The DOI matches its Crossref record; 133 of the 134 references it cites were found in a registry or an index.
Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide
Abstract
In the present perspective, we give a critical review on the coordination chemistry of the metal ions copper and zinc to the amyloid-beta (Abeta) peptide; such complexes have been linked to Alzheimer's disease. We focus on two main issues: the identification of the coordination sphere of the Cu(ii) and Zn(ii) ions and the affinity of these metal ions towards the peptide. With the aim to come up with as few as possible valuable structural models and binding affinity values, we critically review the divergent propositions reported in the literature and take into account the experimental differences and the limits of the methods used in the published studies. We propose that: (i) the conditional dissociation constant of the Cu(Abeta) complexes lies in the range of 10 pM to 100 nM, with a preference for the region between 100 pM to 1 nM. (ii) Two most likely coordination modes for the predominant form of the Cu(Abeta) complexes at physiological pH can be retained, both being 3N1O distorted square planar. In the first model, the Cu(ii) ion is coordinated by the Ntau atoms of the three His residues and the carboxylate of the Asp1. In the second model, both the N-terminus and the carboxylate functions of Asp1 are ligated together with the Ntau of His6 and of His13 (or His14). An equilibrium between these two forms at room temperature, and a preferentially freezing out of the second one would explain most of the divergences in the published results (in particular, between those obtai…
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Post-mortem examination of the brain suggested that bio-available metals (i.e., copper, zinc, and iron) are found in high concentration in the amyloid plaques.”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [13]
In the citing paper
“as well as lead to formation of reactive oxygen species (ROS) and oxidative stress.3,26–31,33–36”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [26]
In the citing paper
“Thus, these metal ions have been shown to promote Aβ40 aggregation,23–27,29–32”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [26]
In the citing paper
“These pM values represent approximate dissociation constants and compare favorably with the Kd values reported for Cu-Aβ (nM-μM) and Zn-Aβ (μM).26,29,31,57,76,79,80”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [26]
In the citing paper
“This is in contrast with a large number of reports showing the aggregation-promoting effect of metal ions on the Aβ peptide.23–27,29–32,37,38”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [26]
Citations
Cites
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Protein Misfolding, Functional Amyloid, and Human Disease
Chiti, F., & Dobson, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.123901 · Cited by 6,497
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Alzheimer's Disease Is a Synaptic Failure
Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420
Flagged first, then by citations
1 of the 134 references couldn’t be matched to a known paper.
Research works printed but not linked: 3
- Multhaup, 1999, Met. Ions Biol. Syst., 36, 365
- Sayre, 2005, Ann Ist Super Sanita, 41, 143
- Krezel, 2008, J. Biol. Chem., 13, 401
Cited by
Sorted by citations
Items 401–500 of 537
Natale, G. D., Sinopoli, A., Grenács, Á., Sanna, D., Sóvágó, I., & Pappalardo, G. (2016) · New Journal of Chemistry · doi:10.1039/c6nj02354a · Cited by 8
