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

Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings

Lipinski, C. A., Lombardo, F., Dominy, B. W., & Feeney, P. J. (1997) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(96)00423-1 · Cited by 11,484 · see citing works

Molecular properties that influence the oral bioavailability of drug candidates

Veber, D. F., Johnson, S. R., Cheng, H.-Y., Smith, B. R., Ward, K. W., & Kopple, K. D. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020017n · Cited by 8,420 · see citing works

α-Synuclein in Lewy bodies

Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382 · see citing works

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · see citing works

Lead- and drug-like compounds: the rule-of-five revolution

Lipinski, C. A. (2004) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2004.11.007 · Cited by 6,339 · see citing works

The cholinergic hypothesis of geriatric memory dysfunction

Bartus, R. T., Dean, R. L., Beer, B., & Lippa, A. S. (1982) · Science · doi:10.1126/science.7046051 · Cited by 5,545 · see citing works

Bioavailability of curcumin: Problems and promises

Anand, P., Kunnumakkara, A. B., Newman, R. A., & Aggarwal, B. B. (2007) · Molecular Pharmaceutics · doi:10.1021/mp700113r · Cited by 5,543 · see citing works

Prions

Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373 · see citing works

Novel Proteinaceous Infectious Particles Cause Scrapie

Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,121 · see citing works

Protein folding and misfolding

Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791 · 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

Fast Calculation of Molecular Polar Surface Area as a Sum of Fragment-Based Contributions and Its Application to the Prediction of Drug Transport Properties

Ertl, P., Rohde, B., & Selzer, P. M. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000942e · Cited by 3,149 · see citing works

The new mutation, E46K, of α‐synuclein causes parkinson and Lewy body dementia

Zarranz, J. J., Alegre, J., Gómez‐Esteban, J. C., Lezcano, E., Ros, R., Ampuero, I., Vidal, L., Hoenicka, J., Rodriguez, O., Atarés, B., et al. (2004) · Annals of Neurology · doi:10.1002/ana.10795 · Cited by 2,737 · see citing works

The Properties of Known Drugs. 1. Molecular Frameworks

Bemis, G. W., & Murcko, M. A. (1996) · Journal of Medicinal Chemistry · doi:10.1021/jm9602928 · Cited by 2,501 · see citing works

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336 · see citing works

The cholinergic hypothesis of Alzheimer’s disease: A review of progress

Francis, P. T., Palmer, A. M., Snape, M., & Wilcock, G. K. (1999) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp.66.2.137 · Cited by 2,198 · 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

Metal–Salen Schiff base complexes in catalysis: practical aspects

Cozzi, P. G. (2004) · Chemical Society Reviews · doi:10.1039/b307853c · Cited by 1,982 · see citing works

Intracellular amyloid-β in Alzheimer's disease

LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942 · see citing works

Curcumin: From ancient medicine to current clinical trials

Hatcher, H., Planalp, R. P., Cho, J., Torti, F. M., & Torti, S. V. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7452-4 · Cited by 1,847 · see citing works

Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution

Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,643 · see citing works

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 · see citing works

Unfolding the role of protein misfolding in neurodegenerative diseases

Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506 · see citing works

Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.

Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,469 · 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

Folding proteins in fatal ways

Selkoe, D. J. (2003) · Nature · doi:10.1038/nature02264 · Cited by 1,412 · see citing works

Human Memory and the Cholinergic System

Drachman, D. A. (1974) · Archives of Neurology · doi:10.1001/archneur.1974.00490320001001 · Cited by 1,398 · see citing works

Simple Selection Criteria for Drug-like Chemical Matter

Muegge, I., Heald, S. L., & Brittelli, D. R. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm015507e · Cited by 1,351 · see citing works

Alzheimer's Disease and Parkinson's Disease

Nussbaum, R. L., & Ellis, C. E. (2003) · New England Journal of Medicine · doi:10.1056/nejm2003ra020003 · Cited by 1,351 · see citing works

The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316 · 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

Parkinson's disease

Samii, A., Nutt, J. G., & Ransom, B. R. (2004) · The Lancet · doi:10.1016/s0140-6736(04)16305-8 · Cited by 1,305 · see citing works

Identification of a Protein That Purifies with the Scrapie Prion

Bolton, D. C., McKinley, M. P., & Prusiner, S. B. (1982) · Science · doi:10.1126/science.6815801 · Cited by 1,281 · see citing works

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,280 · see citing works

Extrinsic Fluorescent Dyes as Tools for Protein Characterization

Hawe, A., Sutter, M., & Jiskoot, W. (2008) · Pharmaceutical Research · doi:10.1007/s11095-007-9516-9 · Cited by 1,199 · see citing works

High throughput artificial membrane permeability assay for blood–brain barrier

Di, L., Kerns, E. H., Fan, K., McConnell, O. J., & Carter, G. T. (2003) · European Journal of Medicinal Chemistry · doi:10.1016/s0223-5234(03)00012-6 · Cited by 1,195 · see citing works

Increased nigral iron content and alterations in other metal ions occurring in brain in Parkinson's disease

Dexter, D. T., Wells, F. R., Lee, A. J., Agid, F., Agid, Y., Jenner, P., & Marsden, C. D. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb07264.x · Cited by 1,149 · see citing works

Amyloid Precursor Protein Trafficking, Processing, and Function

Thinakaran, G., & Koo, E. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800019200 · Cited by 1,141 · 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

Metal-triggered Structural Transformations, Aggregation, and Fibrillation of Human α-Synuclein

Uversky, V. N., Li, J., & Fink, A. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105343200 · Cited by 1,103 · see citing works

Interactions of Flavonoids with Iron and Copper Ions: A Mechanism for their Antioxidant Activity

Mira, L., Fernandez, M. T., Santos, M., Rocha, R., Florêncio, M. H., & Jennings, K. R. (2002) · Free Radical Research · doi:10.1080/1071576021000016463 · Cited by 1,055 · see citing works

Depression in Parkinson's disease: loss of dopamine and noradrenaline innervation in the limbic system

Rémy, P., Doder, M., Lees, A. J., Turjanski, N., & Brooks, D. J. (2005) · Brain · doi:10.1093/brain/awh445 · Cited by 1,046 · 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

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

Tau in Alzheimer's disease.

Mandelkow, E., & Mandelkow, E. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01368-3 · Cited by 951 · see citing works

Hybrid Molecules with a Dual Mode of Action: Dream or Reality?

Meunier, B. (2007) · Accounts of Chemical Research · doi:10.1021/ar7000843 · Cited by 942 · see citing works

The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease

Selkoe, D. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01363-4 · Cited by 862 · see citing works

Hepatotoxic Effects of Tacrine Administration in Patients With Alzheimer's Disease

Watkins, P. B. (1994) · JAMA: The Journal of the American Medical Association · doi:10.1001/jama.1994.03510370044030 · Cited by 829 · see citing works

Polar Molecular Surface as a Dominating Determinant for Oral Absorption and Brain Penetration of Drugs

Kelder, J., Grootenhuis, P. D. J., Bayada, D. M., Delbressine, L. P. C., & Ploemen, J.-P. H. T. M. (1999) · Pharmaceutical Research · doi:10.1023/a:1015040217741 · Cited by 819 · see citing works

Green tea and its polyphenolic catechins: Medicinal uses in cancer and noncancer applications

Zaveri, N. T. (2006) · Life Sciences · doi:10.1016/j.lfs.2005.12.006 · Cited by 811 · see citing works

Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

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., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762 · see citing works

Resveratrol Promotes Clearance of Alzheimer's Disease Amyloid-β Peptides

Marambaud, P., Zhao, H., & Davies, P. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508246200 · Cited by 750 · see citing works

Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer β-amyloid peptide in rodent

Greig, N. H., Utsuki, T., Ingram, D. K., Wang, Y., Pepeu, G., Scali, C., Yu, Q.-S., Mamczarz, J., Holloway, H. W., Giordano, T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508575102 · Cited by 745 · 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

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

Flavonoid Antioxidants

Rice-Evans, C. A. (2001) · Current Medicinal Chemistry · doi:10.2174/0929867013373011 · Cited by 719 · see citing works

Pharmacokinetics of tea catechins after ingestion of green tea and (-)-epigallocatechin-3-gallate by humans: formation of different metabolites and individual variability.

