Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

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

Amyloid β-peptide is produced by cultured cells during normal metabolism

Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921

Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids

Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731

Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus

Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522

Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing

Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447

The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene

Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367

Binding of human apolipoprotein E to synthetic amyloid beta peptide: isoform-specific effects and implications for late-onset Alzheimer disease.

Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363

Aggregation of Human Wild-Type and H27A-Prolactin in Cells and in Solution: Roles of Zn2+, Cu2+, and pH

Sankoorikal, B.-J., Zhu, Y. L., Hodsdon, M. E., Lolis, E., & Dannies, P. S. (2002) · Endocrinology · doi:10.1210/endo.143.4.8732 · Cited by 30

Role of monocarboxylate transporter 4 in Alzheimer disease

Hong, P., Zhang, X., Gao, S., & Wang, P. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.11.006 · Cited by 29

Drug-like chelating agents: a potential lead for Alzheimer's disease

Huang, W., Wei, W., & Shen, Z. (2014) · RSC Advances · doi:10.1039/c4ra09193k · Cited by 29

Effective screen for amyloid β aggregation inhibitor using amyloid β-conjugated gold nanoparticles

Mook‐Jung, I., Han, S.-H., Chang, Y. J., Jung, E. S., Kim, J., & Na, D. L. (2010) · International Journal of Nanomedicine · doi:10.2147/ijn.s15278 · Cited by 29

Reversible precipitation of bovine serum albumin by metal ions and synthesis, structure and reactivity of new tetrathiometallate chelating agents

Lee, V. E., Schulman, J. M., Stiefel, E. I., & Lee, C. C. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.07.015 · Cited by 29

New force field parameters for metalloproteins I: Divalent copper ion centers including three histidine residues and an oxygen‐ligated amino acid residue

Wise-Scira, O., & Coskuner‐Weber, O. (2014) · Journal of Computational Chemistry · doi:10.1002/jcc.23622 · Cited by 29

Effects of Intrinsic and Extrinsic Factors on Aggregation of Physiologically Important Intrinsically Disordered Proteins

Breydo, L., Redington, J., & Uversky, V. N. (2016) · International review of cytology · doi:10.1016/bs.ircmb.2016.08.011 · Cited by 29

Transition metal chelator therapy - a potential treatment for Alzheimer's disease?

Gnjec, A. (2002) · Frontiers in bioscience · doi:10.2741/gnjec · Cited by 29

Aggregation‐Prone Amyloid‐β⋅CuII Species Formed on the Millisecond Timescale under Mildly Acidic Conditions

Pedersen, J. T., Borg, C. B., Michaels, T. C. T., Knowles, T. P. J., Faller, P., Teilum, K., & Hemmingsen, L. (2015) · ChemBioChem · doi:10.1002/cbic.201500080 · Cited by 28

Antibodies to Potato Virus Y Bind the Amyloid β Peptide

Friedland, R. P., Tedesco, J. M., Wilson, A. C., Atwood, C., Smith, M. A., Perry, G. L., & Zagorski, M. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802088200 · Cited by 28

A Synthetic Peptide with the Putative Iron Binding Motif of Amyloid Precursor Protein (APP) Does Not Catalytically Oxidize Iron

Ebrahimi, K. H., Hagedoorn, P., & Hagen, W. R. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040287 · Cited by 28

Inorganic Stressors of Ubiquitin

Arena, G., Bellia, F., Frasca, G., Grasso, G., Lanza, V., Rizzarelli, E., Tabbı̀, G., Zito, V., & Milardi, D. (2013) · Inorganic Chemistry · doi:10.1021/ic401276x · Cited by 28

Ferulic Acid Activates SIRT1-Mediated Ferroptosis Signaling Pathway to Improve Cognition Dysfunction in Wilson’s Disease

Wang, X., Shao, N., Zhang, X., Chen, H., Chang, Z., Xie, D., & Zhang, J. (2023) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s443278 · Cited by 30

Dual role of glutamatergic neurotransmission on amyloid β1–42 aggregation and neurotoxicity in embryonic avian retina