Interactions of pyridinecarboxylic acid chelators with brain metal ions: Cu(II), Zn(II), and Al(III)
Sija, É., Dean, A., Jakusch, T., Marco, V. D., Venzo, A., & Kiss, T. (2011) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/s00706-011-0482-x · Cited by 8
A zinc complex of heparan sulfate destabilises lysozyme and alters its conformation
Hughes, A. J., Hussain, R., Cosentino, C., Guerrini, M., Siligardi, G., Yates, E. A., & Rudd, T. R. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.154 · Cited by 8
Wang, C., Wang, K., & Wang, Z. (2014) · Analytica Chimica Acta · doi:10.1016/j.aca.2014.12.006 · Cited by 8
Benn, M. H., Rauk, A., & SWADDLE, T. W. (2011) · Canadian Journal of Chemistry · doi:10.1139/v11-101 · 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
Despotović, I. (2015) · New Journal of Chemistry · doi:10.1039/c5nj00459d · Cited by 8
Ligand Design to Target and Modulate Metal–Protein Interactions in Neurodegenerative Diseases
Beck, M. W., Pithadia, A. S., DeToma, A. S., Korshavn, K. J., & Lim, M. H. (2014) · Wiley eBooks · doi:10.1002/9781118697191.ch10 · Cited by 8
Dias, I., van Bon, L., Banaś, A., Chavarria, D., Borges, F., Guerreiro-Oliveira, C., Cardoso, S. M., Sanna, D., Garribba, E., Chaves, S., et al. (2024) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2024.112734 · Cited by 7
Juarez-Romero, G. U., Sun, X., Gerez, J., Auwer, C. D., Landrot, G., Nachtegaal, M., Riek, R., Luo, J., & Quintanar, L. (2026) · Chemical Science · doi:10.1039/d5sc08604c · Cited by 7
Chen, W., Wang, Y., Wang, H., An, D., Sun, D., Li, P., Zhang, T., Lu, W., & Liu, Y. (2021) · Molecular Brain · doi:10.1186/s13041-021-00837-z · Cited by 7
Superoxide Reduction by Cu‐Amyloid Beta Peptide Complexes: A Density Functional Theory Study
Arrigoni, F., Carlo, C. D., Rovetta, A., GIOIA, L. D., Zampella, G., & Bertini, L. (2022) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202200245 · Cited by 7
Cavaleri, F. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1550709 · Cited by 7
Azimi, S., & Rauk, A. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400364b · Cited by 7
Banerjee, R. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-815461-8.00019-0 · Cited by 7
Oliveri, V., & Vecchio, G. (2021) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202100079 · Cited by 7
Bin, Y., Jiang, Z., & Xiang, J. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1512-7 · Cited by 7
Copper induced spin state change of heme–Aβ associated with Alzheimer's disease
Mukherjee, S., Ghosh, C., Seal, M., & Dey, S. G. (2017) · Dalton Transactions · doi:10.1039/c7dt01700f · Cited by 7
Impact of Cu( ii ) and Al( iii ) on the conformational landscape of amyloidβ 1-42
Roldán-Martín, L., Peccati, F., Sciortino, G., Sodupe, M., & Maréchal, J. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp01561c · Cited by 7
Kennedy, R. H., Wiqas, A., & Curley, J. P. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.04.037 · Cited by 7
Magrì, A. L., Natale, G. D., & Rizzarelli, E. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.10.032 · Cited by 7
Histidine-Lacked Aβ(1–16) Peptides: pH-Dependent Conformational Changes in Metal Ion Binding
Habasescu, L., Jureschi, M., Petre, B. A., Mihai, M., Grădinaru, V. R., Murariu, M., & Drochioiu, G. (2020) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-020-10048-0 · Cited by 7
Rational Design of Copper and Iron Chelators to Treat Wilson's Disease and Hemochromatosis
Gateau, C., Mintz, E., & Delangle, P. (2014) · Wiley eBooks · doi:10.1002/9781118697191.ch11 · Cited by 7