Lee, M., Maliakal, P. P., Chen, L., Meng, X., Bondoc, F. Y., Prabhu, S., Lambert, G. H., Mohr, S. N., & Yang, C. S. (2002) · PubMed · Cited by 716 · see citing works

Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs

Forman, M. S., Trojanowski, J. Q., & Lee, V. M.-Y. (2004) · Nature Medicine · doi:10.1038/nm1113 · Cited by 715 · see citing works

Green tea Epigallocatechin-3-Gallate (EGCG) Modulates Amyloid Precursor Protein Cleavage and Reduces Cerebral Amyloidosis in Alzheimer Transgenic Mice

Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1521-05.2005 · Cited by 713 · see citing works

Penicillamine, a new oral therapy for Wilson's disease

Walshe, J. M. (1956) · The American Journal of Medicine · doi:10.1016/0002-9343(56)90066-3 · Cited by 711 · see citing works

Expression of Concern: Potent anti‐amyloidogenic and fibril‐destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease

Ono, K., Yoshiike, Y., Takashima, A., Hasegawa, K., Naiki, H., & Yamada, M. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01976.x · Cited by 681 · 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

Property distribution of drug-related chemical databases*

Oprea, T. I. (2000) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1008130001697 · Cited by 629 · see citing works

Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.

Klunk, W. E., Pettegrew, J. W., & Abraham, D. J. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.8.2666510 · Cited by 625 · 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

1,10-Phenanthroline: A versatile building block for the construction of ligands for various purposes

Bencini, A., & Lippolis, V. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.04.008 · Cited by 617 · see citing works

Physiology of the prion protein

Linden, R., Martins, V. R., Prado, M. A. M., Cammarota, M., Izquierdo, I., & Brentani, R. R. (2008) · Physiological Reviews · doi:10.1152/physrev.00007.2007 · Cited by 617 · 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

Animal models of Parkinson's disease

Betarbet, R. S., Sherer, T., & Greenamyre, J. T. (2002) · BioEssays · doi:10.1002/bies.10067 · Cited by 600 · see citing works

Computational methods for the prediction of ‘drug-likeness’

Clark, D. E., & Pickett, S. D. (2000) · Drug Discovery Today · doi:10.1016/s1359-6446(99)01451-8 · Cited by 583 · 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

Green tea polyphenol (–)‐epigallocatechin‐3‐gallate prevents N ‐methyl‐4‐phenyl‐1,2,3,6‐tetrahydropyridine‐induced dopaminergic neurodegeneration

Levites, Y., Weinreb, O., Maor, G., Youdim, M. B. H., & Mandel, S. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00490.x · Cited by 567 · 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

Zinc Metabolism in the Brain: Relevance to Human Neurodegenerative Disorders

Cuajungco, M. P., & Lees, G. J. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0163 · Cited by 540 · 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

Rapid calculation of polar molecular surface area and its application to the prediction of transport phenomena. 2. Prediction of blood–brain barrier penetration

Clark, D. E. (1999) · Journal of Pharmaceutical Sciences · doi:10.1021/js980402t · Cited by 523 · see citing works

1,10-Phenanthroline: a versatile ligand

Sammes, P. G., & Yahioglu, G. (1994) · Chemical Society Reviews · doi:10.1039/cs9942300327 · Cited by 518 · see citing works

Neurological mechanisms of green tea polyphenols in Alzheimer's and Parkinson's diseases

Weinreb, O., Mandel, S. A., Amit, T., & Youdim, M. B. H. (2004) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2004.05.002 · Cited by 506 · see citing works

Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site

Bourne, Y., Taylor, P., Radić, Z., & Marchot, P. (2002) · The EMBO Journal · doi:10.1093/emboj/cdg005 · Cited by 490 · see citing works

In silico prediction of blood–brain barrier permeation

Clark, D. E. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02827-7 · Cited by 484 · see citing works

Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer’s disease animal models

Baum, L., & Ng, A. (2004) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6403 · Cited by 483 · 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

Neuroprotective properties of the natural phenolic antioxidants curcumin and naringenin but not quercetin and fisetin in a 6-OHDA model of Parkinson's disease

Zbarsky, V., Datla, K. P., Parkar, S., Rai, D. K., Aruoma, O. I., & Dexter, D. T. (2005) · Free Radical Research · doi:10.1080/10715760500233113 · Cited by 462 · see citing works

PET imaging of amyloid in Alzheimer's disease

Nordberg, A. K. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00853-1 · Cited by 462 · see citing works

Dose-dependent lesions of the dopaminergic nigrostriatal pathway induced by instrastriatal injection of 6-hydroxydopamine

Przedbroski, S., Leviver, M., Jiang, H., Ferreira, M., Jackson-Lewis, V. R., Donaldson, D. M., & Togasaki, D. M. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00066-r · Cited by 453 · see citing works

The use of PET in Alzheimer disease

Nordberg, A. K., Rinne, J. O., Kadir, A., & Långström, B. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2009.217 · Cited by 451 · see citing works

REVIEW: Curcumin and Alzheimer’s disease

Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450 · see citing works

Alzheimer Disease

Cummings, J. L. (2002) · JAMA · doi:10.1001/jama.287.18.2335 · Cited by 443 · see citing works

Recent advances in the multitarget‐directed ligands approach for the treatment of Alzheimer's disease

Leon, R. M., Garcı́a, A. G., & Marco, J. L. (2011) · Medicinal Research Reviews · doi:10.1002/med.20248 · Cited by 442 · see citing works

Challenges for Research on Polyphenols from Foods in Alzheimer’s Disease: Bioavailability, Metabolism, and Cellular and Molecular Mechanisms

Singh, M., Arseneault, M., Sanderson, J. T., Murthy, V., & Ramassamy, C. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0735073 · Cited by 438 · 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

Preclinical Properties of 18F-AV-45: A PET Agent for Aβ Plaques in the Brain

Choi, S., Golding, G., Zhuang, Z., Zhang, W., Lim, N. C., Hefti, F. F., Benedum, T. E., Kilbourn, M. R., Skovronsky, D., & Kung, H. F. (2009) · Journal of Nuclear Medicine · doi:10.2967/jnumed.109.065284 · Cited by 431 · see citing works

Carbohydrates as ligands: coordination equilibria and structure of the metal complexes

Gyurcsik, B., & Nagy, L. (2000) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(99)00183-6 · Cited by 428 · see citing works

Protective effect of quercetin in primary neurons against Aβ(1–42): relevance to Alzheimer's disease

Ansari, M. A., Abdul, H. M., Gururaj Joshi, A., Opii, W. O., & Butterfield, D. A. (2008) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2008.03.002 · Cited by 421 · 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

PBT2 Rapidly Improves Cognition in Alzheimer's Disease: Additional Phase II Analyses

Faux, N. G., Ritchie, C. W., Gunn, A. P., Rembach, A., Tsatsanis, A., Bedő, J., Harrison, J., Lannfelt, L., Blennow, K., Zetterberg, H., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1390 · Cited by 406 · see citing works

Congo red and protein aggregation in neurodegenerative diseases

Frid, P., Anisimov, S. V., & Popović, N. (2006) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.08.001 · Cited by 398 · see citing works

Curcumin Protects the Rat Liver from CCl4-Caused Injury and Fibrogenesis by Attenuating Oxidative Stress and Suppressing Inflammation

Fu, Y., Zheng, S., Lin, J., Ryerse, J. S., & Chen, A. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.039818 · Cited by 394 · 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

Finishing a whole-genome shotgun: Release 3 of the Drosophila melanogastereuchromatic genome sequence

Celniker, S., Wheeler, D. A., Kronmiller, B. A., Carlson, J. W., Halpern, A. L., Patel, S. A., Adams, M. D., Champe, M., Dugan, S., Frise, E., et al. (2002) · Genome biology · doi:10.1186/gb-2002-3-12-research0079 · Cited by 387 · see citing works

Interaction of α-Synuclein with Divalent Metal Ions Reveals Key Differences: A Link between Structure, Binding Specificity and Fibrillation Enhancement

Binolfi, A., Rasia, R. M., Bertoncini, C. W., Ceolín, M. R., Zweckstetter, M., Griesinger, C., Jovin, T. M., & Fernández, C. O. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0618649 · Cited by 382 · see citing works

TREATMENT OF WILSON'S DISEASE WITH TRIENTINE (TRIETHYLENE TETRAMINE) DIHYDROCHLORIDE

Walshe, J. M. (1982) · The Lancet · doi:10.1016/s0140-6736(82)92201-2 · Cited by 381 · see citing works

Neuroprotection and neurorescue against Aβ toxicity and PKC‐dependent release of non‐amyloidogenic soluble precursor protein by green tea polyphenol (‐)‐epigallocatechin‐3‐gallate

Levites, Y., Amit, T., Mandel, S. A., & Youdim, M. B. H. (2003) · The FASEB Journal · doi:10.1096/fj.02-0881fje · Cited by 372 · see citing works

Copper Mediates Dityrosine Cross-Linking of Alzheimer's Amyloid-β

Atwood, C., Perry, G. L., Zeng, H., Kato, Y., Jones, W. D., Ling, K.-Q., Huang, X., Moir, R. D., Wang, D., Sayre, L. M., et al. (2003) · Biochemistry · doi:10.1021/bi0358824 · Cited by 371 · see citing works

Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan

Alavez, S., Vantipalli, M. C., Zucker, D. J. S., Klang, I. M., & Lithgow, G. J. (2011) · Nature · doi:10.1038/nature09873 · Cited by 370 · see citing works

Protein Misfolding and Neurodegeneration

Soto, C. A., & Estrada, L. D. (2008) · Archives of Neurology · doi:10.1001/archneurol.2007.56 · Cited by 352 · see citing works

The effect of age on the activity and molecular properties of human brain monoamine oxidase

Fowler, C. J., Wiberg, �., Oreland, L., Marcusson, J. O., & Winblad, B. G. (1980) · Journal of Neural Transmission · doi:10.1007/bf01249185 · Cited by 349 · see citing works

The green tea polyphenol (−)-epigallocatechin gallate attenuates β-amyloid-induced neurotoxicity in cultured hippocampal neurons

Choi, Y.-T., Jung, C., Lee, S., Bae, J., Baek, W., Suh, M., Park, J., Park, C., & Suh, S. (2001) · Life Sciences · doi:10.1016/s0024-3205(01)01438-2 · Cited by 342 · see citing works

Protein-misfolding diseases: Getting out of shape

Dobson, C. M. (2002) · Nature · doi:10.1038/418729a · Cited by 341 · see citing works

REHABILITATION IN SCHIZOPHRENIA.

Hadfield, J. A., & WATKIN, D. (1965) · PubMed · Cited by 341 · see citing works

Protein misfolding and disease; protein refolding and therapy

Soto, C. A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02486-3 · Cited by 339 · see citing works

Role of Oxidative Stress and Antioxidants in Neurodegenerative Diseases

Rao, A. V., & Balachandran, B. (2002) · Nutritional Neuroscience · doi:10.1080/1028415021000033767 · Cited by 337 · see citing works

In Vivo Optical Imaging of Amyloid Aggregates in Brain: Design of Fluorescent Markers

Nesterov, E. E., Skoch, J. M., Hyman, B. T., Klunk, W. E., Bacskai, B. J., & Swager, T. M. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500845 · Cited by 337 · see citing works

Diffuse senile plaques occur commonly in the cerebellum in Alzheimer's disease.

Joachim, C. L., Morris, J. H., & Selkoe, D. J. (1989) · PubMed · Cited by 336 · 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

Modulation of A beta adhesiveness and secretase site cleavage by zinc.

Bush, A. I., Pettingell, W. H., Paradis, M. D., & Tanzi, R. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32694-7 · Cited by 331 · see citing works

World Alzheimer Report 2012

Batsch, N., & Mittelman, M. S. (2012) · Cited by 329 · see citing works

A review of specific dietary antioxidants and the effects on biochemical mechanisms related to neurodegenerative processes

Esposito, E., Rotilio, D., DIMATTEO, V., Giulio, C. D., Cacchio, M., & Algeri, S. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00078-7 · Cited by 327 · see citing works

Cyclam complexes and their applications in medicine

Liang, X., & Sadler, P. J. (2004) · Chemical Society Reviews · doi:10.1039/b313659k · Cited by 322 · see citing works

In-Vivo Imaging of Alzheimer Disease -Amyloid With [11C]SB-13 PET

Verhoeff, N. P. L. G. (2004) · American Journal of Geriatric Psychiatry · doi:10.1176/appi.ajgp.12.6.584 · Cited by 318 · see citing works

A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains

Connor, J. R., Snyder, B. S., Arosio, P., Loeffler, D. A., & LeWitt, P. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65020717.x · Cited by 317 · see citing works

Role of metal dyshomeostasis in Alzheimer's disease

Bonda, D., Lee, H., Blair, J. A., Zhu, X., Perry, G. L., & Smith, M. A. (2011) · Metallomics · doi:10.1039/c0mt00074d · Cited by 316 · see citing works

Zinc-induced Alzheimer's Aβ1–40 Aggregation Is Mediated by Conformational Factors

Huang, X., Atwood, C., Moir, R. D., Hartshorn, M. A., Vonsattel, J., Tanzi, R. E., & Bush, A. I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.42.26464 · Cited by 313 · 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

The Iron Chelator Desferrioxamine (Desferal) Retards 6‐Hydroxydopamine‐Induced Degeneration of Nigrostriatal Dopamine Neurons

Ben‐Shachar, D., Eshel, G., Finberg, J. P. M., & Youdim, M. B. H. (1991) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1991.tb11444.x · Cited by 299 · see citing works

Highly potent and selective inhibition of human immunodeficiency virus by the bicyclam derivative JM3100

Clercq, E. D., Yamamoto, N., Pauwels, R., Balzarini, J. M., Witvrouw, M., de Vreese, K., Debyser, Z., Rosenwirth, B., Peichl, P., & DATEMA, R. (1994) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.38.4.668 · Cited by 296 · see citing works

Green tea catechins as brain‐permeable, natural iron chelators‐antioxidants for the treatment of neurodegenerative disorders

Mandel, S. A., Amit, T., Reznichenko, L., Weinreb, O., & Youdim, M. B. H. (2006) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200500156 · Cited by 293 · see citing works

α-Synuclein and dopamine at the crossroads of Parkinson's disease

Venda, L. L., Cragg, S. J., Buchman, V. L., & Wade‐Martins, R. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.09.004 · Cited by 288 · see citing works

A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease

Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B. A., Pollwein, P., Beyreuther, K. T., & Masters, C. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85394-2 · Cited by 286 · see citing works

Parkinson disease: A new link between monoamine oxidase and mitochondrial electron flow

Cohen, G., Farooqui, R., & Kesler, N. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.4890 · Cited by 286 · see citing works

Neuroprotective effects of green and black teas and their catechin gallate esters against β‐amyloid‐induced toxicity

Bastianetto, S., Yao, Z., Papadopoulos, V., & Quirion, R. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04532.x · Cited by 283 · 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

Treatment interventions for Parkinson's disease: an evidence based assessment

Rascol, O., Goetz, C. G., Koller, W. C., Poewe, W. H., & Sampaio, C. (2002) · The Lancet · doi:10.1016/s0140-6736(02)08520-3 · Cited by 279 · see citing works

Design, synthesis, and evaluation of novel bifunctional iron-chelators as potential agents for neuroprotection in Alzheimer’s, Parkinson’s, and other neurodegenerative diseases

Zheng, H., Weiner, L. M., Bar-Am, O., Epsztejn, S., Cabantchik, Z. I., Warshawsky, A., Youdim, M. B. H., & Fridkin, M. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.10.037 · Cited by 278 · see citing works

Dietary Antioxidants and Long-term Risk of Dementia

Devore, E. E., Grodstein, F., van Rooij, F. J. A., Albert Hofman, D., Stampfer, M. J., Witteman, J. C. M., & Breteler, M. M. B. (2010) · Archives of Neurology · doi:10.1001/archneurol.2010.144 · Cited by 277 · 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

Design of small molecules that target metal-Aβ species and regulate metal-induced Aβ aggregation and neurotoxicity

Choi, J.-S., Braymer, J. J., Nanga, R. P. R., Ramamoorthy, A., & Lim, M. H. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1006091107 · Cited by 264 · see citing works

Multi-Target-Directed Drug Design Strategy: From a Dual Binding Site Acetylcholinesterase Inhibitor to a Trifunctional Compound against Alzheimer’s Disease

Bolognesi, M. L., Cavalli, A., Valgimigli, L., Bartolini, M., Rosini, M., Andrisano, V., Recanatini, M., & Melchiorre, C. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm701225u · Cited by 262 · see citing works

Donepezil preserves cognition and global function in patients with severe Alzheimer disease

Black, S. E., Doody, R., Li, H., McRae, T. D., Jambor, K. M., Xu, Y., Sun, Y., Perdomo, C. A., & Richardson, S. (2007) · Neurology · doi:10.1212/01.wnl.0000266627.96040.5a · Cited by 255 · see citing works

VIP: Molecular biology and neurobiological function

Gozes, I., & Brenneman, D. E. (1989) · Molecular Neurobiology · doi:10.1007/bf02740606 · Cited by 255 · see citing works

Thioflavine T interaction with amyloid β-sheet structures

LeVine, H. (1995) · Amyloid · doi:10.3109/13506129509031881 · Cited by 254 · see citing works

Monoamine Oxidase-B Inhibition in Alzheimer's Disease

Riederer, P. F. (2003) · NeuroToxicology · doi:10.1016/s0161-813x(03)00106-2 · Cited by 254 · see citing works

Clioquinol: Review of its Mechanisms of Action and Clinical Uses in Neurodegenerative Disorders

Bareggi, S. R., & Cornelli, U. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00231.x · Cited by 247 · see citing works

Neuroprotection by a novel brain permeable iron chelator, VK-28, against 6-hydroxydopamine lession in rats

Shachar, D. B., Kahana, N., Kampel, V., Warshawsky, A., & Youdim, M. B. H. (2004) · Neuropharmacology · doi:10.1016/j.neuropharm.2003.09.005 · Cited by 246 · see citing works

Protective effects of the green tea polyphenol (−)-epigallocatechin gallate against hippocampal neuronal damage after transient global ischemia in gerbils

Lee, S., Suh, S., & Kim, S.-P. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01159-9 · Cited by 245 · 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

Acetylcholinesterase inhibitors as disease-modifying therapies for Alzheimer's disease.

