Rapid induction of Alzheimer A beta amyloid formation by zinc

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

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

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022

Amyloid Deposits and Amyloidosis

Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780

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

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

A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L. (1992) · Nature Genetics · doi:10.1038/ng0892-345 · Cited by 1,513

Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

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

Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type

Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399

Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene

Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214

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

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864

Oxidative stress, aging, and diseases

Liguori, I., Russo, G., Curcio, F., Bulli, G., Aran, L., Della-Morte, D., Gargiulo, G., Testa, G., Cacciatore, F., Bonaduce, D., et al. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s158513 · Cited by 3,979

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

Metals in Neurobiology: Probing Their Chemistry and Biology with Molecular Imaging

Que, E. L., Domaille, D. W., & Chang, C. J. (2008) · Chemical Reviews · doi:10.1021/cr078203u · Cited by 2,077

The neurobiology of zinc in health and disease

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

Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease

Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750

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

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

MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins

Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652

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

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

Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357

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

Trace elements in human physiology and pathology: zinc and metallothioneins

Tapiero, H., & Tew, K. D. (2003) · Biomedicine & Pharmacotherapy · doi:10.1016/s0753-3322(03)00081-7 · Cited by 1,324

Oxidative stress and Alzheimer disease

Christen, Y. (2000) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/71.2.621s · Cited by 1,176

Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies.

Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138

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 1,117

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

Fluorescent chemosensors for Zn2+

Xu, Z., Yoon, J., & Spring, D. R. (2010) · Chemical Society Reviews · doi:10.1039/b916287a · Cited by 983

Age-related macular degeneration: etiology, pathogenesis, and therapeutic strategies

Ambati, J., Ambati, B. K., Yoo, S. H., Ianchulev, S., & Adamis, A. P. (2003) · Survey of Ophthalmology · doi:10.1016/s0039-6257(03)00030-4 · Cited by 959

Mechanisms of Neuronal Degeneration in Alzheimer's Disease

Yankner, B. A. (1996) · Neuron · doi:10.1016/s0896-6273(00)80115-4 · Cited by 953

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

Wei, G., Su, Z., Reynolds, N. P., Arosio, P., Hamley, I. W., Gazit, E., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00542j · Cited by 913

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

Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 892

Oxidative Stress and the Pathogenesis of Alzheimer's Disease

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

Inclusion body myositis and myopathies

Griggs, R. C., Askanas, V., DiMauro, S., Engel, A., Karpati, G., Mendell, J. R., & Rowland, L. P. (1995) · Annals of Neurology · doi:10.1002/ana.410380504 · Cited by 834

Zinc in the physiology and pathology of the CNS

Sensi, S. L., Paoletti, P., Bush, A. I., & Sekler, I. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2734 · Cited by 759

ZINC AND BRAIN INJURY

Choi, D. W., & Koh, J. Y. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.347 · Cited by 752

Molecular pathways to neurodegeneration

Bossy-Wetzel, E., Schwarzenbacher, R., & Lipton, S. A. (2004) · Nature Medicine · doi:10.1038/nm1067 · Cited by 740

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

History and progress of hypotheses and clinical trials for Alzheimer’s disease

Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723

Overcoming the Blood–Brain Barrier: The Role of Nanomaterials in Treating Neurological Diseases

Furtado, D., Björnmalm, M., Ayton, S., Bush, A. I., Kempe, K., & Caruso, F. (2018) · Advanced Materials · doi:10.1002/adma.201801362 · Cited by 708

Zn2+-Triggered Amide Tautomerization Produces a Highly Zn2+-Selective, Cell-Permeable, and Ratiometric Fluorescent Sensor

Xu, Z., Baek, K.-H., Kim, H., Cui, J., Qian, X. H., Spring, D. R., Shin, I., & Yoon, J. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907334j · Cited by 692

Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. Cohen

Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 690

Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease

Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 695

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683

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

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

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 658

Amyloid β protein forms ion channels: implications for Alzheimer's disease pathophysiology

LIN, H., Bhatia, R., & Lal, R. (2001) · The FASEB Journal · doi:10.1096/fj.01-0377com · Cited by 656

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

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

Water-soluble Aβ(N-40, N-42) oligomers in normal and Alzheimer disease brains

Kuo, Y.-M., Emmerling, M. R., Vigo-Pelfrey, C., Kasunic, T. C., Kirkpatrick, J. B., Murdoch, G. H., Ball, M. J., & Roher, A. E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4077 · Cited by 618

Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer’s Disease, Parkinson’s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade

Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 612

Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase

Estévez, A. G., Crow, J. P., Sampson, J. B., Reiter, C., Zhuang, Y., Richardson, G. J., Tarpey, M. M., Barbeito, L., & Beckman, J. S. (1999) · Science · doi:10.1126/science.286.5449.2498 · Cited by 596

Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer’s disease

Miller, L. M., Wang, Q., Telivala, T. P., Smith, R., Lanzirotti, A., & Judith Miklossy, A. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.09.004 · Cited by 588