Ekanayake, R. S. K., Streltsov, V. A., Best, S. P., & Chantler, C. T. (2024) · IUCrJ · doi:10.1107/s2052252524001830 · Cited by 6
Smart, A., Singewald, K., Hasanbasri, Z., Britt, R. D., & Millhauser, G. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108311 · Cited by 6
Dicarboxylated ethynylarenes as buffer-dependent chemosensors for Cd(II), Pb(II), and Zn(II)
FLETCHER, J. T., Bruck, B. S., & Deever, D. E. (2013) · Tetrahedron Letters · doi:10.1016/j.tetlet.2013.07.111 · Cited by 6
Duroux, C., & Hagège, A. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03769-8 · Cited by 6
Rational Design of a Cu Chelator That Mitigates Cu‐Induced ROS Production by Amyloid Beta
Mitra, S., Talukdar, K., Prasad, P., Misra, S. K., Khan, S. I., Sharp, J. S., Jurss, J. W., & Chakraborty, S. (2021) · ChemBioChem · doi:10.1002/cbic.202100485 · Cited by 6
A phosphorylated zinc finger peptide bearing a gadolinium complex for zinc detection by MRI
Malikidogo, K. P., Pallier, A., Szeremeta, F., Bonnet, C. S., & Sénèque, O. (2023) · Dalton Transactions · doi:10.1039/d3dt00728f · Cited by 6
Segal‐Gavish, H., Danino, O., Barhum, Y., Ben‐Zur, T., Shai, E., Varon, D., Offen, D., & Fischer, B. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161236 · Cited by 6
Makowska, J., Wyrzykowski, D., Pilarski, B., Neubauer, D., Kamysz, E., Tesmar, A., & Chmurzyński, L. (2018) · The Journal of Chemical Thermodynamics · doi:10.1016/j.jct.2018.08.040 · Cited by 6
Cu2+ Effects on Beta‐Amyloid Oligomerisation Monitored by the Fluorescence of Intrinsic Tyrosine
Alghamdi, A., Wellbrock, T., Birch, D. J. S., Vyshemirsky, V., & Rolinski, O. J. (2019) · ChemPhysChem · doi:10.1002/cphc.201900565 · Cited by 6
Novel strategies for the fight of Alzheimer’s disease targeting amyloid-β protein
Xie, Y., Wang, Y., Jiang, S., Xiang, X., Wang, J., & Ning, L. (2021) · Journal of drug targeting · doi:10.1080/1061186x.2021.1973482 · Cited by 6
Nelson, J. (2010) · Annual Reports Section A (Inorganic Chemistry) · doi:10.1039/b918386h · Cited by 6
Kurronen, A., Pihlaja, R., Pollari, E., Kanninen, K. M., Storvik, M., Wong, G., Koistinaho, M., & Koıstınaho, J. (2012) · World Journal of Neuroscience · doi:10.4236/wjns.2012.22009 · Cited by 6
Atomistic molecular simulations of Aβ‐Zn conformational ensembles
Aduriz‐Arrizabalaga, J., López, X., & Sancho, D. D. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26590 · Cited by 5
Redox reactivities of membrane-bound amyloid-β-Cu complexes and their targeting by metallothionein-3
Perez-Medina, L., & Meloni, G. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.08.047 · Cited by 5
Asadbegi, M., & Shamloo, A. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01264 · Cited by 5
Wegermann, C. A., Pirota, V., Monzani, E., Casella, L., Costa, L. A. S., Novato, W. T. G., Machini, M. T., & Ferreira, A. M. D. C. (2023) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2023.112227 · Cited by 5
Daniele, F., Marasco, D., & Manna, S. L. (2024) · Inorganica Chimica Acta · doi:10.1016/j.ica.2024.122474 · Cited by 5
Okamura, E., & Aki, K. (2020) · Pure and Applied Chemistry · doi:10.1515/pac-2019-1201 · Cited by 5
Wiloch, M. Z., Baran, N., & Jönsson‐Niedziółka, M. (2022) · ChemElectroChem · doi:10.1002/celc.202200623 · Cited by 5
Penna, G. L., & Morante, S. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1546-1_14 · Cited by 5
Metal Ion Imbalance in the Body
Dabrowiak, J. C. (2017) · Wiley eBooks · doi:10.1002/9781119191377.ch8 · Cited by 5
Zn( ii )-driven impact of monomeric transthyretin on amyloid-β amyloidogenesis