Muñoz-Torrero, D. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909067 · Cited by 241 · see citing works

Vitamin E Prevents Alzheimer's Amyloid ß-Peptide (1-42)-Induced Neuronal Protein Oxidation and Reactive Oxygen Species Production

Yatin, S. M., Varadarajan, S., & Butterfield, D. A. (2000) · Journal of Alzheimer s Disease · doi:10.3233/jad-2000-2212 · Cited by 239 · see citing works

Evaluation of a new copper(II)–curcumin complex as superoxide dismutase mimic and its free radical reactions

Barik, A., Mishra, B., Shen, L., Mohan, H., Kadam, R. M., Dutta, S., Zhang, H., & Priyadarsini, K. I. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.05.005 · Cited by 235 · see citing works

Recent Advances in Blood-Brain Barrier Transport

Pardridge, W. M. (1988) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.28.040188.000325 · Cited by 234 · see citing works

The deamination of dopamine by human brain monoamine oxidase

O’Carroll, A., Fowler, C. J., Phillips, J. P., Tobbia, I., & Tipton, K. F. (1983) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/bf00500765 · Cited by 231 · see citing works

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 222 · see citing works

Synthesis, physicochemical properties, and biological evaluation of N-substituted 2-alkyl-3-hydroxy-4(1H)-pyridinones: orally active iron chelators with clinical potential

Dobbin, P. S., Hider, R. C., Hall, A. D., Taylor, P. D., Sarpong, P., Porter, J. B., Xiao, G., & der Helm, D. V. (1993) · Journal of Medicinal Chemistry · doi:10.1021/jm00069a002 · Cited by 217 · see citing works

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 215 · 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

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 · see citing works

11C-labeled stilbene derivatives as Aβ-aggregate-specific PET imaging agents for Alzheimer’s disease

Ono, M., Wilson, A. A., Nóbrega, J. N., Westaway, D. A., Verhoeff, P., Zhuang, Z., Kung, M., & Kung, H. F. (2003) · Nuclear Medicine and Biology · doi:10.1016/s0969-8051(03)00049-0 · Cited by 209 · see citing works

Elucidating Amyloid β-Protein Folding and Assembly: A Multidisciplinary Approach

Teplow, D. B., Lazo, N. D., Bitan, G., Bernstein, S. L., Wyttenbach, T., Bowers, M. T., Baumketner, A., Shea, J., Urbanc, B., Cruz, L., et al. (2006) · Accounts of Chemical Research · doi:10.1021/ar050063s · Cited by 207 · see citing works

Small Molecule Modulators of Copper-Induced Aβ Aggregation

Hindo, S. S., Mancino, A. M., Braymer, J. J., Liu, Y., Vivekanandan, S., Ramamoorthy, A., & Lim, M. H. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907045h · Cited by 203 · 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

IMPY: an improved thioflavin-T derivative for in vivo labeling of β-amyloid plaques

Kung, M., Hou, C., Zhuang, Z., Zhang, B., Skovronsky, D., Trojanowski, J. Q., Lee, V. M. ‐., & Kung, H. F. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03436-4 · Cited by 196 · see citing works

Antioxidant strategies for Alzheimer's disease

Grundman, M., & Delaney, P. (2002) · Proceedings of The Nutrition Society · doi:10.1079/pns2002146 · Cited by 193 · see citing works

Curcumin Decreases Amyloid-β Peptide Levels by Attenuating the Maturation of Amyloid-β Precursor Protein

Zhang, C. M., Browne, A., Child, D. D., & Tanzi, R. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133520 · Cited by 190 · 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

Effective use of reducing agents and nanoparticle encapsulation in stabilizing catechins in alkaline solution

Dube, A., Ng, K., Nicolazzo, J. A., & Larson, I. C. (2010) · Food Chemistry · doi:10.1016/j.foodchem.2010.03.027 · Cited by 187 · see citing works

L-Deprenyl in Alzheimer's Disease

Tariot, P. N. (1987) · Archives of General Psychiatry · doi:10.1001/archpsyc.1987.01800170041007 · Cited by 186 · see citing works

Novel multifunctional neuroprotective iron chelator‐monoamine oxidase inhibitor drugs for neurodegenerative diseases.<i>In vivo</i>selective brain monoamine oxidase inhibition and prevention of MPTP‐induced striatal dopamine depletion

Gal, S., Zheng, H., Fridkin, M., & Youdim, M. B. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03341.x · Cited by 185 · see citing works

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 · see citing works

Role of Free Radicals and Metal Ions in the Pathogenesis of Alzheimer’s Disease

Atwood, C. S., Huang, X., Moir, R. D., Tanzi, R. E., & Bush, A. I. (2018) · Routledge eBooks · doi:10.1201/9780203747605-10 · Cited by 183 · see citing works

Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease.

Klunk, W., Debnath, M., & Pettegrew, J. (1994) · Neurobiology of Aging · doi:10.1016/0197-4580(94)90050-7 · Cited by 180 · see citing works

Novel Stilbenes as Probes for Amyloid Plaques

Kung, H. F., Lee, C., Zhuang, Z., Kung, M., Hou, C., & Plöessl, K. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0167147 · Cited by 179 · see citing works

Studies in Desferrioxamine and Ferrioxamine Metabolism in Normal and Iron‐Loaded Subjects

Summers, M. R., Jacobs, A., Tudway, D. C., Perera, P., & Ricketts, C. (1979) · British Journal of Haematology · doi:10.1111/j.1365-2141.1979.tb01167.x · Cited by 179 · see citing works

1,2-DIMETHYL-3-HYDROXYPYRID-4-ONE, AN ORALLY ACTIVE CHELATOR FOR TREATMENT OF IRON OVERLOAD

Kontoghiorghes, G., Sheppard, L. N., Aldouri, M. A., & Hoffbrand, A. V. (1987) · The Lancet · doi:10.1016/s0140-6736(87)90545-9 · Cited by 177 · see citing works

Nanoparticle iron chelators: A new therapeutic approach in Alzheimer disease and other neurologic disorders associated with trace metal imbalance

Liu, G., Men, P., Harris, P. L. R., Rolston, R. K., Perry, G. L., & Smith, M. A. (2006) · Neuroscience Letters · doi:10.1016/j.neulet.2006.07.020 · Cited by 177 · see citing works

Butyrylcholinesterase attenuates amyloid fibril formation in vitro

Diamant, S., Podoly, E., Friedler, A., Ligumsky, H., Livnah, O., & Soreq, H. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602922103 · Cited by 177 · see citing works

Vitamin C and Vitamin E for Alzheimer's Disease

Boothby, L. A., & Doering, P. L. (2005) · Annals of Pharmacotherapy · doi:10.1345/aph.1e495 · Cited by 175 · see citing works

Metal complexes of cyclen and cyclam derivatives useful for medical applications: a discussion based on thermodynamic stability constants and structural data

Delgado, R., Félix, V. M. S., Lima, L. M. P., & Price, D. W. J. (2007) · Dalton Transactions · doi:10.1039/b704360k · Cited by 175 · see citing works

Direct visualisation of the β-sheet structure of synthetic Alzheimer’s amyloid 1 1Edited by F. E. Cohen

Serpell, L. C., & Smith, J. M. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3650 · Cited by 174 · see citing works

Antibacterial and antifungal activity of cicerfuran and related 2-arylbenzofurans and stilbenes

Aslam, S. N., Stevenson, P. C., Kokubun, T., & Hall, D. R. (2007) · Microbiological Research · doi:10.1016/j.micres.2006.11.012 · Cited by 171 · see citing works

Insight into Amyloid Structure Using Chemical Probes

Reinke, A. A., & Gestwicki, J. E. (2011) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2011.01110.x · Cited by 169 · see citing works

Prion hypothesis: the end of the controversy?

