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Recent Development of Bifunctional Small Molecules to Study Metal‐Amyloid‐β Species in Alzheimer′s Disease

Braymer, J. J., DeToma, A. S., Choi, J.-S., Ko, K. S., & Lim, M. H. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/623051 · Cited by 50

Interference of a new cyclometallated Pt compound with Cu binding to amyloid-β peptide

Sasaki, I., Bijani, C., Mallet‐Ladeira, S., Bourdon, V., Faller, P., & Hureau, C. (2012) · Dalton Transactions · doi:10.1039/c2dt12177h · Cited by 50

Two Functions, One Molecule: A Metal‐Binding and a Targeting Moiety to Combat Alzheimer's Disease

Hureau, C., Sasaki, I., Gras, E., & Faller, P. (2010) · ChemBioChem · doi:10.1002/cbic.201000102 · Cited by 49

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 50

Acetylcholinesterase and Aβ Aggregation Inhibition by Heterometallic Ruthenium(II)–Platinum(II) Polypyridyl Complexes

Vyas, N. A., Singh, S. B., Kumbhar, A. S., Ranade, D. S., Walke, G. R., Kulkarni, P. P., Jani, V., Sonavane, U., Joshi, R., & Rapole, S. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b00091 · Cited by 49

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

Microglia and Astrocytes in Alzheimer’s Disease in the Context of the Aberrant Copper Homeostasis Hypothesis

Pal, A., Rani, I., Pawar, A. T., Picozza, M., Rongioletti, M. C. A., & Squitti, R. (2021) · Biomolecules · doi:10.3390/biom11111598 · Cited by 48

34 GHz Pulsed ENDOR Characterization of the Copper Coordination of an Amyloid β Peptide Relevant to Alzheimer’s Disease

Kim, D., Kim, N. H., & Kim, S. H. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201208108 · Cited by 46

Biocompatible CuO-decorated carbon nanoplatforms for multiplexed imaging and enhanced antitumor efficacy via combined photothermal therapy/chemodynamic therapy/chemotherapy

Jiang, F., Ding, B., Zhao, Y., Liang, S., Cheng, Z., Xing, B., Teng, B., Ma, P., & Lin, J. (2020) · Science China Materials · doi:10.1007/s40843-019-1397-0 · Cited by 46

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 46

A Water‐Soluble Peptoid Chelator that Can Remove Cu2+ from Amyloid‐β Peptides and Stop the Formation of Reactive Oxygen Species Associated with Alzheimer's Disease

Behar, A. E., Sabater, L., Baskin, M., Hureau, C., & Maayan, G. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202109758 · Cited by 45

Electrically pulsatile responsive drug delivery platform for treatment of Alzheimer’s disease

Wu, L. J., Wang, J., Gao, N., Ren, J., Zhao, A., & Qu, X. (2015) · Nano Research · doi:10.1007/s12274-015-0750-x · Cited by 43

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

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

Oxysterols in biological systems: The gastrointestinal tract, liver, vascular wall and central nervous system

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Identification of key structural features of the elusive Cu–Aβ complex that generates ROS in Alzheimer’s disease

Cheignon, C., Jones, M., Atrián-Blasco, E., Kieffer, I., Faller, P., Collin, F., & Hureau, C. (2017) · Chemical Science · doi:10.1039/c7sc00809k · Cited by 132

Copper reduction and dioxygen activation in Cu–amyloid beta peptide complexes: insight from molecular modelling

Arrigoni, F., Prosdocimi, T., Mollica, L., GIOIA, L. D., Zampella, G., & Bertini, L. (2018) · Metallomics · doi:10.1039/c8mt00216a · Cited by 43

Phospholipids and amyloid-β compete for copper-induced reactive oxygen species production in the context of Alzheimer's disease

Cerlati, O., Putaux, J., Marty, J., Mingotaud, A., Vicendo, P., Pimienta, V., & Collin, F. (2026) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2026.141831

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

Interactions of copper and copper chelate compounds with the amyloid beta peptide: An investigation into electrochemistry, reactive oxygen species and peptide aggregation

Crnich, E., Lullo, R., Tabaka, A. L., Havens, M. A., & Kissel, D. S. (2021) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2021.111493 · Cited by 14