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

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

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

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

Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921

Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731

Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus

Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522

Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447

The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene

Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367

Iron accumulation in Alzheimer disease is a source of redox-generated free radicals

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,365

Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice

White, A. R., Reyes, R., Mercer, J. F. B., Camakaris, J., Zheng, H., Bush, A. I., Multhaup, G., Beyreuther, K. T., Masters, C. L., & Cappai, R. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01861-2 · Cited by 287

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 288

Iron and Alzheimer’s Disease: An Update on Emerging Mechanisms

Lane, D. J. R., Ayton, S., & Bush, A. I. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-179944 · Cited by 287

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

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 273

Drosophila melanogaster as a model organism for Alzheimer’s disease

Prüßing, K., Voigt, A., & Schulz, J. B. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-35 · Cited by 235

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

Copper and Zinc Binding Modulates the Aggregation and Neurotoxic Properties of the Prion Peptide PrP106−126

Jobling, M. F., Huang, X., Stewart, L. R., Barnham, K. J., Curtain, C. C., Volitakis, I., Perugini, M. A., White, A. R., Cherny, R. A., Masters, C. L., et al. (2001) · Biochemistry · doi:10.1021/bi0029088 · Cited by 263

Maculas Affected by Age-Related Macular Degeneration Contain Increased Chelatable Iron in the Retinal Pigment Epithelium and Bruch's Membrane

Hahn, P. (2003) · Archives of Ophthalmology · doi:10.1001/archopht.121.8.1099 · Cited by 258

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 261

High-Efficiency in Vitro and in Vivo Detection of Zn2+ by Dye-Assembled Upconversion Nanoparticles

Peng, J., Wang, X., Teoh, C. L., Han, S., Kim, B., Samanta, A., Er, J. C., Wang, L., Yuan, L., Liu, X., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/ja5115248 · Cited by 255

Dopamine promotes α‐synuclein aggregation into SDS‐resistant soluble oligomers via a distinct folding pathway

Cappai, R., Leck, S., Tew, D. J., Williamson, N. A., Smith, D. P., Galatis, D., Sharpies, R. A., Curtain, C. C., Ali, F. E. A., Cherny, R. A., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-3437fje · Cited by 254

High‐resolution NMR studies of the zinc‐binding site of the Alzheimer's amyloid β‐peptide

Danielsson, J., Pierattelli, R., Banci, L., & Gräslund, A. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05563.x · Cited by 253

Copper(II) Binding to α-Synuclein, the Parkinson’s Protein

Lee, J. C., Gray, H. B., & Winkler, J. R. (2008) · Journal of the American Chemical Society · doi:10.1021/ja711415b · Cited by 246

Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry

Whittal, R. M., Ball, H. L., Cohen, F. E., Burlingame, A. L., Prusiner, S. B., & Baldwin, M. A. (2000) · Protein Science · doi:10.1110/ps.9.2.332 · Cited by 245

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

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 254

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 245

Trace metal contamination initiates the apparent auto-aggregation, amyloidosis, and oligomerization of Alzheimer?s A? peptides

Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0602-8 · Cited by 241

Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics

Masters, C. L., Cappai, R., Barnham, K. J., & Villemagne, V. L. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03989.x · Cited by 242

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 237

Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis

Jaikaran, E. T. A. S., Higham, C. E., Serpell, L. C., Zurdo, J., Gross, M., Clark, A., & Fraser, P. E. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4593 · Cited by 236

Role of Copper in the Onset of Alzheimer’s Disease Compared to Other Metals

Bagheri, S., Squitti, R., Haertlé, T., Siotto, M., & Saboury, A. A. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00446 · Cited by 235

Metal Ions Differentially Influence the Aggregation and Deposition of Alzheimer's β-Amyloid on a Solid Template

Ha, C., Ryu, J., & Park, C. B. (2007) · Biochemistry · doi:10.1021/bi7000032 · Cited by 231

Design, Synthesis, and Evaluation of Multitarget-Directed Resveratrol Derivatives for the Treatment of Alzheimer’s Disease

