Why the Ala-His-His Peptide Is an Appropriate Scaffold to Remove and Redox Silence Copper Ions from the Alzheimer’s-Related Aβ Peptide

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

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The Amyloid-β Pathway in Alzheimer’s Disease

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Role of Catalase in Oxidative Stress- and Age-Associated Degenerative Diseases

Nandi, A., Yan, L.-J., Jana, C. K., & Das, N. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9613090 · Cited by 1,185 · see citing works

Ascorbate regulation and its neuroprotective role in the brain

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Alzheimer’s disease drug development pipeline: 2022

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Vitamin C function in the brain: Vital role of the ascorbate transporter SVCT2

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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

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Amino Terminal Cu(II)- and Ni(II)-Binding (ATCUN) Motif of Proteins and Peptides: Metal Binding, DNA Cleavage, and Other Properties

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Binding of transition metal ions to albumin: Sites, affinities and rates

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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 483 · see citing works

Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State

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Recent advances on drug development and emerging therapeutic agents for Alzheimer’s disease

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Brain penetrating peptides and peptide–drug conjugates to overcome the blood–brain barrier and target CNS diseases

Zhou, X., Smith, Q. R., & Liu, X. (2021) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1695 · Cited by 218 · see citing works

Regulation of Copper and Iron Homeostasis by Metal Chelators: A Possible Chemotherapy for Alzheimer’s Disease

Robert, A., Liu, Y., Nguyen, M., & Meunier, B. (2015) · Accounts of Chemical Research · doi:10.1021/acs.accounts.5b00119 · Cited by 212 · see citing works

Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1–16 Amyloid‐β Peptide: A Key Role of the First Two N‐Terminus Residues

Dorlet, P., Gambarelli, S., Faller, P., & Hureau, C. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200904567 · Cited by 196 · see citing works

The Alzheimer’s therapeutic PBT2 promotes amyloid‐β degradation and GSK3 phosphorylation via a metal chaperone activity

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Peptides as complexing agents: Factors influencing the structure and thermodynamic stability of peptide complexes

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Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 1: An overview

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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

Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance

Atrián‐Blasco, E., Gonzalez, P., Santoro, A., Aliès, B., Faller, P., & Hureau, C. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.007 · Cited by 168 · see citing works

Metallobiology and therapeutic chelation of biometals (copper, zinc and iron) in Alzheimer’s disease: Limitations, and current and future perspectives

Fasae, K. D., Abolaji, A. O., Faloye, T. R., Odunsi, A., Oyetayo, B. O., Enya, J. I., Rotimi, J. A., Akinyemi, R., Whitworth, A. J., & Aschner, M. (2021) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2021.126779 · Cited by 160 · see citing works

Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data

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Advances in Lipid and Metal Nanoparticles for Antimicrobial Peptide Delivery

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Challenges of peptide and protein drug delivery by oral route: Current strategies to improve the bioavailability

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

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N‐Terminal Cu‐Binding Motifs (Xxx‐Zzz‐His, Xxx‐His) and Their Derivatives: Chemistry, Biology and Medicinal Applications

Gonzalez, P., Bossak‐Ahmad, K., Stefaniak, E., Hureau, C., Raibaut, L., Bal, W., & Faller, P. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201705398 · Cited by 142 · see citing works

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

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Porous organic polymers for drug delivery: hierarchical pore structures, variable morphologies, and biological properties

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Importance of dynamical processes in the coordination chemistry and redox conversion of copper amyloid-β complexes

Hureau, C., Balland, V., Coppel, Y., Solari, P. L., Fonda, E., & Faller, P. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0570-0 · Cited by 134 · see citing works

A Functional Role for Aβ in Metal Homeostasis? N‐Truncation and High‐Affinity Copper Binding

Mital, M., Wezynfeld, N. E., Frączyk, T., Wiloch, M. Z., Wawrzyniak, U. E., Bonna, A., Tumpach, C., Barnham, K. J., Haigh, C. L., Bal, W., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502644 · Cited by 132 · see citing works

Therapeutic Redistribution of Metal Ions To Treat Alzheimer’s Disease

Crouch, P. J., & Barnham, K. J. (2012) · Accounts of Chemical Research · doi:10.1021/ar300074t · Cited by 125 · see citing works

X-ray and solution structures of Cu(II) GHK and Cu(II) DAHK complexes: influence on their redox properties.

