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

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

An N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: a molecular dynamics study

Gómez-Castro, C. Z., Quintanar, L., & Vela, A. (2024) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-024-02061-1 · Cited by 9

Conformation-dependent affinity of Cu(II) ions peptide complexes derived from the human Pin1 protein

Uber, D., Wyrzykowski, D., Tiberi, C., Sabatino, G., Żmudzińska, W., Chmurzyński, L., Papini, A. M., & Makowska, J. (2016) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-016-5387-9 · Cited by 9

Mapping local structural perturbations in the native state of stefin B (cystatin B) under amyloid forming conditions

Paramore, R., Morgan, G. J., Davis, P. J., Sharma, C.-A., Hounslow, A. M., Taler‐Verčič, A., Žerovnik, E., Waltho, J. P., Cliff, M. J., & Staniforth, R. A. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00094 · Cited by 9

Structural differences between native Hen egg white lysozyme and its fibrils under different environmental conditions

Bhattacharya, S., Ghosh, S., Dasgupta, S., & Roy, A. (2013) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2013.05.060 · Cited by 9

Conformational Regulation of Amyloid β-peptide by Lipid Membranes and Metal Ions

Miura, T., Yoda, M., TSUTSUMI, C., Murayama, K. S., & Takeuchi, H. (2010) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.130.495 · Cited by 9

Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin

Gaudry-Talarmain, Y. M., Rézaei, H., Lane, L., Tréguer, E., & Grosclaude, J. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02111.x · Cited by 9

Molecular Determinants of Alzheimer’s Disease Aβ Peptide Neurotoxicity

Cappai, R., & Barnham, K. J. (2007) · Future Neurology · doi:10.2217/14796708.2.4.397 · Cited by 9

Leveraging heterocycle-fused 1,4-benzoquinone to design chemical modulators for both metal-free and metal-bound amyloid-β

Yi, Y., Kim, K., Kim, H., & Lim, M. H. (2025) · Chemical Science · doi:10.1039/d4sc06070a · Cited by 8

Redox-active Cu(II)–Aβ causes substantial changes in axonal integrity in cultured cortical neurons in an oxidative-stress dependent manner

Howells, C., Saar, K., Eaton, E. D., Ray, S., Palumaa, P., Shabala, L., Adlard, P. A., Bennett, W. R., West, A. K., Guillemin, G. J., et al. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.06.002 · Cited by 8

The opposite effects of Cu(ii) and Fe(iii) on the assembly of glucagon amyloid fibrils

Zhou, X., Tan, J., Zheng, L., Pillai, S., Li, B., Xu, P., Zhang, B., & Zhang, Y. (2012) · RSC Advances · doi:10.1039/c2ra20651j · Cited by 8

Copper( ii ) coordination properties of the Aβ(1–16) 2 peptidomimetic: experimental evidence of intermolecular macrochelate complex species in the Aβ dimer

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

Lipid peroxidation and Alzheimer’s disease: Key role of Amyloid-β

Kontush, A. (2006) · Oléagineux Corps gras Lipides · doi:10.1051/ocl.2006.2222 · Cited by 8

Molecular Hybridization

Zhang, S., Saathoff, J. M., & Liu, H. (2017) · Elsevier eBooks · doi:10.1016/b978-0-08-101011-2.00008-8 · 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

Copper

Møller, L. B., & Aaseth, J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822946-0.00009-x · Cited by 8

The Association of Aluminium and β Amyloid in Alzheimer’s Disease

Exley, C., & Korchazhkina, O. V. (2001) · Elsevier eBooks · doi:10.1016/b978-044450811-9/50047-1 · 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

Alzheimer’s disease: a jigsaw puzzle comprised of different types of programmed cell death pieces

Wang, Y., Mu, D., Li, Y., Liu, C., Feng, J., Lai, Y., & Lou, G. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149861 · Cited by 7

Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation

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

Bis(8‐hydroxyquinoline) Ligands: Exploring their Potential as Selective Copper‐Binding Agents for Alzheimer's Disease

Oliveri, V., & Vecchio, G. (2021) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202100079 · Cited by 7