Louzada, P. R., Paula-Lima, A. C., Mello, F. G. D., & Ferreira, S. T. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01585-3 · Cited by 28

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

Dai, X., Sun, Y., & Jiang, Z.-F. (2007) · Acta Biochimica et Biophysica Sinica · doi:10.1111/j.1745-7270.2007.00261.x · Cited by 28

Reduced neuronal expression of synaptic transmission modulator HNK‐1/neural cell adhesion molecule as a potential consequence of amyloid β‐mediated oxidative stress: a proteomic approach

Thomas, S. N., Soreghan, B. A., Nistor, M., Sarsoza, F. M., Head, E., & Yang, A. J. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02892.x · Cited by 29

Correlation between metal ions and clinical findings in subjects affected by Alzheimer's disease.

Bomboi, G., Marchione, F., Sepe‐Monti, M., Carolis, A. D., Bianchi, V., Medda, E., Pino, A., Bocca, B., Forte, G., D’Ippolito, C., et al. (2005) · PubMed · Cited by 27

Small angle X-ray scattering analysis of Cu2+-induced oligomers of the Alzheimer's amyloid β peptide

Ryan, T. M., Kirby, N. M., Mertens, H. D. T., Roberts, B. R., Barnham, K. J., Cappai, R., Pham, C. L. L., Masters, C. L., & Curtain, C. C. (2015) · Metallomics · doi:10.1039/c4mt00323c · Cited by 27

Enantiomers of cysteine-modified SeNPs ( d / l SeNPs) as inhibitors of metal-induced Aβ aggregation in Alzheimer's disease

Zhou, X., Sun, J., Yin, T., Le, F., Yang, L., Liu, Y., & Liu, J. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb00731c · Cited by 28

Oxidative Alterations in Neurodegenerative Diseases

Markesbery, W. R., Montine, T. J., & Lovell, M. A. (2001) · Humana Press eBooks · doi:10.1007/978-1-59259-106-0_2 · Cited by 27

Ruthenium(III) complexes with imidazole ligands that modulate the aggregation of the amyloid-β peptide via hydrophobic interactions

Yawson, G. K., Huffman, S. E., Fisher, S. S., Bothwell, P. J., Platt, D. C., Jones, M. A., Ferrence, G. M., Hamaker, C. G., & Webb, M. I. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111303 · Cited by 26

Alzheimer’s Drug PBT2 Interacts with the Amyloid β 1–42 Peptide Differently than Other 8-Hydroxyquinoline Chelating Drugs

Summers, K. L., Roseman, G. P., Schilling, K. M., Dolgova, N. V., Pushie, M. J., Sokaras, D., Kröll, T., Harris, H. H., Millhauser, G. L., Pickering, I. J., et al. (2022) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.2c01694 · Cited by 28

Ca2+ enhances Aβ polymerization rate and fibrillar stability in a dynamic manner

Brännström, K., Öhman, A., Lindhagen‐Persson, M., & Olofsson, A. (2012) · Biochemical Journal · doi:10.1042/bj20121583 · Cited by 26

Cysteine-Mediated Dynamic Hydrogen-Bonding Network in the Active Site of Pin1

Barman, A., & Hamelberg, D. (2014) · Biochemistry · doi:10.1021/bi5000977 · Cited by 26

Does human βA4 exert a protective function against oxidative stress in Alzheimer’s disease?