Soto, C. A. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.11.001 · Cited by 168 · see citing works

The Anti-Amyloidogenic Effect Is Exerted against Alzheimer's β-Amyloid Fibrils in Vitro by Preferential and Reversible Binding of Flavonoids to the Amyloid Fibril Structure

Hirohata, M., Hasegawa, K., Tsutsumi, S., Ohhashi, Y., Ookoshi, T., Ono, K., Yamada, M., & Naiki, H. (2007) · Biochemistry · doi:10.1021/bi061540x · Cited by 167 · see citing works

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 · see citing works

Quinoline‐n‐butylcyanoacrylate‐based nanoparticles for brain targeting for the diagnosis of Alzheimer's disease

Kulkarni, P. V., Roney, C. A., Antich, P. P., Bonte, F. J., Raghu, A. V., & Aminabhavi, T. M. (2009) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.59 · Cited by 159 · see citing works

Iron Chelators for Thalassaemia

Hershko, C., Konijn, A. M., & Link, G. (1998) · British Journal of Haematology · doi:10.1046/j.1365-2141.1998.00726.x · Cited by 159 · 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

Perez, L. R., & Franz, K. J. (2010) · Dalton Trans. · doi:10.1039/b919237a · Cited by 156 · see citing works

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 · see citing works

Neuroprotection by propargylamines in Parkinson's disease

Maruyama, W., Akao, Y., Carrillo, M.-C., Kitani, K., Youdium, M. B. H., & Naoi, M. (2002) · Neurotoxicology and Teratology · doi:10.1016/s0892-0362(02)00221-0 · Cited by 154 · see citing works

F-18 Stilbenes as PET Imaging Agents for Detecting β-Amyloid Plaques in the Brain

Zhang, W., Oya, S., Kung, M., Hou, C., Maier, D. L., & Kung, H. F. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm050166g · Cited by 151 · see citing works

Nanoparticle–chelator conjugates as inhibitors of amyloid-β aggregation and neurotoxicity: A novel therapeutic approach for Alzheimer disease

Liu, G., Men, P., Kudo, W., Perry, G., & Smith, M. A. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.03.064 · Cited by 148 · see citing works

Vasoactive intestinal peptide (VIP) prevents neurotoxicity in neuronal cultures: relevance to neuroprotection in Parkinson's disease1This manuscript is based on a poster presented at the Brain Research Interactive Symposium on “Neuropeptides at the Millennium”, Miami, October 1999.1

Offen, D., Gilgun‐Sherki, Y., Melamed, E., Fridkin, M., Brenneman, D. E., & Gozes, I. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02375-6 · Cited by 143 · see citing works

Site-Activated Multifunctional Chelator with Acetylcholinesterase and Neuroprotective−Neurorestorative Moieties for Alzheimer’s Therapy

Zheng, H., Youdim, M. B. H., & Fridkin, M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900504c · Cited by 141 · see citing works

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

One‐compound‐multiple‐targets strategy to combat Alzheimer's disease

Zhang, H. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.09.006 · Cited by 139 · see citing works

Affinity of copper and zinc ions to proteins and peptides related to neurodegenerative conditions (Aβ, APP, α-synuclein, PrP)

Zawisza, I. A., Rózga, M., & Bal, W. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.012 · Cited by 138 · see citing works

Increased Iron in the Substantia Nigra Compacta of the MPTP‐Lesioned Hemiparkinsonian African Green Monkey: Evidence from Proton Microprobe Elemental Microanalysis

Temlett, J. A., Landsberg, J. P., Watt, F., & Orime, G. W. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62010134.x · Cited by 137 · see citing works

Wilson's disease: clinical management and therapy

Brewer, G. J., & Askari, F. K. (2004) · Journal of Hepatology · doi:10.1016/j.jhep.2004.11.013 · Cited by 136 · see citing works

Mechanisms Behind the Neuroprotective Actions of Cholinesterase Inhibitors in Alzheimer Disease

Nordberg, A. K. (2006) · Alzheimer Disease & Associated Disorders · doi:10.1097/01.wad.0000213804.59187.2d · Cited by 134 · see citing works

Enkephalin Glycopeptide Analogues Produce Analgesia with Reduced Dependence Liability

Bilsky, E. J., Egleton, R. D., Mitchell, S. A., Palian, M. M., Davis, P., Huber, J. D., Jones, H., Yamamura, H. I., Janders, J., Davis, T. P., et al. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm000077y · Cited by 133 · see citing works

Metallodrugs in Medicinal Inorganic Chemistry

Mjos, K. D., & Orvig, C. (2014) · Chemical Reviews · doi:10.1021/cr400460s · Cited by 1,311 · see citing works

Metal N-heterocyclic carbene complexes as potential antitumor metallodrugs

Liu, W., & Gust, R. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35314h · Cited by 758 · see citing works

Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies

Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N., Côté, S., Simone, A. D., Doig, A. J., Faller, P., Garcı́a, A. E., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 583 · 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

Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease

Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H. (2013) · ACS Chemical Biology · doi:10.1021/cb400080f · Cited by 398 · see citing works

Role of Metal Ions in the Self-assembly of the Alzheimer’s Amyloid-β Peptide

Faller, P., Hureau, C., & Berthoumieu, O. (2013) · Inorganic Chemistry · doi:10.1021/ic4003059 · Cited by 355 · see citing works

Peptide self-assembly triggered by metal ions

Zou, R., Wang, Q., Wu, J., Wu, J., Schmuck, C., & Tian, H. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00234f · Cited by 301 · see citing works

Insights into antiamyloidogenic properties of the green tea extract (−)-epigallocatechin-3-gallate toward metal-associated amyloid-β species

Hyung, S., DeToma, A. S., Brender, J., Lee, S., Vivekanandan, S., Kochi, A., Choi, J.-S., Ramamoorthy, A., Ruotolo, B. T., & Lim, M. H. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1220326110 · Cited by 238 · see citing works

The benzazole scaffold: a SWAT to combat Alzheimer's disease

Noël, S., Cadet, S., Gras, E., & Hureau, C. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60086f · Cited by 217 · see citing works

Rational Design of a Structural Framework with Potential Use to Develop Chemical Reagents That Target and Modulate Multiple Facets of Alzheimer’s Disease

Lee, S., Zheng, X., Krishnamoorthy, J., Savelieff, M. G., Park, H. M., Brender, J., Kim, J. H., Derrick, J. S., Kochi, A., Lee, H. J., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja409801p · Cited by 185 · see citing works

Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease

Hayne, D. J., Lim, S., & Donnelly, P. S. (2014) · Chemical Society Reviews · doi:10.1039/c4cs00026a · Cited by 176 · see citing works

The Ongoing Search for Small Molecules to Study Metal-Associated Amyloid-β Species in Alzheimer’s Disease

Savelieff, M. G., DeToma, A. S., Derrick, J. S., & Lim, M. H. (2014) · Accounts of Chemical Research · doi:10.1021/ar500152x · Cited by 174 · see citing works

Cu(II) Affinity for the Alzheimer’s Peptide: Tyrosine Fluorescence Studies Revisited

Aliès, B., Renaglia, E., Rózga, M., Bal, W., Faller, P., & Hureau, C. (2012) · Analytical Chemistry · doi:10.1021/ac302629u · Cited by 172 · see citing works

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 · see citing works

Alzheimer’s disease: How metal ions define β-amyloid function

Kepp, K. P. (2017) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2017.05.007 · Cited by 151 · see citing works

Recent progress in multifunctional metal chelators as potential drugs for Alzheimer's disease

Santos, M. A., Chand, K., & Chaves, S. (2016) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2016.04.013 · Cited by 149 · see citing works

Copper Toxicity Links to Pathogenesis of Alzheimer’s Disease and Therapeutics Approaches

Ijaz, H. W., Wang, W., & Lang, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207660 · Cited by 146 · see citing works

The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity

Sharma, A. K., Pavlova, S. T., Kim, J., Kim, J., & Mirica, L. M. (2013) · Metallomics · doi:10.1039/c3mt00161j · Cited by 135 · see citing works

Design, synthesis and anti-Alzheimer’s activity of novel 1,2,3-triazole-chromenone carboxamide derivatives

Rastegari, A., Nadri, H., Mahdavi, M. R., Moradi, A., Mirfazli, S. S., Edraki, N., Moghadam, F. H., Larijani, B. A., Akbarzadeh, T., & Saeedi, M. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.10.065 · Cited by 122 · see citing works

Cu and Zn interactions with Aβ peptides: consequence of coordination on aggregation and formation of neurotoxic soluble Aβ oligomers.