Hydrogen Ion Dynamics as the Fundamental Link between Neurodegenerative Diseases and Cancer: Its Application to the Therapeutics of Neurodegenerative Diseases with Special Emphasis on Multiple Sclerosis

Harguindey, S., Alfarouk, K. O., Orozco, J. D. P., Reshkin, S. J., & Devesa, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052454 · Cited by 7

Side Effect of Tris on the Interaction of Amyloid β-peptide with Cu2+: Evidence for Tris–Aβ–Cu2+ Ternary Complex Formation

Bin, Y., Jiang, Z., & Xiang, J. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1512-7 · Cited by 7

Dynamics of Trace Element Concentration During Development and Excitotoxic Cell Death in the Cerebellum of Lurcher Mutant Mice

Bäurle, J., Kučera, J., Frischmuth, S., Lambertz, M., & Kranda, K. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00200.x · Cited by 7

The Role of Metals in Alzheimer’s Disease

Hajji, N., Calvert, C., Ritchie, C. W., & Sastre, M. (2013) · Royal Society of Chemistry eBooks · doi:10.1039/9781849735896-00080 · Cited by 7

Synthesis and characterization of copper-specific tetradendate ligands as potential treatment for Alzheimer's disease

Zhang, W., Huang, M., Bijani, C., Liu, Y., Robert, A., & Meunier, B. (2018) · Comptes Rendus Chimie · doi:10.1016/j.crci.2018.01.005 · Cited by 7

Impact of the Rat R5G, Y10F, and H13R Mutations on Tetrameric Aβ42 β-Barrel in a Lipid Bilayer Membrane Model

Ngô, S. T., Nguyen, P. H., & Derreumaux, P. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00030 · Cited by 7

Mitochondrial Medicine

Wallace, D. C., Lott, M. T., & Procaccio, V. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00013-6 · Cited by 8

Copper-assisted interaction between amyloid-β and prion: Ternary metal complexes with Aβ N-terminus and octarepeat

Magrì, A. L., Natale, G. D., & Rizzarelli, E. (2017) · Inorganica Chimica Acta · doi:10.1016/j.ica.2017.10.032 · Cited by 7

Molecular modeling on Zn(II) binding modes of Alzheimer?s amyloid ?-peptide in insoluble aggregates and soluble complexes

Han, D. (2004) · Science China Chemistry · doi:10.1360/03yb0163 · Cited by 7

Disturbances of Copper Homeostasis and Brain Function

Rotilio, G., Ciriolo, M. R., Carrı̀, M. T., & Rossi, L. C. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-288-3_16 · Cited by 7

Brain tissue metal concentrations and Alzheimer’s disease neuropathology in total joint arthroplasty patients versus controls

Ebner, B. A., Erdahl, S. A., Lundgreen, C. S., Vassilaki, M. E., Kremers, W. K., Knopman, D. S., Petersen, R. C., Berry, D. J., Lewallen, D. G., Jannetto, P. J., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02856-9 · Cited by 6

Identifying the copper coordination environment between interacting neurodegenerative proteins: A new approach using pulsed EPR with 14N/15N isotopic labeling

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

Interactions between copper (II) and β-amyloid peptide using capillary electrophoresis–ICP–MS: Kd measurements at the nanogram scale

Duroux, C., & Hagège, A. (2021) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-021-03769-8 · Cited by 6

Metal Ions and Alzheimer's Disease

Adlard, P. A., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/978-0-387-70830-0_15 · Cited by 6

NOSH aspirin may have a protective role in Alzheimer’s disease

Drochioiu, G., Tudorachi, L., & Murariu, M. (2015) · Medical Hypotheses · doi:10.1016/j.mehy.2015.01.008 · Cited by 6

A possible pathogenesis for Alzheimer’s disease: Craniomaxillofacial dysfunction leading to localized cerebrospinal fluid stasis

Lee, S. J. (2008) · Medical Hypotheses · doi:10.1016/j.mehy.2008.09.044 · Cited by 6

β‐amyloid (25–35) enhances lipid metabolism and protein ubiquitination in cultured neurons

