Metal ions, Alzheimer's disease and chelation therapy

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

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Amyloid plaque core protein in Alzheimer disease and Down syndrome.

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Pathways towards and Away from Alzheimer’s Disease

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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

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Copper, iron and zinc in Alzheimer's disease senile plaques

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3D structure of Alzheimer's amyloid-β(1–42) fibrils

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

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Rapid induction of Alzheimer A beta amyloid formation by zinc

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Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

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

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Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red.

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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

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988 · see citing works

Intramuscular desferrioxamine in patients with Alzheimer's disease

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Safety, efficacy, and biomarker findings of PBT2 in targeting Aβ as a modifying therapy for Alzheimer's disease: a phase IIa, double-blind, randomised, placebo-controlled trial

Lannfelt, L., Blennow, K., Zetterberg, H., Batsman, S., Ames, D., Harrison, J., Masters, C. L., Targum, S., Bush, A. I., Murdoch, R., et al. (2008) · The Lancet Neurology · doi:10.1016/s1474-4422(08)70167-4 · Cited by 725 · 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

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

EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION

KLATZO, I., Wı́sniewski, H. M., & STREICHER, E. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00002 · Cited by 609 · 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

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

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

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E PIDEMIOLOGY OF N EURODEGENERATION

Mayeux, R. P. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.043002.094919 · Cited by 511 · 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

A Portrait of Alzheimer Secretases--New Features and Familiar Faces

Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493 · 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

Selective accumulation of aluminum and iron in the neurofibrillary tangles of Alzheimer's disease: A laser microprobe (LAMMA) study

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A selective defect of cytochrome c oxidase is present in brain of Alzheimer disease patients

Maurer, I. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00112-3 · Cited by 475 · see citing works

Copper, iron, and zinc ions homeostasis and their role in neurodegenerative disorders (metal uptake, transport, distribution and regulation)

Kozłowski, H., Janicka-Kłos, A., Brasuń, J., Gaggelli, E., Valensin, D., & Valensin, G. (2009) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2009.05.011 · Cited by 467 · see citing works

Aluminum, Iron, and Zinc Ions Promote Aggregation of Physiological Concentrations of β‐Amyloid Peptide

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Alzheimer's disease: Aβ, tau and synaptic dysfunction

LaFerla, F. M., & Oddo, S. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.02.009 · Cited by 461 · see citing works

NEURODEGENERATIVE DISEASES: New Concepts of Pathogenesis and Their Therapeutic Implications

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The chemistry of Alzheimer’s disease

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

The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy

Gaeta, A., & Hider, R. C. (2005) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0706416 · Cited by 411 · see citing works

Rapid Communication: Characterization of β‐Amyloid Peptide from Human Cerebrospinal Fluid

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Alzheimer's disease, metal ions and metal homeostatic therapy

Zatta, P., Drago, D., Bolognin, S., & Sensi, S. L. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.05.002 · Cited by 369 · see citing works

EXPERIMENTAL PRODUCTION OF NEUROFIBRILLARY DEGENERATION

Terry, R. D., & Peña, C. (1965) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-196504000-00003 · Cited by 332 · 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

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

Clioquinol, a Drug for Alzheimer's Disease Specifically Interfering with Brain Metal Metabolism:  Structural Characterization of Its Zinc(II) and Copper(II) Complexes

Di Vaira, M., Bazzicalupi, C., Orioli, P., Messori, L., Bruni, B., & Zatta, P. (2004) · Inorganic Chemistry · doi:10.1021/ic0494051 · Cited by 292 · 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

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

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

The C‐Terminus of the β Protein is Critical in Amyloidogenesis a

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Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 246 · 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

Novel multifunctional neuroprotective iron chelator‐monoamine oxidase inhibitor drugs for neurodegenerative diseases: in vitro studies on antioxidant activity, prevention of lipid peroxide formation and monoamine oxidase inhibition

Zheng, H., Gal, S., Weiner, L. M., Bar‐Am, O., Warshawsky, A., Fridkin, M., & Youdim, M. B. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03340.x · Cited by 215 · see citing works

REVIEW: tau protein pathology in Alzheimer’s disease and related disorders

Tolnay, M., & Probst (1999) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.1999.00182.x · Cited by 210 · see citing works

Novel -penicillamine carrying nanoparticles for metal chelation therapy in Alzheimer's and other CNS diseases

Cui, Z., Lockman, P. R., Atwood, C., Hsu, C. C., Gupte, A., ALLEN, D., & Mumper, R. J. (2004) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2004.07.009 · Cited by 203 · see citing works

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 · see citing works

Low Micromolar Zinc Accelerates the Fibrillization of Human Tau via Bridging of Cys-291 and Cys-322