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 587

Zn2+: a novel ionic mediator of neural injury in brain disease

Weiss, J. H., Sensi, S. L., & Koh, J. Y. (2000) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)01541-8 · Cited by 575

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 582

An iron-responsive element type II in the 5'-untranslated region of the Alzheimer's amyloid precursor protein transcript

Rogers, J. T., Randall, J. D., Cahill, C. M., Eder, P. S., Huang, X., Gunshin, H., Leiter, L., McPhee, J., Sarang, S. S., Utsuki, T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207435200 · Cited by 551

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 544

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

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

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

Prion Protein Selectively Binds Copper(II) Ions

Stöckel, J., Safar, J., Wallace, A. C., Cohen, F. E., & Prusiner, S. B. (1998) · Biochemistry · doi:10.1021/bi972827k · Cited by 527

Critical Review of Exposure and Effects: Implications for Setting Regulatory Health Criteria for Ingested Copper

Taylor, A. A., Tsuji, J. S., Garry, M. R., McArdle, M. E., Goodfellow, W. L., Adams, W. J., & Menzie, C. A. (2019) · Environmental Management · doi:10.1007/s00267-019-01234-y · Cited by 518

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

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

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

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

Myelin dysfunction drives amyloid-β deposition in models of Alzheimer’s disease

Depp, C., Sun, T., Sasmita, A. O., Spieth, L., Berghoff, S. A., Nazarenko, T., Overhoff, K., Steixner-Kumar, A. A., Subramanian, S., Arinrad, S., et al. (2023) · Nature · doi:10.1038/s41586-023-06120-6 · Cited by 493

Metal Toxicity Links to Alzheimer's Disease and Neuroinflammation

Huat, T. J., Camats‐Perna, J., Newcombe, E. A., Valmas, N., Kitazawa, M., & Medeiros, R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.01.018 · Cited by 501

Amyloid Precursor Protein, Presenilins, and α-Synuclein: Molecular Pathogenesis and Pharmacological Applications in Alzheimer’s Disease

Suh, Y.-H., & Checler, F. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.3.469 · Cited by 476

Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease

Syme, C. D., Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313572200 · Cited by 459

The Role of Environmental Exposures in Neurodegeneration and Neurodegenerative Diseases

Cannon, J. R., & Greenamyre, J. T. (2011) · Toxicological Sciences · doi:10.1093/toxsci/kfr239 · Cited by 475

Metal dyshomeostasis and oxidative stress in Alzheimer’s disease

Greenough, M. A., Camakaris, J., & Bush, A. I. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.08.014 · Cited by 447

Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice

Lee, J., Cole, T. B., Palmiter, R. D., Suh, S. W., & Koh, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092034699 · Cited by 432

The toxicity in vitro of β-amyloid protein

Iversen, L. L., Mortishire‐Smith, R. J., Pollack, S. J., & Shearman, M. S. (1995) · Biochemical Journal · doi:10.1042/bj3110001 · Cited by 428

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

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

Movement of zinc and its functional significance in the brain

Takeda, A. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00044-8 · Cited by 422

Overview of mammalian zinc transporters

Kambe, T., Yamaguchi‐Iwai, Y., Sasaki, R., & Nagao, M. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3148-y · Cited by 406

Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases

Viles, J. H. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.003 · Cited by 404

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 407

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

Structure of the Zinc Transporter YiiP

Lu, M., & Fu, D. (2007) · Science · doi:10.1126/science.1143748 · Cited by 386

Crosstalk between Nitric Oxide and Zinc Pathways to Neuronal Cell Death Involving Mitochondrial Dysfunction and p38-Activated K+ Channels

Bossy‐Wetzel, E., Talantova, M. V., Lee, W. D., Schölzke, M. N., Harrop, A., Mathews, E. A., Götz, T., Han, J., Ellisman, M. H., Perkins, G. A., et al. (2004) · Neuron · doi:10.1016/s0896-6273(04)00015-7 · Cited by 385

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

Aggregation of Secreted Amyloid β-Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture

Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydel, R. E., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9564 · Cited by 369

Aluminium speciation in relation to aluminium bioavailability, metabolism and toxicity

Berthon, G. (2002) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(02)00021-8 · Cited by 366

Synaptically released zinc: Physiological functions and pathological effects

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

Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau

Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363

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 360

Metallostasis in Alzheimer's disease

Ayton, S., Lei, P., & Bush, A. I. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.558 · Cited by 359

Metals and amyloid‐β in Alzheimer's disease

Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., & Li, Q. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00434.x · Cited by 356

Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains

Suh, S. W., Jensen, K. B., Jensen, M. S., Silva, D. S., Kesslak, P. J., Danscher, G., & Frederickson, C. J. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02096-x · Cited by 353

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

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

Fibrillar β-Amyloid Induces Microglial Phagocytosis, Expression of Inducible Nitric Oxide Synthase, and Loss of a Select Population of Neurons in the Rat CNS In Vivo