Cazzaniga, E., Bulbarelli, A., Cassetti, A., Lonati, E., Re, F., Palestini, P., Mutoh, T., & Masserini, M. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21354 · Cited by 6

Effects of Cu Ions and Explicit Water Molecules on the Copper Binding Domain of Amyloid Precursor Protein APP(131–189): A Molecular Dynamics Study

Wang, Q., Werstiuk, N. H., Kramer, J. R., & Bell, R. A. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp200260e · Cited by 6

Zinc and Alzheimer's Disease: An Update

Cuajungco, M. P., Lees, G. J., Kydd, R. R., Tanzi, R. E., & Bush, A. I. (1999) · Nutritional Neuroscience · doi:10.1080/1028415x.1999.11747277 · Cited by 6

An urgent need to assess safe levels of inorganic copper in nutritional supplements/parenteral nutrition for subset of Alzheimer’s disease patients

Kumar, A., Sharma, P., Prasad, R., & Pal, A. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.04.001 · Cited by 6

Nanodroplet Oligomers (NanDOs) of Aβ40

Pittman, J. M., Srivastava, A. K., Boughter, C. T., Venkata, B. S., Zerweck, J., Moore, P. C., Smok, I., Tonelli, M., Sachleben, J. R., & Meredith, S. C. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00147 · Cited by 6

Sequence‐based modeling of Aβ42 soluble oligomers

Dulin, F., Callebaut, I., Colloc’h, N., & Mornon, J. (2007) · Biopolymers · doi:10.1002/bip.20675 · Cited by 6

Ubiquitin Stability and the Lys 63‐Linked Polyubiquitination Site Are Compromised on Copper Binding

Milardi, D., Arnesano, F., Grasso, G., Magrì, A. L., Tabbı̀, G., Scintilla, S., Natile, G., & Rizzarelli, E. (2007) · Angewandte Chemie · doi:10.1002/ange.200701987 · Cited by 6

Potential therapeutic targets for Alzheimer’s disease

McKeon‐O'Malley, C., Saunders, A. J., Bush, A. I., & Tanzi, R. E. (1998) · Emerging Therapeutic Targets · doi:10.1517/14728222.2.2.157 · Cited by 6

Potentiometric and NMR studies on Cd2+ coordination with the histidine-containing Ac184–188NH2 prion protein fragment

Guantieri, V., Venzo, A., Marco, V. D., Acampora, M., & Biondi, B. (2007) · Inorganica Chimica Acta · doi:10.1016/j.ica.2007.05.026 · Cited by 5

Pathophysiology of Alzheimer’s disease revealed by chemical exchange saturation transfer MRI

Zhuang, C., Chen, B., Chen, Y., Zhang, X., & Wu, R. (2023) · Radiology Science · doi:10.15212/radsci-2023-0004 · Cited by 5

ESI-MS study of self-assembly-formed tetraglycine macrocyclic ligand complex of Cu(II)

Murariu, M. (2013) · International Journal of Mass Spectrometry · doi:10.1016/j.ijms.2013.05.009 · Cited by 5

Anti-fibrillogenic and fibril destabilizing effects of metal ions on cystatin fibrils

Bhat, W. F., Bhat, S. A., Bhat, I. A., Sohail, A., Shah, A., & Bano, B. (2017) · Process Biochemistry · doi:10.1016/j.procbio.2017.03.021 · Cited by 5

Inhibition of Amyloid β Aggregation Using Optimized Nano-Encapsulated Formulations of Plant Extracts with High Metal Chelator Activities

Kazdal, F., Bahadorı, F., Çelik, B., Ertaş, A., & Topçu, G. (2019) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201021666191210125851 · Cited by 5

Sialic Acid Hydroxamate: A Potential Antioxidant and Inhibitor of Metal‐Induced β‐Amyloid Aggregates

Yadav, R., Murthy, R. V., & Kikkeri, R. V. (2015) · ChemBioChem · doi:10.1002/cbic.201500162 · Cited by 5

Amyloidogenic metal-binding proteins: new investigative pathways

Davies, P., Fontaine, S. N., Moualla, D., Wang, X., Wright, J. A., & Brown, D. R. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361299 · Cited by 5