Berthon, G. (2000) · Medical Hypotheses · doi:10.1054/mehy.1999.0924 · Cited by 26

Amyloid fibrils: modulation of formation and structure by copper(ii)

Pradines, V., Stroia, A. J., & Faller, P. (2008) · New Journal of Chemistry · doi:10.1039/b719556g · Cited by 25

Copper(II)‐Mediated Self‐Assembly of Hairpin Peptides and Templated Synthesis of CuS Nanowires

Wang, C., Sun, Y., Wang, J., Xu, H., & Lu, J. R. (2015) · Chemistry - An Asian Journal · doi:10.1002/asia.201500467 · Cited by 25

Cyclodextrin Nanoparticles Bearing 8‐Hydroxyquinoline Ligands as Multifunctional Biomaterials

Oliveri, V., Bellia, F., & Vecchio, G. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201700031 · Cited by 25

Tau-peptide fragments and their copper(II) complexes: Effects on Amyloid-β aggregation

Natale, G. D., Bellia, F., Sciacca, M. F. M., Campagna, T., & Pappalardo, G. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.09.061 · Cited by 25

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

Zhao, J. J., Gao, W., Yang, Z., Li, H., & Gao, Z. (2018) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2018.10.005 · Cited by 25

Alzheimer risk factors age and female sex induce cortical Aβ aggregation by raising extracellular zinc

Datki, Z., Galik-Olah, Z., Mózes, E., Szegedi, V., Kálmán, J., Hunya, Á. G., Fülöp, L., Tamano, H., Takeda, A., Adlard, P. A., et al. (2020) · Molecular Psychiatry · doi:10.1038/s41380-020-0800-y · Cited by 25

The binding of zinc and copper ions to nerve growth factor is differentially affected by pH: implications for cerebral acidosis

Ross, G. M., Shamovsky, I. L., Woo, S. B., Post, J. I., Vrkljan, P. N., Lawrance, G. M., Solc, M., Dostaler, S. M., Neet, K., & Riopelle, R. J. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00427.x · Cited by 25

A pH-dependent conformational transition of Aβ peptide and physicochemical properties of the conformers in the glial cell

Matsunaga, Y., SAITO, N., Fujii, A., Yokotani, J., Takakura, T., NISHIMURA, T., ESAKI, H., & Yamada, T. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610547 · Cited by 25

Early diagnostics and therapeutics for Alzheimer’s disease – how early can we get there?

Monien, B. H., Apostolova, L. G., & Bitan, G. (2006) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.6.9.1293 · Cited by 27

Lysosomal deposition of Aβ in cultures of brain vascular smooth muscle cells is enhanced by iron

Frackowiak, J., Sukontasup, T., Potempska, A., & Mazur‐Kolecka, B. (2004) · Brain Research · doi:10.1016/j.brainres.2003.12.015 · Cited by 25

Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II)

PANDEY, N. K., Ghosh, S., May, N. V., & Dasgupta, S. (2013) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2013.819300 · Cited by 24

Peroxidase activity of heme bound amyloid β peptides associated with Alzheimer's disease

Roy, M., Pal, I., Nath, A. K., & Dey, S. G. (2020) · Chemical Communications · doi:10.1039/c9cc09758a · Cited by 24

An overview of various mammalian models to study chronic copper intoxication associated Alzheimer’s disease like pathology

Pal, A., & Prasad, R. (2014) · BioMetals · doi:10.1007/s10534-014-9799-3 · Cited by 24

The Necessity of Having a Tetradentate Ligand to Extract Copper(II) Ions from Amyloids

Nguyen, M., Rechignat, L., Robert, A., & Meunier, B. (2014) · ChemistryOpen · doi:10.1002/open.201402075 · Cited by 24

Characterizing bathocuproine self‐association and subsequent binding to Alzheimer's disease amyloid β‐peptide by NMR

Yao, S., Cherny, R. A., Bush, A. I., Masters, C. L., & Barnham, K. J. (2003) · Journal of Peptide Science · doi:10.1002/psc.539 · Cited by 24

Metals in Alzheimer’s and Parkinson’s Disease: Relevance to Dementia with Lewy Bodies

McAllum, E. J., & Finkelstein, D. I. (2016) · Journal of Molecular Neuroscience · doi:10.1007/s12031-016-0809-5 · Cited by 24

Copper in Glucose Intolerance, Cognitive Decline, and Alzheimer Disease

Squitti, R., Mendez, A. J., Ricordi, C., Siotto, M., & Goldberg, R. (2019) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0000000000000280 · Cited by 24