Lu, C., Guo, Y., Yan, J., Luo, Z., Luo, H., Yan, M., Huang, L., & Li, X. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400567s · Cited by 230

Coordination abilities of the 1–16 and 1–28 fragments of β-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study

Kowalik‐Jankowska, T., Ruta, M., Wiśniewska, K., & Łankiewicz, L. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(03)00128-4 · Cited by 222

Interactions of Zn(ii) and Cu(ii) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity

Tõugu, V., Tiiman, A., & Palumaa, P. (2011) · Metallomics · doi:10.1039/c0mt00073f · Cited by 224

Toxicity of Amyloid β Peptide: Tales of Calcium, Mitochondria, and Oxidative Stress

Canevari, L., Abramov, A. Y., & Duchen, M. R. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000014834.06405.af · Cited by 227

Treatment of Alzheimer’s Disease with Clioquinol

Regland, B., Lehmann, W., Abedini, I., Blennow, K., Jonsson, M., Karlsson, I., Sjögren, M., Wallin, A., Xilinas, M., & Gottfries, C.-G. (2001) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000051288 · Cited by 220

The Alzheimer's Disease Amyloid Precursor Protein Modulates Copper-Induced Toxicity and Oxidative Stress in Primary Neuronal Cultures

White, A. R., Multhaup, G., Maher, F., Bellingham, S. A., Camakaris, J., Zheng, H., Bush, A. I., Beyreuther, K., Masters, C. L., & Cappai, R. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-21-09170.1999 · Cited by 220

Review: Modulating Factors in Amyloid-β Fibril Formation

McLaurin, J., Yang, D.-S., Yip, C. M., & Fraser, P. E. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4289 · Cited by 217

Redox metals and neu rodegenerative disease

Sayre, L. M., Perry, G. L., & Smith, M. A. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80035-0 · Cited by 217

Benefits from Dietary Polyphenols for Brain Aging and Alzheimer’s Disease

Rossi, L. C., Mazzitelli, S., Arciello, M., Capo, C. R., & Rotilio, G. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9696-7 · Cited by 223

Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide

Tõugu, V., Tiiman, A., & Palumaa, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05061.x · Cited by 219

Designing Stimuli‐Responsive Upconversion Nanoparticles that Exploit the Tumor Microenvironment

Ovais, M., Mukherjee, S., Pramanik, A., Das, D., Mukherjee, A., Raza, A., & Chen, C. (2020) · Advanced Materials · doi:10.1002/adma.202000055 · Cited by 218

Zinc-Amyloid β Interactions on a Millisecond Time-Scale Stabilize Non-fibrillar Alzheimer-Related Species

Noy, D., Solomonov, I., Sinkevich, O., Arad, T., Kjær, K., & Sagi, I. (2008) · Journal of the American Chemical Society · doi:10.1021/ja076282l · Cited by 216

Magnesium Inhibits Spontaneous and Iron-induced Aggregation of α-Synuclein

Golts, N., Snyder, H. M., Frasier, M. A., Theisler, C. M., Choi, P., & Wolozin, B. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107866200 · Cited by 221

Metal Chelation as a Potential Therapy for Alzheimer's Disease

Cuajungco, M. P., Faget, K. Y., Huang, X., Tanzi, R. E., & Bush, A. I. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06938.x · Cited by 220

Design, Selection, and Characterization of Thioflavin-Based Intercalation Compounds with Metal Chelating Properties for Application in Alzheimer’s Disease

Rodríguez-Rodríguez, C., Sánchez de Groot, N., Rimola, A., Álvarez-Larena, Á., Lloveras, V., Vidal-Gancedo, J., Ventura, S., Vendrell, J., Sodupe, M., & González-Duarte, P. (2009) · Journal of the American Chemical Society · doi:10.1021/ja806062g · Cited by 210

Copper(II) Binding to Amyloid-β Fibrils of Alzheimer’s Disease Reveals a Picomolar Affinity: Stoichiometry and Coordination Geometry Are Independent of Aβ Oligomeric Form