Therapeutic strategies of Alzheimer's disease through manipulation of Aβ metabolism: a focus on Aβ‐degrading peptidase, neprilysin

Fukami, S., Iwata, N., & Saido, T. C. (2002) · Drug Development Research · doi:10.1002/ddr.10073 · Cited by 5

Aluminum-Induced Conformational Changes of .BETA.-Amyloid Protein and the Pathogenesis of Alzheimer's Disease

Kawahara, M. (2003) · Eisei kagaku · doi:10.1248/jhs.49.341 · Cited by 5

Computational Insights into the Development of Novel Therapeutic Strategies for Alzheimer’s Disease

Prabhakar, R. S. (2009) · Future Medicinal Chemistry · doi:10.4155/fmc.09.10 · Cited by 5

Toxic Levels of Amyloid Beta Peptide Do Not Induce VEGF Synthesis

Park, S.-Y., & Chae, C. (2007) · Molecules and Cells · doi:10.1016/s1016-8478(23)10757-6 · Cited by 5

Does closure of acid-sensing ion channels reduce ischemia/reperfusion injury in the rat brain?

Dong, B., Wang, J., Xu, Y., Lian, Z., Zhang, J., Zhu, T., Li, M., & Wei, Y. (2013) · Neural Regeneration Research · doi:10.4103/1673-5374.112851 · Cited by 5

Effect of Zn2+ during Reactivation and Refolding of Urea-Denatured Creatine Kinase

Li, S., Xu, Z., & Hai‐Meng, Z. H. O. U. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1016340522490 · Cited by 5

Inflammation, Free Radicals, Glycation, Metabolism and Apoptosis, and Heavy Metals

Mattson, M. P. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50025-1 · Cited by 5

Copper in Brain and Neurodegeneration

Liddell, J. R., Bush, A. I., & White, A. R. (2004) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc2143 · Cited by 5

Modifiers of Protein Aggregation—From Nonspecific to Specific Interactions

Levy‐Sakin, M., Scherzer‐Attali, R., & Gazit, E. (2012) · Wiley eBooks · doi:10.1002/9781118183373.ch15 · Cited by 5

Heme–Aβ compound 0: a common intermediate in ROS generation and peroxidase activity

Dey, C., Pal, P., Samanta, S., & Dey, S. G. (2025) · Dalton Transactions · doi:10.1039/d5dt00234f · Cited by 4

Protective Effects of Purple Sweet Potato Added to Bacillus subtilis-Fermented Soymilk against Amyloid beta-Induced Memory Impairment

Kim, J. H., Choi, J. M., Lee, S., & Cho, E. J. (2012) · Journal of Agricultural Science · doi:10.5539/jas.v4n4p223 · Cited by 4

Copper-Induced Oligomerization of Ceruloplasmin

Petoukhov, M. V., Av, S., Kostevich, V. A., & Самыгина, В. Р. (2021) · Crystallography Reports · doi:10.1134/s1063774521050175 · Cited by 4

The Aβcentric Pathway of Alzheimer’s Disease

Villemagne, V. L., Cappai, R., Barnham, K. J., Cherny, R. A., Opazo, C., Novakovic, K. E., Rowe, C. C., & Masters, C. L. (2006) · Springer eBooks · doi:10.1007/978-1-84628-440-3_2 · Cited by 4

The α and β domains of human metallothionein-3 co-operatively protect against Aβ1–42–Cu2+ cytotoxicity

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

Ionophoric polyphenols are permeable to the blood–brain barrier, interact with human serum albumin and Calf Thymus DNA, and inhibit AChE enzymatic activity

Martínez, A., Zahran, M., Gomez, M., Guevara, J., Pichardo-Bueno, R., Asim, J., Ortiz, G., Andoh, Y., Shibutani, S., & Kaur, B. (2020) · Medicinal Chemistry Research · doi:10.1007/s00044-020-02615-3 · Cited by 4

Deletion of Dcf1 Reduces Amyloid-β Aggregation and Mitigates Memory Deficits

Li, W., Gan, L., Ma, F.-F., Feng, R., Wang, J., Li, Y., Sun, Y., Wang, Y.-J., Diao, X., Qian, F.-Y., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-200619 · Cited by 4