Mo, Z., Zhu, Y.-Z., Zhu, H., Fan, J.-B., Chen, J., & Liang, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.058883 · Cited by 189 · see citing works

Free copper, ferroxidase and SOD1 activities, lipid peroxidation and NO(x) content in the CSF. A different marker profile in four neurodegenerative diseases

Boll, M.-C., Alcaraz-Zubeldia, M., Montes, S., & Rios, C. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9610-3 · Cited by 173 · see citing works

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 · see citing works

Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease

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The Role of Zinc in Alzheimer′s Disease

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Preliminary studies of a novel bifunctional metal chelator targeting Alzheimer's amyloidogenesis

Dedeoglu, A., Cormier, K., Payton, S., Tseitlin, K. A., Kremsky, J. N., Lai, L., Li, X., Moir, R. D., Tanzi, R. E., Bush, A. I., et al. (2004) · Experimental Gerontology · doi:10.1016/j.exger.2004.08.016 · Cited by 141 · see citing works

Clioquinol Decreases Amyloid-β Burden and Reduces Working Memory Impairment in a Transgenic Mouse Model of Alzheimer's Disease

Grossi, C., Francese, S., Casini, A., Rosi, M. C., Luccarini, I., Fiorentini, A., Gabbiani, C., Luigi Messori, A., Moneti, G., & Casamenti, F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1063 · Cited by 130 · see citing works

Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS

Ma, Q., Li, Y., Du, J., Liu, H., Kanazawa, K., Nemoto, T., Nakanishi, H., & Zhao, Y. (2006) · Peptides · doi:10.1016/j.peptides.2005.09.002 · Cited by 123 · see citing works

Changes in uptake of vitamin B12 and trace metals in brains of mice treated with clioquinol

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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 97 · see citing works

Amyloid‐Beta Peptide Forms Monomeric Complexes With CuII and ZnII Prior to Aggregation

Talmard, C., Guilloreau, L., Coppel, Y., Mazarguil, H., & Faller, P. (2006) · ChemBioChem · doi:10.1002/cbic.200600319 · Cited by 96 · see citing works

Subacute myelo‐optico‐neuropathy: Clioquinol intoxication in humans and animals

Tateishi, J. (2000) · Neuropathology · doi:10.1046/j.1440-1789.2000.00296.x · Cited by 92 · see citing works

A novel trivalent cation chelator Feralex dissociates binding of aluminum and iron associated with hyperphosphorylated τ of Alzheimer’s disease

Shin, R., Kruck, T. P. A., Murayama, H., & Kitamoto, T. (2003) · Brain Research · doi:10.1016/s0006-8993(02)03893-3 · Cited by 88 · see citing works

Chelation and Intercalation: Complementary Properties in a Compound for the Treatment of Alzheimer's Disease

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 · see citing works

Potential pathogenic role of β-amyloid1–42–aluminum complex in Alzheimer's disease

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Investigations of the Molecular Mechanism of Metal-Induced Aβ (1−40) Amyloidogenesis

Lim, K. H., Kim, Y. K., & Chang, Y. (2007) · Biochemistry · doi:10.1021/bi701112z · Cited by 71 · see citing works

Hydroxyquinoline based binders: Promising ligands for chelatotherapy?

Budimir, A., Humbert, N., Elhabiri, M., Nierengarten, I., Biruš, M., & Albrecht‐Gary, A. (2010) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2010.08.014 · Cited by 69 · see citing works

Aggregation of tau protein by aluminum.

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Bis-8-hydroxyquinoline ligands as potential anti-Alzheimer agents

Deraeve, C., Piti, M., Mazarguil, H., & Meunier, B. (2007) · New Journal of Chemistry · doi:10.1039/b616085a · Cited by 53 · see citing works

Therapeutic Treatments for Alzheimer's Disease Based on Metal Bioavailability

Crouch, P. J., Barnham, K. J., Bush, A. I., & White, A. R. (2006) · Drug News & Perspectives · doi:10.1358/dnp.2006.19.8.1021492 · Cited by 36 · see citing works

1,1′-Xylyl bis-1,4,8,11-tetraaza cyclotetradecane: A new potential copper chelator agent for neuroprotection in Alzheimer’s disease. Its comparative effects with clioquinol on rat brain copper distribution

Moret, V., Laras, Y., Pietrancosta, N., Garino, C., Quéléver, G., Rolland, A., Mallet, B., Norreel, J.-C., & Kraus, J. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.03.026 · Cited by 29 · see citing works

Synthesis and evaluation of peptidic metal chelators for neuroprotection in neurodegenerative diseases

Zheng, H., Youdim, M. B. H., Weiner, L. M., & Fridkin, M. (2005) · Journal of Peptide Research · doi:10.1111/j.1399-3011.2005.00289.x · Cited by 27 · see citing works