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Free Superoxide is an Intermediate in the Production of H 2 O 2 by Copper(I)‐Aβ Peptide and O 2

Reybier, K., Ayala, S., Aliès, B., Rodrigues, J. V., Rodriguez, S. B., Penna, G. L., Collin, F., Gomes, C. M., Hureau, C., & Faller, P. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201508597 · Cited by 120 · see citing works

Peptidomimetics: An Overview of Recent Medicinal Chemistry Efforts toward the Discovery of Novel Small Molecule Inhibitors

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Oral Treatment with the d -Enantiomeric Peptide D3 Improves the Pathology and Behavior of Alzheimer’s Disease Transgenic Mice

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

Rana, M., & Sharma, A. K. (2018) · Metallomics · doi:10.1039/c8mt00203g · Cited by 113 · see citing works

Cupric–amyloid β peptide complex stimulates oxidation of ascorbate and generation of hydroxyl radical

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Antimicrobial Peptides and Copper(II) Ions: Novel Therapeutic Opportunities

Portelinha, J., Duay, S. S., Yu, S. I., Heilemann, K., Libardo, M. D. J., Juliano, S. A., Klassen, J. L., & Angeles-Boza, A. M. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00921 · Cited by 109 · see citing works

Multi-Targets: An Unconventional Drug Development Strategy for Alzheimer’s Disease

Gong, C., Dai, C., Liu, F., & Iqbal, K. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.837649 · Cited by 109 · see citing works

Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides

Aliès, B., Conte‐Daban, A., Sayen, S., Collin, F., Kieffer, I., Guillon, E., Faller, P., & Hureau, C. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b01733 · Cited by 106 · see citing works

Thermodynamic study of Cu2+ binding to the DAHK and GHK peptides by isothermal titration calorimetry (ITC) with the weaker competitor glycine

Trapaidze, A., Hureau, C., Bal, W., Winterhalter, M., & Faller, P. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-011-0824-5 · Cited by 103 · see citing works

Recent Advances in Poly(α-L-glutamic acid)-Based Nanomaterials for Drug Delivery

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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

Reevaluation of Copper(I) Affinity for Amyloid‐β Peptides by Competition with Ferrozine—An Unusual Copper(I) Indicator

Aliès, B., Badei, B., Faller, P., & Hureau, C. (2011) · Chemistry - A European Journal · doi:10.1002/chem.201102746 · Cited by 99 · 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

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

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A Prochelator Activated by β-Secretase Inhibits Aβ Aggregation and Suppresses Copper-Induced Reactive Oxygen Species Formation

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Protective effects of GHK-Cu in bleomycin-induced pulmonary fibrosis via anti-oxidative stress and anti-inflammation pathways

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Evaluation of quantitative probes for weaker Cu(i) binding sites completes a set of four capable of detecting Cu(i) affinities from nanomolar to attomolar

Xiao, Z., Gottschlich, L., van der Meulen, R., Udagedara, S. R., & Wedd, A. G. (2013) · Metallomics · doi:10.1039/c3mt00032j · Cited by 77 · see citing works

Intelligent poly(l-histidine)-based nanovehicles for controlled drug delivery

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Copper and Heme-Mediated Abeta Toxicity: Redox Chemistry, Abeta Oxidations and Anti-ROS Compounds

Chassaing, S., Collin, F., Dorlet, P., Gout, J., Hureau, C., & Faller, P. (2013) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026611212220011 · Cited by 73 · see citing works

An integrated study of the affinities of the Aβ16 peptide for Cu( i ) and Cu( ii ): implications for the catalytic production of reactive oxygen species

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New generation of cell‐penetrating peptides: Functionality and potential clinical application

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Zn impacts Cu coordination to amyloid-β, the Alzheimer's peptide, but not the ROS production and the associated cell toxicity

Aliès, B., Sasaki, I., Proux, O., Sayen, S., Guillon, E., Faller, P., & Hureau, C. (2013) · Chemical Communications · doi:10.1039/c2cc38236a · Cited by 68 · see citing works

Copper-mediated β-amyloid toxicity and its chelation therapy in Alzheimer's disease

Singh, S. K., Balendra, V., Obaid, A. A., Esposto, J., Tikhonova, M. A., Gautam, N. K., & Pöeggeler, B. (2022) · Metallomics · doi:10.1093/mtomcs/mfac018 · Cited by 68 · see citing works

Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine

Maiti, B. K., Govil, N., Kundu, T., & Moura, J. J. G. (2020) · iScience · doi:10.1016/j.isci.2020.101792 · Cited by 62 · see citing works

Key Intermediate Species Reveal the Copper(II)‐Exchange Pathway in Biorelevant ATCUN/NTS Complexes

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Recent advances in proteolytic stability for peptide, protein, and antibody drug discovery

Lai, X., Tang, J. X., & ElSayed, M. E. H. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1942837 · Cited by 58 · see citing works

GHK-Cu-liposomes accelerate scald wound healing in mice by promoting cell proliferation and angiogenesis

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

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Emerging drug targets for A β and tau in Alzheimer's disease: a systematic review

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

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Lights and Shadows on the Therapeutic Use of Antimicrobial Peptides

Bellotti, D., & Remelli, M. (2022) · Molecules · doi:10.3390/molecules27144584 · Cited by 50 · see citing works

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

Hu, X., Zhang, Q., Wang, W., Yuan, Z., Zhu, X., Chen, B., & Chen, X.-Y. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00145 · Cited by 49 · see citing works

Cu II Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes?