L-Histidine with nitric acid: A comparison of crystal structures and Hirshfeld surfaces analysis

Chitra, R., Choudhury, R. R., Rajan, R. V., Sajan, D., & Kumar, M. (2022) · Journal of Molecular Structure · doi:10.1016/j.molstruc.2022.133550 · Cited by 4

Free Radicals, Metal Ions, and Aβ Aggregation and Neurotoxicity

Barnham, K. J., Curtain, C. C., & Bush, A. I. (2007) · Springer eBooks · doi:10.1007/978-0-387-36534-3_2 · Cited by 4

Age-dependent oxidation and aggregation of ZnT-1: A role for metal catalyzed oxidation?

Sadineni, V., & Schöneich, C. (2007) · Experimental Gerontology · doi:10.1016/j.exger.2007.09.007 · Cited by 4

Membrane‐targeted strategies for modulating APP and Aβ‐mediated toxicity

Price, K. A., Crouch, P. J., Donnelly, P. S., Masters, C. L., White, A. R., & Curtain, C. C. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00642.x · Cited by 4

Probing the role of metal cations on the aggregation behavior of amyloid β-peptide at a single molecule level by AFM

Xie, Y., Wang, J., & Liu, C. (2016) · Journal of Nanoparticle Research · doi:10.1007/s11051-016-3600-1 · Cited by 4

Link Between Metal Homeostasis and Neurodegenerative Diseases: Crosstalk of Metals and Amyloidogenic Proteins at the Synapse

Mizuno, D., & Kawahara, M. (2017) · Springer eBooks · doi:10.1007/978-4-431-56463-8_14 · Cited by 4

Alzheimer's Pathogenesis, Metal-Mediated Redox Stress, and Potential Nanotheranostics.

Wang, W. T., Tailor, B. A., Cohen, D. S., & Huang, X. (2019) · PubMed · Cited by 4

ATP7B and Alzheimer Disease

Squitti, R., Siotto, M., Ivanova, I. D., & Rongioletti, M. C. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-810532-0.00042-2 · Cited by 4

β‐amyloid model core peptides: Effects of hydrophobes and disulfides

Hawk, L. M. L., Pittman, J. M., Moore, P. C., Srivastava, A. K., Zerweck, J., Williams, J. T. B., Hawk, A. J., Sachleben, J. R., & Meredith, S. C. (2019) · Protein Science · doi:10.1002/pro.3778 · Cited by 5

Role of Copper and Other Transition Metal Ions in the Pathogenesis of Parkinson's Disease, Prion Diseases, Familial Amyotrophic Lateral Sclerosis, and Alzheimer's Disease

Multhaup, G., Dieter, H. H., Beyreuther, K. T., & Bayer, T. A. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-288-3_17 · Cited by 4

A Question of Origins: Non-neuronal Sources of Amyloid-β

Sasmita, A. O., & Depp, C. (2026) · Neuroscience Bulletin · doi:10.1007/s12264-025-01572-4 · Cited by 4

An Electrochemistry and Computational Study at an Electrified Liquid–Liquid Interface for Studying Beta-Amyloid Aggregation

Silwane, B., Wilson, M. R., & Kataky, R. (2023) · Membranes · doi:10.3390/membranes13060584 · Cited by 3

Antioxidant promotion of tyrosine nitration in the presence of copper(ii)

Qiao, L., Liu, B., & Girault, H. H. (2013) · Metallomics · doi:10.1039/c3mt00048f · Cited by 3

Crosstalk between Metals and Neurodegenerative Diseases

Kawahara, M., & Mizuno, D. (2014) · Nippon Eiseigaku Zasshi (Japanese Journal of Hygiene) · doi:10.1265/jjh.69.155 · Cited by 3

Metales de transición y enfermedad de Alzheimer

Opazo, C. (2005) · Revista Española de Geriatría y Gerontología · doi:10.1016/s0211-139x(05)74885-x · Cited by 3

The influence of acidic media on the effect of beta-amyloid peptide on the function of glycine receptor in hippocampal neurons

