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

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Stabilization and Characterization of Cytotoxic Aβ 40 Oligomers Isolated from an Aggregation Reaction in the Presence of Zinc Ions

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The Second Cu(II)-Binding Site in a Proton-Rich Environment Interferes with the Aggregation of Amyloid-β(1−40) into Amyloid Fibrils

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Copper(ii)–human amylin complex protects pancreatic cells from amylin toxicity

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CuII Binding Properties of N-Truncated Aβ Peptides: In Search of Biological Function

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Label-free electrochemical detection of Amyloid beta aggregation in the presence of iron, copper and zinc

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Phage Display Affords Peptides that Modulate β-Amyloid Aggregation

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Coordination of copper(II) ions by the 11–20 and 11–28 fragments of human and mouse β-amyloid peptide

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Current understanding of metal-dependent amyloid-β aggregation and toxicity

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Mechanism of zinc(II)-promoted amyloid formation: zinc(II) binding facilitates the transition from the partially α-helical conformer to aggregates of amyloid β protein(1–28)

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Study of a Bifunctional Aβ Aggregation Inhibitor with the Abilities of Antiamyloid-β and Copper Chelation

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Effects of Cu(II) on the aggregation of amyloid-β

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Intercommunication between metal ions and amyloidogenic peptides or proteins in protein misfolding disorders

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Tripeptide GGH as the Inhibitor of Copper-Amyloid-β-Mediated Redox Reaction and Toxicity

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Zn2+’s Ability to Alter the Distribution of Cu2+ among the Available Binding Sites of Aβ(1–16)-Polyethylenglycol-ylated Peptide: Implications in Alzheimer’s Disease

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Copper Enhances Amyloid-β Peptide Neurotoxicity and non β-Aggregation: A Series of Experiments Conducted upon Copper-Bound and Copper-Free Amyloid-β Peptide

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Thermal aggregation of β-lactoglobulin in presence of metal ions

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Direct electrochemical and AFM detection of amyloid-β peptide aggregation on basal plane HOPG

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

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Sn-Triggered Two-Dimensional Fast Protein Assembly with Emergent Functions

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A label-free and signal-on electrochemiluminescence strategy for sensitive amyloid-beta assay

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Quenched hydrogen/deuterium exchange NMR characterization of amyloid‐β peptide aggregates formed in the presence of Cu2+ or Zn2+

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Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1–40) and zinc(II)-bound amyloid-β(1–42) with dynamics

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Iminodiacetic acid-conjugated nanoparticles as a bifunctional modulator against Zn2+-mediated amyloid β-protein aggregation and cytotoxicity

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Inhibition of the Escherichia coli RecA protein: zinc(II), copper(II) and mercury(II) trap RecA as inactive aggregates

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Role of zinc along with ascorbic acid and folic acid during long-termin vitroalbumin glycation

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Metallostasis and amyloid β-degrading enzymes

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Rapid label-free detection of metal-induced Alzheimer’s amyloid β peptide aggregation by electrochemical method

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Redox-Dependent Copper Ion Modulation of Amyloid-β (1-42) Aggregation In Vitro

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Copper in Alzheimer’s disease: Implications in amyloid aggregation and neurotoxicity

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Electrochemical Oxidation of Benzothiazole Dyes for Monitoring Amyloid Formation Related to the Alzheimer’s Disease

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Amyloid-β peptide (1–42) aggregation induced by copper ions under acidic conditions

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Metal-mediated formation of fibrillar ABri amyloid

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Copper inducing Aβ42 rather than Aβ40 nanoscale oligomer formation is the key process for Aβ neurotoxicity

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Secondary Metabolites from Plants Possessing Inhibitory Properties against Beta-Amyloid Aggregation as Revealed by Thioflavin-T Assay and Correlations with Investigations on Transgenic Mouse Models of Alzheimer's Disease

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Electrochemical and Conformational Consequences of Copper (CuI and CuII) Binding to β‐Amyloid(1–40)

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Real-Time Monitoring of Self-Aggregation of β-Amyloid by a Fluorescent Probe Based on Ruthenium Complex

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Protective effect of zinc on amyloid-ß 25–35 and 1–40 mediated toxicity

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Cu(II) Potentiation of Alzheimer Aβ1-40 Cytotoxicity and Transition on its Secondary Structure

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The Rapid Exchange of Zinc2+ Enables Trace Levels to Profoundly Influence Amyloid-β Misfolding and Dominates Assembly Outcomes in Cu2+/Zn2+ Mixtures

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Metal attenuating therapies in neurodegenerative disease

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Alzheimer’s amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity

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NMR studies of zinc binding in a multi-histidinic peptide fragment

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Brazilin inhibits the Zn2+-mediated aggregation of amyloid β-protein and alleviates cytotoxicity

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Protective Effects of Vitamin E against Oxidative Damage Induced by Aβ1–40Cu(II) Complexes

