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

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Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?

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Circular Dichroism and the Conformational Analysis of Biomolecules

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Rapid induction of Alzheimer A beta amyloid formation by zinc

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Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state

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

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Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T

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

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Neurobiology of Zinc and Zinc-Containing Neurons

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

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In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity

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Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

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

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

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Synthesis of β-Tubulin, Actin, and Other Proteins in Axons of Sympathetic Neurons in Compartmented Cultures

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Aβ Deposition Is Associated with Neuropil Changes, but not with Overt Neuronal Loss in the Human Amyloid Precursor Protein V717F (PDAPP) Transgenic Mouse

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Morphology and Toxicity of Aβ-(1-42) Dimer Derived from Neuritic and Vascular Amyloid Deposits of Alzheimer's Disease

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

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

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

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The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease.

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GATA-3 Is Involved in the Development of Serotonergic Neurons in the Caudal Raphe Nuclei

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

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Regional distribution of iron and iron‐regulatory proteins in the brain in aging and Alzheimer's disease

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Secondary structure of amyloid beta peptide correlates with neurotoxic activity in vitro.

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Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease

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

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Amyloidogenicity of beta A4 and beta A4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation.

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Physical, morphological and functional differences between ph 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide Abeta.

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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

Prolines and Aamyloidogenicity in Fragments of the Alzheimer's Peptide .beta./A4

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An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar aβ-amyloid in rat brain

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Perlecan Binds to the β‐Amyloid Proteins (Aβ) of Alzheimer's Disease, Accelerates Aβ Fibril Formation, and Maintains Aβ Fibril Stability

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Enzyme Activities in Relation to pH and Lactate in Postmortem Brain in Alzheimer‐Type and Other <i>Dementias</i>

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Structural Analysis of Alzheimer's β(1–40) Amyloid: Protofilament Assembly of Tubular Fibrils

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Measurements of plasma zinc

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Effects of Sulfate Ions on Alzheimer β/A4 Peptide Assemblies: Implications for Amyloid Fibril‐Proteoglycan Interactions

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

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Suppression of Mitochondrial Succinate Dehydrogenase, a Primary Target of β‐Amyloid, and Its Derivative Racemized at Ser Residue

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

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pH‐Dependent Binding of Synthetic β‐Amyloid Peptides to Glycosaminoglycans

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

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A Model for Structure-Dependent Binding of Congo Red to Alzheimer β-Amyloid Fibrils

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Mitochondrial function impairment induced by amyloid β-peptide on PC12 cells

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Alzheimer's Disease, β-Amyloid Protein and Zinc

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Differential Effects of Apolipoprotein E Isoforms on Metal-Induced Aggregation of Aβ Using Physiological Concentrations

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Amyloid β protein-induced neuronal cell death: neurotoxic properties of aggregated amyloid β protein

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Protection against amyloid beta peptide toxicity by zinc

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Molecular modeling of the Abeta1-42 peptide from Alzheimer's disease

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Amyloid β protein inhibits cellular MTT reduction not by suppression of mitochondrial succinate dehydrogenase but by acceleration of MTT formazan exocytosis in cultured rat cortical astrocytes

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The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis

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

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Effect of divalent metal ions and pH upon the binding reactivity of human serum amyloid P component, a C-reactive protein homologue, for zymosan. Preferential reactivity in the presence of copper and acidic pH.

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Can Deposition of Amyloid Be Prevented in Alzheimer's Disease?a

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Transcutaneous electrical nerve stimulation

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

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

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Bioinorganic Chemistry of Alzheimer’s Disease

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The redox chemistry of the Alzheimer's disease amyloid β peptide

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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 603 · see citing works

Curcumin and its Derivatives: Their Application in Neuropharmacology and Neuroscience in the 21st Century

Lee, W., Loo, C., Bebawy, M., Luk, F., Mason, R. S., & Rohanizadeh, R. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311040002 · Cited by 539 · 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

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

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

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

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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

Granular Tau Oligomers as Intermediates of Tau Filaments

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

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

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 304 · see citing works

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

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

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

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

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

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

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

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

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

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

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

Tabner, B. J., El‐Agnaf, O. M. A., Turnbull, S., German, M. J., Paleologou, K. E., Hayashi, Y., Cooper, L. J., Fullwood, N. J., & Allsop, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500238200 · Cited by 241 · see citing works

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

Masters, C. L., Cappai, R., Barnham, K. J., & Villemagne, V. L. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03989.x · Cited by 237 · 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

A Rapid Label-Free Electrochemical Detection and Kinetic Study of Alzheimer's Amyloid Beta Aggregation

Vestergaard, M. C. M., Kerman, K., Saito, M., Nagatani, N., Takamura, Y., & Tamiya, E. (2005) · Journal of the American Chemical Society · doi:10.1021/ja052522q · Cited by 218 · see citing works

Implications of the kynurenine pathway and quinolinic acid in Alzheimer's disease

Guillemin, G. J., & Brew, B. J. (2002) · Redox Report · doi:10.1179/135100002125000550 · Cited by 212 · see citing works

Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-β Peptides

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

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