Sarell, C. J., Syme, C. D., Rigby, S. E. J., & Viles, J. H. (2009) · Biochemistry · doi:10.1021/bi900254n · Cited by 209

Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease

Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204

Amyloid beta ion channel: 3D structure and relevance to amyloid channel paradigm

Lal, R., Lin, H., & Quist, A. P. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.04.021 · Cited by 207

Current Status of Metals as Therapeutic Targets in Alzheimer's Disease

Finefrock, A. E., Bush, A. I., & Doraiswamy, P. M. (2003) · Journal of the American Geriatrics Society · doi:10.1046/j.1532-5415.2003.51368.x · Cited by 203

Natural product-based amyloid inhibitors

Velander, P., Wu, L., Henderson, F. E., Zhang, S., Bevan, D. R., & Xu, B. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.04.004 · Cited by 207

Metal ions, Alzheimer's disease and chelation therapy

Budimir, A. (2011) · Acta Pharmaceutica · doi:10.2478/v10007-011-0006-6 · Cited by 202

Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide

Sharma, A. K., Pavlova, S. T., Kim, J., Finkelstein, D., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja210588m · Cited by 202

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 204

In vivo reduction of amyloid-β by a mutant copper transporter

Phinney, A. L., Drisaldi, B., Schmidt, S. D., Lugowski, S. J., Coronado, V. A., Liang, Y., Horne, P., Yang, J., Sekoulidis, J., Coomaraswamy, J., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332851100 · Cited by 204

Metal Ions, pH, and Cholesterol Regulate the Interactions of Alzheimer's Disease Amyloid-β Peptide with Membrane Lipid

Curtain, C. C., Ali, F. E. A., Smith, D. G., Bush, A. I., Masters, C. L., & Barnham, K. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m205455200 · Cited by 200

Substoichiometric Levels of Cu2+ Ions Accelerate the Kinetics of Fiber Formation and Promote Cell Toxicity of Amyloid-β from Alzheimer Disease

Sarell, C. J., Wilkinson, S. R., & Viles, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.171355 · Cited by 199

Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s β by Solid-State NMR Spectroscopy

Parthasarathy, S., Long, F., Miller, Y., Xiao, Y., McElheny, D., Thurber, K. R., Ma, B., Nussinov, R., & Ishii, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja1072178 · Cited by 200

Free Radical Reactions of Methionine in Peptides: Mechanisms Relevant to β-Amyloid Oxidation and Alzheimer's Disease

Schöneich, C., Pogocki, D., Hug, G. L., & Bobrowski, K. (2003) · Journal of the American Chemical Society · doi:10.1021/ja036733b · Cited by 199

Histidine-13 Is a Crucial Residue in the Zinc Ion-Induced Aggregation of the Aβ Peptide of Alzheimer's Disease

Liu, S.-T., Howlett, G. J., & Barrow, C. J. (1999) · Biochemistry · doi:10.1021/bi990205o · Cited by 199

Copper as a key regulator of cell signalling pathways

Grubman, A., & White, A. R. (2014) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2014.11 · Cited by 199

Concentration Dependent Cu2+Induced Aggregation and Dityrosine Formation of the Alzheimer's Disease Amyloid-β Peptide

Smith, D. P., Ciccotosto, G. D., Tew, D. J., Fodero‐Tavoletti, M. T., Johanssen, T., Masters, C. L., Barnham, K. J., & Cappai, R. (2007) · Biochemistry · doi:10.1021/bi0620961 · Cited by 193

Metal swap between Zn7-metallothionein-3 and amyloid-β–Cu protects against amyloid-β toxicity

Meloni, G., Sonois, V., Delaine, T., Guilloreau, L., Gillet, A., Teissié, J., Faller, P., & Vašák, M. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.89 · Cited by 190

The lipophilic metal chelator DP-109 reduces amyloid pathology in brains of human β-amyloid precursor protein transgenic mice

Lee, J., Friedman, J. E., Angel, I., Kozak, A., & Koh, J. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.01.005 · Cited by 190

