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Identification of a prosurvival neuroprotective mitochondrial peptide in a mammalian hibernator

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Copper(II) and nickel(II) binding sites of peptide containing adjacent histidyl residues

Grenács, Á., Sanna, D., & Sóvágó, I. (2015) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2015.06.020 · Cited by 13

Multi‐Frequency, Multi‐Technique Pulsed EPR Investigation of the Copper Binding Site of Murine Amyloid β Peptide

Kim, D., Bang, J. K., & Kim, S. H. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201410389 · Cited by 12

Stability of transient Cu+Aβ (1–16) species and influence of coordination and peptide configuration on superoxide formation

Mirats, A., Alí‐Torres, J., Rodrı́guez-Santiago, L., & Sodupe, M. (2016) · Theoretical Chemistry Accounts · doi:10.1007/s00214-016-1836-6 · Cited by 12

A new triazine bearing a pyrazolone group capable of copper, nickel, and zinc chelation

Yepremyan, A., Mehmood, A., Brewer, S. M., Barnett, M. M., Janesko, B. G., Akkaraju, G. R., Simanek, E. E., & Green, K. N. (2018) · RSC Advances · doi:10.1039/c7ra09459k · Cited by 12

Potent therapeutic targets for treatment of Alzheimer's disease: Amyloid degrading enzymes

Choi, H. S., Kim, E., Choi, J. Y., Park, E., & Lee, H. J. (2021) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.12390 · Cited by 11

Mn 2+ -induced structural flexibility enhances the entire catalytic cycle and the cleavage of mismatches in prokaryotic argonaute proteins

Zheng, L., Zhou, B., Yang, Y., Zan, B., Zhong, B., Wu, B., Feng, Y., Liu, Q., & Hong, L. (2024) · Chemical Science · doi:10.1039/d3sc06221j · Cited by 11

Power of Dopamine: Multifunctional Compound Assisted Conversion of the Most Risk Factor into Therapeutics of Alzheimer’s Disease

Gharai, P. K., Khan, J., Pradhan, K., Mallesh, R., Garg, S., Arshi, M. U., Barman, S., & Ghosh, S. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00777 · Cited by 11

Cu2+-selective Sensors Based on a New Ion-Carrier and Their Application for the Analysis of Copper Content of Water Samples

Faridbod, F., Davarkhah, N., Beikzadeh, M., Yekefallah, M., & Rezapour, M. (2017) · International Journal of Electrochemical Science · doi:10.20964/2017.02.11 · Cited by 11

Molecular interactions of resveratrol with Aβ 42 peptide and fibril during in-vitro Aβ 42 aggregation

Sharma, S., Goyal, H., Joshi, S., Nehru, B., & Saini, A. (2023) · Advances in Redox Research · doi:10.1016/j.arres.2023.100060 · Cited by 11

Copper(II) complexes with Fusobacterium nucleatum adhesin FadA: Coordination pattern, physicochemical properties and reactivity

Krupa, K., Lesiów, M. K., Stokowa‐Sołtys, K., Starosta, R., Ptaszyńska, N., Łęgowska, A., Rolka, K., Wernecki, M., Cal, M., & Jeżowska‐Bojczuk, M. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.09.012 · Cited by 12

Simultaneous binding of heme and Cu with amyloid β peptides: active site and reactivities

Nath, A. K., & Dey, S. G. (2022) · Dalton Transactions · doi:10.1039/d2dt00162d · Cited by 11

A cocktail of Cu 2+ - and Zn 2+ -peptoid-based chelators can stop ROS formation for Alzheimer's disease therapy

Behar, A. E., & Maayan, G. (2024) · Chemical Science · doi:10.1039/d4sc04313h · Cited by 10

Amyloid scaffolds as alternative chlorosomes

Rengifo, R. F., Li, N. X., Sementilli, A., & Lynn, D. G. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob01170a · Cited by 10

Advanced Electron Paramagnetic Resonance Studies of a Ternary Complex of Copper, Amyloid-β, and a Chemical Regulator

Hong, S., Go, Y. K., Derrick, J. S., Han, S., Kim, J., Lim, M. H., & Kim, S. H. (2018) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.8b01824 · Cited by 10

Evaluation of the irritating influence of carane derivatives and their antioxidant properties in a deoxyribose degradation test

Moniczewski, A., Librowski, T., Lochyński, S., & Strub, D. J. (2011) · Pharmacological Reports · doi:10.1016/s1734-1140(11)70406-6 · Cited by 10

Adsorption and desorption studies of Delonix regia pods and leaves: removal and recovery of Ni(II) and Cu(II) ions from aqueous solution

Babalola, B. M., Babalola, A. O., Akintayo, C. O., Lawal, O. S., Abimbade, S. F., Oseghe, E. O., Akinola, L. S., & Ayanda, O. S. (2020) · Drinking water engineering and science · doi:10.5194/dwes-13-15-2020 · Cited by 10

Solving the Amyloid Paradox: Unveiling the Complex Pathogenicity of Amyloid Fibrils

Sulatsky, M. I., Stepanenko, O. V., Stepanenko, O. V., & Sulatskaya, A. I. (2025) · Aggregate · doi:10.1002/agt2.70078 · Cited by 9

N,N′-1,10-Bis(Naringin) Triethylenetetraamine, Synthesis and as a Cu(II) Chelator for Alzheimer’s Disease Therapy

Guo, L., & Sun, B. (2020) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b20-00574 · Cited by 9

Determination of nanomolar levels of reactive oxygen species in microorganisms and aquatic environments using a single nanoparticle-based optical sensor

Kim, Y., Kim, Y., Choi, J., Kang, T., & Choi, I. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.03.012 · Cited by 9

Repurposing melatonin's therapeutic potential in Wilson disease: Addressing copper overload and redox imbalance

Pandey, R., Roy, A. N., Sarkar, S., Rohman, R., Chakraborty, K., Bargakshatriya, R., Pandey, S., Pruthwiraj, Bhattacharya, D., Kumar, S., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103971 · Cited by 8

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