Oxidation of cholesterol catalyzed by amyloid β-peptide (Aβ)–Cu complex on lipid membrane

Yoshimoto, N., Tasaki, M., Shimanouchi, T., Umakoshi, H., & Kuboi, R. (2005) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.100.455 · Cited by 24

Primary structure determinants of the pH- and temperature-dependent aggregation of thioredoxin

Lemaire, S. D., Richardson, J. M., Goyer, A., Keryer, E., Lancelin, J., Makhatadze, G. I., & Jacquot, J. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00235-6 · Cited by 24

Will Preventing Protein Aggregates Live Up to Its Promise as Prophylaxis Against Neurodegenerative Diseases?

Lee, H., Petersen, R. B., Zhu, X., Honda, K., Aliev, G., Smith, M. A., & Perry, G. L. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00491.x · Cited by 24

Cerebral Hemorrhage and Amyloid-β

Atwood, C., Perry, G. L., & Smith, M. A. (2003) · Science · doi:10.1126/science.299.5609.1014a · Cited by 24

Cyclodextrin 3‐Functionalized with 8‐Hydroxyquinoline as an Antioxidant Inhibitor of Metal‐Induced Amyloid Aggregation

Oliveri, V., Bellia, F., & Vecchio, G. (2015) · ChemPlusChem · doi:10.1002/cplu.201402450 · Cited by 23

Binding of Cu(II) ions to peptides studied by fluorescence spectroscopy and isothermal titration calorimetry

Makowska, J., Żamojć, K., Wyrzykowski, D., Uber, D., Wierzbicka, M., Wiczk, W. M., & Chmurzyński, L. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.08.016 · Cited by 23

Conserved Rhodopsin Intradiscal Structural Motifs Mediate Stabilization: Effects of Zinc

Gleim, S., Stojanovic, A., Arehart, E. J., Byington, D., & Hwa, J. (2009) · Biochemistry · doi:10.1021/bi800968w · Cited by 23

Dual functions of β-amyloid oligomer and fibril in Cu(II)-induced H2O2 production

Fang, C.-L., Wu, W., Liu, Q. R., Sun, X., Ma, Y., Zhao, Y., & Li, Y. (2010) · Regulatory Peptides · doi:10.1016/j.regpep.2010.05.001 · Cited by 23

Issues Raised Involving the Copper Hypotheses in the Causation of Alzheimer′s Disease

Brewer, G. J. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/537528 · Cited by 23

Iron is a specific cofactor for distinct oxidation- and aggregation-dependent Aβ toxicity mechanisms

Ott, S., Dziadulewicz, N., & Crowther, D. C. (2015) · Disease Models & Mechanisms · doi:10.1242/dmm.019042 · Cited by 23

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

Goch, W., & Bal, W. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170749 · Cited by 24

A selective emissive chromogenic and fluorogenic seleno-coumarin probe for Cu2+ detection in aprotic media

Gonçalves, A. C., Capelo, J. L., Lodeiro, C., & Santos, A. A. D. (2017) · Photochemical & Photobiological Sciences · doi:10.1039/c7pp00036g · Cited by 23

Molecular modeling of zinc and copper binding with Alzheimer’s amyloid β-peptide

Han, D., Wang, H., & Yang, P. (2007) · BioMetals · doi:10.1007/s10534-007-9107-6 · Cited by 23

Computational Studies of Cu(II)/Met and Cu(I)/Met Binding Motifs Relevant for the Chemistry of Alzheimer's Disease

Gómez‐Balderas, R., Raffa, D. F., Rickard, G. A., Brunelle, P., & Rauk, A. (2005) · The Journal of Physical Chemistry A · doi:10.1021/jp050843i · Cited by 23

Apolipoprotein E ablation decreases synaptic vesicular zinc in the brain

Lee, J., Cho, E., Kim, T.-Y., Kim, D., Palmiter, R. D., Volitakis, I., Kim, J. S., Bush, A. I., & Koh, J. (2010) · BioMetals · doi:10.1007/s10534-010-9354-9 · Cited by 23