Rana, M., & Sharma, A. (2019) · Metallomics · doi:10.1039/c8mt00203g · Cited by 80 · see citing works

Werner coordination chemistry and neurodegeneration

Telpoukhovskaia, M. A., & Orvig, C. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35236b · Cited by 112 · see citing works

A Bioinorganic View of Alzheimer’s Disease: When Misplaced Metal Ions (Re)direct the Electrons to the Wrong Target

Faller, P., & Hureau, C. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201202697 · Cited by 107 · see citing works

Copper-Targeting Approaches in Alzheimer’s Disease: How To Improve the Fallouts Obtained from in Vitro Studies

Esmieu, C., Guettas, D., Conte‐Daban, A., Sabater, L., Faller, P., & Hureau, C. (2019) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.9b00995 · Cited by 100 · see citing works

Multi-target-directed phenol–triazole ligands as therapeutic agents for Alzheimer's disease

Jones, M. R., Mathieu, É., Dyrager, C., Faissner, S., Vaillancourt, Z., Korshavn, K. J., Lim, M. H., Ramamoorthy, A., Yong, V. W., Tsutsui, S., et al. (2017) · Chemical Science · doi:10.1039/c7sc01269a · Cited by 96 · see citing works

Mutual interference of Cu and Zn ions in Alzheimer's disease: perspectives at the molecular level

Atrián‐Blasco, E., Conte‐Daban, A., & Hureau, C. (2017) · Dalton Transactions · doi:10.1039/c7dt01344b · Cited by 96 · see citing works

Structure-mechanism-based engineering of chemical regulators targeting distinct pathological factors in Alzheimer’s disease

Beck, M. W., Derrick, J. S., Kerr, R. A., Oh, S. B., Cho, W. J., Lee, S. J. C., Ji, Y., Han, J., Tehrani, Z. A., Suh, N., et al. (2016) · Nature Communications · doi:10.1038/ncomms13115 · Cited by 93 · see citing works

8-Hydroxyquinoline Schiff-base compounds as antioxidants and modulators of copper-mediated Aβ peptide aggregation

Gomes, L. M., Vieira, R. P., Jones, M. R., Wang, M. C. P., Dyrager, C., de Souza-Fagundes, E. M., Silva, J. G. D., Storr, T., & Beraldo, H. D. O. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.04.011 · Cited by 92 · see citing works

Novel Tacrine-Hydroxyphenylbenzimidazole hybrids as potential multitarget drug candidates for Alzheimer's disease

Hiremathad, A., Keri, R. S., Esteves, A. R., Cardoso, S. M., Chaves, S., & Santos, M. A. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.023 · Cited by 82 · see citing works

Discovery of novel propargylamine-modified 4-aminoalkyl imidazole substituted pyrimidinylthiourea derivatives as multifunctional agents for the treatment of Alzheimer's disease

Xu, Y., Wang, H., Li, X., Dong, S., Liu, W., Gong, Q., Wang, T., Tang, Y., Zhu, J., Li, J., et al. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.08.025 · Cited by 80 · see citing works

Synthesis of 2-Pyridyl-benzimidazole Iridium(III), Ruthenium(II), and Platinum(II) Complexes. Study of the Activity as Inhibitors of Amyloid-β Aggregation and Neurotoxicity Evaluation

Yellol, G. S., Yellol, J., Kenche, V. B., Liu, X. M., Barnham, K. J., Donaire, A., Janiak, C., & Ruiz, J. (2014) · Inorganic Chemistry · doi:10.1021/ic502119b · Cited by 73 · see citing works

Effect of metal chelators on the aggregation of beta-amyloid peptides in the presence of copper and iron

Tahmasebinia, F., & Emadi, S. (2017) · BioMetals · doi:10.1007/s10534-017-0005-2 · Cited by 73 · see citing works

Recent Developments in Metal-Based Drugs and Chelating Agents for Neurodegenerative Diseases Treatments

Sales, T. A., Prandi, I. G., de Castro, A. A., Leal, D. H. S., da Cunha, E. F. F., Kuča, K., & Ramalho, T. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081829 · Cited by 73 · see citing works

A rationally designed small molecule for identifying an in vivo link between metal–amyloid-β complexes and the pathogenesis of Alzheimer's disease

Beck, M. W., Oh, S. B., Kerr, R. A., Lee, H. J., Kim, S., Kim, S., Jang, M., Ruotolo, B. T., Lee, J., & Lim, M. H. (2015) · Chemical Science · doi:10.1039/c4sc03239j · Cited by 71 · see citing works

Metal-involved theranostics: An emerging strategy for fighting Alzheimer’s disease

Wang, X., Wang, X., & Guo, Z. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.03.010 · Cited by 71 · see citing works

A Redox-Active, Compact Molecule for Cross-Linking Amyloidogenic Peptides into Nontoxic, Off-Pathway Aggregates: In Vitro and In Vivo Efficacy and Molecular Mechanisms

Derrick, J. S., Kerr, R. A., Nam, Y., Oh, S. B., Lee, H. J., Earnest, K. G., Suh, N., Peck, K. L., Özbil, M., Korshavn, K. J., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b10043 · Cited by 70 · see citing works

Mechanistic Insights into Tunable Metal-Mediated Hydrolysis of Amyloid-β Peptides

Derrick, J. S., Lee, J., Lee, S. J. C., Kim, Y., Nam, E., Tak, H., Kang, J., Lee, M., Kim, S. H., Park, K., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b09681 · Cited by 69 · see citing works

Pt(ii) compounds interplay with Cu(ii) and Zn(ii) coordination to the amyloid-β peptide has metal specific consequences on deleterious processes associated to Alzheimer's disease

Collin, F., Sasaki, I., Eury, H., Faller, P., & Hureau, C. (2013) · Chemical Communications · doi:10.1039/c3cc38537j · Cited by 68 · see citing works

Advances in Multi-Functional Ligands and the Need for Metal-Related Pharmacology for the Management of Alzheimer Disease

Sharma, A., Pachauri, V., & Flora, S. J. S. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01247 · Cited by 67 · see citing works

Role of Metal Cations of Copper, Iron, and Aluminum and Multifunctional Ligands in Alzheimer’s Disease: Experimental and Computational Insights

Puentes-Díaz, N., Chaparro, D., Morales-Morales, D., Flores-Gaspar, A., & Alí-Torres, J. (2023) · ACS Omega · doi:10.1021/acsomega.2c06939 · Cited by 67 · see citing works

Neurodegenerative diseases – Understanding their molecular bases and progress in the development of potential treatments

Rowińska‐Żyrek, M., Salerno, M., & Kozłowski, H. (2014) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2014.03.026 · Cited by 64 · see citing works

Inhibition of Aβ aggregates in Alzheimer’s disease by epigallocatechin and epicatechin-3-gallate from green tea

Chen, T., Yang, Y., Zhu, S., Lu, Y., Zhu, L., Wang, Y., & Wang, X. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104382 · Cited by 64 · see citing works

Interaction and reactivity of synthetic aminoisoflavones with metal-free and metal-associated amyloid-β

DeToma, A. S., Krishnamoorthy, J., Nam, Y., Lee, H. J., Brender, J., Kochi, A., Lee, D., Onnis, V., Congiu, C., Manfredini, S., et al. (2014) · Chemical Science · doi:10.1039/c4sc01531b · Cited by 58 · see citing works

Biological Potential, Gastrointestinal Digestion, Absorption, and Bioavailability of Algae-Derived Compounds with Neuroprotective Activity: A Comprehensive Review

Martins, B., Vieira, M., Delerue-Matos, C. M., Grosso, C., & Soares, C. M. D. (2022) · Marine Drugs · doi:10.3390/md20060362 · Cited by 56 · see citing works

Copper Chelators: Chemical Properties and Bio-medical Applications

Tegoni, M., Valensin, D., Toso, L., & Remelli, M. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140601161939 · Cited by 56 · see citing works

New Tacrine Hybrids with Natural‐Based Cysteine Derivatives as Multitargeted Drugs for Potential Treatment of Alzheimer's Disease

Keri, R. S., Quintanova, C., Chaves, S., Silva, D. F., Cardoso, S. M., & Santos, M. A. (2015) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12633 · Cited by 56 · see citing works

A promising future of metal‐ N ‐heterocyclic carbene complexes in medicinal chemistry: The emerging bioorganometallic antitumor agents

Zhao, Q., Han, B., Peng, C. Y., Zhang, N., Huang, W., He, G., & Li, J. (2024) · Medicinal Research Reviews · doi:10.1002/med.22039 · Cited by 53 · see citing works

A Multifunctional Chemical Agent as an Attenuator of Amyloid Burden and Neuroinflammation in Alzheimer’s Disease

Cho, H., Sharma, A. K., Zhang, Y., Gross, M. L., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00114 · Cited by 53 · see citing works

Novel Fluorinated 8-Hydroxyquinoline Based Metal Ionophores for Exploring the Metal Hypothesis of Alzheimer’s Disease

Liang, S. H., Southon, A. G., Fraser, B. H., Krause‐Heuer, A. M., Zhang, B., Shoup, T. M., Lewis, R., Volitakis, I., Han, Y., Greguric, I. D., et al. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00281 · Cited by 52 · see citing works