Two-Dimensional Structure of β-Amyloid(10−35) Fibrils

Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C. (2000) · Biochemistry · doi:10.1021/bi991527v · Cited by 188

Neurotoxic, Redox-competent Alzheimer's β-Amyloid Is Released from Lipid Membrane by Methionine Oxidation

Barnham, K. J., Ciccotosto, G. D., Tickler, A. K., Ali, F. E. A., Smith, D. G., Williamson, N. A., Lam, Y.-H., Carrington, D., Tew, D. J., Kocak, G., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305494200 · Cited by 191

Oxidation of Cholesterol by Amyloid Precursor Protein and β-Amyloid Peptide

Nelson, T. J., & Alkon, D. L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409071200 · Cited by 185

A central role for dityrosine crosslinking of Amyloid-β in Alzheimer’s disease

Al‐Hilaly, Y. K., Williams, T. L., Stewart-Parker, M., Ford, L. K., Skaria, E., Cole, M., Bucher, W. G., Morris, K. L., Sada, A. A., Thorpe, J. R., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-83 · Cited by 187

Brain Ferritin Iron as a Risk Factor for Age at Onset in Neurodegenerative Diseases

Bartzokis, G., Tishler, T. A., Shin, I., Lu, P. H., & Cummings, J. L. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.019 · Cited by 184

Copper in Alzheimer's Disease: A Meta-Analysis of Serum, Plasma, and Cerebrospinal Fluid Studies

Bucossi, S., Ventriglia, M., Panetta, V., Salustri, C., Pasqualetti, P., Mariani, S., Siotto, M., Rossini, P. M., & Squitti, R. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-101473 · Cited by 186

The Alzheimer’s therapeutic PBT2 promotes amyloid‐β degradation and GSK3 phosphorylation via a metal chaperone activity

Crouch, P. J., Savva, M. S., Hung, L. W., Donnelly, P. S., Mot, A. I., Parker, S. J., Greenough, M. A., Volitakis, I., Adlard, P. A., Cherny, R. A., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07402.x · Cited by 183

Effect of Metallic Ions on Silk Formation in the Mulberry Silkworm, Bombyx m ori

Li, Z., Chen, X., Shao, Z., Huang, Y., & Knight, D. P. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp050883m · Cited by 183

Metal ions as modulators of protein conformation and misfolding in neurodegeneration

Leal, S. S., Botelho, H. M., & Gomes, C. M. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.04.004 · Cited by 187

Zn(II)‐ and Cu(II)‐induced non‐fibrillar aggregates of amyloid‐β (1–42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators

Tõugu, V., Karafin, A., Zovo, K., Chung, R. S., Howells, C., West, A. K., & Palumaa, P. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06269.x · Cited by 181

Iron: The Redox-active Center of Oxidative Stress in Alzheimer Disease

Castellani, R. J., Moreira, P. I., Liu, G., Dobson, J., Perry, G., Smith, M. A., & Zhu, X. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9360-7 · Cited by 180

Amyloid-β is an antioxidant for lipoproteins in cerebrospinal fluid and plasma

Kontush, A., Berndt, C., Weber, W., Akopyan, V., Arlt, S., Schippling, S., & Beisiegel, U. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00458-5 · Cited by 180

Novel Approaches for the Treatment of Alzheimer’s and Parkinson’s Disease

Bulck, M. V., Sierra‐Magro, A., Alarcón-Gil, J., Pérez‐Castillo, A., & Morales-Garcia, J. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030719 · Cited by 186

N-Terminal Deletions Modify the Cu2+Binding Site in Amyloid-β

Karr, J. W., Akintoye, H., Kaupp, L. J., & Szalai, V. A. (2005) · Biochemistry · doi:10.1021/bi047611e · Cited by 178

Amyloid-β: an antioxidant that becomes a pro-oxidant and critically contributes to Alzheimer’s disease

Kontush, A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00688-8 · Cited by 178