Borghesani, V., Aliès, B., & Hureau, C. (2017) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201700776 · Cited by 49 · see citing works

Mechanistic Insights for Drug Repurposing and the Design of Hybrid Drugs for Alzheimer’s Disease

Padhi, D., & Govindaraju, T. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00335 · Cited by 47 · 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

Designing metallodrugs with nuclease and protease activity

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Impact of N‐Truncated Aβ Peptides on Cu‐ and Cu(Aβ)‐Generated ROS: Cu^I Matters!

Esmieu, C., Ferrand, G., Borghesani, V., & Hureau, C. (2021) · Chemistry – A European Journal · doi:10.1002/chem.202003949 · Cited by 43 · see citing works

The role of metals in modulating metalloprotease activity in the AD brain

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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

Inhibition of Cu‐Amyloid‐β by using Bifunctional Peptides with β‐Sheet Breaker and Chelator Moieties

Jensen, M., Canning, A., Chiha, S., Bouquerel, P., Pedersen, J. T., Østergaard, J., Cuvillier, O., Sasaki, I., Hureau, C., & Faller, P. (2012) · Chemistry - A European Journal · doi:10.1002/chem.201103546 · Cited by 37 · see citing works

Structural Insight into Redox Dynamics of Copper Bound N-Truncated Amyloid-β Peptides from in Situ X-ray Absorption Spectroscopy

Streltsov, V. A., Ekanayake, R. S. K., Drew, S. C., Chantler, C. T., & Best, S. P. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b01255 · Cited by 34 · see citing works

Structural analysis of copper(I) interaction with amyloid β peptide

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Oligopeptides Generated by Neprilysin Degradation of β-Amyloid Have the Highest Cu(II) Affinity in the Whole Aβ Family

Bossak‐Ahmad, K., Mital, M., Płonka, D., Drew, S. C., & Bal, W. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b03051 · Cited by 32 · see citing works

Cu(II) Binding to the Peptide Ala-His-His, a Chimera of the Canonical Cu(II)-Binding Motifs Xxx-His and Xxx-Zzz-His

Gonzalez, P., Vileno, B., Bossak‐Ahmad, K., Khoury, Y. E., Hellwig, P., Bal, W., Hureau, C., & Faller, P. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01996 · Cited by 31 · see citing works

Low catalytic activity of the Cu( ii )-binding motif (Xxx-Zzz-His; ATCUN) in reactive oxygen species production and inhibition by the Cu( i )-chelator BCS

Santoro, A., Walke, G. R., Vileno, B., Kulkarni, P. P., Raibaut, L., & Faller, P. (2018) · Chemical Communications · doi:10.1039/c8cc06040a · Cited by 31 · see citing works

Histidine‐Rich Oligopeptides To Lessen Copper‐Mediated Amyloid‐β Toxicity

Caballero, A. B., Terol‐Ordaz, L., Espargaró, A., Vázquez, G., Nicolás, E., Sabaté, R., & Gámez, P. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201600286 · Cited by 30 · 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

Aβ5– x Peptides: N-Terminal Truncation Yields Tunable Cu(II) Complexes

Wezynfeld, N. E., Tobolska, A., Mital, M., Wawrzyniak, U. E., Wiloch, M. Z., Płonka, D., Bossak‐Ahmad, K., Wróblewski, W., & Bal, W. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c01773 · Cited by 26 · see citing works

Ternary Cu(II) Complex with GHK Peptide and Cis-Urocanic Acid as a Potential Physiologically Functional Copper Chelate

Bossak-Ahmad, K., Wiśniewska, M. D., Bal, W., Drew, S. C., & Frączyk, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176190 · Cited by 25 · see citing works

RTHLVFFARK-NH2: A potent and selective modulator on Cu2+-mediated amyloid-β protein aggregation and cytotoxicity

Meng, J., Zhang, H., Dong, X., Liu, F., & Sun, Y. P. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.01.012 · Cited by 25 · see citing works