Zinc Enhances Synthesis of Presenilin 1 in Mouse Primary Cortical Culture

Park, I.-H., Jung, M. W., Mori, H., & Mook‐Jung, I. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5243 · Cited by 23

Mounting evidence for the involvement of zinc and copper in Alzheimer's disease

Moir, R. D., Atwood, Huang, Tanzi, & Bush, A. I. (1999) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.1999.00472.x · Cited by 23

Neuron-glia: understanding cellular copper homeostasis, its cross-talk and their contribution towards neurodegenerative diseases

Bhattacharjee, A., Ghosh, S., Chatterji, A., & Chakraborty, K. (2020) · Metallomics · doi:10.1039/d0mt00168f · Cited by 23

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

Asthana, A., Madhuri, B., Ramakrishna, T., Raman, B., & Rao, C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.04.012 · Cited by 23

Metals and oxidative homeostasis in Alzheimer's disease

Perry, G. L., Cash, A., Srinivas, R., & Smith, M. A. (2002) · Drug Development Research · doi:10.1002/ddr.10099 · Cited by 22

Conformational Transitions of the Amyloid‐β Peptide Upon Copper(II) Binding and pH Changes

Liao, Q., Owen, M. C., Olubiyi, O. O., Barz, B., & Strodel, B. (2017) · Israel Journal of Chemistry · doi:10.1002/ijch.201600108 · Cited by 22

Implications of Metal Binding and Asparagine Deamidation for Amyloid Formation

Sadakane, Y., & Kawahara, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082449 · Cited by 22

Tailoring solulan C24 based niosomes for transdermal delivery of donepezil: In vitro characterization, evaluation of pH sensitivity, and microneedle-assisted Ex vivo permeation studies

Nayak, A. S., Chodisetti, S., Gadag, S., Nayak, U. Y., Govindan, S., & Raval, K. (2020) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2020.101945 · Cited by 23

Novel neuroprotective neurotrophic NAP analogs targeting metal toxicity and oxidative stress: potential candidates for the control of neurodegenerative diseases

Zheng, H., Blat, D., & Fridkin, M. (2006) · Springer eBooks · doi:10.1007/978-3-211-33328-0_18 · Cited by 22

Aβ(25–35) as proxyholder for amyloidogenic peptides: In vivo evidence

Gulyaeva, N. V., & Stepanichev, M. Y. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2009.12.019 · Cited by 22

Mapping the interaction site of prion protein and Sho

Jiayu, W., Zhu, H., Ming, X., Xiong, W., Songbo, W., Bocui, S., Wensen, L., Li, J., Keying, M., Li, Z., et al. (2009) · Molecular Biology Reports · doi:10.1007/s11033-009-9722-0 · Cited by 22

The influence of phospholipid membranes on bovine calcitonin secondary structure and amyloid formation

Wang, S. S. ‐., Good, T. A., & Rymer, D. L. (2005) · Protein Science · doi:10.1110/ps.041240105 · Cited by 22

Interaction of selected divalent metal ions with human ataxin-3 Q36

Stawoska, I., Wesełucha‐Birczyńska, A., Regonesi, M. E., Riva, M., Tortora, P., & Stochel, G. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0561-1 · Cited by 22

Copper-Induced Oligomerization of Peptides: A Model Study

Schlosser, G., Ştefănescu, R., Przybylski, M., Murariu, M., Hudecz, F., & Drochioiu, G. (2007) · European Journal of Mass Spectrometry · doi:10.1255/ejms.889 · Cited by 22

Physiopathological modulators of amyloid aggregation and novel pharmacological approaches in Alzheimer's disease

DEFELICE, F. G., & Ferreira, S. T. (2002) · Anais da Academia Brasileira de Ciências · doi:10.1590/s0001-37652002000200006 · Cited by 24

Divalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms

Coskuner‐Weber, O. (2016) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-016-1392-5 · Cited by 22

Copper selectively triggers β-sheet assembly of an N-terminally truncated amyloid β-peptide beginning with Glu3