Attenuation of Oxidative Stress by Cannabinoids and Cannabis Extracts in Differentiated Neuronal Cells

Raja, A., Ahmadi, S., de Costa, F., Li, N., & Kerman, K. (2020) · Pharmaceuticals · doi:10.3390/ph13110328 · Cited by 52 · see citing works

A small molecule that displays marked reactivity toward copper– versus zinc–amyloid-β implicated in Alzheimer's disease

Savelieff, M. G., Liu, Y., Senthamarai, R. R. P., Korshavn, K. J., Lee, H. J., Ramamoorthy, A., & Lim, M. H. (2013) · Chemical Communications · doi:10.1039/c3cc48473d · Cited by 51 · see citing works

Soluble Sugar-Based Quinoline Derivatives as New Antioxidant Modulators of Metal-Induced Amyloid Aggregation

Oliveri, V., Grasso, G. I., Bellia, F., Attanasio, F., Viale, M., & Vecchio, G. (2015) · Inorganic Chemistry · doi:10.1021/ic502713f · Cited by 51 · see citing works

Multifunctional iron-chelators with protective roles against neurodegenerative diseases

Nunes, A. C. C., Marques, S. M., Quintanova, C., Silva, D. F., Cardoso, S. M., Chaves, S., & Santos, M. A. (2013) · Dalton Transactions · doi:10.1039/c3dt50406a · Cited by 51 · see citing works

Clawing back: broadening the notion of metal chelators in medicine

Franz, K. J. (2013) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.12.021 · Cited by 50 · see citing works

Copper‐Binding Peptides Attenuate Microglia Inflammation through Suppression of NF‐kB Pathway

Caetano‐Silva, M. E., Rund, L. A., Vailati-Riboni, M., Pacheco, M. T. B., & Johnson, R. W. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202100153 · Cited by 49 · see citing works

Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity

Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48 · see citing works

How Zn can impede Cu detoxification by chelating agents in Alzheimer's disease: a proof-of-concept study

Conte‐Daban, A., Day, A. H., Faller, P., & Hureau, C. (2016) · Dalton Transactions · doi:10.1039/c6dt02308h · Cited by 45 · see citing works

Amentoflavone: A Bifunctional Metal Chelator that Controls the Formation of Neurotoxic Soluble Aβ 42 Oligomers

Sun, L., Sharma, A. K., Han, B.-H., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00376 · Cited by 45 · see citing works

Multiple Function Fluorescein Probe Performs Metal Chelation, Disaggregation, and Modulation of Aggregated Aβ and Aβ-Cu Complex

Balakrishnan, M., Layek, S., Balaji, S., Trivedi, V., & Iyer, P. K. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00205 · Cited by 42 · see citing works

Copper( i ) targeting in the Alzheimer's disease context: a first example using the biocompatible PTA ligand

Atrián‐Blasco, E., Cerrada, E., Conte‐Daban, A., Testemale, D., Faller, P., Laguna, M., & Hureau, C. (2015) · Metallomics · doi:10.1039/c5mt00077g · Cited by 42 · see citing works

Azo-dyes based small bifunctional molecules for metal chelation and controlling amyloid formation

Rana, M., Cho, H., Roy, T. K., Mirica, L. M., & Sharma, A. K. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.11.029 · Cited by 40 · see citing works

Is ascorbate Dr Jekyll or Mr Hyde in the Cu(Aβ) mediated oxidative stress linked to Alzheimer's disease?

Cheignon, C., Collin, F., Faller, P., & Hureau, C. (2016) · Dalton Transactions · doi:10.1039/c6dt01979j · Cited by 39 · see citing works

Targeting Biometals in Alzheimer’s Disease with Metal Chelating Agents Including Coumarin Derivatives

Gucký, A., & Hamuľaková, S. (2024) · CNS Drugs · doi:10.1007/s40263-024-01093-0 · Cited by 39 · see citing works

The Treatment of Wilson's Disease, a Rare Genetic Disorder of Copper Metabolism

Purchase, R. (2013) · Science Progress · doi:10.3184/003685013x13587771579987 · Cited by 39 · see citing works

Reactivity of Diphenylpropynone Derivatives Toward Metal-Associated Amyloid-β Species

Pithadia, A. S., Kochi, A., Soper, M. T., Beck, M. W., Liu, Y., Lee, S., DeToma, A. S., Ruotolo, B. T., & Lim, M. H. (2012) · Inorganic Chemistry · doi:10.1021/ic302084g · Cited by 38 · see citing works

Tools of the Trade: Investigations into Design Strategies of Small Molecules to Target Components in Alzheimer's Disease

Derrick, J. S., & Lim, M. H. (2015) · ChemBioChem · doi:10.1002/cbic.201402718 · Cited by 38 · see citing works

Development of coumarin–benzofuran hybrids as versatile multitargeted compounds for the treatment of Alzheimer’s Disease

Hiremathad, A., Chand, K., & Keri, R. S. (2018) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13316 · Cited by 38 · see citing works

Natural Scaffolds with Multi-Target Activity for the Potential Treatment of Alzheimer’s Disease

Piemontese, L., Vitucci, G., Catto, M., Laghezza, A., Perna, F. M., Rullo, M., Loiodice, F., Capriati, V., & Solfrizzo, M. (2018) · Molecules · doi:10.3390/molecules23092182 · Cited by 38 · see citing works

A rapid and sensitive detection of ferritin at a nanomolar level and disruption of amyloid β fibrils using fluorescent conjugated polymer

Balakrishnan, M., Hussain, S., & Iyer, P. K. (2013) · Polymer Chemistry · doi:10.1039/c3py00680h · Cited by 36 · see citing works

Effects of hydroxyl group variations on a flavonoid backbone toward modulation of metal-free and metal-induced amyloid-β aggregation

Lee, H. J., Kerr, R. A., Korshavn, K. J., Lee, J., Kang, J., Ramamoorthy, A., Ruotolo, B. T., & Lim, M. H. (2016) · Inorganic Chemistry Frontiers · doi:10.1039/c5qi00219b · Cited by 36 · see citing works

Specific self-monitoring of metal-associated amyloid-β peptide disaggregation by a fluorescent chelator

Yang, T., Wang, X., Zhang, C., Ma, X., Wang, K., Wang, Y., Luo, J. H., Liu, Y., Yao, C., & Wang, X. (2015) · Chemical Communications · doi:10.1039/c5cc08898d · Cited by 35 · see citing works

Effect of glucosamine conjugation to zinc(II) complexes of a bis-pyrazole ligand: Syntheses, characterization and anticancer activity

Bhattacharyya, S., Sarkar, A., Dey, S. K., & Mukherjee, A. (2014) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2014.07.009 · Cited by 34 · see citing works

Multifunctional quinoline-triazole derivatives as potential modulators of amyloid-β peptide aggregation

Jones, M. R., Dyrager, C., Hoarau, M., Korshavn, K. J., Lim, M. H., Ramamoorthy, A., & Storr, T. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.04.022 · Cited by 34 · see citing works

n Bu 4 NPF 6 promoted regioselective cascade synthesis of functionally embellished naphthofurans under acid, metal & solvent free conditions

Pareek, A., Dada, R., Rana, M., Sharma, A. K., & Yaragorla, S. (2016) · RSC Advances · doi:10.1039/c6ra17411f · Cited by 34 · see citing works

Exploring the multifunctionality of thioflavin- and deferiprone-based molecules as acetylcholinesterase inhibitors for potential application in Alzheimer's disease

Telpoukhovskaia, M. A., Patrick, B. O., Rodríguez‐Rodríguez, C., & Orvig, C. (2013) · Molecular BioSystems · doi:10.1039/c3mb25600f · Cited by 33 · see citing works

Multifunctional 8‐Hydroxyquinoline‐Appended Cyclodextrins as New Inhibitors of Metal‐Induced Protein Aggregation

Oliveri, V., Attanasio, F., Puglisi, A., Spencer, J., Sgarlata, C., & Vecchio, G. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201402690 · Cited by 33 · see citing works

Azo-Stilbene and Pyridine–Amine Hybrid Multifunctional Molecules to Target Metal-Mediated Neurotoxicity and Amyloid-β Aggregation in Alzheimer’s Disease

Rana, M., Cho, H., Arya, H., Bhatt, T. K., Bhar, K., Bhatt, S., Mirica, L. M., & Sharma, A. K. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.2c00502 · Cited by 33 · see citing works

New 4-N-phenylaminoquinoline derivatives as antioxidant, metal chelating and cholinesterase inhibitors for Alzheimer’s disease

Cai, R., Wang, L., Fan, J., Geng, S.-Q., & Liu, Y. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103328 · Cited by 32 · see citing works