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Detection of Alzheimer’s amyloid beta aggregation by capturing molecular trails of individual assemblies

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Aβ20–29 peptide blocking apoE/Aβ interaction reduces full-length Aβ42/40 fibril formation and cytotoxicity in vitro

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Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions

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Kinetic Insights into Zn2+-Induced Amyloid β-Protein Aggregation Revealed by Stopped-Flow Fluorescence Spectroscopy

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Nitration of amyloid-β peptide (1–42) as a protective mechanism for the amyloid-β peptide (1–42) against copper ion toxicity

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Numerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic Synapses

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Hsp27 suppresses the Cu2+-induced amyloidogenicity, redox activity, and cytotoxicity of α-synuclein by metal ion stripping

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Histidine-rich protein Hpn from Helicobacter pylori forms amyloid-like fibrils in vitro and inhibits the proliferation of gastric epithelial AGS cells

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Zinc binding agonist effect on the recognition of the β-amyloid (4–10) epitope by anti-β-amyloid antibodies

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Aβ Aggregation inhibitors. Part 1: Synthesis and biological activity of phenylazo benzenesulfonamides

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Inhibition of Alzheimer amyloid β aggregation by polyvalent trehalose

Miura, Y., You, C., & Ohnishi, R. (2008) · Science and Technology of Advanced Materials · doi:10.1088/1468-6996/9/2/024407 · Cited by 21

Distribution of synaptic zinc in the macaque monkey amygdala

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Development of aggregation inhibitors for amyloid‐β peptides and their evaluation by quartz‐crystal microbalance

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Methods for analyzing the coordination and aggregation of metal–amyloid-β

Park, S., Na, C., Han, J., & Lim, M. H. (2023) · Metallomics · doi:10.1093/mtomcs/mfac102 · Cited by 19

Different zinc(II) complex species and binding modes at Aβ N-terminus drive distinct long range cross-talks in the Aβ monomers

Pietropaolo, A., Satriano, C., Strano, G., Mendola, D. L., & Rizzarelli, E. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.08.013 · Cited by 20

Role of Amyloid-β–Metal Interactions In Alzheimer‘s Disease

Duce, J. A., Bush, A. I., & Adlard, P. A. (2011) · Future Neurology · doi:10.2217/fnl.11.43 · Cited by 20

The in vivo functions of a histidine-rich protein Hpn in Helicobacter pylori: Linking gastric and Alzheimer’s diseases together?

Ge, R., & Sun, X. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.07.038 · Cited by 20

Zn2+ Interaction with Amyloid-B: Affinity and Speciation

Arena, G., & Rizzarelli, E. (2019) · Molecules · doi:10.3390/molecules24152796 · Cited by 20

Ameliorative Effects of Apple Cider Vinegar on Neurological Complications via Regulation of Oxidative Stress Markers

Tripathi, S., Kumari, U., & Mitra Mazumder, P. (2020) · Journal of Food Biochemistry · doi:10.1111/jfbc.13504 · Cited by 19

pH-dependent kinetics of copper ions binding to amyloid-β peptide

Bin, Y., Chen, S., & Xiang, J. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.10.013 · Cited by 19

The initial stage of structural transformation of Aβ42 peptides from the human and mole rat in the presence of Fe2+ and Fe3+: Related to Alzheimer's disease

Vahed, M., Sweeney, A., Shirasawa, H., & Vahed, M. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107128 · Cited by 19

Aluminium, Tau and Alzheimer's Disease

Exley, C. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12403 · Cited by 19

An inorganic overview of natural Aβ fragments: Copper(II) and zinc(II)-mediated pathways

Lanza, V., Bellia, F., & Rizzarelli, E. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.004 · Cited by 18

NMR metabolomic investigation of astrocytes interacted with Aβ42 or its complexes with either copper(II) or zinc(II)

Rocchi, A., Valensin, D., Aldinucci, C., Giani, G., Barbucci, R., Gaggelli, E., Kozłowski, H., & Valensin, G. (2012) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2012.08.021 · Cited by 18

New curcumin-derived ligands and their affinity towards Ga 3+ , Fe 3+ and Cu 2+ : spectroscopic studies on complex formation and stability in solution

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Intertwined Pathologies of Amyloid-β and Metal Ions in Alzheimer’s Disease: Metal–Amyloid-β

Nam, G., & Lim, M. H. (2019) · Chemistry Letters · doi:10.1246/cl.190281 · Cited by 16

The Kynurenine Pathway

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Rapid Formation of a Preoligomeric Peptide–Metal–Peptide Complex Following Copper(II) Binding to Amyloid β Peptides

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Aβ8-20 Fragment as an Anti-Fibrillogenic and Neuroprotective Agent: Advancing toward Efficient Alzheimer’s Disease Treatment

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A novel method for expression and purification of authentic amyloid-β with and without 15N labels