Kinetics Are Crucial When Targeting Copper Ions to Fight Alzheimer's Disease: An Illustration with Azamacrocyclic Ligands

Conte‐Daban, A., Beyler, M., Tripier, R., & Hureau, C. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201801520 · Cited by 25 · see citing works

N-terminally truncated Aβ4-x proteoforms and their relevance for Alzheimer’s pathophysiology

Rostagno, A. A., Cabrera, E., Lashley, T., & Ghiso, J. A. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00303-3 · Cited by 23 · see citing works

Using N-Terminal Coordination of Cu(II) and Ni(II) to Isolate the Coordination Environment of Cu(I) and Cu(II) Bound to His13 and His14 in Amyloid-β(4–16)

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N-Terminally Truncated and Pyroglutamate-Modified Aβ Forms Are Measurable in Human Cerebrospinal Fluid and Are Potential Markers of Disease Progression in Alzheimer’s Disease

Domingo, G., Benussi, L., Saraceno, C., Bertuzzi, M., Nicsanu, R., Longobardi, A., Bellini, S., Cagnotto, A., Salmona, M., Binetti, G. G., et al. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.708119 · Cited by 21 · see citing works

Triggering Cu-coordination change in Cu( <scp>ii</scp> )-Ala-His-His by external ligands

Gonzalez, P., Bossak-Ahmad, K., Vileno, B., Wezynfeld, N. E., El Khoury, Y., Hellwig, P., Hureau, C., Bal, W., & Faller, P. (2019) · Chemical Communications · doi:10.1039/c9cc03174j · Cited by 21 · see citing works

Peptidomimetics – An infinite reservoir of metal binding motifs in metabolically stable and biologically active molecules

Wątły, J., Miller, A., Kozłowski, H., & Rowińska‐Żyrek, M. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111386 · Cited by 18 · see citing works

Hierarchical binding of copperII to N-truncated Aβ4–16 peptide

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Measurement of Interpeptidic Cu(II) Exchange Rate Constants by Static Fluorescence Quenching of Tryptophan

Beuning, C. N., Mestre-Voegtlé, B., Faller, P., Hureau, C., & Crans, D. C. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b00182 · Cited by 16 · see citing works

Kinetics of Cu( ii ) complexation by ATCUN/NTS and related peptides: a gold mine of novel ideas for copper biology

Kotuniak, R., & Bal, W. (2021) · Dalton Transactions · doi:10.1039/d1dt02878b · Cited by 16 · see citing works

Copper( ii ) complex of N-truncated amyloid-β peptide bearing a His-2 motif as a potential receptor for phosphate anions

Tobolska, A., Wezynfeld, N. E., Wawrzyniak, U. E., Bal, W., & Wróblewski, W. (2021) · Dalton Transactions · doi:10.1039/d0dt03898a · Cited by 13 · see citing works

Nano-Inspired Technologies for Peptide Delivery

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Recent Progress in the Drug Development for the Treatment of Alzheimer’s Disease Especially on Inhibition of Amyloid-peptide Aggregation

Liu, Y., Cong, L., Han, C., Li, B., & Dai, R. (2020) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557520666201127104539 · Cited by 10 · see citing works

Measurement of Interpeptidic CuII Exchange Rate Constants of CuII-Amyloid-β Complexes to Small Peptide Motifs by Tryptophan Fluorescence Quenching

Beuning, C. N., Zocchi, L. J., Malikidogo, K. P., Esmieu, C., Dorlet, P., Crans, D. C., & Hureau, C. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c03555 · Cited by 9 · see citing works

Corrigendum: Kinetics Are Crucial When Targeting Copper Ions to Fight Alzheimer's Disease: An Illustration with Azamacrocyclic Ligands

Conte‐Daban, A., Beyler, M., Tripier, R., & Hureau, C. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201803841 · Cited by 5 · see citing works

Interacting Models of Amyloid-β and Tau Proteins: An Approach to Identify Drug Targets in Alzheimer’s Disease

Khadgawat, P., Siddesha, J. M., Shashank, D., & Shashanka, K. P. (2021) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-210018 · Cited by 4 · see citing works

Neglected N-Truncated Amyloid-β Peptide and Its Mixed Cu–Zn Complexes

Frączyk, T., & Cieplak, P. (2022) · The Protein Journal · doi:10.1007/s10930-022-10056-7 · Cited by 2 · see citing works

Peptide-based amyloid-beta aggregation inhibitors

Sehra, N., Parmar, R., & Jain, R. (2024) · RSC Medicinal Chemistry · doi:10.1039/d4md00729h · Cited by 27 · see citing works