Effects of aluminum on the neurotoxicity of primary cultured neurons and on the aggregation of β-amyloid protein

Kawahara, M., Kato, M., & Kuroda, Y. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00475-0 · Cited by 173

Site-Specific Interactions of Cu(II) with α and β-Synuclein: Bridging the Molecular Gap between Metal Binding and Aggregation

Binolfi, A., Lamberto, G. R., Durán, R., Quintanar, L., Bertoncini, C. W., Souza, J. M., Červeñanský, C., Zweckstetter, M., Griesinger, C., & Fernández, C. O. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803494v · Cited by 173

Roles of Oxidative Stress in Synaptic Dysfunction and Neuronal Cell Death in Alzheimer’s Disease

Plascencia‐Villa, G., & Perry, G. L. (2023) · Antioxidants · doi:10.3390/antiox12081628 · Cited by 178

Cerium oxide caged metal chelator: anti-aggregation and anti-oxidation integrated H2O2-responsive controlled drug release for potential Alzheimer's disease treatment

Li, M., Shi, P., Xu, C., Ren, J., & Qu, X. (2013) · Chemical Science · doi:10.1039/c3sc50697e · Cited by 166

Challenges Associated with Metal Chelation Therapy in Alzheimer's Disease

Hegde, M. L., Bharathi, P., Suram, A., Venugopal, C., Jagannathan, R., Poddar, P., Srinivas, P., Sambamurti, K., Rao, K. S. J., Ščančar, J., et al. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1068 · Cited by 167

Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity

Matlack, K. E. S., Tardiff, D. F., Narayan, P. S., Hamamichi, S., Caldwell, K. A., Caldwell, G. A., & Lindquist, S. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402228111 · Cited by 166

Chronic copper exposure exacerbates both amyloid and tau pathology and selectively dysregulates cdk5 in a mouse model of AD

Kitazawa, M., Cheng, D., & LaFerla, F. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05901.x · Cited by 165

Iron dysregulation in Alzheimer's disease: Multimodal brain permeable iron chelating drugs, possessing neuroprotective-neurorescue and amyloid precursor protein-processing regulatory activities as therapeutic agents

Mandel, S., Amit, T., Bar-Am, O., & Youdim, M. B. H. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.06.001 · Cited by 164

Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation

Morgan, C. J., Gelfand, M. A., Atreya, C., & Miranker, A. D. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4661 · Cited by 164

Serum Albumin Prevents Protein Aggregation and Amyloid Formation and Retains Chaperone-like Activity in the Presence of Physiological Ligands

Finn, T., Nunez, A. C., Sunde, M., & Easterbrook‐Smith, S. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.372961 · Cited by 165

Copper and prion disease

Brown, D. R. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00453-1 · Cited by 161

Metallobiology and therapeutic chelation of biometals (copper, zinc and iron) in Alzheimer’s disease: Limitations, and current and future perspectives

Fasae, K. D., Abolaji, A. O., Faloye, T. R., Odunsi, A., Oyetayo, B. O., Enya, J. I., Rotimi, J. A., Akinyemi, R., Whitworth, A. J., & Aschner, M. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126779 · Cited by 161

Aluminium(III) as a promoter of cellular oxidation

Zatta, P. F., Kiss, T., Suwalsky, M., & Berthon, G. (2002) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(02)00074-7 · Cited by 160

Amyloid-β Binds Cu 2+ in a Mononuclear Metal Ion Binding Site

Karr, J. W., Kaupp, L. J., & Szalai, V. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0488028 · Cited by 160

Metal Ion-dependent Effects of Clioquinol on the Fibril Growth of an Amyloid β Peptide

Raman, B., Ban, T., Yamaguchi, K., Sakai, M., Kawai, T., Naiki, H., & Goto, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500309200 · Cited by 158

Protein aggregation: Mechanisms and functional consequences

Invernizzi, G., Papaleo, E., Sabaté, R., & Ventura, S. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.05.023 · Cited by 165

Copper deficiency and neurological disorders in man and animals

Zatta, P. F., & Frank, A. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.10.001 · Cited by 159