Weldon, D. T., Rogers, S. D., Ghilardi, J. R., Finke, M. P., Cleary, J. P., O’Hare, E., Esler, W. P., Maggio, J. E., & Mantyh, P. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-06-02161.1998 · Cited by 348

Implications of peptide assemblies in amyloid diseases

Ke, P. C., Sani, M., Ding, F., Käkinen, A., Javed, I., Separovic, F., Davis, T. P., & Mezzenga, R. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00372b · Cited by 340

Copper(II)-induced self-oligomerization of α-synuclein

Paik, S. R., Shin, H.-J., Lee, J., Chang, C., & Kim, J. (1999) · Biochemical Journal · doi:10.1042/bj3400821 · Cited by 340

The Neurophysiology and Pathology of Brain Zinc

Sensi, S. L., Paoletti, P., Koh, J., Aizenman, E., Bush, A. I., & Hershfinkel, M. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3454-11.2011 · Cited by 333

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

The essential elements of Alzheimer’s disease

Lei, P., Ayton, S., & Bush, A. I. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.008207 · Cited by 344

Detection of single amyloid β-protein aggregates in the cerebrospinal fluid of Alzheimer's patients by fluorescence correlation spectroscopy

Pitschke, M., Prior, R., Haupt, M., & Riesner, D. (1998) · Nature Medicine · doi:10.1038/nm0798-832 · Cited by 326

Probing oxidative stress: Small molecule fluorescent sensors of metal ions, reactive oxygen species, and thiols

Hyman, L. M., & Franz, K. J. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.009 · Cited by 328

Link between Aluminum and the Pathogenesis of Alzheimer′s Disease: The Integration of the Aluminum and Amyloid Cascade Hypotheses

Kawahara, M., & Kato-Negishi, M. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/276393 · Cited by 509

Mouse models of Alzheimer's disease

Hall, A. M., & Roberson, E. D. (2012) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2011.11.017 · Cited by 317

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 317

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

Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer’s disease 1 1Edited by P. E. Wright

Shao, H., Jao, S., Ma, K., & Zagorski, M. G. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2348 · Cited by 308

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

Zou, K., Gong, J.-S., Yanagisawa, K., & Michikawa, M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04833.2002 · Cited by 305

Zinc ions promote Alzheimer Aβ aggregation via population shift of polymorphic states

Miller, Y., Ma, B., & Nussinov, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913114107 · Cited by 305

Structural Changes of Region 1-16 of the Alzheimer Disease Amyloid β-Peptide upon Zinc Binding and in Vitro Aging

Zirah, S., Kozin, S. A., Mazur, A. K., Blond, A., Cheminant, M., Ségalas-Milazzo, I., Debey, P., & Rebuffat, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504454200 · Cited by 306

Synthesis, optimization and applications of ZnO/polymer nanocomposites

Ponnamma, D., Cabibihan, J., Rajan, M., Pethaiah, S. S., Deshmukh, K., Gogoi, J. P., Pasha, S. K. K., Ahamed, M. B., Jagadish, K., Chandrashekar, B. N., et al. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.01.081 · Cited by 311

The function of metallothionein.

Vallee, B. (1995) · Neurochemistry International · doi:10.1016/0197-0186(94)00165-q · Cited by 303

Structure of Amyloid A4‐(1–40)‐Peptide of Alzheimer's Disease

Sticht, H., Bayer, P., Willbold, D., Dames, S. A., Hilbich, C., Beyreuther, K. T., Frank, R. W., & ROSCH, P. J. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.293_1.x · Cited by 305

Copper complexes of bis(thiosemicarbazones): from chemotherapeutics to diagnostic and therapeutic radiopharmaceuticals

Paterson, B. M., & Donnelly, P. S. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00215a · Cited by 298

Selenium, selenoproteins and neurodegenerative diseases

Cardoso, B. R., Roberts, B. R., Bush, A. I., & Hare, D. J. (2015) · Metallomics · doi:10.1039/c5mt00075k · Cited by 300

Selective Aggregation of Endogenous β‐Amyloid Peptide and Soluble Amyloid Precursor Protein in Cerebrospinal Fluid by Zinc

Brown, A. M., Tummolo, D. M., Rhodes, K. J., Hofmann, J. R., Jacobsen, J. S., & Sonnenberg‐Reines, J. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031204.x · Cited by 55

The role of zinc in the cerebral deposition of A beta amyloid in Alzheimer's disease

Bush, A. I., & Re, T. (1995)

Role of Interaction between Zinc and Amyloid Beta in Pathogenesis of Alzheimer’s Disease

Kozin, S. A. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923140055 · Cited by 14

Zinc‐Induced Aggregation of Human and Rat β‐Amyloid Peptides In Vitro

Esler, W. P., Stimson, E. R., Jennings, J. M., Ghilardi, J. R., Mantyh, P. W., & Maggio, J. E. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66020723.x · Cited by 135

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