The Effects of Andrographis paniculata (Burm.F.) Wall. Ex Nees and Andrographolide on Neuroinflammation in the Treatment of Neurodegenerative Diseases

Bosco, F., Ruga, S., Citraro, R., Leo, A., Guarnieri, L., Maiuolo, J., Oppedisano, F., Macrì, R., Scarano, F., Nucera, S., et al. (2023) · Nutrients · doi:10.3390/nu15153428 · Cited by 23 · see citing works

Sequence–Activity Relationship of ATCUN Peptides in the Context of Alzheimer’s Disease

Lefèvre, M., Malikidogo, K. P., Esmieu, C., & Hureau, C. (2022) · Molecules · doi:10.3390/molecules27227903 · Cited by 16 · see citing works

Fluorescent Peptides Sequester Redox Copper to Mitigate Oxidative Stress, Amyloid Toxicity, and Neuroinflammation

Mandal, S., Suseela, Y. V., Samanta, S., Vileno, B., Faller, P., & Govindaraju, T. (2024) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.4c00283 · Cited by 15 · see citing works

Efficacy and Safety of Natural Apigenin Treatment for Alzheimer's Disease: Focus on In vivo Research Advancements

Zhang, N., Nao, J., & Dong, X. (2024) · Current Neuropharmacology · doi:10.2174/1570159x23666241211095018 · Cited by 11 · see citing works

The effect of histidine, histamine, and imidazole on electrochemical properties of Cu( ii ) complexes of Aβ peptides containing His-2 and His-3 motifs

Tobolska, A., Jabłońska, A., Suwińska, A., Wawrzyniak, U. E., Wróblewski, W., & Wezynfeld, N. E. (2024) · Dalton Transactions · doi:10.1039/d4dt01354a · Cited by 9 · see citing works

Oxidative Activity of Copper Ions in Ternary Systems With N‐Truncated Amyloid Beta Peptides and Low Molecular Weight Substances

Sudzik, D., Bal, W., & Wezynfeld, N. E. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70145 · Cited by 4 · see citing works

Reduced Schiff-base derivatives to stop reactive oxygen species production by the Cu(A β ) species: a structure–activity relationship

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Semax, a Copper Chelator Peptide, Decreases the Cu(II)-Catalyzed ROS Production and Cytotoxicity of Aβ by Metal Ion Stripping and Redox Silencing

Tomasello, M. F., Di Rosa, M. C., Naletova, I., Sciacca, M. F. M., Giuffrida, A., Maccarrone, G., & Attanasio, F. (2025) · Bioinorganic Chemistry and Applications · doi:10.1155/bca/4226220 · Cited by 3 · see citing works

A Cocktail of Two Chelators Is Not Better than One Ligand in Excess to Halt Cu,Zn-(Amyloid-β)-Induced ROS Production in the Context of Alzheimer’s Disease

Bagrel, M., Hureau, C., & Falcone, E. (2025) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.5c03352 · Cited by 1 · see citing works

Optimizing the amino terminal Cu( ii )- and Ni( ii )-binding (ATCUN) motif for Cu( ii ) complexes with improved inertness

Djemili, R., Naudin, E. A., Wang, A., Ouadi, A., Gonzalez, P., Raibaut, L., Faller, P., & Lebrun, V. (2026) · Chemical Communications · doi:10.1039/d5cc05119c · Cited by 1 · see citing works

Cu(I) Is a Game Changer in the Arrest of Cu(Aβ)‐Induced ROS Production in the Presence of Competing Zn(II) Ions

Drommi, M., Malikidogo, K. P., Atrián‐Blasco, E., Esmieu, C., & Hureau, C. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202502352

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Климов, Н. А., Орлов, Д. С., Гришина, Т. В., Леонова, Л. Е., & Валерьевна, Ш. О. (2026) · Успехи геронтологии · doi:10.34922/ae.2026.39.4.002

Unexpected Trends in Copper Removal from Aβ Peptide: When Less Ligand Is Better and Zn Helps

Esmieu, C., Balderrama-Martínez-Sotomayor, R., Conte‐Daban, A., Iranzo, O., & Hureau, C. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c03407 · Cited by 14 · 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

Histidine‐Rich Oligopeptides To Lessen Copper‐Mediated Amyloid‐β Toxicity

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Hybrid Bis-Histidine Phenanthroline-Based Ligands to Lessen Aβ-Bound Cu ROS Production: An Illustration of Cu(I) Significance

Drommi, M., Rulmont, C., Esmieu, C., & Hureau, C. (2021) · Molecules · doi:10.3390/molecules26247630 · Cited by 10 · 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