Vibrational spectra of clioquinol and its Cu(II) complex

Wagner, C. C., Calvo, S., Torre, M. H., & Baran, E. J. (2006) · Journal of Raman Spectroscopy · doi:10.1002/jrs.1654 · Cited by 24 · see citing works

Preparation of Cyclo‐Phen‐Type Ligands: Chelators of Metal Ions as Potential Therapeutic Agents in the Treatment of Neurodegenerative Diseases

Boldron, C., der Auwera, I. V., Deraeve, C., Gornitzka, H., Wera, S., Pitié, M., LEUVEN, F. V., & Meunier, B. (2005) · ChemBioChem · doi:10.1002/cbic.200500220 · Cited by 21 · see citing works

Molecular Determinants of Alzheimer’s Disease Aβ Peptide Neurotoxicity

Cappai, R., & Barnham, K. J. (2007) · Future Neurology · doi:10.2217/14796708.2.4.397 · Cited by 9 · see citing works

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.abs · Cited by 5 · see citing works

Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease

Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820 · see citing works

Exploration of the medical periodic table: towards new targets

Barry, N. P. E., & Sadler, P. J. (2013) · Chemical Communications · doi:10.1039/c3cc41143e · Cited by 720 · see citing works

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 672 · see citing works

The outdoor air pollution and brain health workshop

Block, M. L., Elder, A., Auten, R. L., Bilbo, S. D., Chen, H., Chen, J.-C., Cory-Slechta, D. A., Costa, D., Diaz-Sanchez, D., Dorman, D. C., et al. (2012) · NeuroToxicology · doi:10.1016/j.neuro.2012.08.014 · Cited by 539 · see citing works

Metabolism and functions of copper in brain

Scheiber, I. F., Mercer, J. F. B., & Dringen, R. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.01.002 · Cited by 511 · see citing works

Molecular Probes, Chemosensors, and Nanosensors for Optical Detection of Biorelevant Molecules and Ions in Aqueous Media and Biofluids

Krämer, J., Kang, R., Grimm, L., Cola, L. D., Picchetti, P., & Biedermann, F. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00746 · Cited by 455 · see citing works

8-Hydroxyquinolines: a review of their metal chelating properties and medicinal applications

Prachayasittikul, V., Prachayasittikul, V., Prachayasittikul, S., & Ruchirawat, S. (2013) · Drug Design Development and Therapy · doi:10.2147/dddt.s49763 · Cited by 451 · 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

Recent development of multifunctional agents as potential drug candidates for the treatment of Alzheimer’s disease

Guzior, N., Wi.eckowska, A., Panek, D., & Malawska, B. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666141106122628 · Cited by 323 · see citing works

Function and toxicity of amyloid beta and recent therapeutic interventions targeting amyloid beta in Alzheimer's disease

Rajasekhar, K., Chakrabarti, M., & Govindaraju, T. (2015) · Chemical Communications · doi:10.1039/c5cc05264e · Cited by 241 · see citing works

Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes

Milardi, D., Gazit, E., Radford, S. E., Xu, Y., Gallardo, R. U., Caflisch, A., Westermark, G. T., Westermark, P., Rosa, C. L., & Ramamoorthy, A. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00981 · Cited by 199 · see citing works

Polyphenols as Potential Metal Chelation Compounds Against Alzheimer’s Disease

Lakey‐Beitia, J., Burillo, A., Penna, G. L., Hegde, M. L., & Rao, K. S. J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200185 · Cited by 185 · see citing works

Mitochondrial DNA Oxidative Damage and Repair in Aging and Alzheimer's Disease

Santos, R. X., Correia, S. C., Zhu, X., Smith, M. A., Moreira, P. I., Castellani, R. J., Nunomura, A., & Perry, G. L. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5039 · Cited by 176 · see citing works

Insights of 8-hydroxyquinolines: A novel target in medicinal chemistry

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A New Paradigm for Enzymatic Control of α-Cleavage and β-Cleavage of the Prion Protein

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Novel 8‐Hydroxyquinoline Derivatives as Multitarget Compounds for the Treatment of Alzheimer′s Disease

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The protective role of plant biophenols in mechanisms of Alzheimer's disease

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The Role of Copper in Tau-Related Pathology in Alzheimer’s Disease

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The Role of Trace Metals in Alzheimer’s Disease

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Discovery of a novel fluorescent probe for the sensitive detection of β-amyloid deposits

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Modification of Aβ Peptide Aggregation via Covalent Binding of a Series of Ru(III) Complexes

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Revisiting Metal Toxicity in Neurodegenerative Diseases and Stroke: Therapeutic Potential.

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