Miura, T., Mitani, S., Takanashi, C., & Mochizuki, N. (2003) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2003.10.008 · Cited by 22

Maternal antibodies facilitate Amyloid-β clearance by activating Fc-receptor-Syk-mediated phagocytosis

Illouz, T., Nicola, R., Ben-Shushan, L., Madar, R., Biragyn, A., & Okun, E. (2021) · Communications Biology · doi:10.1038/s42003-021-01851-6 · Cited by 21

Mechanism of oxidative stress and neurotoxicity associated with heme and copper–Aβ relevant to Alzheimer's disease

Dey, C., Roy, M., Pal, P., Ghosh, R., & Dey, S. G. (2025) · Chemical Society Reviews · doi:10.1039/d5cs00544b · Cited by 22

Insights into the thermodynamics of copper association with amyloid-β, α-synuclein and prion proteins

Hong, L., & Simon, J. D. (2010) · Metallomics · doi:10.1039/c0mt00052c · Cited by 21

Potential roles of Alzheimer precursor protein A4 and β‐amyloid in survival and function of aged spinal motor neurons after axonal injury

Xie, Y., Yao, Z., Chai, H., Wong, W., & Wu, W. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10667 · Cited by 21

Monoisoamyl DMSA reduced copper-induced neurotoxicity by lowering 8-OHdG level, amyloid beta and Tau protein expressions in Sprague-Dawley rats

Patwa, J., Thakur, A., Sharma, A., & Flora, S. J. S. (2020) · Metallomics · doi:10.1039/d0mt00083c · Cited by 21

Effect of Zinc, Copper, and Calcium on the Structure and Stability of Serum Amyloid A

Wang, L., & Colón, W. (2007) · Biochemistry · doi:10.1021/bi602629y · Cited by 21

Disaggregation Ability of Different Chelating Molecules on Copper Ion-Triggered Amyloid Fibers

Zhu, L., Han, Y., He, C., Huang, X., & Wang, Y. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp503282m · Cited by 21

Ionophoric polyphenols selectively bind Cu2+, display potent antioxidant and anti-amyloidogenic properties, and are non-toxic toward Tetrahymena thermophila

Martínez, A., Alcendor, R. R., Rahman, T., Magdalena, P., Ismaila, S., & McCurdy, R. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.06.012 · Cited by 21

Theoretical and Biochemical Studies on the Selectivity of Nerve Growth Factor for Transition Metal Cations

Shamovsky, I. L., Ross, G. M., Riopelle, R. J., & Weaver, D. F. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983303q · Cited by 21

Apolipoprotein Aβ: Black Sheep in a Good Family

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Melov, S. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)02086-5 · Cited by 21

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Ciaglia, T., Miranda, M. R., Micco, S. D., Vietri, M., Smaldone, G., Musella, S., Sarno, V. D., Auriemma, G., Sardo, C., Moltedo, O., et al. (2024) · Antioxidants · doi:10.3390/antiox13121585 · Cited by 20

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Yu, M., Ryan, T. M., Ellis, S., Bush, A. I., Triccas, J. A., Rutledge, P. J., & Todd, M. H. (2014) · Metallomics · doi:10.1039/c4mt00122b · Cited by 20

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Luo, Y., Xu, Y., Bao, Q., Ding, Z., Zhu, C., Huang, Z., & Tan, X. (2012) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-012-0947-3 · Cited by 20

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Li, L., Xu, S., Liu, L., Feng, R., Gong, Y., Zhao, X., Li, J., Cai, J., Feng, N., Wang, L., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160587 · Cited by 20

Alkali ion influence on structure and stability of fibrillar amyloid-β oligomers

Huraskin, D., & Horn, A. H. C. (2019) · Journal of Molecular Modeling · doi:10.1007/s00894-018-3920-4 · Cited by 20

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Liao, Q. (2016)

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Tõugu, V., Tiiman, A., & Palumaa, P. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05061.x · Cited by 219