Synthesis, Characterization, and Metal Coordinating Ability of Multifunctional Carbohydrate-Containing Compounds for Alzheimer's Therapy

Storr, T., Merkel, M., Song-Zhao, G. X., Scott, L. E., Green, D. E., Bowen, M. L., Thompson, K. H., Patrick, B. O., Schugar, H. J., & Orvig, C. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068965r · Cited by 156

Amyloid β‐protein (Aβ)1–40 protects neurons from damage induced by Aβ1–42 in culture and in rat brain

Zou, K., Kim, D. S., Kakio, A., Byun, K., Gong, J., Kim, J. W., Kim, M. J., Sawamura, N., Nishimoto, S., Matsuzaki, K., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02018.x · Cited by 160

Zinc and copper modulate Alzheimer Aβ levels in human cerebrospinal fluid

Altschul, D., Launer, L. J., Adlard, P. A., Cherny, R. A., Tsatsanis, A., Volitakis, I., Blennow, K., Petrovitch, H., White, L. R., & Bush, A. I. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.10.012 · Cited by 154

Aβ as a bioflocculant: implications for the amyloid hypothesis of Alzheimer’s disease

Robinson, S. R., & Bishop, G. M. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00342-6 · Cited by 155

The art of building multifunctional metal-binding agents from basic molecular scaffolds for the potential application in neurodegenerative diseases

Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151

Oxidative processes in Alzheimer's disease: the role of Aβ-metal interactions

Lynch, T. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00112-1 · Cited by 151

Binding of Zn(II), Cu(II), and Fe(II) ions to alzheimer's Aß peptide studied by fluorescence

Garzon-Rodriguez, W., Yatsimirsky, A. K., & Glabe, C. G. (1999) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00357-1 · Cited by 148

Clioquinol Mediates Copper Uptake and Counteracts Copper Efflux Activities of the Amyloid Precursor Protein of Alzheimer's Disease

Treiber, C., Simons, A., Strauß, M., Hafner, M., Cappai, R., Bayer, T. A., & Multhaup, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407410200 · Cited by 147

APP Transgenic Mice Tg2576 Accumulate Aβ Peptides That Are Distinct from the Chemically Modified and Insoluble Peptides Deposited in Alzheimer's Disease Senile Plaques

Kalback, W. M., Watson, M. D., Kokjohn, T. A., Kuo, Y., Weiss, N., Luehrs, D. C., Lopez, J. C., Brune, D. C., Sisodia, S. S., Staufenbiel, M., et al. (2001) · Biochemistry · doi:10.1021/bi015685+ · Cited by 147

Oxidative Imbalance in Alzheimer's Disease

Zhu, X., Lee, H., Casadesús, G., Ávila, J., Drew, K. L., Perry, G. L., & Smith, M. A. (2005) · Molecular Neurobiology · doi:10.1385/mn:31:1-3:205 · Cited by 146

Impaired Cu/Zn-SOD activity contributes to increased oxidative damage in APP transgenic mice

Schüssel, K., Schäfer, S., Bayer, T. A., Czech, C., Pradier, L., Müller-Spahn, F., Müller, W. E., & Eckert, A. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.09.003 · Cited by 149

Metal Binding Modes of Alzheimer's Amyloid β-Peptide in Insoluble Aggregates and Soluble Complexes

Miura, T., Suzuki, K., Kohata, N., & Takeuchi, H. (2000) · Biochemistry · doi:10.1021/bi0002479 · Cited by 457

Roles of Cu2+ in the conformational transitions and dimerization of amyloid-beta peptide and its implications in Alzheimer's disease

Liao, Q. (2016)

Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Suzuki, K., Miura, T., & Takeuchi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5263 · Cited by 90

pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

Ghalebani, L., Wahlström, A., Danielsson, J., Wärmländer, S. K. T. S., & Gräslund, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.043 · Cited by 48

Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide

Tõugu, V., Tiiman, A., & Palumaa, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05061.x · Cited by 219