Structural and Mechanistic Insights into Development of Chemical Tools to Control Individual and Inter‐Related Pathological Features in Alzheimer's Disease

Lee, H. J., Korshavn, K. J., Nam, Y., Kang, J., Paul, T. J., Kerr, R. A., Youn, I. S., Özbil, M., Kim, K. S., Ruotolo, B. T., et al. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201605401 · Cited by 32 · see citing works

Cuproptosis: A Copper‐Mediated Programmed Cell Death

Meena, R., Sahoo, S. S., Sunil, A., & Manna, D. (2024) · Chemistry - An Asian Journal · doi:10.1002/asia.202400934 · Cited by 31 · see citing works

A Near‐Infrared‐Controllable Artificial Metalloprotease Used for Degrading Amyloid‐β Monomers and Aggregates

Ma, M., Wang, Y., Gao, N., Liu, X., Sun, Y., Ren, J., & Qu, X. (2019) · Chemistry - A European Journal · doi:10.1002/chem.201902828 · Cited by 31 · see citing works

Tuning Reactivity of Diphenylpropynone Derivatives with Metal-Associated Amyloid-β Species via Structural Modifications

Liu, Y., Kochi, A., Pithadia, A. S., Lee, S., Nam, Y., Beck, M. W., He, X., Lee, D., & Lim, M. H. (2013) · Inorganic Chemistry · doi:10.1021/ic400851w · Cited by 30 · see citing works

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

Gomes, L. M., Bataglioli, J. C., Jussila, A. J., Smith, J. R., Walsby, C. J., & Storr, T. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00838 · Cited by 29 · see citing works

Drug-like chelating agents: a potential lead for Alzheimer's disease

Huang, W., Wei, W., & Shen, Z. (2014) · RSC Advances · doi:10.1039/c4ra09193k · Cited by 29 · see citing works

Thioflavin-based molecular probes for application in Alzheimer's disease: from in silico to in vitro models

Rodríguez‐Rodríguez, C., Telpoukhovskaia, M. A., Alí‐Torres, J., Rodrı́guez-Santiago, L., Manso, Y., Bailey, G. A., Hidalgo, J., Sodupe, M., & Orvig, C. (2014) · Metallomics · doi:10.1039/c4mt00167b · Cited by 29 · see citing works

A Trishistidine Pseudopeptide with Ability to Remove Both CuΙ and CuΙΙ from the Amyloid‐β Peptide and to Stop the Associated ROS Formation

Conte‐Daban, A., Boff, B., Matias, A. C., Aparicio, C. N. M., Gateau, C., Lebrun, C., Cerchiaro, G., Kieffer, I., Sayen, S., Guillon, E., et al. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201703429 · Cited by 29 · see citing works

Recent Discoveries on the Functions of Astrocytes in the Copper Homeostasis of the Brain: A Brief Update

Pal, A., & Prasad, R. (2014) · Neurotoxicity Research · doi:10.1007/s12640-013-9453-9 · Cited by 28 · see citing works

Importance of the Dimethylamino Functionality on a Multifunctional Framework for Regulating Metals, Amyloid-β, and Oxidative Stress in Alzheimer’s Disease

Derrick, J. S., Kerr, R. A., Korshavn, K. J., McLane, M. J., Kang, J., Nam, E., Ramamoorthy, A., Ruotolo, B. T., & Lim, M. H. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b00525 · Cited by 26 · see citing works

Computational approach to suggest a new multi-target-directed ligand as a potential medication for Alzheimer’s disease

Eslami, M., Nezafat, N., Negahdaripour, M., & Ghasemi, Y. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1564701 · Cited by 27 · see citing works

Two macrocyclic polyamines as modulators of metal-mediated Aβ40aggregation

Yang, Y., Chen, T., Zhu, S., Gu, X., Jia, X., Lu, Y., & Zhu, L. (2015) · Integrative Biology · doi:10.1039/c5ib00064e · Cited by 25 · see citing works

Rearrangement regulated cysteine fluorescent probe for cellular oxidative stress evaluation induced by copper(II)

Zhou, N., Huo, F., Yue, Y., Ma, K., & Yin, C. (2020) · Chinese Chemical Letters · doi:10.1016/j.cclet.2020.07.001 · Cited by 25 · see citing works

New Zn(II) and Cu(II) complexes with in situ generated N2O2 siloxane Schiff base ligands

Vlad, A., Zaltariov, M., Shova, S. G., Cazacu, M., Avădanei, M., Soroceanu, A., & Samoilă, P. (2016) · Polyhedron · doi:10.1016/j.poly.2016.04.038 · Cited by 25 · see citing works

Copper(II) complexation of tacrine hybrids with potential anti-neurodegenerative roles

Quintanova, C., Keri, R. S., Chaves, S., & Santos, M. A. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.06.008 · Cited by 23 · see citing works

3-Hydroxy-4-pyridinone derivatives as metal ion and amyloid binding agents

Telpoukhovskaia, M. A., Rodríguez‐Rodríguez, C., Cawthray, J. F., Scott, L. E., Page, B. D. G., Alí‐Torres, J., Sodupe, M., Bailey, G. A., Patrick, B. O., & Orvig, C. (2013) · Metallomics · doi:10.1039/c3mt00135k · Cited by 23 · see citing works

Synthesis and Biological Activity of Some Benzochromenoquinolinones: Tacrine Analogs as Potent Anti‐Alzheimer's Agents

Mahdavi, M. R., Hariri, R., Mirfazli, S. S., Lotfian, H., Rastergari, A., Firuzi, O., Edraki, N., Larijani, B. A., Akbarzadeh, T., & Saeedi, M. (2019) · Chemistry & Biodiversity · doi:10.1002/cbdv.201800488 · Cited by 21 · see citing works

Platinoid complexes to target monomeric disordered peptides: a forthcoming solution against amyloid diseases?

Hureau, C., & Faller, P. (2014) · Dalton Transactions · doi:10.1039/c3dt52954a · Cited by 20 · see citing works

A bifunctional non-natural tetrapeptide modulates amyloid-beta peptide aggregation in the presence of Cu( ii )

Márquez, M., Blancas‐Mejía, L. M., Campos, A., Rojas-Ochoa, L. F., Castañeda‐Hernández, G., & Quintanar, L. (2014) · Metallomics · doi:10.1039/c4mt00257a · Cited by 20 · see citing works

Metal-based biologically active compounds: design, synthesis, medicinal, toxicity and DNA interaction assay

Gajera, S. B., Mehta, J. V., & Patel, M. N. (2016) · Medicinal Chemistry Research · doi:10.1007/s00044-016-1503-4 · Cited by 17 · see citing works

Design of a water soluble 1,8-naphthalimide/3-hydroxy-4-pyridinone conjugate: Investigation of its spectroscopic properties at variable pH and in the presence of Fe3+, Cu2+ and Zn2+

Moniz, T., Queirós, C., Ferreira, R., Leite, A., Gameiro, P., Silva, A. M. G., & Rangel, M. (2013) · Dyes and Pigments · doi:10.1016/j.dyepig.2013.02.020 · Cited by 17 · see citing works

Aryldiazoquinoline based multifunctional small molecules for modulating Aβ 42 aggregation and cholinesterase activity related to Alzheimer's disease

Rana, M., Pareek, A., Bhardwaj, S., Arya, G., Nimesh, S., Arya, H., Bhatt, T. K., Yaragorla, S., & Sharma, A. K. (2020) · RSC Advances · doi:10.1039/d0ra05172a · Cited by 17 · see citing works

Orally Bioavailable Metal Chelators and Radical Scavengers: Multifunctional Antioxidants for the Coadjutant Treatment of Neurodegenerative Diseases

Kawada, H., & Kador, P. F. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00272 · Cited by 17 · see citing works

Minding metals: Tailoring multifunctional chelating agents for neurodegenerative disease

Perez, L. R., & Franz, K. J. (2010) · Dalton Trans. · doi:10.1039/b919237a · Cited by 156 · see citing works

Metal ion chelation in neurodegenerative disorders

Angel, I., Bar, A., Horovitz, T., Taler, G., Krakovsky, M., Resnitsky, D., Rosenberg, G., Striem, S., Friedman, J. E., & Kozak, A. (2002) · Drug Development Research · doi:10.1002/ddr.10083 · Cited by 42 · see citing works

Reorganizing Metals: the Use of Chelating Compounds as Potential Therapies for Metal-Related Neurodegenerative Disease

Badrick, A. C., & Jones, C. E. (2011) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611794785181 · Cited by 16 · 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

An Overview of Multifunctional Metal Chelators as Potential Treatments for Neurodegenerative Diseases

Lewis, F. W., & Tétard, D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804562-6.00020-8 · Cited by 1 · see citing works