Yi, Y., Kim, B., Kim, M., Ko, Y. H., Kim, J. H., & Lim, M. H. (2025) · Chemical Science · doi:10.1039/d4sc08771b · Cited by 4
A Copper-Selective Sensor and Its Inhibition of Copper-Amyloid Beta Aggregation
Nguyen, N. K., Poduska, B., Franks, M., Bera, M., MacCormack, I., Lin, G., Petroff, A. P., Das, S., & Nag, A. (2024) · Biosensors · doi:10.3390/bios14050247 · Cited by 4
Piano-stool metal complexes as inhibitors of amyloid-β aggregation in vitro and in vivo
Vigueras, G., Sabaté, R., Barrios, L. A., Caballero, A. B., Hernández‐García, S., Bayón, P., Gandía‐Herrero, F., Ruiz, J., & Gámez, P. (2024) · Inorganic Chemistry Frontiers · doi:10.1039/d4qi01460j · Cited by 4
The role of ligand covalency in the selective activation of metalloenediynes for Bergman cyclization
Porter, M. R., & Zaleski, J. M. (2015) · Polyhedron · doi:10.1016/j.poly.2015.10.041 · Cited by 4
Liu, L., & Xia, N. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.11.074 · Cited by 4
RetractedGogineni, D. P., Spuches, A. M., & Burns, C. (2014) · Inorganic Chemistry · doi:10.1021/ic502014x · Cited by 4
Holder, A. A. (2010) · Annual Reports Section A (Inorganic Chemistry) · doi:10.1039/b918408m · Cited by 4
Luo, Y., Xu, Y. X., Bao, Q., Ding, Z., Zhu, C.-Q., Huang, Z. X., & Tan, X. S. (2012) · Chinese Chemical Letters · doi:10.1016/j.cclet.2012.08.002 · Cited by 4
Pseudopeptide Designed to Inhibit Oligomerization and Redox Chemistry in Alzheimer’s Disease
Opare, S. K. A., & Rauk, A. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b01665 · Cited by 4
Shuster, S. O., Fica-Contreras, S. M., Hedges, J. S., Henning, N. J., & Choi, S. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.10.008 · Cited by 4
Behar, A. E., Sabater, L., Baskin, M., Hureau, C., & Maayan, G. (2021) · Angewandte Chemie · doi:10.1002/ange.202109758 · Cited by 4
Self-citationModelling Copper Binding to the Amyloid-ß Peptide in Alzheimer’s Disease
Epa, V. C., Streltsov, V. A., & Varghese, J. N. (2010) · Australian Journal of Chemistry · doi:10.1071/ch09454 · Cited by 4
Lung nodules after whole lung radiation.
Cohen, M. D., Mirkin, D. L., Provisor, A. J., Hornback, N. B., Smith, J. A., & Slabaugh, R. D. (1983) · PubMed · Cited by 4
Metal Ions and Complexes in A lzheimer's Disease: From Fundamental to Therapeutic Perspectives
Hureau, C. (2018) · Wiley eBooks · doi:10.1002/9781119951438.eibc2635 · Cited by 4
Self-citationWaly, O. M., El‐Sayed, S. M., Ghaly, M. A., & El‐Subbagh, H. I. (2025) · Archiv der Pharmazie · doi:10.1002/ardp.70025 · Cited by 3
Despotović, I. (2020) · Structural Chemistry · doi:10.1007/s11224-020-01542-8 · Cited by 3
Dipeptide interactions with Zn(II)–cyclen artificial model for molecular recognition
Rostášová, I., Vilková, M., Vargová, Z., Walko, M., Almáši, M., Imrich, J., Hermann, P., & Lukeš, I. (2015) · Journal of Molecular Recognition · doi:10.1002/jmr.2416 · Cited by 3
Protein interaction in the mechanism of platinum anticancer drugs
Zhao, L., Fang, T., Liu, Y., Cao, K., & Cheng, L. (2017) · Scientia Sinica Chimica · doi:10.1360/n032016-00167 · Cited by 3
Indeykina, M. I., Kononikhin, A. S., Popov, I. A., Kostyukevich, Y., Kulikova, A. A., Mitkevich, V. A., Kozin, S. A., Makarov, A. А., & Николаев, Е. Н. (2016) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2016.09.009 · Cited by 3
Sija, É., May, N. V., Gandin, V., Marzano, C., Jakusch, T., Dean, A., Marco, V. D., & Kiss, T. (2013) · Polyhedron · doi:10.1016/j.poly.2013.09.043 · Cited by 3
Copper Complexation by Peptides Implicated in Neurodegenerative Diseases