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Distribution and progression of amyloid-β deposits in the amygdala of the aged macaque monkey, and parallels with zinc distribution

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Electrochemical “Signal‐On” Reporter for Amyloid Aggregates

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Reversibility of β-Amyloid Self-Assembly: Effects of pH and Added Salts Assessed by Fluorescence Photobleaching Recovery

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Coordinating to Three Histidine Residues: Cu(II) Promotes Oligomeric and Fibrillar Amyloid-β Peptide to Precipitate in a Non-β Aggregation Manner

Yang, X., Huang, H., Chen, L., Xu, W. X., & Jiang, Z.-F. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1186 · Cited by 13

Attenuated cytotoxicity but enhanced βfibril of a mutant amyloid β‐peptide with a methionine to cysteine substitution

Dai, X., Sun, Y., & Jiang, Z.-F. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.02.038 · Cited by 13

Aβ-40 Y10F Increases βfibrils Formation but Attenuates the Neurotoxicity of Amyloid-β Peptide

Dai, X., Chang, P., Liu, W., Xu, K., Sun, Y., Zhu, S., & Jiang, Z.-F. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13055324 · Cited by 13

Prediction of amyloid aggregation rates by machine learning and feature selection

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Racemization of the Aspartic Acid Residue of Amyloid-β Peptide by a Radical Reaction

TAMBO, K., Yamaguchi, T., Kobayashi, K., Terauchi, E., Ichi, I., & Kojo, S. (2013) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.120797 · Cited by 13

Copper is a potent inhibitor of the propensity for human ProIAPP1-48 to form amyloid fibrils in vitro

Exley, C., Mold, M. J., Shardlow, E., Shuker, B., Ikpe, B., Wu, L., & Fraser, P. E. (2012) · journal of Diabetes Research and Clinical Metabolism · doi:10.7243/2050-0866-1-3 · Cited by 12

Reciprocal modulation of Aβ42 aggregation by copper and homocysteine

Keskitalo, S., Farkas, M., Hanenberg, M., Szodorai, A., Kulic, L., Semmler, A., Weller, M., Nitsch, R. M., & Linnebank, M. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00237 · Cited by 13

Role of PTA in the prevention of Cu(amyloid-β) induced ROS formation and amyloid-β oligomerisation in the presence of Zn

Atrián‐Blasco, E., Cerrada, E., Faller, P., Laguna, M., & Hureau, C. (2019) · Metallomics · doi:10.1039/c9mt00011a · Cited by 12

Nonfibrous β-structured aggregation of an Aβ model peptide (Ad-2α) on GM1/DPPC mixed monolayer surfaces

Kawasaki, T., Asaoka, K., Mihara, H., & Okahata, Y. (2005) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2005.07.027 · Cited by 11

Heparin Modulates the Kinetics of Zinc-Induced Aggregation of Amyloid-β Peptides

Radko, S. P., Khmeleva, S. A., Mantsyzov, A. B., Kiseleva, Y. Y., Mitkevich, V. A., Kozin, S. A., & Makarov, A. А. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171120 · Cited by 11

Molecular dynamics simulations of copper binding to amyloid-β Glu22 mutants

Mutter, S. T., Turner, M., Deeth, R. J., & Platts, J. A. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e03071 · Cited by 10

Effects of zinc and carnosine on aggregation kinetics of Amyloid-β40 peptide

Shen, F., Regmi, D., Islam, M., Somu, D. R., Merk, V. M., & Du, D. (2022) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2022.101333 · Cited by 9

Heart Failure with Preserved Ejection Fraction and Diabetes Mellitus

Magri, C. J., Cassar, A., Fava, S., & Felice, H. (2012) · journal of Diabetes Research and Clinical Metabolism · doi:10.7243/2050-0866-1-2 · Cited by 9

Boron: An intriguing factor in retarding Alzheimer's progression

Das, A., Rajput, V., Chowdhury, D., Choudhary, R., & Bodakhe, S. H. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105897 · Cited by 9

Novel conformation-sensitive antibodies specific to three- and four-repeat tau

Ueno, H., Murayama, O., Maeda, S., Sahara, N., Park, J.-M., Murayama, M., Sanda, A., Iwahashi, K., Matsuda, M., & Takashima, A. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.176 · Cited by 8

Revisiting Cu(II) Bound Amyloid-β40 and Amyloid-β42 Peptides: Varying Coordination Chemistries

Coskuner‐Weber, O. (2018) · Journal of the Turkish Chemical Society Section A Chemistry · doi:10.18596/jotcsa.424144 · Cited by 8

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

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

Current understanding of metal-dependent amyloid-β aggregation and toxicity

Yi, Y., & Lim, M. H. (2022) · RSC Chemical Biology · doi:10.1039/d2cb00208f · Cited by 50

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

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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

Effects of zinc and copper on β-aggregation and cytotoxicity of amyloid-β protein

Yoshiike, Y. (2002)