Ribosomal RNA in Alzheimer Disease Is Oxidized by Bound Redox-active Iron

Honda, K., Smith, M. A., Zhu, X., Baus, D., Merrick, W. C., Tartakoff, A. M., Hattier, T., Harris, P. L., Siedlak, S. L., Fujioka, H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500526200 · Cited by 280 · see citing works

Neuroprotective effects of apigenin against inflammation, neuronal excitability and apoptosis in an induced pluripotent stem cell model of Alzheimer’s disease

Balez, R., Steiner, N., Engel, M., Muñoz, S. S., Lum, J. S., Wu, Y., Wang, D., Vallotton, P., Sachdev, P. S., O’Connor, M. D., et al. (2016) · Scientific Reports · doi:10.1038/srep31450 · Cited by 278 · see citing works

Elevated cortical zinc in Alzheimer disease

Religa, D., Strozyk, D., Cherny, R. A., Volitakis, I., Haroutunian, V., Winblad, B. G., Näslund, J., & Bush, A. I. (2006) · Neurology · doi:10.1212/01.wnl.0000223644.08653.b5 · Cited by 272 · see citing works

Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain

Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300629200 · Cited by 274 · see citing works

Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State

Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P. (2007) · ChemBioChem · doi:10.1002/cbic.200700111 · Cited by 273 · see citing works

Homocysteine potentiates β‐amyloid neurotoxicity: role of oxidative stress

Ho, P. I., Collins, S. C., Dhitavat, S., Ortiz, D., Ashline, D. J., Rogers, E. J., & Shea, T. B. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00384.x · Cited by 271 · see citing works

Novel Tacrine−8-Hydroxyquinoline Hybrids as Multifunctional Agents for the Treatment of Alzheimer’s Disease, with Neuroprotective, Cholinergic, Antioxidant, and Copper-Complexing Properties

Fernández‐Bachiller, M. I., Pérez, C., González-Muñoz, G. C., Conde, S., López, M. G., Villarroya, M., Garcı́a, A. G., & Rodrı́guez-Franco, M. I. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100329q · Cited by 270 · see citing works

Dietary Copper and High Saturated and trans Fat Intakes Associated With Cognitive Decline

Morris, M. C., Evans, D. A., Tangney, C., Bienias, J. L., Schneider, J. A., Wilson, R. S., & Scherr, P. A. (2006) · Archives of Neurology · doi:10.1001/archneur.63.8.1085 · Cited by 268 · see citing works

The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1–42)-induced oxidative stress and neurotoxicity

Butterfield, D. A., & Debra Boyd-kimball, A. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.10.014 · Cited by 267 · see citing works

The role of metallobiology and amyloid-β peptides in Alzheimer's disease

Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266 · see citing works

Tyrosine gated electron transfer is key to the toxic mechanism of Alzheimer's disease β‐amyloid

Barnham, K. J., Hæffner, F., Ciccotosto, G. D., Curtain, C. C., Tew, D. J., Mavros, C., Beyreuther, K. T., Carrington, D., Masters, C. L., Cherny, R. A., et al. (2004) · The FASEB Journal · doi:10.1096/fj.04-1890fje · Cited by 262 · see citing works

Formation of hydrogen peroxide and hydroxyl radicals from Aβ and α-synuclein as a possible mechanism of cell death in Alzheimer’s disease and Parkinson’s disease

Tabner, B. J., Turnbull, S., El‐Agnaf, O. M. A., & Allsop, D. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00801-8 · Cited by 261 · see citing works

Homocysteine potentiates copper‐ and amyloid beta peptide‐mediated toxicity in primary neuronal cultures: possible risk factors in the Alzheimer's‐type neurodegenerative pathways

White, A. R., Huang, X., Jobling, M. F., Barrow, C. J., Beyreuther, K., Masters, C. L., Bush, A. I., & Cappai, R. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00178.x · Cited by 258 · see citing works

Aβ-mediated ROS production by Cu ions: Structural insights, mechanisms and relevance to Alzheimer's disease

Hureau, C., & Faller, P. (2009) · Biochimie · doi:10.1016/j.biochi.2009.03.013 · Cited by 259 · see citing works

Low levels of copper disrupt brain amyloid-β homeostasis by altering its production and clearance

Singh, I., Sagare, A. P., Coma, M., Perlmutter, D., Gelein, R. M., Bell, R. D., Deane, R. J., Zhong, E., Parisi, M., Ciszewski, J. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302212110 · Cited by 253 · see citing works

Antioxidants as treatment for neurodegenerative disorders

Moosmann, B., & Behl, C. (2002) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.11.10.1407 · Cited by 253 · see citing works

Selective and sensitive detection of metal ions by plasmonic resonance energy transfer-based nanospectroscopy

Choi, Y., Park, Y., Kang, T., & Lee, L. P. (2009) · Nature Nanotechnology · doi:10.1038/nnano.2009.258 · Cited by 250 · see citing works

The transition metals copper and iron in neurodegenerative diseases

Rivera-Mancía, S., Pérez‐Neri, I., Rı́os, C., Tristán-López, L. A., Rivera-Espinosa, L., & Montes, S. (2010) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2010.04.010 · Cited by 243 · see citing works

Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease

Crouch, P. J., Harding, S.-M. E., White, A. R., Camakaris, J., Bush, A. I., & Masters, C. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.013 · Cited by 244 · see citing works

New Insights on How Metals Disrupt Amyloid β-Aggregation and Their Effects on Amyloid-β Cytotoxicity

Yoshiike, Y., Tanemura, K., Murayama, O., Akagi, T., Murayama, M., Sato, S., Sun, X., Tanaka, N., & Takashima, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010706200 · Cited by 244 · see citing works

Zinc takes the center stage: its paradoxical role in Alzheimer’s disease

Cuajungco, M. P., & Faget, K. Y. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(02)00219-9 · Cited by 242 · see citing works

Hydrogen Peroxide Is Generated during the Very Early Stages of Aggregation of the Amyloid Peptides Implicated in Alzheimer Disease and Familial British Dementia

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 241 · see citing works

Redox active metal-induced oxidative stress in biological systems

Jomová, K., Baroš, S., & Valko, M. (2012) · Transition Metal Chemistry · doi:10.1007/s11243-012-9583-6 · Cited by 244 · see citing works

Elevation of serum copper levels in Alzheimer’s disease

Squitti, R., Lupoi, D., Pasqualetti, P., Forno, G. D., Vernieri, F., Chiovenda, P., Rossi, L. C., Cortesi, M., Cassetta, E., & Rossini, P. M. (2002) · Neurology · doi:10.1212/wnl.59.8.1153 · Cited by 236 · see citing works

Cu(II) Potentiation of Alzheimer Aβ1-40 Cytotoxicity and Transition on its Secondary Structure

Dai, X., Sun, Y., & Jiang, Z.-F. (2006) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2006.00228.x · Cited by 34 · see citing works

Copper and amyloid β: interactions in Alzheimer's disease

Yusof, M., & Sun, A. Y. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.81.s1.20_14.x · Cited by 1 · see citing works

Redox Reactions of Copper Complexes Formed with Different β-Amyloid Peptides and Their Neuropathalogical Relevance

Jiang, D., Men, L., Wang, J., Zhang, Y., Chickenyen, S., Wang, Y., & Zhou, F. (2007) · Biochemistry · doi:10.1021/bi700508n · Cited by 202 · see citing works

The Cu(II)/Aβ/Human Serum Albumin Model of Control Mechanism for Copper-Related Amyloid Neurotoxicity

Rózga, M., & Bal, W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900358j · Cited by 51 · see citing works

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 580 · see citing works