Dorlet, P., & Hureau, C. (2020) · Springer eBooks · doi:10.1007/978-3-030-39668-8_4 · Cited by 3
Self-citationBerntsson, E., Noormägi, A., Padari, K., Jarvet, J., Gräslund, A., Pooga, M., Palumaa, P., & Wärmländer, S. K. T. S. (2025) · ChemBioChem · doi:10.1002/cbic.202500252 · Cited by 2
Lu, W., Kang, S., Liu, S., Wang, Y., & Wang, H. (2026) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-026-00447-7 · Cited by 2
Condensate State as Determinant of Amyloid Pathology in Neurodegeneration
Lucas, L., Ferreon, J. C., & Ferreon, A. C. M. (2026) · Biomolecules · doi:10.3390/biom16040560 · Cited by 2
The aggregation of amyloid-β: from condensation, nucleation, and conformation to targeting therapy
Chen, B., Chen, T., Sun, Z., Liu, L., Jia, Y., Ji, Y., Wang, J., Sun, F., & Huang, Y. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124397 · Cited by 2
Simple In Vivo Models of Alzheimer’s Disease
Caito, S. W., & Newell-Caito, J. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00011-8 · Cited by 2
Martinez‐Finley, E. J., Chakraborty, S., Caito, S., Fretham, S. J. B., & Aschner, M. (2012) · PubMed · Cited by 3
Heme/Cu-oxygen intermediates of amyloid β peptides associated with Alzheimer's disease
Roy, M., & Dey, S. G. (2022) · Advances in inorganic chemistry · doi:10.1016/bs.adioch.2022.07.003 · Cited by 2
Zhao, Q., Zhang, J., Li, X., Tang, P., Yang, F., Ma, J., Hu, Z., Sun, H., Wang, X., Sun, Z., et al. (2025) · Physical Chemistry Chemical Physics · doi:10.1039/d5cp00807g · Cited by 2
Metal ions and beta amyloid: conformational modifications and biological aspects
Granzotto, A., & Zatta, P. F. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1001-0_7 · Cited by 2
Metals in Alzheimer’s Disease: A Combined Experimental and Numerical Approach
MORANTE, S., & Rossi, G. C. (2014) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781608058525114020006 · Cited by 2
The Amyloid _-Protein and Alzheimer's Disease
Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2
Zerweck, J., Venkata, B. S., Pittman, J. M., Srivastava, A. K., Moore, P. C., Sachleben, J. R., Thinakaran, G., & Meredith, S. C. (2019) · Protein Expression and Purification · doi:10.1016/j.pep.2019.04.006 · Cited by 2
Penta-glycine copper(II) complexes in slightly alkaline solutions
Gaisin, Z., Gellerman, G., & Meyerstein, D. (2016) · Inorganica Chimica Acta · doi:10.1016/j.ica.2016.05.055 · Cited by 2
Justo, R. M. S., Borba-Santos, L. P., Sade, Y. B., Ferreira, F. H. D. C., Rosa, N. M. P., Costa, L. A. S., Visbal, G., Rozental, S., & Navarro, M. (2021) · New Journal of Chemistry · doi:10.1039/d1nj03656d · Cited by 2
Candidate Environmental Factors for the Alzheimer’s Epidemic Part 1
Brewer, G. J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-811162-8.00004-4 · Cited by 1
Mohan, B., & Choudhary, M. (2021) · Asian Journal of Chemistry · doi:10.14233/ajchem.2021.23339 · Cited by 1
Bacchella, C., Novellini, S., Miotto, E., Nicolis, S., Monzani, E., & Dell’Acqua, S. (2025) · ChemPlusChem · doi:10.1002/cplu.202500304 · Cited by 1
Zimmeter, K., Vileno, B., Pallier, A., Platas‐Iglesias, C., Faller, P., Bonnet, C. S., & Sour, A. (2025) · Dalton Transactions · doi:10.1039/d5dt01735a · Cited by 1
Self-citationMathematical Modeling of Oxidative Stress in Alzheimer’s Disease: A Differential Equations Approach
Meteumba, L. G., & Yarahmadian, S. (2026) · Mathematics · doi:10.3390/math14081390 · Cited by 1
Mia, M., Dutta, A., Hossain, M. M., Adhikari, J., Rahman, M. M., & Shibly, A. Z. (2026) · Journal of Genetic Engineering and Biotechnology · doi:10.1016/j.jgeb.2026.100706 · Cited by 1