Bukanova, J. V., Solntseva, E. I., Kondratenko, R. V., & Skrebitsky, V. G. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.09.007 · Cited by 3

Electrochemical Monitoring of the Interaction of Cu(II) with Amyloid-B Peptides on Boron-Doped Diamond Electrode

Zhou, Y., Huo, Z., Zhu, X., Zhu, X., Xu, M., & Liang, Y. L. (2012) · International Journal of Electrochemical Science · doi:10.1016/s1452-3981(23)13937-x · Cited by 3

Neuroinflammatory Environments Promote Amyloid-ß Deposition and Posttranslational Modification

Atwood, C., Smith, M. A., Martins, R. N., Tanzi, R. E., Roher, A. E., Bush, A. I., & Perry, G. L. (2003) · Humana Press eBooks · doi:10.1007/978-1-59259-297-5_12 · Cited by 3

Cu(II) effect on the conformation of regenerated silk fibroin in dilute aqueous solution

Zong, X.-H. (2005) · Chinese Science Bulletin · doi:10.1360/982004-717 · 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

Polymorphism of Alzheimer’s Aβ Amyloid Fibrils

Antzutkin, O. N. (2007) · Springer eBooks · doi:10.1007/1-4020-3910-7_2 · Cited by 3

Amyloid-β: Acute-phase apolipoprotein with metal-binding activity

Kontush, A. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8205 · Cited by 3

Probable lecanemab-associated pontine hemorrhage following cardiovascular intervention: Clinical implications for lecanemab use

Chen, S., Sun, Y., Yao, L., & Peng, Q. (2025) · Journal of Alzheimer s Disease Reports · doi:10.1177/25424823251366998 · Cited by 2

Zinc and Neurodegenerative Diseases

Kawahara, M., Konoha, K., Koyama, H., Ohkawara, S., & Sadakane, Y. (2013) · InTech eBooks · doi:10.5772/54489 · Cited by 2

Nicotine: A Possible Neuroprotector in Brain Disorders

Alkadhi, K. A., Salim, S., & Alzoubi, K. H. (2025) · Springer eBooks · doi:10.1007/978-3-642-36202-6_178-1 · Cited by 2

Metals Involvement in Alzheimer’s Disease — A Patho-Genetic View

Salustri, C., Siotto, M., Bucossi, S., & Squitti, R. (2015) · InTech eBooks · doi:10.5772/60447 · Cited by 2

High Order W02-Reactive Stable Oligomers of Amyloid-β are Produced in vivo and in vitro via Dialysis and Filtration of Synthetic Amyloid-β Monomer

Robb, E. L., Perez, K. A., Hung, L. W., Masters, C. L., Barnham, K. J., Cherny, R. A., Bush, A. I., Adlard, P. A., & Finkelstein, D. I. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-132024 · Cited by 2

Neuropathology and Iron: Central Nervous System Iron Homeostasis

Texel, S. J., Xu, X., Pin, S., & Harris, Z. L. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_23 · 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

Free radical reactions in atherosclerosis; An EPR spectrometry study

Taiwo, F. A., Powers, H. J., Nakano, E., Griffiths, H. R., & Nugent, D. F. (2006) · Journal of Spectroscopy · doi:10.1155/2006/474183 · 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

Metal Binding Modes of Alzheimer's Amyloid β-Peptide in Insoluble Aggregates and Soluble Complexes

Miura, T., Suzuki, K., Kohata, N., & Takeuchi, H. (2000) · Biochemistry · doi:10.1021/bi0002479 · Cited by 457

Roles of Cu2+ in the conformational transitions and dimerization of amyloid-beta peptide and its implications in Alzheimer's disease

Liao, Q. (2016)

Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide

Suzuki, K., Miura, T., & Takeuchi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5263 · Cited by 90

pH-dependence of the specific binding of Cu(II) and Zn(II) ions to the amyloid-β peptide

Ghalebani, L., Wahlström, A., Danielsson, J., Wärmländer, S. K. T. S., & Gräslund, A. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.04.043 · Cited by 48

Binding of zinc(II) and copper(II) to the full‐length Alzheimer’s amyloid‐β peptide

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