Soluble zinc-induced amyloid β oligomers probed through fluorine NMR spectroscopy
Russo, L., Chakrabarti, K. S., Backer, R., Overkamp, K., Gambarelli, S., Willbold, D., Sicoli, G., & Rezaei‐Ghaleh, N. (2026) · Communications Chemistry · doi:10.1038/s42004-026-02121-4 · Cited by 1
Zhang, Z., Sun, S. S., Xu, J., Zhang, J., Huang, Y., Zhang, B., & Tao, Y. (2013) · Journal of Physics Conference Series · doi:10.1088/1742-6596/430/1/012041 · Cited by 1
Hane, F. T., Drolle, E., & Leonenko, Z. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp00040d · Cited by 1
Aki, K., & Okamura, E. (2022) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2022.120050 · Cited by 1
Stokowa‐Sołtys, K., Kierpiec, K., Szczerba, K., & Wieczorek, R. (2023) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2023.112307 · Cited by 1
Só, Y. A. D. O., Silva, M. D. A., Kiametis, A. S., Sette, C. D. B., Pereira, M. L., Ribeiro, L. A., & Gargano, R. (2023) · Journal of Computational Biophysics and Chemistry · doi:10.1142/s2737416523500436 · Cited by 1
Modulation of Aβ 1–40 and Aβ 4–40 co-assembly by zinc: getting closer to the biological reality
de Cremoux, L., Falcone, E., Schmitt, D. A., Stefaniak, E., Wiśniewska, M., Vitale, N., Bal, W., & Hureau, C. (2025) · Inorganic Chemistry Frontiers · doi:10.1039/d5qi00850f · Cited by 2
Self-citationMatsunaga, Y., & Suenaga, M. (2012) · Journal of Amino Acids · doi:10.1155/2012/206520 · Cited by 1
Direct- And Spacer-Coupled Codrug Strategies for the Treatment of Alzheimer's Disease
Fornasari, E., Stefano, V. D., & Cacciatore, I. (2014) · Cited by 1
Ershov, P. V., Mezentsev, Y. V., Yablokov, E. O., Kaluzgskiy, L. A., Ivanov, A. S., Gnuchev, N. V., Mitkevich, V. A., Makarov, A. А., & Kozin, S. A. (2020) · Molecular Biology · doi:10.1134/s0026893320060035 · Cited by 1
Gade, S. (2012) · The Scholarship East Carolina University's Institutional Repository (East Carolina University) · Cited by 1
Single Molecule Force Spectroscopy Investigations of Amyloid-β Aggregation
Hane, F. T. (2013) · UWSpace (University of Waterloo) · Cited by 1
Silva, K. I. (2015) · D-Scholarship@Pitt (University of Pittsburgh)
Structural and Computational Studies of Interactions of Metals with Amyloid Beta
Chandana, V. (2012) · InTech eBooks · doi:10.5772/32786
Vanadium, Copper and Zinc in Medicine
Dabrowiak, J. C. (2009) · Wiley eBooks · doi:10.1002/9780470684986.ch7
Metadata
- Authors
- Faller, P., & Hureau, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Faller, Peter
- Venue
- Dalton Trans.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2009
- Issue
- 7
- Pages
- 1080-1094
- ISSN
- 1477-9226 (ISSN-L)
- 1477-9234
- OpenAlex
- W2062820102
- Cited by
- 530
- References
- 134
- Citations by year
- 2026: 12 · 2025: 19 · 2024: 17 · 2023: 20 · 2022: 14 · 2021: 25 · 2020: 23 · 2019: 29 · 2018: 34 · 2017: 37 · 2016: 25 · 2015: 28 · 2014: 36 · 2013: 40 · 2012: 58
- FWCI
- 4.03
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Dalton Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Metal complexes synthesis and properties
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- amyloid-beta, copper(II) complexes, zinc(II) complexes, metal-peptide coordination, Alzheimer's disease, coordination sphere, dissociation constant, binding affinity, square-planar coordination, histidine ligands, structural model
- MeSH terms
- Alzheimer Disease, Copper, Humans, Peptide Fragments, Zinc, Chemistry, Bioinorganic, Amyloid beta-Peptides
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review